Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P03567
|
REP_TGMVY
|
MPSHPKRFQINAKNYFLTYPQCSLSKEESLSQLQALNTPINKKFIKICRELHEDGQPHLHVLIQFEGKYCCQNQRFFDLVSPTRSAHFHPNIQRAKSSSDVKTYIDKDGDTLVWGEFQVDGRSARGGCQTSNDAAAEALNASSKEEALQIIREKIPEKYLFQFHNLNSNLDRIFDKTPEPWLPPFHVSSFTNVPDEMRQWAENYFGKSSAARPERPISIIIEGDSRTGKTMWARSLGPHNYLSGHLDLNSRVYSNKVEYNVIDDVTPQYLKLKHWKELIGAQRDWQTNCKYGKPVQIKGGIPSIVLCNPGEGASYKVFLDKEENTPLKNWTFHNAKFVFLNSPLYQSSTQSS
|
2.7.7.-; 3.1.21.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU01364}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU01364}; Note=Divalent metal cations, possibly Mg(2+) or Mn(2+). {ECO:0000255|PROSITE-ProRule:PRU01364};
|
DNA replication [GO:0006260]; rolling circle single-stranded viral DNA replication [GO:0039684]
|
host cell nucleus [GO:0042025]
|
ATP binding [GO:0005524]; DNA binding [GO:0003677]; endodeoxyribonuclease activity, producing 5'-phosphomonoesters [GO:0016888]; helicase activity [GO:0004386]; metal ion binding [GO:0046872]; nucleotidyltransferase activity [GO:0016779]; structural molecule activity [GO:0005198]
|
PF00799;PF08283;
|
3.40.1310.20;
|
Geminiviridae Rep protein family
| null |
SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Essential for the replication of viral ssDNA. The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep binds a specific region at the genome origin of replication. It introduces an endonucleolytic nick within the conserved sequence 5'-TAATATTAC-3' in the intergenic region of the genome present in all geminiviruses, thereby initiating the rolling circle replication (RCR). Following cleavage, binds covalently to the 5'-phosphate of DNA as a tyrosyl ester. The cleavage gives rise to a free 3'-OH that serves as a primer for the cellular DNA polymerase. The polymerase synthesizes the (+) strand DNA by rolling circle mechanism. After one round of replication, a Rep-catalyzed nucleotidyl transfer reaction releases a circular single-stranded virus genome, thereby terminating the replication. Displays origin-specific DNA cleavage, nucleotidyl transferase, ATPase and helicase activities (By similarity). {ECO:0000250}.
|
Tomato golden mosaic virus (strain Yellow vein) (TGMV)
|
P03586
|
RDRP_TMV
|
MAYTQTATTSALLDTVRGNNSLVNDLAKRRLYDTAVEEFNARDRRPKVNFSKVISEEQTLIATRAYPEFQITFYNTQNAVHSLAGGLRSLELEYLMMQIPYGSLTYDIGGNFASHLFKGRAYVHCCMPNLDVRDIMRHEGQKDSIELYLSRLERGGKTVPNFQKEAFDRYAEIPEDAVCHNTFQTMRHQPMQQSGRVYAIALHSIYDIPADEFGAALLRKNVHTCYAAFHFSENLLLEDSYVNLDEINACFSRDGDKLTFSFASESTLNYCHSYSNILKYVCKTYFPASNREVYMKEFLVTRVNTWFCKFSRIDTFLLYKGVAHKSVDSEQFYTAMEDAWHYKKTLAMCNSERILLEDSSSVNYWFPKMRDMVIVPLFDISLETSKRTRKEVLVSKDFVFTVLNHIRTYQAKALTYANVLSFVESIRSRVIINGVTARSEWDVDKSLLQSLSMTFYLHTKLAVLKDDLLISKFSLGSKTVCQHVWDEISLAFGNAFPSVKERLLNRKLIRVAGDALEIRVPDLYVTFHDRLVTEYKASVDMPALDIRKKMEETEVMYNALSELSVLRESDKFDVDVFSQMCQSLEVDPMTAAKVIVAVMSNESGLTLTFERPTEANVALALQDQEKASEGALVVTSREVEEPSMKGSMARGELQLAGLAGDHPESSYSKNEEIESLEQFHMATADSLIRKQMSSIVYTGPIKVQQMKNFIDSLVASLSAAVSNLVKILKDTAAIDLETRQKFGVLDVASRKWLIKPTAKSHAWGVVETHARKYHVALLEYDEQGVVTCDDWRRVAVSSESVVYSDMAKLRTLRRLLRNGEPHVSSAKVVLVDGVPGCGKTKEILSRVNFDEDLILVPGKQAAEMIRRRANSSGIIVATKDNVKTVDSFMMNFGKSTRCQFKRLFIDEGLMLHTGCVNFLVAMSLCEIAYVYGDTQQIPYINRVSGFPYPAHFAKLEVDEVETRRTTLRCPADVTHYLNRRYEGFVMSTSSVKKSVSQEMVGGAAVINPISKPLHGKILTFTQSDKEALLSRGYSDVHTVHEVQGETYSDVSLVRLTPTPVSIIAGDSPHVLVALSRHTCSLKYYTVVMDPLVSIIRDLEKLSSYLLDMYKVDAGTQXQLQIDSVFKGSNLFVAAPKTGDISDMQFYYDKCLPGNSTMMNNFDAVTMRLTDISLNVKDCILDMSKSVAAPKDQIKPLIPMVRTAAEMPRQTGLLENLVAMIKRNFNAPELSGIIDIENTASLVVDKFFDSYLLKEKRKPNKNVSLFSRESLNRWLEKQEQVTIGQLADFDFVDLPAVDQYRHMYKAQPKQKLDTSIQTEYPALQTIVYHSKKINAIFGPLFSELTRQLLDSVDSSRFLFFTRKTPAQIEDFFGDLDSHVPMDVLELDISKYDKSQNEFHCAVEYEIWRRLGFEDFLGEVWKQGHRKTTLKDYTAGIKTCIWYQRKSGDVTTFIGNTVIIAACLASMLPMEKIIKGAFCGDDSLLYFPKGCEFPDVQHSANLMWNFEAKLFKKQYGYFCGRYVIHHDRGCIVYYDPLKLISKLGAKHIKDWEHLEEFRRSLCDVAVSLNNCAYYTQLDDAVWEVHKTAPPGSFVYKSLVKYLSDKVLFRSLFIDGSSC
|
2.1.1.-; 2.7.7.-; 2.7.7.48; 3.6.4.13
| null |
DNA-templated transcription [GO:0006351]; RNA processing [GO:0006396]; viral RNA genome replication [GO:0039694]; virus-mediated perturbation of host defense response [GO:0019049]
| null |
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; mRNA methyltransferase activity [GO:0008174]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]
|
PF00978;PF20896;PF01443;PF01660;
|
3.30.450.420;3.40.50.300;
|
SsRNA positive-strand viruses RNA-directed RNA polymerase family
| null | null |
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
| null | null | null | null |
FUNCTION: [Replicase large subunit]: Is an RNA-dependent RNA polymerase active in viral RNA replication. {ECO:0000269|PubMed:17634237}.; FUNCTION: [Replicase small subunit]: Is a methyltransferase active in RNA capping and an RNA helicase. Methyltransferase displays a cytoplasmic capping enzyme activity. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. Helicase region probably exhibits NTPase and RNA unwinding activities (Potential). It also acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May mediate silencing suppression through either inhibition of HEN1-mediated siRNA or siRNA demethylation. {ECO:0000269|PubMed:17634237, ECO:0000305}.
|
Tobacco mosaic virus (strain vulgare) (TMV) (Tobacco mosaic virus (strain U1))
|
P03587
|
RDRP_TOML
|
MAYTQTATSSALLETVRGNNTLVNDLAKRRLYDTAVDEFNARDRRPKVNFSKVVSEEQTLIATKAYPEFQITFYNTQNAVHSLAGGLRSLELEYLMMQIPYGSLTYDIGGNFASHLFKGRAYVHCCMPNLDVRDIMRHEGQKDSIELYLSRLERGNKHVPNFQKEAFDRYAEMPNEVVCHDTFQTCRHSQECYTGRVYAIALHSIYDIPADEFGAALLRKNVHVCYAAFHFSENLLLEDSHVNLDEINACFQRDGDRLTFSFASESTLNYSHSYSNILKYVCKTYFPASNREVYMKEFLVTRVNTWFCKFSRIDTFLLYKGVAHKGVDSEQFYKAMEDAWHYKKTLAMCNSERILLEDSSSVNYWFPKMRDMVIVPLFDISLETSKRTRKEVLVSKDFVYTVLNHIRTYQAKALTYSNVLSFVESIRSRVIINGVTARSEWDVDKSLLQSLSMTFFLHTKLAVLKDDLLISKFALGPKTVSQHVWDEISLAFGNAFPSIKERLINRKLIKITENALEIRVPDLYVTFHDRLVSEYKMSVDMPVLDIRKKMEETEEMYNALSELSVLKNSDKFDVDVFSQMCQSLEVDPMTAAKVIVAVMSNESGLTLTFEQPTEANVALALQDSEKASDGALVVTSRDVEEPSIKGSMARGELQLAGLSGDVPESSYTRSEEIESLEQFHMATASSLIHKQMCSIVYTGPLKVQQMKNFIDSLVASLSAAVSNLVKILKDTAAIDLETRQKFGVLDVASKRWLVKPSAKNHAWGVVETHARKYHVALLEHDEFGIITCDNWRRVAVSSESVVYSDMAKLRTLRRLLKDGEPHVSSAKVVLVDGVPGCGKTKEILSRVNFEEDLILVPGRQAAEMIRRRANASGIIVATKDNVRTVDSFLMNYGKGARCQFKRLFIDEGLMLHTGCVNFLVEMSLCDIAYVYGDTQQIPYINRVTGFPYPAHFAKLEVDEVETRRTTLRCPADVTHFLNQRYEGHVMCTSSEKKSVSQEMVSGAASINPVSKPLKGKILTFTQSDKEALLSRGYADVHTVHEVQGETYADVSLVRLTPTPVSIIARDSPHVLVSLSRHTKSLKYYTVVMDPLVSIIRDLERVSSYLLDMYKVDAGTQXQLQVDSVFKNFNLFVAAPKTGDISDMQFYYDKCLPGNSTLLNNYDAVTMKLTDISLNVKDCILDMSKSVAAPKDVKPTLIPMVRTAAEMPRQTGLLENLVAMIKRNFNSPELSGVVDIENTASLVVDKFFDSYLLKEKRKPNKNFSLFSRESLNRWIAKQEQVTIGQLADFDFVDLPAVDQYRHMIKAQPKQKLDLSIQTEYPALQTIVYHSKKINAIFGPLFSELTRQLLDSIDSSRFLFFTRKTPAQIEDFFGDLDSHVPMDVLELDVSKYDKSQNEFHCAVEYEIWRRLGLEDFLAEVWKQGHRKTTLKDYTAGIKTCLWYQRKSGDVTTFIGNTVIIASCLASMLPMEKLIKGAFCGDDSLLYFPKGCEYPDIQQAANLMWNFEAKLFKKQYGYFCGRYVIHHDRGCIVYYDPLKLISKLGAKHIKDWDHLEEFRRSLCDVAESLNNCAYYTQLDDAVGEVHKTAPPGSFVYKSLVKYLSDKVLFRSLFLDGSSC
|
2.1.1.-; 2.7.7.-; 2.7.7.48; 3.6.4.13
| null |
DNA-templated transcription [GO:0006351]; RNA processing [GO:0006396]; viral RNA genome replication [GO:0039694]; virus-mediated perturbation of host defense response [GO:0019049]
| null |
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; mRNA methyltransferase activity [GO:0008174]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]
|
PF00978;PF01443;PF01660;
|
3.30.450.420;3.40.50.300;
|
SsRNA positive-strand viruses RNA-directed RNA polymerase family
| null | null |
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
| null | null | null | null |
FUNCTION: [Replicase large subunit]: Is an RNA-dependent RNA polymerase active in viral RNA replication. {ECO:0000269|PubMed:14512550}.; FUNCTION: [Replicase small subunit]: Is a methyltransferase active in RNA capping and an RNA helicase. Methyltransferase displays a cytoplasmic capping enzyme activity. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. Helicase region probably exhibits NTPase and RNA unwinding activities (Potential). It also acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May mediate silencing suppression through either inhibition of HEN1-mediated siRNA or siRNA demethylation (By similarity). {ECO:0000250, ECO:0000305}.
|
Tomato mosaic virus (strain L) (ToMV) (TMV strain tomato)
|
P03588
|
1A_BMV
|
MSSSIDLLKLIAEKGADSQSAQDIVDNQVAQQLSAQIEYAKRSKKINVRNKLSIEEADAFRDRYGGAFDLNLTQQYHAPHSLAGALRVAEHYDCLDSFPPEDPVIDFGGSWWHHFSRRDKRVHSCCPVLGVRDAARHEERMCRMRKILQESDDFDEVPNFCLNRAQDCDVQADWAICIHGGYDMGFQGLCDAMHSHGVRVLRGTVMFDGAMLFDREGFLPLLKCHWQRDGSGADEVIKFDFENESTLSYIHGWQDLGSFFTESVHCIDGTTYLLEREMLKCNIMTYKIIATNLRCPRETLRHCVWFEDISKYVGVSIPEDWSLNRWKCVRVAKTTVREVEEIAFRCFKESKEWTENMKAVASILSAKSSTVIINGQAIMAGERLDIEDYHLVAFALTLNLYQKYEKLTALRDGMEWKGWCHHFKTRFWWGGDSSRAKVGWLRTLASRFPLLRLDSYADSFKFLTRLSNVEEFEQDSVPISRLRTFWTEEDLFDRLEHEVQTAKTKRSKKKAKVPPAAEIPQEEFHDAPESSSPESVSDDVKPVTDVVPDAEVSVEVPTDPRGISRHGAMKEFVRYCKRLHNNSESNLRHLWDISGGRGSEIANKSIFETYHRIDDMVNVHLANGNWLYPKKYDYTVGYNEHGLGPKHADETYIVDKTCACSNLRDIAEASAKVSVPTCDISMVDGVAGCGKTTAIKDAFRMGEDLIVTANRKSAEDVRMALFPDTYNSKVALDVVRTADSAIMHGVPSCHRLLVDEAGLLHYGQLLVVAALSKCSQVLAFGDTEQISFKSRDAGFKLLHGNLQYDRRDVVHKTYRCPQDVIAAVNLLKRKCGNRDTKYQSWTSESKVSRSLTKRRITSGLQVTIDPNRTYLTMTQADKAALQTRAKDFPVSKDWIDGHIKTVHEAQGISVDNVTLVRLKSTKCDLFKHEEYCLVALTRHKKSFEYCFNGELAGDLIFNCVK
|
2.1.1.-; 3.6.4.-
| null |
positive stranded viral RNA replication [GO:0039690]; RNA processing [GO:0006396]
|
host cell cytoplasm [GO:0030430]; host cell endoplasmic reticulum membrane [GO:0044167]; membrane [GO:0016020]
|
ATP binding [GO:0005524]; helicase activity [GO:0004386]; hydrolase activity, acting on acid anhydrides [GO:0016817]; mRNA methyltransferase activity [GO:0008174]; RNA binding [GO:0003723]
|
PF12503;PF01443;PF01660;
|
3.40.50.300;
|
Bromoviridae replication protein 1a family
| null |
SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:19325881}; Peripheral membrane protein {ECO:0000269|PubMed:19325881}.
| null | null | null | null | null |
FUNCTION: Involved in the virus replication. Contains a helicase domain and a methyltransferase domain. The methyltransferase domain is probably involved in viral RNA capping. Involved in the formation of ER membrane spherular invaginations in which RNA replication complexes form. {ECO:0000269|PubMed:19325881}.
|
Brome mosaic virus (BMV)
|
P03599
|
POL2_CPMVS
|
MFSFTEAKSKISLWTRSAAPLNNVYLSYSCRCGLGKRKLAGGCCSAPYITCYDSADFRRVQYLYFCLTRYCCLYFFLLLLADWFYKKSSIFFETEFSRGFRTWRKIVKLLYILPKFEMESIMSRGIPSGILEEKAIQFKRAKEGNKPLKDEIPKPEDMYVSHTSKWNVLRKMSQKTVDLSKAAAGMGFINKHMLTGNILAQPTTVLDIPVTKDKTLAMASDFIRKENLKTSAIHIGAIEIIIQSFASPESDLMGGFLLVDSLHTDTANAIRSIFVAPMRGGRPVRVVTFPNTLAPVSCDLNNRFKLICSLPNCDIVQGSQVAEVSVNVAGCATSIEKSHTPSQLYTEEFEKEGAVVVEYLGRQTYCAQPSNLPTEEKLRSLKFDFHVEQPSVLKLSNSCNAHFVKGESLKYSISGKEAENHAVHATVVSREGASAAPKQYDPILGRVLDPRNGNVAFPQMEQNLFALSLDDTSSVRGSLLDTKFAQTRVLLSKAMAGGDVLLDEYLYDVVNGQDFRATVAFLRTHVITGKIKVTATTNISDNSGCCLMLAINSGVRGKYSTDVYTICSQDSMTWNPGCKKNFSFTFNPNPCGDSWSAEMISRSRVRMTVICVSGWTLSPTTDVIAKLDWSIVNEKCEPTIYHLADCQNWLPLNRWMGKLTFPQGVTSEVRRMPLSIGGGAGATQAFLANMPNSWISMWRYFRGELHFEVTKMSSPYIKATVTFLIAFGNLSDAFGFYESFPHRIVQFAEVEEKCTLVFSQQEFVTAWSTQVNPRTTLEADGCPYLYAIIHDSTTGTISGDFNLGVKLVGIKDFCGIGSNPGIDGSRLLGAIAQGPVCAEASDVYSPCMIASTPPAPFSDVTAVTFDLINGKITPVGDDNWNTHIYNPPIMNVLRTAAWKSGTIHVQLNVRGAGVKRADWDGQVFVYLRQSMNPESYDARTFVISQPGSAMLNFSFDIIGPNSGFEFAESPWANQTTWYLECVATNPRQIQQFEVNMRFDPNFRVAGNILMPPFPLSTETPPLLKFRFRDIERSKRSVMVGHTATAA
| null | null |
transport of virus in host, cell to cell [GO:0046740]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell nucleus [GO:0042025]; host cell plasmodesma [GO:0044219]; T=3 icosahedral viral capsid [GO:0039617]
|
DNA binding [GO:0003677]; GTP binding [GO:0005525]; RNA binding [GO:0003723]; structural molecule activity [GO:0005198]
|
PF02247;PF02248;
|
2.60.120.20;
| null |
PTM: [RNA2 polyprotein]: Specific enzymatic cleavages by picornain 3C-like protease in vivo yield mature proteins. {ECO:0000269|PubMed:16789216}.; PTM: [Small capsid protein precursor]: The C-terminal 24 amino acids of the small capsid protein are specifically cleaved by the RNA1 encoded picornain 3C-like protease during maturation. {ECO:0000269|PubMed:10049828, ECO:0000269|PubMed:27021160}.; PTM: [Large capsid protein]: Not glycosylated. {ECO:0000269|PubMed:10725439}.; PTM: [Mature small capsid protein]: Not glycosylated. {ECO:0000269|PubMed:10725439}.
|
SUBCELLULAR LOCATION: [VP58]: Host nucleus {ECO:0000269|PubMed:8497075}.; SUBCELLULAR LOCATION: [Movement protein]: Host cell junction, host plasmodesma {ECO:0000269|PubMed:14579172, ECO:0000269|PubMed:27339685}. Note=Assembles in tubules that are embedded within modified plasmodesmata. {ECO:0000269|PubMed:10864669, ECO:0000269|PubMed:14579172, ECO:0000269|PubMed:27339685}.; SUBCELLULAR LOCATION: [Large capsid protein]: Virion {ECO:0000269|PubMed:10603314, ECO:0000269|PubMed:26657148, ECO:0000269|PubMed:27021160, ECO:0000269|PubMed:28373698}.; SUBCELLULAR LOCATION: [Mature small capsid protein]: Virion {ECO:0000269|PubMed:10603314, ECO:0000269|PubMed:26657148, ECO:0000269|PubMed:27021160, ECO:0000269|PubMed:28373698}.
| null | null | null | null | null |
FUNCTION: [VP58]: Responsible for viral RNA2 accumulation. May function by recruiting the RNA1-encoded polyprotein that contains the replication protein to RNA2 and enable its replication. {ECO:0000250|UniProtKB:P23009}.; FUNCTION: [Movement protein]: Transports the viral genome to neighboring plant cells directly through plasmosdesmata, without any budding (PubMed:9501035). The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Acts by forming a tubular structure at the host plasmodesmata, enlarging it enough to allow free passage of virion capsids (Probable) (PubMed:12556992, PubMed:14579172). Binds to GTP and to single-stranded RNA and single-stranded DNA in a non-sequence-specific manner (PubMed:14722313). {ECO:0000269|PubMed:12556992, ECO:0000269|PubMed:14579172, ECO:0000269|PubMed:14722313, ECO:0000269|PubMed:9501035, ECO:0000305|PubMed:8497075}.; FUNCTION: [Large capsid protein]: Together with the mature small capsid protein, forms an icosahedral capsid (T=3) enclosing the viral positive strand RNA genome, with a diameter of approximately 300 Angstroms (PubMed:10603314, PubMed:26657148, PubMed:27021160, PubMed:28373698). The capsid is formed from 60 copies each of the large and the small capsid protein (PubMed:10603314, PubMed:26657148, PubMed:27021160, PubMed:28373698). The large capsid protein interacts with the viral RNA (PubMed:26657148, PubMed:28373698). {ECO:0000269|PubMed:10603314, ECO:0000269|PubMed:26657148, ECO:0000269|PubMed:27021160, ECO:0000269|PubMed:28373698}.; FUNCTION: [Mature small capsid protein]: Together with the large capsid protein, forms an icosahedral capsid (T=3) enclosing the viral positive strand RNA genome, with a diameter of approximately 300 Angstroms. The capsid is formed from 60 copies each of the large and the small capsid protein. The mature small capsid protein forms the turrets at the fivefold axes of the viral particle. {ECO:0000269|PubMed:10603314, ECO:0000269|PubMed:26657148, ECO:0000269|PubMed:27021160, ECO:0000269|PubMed:28373698}.; FUNCTION: [Small capsid protein precursor]: The cleavable C-terminus of small capsid protein seems to be involved in viral assembly and RNA packaging (PubMed:10049828). After virus assembly, these amino acids are cleaved off during the normal maturation of the virus (PubMed:10049828, PubMed:26657148). Also seems to act as suppressor of post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs (PubMed:15165817, PubMed:15483261). {ECO:0000269|PubMed:10049828, ECO:0000269|PubMed:15165817, ECO:0000269|PubMed:15483261, ECO:0000269|PubMed:26657148}.; FUNCTION: [Small capsid protein C-terminus part]: Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. {ECO:0000269|PubMed:15165817, ECO:0000269|PubMed:15483261}.
|
Cowpea mosaic virus (strain SB) (CPMV)
|
P03600
|
POL1_CPMVS
|
MGLPEYEADSEALLSQLTIEFTPGMTVSSLLAQVTTNDFHSAIEFFAAEKAVDIEGVHYNAYMQQIRKNPSLLRISVVAYAFHVSDMVAETMSYDVYEFLYKHYALFISNLVTRTLRFKELLLFCKQQFLEKMQASIVWAPELEQYLQVEGDAVAQGVSQLLYKMVTWVPTFVRGAVDWSVDAILVSFRKHFEKMVQEYVPMAHRVCSWLSQLWDKIVQWISQASETMGWFLDGCRDLMTWGIATLATCSALSLVEKLLVAMGFLVEPFGLSGIFLRTGVVAAACYNYGTNSKGFAEMMALLSLAANCVSTVIVGGFFPGEKDNAQSSPVILLEGLAGQMQNFCETTLVSVGKTCTAVNAISTCCGNLKALAGRILGMLRDFIWKTLGFETRFLADASLLFGEDVDGWLKAISDLRDQFIAKSYCSQDEMMQILVLLEKGRQMRKSGLSKGGISPAIINLILKGINDLEQLNRSCSVQGVRGVRKMPFTIFFQGKSRTGKSLLMSQVTKDFQDHYGLGGETVYSRNPCDQYWSGYRRQPFVLMDDFAAVVTEPSAEAQMINLISSAPYPLNMAGLEEKGICFDSQFVFVSTNFLEVSPEAKVRDDEAFKNRRHVIVQVSNDPAKAYDAANFASNQIYTILAWKDGRYNTVCVIEDYDELVAYLLTRSQQHAEEQEKNLANMMKSATFESHFKSLVEVLELGSMISAGFDIIRPEKLPSEAKEKRVLYSIPYNGEYCNALIDDNYNVTCWFGECVGNPEQLSKYSEKMLLGAYEFLLCSESLNVVIQAHLKEMVCPHHYDKELNFIGKIGETYYHNQMVSNIGSMQKWHRAILFGIGVLLGKEKEKTWYQVQVANVKQALYDMYTKEIRDWPMPIKVTCGIVLAAIGGSAFWKVFQQLVGSGNGPVLMGVAAGAFSAEPQSRKPNRFDMQQYRYNNVPLKRRVWADAQMSLDQSSVAIMSKCRANLVFGGTNLQIVMVPGRRFLACKHFFTHIKTKLRVEIVMDGRRYYHQFDPANIYDIPDSELVLYSHPSLEDVSHSCWDLFCWDPDKELPSVFGADFLSCKYNKFGGFYEAQYADIKVRTKKECLTIQSGNYVNKVSRYLEYEAPTIPEDCGSLVIAHIGGKHKIVGVHVAGIQGKIGCASLLPPLEPIAQAQGAEEYFDFLPAEENVSSGVAMVAGLKQGVYIPLPTKTALVETPSEWHLDTPCDKVPSILVPTDPRIPAQHEGYDPAKSGVSKYSQPMSALDPELLGEVANDVLELWHDCAVDWDDFGEVSLEEALNGCEGVEYMERIPLATSEGFPHILSRNGKEKGKRRFVQGDDCVVSLIPGTTVAKAYEELEASAHRFVPALVGIECPKDEKLPMRKVFDKPKTRCFTILPMEYNLVVRRKFLNFVRFIMANRHRLSCQVGINPYSMEWSRLAARMKEKGNDVLCCDYSSFDGLLSKQVMDVIASMINELCGGEDQLKNARRNLLMACCSRLAICKNTVWRVECGIPSGFPMTVIVNSIFNEILIRYHYKKLMREQQAPELMVQSFDKLIGLVTYGDDNLISVNAVVTPYFDGKKLKQSLAQGGVTITDGKDKTSLELPFRRLEECDFLKRTFVQRSSTIWDAPEDKASLWSQLHYVNCNNCEKEVAYLTNVVNVLRELYMHSPREATEFRRKVLKKVSWITSGDLPTLAQLQEFYEYQRQQGGADNNDTCDLLTSVDLLGPPLSFEKEAMHGCKVSEEIVTKNLAYYDFKRKGEDEVVFLFNTLYPQSSLPDGCHSVTWSQGSGRGGLPTQSWMSYNISRKDSNINKIIRTAVSSKKRVIFCARDNMVPVNIVALLCAVRNKLMPTAVSNATLVKVMENAKAFKFLPEEFNFAFSDV
|
2.7.7.48; 3.4.22.-; 3.6.4.-
| null |
DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; viral RNA genome replication [GO:0039694]
|
host cell endoplasmic reticulum [GO:0044165]; host cell membrane [GO:0033644]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]
|
ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]
|
PF00548;PF00680;PF00910;
|
3.30.70.270;2.40.10.10;
| null |
PTM: [RNA1 polyprotein]: Specific enzymatic cleavages by picornain 3C-like protease in vivo yield mature proteins (PubMed:1431806, PubMed:16789216, PubMed:16789257, PubMed:7964626). Picornain 3C-like protease is autocatalytically processed. {ECO:0000269|PubMed:1431806, ECO:0000269|PubMed:16789216, ECO:0000269|PubMed:16789257, ECO:0000269|PubMed:7964626}.; PTM: [Viral genome-linked protein]: Uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase. {ECO:0000269|Ref.5}.
|
SUBCELLULAR LOCATION: [Putative helicase]: Host membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:12021362}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host endoplasmic reticulum {ECO:0000269|PubMed:10864669}.; SUBCELLULAR LOCATION: [Protease cofactor]: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:12021362}.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
| null | null | null | null |
FUNCTION: [Picornain 3C-like protease]: Thiol protease that cleaves the RNA1 and RNA2 polyproteins. {ECO:0000269|PubMed:16453750, ECO:0000269|PubMed:16789216, ECO:0000269|PubMed:8811039}.; FUNCTION: [Viral genome-linked protein]: Plays a role in RNA replication. It is covalently linked to the 5'terminus of both viral single-stranded RNA1 and RNA2 molecules. {ECO:0000269|PubMed:11883002, ECO:0000269|PubMed:16453534}.; FUNCTION: [Protease cofactor]: Down-regulates the RNA1 polyprotein processing and enhances trans-cleavage of RNA2 polyproteins (PubMed:1413528). The protease cofactor and the putative helicase seem to target the replication complexes to ER membranes. Their physical association causes the membrane rearrangement of host ER that may result in formation of the small membranous vesicles that are the site of viral RNA synthesis (PubMed:12021362). {ECO:0000269|PubMed:12021362, ECO:0000269|PubMed:1413528}.; FUNCTION: [Putative helicase]: The protease cofactor and the putative helicase seem to target the replication complexes to ER membranes. Their physical association causes the membrane rearrangement of host ER that may result in formation of the small membranous vesicles that are the site of viral RNA synthesis. {ECO:0000269|PubMed:12021362}.; FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral genome. {ECO:0000305|PubMed:1431806}.
|
Cowpea mosaic virus (strain SB) (CPMV)
|
P03607
|
CAPSD_SCPMV
|
MSGLFHHRTKPREIRAFVMATRLTKKQLAQAIQNTLPNPPRRKRRAKRRAAQVPKPTQAGVSMAPIAQGTMVKLRPPMLRSSMDVTILSHCELSTELAVTVTIVVTSELVMPFTVGTWLRGVAQNWSKYAWVAIRYTYLPSCPTTTSGAIHMGFQYDMADTLPVSVNQLSNLKGYVTGPVWEGQSGLCFVNNTKCPDTSRAITIALDTNEVSEKRYPFKTATDYATAVGVNANIGNILVPARLVTAMEGGSSKTAVNTGRLYASYTIRLIEPIAAALNL
| null | null | null |
T=3 icosahedral viral capsid [GO:0039617]
|
calcium ion binding [GO:0005509]; lipid binding [GO:0008289]; RNA binding [GO:0003723]; structural constituent of virion [GO:0039660]
|
PF00729;
|
2.60.120.20;
|
Icosahedral plant coat protein family
| null |
SUBCELLULAR LOCATION: Virion {ECO:0000305}.
| null | null | null | null | null | null |
Southern cowpea mosaic virus (SCPMV) (Southern bean mosaic virus (strain cowpea))
|
P03612
|
CAPSD_BPMS2
|
MASNFTQFVLVDNGGTGDVTVAPSNFANGVAEWISSNSRSQAYKVTCSVRQSSAQNRKYTIKVEVPKVATQTVGGVELPVAAWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGIY
| null | null |
negative regulation of viral translation [GO:1904972]; regulation of translation [GO:0006417]
|
T=3 icosahedral viral capsid [GO:0039617]
|
identical protein binding [GO:0042802]; RNA binding [GO:0003723]; structural molecule activity [GO:0005198]
|
PF01819;
|
3.30.380.10;
|
Leviviricetes capsid protein family
| null |
SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:8254664}. Note=The shell is composed of 178 copies of the capsid protein and 1 copy of the maturation protein. {ECO:0000269|PubMed:23810697, ECO:0000305|PubMed:8254664}.
| null | null | null | null | null |
FUNCTION: Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins) (PubMed:18662904, PubMed:8254664). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome (PubMed:26608810, PubMed:7523953, PubMed:9469847). The capsid contains also 1 copy of the A2 maturation protein (PubMed:8254664). {ECO:0000269|PubMed:12948491, ECO:0000269|PubMed:18662904, ECO:0000269|PubMed:26608810, ECO:0000269|PubMed:7523953, ECO:0000269|PubMed:9469847, ECO:0000305|PubMed:8254664}.; FUNCTION: Acts as a translational repressor of viral replicase synthesis late in infection. This latter function is the result of capsid protein interaction with an RNA hairpin which contains the replicase ribosome-binding site. {ECO:0000269|PubMed:16531233, ECO:0000269|PubMed:9207028, ECO:0000269|PubMed:9245600}.
|
Escherichia phage MS2 (Bacteriophage MS2)
|
P03615
|
CAPSD_BPQBE
|
MAKLETVTLGNIGKDGKQTLVLNPRGVNPTNGVASLSQAGAVPALEKRVTVSVSQPSRNRKNYKVQVKIQNPTACTANGSCDPSVTRQAYADVTFSFTQYSTDEERAFVRTELAALLASPLLIDAIDQLNPAY
| null | null | null |
T=3 icosahedral viral capsid [GO:0039617]
|
RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; translation repressor activity [GO:0030371]
|
PF01819;
|
3.30.380.10;
|
Leviviricetes capsid protein family
| null |
SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:27671640, ECO:0000269|PubMed:29078304}. Note=The shell is composed of 89 dimers of the capsid protein, one of them being sequestered inside the virion, and 1 copy of the maturation protein. {ECO:0000269|PubMed:27671640, ECO:0000269|PubMed:29078304}.
| null | null | null | null | null |
FUNCTION: Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins) (PubMed:19913556, PubMed:27671640). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome (PubMed:27671640, PubMed:8943226). Binding of the capsid proteins to the viral RNA induces a conformational change required for efficient T=3 shell formation (PubMed:19913556). The capsid contains also 1 copy of the A2 maturation protein (PubMed:27671640). {ECO:0000269|PubMed:19913556, ECO:0000269|PubMed:27671640, ECO:0000269|PubMed:8943226}.; FUNCTION: Acts as a translational repressor of viral replicase synthesis late in infection. This latter function is the result of capsid protein interaction with an RNA hairpin which contains the replicase ribosome-binding site. {ECO:0000269|PubMed:8943226}.
|
Escherichia virus Qbeta (Bacteriophage Q-beta)
|
P03630
|
CAPSD_BPPP7
|
MSKTIVLSVGEATRTLTEIQSTADRQIFEEKVGPLVGRLRLTASLRQNGAKTAYRVNLKLDQADVVDCSTSVCGELPKVRYTQVWSHDVTIVANSTEASRKSLYDLTKSLVATSQVEDLVVNLVPLGR
| null | null |
regulation of translation [GO:0006417]
|
T=3 icosahedral viral capsid [GO:0039617]
|
identical protein binding [GO:0042802]; RNA binding [GO:0003723]
|
PF09063;
|
3.30.380.10;
|
Leviviricetes capsid protein family
| null |
SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:109813}. Note=The shell is composed of 178 copies of the capsid protein and 1 copy of the maturation protein. {ECO:0000250|UniProtKB:P03612}.
| null | null | null | null | null |
FUNCTION: Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins) (PubMed:10739912). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome (By similarity). {ECO:0000250|UniProtKB:P03612, ECO:0000269|PubMed:10739912}.; FUNCTION: Acts as a translational repressor of viral replicase synthesis late in infection. This latter function is the result of capsid protein interaction with an RNA hairpin which contains the replicase ribosome-binding site. {ECO:0000269|PubMed:11306589}.
|
Pseudomonas phage PP7 (Bacteriophage PP7)
|
P03631
|
REPA_BPPHS
|
MVRSYYPSECHADYFDFERIEALKPAIEACGISTLSQSPMLGFHKQMDNRIKLLEEILSFRMQGVEFDNGDMYVDGHKAASDVRDEFVSVTEKLMDELAQCYNVLPQLDINNTIDHRPEGDEKWFLENEKTVTQFCRKLAAERPLKDIRDEYNYPKKKGIKDECSRLLEASTMKSRRGFAIQRLMNAMRQAHADGWFIVFDTLTLADDRLEAFYDNPNALRDYFRDIGRMVLAAEGRKANDSHADCYQYFCVPEYGTANGRLHFHAVHFMRTLPTGSVDPNFGRRVRNRRQLNSLQNTWPYGYSMPIAVRYTQDAFSRSGWLWPVDAKGEPLKATSYMAVGFYVAKYVNKKSDMDLAAKGLGAKEWNNSLKTKLSLLPKKLFRIRMSRNFGMKMLTMTNLSTECLIQLTKLGYDATPFNQILKQNAKREMRLRLGKVTVADVLAAQPVTTNLLKFMRASIKMIGVSNLQSFIASMTQKLTLSDISDESKNYLDKAGITTACLRIKSKWTAGGK
|
3.1.21.-; 6.5.1.1
| null |
DNA replication [GO:0006260]; rolling circle single-stranded viral DNA replication [GO:0039684]
| null |
ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA ligase (ATP) activity [GO:0003910]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]
|
PF05840;
| null |
Microviridae Rep protein family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.; EC=6.5.1.1;
| null | null | null | null |
FUNCTION: Plays an essential role in viral DNA replication. Binds the origin of replication and cleaves the dsDNA replicative form I (RFI) and becomes covalently bound to it via phosphotyrosine bond, generating the dsDNA replicative form II (RFII). In turn, viral DNA replication initiates in the presence of host Rep and DNA polymerase III at the 3'-OH of the cleavage site. After one round of rolling circle synthesis, protein A is linked to the newly synthesized ssDNA and joins the ends of the displaced strand to generate a circular single-stranded molecule ready to be packed into a virion.; FUNCTION: The A* protein binds to double-stranded DNA and prevents hydrolysis by nucleases. Additionally, A* is an inhibitor of DNA replication and may have a role in the transition from semiconservative replicative form DNA replication to single-stranded DNA synthesis in the life cycle.
|
Enterobacteria phage phiX174 (Isolate Sanger) (Bacteriophage phi-X174)
|
P03661
|
G3P_BPFD
|
MKKLLFAIPLVVPFYSHSAETVESCLAKPHTENSFTNVWKDDKTLDRYANYEGCLWNATGVVVCTGDETQCYGTWVPIGLAIPENEGGGSEGGGSEGGGSEGGGTKPPEYGDTPIPGYTYINPLDGTYPPGTEQNPANPNPSLEESQPLNTFMFQNNRFRNRQGALTVYTGTVTQGTDPVKTYYQYTPVSSKAMYDAYWNGKFRDCAFHSGFNEDPFVCEYQGQSSDLPQPPVNAGGGSGGGSGGGSEGGGSEGGGSEGGGSEGGGSGGGSGSGDFDYEKMANANKGAMTENADENALQSDAKGKLDSVATDYGAAIDGFIGDVSGLANGNGATGDFAGSNSQMAQVGDGDNSPLMNNFRQYLPSLPQSVECRPYVFGAGKPYEFSIDCDKINLFRGVFAFLLYVATFMYVFSTFANILRNKES
| null | null |
adhesion receptor-mediated virion attachment to host cell [GO:0098671]; entry receptor-mediated virion attachment to host cell [GO:0098670]; viral extrusion [GO:0099045]; virion attachment to host cell pilus [GO:0039666]
|
host cell membrane [GO:0033644]; membrane [GO:0016020]; viral capsid [GO:0019028]
| null |
PF05357;
|
2.30.27.10;
|
Inovirus G3P protein family
| null |
SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Prior to assembly, G3P is found associated with the bacterial host inner membrane. There are about five copies of this protein per mature phage that are located on the head side of the filamentous virion.
| null | null | null | null | null |
FUNCTION: Plays essential roles both in the penetration of the viral genome into the bacterial host via pilus retraction and in the extrusion process. During the initial step of infection, G3P mediates adsorption of the phage to its primary receptor, the tip of host F-pilus. Subsequent interaction with the host entry receptor tolA induces penetration of the viral DNA into the host cytoplasm. In the extrusion process, G3P mediates the release of the membrane-anchored virion from the cell via its C-terminal domain. {ECO:0000269|PubMed:12054858, ECO:0000269|PubMed:21110981}.
|
Enterobacteria phage fd (Bacteriophage fd)
|
P03679
|
GP1_BPPH2
|
MGKIFDQEKRLEGTWKNSKWGNQGIIAPVDGDLKMIDLELEKKMTKLEHENKLMKNALYELSRMENNDYATWVIKVLFGGAPHGAK
| null | null |
DNA replication [GO:0006260]; viral DNA genome replication [GO:0039693]
|
host cell membrane [GO:0033644]; membrane [GO:0016020]
|
RNA binding [GO:0003723]
| null | null |
Phi29likevirus DNA replication protein 1 family
| null |
SUBCELLULAR LOCATION: Host membrane {ECO:0000269|PubMed:11032825, ECO:0000269|PubMed:12904294}; Peripheral membrane protein {ECO:0000269|PubMed:12904294}.
| null | null | null | null | null |
FUNCTION: Protein that assembles into highly ordered structures and provides a specific site for viral DNA replication. Probably anchors the viral DNA replisome to the host membrane. {ECO:0000269|PubMed:11032825, ECO:0000269|PubMed:12904294, ECO:0000269|PubMed:9193003, ECO:0000269|PubMed:9774353}.
|
Bacillus phage phi29 (Bacteriophage phi-29)
|
P03680
|
DPOL_BPPH2
|
MKHMPRKMYSCDFETTTKVEDCRVWAYGYMNIEDHSEYKIGNSLDEFMAWVLKVQADLYFHNLKFDGAFIINWLERNGFKWSADGLPNTYNTIISRMGQWYMIDICLGYKGKRKIHTVIYDSLKKLPFPVKKIAKDFKLTVLKGDIDYHKERPVGYKITPEEYAYIKNDIQIIAEALLIQFKQGLDRMTAGSDSLKGFKDIITTKKFKKVFPTLSLGLDKEVRYAYRGGFTWLNDRFKEKEIGEGMVFDVNSLYPAQMYSRLLPYGEPIVFEGKYVWDEDYPLHIQHIRCEFELKEGYIPTIQIKRSRFYKGNEYLKSSGGEIADLWLSNVDLELMKEHYDLYNVEYISGLKFKATTGLFKDFIDKWTYIKTTSEGAIKQLAKLMLNSLYGKFASNPDVTGKVPYLKENGALGFRLGEEETKDPVYTPMGVFITAWARYTTITAAQACYDRIIYCDTDSIHLTGTEIPDVIKDIVDPKKLGYWAHESTFKRAKYLRQKTYIQDIYMKEVDGKLVEGSPDDYTDIKFSVKCAGMTDKIKKEVTFENFKVGFSRKMKPKPVQVPGGVVLVDDTFTIK
|
2.7.7.7; 3.1.11.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:1310035, ECO:0000269|PubMed:15608377, ECO:0000269|PubMed:17611604, ECO:0000269|PubMed:9784372};
|
DNA replication [GO:0006260]; viral DNA genome replication [GO:0039693]
| null |
DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exonuclease activity [GO:0004527]; metal ion binding [GO:0046872]; nucleoside binding [GO:0001882]; nucleotide binding [GO:0000166]
|
PF03175;
|
1.10.287.690;3.90.1600.10;3.30.420.10;3.30.1770.10;
|
DNA polymerase type-B family
| null | null |
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000269|PubMed:3863101};
| null | null | null | null |
FUNCTION: Polymerase responsible for protein-primed viral DNA replication by strand displacement with high processivity and fidelity (PubMed:2498321, PubMed:3863101). To start replication, the DNA polymerase forms a heterodimer with a free primer terminal protein (TP), recognizes the replication origins at both 5' ends of the linear chromosome, and initiates replication using as primer the OH-group of Ser-232 of the TP (PubMed:22210885). This polymerase possesses three enzymatic activities: DNA synthesis (polymerase), primer terminal protein (TP) deoxynucleotidylation, which is the formation of a covalent linkage (phosphoester) between the hydroxyl group of a specific serine residue in TP and 5'-dAMP, a reaction directed by the second T at the 3' end, and 3' to 5' exonuclease activity (PubMed:2790959). Exonuclease activity has a proofreading purpose (PubMed:2790959). DNA polymerase edits the polymerization errors using an intramolecular pathway as the primer terminus travels from one active site to the other without dissociation from the DNA (PubMed:10493855). DNA polymerization catalyzed by the DNA polymerase is a highly accurate process, but the protein-primed initiation is a quite inaccurate reaction (PubMed:8428945). Since the polymerase initiates the replication on the second thymine, the TP-dAMP initiation product translocates backwards to recover the template information of the first nucleotide (sliding back-mechanism) (PubMed:19011105). {ECO:0000269|PubMed:10493855, ECO:0000269|PubMed:1730646, ECO:0000269|PubMed:19011105, ECO:0000269|PubMed:22210885, ECO:0000269|PubMed:2498321, ECO:0000269|PubMed:2790959, ECO:0000269|PubMed:3863101, ECO:0000269|PubMed:8428945, ECO:0000269|PubMed:9171364}.
|
Bacillus phage phi29 (Bacteriophage phi-29)
|
P03681
|
TERM_BPPH2
|
MARSPRIRIKDNDKAEYARLVKNTKAKIARTKKKYGVDLTAEIDIPDLDSFETRAQFNKWKEQASSFTNRANMRYQFEKNAYGVVASKAKIAEIERNTKEVQRLVDEKIKAMKDKEYYAGGKPQGTIEQRIAMTSPAHVTGINRPHDFDFSKVRSYSRLRTLEESMEMRTDPQYYEKKMIQLQLNFIKSVEGSFNSFDAADELIEELKKIPPDDFYELFLRISEISFEEFDSEGNTVENVEGNVYKILSYLEQYRRGDFDLSLKGF
| null | null |
DNA replication, synthesis of RNA primer [GO:0006269]; symbiont entry into host cell via disruption of host cell envelope [GO:0098994]; symbiont entry into host cell via disruption of host cell wall peptidoglycan [GO:0098932]; viral DNA genome packaging [GO:0019073]; viral DNA genome replication [GO:0039693]
|
host cell nucleus [GO:0042025]; viral terminase complex [GO:0043493]; virion component [GO:0044423]
|
DNA binding [GO:0003677]; hydrolase activity [GO:0016787]
|
PF05435;
|
6.10.250.960;1.20.1270.230;
|
Phi29likevirus DNA terminal protein family
| null |
SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:14763988}. Host nucleus {ECO:0000269|PubMed:23091024}. Note=Associates with the host bacterial nucleoid through its N-terminal region. {ECO:0000269|PubMed:20823229}.
| null | null | null | null | null |
FUNCTION: Acts as a primer for DNA elongation during viral genomic replication (PubMed:6813861). Acts as the small terminase protein during packaging (PubMed:18674782). Recruits the phage DNA polymerase to the bacterial nucleoid (PubMed:20823229). Primer terminal protein (TP) is covalently linked to the 5'-ends of both strands of the genome through a phosphodiester bond between the beta-hydroxyl group of a serine residue and the 5'-phosphate of the terminal deoxyadenylate (dAMP) (PubMed:6813861). To start replication, the DNA polymerase forms a heterodimer with a free TP that recognizes the replication origins at both 5' ends of the linear chromosome, and initiates replication using as primer the OH-group of Ser-232 of the TP (PubMed:22210885, PubMed:25081208). Since the polymerase initiates the replication on the second thymine, the TP-dAMP initiation product slides backwards to recover the template information of the first nucleotide (PubMed:19011105). {ECO:0000269|PubMed:18674782, ECO:0000269|PubMed:19011105, ECO:0000269|PubMed:20823229, ECO:0000269|PubMed:22210885, ECO:0000269|PubMed:25081208, ECO:0000269|PubMed:6813861}.; FUNCTION: Hydrolyzes host peptidoglycans during virus entry. {ECO:0000269|PubMed:14763988}.
|
Bacillus phage phi29 (Bacteriophage phi-29)
|
P03685
|
NP_BPPH2
|
MAKMMQREITKTTVNVAKMVMVDGEVQVEQLPSETFVGNLTMEQAQWRMKRKYKGEPVQVVSVEPNTEVYELPVEKFLEVATVRVEKDEDQEEQTEAPEEQVAE
| null | null |
chromosome condensation [GO:0030261]; DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; regulation of viral transcription [GO:0046782]; viral DNA genome replication [GO:0039693]
|
transcription repressor complex [GO:0017053]
|
DNA binding [GO:0003677]; DNA-binding transcription repressor activity [GO:0001217]
|
PF17548;
| null |
Phi29likevirus histone-like protein p6 family
| null | null | null | null | null | null | null |
FUNCTION: Histone-like nucleoprotein that binds to the viral dsDNA and responsible for wrapping and compacting the viral DNA about 4-fold. Forms a nucleoprotein complex in which the DNA adopts a right-handed toroidal conformation winding around a protein core. Binds ito most, if not all, the viral genome, although with different affinity, the highest one corresponding to the genome ends. The formation of the nucleoprotein complex at the genome ends, activates the initiation of viral DNA replication. The binding of p6 would recruit the complex formed by the TP and the DNA polymerase to the origin. Protein p6 also represses early transcription from promoter C2, and, together with protein p4, represses transcription from promoters A2b and A2c and activates late transcription from promoter A3. Protein p6 is therefore involved in the early to late transcription switch. The formation of the nucleoprotein complex at the right end of the phage genome where the early promoter C2 is located affects local topology, which may contribute to the promoter repression. {ECO:0000269|PubMed:11384991, ECO:0000269|PubMed:12426390, ECO:0000269|PubMed:15118076, ECO:0000269|PubMed:15247336, ECO:0000269|PubMed:2111580}.
|
Bacillus phage phi29 (Bacteriophage phi-29)
|
P03692
|
HELIC_BPT7
|
MDNSHDSDSVFLYHIPCDNCGSSDGNSLFSDGHTFCYVCEKWTAGNEDTKERASKRKPSGGKPMTYNVWNFGESNGRYSALTARGISKETCQKAGYWIAKVDGVMYQVADYRDQNGNIVSQKVRDKDKNFKTTGSHKSDALFGKHLWNGGKKIVVTEGEIDMLTVMELQDCKYPVVSLGHGASAAKKTCAANYEYFDQFEQIILMFDMDEAGRKAVEEAAQVLPAGKVRVAVLPCKDANECHLNGHDREIMEQVWNAGPWIPDGVVSALSLRERIREHLSSEESVGLLFSGCTGINDKTLGARGGEVIMVTSGSGMGKSTFVRQQALQWGTAMGKKVGLAMLEESVEETAEDLIGLHNRVRLRQSDSLKREIIENGKFDQWFDELFGNDTFHLYDSFAEAETDRLLAKLAYMRSGLGCDVIILDHISIVVSASGESDERKMIDNLMTKLKGFAKSTGVVLVVICHLKNPDKGKAHEEGRPVSITDLRGSGALRQLSDTIIALERNQQGDMPNLVLVRILKCRFTGDTGIAGYMEYNKETGWLEPSSYSGEEESHSESTDWSNDTDF
|
2.7.7.-; 3.6.4.12
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_04154, ECO:0000269|PubMed:12769857}; Note=Binds 2 Mg(2+), one of which is catalytic. {ECO:0000255|HAMAP-Rule:MF_04154, ECO:0000269|PubMed:12769857, ECO:0000269|PubMed:30679383};
|
viral DNA genome replication [GO:0039693]
| null |
5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA helicase activity [GO:0003678]; DNA primase activity [GO:0003896]; identical protein binding [GO:0042802]; single-stranded DNA binding [GO:0003697]; zinc ion binding [GO:0008270]
|
PF03796;PF21268;PF08273;PF13155;
|
2.20.25.10;2.20.25.180;3.40.1360.10;3.40.50.300;
|
Teseptimavirus DNA helicase/primase family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000255|HAMAP-Rule:MF_04154, ECO:0000269|PubMed:2829184, ECO:0000269|PubMed:9185573};
| null | null | null | null |
FUNCTION: ATP-dependent DNA helicase and primase essential for viral DNA replication and recombination (PubMed:21606333, PubMed:22977246, PubMed:32009150). The helicase moves 5' -> 3' on the lagging strand template, unwinding the DNA duplex ahead of the leading strand polymerase at the replication fork and generating ssDNA for both leading and lagging strand synthesis (PubMed:21606333, PubMed:22977246, PubMed:32009150). ATP or dTTP hydrolysis propels each helicase domain to translocate 2 nt per step sequentially along DNA (PubMed:17604719, PubMed:30679383). Mediates strand transfer when a joint molecule is available and participates in recombinational DNA repair through its role in strand exchange (PubMed:8617248, PubMed:9096333). Primase activity synthesizes short RNA primers at the sequence 5'-GTC-3' on the lagging strand that the polymerase elongates using dNTPs and providing the primase is still present (PubMed:6454135, PubMed:9139692). {ECO:0000255|HAMAP-Rule:MF_04154, ECO:0000269|PubMed:17604719, ECO:0000269|PubMed:21606333, ECO:0000269|PubMed:22977246, ECO:0000269|PubMed:30679383, ECO:0000269|PubMed:32009150, ECO:0000269|PubMed:6454135, ECO:0000269|PubMed:8617248, ECO:0000269|PubMed:9096333, ECO:0000269|PubMed:9139692}.
|
Escherichia phage T7 (Bacteriophage T7)
|
P03705
|
HOLIN_LAMBD
|
MKMPEKHDLLAAILAAKEQGIGAILAFAMAYLRGRYNGGAFTKTVIDATMCAIIAWFIRDLLDFAGLSSNLAYITSVFIGYIGTDSIGSLIKRFAAKKAGVEDGRNQ
| null | null |
negative regulation of cytolysis [GO:0045918]; viral release from host cell by cytolysis [GO:0044659]
|
host cell plasma membrane [GO:0020002]; membrane [GO:0016020]
|
pore-forming activity [GO:0140911]
|
PF05106;
| null |
Lambdavirus holin family
| null |
SUBCELLULAR LOCATION: Host cell inner membrane {ECO:0000269|PubMed:2137120}; Multi-pass membrane protein {ECO:0000269|PubMed:19897658}. Note=Classified as a class I holin. {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: [Isoform Holin]: Accumulates harmlessly in the cytoplasmic membrane until it reaches a critical concentration that triggers the formation of micron-scale pores (holes) causing host cell membrane disruption and endolysin escape into the periplasmic space (PubMed:18788120, PubMed:21187415). Determines the precise timing of host cell lysis (PubMed:21187415). Participates with the endolysin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles from the host cell (PubMed:21187415). {ECO:0000269|PubMed:18788120, ECO:0000269|PubMed:21187415}.; FUNCTION: [Isoform Antiholin]: Counteracts the aggregation of the holin molecules and thus of pore formation. {ECO:0000269|PubMed:21187415, ECO:0000269|PubMed:2138979}.
|
Escherichia phage lambda (Bacteriophage lambda)
|
P03706
|
ENLYS_LAMBD
|
MVEINNQRKAFLDMLAWSEGTDNGRQKTRNHGYDVIVGGELFTDYSDHPRKLVTLNPKLKSTGAGRYQLLSRWWDAYRKQLGLKDFSPKSQDAVALQQIKERGALPMIDRGDIRQAIDRCSNIWASLPGAGYGQFEHKADSLIAKFKEAGGTVREIDV
|
4.2.2.n2
| null |
cell wall macromolecule catabolic process [GO:0016998]; defense response to bacterium [GO:0042742]; peptidoglycan catabolic process [GO:0009253]; viral release from host cell by cytolysis [GO:0044659]
|
host cell cytoplasm [GO:0030430]
|
lysozyme activity [GO:0003796]; lytic transglycosylase activity [GO:0008933]
|
PF00959;
|
1.10.530.10;
|
Glycosyl hydrolase 24 family
| null |
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04109}. Note=The endolysin is cytoplasmic, but can reach the periplasmic space with the help of the holins which disrupt the host cell membrane. {ECO:0000255|HAMAP-Rule:MF_04109, ECO:0000305|PubMed:24113139}.
|
CATALYTIC ACTIVITY: Reaction=Endolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n2; Evidence={ECO:0000255|HAMAP-Rule:MF_04109, ECO:0000269|PubMed:10556513, ECO:0000269|PubMed:6448076};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.6. {ECO:0000269|PubMed:6448076};
| null |
FUNCTION: Endolysin with transglycosylase activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer. {ECO:0000255|HAMAP-Rule:MF_04109, ECO:0000305|PubMed:10556513, ECO:0000305|PubMed:24113139}.
|
Escherichia phage lambda (Bacteriophage lambda)
|
P03707
|
TERS_LAMBD
|
MEVNKKQLADIFGASIRTIQNWQEQGMPVLRGGGKGNEVLYDSAAVIKWYAERDAEIENEKLRREVEELRQASEADLQPGTIEYERHRLTRAQADAQELKNARDSAEVVETAFCTFVLSRIAGEIASILDGLPLSVQRRFPELENRHVDFLKRDIIKAMNKAAALDELIPGLLSEYIEQSG
|
3.6.4.-
| null |
viral DNA genome packaging [GO:0019073]
|
host cell cytoplasm [GO:0030430]; viral terminase, small subunit [GO:0097710]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; sequence-specific DNA binding, bending [GO:0044374]
|
PF07471;
|
1.10.10.10;
|
Terminase small subunit family
| null |
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}. Note=The terminase lies at a unique vertex of the procapsid during viral DNA packaging. {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:2965248, ECO:0000269|PubMed:8611586};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=469 uM for ATP {ECO:0000269|PubMed:8611586};
| null | null | null |
FUNCTION: The small subunit is responsible for the binding to multiple recognition elements within the packaging initiation site cos (PubMed:15755448, PubMed:16618107, PubMed:2989542). The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (binding to packaging sequence cos), and a large terminase subunit possessing endonucleolytic, ATPase and helicase activities (DNA maturation and packaging) (Probable). The terminase binds, cooperatively with the host factor IHFA/IHFB, to the cos site at the junction of adjacent viral genomes in the concatemeric DNA (PubMed:16618107). The endonuclease and helicase activities of the large subunit cleave the viral DNA generating 5'overhangs of 12 bp in length (Probable). The terminase remains bound to the left end of the genome to be packaged, forming a stable DNA-terminase complex (Probable). In a reaction facilitated by the viral assembly catalyst gpFI, the DNA-terminase complex binds to the portal of the procapsid and the terminase packages the viral DNA into the procapsid until the next cos site on the concatemer reaches the complex (Probable). The downstream cos site is then cut generating the mature right end of the genome, the heterotrimer undocks from the DNA-filled head and remains bound to the left end of concatemer's next genome (Probable). {ECO:0000269|PubMed:15755448, ECO:0000269|PubMed:16618107, ECO:0000269|PubMed:2989542, ECO:0000305}.
|
Escherichia phage lambda (Bacteriophage lambda)
|
P03708
|
TERL_LAMBD
|
MNISNSQVNRLRHFVRAGLRSLFRPEPQTAVEWADANYYLPKESAYQEGRWETLPFQRAIMNAMGSDYIREVNVVKSARVGYSKMLLGVYAYFIEHKQRNTLIWLPTDGDAENFMKTHVEPTIRDIPSLLALAPWYGKKHRDNTLTMKRFTNGRGFWCLGGKAAKNYREKSVDVAGYDELAAFDDDIEQEGSPTFLGDKRIEGSVWPKSIRGSTPKVRGTCQIERAASESPHFMRFHVACPHCGEEQYLKFGDKETPFGLKWTPDDPSSVFYLCEHNACVIRQQELDFTDARYICEKTGIWTRDGILWFSSSGEEIEPPDSVTFHIWTAYSPFTTWVQIVKDWMKTKGDTGKRKTFVNTTLGETWEAKIGERPDAEVMAERKEHYSAPVPDRVAYLTAGIDSQLDRYEMRVWGWGPGEESWLIDRQIIMGRHDDEQTLLRVDEAINKTYTRRNGAEMSISRICWDTGGIDPTIVYERSKKHGLFRVIPIKGASVYGKPVASMPRKRNKNGVYLTEIGTDTAKEQIYNRFTLTPEGDEPLPGAVHFPNNPDIFDLTEAQQLTAEEQVEKWVDGRKKILWDSKKRRNEALDCFVYALAALRISISRWQLDLSALLASLQEEDGAATNKKTLADYARALSGEDE
|
3.1.21.4; 3.6.4.-; 3.6.4.12
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_04144, ECO:0000269|PubMed:8175794, ECO:0000269|PubMed:8428984}; Note=Probably binds 2 Mg(2+) ions per subunit (By similarity). Necessary for the ATPase activity (PubMed:8175794, PubMed:8428984). Zn(2+) Co(2+), Cd(2+), Cu(2+), Ca(2+), Sr(2+) and Ba(2+) do not function as cofactor (PubMed:8428984). {ECO:0000250|UniProtKB:P0A7Y4, ECO:0000269|PubMed:8175794, ECO:0000269|PubMed:8428984};
|
viral DNA genome packaging [GO:0019073]
|
host cell cytoplasm [GO:0030430]; viral terminase, large subunit [GO:0098009]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA helicase activity [GO:0003678]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; type II site-specific deoxyribonuclease activity [GO:0009036]
|
PF05876;PF20454;
|
3.40.50.300;
|
Lambdavirus large terminase family
| null |
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04144}. Note=The terminase lies at a unique vertex of the procapsid during viral DNA packaging. {ECO:0000255|HAMAP-Rule:MF_04144}.
|
CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4; Evidence={ECO:0000255|HAMAP-Rule:MF_04144, ECO:0000269|PubMed:1534952, ECO:0000269|PubMed:17870092, ECO:0000269|PubMed:23134123, ECO:0000269|PubMed:2970303, ECO:0000269|PubMed:7813453}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000255|HAMAP-Rule:MF_04144, ECO:0000269|PubMed:10993723, ECO:0000269|PubMed:11866517, ECO:0000269|PubMed:23134123, ECO:0000269|PubMed:30541105, ECO:0000269|PubMed:8175794, ECO:0000269|PubMed:8428984, ECO:0000269|PubMed:8794874};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.6 uM for ATP for the high affinity ATPase {ECO:0000269|PubMed:8428984, ECO:0000269|PubMed:8611586, ECO:0000269|PubMed:8794874}; KM=23 uM for ATP for helicase {ECO:0000269|PubMed:8175794}; Note=The high affinity ATPase activity corresponds to the packaging ATPase site at the N-terminus. {ECO:0000269|PubMed:11866517, ECO:0000303|PubMed:17870092};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-9.0 for the ATPase and helicase. {ECO:0000269|PubMed:8175794};
| null |
FUNCTION: The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome from the concetamer to initiate and to end the packaging reaction (PubMed:11866517, PubMed:23134123). The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (binding to packaging sequence cos), and a large terminase subunit possessing endonucleolytic, ATPase and helicase activities (DNA maturation and packaging) (PubMed:11866517, PubMed:23134123). The terminase binds cooperatively with the host factor IHFA/IHFB to the cos site at the junction of adjacent viral genomes (PubMed:15755448, PubMed:22191393, PubMed:28445747). The endonuclease activity cleaves the viral DNA generating 5'overhangs of 12 bp in length (PubMed:2970303, PubMed:6315731, PubMed:7813453, PubMed:8428984). The helicase activity separates the cohesive ends generating the single-stranded 'sticky' ends of the mature genome (PubMed:2970303, PubMed:6315731, PubMed:8175794). IHFA/IHFB is also necessary for the strand separation activity of the terminase (PubMed:22191393). The terminase remains bound to the left end of the genome to be packaged, forming a stable DNA-terminase complex (PubMed:860405). In a reaction facilitated by the viral assembly catalyst gpFI, the DNA-terminase complex binds to the portal of the procapsid thereby activating the translocase activity of the terminase (PubMed:2965251). The terminase packages the viral DNA into the procapsid until the next cos site on the concatemer reaches the complex (Probable) (PubMed:2965251, PubMed:860405). The downstream cos site is then cut generating the mature right end of the genome, the heterotrimer undocks from the DNA-filled head and remains bound to the left end of concatemer's next genome (PubMed:2970303). {ECO:0000255|HAMAP-Rule:MF_04144, ECO:0000269|PubMed:11866517, ECO:0000269|PubMed:15755448, ECO:0000269|PubMed:22191393, ECO:0000269|PubMed:23134123, ECO:0000269|PubMed:28445747, ECO:0000269|PubMed:2965251, ECO:0000269|PubMed:2970303, ECO:0000269|PubMed:6315731, ECO:0000269|PubMed:7813453, ECO:0000269|PubMed:8175794, ECO:0000269|PubMed:8428984, ECO:0000269|PubMed:860405, ECO:0000305|PubMed:11866517}.
|
Escherichia phage lambda (Bacteriophage lambda)
|
P03711
|
SCAF_LAMBD
|
MTAELRNLPHIASMAFNEPLMLEPAYARVFFCALAGQLGISSLTDAVSGDSLTAQEALATLALSGDDDGPRQARSYQVMNGIAVLPVSGTLVSRTRALQPYSGMTGYNGIIARLQQAASDPMVDGILLDMDTPGGMVAGAFDCADIIARVRDIKPVWALANDMNCSAGQLLASAASRRLVTQTARTGSIGVMMAHSNYGAALEKQGVEITLIYSGSHKVDGNPYSHLPDDVRETLQSRMDATRQMFAQKVSAYTGLSVQVVLDTEAAVYSGQEAIDAGLADELVNSTDAITVMRDALDARKSRLSGGRMTKETQSTTVSATASQADVTDVVPATEGENASAAQPDVNAQITAAVAAENSRIMGILNCEEAHGREEQARVLAETPGMTVKTARRILAAAPQSAQARSDTALDRLMQGAPAPLAAGNPASDAVNDLLNTPV
|
3.4.21.-
| null |
proteolysis [GO:0006508]; viral procapsid maturation [GO:0046797]
|
host cell cytoplasm [GO:0030430]; viral capsid [GO:0019028]
|
identical protein binding [GO:0042802]; serine-type peptidase activity [GO:0008236]
|
PF01343;
|
6.20.330.10;
|
Peptidase S49 family
| null |
SUBCELLULAR LOCATION: [Isoform Capsid assembly protease C]: Virion. Host cytoplasm.; SUBCELLULAR LOCATION: [Isoform Capsid scaffolding protein Nu3]: Host cytoplasm.
| null | null | null | null | null |
FUNCTION: Assembly protease promotes icosahedral procapsid assembly. Autocatalytic cleavage may release the capsid scaffolding protein. The protease domain catalyzes the cleavage of the capsid scaffolding protein after complete procapsid formation. Assembly protease and cleavages products are evicted from the capsid before or during DNA packaging.; FUNCTION: Scaffolding protein Nu3 promotes icosahedral procapsid assembly. Acts by binding the major capsid protein gpE and multimerizing in interaction with portal dodecamer, thereby placing gpE in a context facilitating icosahedral procapsid formation. Cleaved by capsid assembly protease C after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging.
|
Escherichia phage lambda (Bacteriophage lambda)
|
P03726
|
EXLYS_BPT7
|
MDKYDKNVPSDYDGLFQKAADANGVSYDLLRKVAWTESRFVPTAKSKTGPLGMMQFTKATAKALGLRVTDGPDDDRLNPELAINAAAKQLAGLVGKFDGDELKAALAYNQGEGRLGNPQLEAYSKGDFASISEEGRNYMRNLLDVAKSPMAGQLETFGGITPKGKGIPAEVGLAGIGHKQKVTQELPESTSFDVKGIEQEATAKPFAKDFWETHGETLDEYNSRSTFFGFKNAAEAELSNSVAGMAFRAGRLDNGFDVFKDTITPTRWNSHIWTPEELEKIRTEVKNPAYINVVTGGSPENLDDLIKLANENFENDSRAAEAGLGAKLSAGIIGAGVDPLSYVPMVGVTGKGFKLINKALVVGAESAALNVASEGLRTSVAGGDADYAGAALGGFVFGAGMSAISDAVAAGLKRSKPEAEFDNEFIGPMMRLEARETARNANSADLSRMNTENMKFEGEHNGVPYEDLPTERGAVVLHDGSVLSASNPINPKTLKEFSEVDPEKAARGIKLAGFTEIGLKTLGSDDADIRRVAIDLVRSPTGMQSGASGKFGATASDIHERLHGTDQRTYNDLYKAMSDAMKDPEFSTGGAKMSREETRYTIYRRAALAIERPELQKALTPSERIVMDIIKRHFDTKRELMENPAIFGNTKAVSIFPESRHKGTYVPHVYDRHAKALMIQRYGAEGLQEGIARSWMNSYVSRPEVKARVDEMLKELHGVKEVTPEMVEKYAMDKAYGISHSDQFTNSSIIEENIEGLVGIENNSFLEARNLFDSDLSITMPDGQQFSVNDLRDFDMFRIMPAYDRRVNGDIAIMGSTGKTTKELKDEILALKAKAEGDGKKTGEVHALMDTVKILTGRARRNQDTVWETSLRAINDLGFFAKNAYMGAQNITEIAGMIVTGNVRALGHGIPILRDTLYKSKPVSAKELKELHASLFGKEVDQLIRPKRADIVQRLREATDTGPAVANIVGTLKYSTQELAARSPWTKLLNGTTNYLLDAARQGMLGDVISATLTGKTTRWEKEGFLRGASVTPEQMAGIKSLIKEHMVRGEDGKFTVKDKQAFSMDPRAMDLWRLADKVADEAMLRPHKVSLQDSHAFGALGKMVMQFKSFTIKSLNSKFLRTFYDGYKNNRAIDAALSIITSMGLAGGFYAMAAHVKAYALPKEKRKEYLERALDPTMIAHAALSRSSQLGAPLAMVDLVGGVLGFESSKMARSTILPKDTVKERDPNKPYTSREVMGAMGSNLLEQMPSAGFVANVGATLMNAAGVVNSPNKATEQDFMTGLMNSTKELVPNDPLTQQLVLKIYEANGVNLRERRK
|
4.2.2.n1
| null |
defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640]; peptidoglycan metabolic process [GO:0000270]; symbiont entry into host [GO:0044409]; symbiont entry into host cell via disruption of host cell envelope [GO:0098994]; symbiont entry into host cell via disruption of host cell wall peptidoglycan [GO:0098932]; symbiont genome ejection through host cell envelope [GO:0039678]; symbiont genome ejection through host cell envelope, short tail mechanism [GO:0099002]
|
host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423]
|
hydrolase activity [GO:0016787]; lytic transglycosylase activity [GO:0008933]
|
PF01464;
|
1.10.530.10;
|
Transglycosylase Slt family
| null |
SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04121, ECO:0000269|PubMed:23884409}. Host cell inner membrane {ECO:0000255|HAMAP-Rule:MF_04121, ECO:0000269|PubMed:23306440}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04121}. Note=The gp15-gp16 complex spans the periplasm and the cytoplasmic membrane. {ECO:0000255|HAMAP-Rule:MF_04121, ECO:0000269|PubMed:23306440}.
|
CATALYTIC ACTIVITY: Reaction=Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n1; Evidence={ECO:0000255|HAMAP-Rule:MF_04121, ECO:0000269|PubMed:14763988};
| null | null | null | null |
FUNCTION: Component of the cylindrical core that assembles on the inner surface of the capsid during capsid formation and plays a role in viral DNA ejection into the host cell. The inner core is composed of stacked rings of gp14, gp15 and gp16 proteins. Following binding to the host cell surface, the internal core is diassembled and gp16 is ejected along with gp14 and gp15 into the infected cell. Gp16 probably inserts in the host inner membrane and remains associated with gp15. The gp15-gp16 complex binds to both the viral DNA and the host inner membrane, probably escorting the leading end of the genome through the periplasm and controlling the extend of DNA translocated into the host cell. Functions as an exolysin that catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycans allowing the local digestion of the bacterial peptidoglycan wall. {ECO:0000255|HAMAP-Rule:MF_04121, ECO:0000269|PubMed:10926491, ECO:0000269|PubMed:14763988, ECO:0000269|PubMed:20036409, ECO:0000269|PubMed:26476287}.
|
Escherichia phage T7 (Bacteriophage T7)
|
P03763
|
TARGB_BPMU
|
MNISDIRAGLRTLVENEETTFKQIALESGLSTGTISSFINDKYNGDNERVSQMLQRWLEKYHAVAELPEPPRFVETQTVKQIWTSMRFASLTESIAVVCGNPGVGKTEAAREYRRTNNNVWMITITPSCASVLECLTELAFELGMNDAPRRKGPLSRALRRRLEGTQGLVIIDEADHLGAEVLEELRLLQESTRIGLVLMGNHRVYSNMTGGNRTVEFARLFSRIAKRTAINKTKKADVKAIADAWQINGEKELELLQQIAQKPGALRILNHSLRLAAMTAHGKGERVNEDYLRQAFRELDLDVDISTLLRN
|
3.6.1.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:23776210};
|
DNA integration [GO:0015074]; DNA replication [GO:0006260]; DNA transposition [GO:0006313]; viral DNA genome replication [GO:0039693]
|
host cell cytoplasm [GO:0030430]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; metal ion binding [GO:0046872]
|
PF13401;PF09077;
|
1.10.1180.10;1.10.260.40;3.40.50.300;
|
AAA ATPase family
| null |
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:23776210};
| null | null | null | null |
FUNCTION: Selects the target DNA sites for transposition. Recruits DDE-recombinase A to the target sites and catalytically activates it. Displays non-specific DNA-binding properties. Polymerizes as helical filaments around the DNA. Coating of the DNA by the target DNA activator B might play a role in favoring target-primed replication over integration. Prevents self-integration into an integrated copy of the viral genome. This mechanism is called target immunity and is achieved by two mechanisms: first, the target DNA activator B dissociates from the viral genome ends upon interaction in cis with DDE-recombinase A, which makes the viral genome ends a poor target for new insertions. Second, the interior of the viral genome may also be protected from integration events by the target DNA activator B being strongly bound throughout the whole viral genome. {ECO:0000269|PubMed:11298282, ECO:0000269|PubMed:14661976, ECO:0000269|PubMed:1646076, ECO:0000269|PubMed:17709741, ECO:0000269|PubMed:17988683, ECO:0000269|PubMed:20226074, ECO:0000269|PubMed:23776210, ECO:0000269|PubMed:24478936}.
|
Escherichia phage Mu (Bacteriophage Mu)
|
P03819
|
KEFC_ECOLI
|
MDSHTLIQALIYLGSAALIVPIAVRLGLGSVLGYLIAGCIIGPWGLRLVTDAESILHFAEIGVVLMLFIIGLELDPQRLWKLRAAVFGCGALQMVICGGLLGLFCMLLGLRWQVAELIGMTLALSSTAIAMQAMNERNLMVTQMGRSAFAVLLFQDIAAIPLVAMIPLLATSSASTTMGAFALSALKVAGALVLVVLLGRYVTRPALRFVARSGLREVFSAVALFLVFGFGLLLEEVGLSMAMGAFLAGVLLASSEYRHALESDIEPFKGLLLGLFFIGVGMSIDFGTLLENPLRIVILLLGFLIIKIAMLWLIARPLQVPNKQRRWFAVLLGQGSEFAFVVFGAAQMANVLEPEWAKSLTLAVALSMAATPILLVILNRLEQSSTEEAREADEIDEEQPRVIIAGFGRFGQITGRLLLSSGVKMVVLDHDPDHIETLRKFGMKVFYGDATRMDLLESAGAAKAEVLINAIDDPQTNLQLTEMVKEHFPHLQIIARARDVDHYIRLRQAGVEKPERETFEGALKTGRLALESLGLGPYEARERADVFRRFNIQMVEEMAMVENDTKARAAVYKRTSAMLSEIITEDREHLSLIQRHGWQGTEEGKHTGNMADEPETKPSS
| null | null |
intracellular pH elevation [GO:0051454]; potassium ion transport [GO:0006813]; proton transmembrane transport [GO:1902600]; regulation of intracellular pH [GO:0051453]; regulation of pH [GO:0006885]; response to hydrogen peroxide [GO:0042542]; response to methylglyoxal [GO:0051595]; response to toxic substance [GO:0009636]
|
membrane [GO:0016020]; plasma membrane [GO:0005886]; potassium:proton antiporter complex [GO:1903103]
|
antiporter activity [GO:0015297]; enzyme binding [GO:0019899]; glutathione-regulated potassium exporter activity [GO:0015503]; nucleotide binding [GO:0000166]; protein homodimerization activity [GO:0042803]; toxic substance binding [GO:0015643]
|
PF00999;PF02254;
|
1.20.1530.20;3.40.50.720;
|
Monovalent cation:proton antiporter 2 (CPA2) transporter (TC 2.A.37) family, KefC subfamily
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01413, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2046548}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01413, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2046548}.
| null | null | null | null | null |
FUNCTION: Pore-forming subunit of a potassium efflux system that confers protection against electrophiles. Catalyzes K(+)/H(+) antiport. Can also export rubidium, lithium and sodium. {ECO:0000255|HAMAP-Rule:MF_01413, ECO:0000269|PubMed:17679694, ECO:0000269|PubMed:21041667, ECO:0000269|PubMed:9023177}.
|
Escherichia coli (strain K12)
|
P03870
|
FLP_YEAST
|
MPQFGILCKTPPKVLVRQFVERFERPSGEKIALCAAELTYLCWMITHNGTAIKRATFMSYNTIISNSLSFDIVNKSLQFKYKTQKATILEASLKKLIPAWEFTIIPYYGQKHQSDITDIVSSLQLQFESSEEADKGNSHSKKMLKALLSEGESIWEITEKILNSFEYTSRFTKTKTLYQFLFLATFINCGRFSDIKNVDPKSFKLVQNKYLGVIIQCLVTETKTSVSRHIYFFSARGRIDPLVYLDEFLRNSEPVLKRVNRTGNSSSNKQEYQLLKDNLVRSYNKALKKNAPYSIFAIKNGPKSHIGRHLMTSFLSMKGLTELTNVVGNWSDKRASAVARTTYTHQITAIPDHYFALVSRYYAYDPISKEMIALKDETNPIEEWQHIEQLKGSAEGSIRYPAWNGIISQEVLDYLSSYINRRI
| null | null |
plasmid recombination [GO:0042150]
| null |
DNA binding, bending [GO:0008301]; double-stranded DNA binding [GO:0003690]; single-stranded DNA binding [GO:0003697]; site-specific recombinase activity [GO:0009009]
|
PF05202;PF03930;
|
3.30.300.80;1.10.443.10;
|
'phage' integrase family
| null | null | null | null | null | null | null |
FUNCTION: Part of the plasmid amplification system, which corrects any decrease in copy number caused by a rare missegregation event. Catalyzes the recombination between the large inverted repetitions of the 2-micron plasmid during plasmid replication. This recombination event changes the direction of one of the two replication forks in the bidirectionally replicating molecule, effectively resulting in multiple rounds of replication from a single initiation event. Binds specifically to the FLP recognition target (FRT) site where it induces DNA to bend. Three types of bend exist. Type I is approximately 60 degrees and results from 1 FLP molecule binding to 1 symmetry element. Type II is >144 degrees and results from FLP molecules binding to symmetry elements a and b. Type III is approximately 65 degrees and results from FLP molecules binding to symmetry elements b and c. {ECO:0000269|PubMed:2040639, ECO:0000269|PubMed:2254930, ECO:0000269|PubMed:3316982}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P03871
|
REP1_YEAST
|
MNGERLLACIKQCIMQHFQPMVYDESRCVIETTRGTFPVPDNYKKYKTLAFAFVGHVLNTDDTPVIEKELDWPDPALVYNTIVDRIINHPELSQFISVAFISQLKATIGEGLDINVKGTLNRRGKGIRRPKGVFFRYMESPFVNTKVTAFFSYLRDYNKIASEYHNNTKFILTFSCQAYWASGPNFSALKNVIRCSIIHEYISKFVEREQDKGHIGDQELPPEEDPSRELNNVQHEVNSLTEQDAEADEGLWGEIDSLCEKWQSEAEDQTEAEIIADRIIGNSQRMANLKIRRTKFKSVLYHILKELIQSQGTVKVYRGSSFSHDSIKISLHYEEQHITAVWVYLTVKFEEHWKPVDVEVEFRCKFKERKVDG
| null | null |
2-micrometer plasmid partitioning [GO:0030543]; protein localization [GO:0008104]
|
nucleus [GO:0005634]
|
identical protein binding [GO:0042802]
|
PF05797;
| null | null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10791970, ECO:0000269|PubMed:9393716, ECO:0000269|PubMed:9819432}. Note=Colocalizes with the STB locus of the 2-micron plasmid as foci in the nucleus near the spindle pole body. Is expelled from STB during a short interval between late G1 and early S phases.
| null | null | null | null | null |
FUNCTION: Part of the plasmid partitioning system, which ensures the equal distribution of replicated plasmid molecules to daughter cells. The plasmids exist as well-organized plasmid foci within the nucleus that stay together throughout the cell-cycle and act as entity during segregation, effetively reducing copy number to one. Plasmid partitioning requires the proteins REP1, REP2, and a cis-acting locus STB (REP3). REP1-REP2 stably associate with CSE4-containing chromatin at STB during S-phase, marking the locus with a centromeric tag, and thereby probably catching mitotic spindle microtubules to the plasmid cluster and coupling plasmid segregation to chromosome segregation. REP1-REP2 are required to recruit the cohesin complex to the STB locus for pairing of the replicated plasmid cluster, a prerequisite for successful plasmid segregation. REP1-REP2 also negatively regulate expression of site-specific recombinase FLP and of RAF1. {ECO:0000269|PubMed:10791970, ECO:0000269|PubMed:12177044, ECO:0000269|PubMed:15169893, ECO:0000269|PubMed:16966420, ECO:0000269|PubMed:2832156}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P03873
|
MBI2_YEAST
|
MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVIIFILTIATAFLGYCCVYGQMSHWGNMNIASNMFNMMKTIYMMMLMLLIYIFYTIMMRQMMKTKEYTMLIKSMDYINKNKYMINLNMTNKKDMNNNIGPLNMNILSIIYGSMLGDGHAEKRKGGKGTRIVFQQEYCNINYLYYLHSLLANLGYCNTNLPLIKTRLGKKGKIRQYLKFNTWTYDSFNMIYSEWYIKNMSGKGNIKVIPKSLDNYLTPLALAIWIMDDGCKLGKGLKFTTNCFSYKDVQYLTYLLHNKYNIKSTITKGNKENTQFVIYVWKESMPILTKIVSPYIIPSMKYKLGNYL
| null | null |
mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; mRNA processing [GO:0006397]; RNA splicing [GO:0008380]
|
mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739]
|
endonuclease activity [GO:0004519]; nuclease activity [GO:0004518]; ubiquinol-cytochrome-c reductase activity [GO:0008121]
|
PF00033;PF03161;
|
3.10.28.10;
|
Cytochrome b family; LAGLIDADG endonuclease family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: This protein is responsible for splicing and maturation of cytochrome b mRNA. Specifically, it may be responsible for the splicing specificity of the second intron. {ECO:0000269|PubMed:11016843, ECO:0000269|PubMed:7004642, ECO:0000269|PubMed:8670880}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P03877
|
SCE3_YEAST
|
MVQRWLYSTNAKDIAVLYFMLAIFSGMAGTAMSLIIRLELAAPGSQYLHGNSQLFNVLVVGHAVLMIFFLVMPALIGGFGNQKRYESNNNNNQVMENKEYNLKLNYDKLGPYLAGLIEGDGTITVQNSSSMKKSKYRPLIVVVFKLEDLELANYLCNLTKCGKVYKKINRNYVLWTIHDLKGVYTLLNIINGYMRTPKYEAFVRGAEFMNNYINSTTITHNKLKNMDNIKIKPLDTSDIGSNAWLAGMTDADGNFSINLMNGKNRSSRAMPYYCLELRQNYQKNSNNNNINFSYFYIMSAIATYFNVNLYSRERNLNLLVSTNNTYKTYYSYKVMVANTYKNIKVMEYFNKYSLLSSKHLDFLDWSKLVILINNEGQSMKTNGSWELGMNLRKDYNKTRTTFTWSHLKNTYLENK
|
3.1.-.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:8367285};
|
electron transport coupled proton transport [GO:0015990]; intron homing [GO:0006314]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mRNA processing [GO:0006397]; RNA splicing [GO:0008380]
|
mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739]
|
cytochrome-c oxidase activity [GO:0004129]; endonuclease activity [GO:0004519]; heme binding [GO:0020037]
|
PF00115;PF00961;
|
1.20.210.10;3.10.28.10;
|
LAGLIDADG endonuclease family
|
PTM: The mature protein may arise from proteolytic cleavage of an in-frame translation of some COX1 exons plus the intron containing the aI3 open reading frame. {ECO:0000269|PubMed:7797552, ECO:0000269|PubMed:8367285}.
|
SUBCELLULAR LOCATION: Mitochondrion. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
| null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:8367285};
| null |
FUNCTION: Mitochondrial DNA endonuclease involved in intron homing. It introduces a specific double-strand break in the DNA of the COX1 gene and thus mediates the insertion of an intron, containing its own coding sequence (group I intron), into an intronless gene. Recognizes with high specificity and cleaves the sequence 5'-GGTTTTGGTAACTATTTATTAC-3'. {ECO:0000269|PubMed:7797552, ECO:0000269|PubMed:8367285}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P03878
|
SCE2_YEAST
|
MVQRWLYSTNAKDIAVLYFMLAIFSGMAGTAMSLIIRLELAAPGSQYLHGNSQLFNVLVVGHAVLMIFFLVMPALIGGFGNYLLPLMIGATDTAFPRINNIAFWVLPMGLVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGAINFIVTTLNMRTNGMTMHKLPLFVWSIFITAFLLLLSLPVLSAGITMLLLDRNFNTSFFEVSGGGDPILYEHLFWFFGQTVATIIMLMMYNDMHFSKCWKLLKKWITNIMSTLFKALFVKMFMSYNNQQDKMMNNTMLKKDNIKRSSETTRKMLNNSMNKKFNQWLAGLIDGDGYFGIVSKKYVSLEITVALEDEMALKEIQNKFGGSIKLRSGVKAIRYRLTNKTGMIKLINAVNGNIRNTKRLVQFNKVCILLGIDFIYPIKLTKDNSWFVGFFDADGTINYSFKNNHPQLTISVTNKYLQDVQEYKNILGGNIYFDKSQNGYYKWSIQSKDMVLNFINDYIKMNPSRTTKMNKLYLSKEFYNLKELKAYNKSSDSMQYKAWLNFENKWKNK
|
3.1.-.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:2172241}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:2172241};
|
electron transport coupled proton transport [GO:0015990]; intron homing [GO:0006314]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mRNA processing [GO:0006397]; RNA splicing [GO:0008380]
|
mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739]
|
cytochrome-c oxidase activity [GO:0004129]; endonuclease activity [GO:0004519]; heme binding [GO:0020037]
|
PF00115;PF00961;
|
1.20.210.10;3.10.28.10;
|
LAGLIDADG endonuclease family; Heme-copper respiratory oxidase family
|
PTM: The mature protein may arise from proteolytic cleavage of an in-frame translation of COX1 exons 1 to 4 plus intron 4, containing the aI4 open reading frame. Cleavage would take place close to the Met-299 resulting in an active endonuclease of about 30 kDa. {ECO:0000269|PubMed:2172241, ECO:0000269|PubMed:2216759, ECO:0000269|PubMed:8352597}.
|
SUBCELLULAR LOCATION: Mitochondrion.
| null | null | null | null | null |
FUNCTION: Mitochondrial DNA endonuclease involved in intron homing. It introduces a specific double-strand break at the junction of the two exons a4-a5 of the COX1 gene and thus mediates the insertion of an intron, containing its own coding sequence (group I intron), into an intronless gene. Recognizes with limited specificity and cleaves the sequence 5'-TTTGGTCACCCTGAAGTA-3'. The protein may acquire mRNA maturase activity, like the closely related bI4, through a single amino acid substitution Glu-362 to Lys or when present together with a mutant form of the imported mitochondrial leucyl-tRNA synthetase NAM2. {ECO:0000269|PubMed:2172241, ECO:0000269|PubMed:2216759, ECO:0000269|PubMed:2536592, ECO:0000269|PubMed:2536593, ECO:0000269|PubMed:8352597}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P03879
|
MBI4_YEAST
|
MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVIIFILTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFSVSNPTIQRFFALHYLVPFIIAAMVIMHLMALHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLILALFVFYSPNTLGQNMALLLITYVINILCAVCWKSLFIKYQWKIYNKTTYYFIIQNILNTKQLNNFVLKFNWTKQYNKMNIVSDLFNPNRVKYYYKEDNQQVTNMNSSNTHLTSNKKNLLVDTSETTRTTKNKFNYLLNIFNMKKMNQIITKRHYSIYKDSNIRFNQWLAGLIDGDGYFCITKNKYASCEITVELKDEKMLRQIQDKFGGSVKLRSGVKAIRYRLQNKEGMIKLINAVNGNIRNSKRLVQFNKVCILLNIDFKEPIKLTKDNAWFMGFFDADGTINYYYSGKLKIRPQLTISVTNKYLHDVEYYREVFGGNIYFDKAKNGYFKWSINNKELHNIFYTYNKSCPSKSNKGKRLFLIDKFYYLYDLLAFKAPHNTALYKAWLKFNEKWNNN
|
3.1.-.-
| null |
Group I intron splicing [GO:0000372]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; mitochondrial mRNA processing [GO:0090615]; mRNA processing [GO:0006397]; proton transmembrane transport [GO:1902600]
|
mitochondrion [GO:0005739]
|
endonuclease activity [GO:0004519]; RNA binding [GO:0003723]
|
PF00033;PF00961;
|
3.10.28.10;
|
LAGLIDADG endonuclease family
|
PTM: The mature protein may arise from proteolytic cleavage of an in-frame translation of COB exons 1 to 4 plus intron 4, containing the bI4 open reading frame. Cleavage would take place close to the Met-385 resulting in an active maturase of about 30 kDa. {ECO:0000269|PubMed:8352597}.
|
SUBCELLULAR LOCATION: Mitochondrion.
| null | null | null | null | null |
FUNCTION: Mitochondrial mRNA maturase required for splicing of intron 4 of the cytochrome b (COB) gene, containing its own coding sequence, and intron 4 in COX1, coding for the related homing endonuclease aI4. In vivo splicing requires in addition the imported mitochondrial leucyl-tRNA synthetase NAM2. Both proteins seem to stimulate the intrinsic ribozyme activity of intron bI4 through binding to and stabilizing specific secondary and tertiary structure elements in the RNA. {ECO:0000269|PubMed:11142386, ECO:0000269|PubMed:2560681, ECO:0000269|PubMed:3284745, ECO:0000269|PubMed:8352597}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P03886
|
NU1M_HUMAN
|
MPMANLLLLIVPILIAMAFLMLTERKILGYMQLRKGPNVVGPYGLLQPFADAMKLFTKEPLKPATSTITLYITAPTLALTIALLLWTPLPMPNPLVNLNLGLLFILATSSLAVYSILWSGWASNSNYALIGALRAVAQTISYEVTLAIILLSTLLMSGSFNLSTLITTQEHLWLLLPSWPLAMMWFISTLAETNRTPFDLAEGESELVSGFNIEYAAGPFALFFMAEYTNIIMMNTLTTTIFLGTTYDALSPELYTTYFVTKTLLLTSLFLWIRTAYPRFRYDQLMHLLWKNFLPLTLALLMWYVSMPITISSIPPQT
|
7.1.1.2
| null |
aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]; response to hydroperoxide [GO:0033194]; response to hypoxia [GO:0001666]; response to organic cyclic compound [GO:0014070]; response to xenobiotic stimulus [GO:0009410]
|
dendrite [GO:0030425]; mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex I [GO:0005747]; neuronal cell body [GO:0043025]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
|
PF00146;
| null |
Complex I subunit 1 family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P03887}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000269|PubMed:1959619};
| null | null | null | null |
FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:1959619). Essential for the catalytic activity and assembly of complex I (PubMed:1959619, PubMed:26929434). {ECO:0000269|PubMed:1959619, ECO:0000269|PubMed:26929434}.
|
Homo sapiens (Human)
|
P03887
|
NU1M_BOVIN
|
MFMINILMLIIPILLAVAFLTLVERKVLGYMQLRKGPNVVGPYGLLQPIADAIKLFIKEPLRPATSSASMFILAPIMALGLALTMWIPLPMPYPLINMNLGVLFMLAMSSLAVYSILWSGWASNSKYALIGALRAVAQTISYEVTLAIILLSVLLMSGSFTLSTLITTQEQMWLILPAWPLAMMWFISTLAETNRAPFDLTEGESELVSGFNVEYAAGPFALFFMAEYANIIMMNIFTAILFLGTSHNPHMPELYTINFTIKSLLLTMSFLWIRASYPRFRYDQLMHLLWKNFLPLTLALCMWHVSLPILTSGIPPQT
|
7.1.1.2
| null |
aerobic respiration [GO:0009060]; mitochondrial respiratory chain complex I assembly [GO:0032981]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
|
PF00146;
| null |
Complex I subunit 1 family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:17060615, ECO:0000269|PubMed:25209663}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000269|PubMed:3141400};
| null | null | null | null |
FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:3141400). Essential for the catalytic activity of complex I (PubMed:3141400). Essential for the assembly of complex I (By similarity). {ECO:0000250|UniProtKB:P03886, ECO:0000269|PubMed:3141400}.
|
Bos taurus (Bovine)
|
P03891
|
NU2M_HUMAN
|
MNPLAQPVIYSTIFAGTLITALSSHWFFTWVGLEMNMLAFIPVLTKKMNPRSTEAAIKYFLTQATASMILLMAILFNNMLSGQWTMTNTTNQYSSLMIMMAMAMKLGMAPFHFWVPEVTQGTPLTSGLLLLTWQKLAPISIMYQISPSLNVSLLLTLSILSIMAGSWGGLNQTQLRKILAYSSITHMGWMMAVLPYNPNMTILNLTIYIILTTTAFLLLNLNSSTTTLLLSRTWNKLTWLTPLIPSTLLSLGGLPPLTGFLPKWAIIEEFTKNNSLIIPTIMATITLLNLYFYLRLIYSTSITLLPMSNNVKMKWQFEHTKPTPFLPTLIALTTLLLPISPFMLMIL
|
7.1.1.2
| null |
aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]; reactive oxygen species metabolic process [GO:0072593]; response to hypoxia [GO:0001666]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]
|
ionotropic glutamate receptor binding [GO:0035255]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]; protein kinase binding [GO:0019901]
|
PF06444;PF00361;
| null |
Complex I subunit 2 family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P03892}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000269|PubMed:16996290};
| null | null | null | null |
FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:16996290). Essential for the catalytic activity and assembly of complex I (PubMed:16996290). {ECO:0000269|PubMed:16996290}.
|
Homo sapiens (Human)
|
P03892
|
NU2M_BOVIN
|
MNPIIFIIILLTIMLGTIIVMISSHWLLVWIGFEMNMLAIIPIMMKNHNPRATEASTKYFLTQSTASMLLMMAVIINLMFSGQWTVMKLFNPMASMLMTMALAMKLGMAPFHFWVPEVTQGIPLSSGLILLTWQKLAPMSVLYQIFPSINLNLILTLSVLSILIGGWGGLNQTQLRKIMAYSSIAHMGWMTAVLPYNPTMTLLNLIIYIIMTSTMFTMFMANSTTTTLSLSHTWNKTPIMTVLILATLLSMGGLPPLSGFMPKWMIIQEMTKNNSIILPTFMAITALLNLYFYMRLTYSTTLTMFPSTNNMKMKWQFPLMKKMTFLPTMVVLSTMMLPLTPMLSVLE
|
7.1.1.2
| null |
mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
|
PF06444;PF00361;
| null |
Complex I subunit 2 family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:17060615, ECO:0000269|PubMed:25209663}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000250|UniProtKB:P03891};
| null | null | null | null |
FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I. {ECO:0000250|UniProtKB:P03891}.
|
Bos taurus (Bovine)
|
P03897
|
NU3M_HUMAN
|
MNFALILMINTLLALLLMIITFWLPQLNGYMEKSTPYECGFDPMSPARVPFSMKFFLVAITFLLFDLEIALLLPLPWALQTTNLPLMVMSSLLLIIILALSLAYEWLQKGLDWTE
|
7.1.1.2
| null |
aerobic respiration [GO:0009060]; cellular response to glucocorticoid stimulus [GO:0071385]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]; response to light intensity [GO:0009642]; response to oxidative stress [GO:0006979]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
|
PF00507;
|
1.20.58.1610;
|
Complex I subunit 3 family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P03898}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000269|PubMed:25118196};
| null | null | null | null |
FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:25118196). Essential for the catalytic activity of complex I (PubMed:25118196). {ECO:0000269|PubMed:25118196}.
|
Homo sapiens (Human)
|
P03898
|
NU3M_BOVIN
|
MNLMLALLTNFTLATLLVIIAFWLPQLNVYSEKTSPYECGFDPMGSARLPFSMKFFLVAITFLLFDLEIALLLPLPWASQTANLNTMLTMALFLIILLAVSLAYEWTQKGLEWTE
|
7.1.1.2
| null |
mitochondrial electron transport, NADH to ubiquinone [GO:0006120]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
|
PF00507;
|
1.20.58.1610;
|
Complex I subunit 3 family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:17060615, ECO:0000269|PubMed:25209663}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000250|UniProtKB:P03897};
| null | null | null | null |
FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I. {ECO:0000250|UniProtKB:P03897}.
|
Bos taurus (Bovine)
|
P03901
|
NU4LM_HUMAN
|
MPLIYMNIMLAFTISLLGMLVYRSHLMSSLLCLEGMMLSLFIMATLMTLNTHSLLANIVPIAMLVFAACEAAVGLALLVSISNTYGLDYVHNLNLLQC
|
7.1.1.2
| null |
aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
|
PF00420;
|
1.10.287.3510;
|
Complex I subunit 4L family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P03902}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000305|PubMed:28844695}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29092; Evidence={ECO:0000305|PubMed:28844695};
| null | null | null | null |
FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:28844695). Part of the enzyme membrane arm which is embedded in the lipid bilayer and involved in proton translocation (PubMed:28844695). {ECO:0000269|PubMed:28844695}.
|
Homo sapiens (Human)
|
P03902
|
NU4LM_BOVIN
|
MSMVYMNIMMAFTVSLVGLLMYRSHLMSSLLCLEGMMLSLFVMAALTILNSHFTLASMMPIILLVFAACEAALGLSLLVMVSNTYGTDYVQNLNLLQC
|
7.1.1.2
| null |
ATP synthesis coupled electron transport [GO:0042773]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
|
PF00420;
|
1.10.287.3510;
|
Complex I subunit 4L family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:17060615, ECO:0000269|PubMed:18721790, ECO:0000269|PubMed:25209663}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000305|PubMed:18721790, ECO:0000305|PubMed:25209663}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29092; Evidence={ECO:0000305|PubMed:18721790, ECO:0000305|PubMed:25209663};
| null | null | null | null |
FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:18721790, PubMed:25209663). Part of the enzyme membrane arm which is embedded in the lipid bilayer and involved in proton translocation (PubMed:18721790, PubMed:25209663). {ECO:0000269|PubMed:18721790, ECO:0000269|PubMed:25209663}.
|
Bos taurus (Bovine)
|
P03905
|
NU4M_HUMAN
|
MLKLIVPTIMLLPLTWLSKKHMIWINTTTHSLIISIIPLLFFNQINNNLFSCSPTFSSDPLTTPLLMLTTWLLPLTIMASQRHLSSEPLSRKKLYLSMLISLQISLIMTFTATELIMFYIFFETTLIPTLAIITRWGNQPERLNAGTYFLFYTLVGSLPLLIALIYTHNTLGSLNILLLTLTAQELSNSWANNLMWLAYTMAFMVKMPLYGLHLWLPKAHVEAPIAGSMVLAAVLLKLGGYGMMRLTLILNPLTKHMAYPFLVLSLWGMIMTSSICLRQTDLKSLIAYSSISHMALVVTAILIQTPWSFTGAVILMIAHGLTSSLLFCLANSNYERTHSRIMILSQGLQTLLPLMAFWWLLASLANLALPPTINLLGELSVLVTTFSWSNITLLLTGLNMLVTALYSLYMFTTTQWGSLTHHINNMKPSFTRENTLMFMHLSPILLLSLNPDIITGFSS
|
7.1.1.2
| null |
aerobic respiration [GO:0009060]; cerebellum development [GO:0021549]; electron transport coupled proton transport [GO:0015990]; in utero embryonic development [GO:0001701]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]; response to ethanol [GO:0045471]; response to hypoxia [GO:0001666]; response to nicotine [GO:0035094]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]; ubiquinone binding [GO:0048039]
|
PF01059;PF00361;
| null |
Complex I subunit 4 family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P03910}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000269|PubMed:15250827, ECO:0000269|PubMed:8344246, ECO:0000269|PubMed:8644732};
| null | null | null | null |
FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:15250827, PubMed:8344246, PubMed:8644732). Essential for the catalytic activity and assembly of complex I (PubMed:15250827, PubMed:8344246, PubMed:8644732). {ECO:0000269|PubMed:15250827, ECO:0000269|PubMed:8344246, ECO:0000269|PubMed:8644732}.
|
Homo sapiens (Human)
|
P03910
|
NU4M_BOVIN
|
MLKYIIPTIMLMPLTWLSKNNMIWVNSTAHSLLISFTSLLLMNQFGDNSLNFSLLFFSDSLSTPLLILTMWLLPLMLMASQHHLSKENLTRKKLFITMLISLQLFLIMTFTAMELILFYILFEATLVPTLIIITRWGNQTERLNAGLYFLFYTLAGSLPLLVALIYIQNTVGSLNFLMLQYWVQPVHNSWSNVFMWLACMMAFMVKMPLYGLHLWLPKAHVEAPIAGSMVLAAVLLKLGGYGMLRITLILNPMTDFMAYPFIMLSLWGMIMTSSICLRQTDLKSLIAYSSVSHMALVIVAILIQTPWSYMGATALMIAHGLTSSMLFCLANSNYERIHSRTMILARGLQTLLPLMATWWLLASLTNLALPPTINLIGELFVVMSTFSWSNITIILMGVNMVITALYSLYMLIMTQRGKYTYHINNISPSFTRENALMSLHILPLLLLTLNPKIILGPLY
|
7.1.1.2
| null |
aerobic respiration [GO:0009060]; electron transport coupled proton transport [GO:0015990]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]; ubiquinone binding [GO:0048039]
|
PF01059;PF00361;
| null |
Complex I subunit 4 family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:17060615}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000250|UniProtKB:P03905};
| null | null | null | null |
FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I. {ECO:0000250|UniProtKB:P03905}.
|
Bos taurus (Bovine)
|
P03915
|
NU5M_HUMAN
|
MTMHTTMTTLTLTSLIPPILTTLVNPNKKNSYPHYVKSIVASTFIISLFPTTMFMCLDQEVIISNWHWATTQTTQLSLSFKLDYFSMMFIPVALFVTWSIMEFSLWYMNSDPNINQFFKYLLIFLITMLILVTANNLFQLFIGWEGVGIMSFLLISWWYARADANTAAIQAILYNRIGDIGFILALAWFILHSNSWDPQQMALLNANPSLTPLLGLLLAAAGKSAQLGLHPWLPSAMEGPTPVSALLHSSTMVVAGIFLLIRFHPLAENSPLIQTLTLCLGAITTLFAAVCALTQNDIKKIVAFSTSSQLGLMMVTIGINQPHLAFLHICTHAFFKAMLFMCSGSIIHNLNNEQDIRKMGGLLKTMPLTSTSLTIGSLALAGMPFLTGFYSKDHIIETANMSYTNAWALSITLIATSLTSAYSTRMILLTLTGQPRFPTLTNINENNPTLLNPIKRLAAGSLFAGFLITNNISPASPFQTTIPLYLKLTALAVTFLGLLTALDLNYLTNKLKMKSPLCTFYFSNMLGFYPSITHRTIPYLGLLTSQNLPLLLLDLTWLEKLLPKTISQHQISTSIITSTQKGMIKLYFLSFFFPLILTLLLIT
|
7.1.1.2
| null |
aerobic respiration [GO:0009060]; electron transport coupled proton transport [GO:0015990]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]; response to hydrogen peroxide [GO:0042542]; response to hypoxia [GO:0001666]; response to organonitrogen compound [GO:0010243]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]; NADH dehydrogenase activity [GO:0003954]
|
PF06455;PF00361;PF00662;
| null |
Complex I subunit 5 family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P03920}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000269|PubMed:15250827};
| null | null | null | null |
FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:15250827). Essential for the catalytic activity and assembly of complex I (PubMed:15250827). {ECO:0000269|PubMed:15250827}.
|
Homo sapiens (Human)
|
P03920
|
NU5M_BOVIN
|
MNMFSSLSLVTLLLLTMPIMMMSFNTYKPSNYPLYVKTAISYAFITSMIPTMMFIHSGQELIISNWHWLTIQTLKLSLSFKMDYFSMMFIPVALFVTWSIMEFSMWYMYSDPNINKFFKYLLLFLITMLILVTANNLFQLFIGWEGVGIMSFLLIGWWYGRADANTAALQAILYNRIGDIGFILAMAWFLTNLNTWDLQQIFMLNPSDSNMPLIGLALAATGKSAQFGLHPWLPSAMEGPTPVSALLHSSTMVVAGIFLLIRFYPLTENNKYIQSITLCLGAITTLFTAMCALTQNDIKKIIAFSTSSQLGLMMVTIGINQPYLAFLHICTHAFFKAMLFMCSGSIIHSLNDEQDIRKMGGLFKAMPFTTTALIVGSLALTGMPFLTGFYSKDLIIEAANTSYTNAWALLMTLIATSFTAIYSTRIIFFALLGQPRFPTLVNINENNPLLINSIKRLLIGSLFAGYIISNNIPPTTIPQMTMPYYLKTTALIVTILGFILALEISNMTKNLKYHYPSNAFKFSTLLGYFPTIMHRLAPYMNLSMSQKSASSLLDLIWLEAILPKTISLAQMKASTLVTNQKGLIKLYFLSFLITILISMILFNFHE
|
7.1.1.2
| null |
electron transport coupled proton transport [GO:0015990]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]; NADH dehydrogenase activity [GO:0003954]
|
PF06455;PF00361;PF00662;
| null |
Complex I subunit 5 family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:17060615}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000250|UniProtKB:P03915};
| null | null | null | null |
FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I. {ECO:0000250|UniProtKB:P03915}.
|
Bos taurus (Bovine)
|
P03923
|
NU6M_HUMAN
|
MMYALFLLSVGLVMGFVGFSSKPSPIYGGLVLIVSGVVGCVIILNFGGGYMGLMVFLIYLGGMMVVFGYTTAMAIEEYPEAWGSGVEVLVSVLVGLAMEVGLVLWVKEYDGVVVVVNFNSVGSWMIYEGEGSGLIREDPIGAGALYDYGRWLVVVTGWTLFVGVYIVIEIARGN
|
7.1.1.2
| null |
aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]; response to cocaine [GO:0042220]; response to hydrogen peroxide [GO:0042542]; response to nicotine [GO:0035094]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
|
PF00499;
| null |
Complex I subunit 6 family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P03924}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000269|PubMed:14595656, ECO:0000269|PubMed:8644732};
| null | null | null | null |
FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:14595656, PubMed:8644732). Essential for the catalytic activity and assembly of complex I (PubMed:14595656, PubMed:8644732). {ECO:0000269|PubMed:14595656, ECO:0000269|PubMed:8644732}.
|
Homo sapiens (Human)
|
P03928
|
ATP8_HUMAN
|
MPQLNTTVWPTMITPMLLTLFLITQLKMLNTNYHLPPSPKPMKMKNYNKPWEPKWTKICSLHSLPPQS
| null | null |
proton motive force-driven ATP synthesis [GO:0015986]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) [GO:0000276]
|
proton transmembrane transporter activity [GO:0015078]
|
PF00895;
| null |
ATPase protein 8 family
| null |
SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
P03945
|
COX1_NEUCR
|
MSSISIWTERWFLSTNAKDIGVLYLIFALFSGLLGTAFSVLIRMELSGPGVQYIADNQLYNAIITAHAILMIFFMVMPALIGGFGNFLLPLLVGGPDMAFPRLNNISFWLLPPSLLLLVFSACIEGGAGTGWTIYPPLSGVQSHSGPSVDLAIFALHLSGVSSLLGSINFITTIVNMRTPGIRLHKLALFGWAVVITAVLLLLSLPVLAGAITMLLTDRNFNTSFFETAGGGDPILFQHLFWFFGHPEVYILIIPGFGIISTTISAYSNKSVFGYIGMVYAMMSIGILGFIVWSHHMYTVGLDVDTRAYFTAATLIIAVPTGIKIFSWLATCYGGSIRLTPSMLFALGFVFMFTIGGLSGVVLANASLDIAFHDTYYVVAHFHYVLSMGAVFAMFSGWYHWVPKILGLNYNMVLSKAQFWLLFIGVNLTFFPQHFLGLQGMPRRISDYPDAFSGWNLISSFGSIVSVVASWLFLYIVYIQLVQGEYAGRYPWSIPQFYTDSLRALLNRSYPSLEWSISSPPKPHSFVSLPLQSSSFFLSFFRLSSYGEQKEISGRQN
|
7.1.1.9
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P00401}; Note=Binds 2 heme A groups non-covalently per subunit. {ECO:0000250|UniProtKB:P00401}; COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P00401}; Note=Binds a copper B center. {ECO:0000250|UniProtKB:P00401};
|
electron transport coupled proton transport [GO:0015990]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]
|
mitochondrial respiratory chain complex IV [GO:0005751]
|
cytochrome-c oxidase activity [GO:0004129]; heme binding [GO:0020037]; metal ion binding [GO:0046872]
|
PF00115;
|
1.20.210.10;
|
Heme-copper respiratory oxidase family
|
PTM: The amino end of the mature protein may be Ser-3. {ECO:0000305|PubMed:6327266}.
|
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:31316820}; Multi-pass membrane protein {ECO:0000269|PubMed:31316820}.
|
CATALYTIC ACTIVITY: Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=7.1.1.9; Evidence={ECO:0000250|UniProtKB:P00401}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; Evidence={ECO:0000250|UniProtKB:P00401};
| null |
PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000250|UniProtKB:P00401}.
| null | null |
FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of Cox2 and heme A of Cox1 to the active site in Cox1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P00401}.
|
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
|
P03946
|
SODC_XIPGL
|
MVLKAVCVLRGAGETTGTVYFEQEGNANAVGKGIILKGLTPGEHGFHVHGFGDNTNGCISAGPHFNPASKKHAGPKDEDRHVGDLGNVTADANGVAKIDITDKISLTGPYSIIGRTMVIHEKADDLGRGGNEESLKTGNAGSRLACGVIGTE
|
1.15.1.1
|
COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Note=Binds 1 copper ion per subunit.; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.;
| null |
cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; peroxisome [GO:0005777]
|
copper ion binding [GO:0005507]; superoxide dismutase activity [GO:0004784]
|
PF00080;
|
2.60.40.200;
|
Cu-Zn superoxide dismutase family
| null |
SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1;
| null | null | null | null |
FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
|
Xiphias gladius (Swordfish) (Tetrapterus imperator)
|
P03949
|
ABL1_CAEEL
|
MGHSHSTGKEINDNELFTCEDPVFDQPVASPKSEISSKLAEEIERSKSPLILEVSPRTPDSVQMFRPTFDTFRPPNSDSSTFRGSQSREDLVACSSMNSVNNVHDMNTVSSSSSSSAPLFVALYDFHGVGEEQLSLRKGDQVRILGYNKNNEWCEARLYSTRKNDASNQRRLGEIGWVPSNFIAPYNSLDKYTWYHGKISRSDSEAILGSGITGSFLVRESETSIGQYTISVRHDGRVFHYRINVDNTEKMFITQEVKFRTLGELVHHHSVHADGLICLLMYPASKKDKGRGLFSLSPNAPDEWELDRSEIIMHNKLGGGQYGDVYEGYWKRHDCTIAVKALKEDAMPLHEFLAEAAIMKDLHHKNLVRLLGVCTHEAPFYIITEFMCNGNLLEYLRRTDKSLLPPIILVQMASQIASGMSYLEARHFIHRDLAARNCLVSEHNIVKIADFGLARFMKEDTYTAHAGAKFPIKWTAPEGLAFNTFSSKSDVWAFGVLLWEIATYGMAPYPGVELSNVYGLLENGFRMDGPQGCPPSVYRLMLQCWNWSPSDRPRFRDIHFNLENLISSNSLNDEVQKQLKKNNDKKLESDKRRSNVRERSDSKSRHSSHHDRDRDRESLHSRNSNPEIPNRSFIRTDDSVSFFNPSTTSKVTSFRAQGPPFPPPPQQNTKPKLLKSVLNSNARHASEEFERNEQDDVVPLAEKNVRKAVTRLGGTMPKGQRIDAYLDSMRRVDSWKESTDADNEGAGSSSLSRTVSNDSLDTLPLPDSMNSSTYVKMHPASGENVFLRQIRSKLKKRSETPELDHIDSDTADETTKSEKSPFGSLNKSSIKYPIKNAPEFSENHSRVSPVPVPPSRNASVSVRPDSKAEDSSDETTKDVGMWGPKHAVTRKIEIVKNDSYPNVEGELKAKIRNLRHVPKEESNTSSQEDLPLDATDNTNDSIIVIPRDEKAKVRQLVTQKVSPLQHHRPFSLQCPNNSTSSAISHSEHADSSETSSLSGVYEERMKPELPRKRSNGDTKVVPVTWIINGEKEPNGMARTKSLRDITSKFEQLGTASTIESKIEEAVPYREHALEKKGTSKRFSMLEGSNELKHVVPPRKNRNQDESGSIDEEPVSKDMIVSLLKVIQKEFVNLFNLASSEITDEKLQQFVIMADNVQKLHSTCSVYAEQISPHSKFRFKELLSQLEIYNRQIKFSHNPRAKPVDDKLKMAFQDCFDQIMRLVDR
|
2.7.10.2
| null |
defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; DNA damage checkpoint signaling [GO:0000077]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell migration [GO:0030336]; negative regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043518]; negative regulation of engulfment of apoptotic cell [GO:1901075]; phosphorylation [GO:0016310]; response to ionizing radiation [GO:0010212]; spermatogenesis [GO:0007283]
|
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713]
|
PF08919;PF07714;PF00017;PF00018;
|
1.20.120.330;3.30.505.10;2.30.30.40;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, ABL subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27780040}. Cytoplasm {ECO:0000269|PubMed:27780040}. Note=Enriched at the leading edge compared to cytoplasm. Targeted to the leading edge of Q neuroblasts by mig-13. {ECO:0000269|PubMed:27780040}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
| null | null | null | null |
FUNCTION: Functions downstream of migratory protein mig-13 and is involved in Q neuroblast migration during larval development (PubMed:27780040). Recruited by mig-13 to the leading edge of Q neuroblasts and their descendents to signal downstream, likely to the wve-1 pathway, and direct migration along the anteroposterior body axis (PubMed:27780040). Promotes germline cell apoptosis in response to oxidative, osmotic and heat shock stresses (PubMed:16729024). {ECO:0000269|PubMed:16729024, ECO:0000269|PubMed:27780040}.
|
Caenorhabditis elegans
|
P03950
|
ANGI_HUMAN
|
MVMGLGVLLLVFVLGLGLTPPTLAQDNSRYTHFLTQHYDAKPQGRDDRYCESIMRRRGLTSPCKDINTFIHGNKRSIKAICENKNGNPHRENLRISKSSFQVTTCKLHGGSPWPPCQYRATAGFRNVVVACENGLPVHLDQSIFRRP
|
3.1.27.-
| null |
actin filament polymerization [GO:0030041]; activation of phospholipase A2 activity [GO:0032431]; activation of phospholipase C activity [GO:0007202]; activation of protein kinase B activity [GO:0032148]; angiogenesis [GO:0001525]; antibacterial humoral response [GO:0019731]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cell communication [GO:0007154]; cell migration [GO:0016477]; defense response to Gram-positive bacterium [GO:0050830]; diacylglycerol biosynthetic process [GO:0006651]; homeostatic process [GO:0042592]; innate immune response [GO:0045087]; negative regulation of smooth muscle cell proliferation [GO:0048662]; negative regulation of translation [GO:0017148]; oocyte maturation [GO:0001556]; ovarian follicle development [GO:0001541]; placenta development [GO:0001890]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of phosphorylation [GO:0042327]; positive regulation of protein secretion [GO:0050714]; response to hormone [GO:0009725]; response to hypoxia [GO:0001666]; rRNA transcription [GO:0009303]; tRNA catabolic process [GO:0016078]
|
actin cytoskeleton [GO:0015629]; angiogenin-PRI complex [GO:0032311]; basement membrane [GO:0005604]; chromosome [GO:0005694]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; growth cone [GO:0030426]; neuronal cell body [GO:0043025]; nucleolus [GO:0005730]; nucleus [GO:0005634]
|
actin binding [GO:0003779]; copper ion binding [GO:0005507]; DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; heparin binding [GO:0008201]; peptide binding [GO:0042277]; protein homodimerization activity [GO:0042803]; RNA endonuclease activity [GO:0004521]; RNA nuclease activity [GO:0004540]; rRNA binding [GO:0019843]; signaling receptor binding [GO:0005102]
|
PF00074;
|
3.10.130.10;
|
Pancreatic ribonuclease family
| null |
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000250|UniProtKB:Q3TMQ6}. Secreted {ECO:0000250|UniProtKB:P10152}. Nucleus {ECO:0000269|PubMed:12051708, ECO:0000269|PubMed:25372031, ECO:0000269|PubMed:8127865}. Nucleus, nucleolus {ECO:0000269|PubMed:7945327}. Note=Rapidly endocytosed by target cells and translocated to the nucleus where it accumulates in the nucleolus and binds to DNA (PubMed:12051708). {ECO:0000269|PubMed:12051708}.
| null | null | null | null | null |
FUNCTION: Ribonuclease that cleaves tRNA within anticodon loops to produce tRNA-derived stress-induced fragments (tiRNAs) which inhibit protein synthesis and triggers the assembly of stress granules (SGs) (PubMed:1400510, PubMed:21855800). Binds to actin on the surface of endothelial cells; once bound, angiogenin is endocytosed and translocated to the nucleus (PubMed:8127865). Stimulates ribosomal RNA synthesis including that containing the initiation site sequences of 45S rRNA (PubMed:12051708). Angiogenin induces vascularization of normal and malignant tissues (PubMed:19354288). Angiogenic activity is regulated by interaction with RNH1 in vivo (PubMed:19354288). {ECO:0000269|PubMed:12051708, ECO:0000269|PubMed:1400510, ECO:0000269|PubMed:19354288, ECO:0000269|PubMed:21855800, ECO:0000269|PubMed:8127865}.
|
Homo sapiens (Human)
|
P03951
|
FA11_HUMAN
|
MIFLYQVVHFILFTSVSGECVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESPSEDPTRWFTCVLKDSVTETLPRVNRTAAISGYSFKQCSHQISACNKDIYVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATRQFPSLEHRNICLLKHTQTGTPTRITKLDKVVSGFSLKSCALSNLACIRDIFPNTVFADSNIDSVMAPDAFVCGRICTHHPGCLFFTFFSQEWPKESQRNLCLLKTSESGLPSTRIKKSKALSGFSLQSCRHSIPVFCHSSFYHDTDFLGEELDIVAAKSHEACQKLCTNAVRCQFFTYTPAQASCNEGKGKCYLKLSSNGSPTKILHGRGGISGYTLRLCKMDNECTTKIKPRIVGGTASVRGEWPWQVTLHTTSPTQRHLCGGSIIGNQWILTAAHCFYGVESPKILRVYSGILNQSEIKEDTSFFGVQEIIIHDQYKMAESGYDIALLKLETTVNYTDSQRPICLPSKGDRNVIYTDCWVTGWGYRKLRDKIQNTLQKAKIPLVTNEECQKRYRGHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWILEKTQAV
|
3.4.21.27
| null |
blood coagulation [GO:0007596]; plasminogen activation [GO:0031639]; positive regulation of fibrinolysis [GO:0051919]
|
extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
heparin binding [GO:0008201]; identical protein binding [GO:0042802]; serine-type aminopeptidase activity [GO:0070009]; serine-type endopeptidase activity [GO:0004252]
|
PF00024;PF00089;
|
3.50.4.10;2.40.10.10;
|
Peptidase S1 family, Plasma kallikrein subfamily
|
PTM: N-glycosylated on both chains. N-glycosylated sites mainly consist of nonfucosylated sialylated biantennary (in high abundance) and/or triantennary (in low abundance) complex structures. Glycosylation at Asn-163 uses a rare non-canonical Asn-X-Cys glycosite. {ECO:0000269|PubMed:25092234}.; PTM: Activated by factor XIIa (or XII), which cleaves each polypeptide after Arg-387 into the light chain, which contains the active site, and the heavy chain, which associates with high molecular weight (HMW) kininogen.
|
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Ala and Arg-|-Val bonds in factor IX to form factor IXa.; EC=3.4.21.27;
| null | null | null | null |
FUNCTION: Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX.
|
Homo sapiens (Human)
|
P03952
|
KLKB1_HUMAN
|
MILFKQATYFISLFATVSCGCLTQLYENAFFRGGDVASMYTPNAQYCQMRCTFHPRCLLFSFLPASSINDMEKRFGCFLKDSVTGTLPKVHRTGAVSGHSLKQCGHQISACHRDIYKGVDMRGVNFNVSKVSSVEECQKRCTSNIRCQFFSYATQTFHKAEYRNNCLLKYSPGGTPTAIKVLSNVESGFSLKPCALSEIGCHMNIFQHLAFSDVDVARVLTPDAFVCRTICTYHPNCLFFTFYTNVWKIESQRNVCLLKTSESGTPSSSTPQENTISGYSLLTCKRTLPEPCHSKIYPGVDFGGEELNVTFVKGVNVCQETCTKMIRCQFFTYSLLPEDCKEEKCKCFLRLSMDGSPTRIAYGTQGSSGYSLRLCNTGDNSVCTTKTSTRIVGGTNSSWGEWPWQVSLQVKLTAQRHLCGGSLIGHQWVLTAAHCFDGLPLQDVWRIYSGILNLSDITKDTPFSQIKEIIIHQNYKVSEGNHDIALIKLQAPLNYTEFQKPICLPSKGDTSTIYTNCWVTGWGFSKEKGEIQNILQKVNIPLVTNEECQKRYQDYKITQRMVCAGYKEGGKDACKGDSGGPLVCKHNGMWRLVGITSWGEGCARREQPGVYTKVAEYMDWILEKTQSSDGKAQMQSPA
|
3.4.21.34
| null |
blood coagulation [GO:0007596]; Factor XII activation [GO:0002542]; fibrinolysis [GO:0042730]; plasminogen activation [GO:0031639]; positive regulation of fibrinolysis [GO:0051919]; proteolysis [GO:0006508]; zymogen activation [GO:0031638]
|
extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
serine-type endopeptidase activity [GO:0004252]
|
PF00024;PF00089;
|
3.50.4.10;2.40.10.10;
|
Peptidase S1 family, Plasma kallikrein subfamily
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Cleaves selectively Arg-|-Xaa and Lys-|-Xaa bonds, including Lys-|-Arg and Arg-|-Ser bonds in (human) kininogen to release bradykinin.; EC=3.4.21.34;
| null | null | null | null |
FUNCTION: Participates in the surface-dependent activation of blood coagulation. Activates, in a reciprocal reaction, coagulation factor XII/F12 after binding to negatively charged surfaces. Releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin.
|
Homo sapiens (Human)
|
P03953
|
CFAD_MOUSE
|
MHSSVYFVALVILGAAVCAAQPRGRILGGQEAAAHARPYMASVQVNGTHVCGGTLLDEQWVLSAAHCMDGVTDDDSVQVLLGAHSLSAPEPYKRWYDVQSVVPHPGSRPDSLEDDLILFKLSQNASLGPHVRPLPLQYEDKEVEPGTLCDVAGWGVVTHAGRRPDVLHQLRVSIMNRTTCNLRTYHDGVVTINMMCAESNRRDTCRGDSGSPLVCGDAVEGVVTWGSRVCGNGKKPGVYTRVSSYRMWIENITNGNMTS
|
3.4.21.46
| null |
complement activation, alternative pathway [GO:0006957]; Notch signaling pathway [GO:0007219]; proteolysis [GO:0006508]; response to bacterium [GO:0009617]
|
extracellular space [GO:0005615]
|
endopeptidase activity [GO:0004175]; serine-type endopeptidase activity [GO:0004252]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:16944957, ECO:0000269|PubMed:17330941}.
|
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Lys bond in complement factor B when in complex with complement subcomponent C3b or with cobra venom factor.; EC=3.4.21.46;
| null | null | null | null |
FUNCTION: Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway.
|
Mus musculus (Mouse)
|
P03954
|
PEPA1_MACFU
|
MKWLLLLGLVALSECIIYKVPLVRKKSLRRNLSEHGLLKDFLKKHNLNPASKYFPQAEAPTLIDEQPLENYLDVEYFGTIGIGTPAQDFTVIFDTGSSNLWVPSVYCSSLACTNHNLFNPQDSSTYQSTSGTLSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISSSGATPVFDNIWDQGLVSQDLFSVYLSADDQSGSVVIFGGIDSSYYTGSLNWVPVSVEGYWQISVDSITMNGEAIACAEGCQAIVDTGTSLLTGPTSPIANIQSDIGASENSDGEMVVSCSAISSLPDIVFTINGIQYPVPPSAYILQSQGSCTSGFQGMDVPTESGELWILGDVFIRQYFTVFDRANNQVGLAPVA
|
3.4.23.1
| null |
digestion [GO:0007586]; proteolysis [GO:0006508]
|
extracellular exosome [GO:0070062]
|
aspartic-type endopeptidase activity [GO:0004190]
|
PF07966;PF00026;
|
6.10.140.60;2.40.70.10;
|
Peptidase A1 family
|
PTM: Each pepsinogen is converted to corresponding pepsin at pH 2.0 in part as a result of the release of a 47 AA activation segment and in part as a result of stepwise proteolytic cleavage via an intermediate form(s).
|
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.; EC=3.4.23.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10094};
| null | null | null | null |
FUNCTION: Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.
|
Macaca fuscata fuscata (Japanese macaque)
|
P03956
|
MMP1_HUMAN
|
MHSFPPLLLLLFWGVVSHSFPATLETQEQDVDLVQKYLEKYYNLKNDGRQVEKRRNSGPVVEKLKQMQEFFGLKVTGKPDAETLKVMKQPRCGVPDVAQFVLTEGNPRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQAIYGRSQNPVQPIGPQTPKACDSKLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQNVLHGYPKDIYSSFGFPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQKANSWFNCRKN
|
3.4.24.7
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754, ECO:0000269|PubMed:8090713, ECO:0000269|PubMed:8278810, ECO:0000269|PubMed:9484219}; Note=Binds 4 Ca(2+) ions per subunit. {ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754, ECO:0000269|PubMed:8090713, ECO:0000269|PubMed:8278810, ECO:0000269|PubMed:9484219}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754, ECO:0000269|PubMed:8090713, ECO:0000269|PubMed:8278810, ECO:0000269|PubMed:9484219}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754, ECO:0000269|PubMed:8090713, ECO:0000269|PubMed:8278810, ECO:0000269|PubMed:9484219};
|
cellular response to UV-A [GO:0071492]; collagen catabolic process [GO:0030574]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; positive regulation of protein-containing complex assembly [GO:0031334]; protein metabolic process [GO:0019538]; proteolysis [GO:0006508]
|
extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
endopeptidase activity [GO:0004175]; metalloendopeptidase activity [GO:0004222]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]; zinc ion binding [GO:0008270]
|
PF00045;PF00413;PF01471;
|
3.40.390.10;2.110.10.10;
|
Peptidase M10A family
|
PTM: Undergoes autolytic cleavage to two major forms (22 kDa and 27 kDa). A minor form (25 kDa) is the glycosylated form of the 22 kDa form. The 27 kDa form has no activity while the 22/25 kDa form can act as activator for collagenase. {ECO:0000269|PubMed:10092871}.; PTM: Tyrosine phosphorylated in platelets by PKDCC/VLK. {ECO:0000269|PubMed:25171405}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305|PubMed:2167156}.
|
CATALYTIC ACTIVITY: Reaction=Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.; EC=3.4.24.7; Evidence={ECO:0000269|PubMed:1645757, ECO:0000269|PubMed:16807369, ECO:0000269|PubMed:2153297, ECO:0000269|PubMed:2557822};
| null | null | null | null |
FUNCTION: Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X (PubMed:1645757, PubMed:2153297, PubMed:2557822). In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity (PubMed:16807369). {ECO:0000269|PubMed:1645757, ECO:0000269|PubMed:16807369, ECO:0000269|PubMed:2153297, ECO:0000269|PubMed:2557822}.
|
Homo sapiens (Human)
|
P03957
|
MMP3_RAT
|
MKGLPVLLWLCTAVCSSYPLHGSEEDAGMEVLQKYLENYYGLEKDVKQFTKKKDSSPVVKKIQEMQKFLGLKMTGKLDSNTMELMHKPRCGVPDVGGFSTFPGSPKWRKNHISYRIVNYTLDLPRESVDSAIERALKVWEEVTPLTFSRISEGEADIMISFAVEEHGDFIPFDGPGMVLAHAYAPGPGTNGDAHFDDDERWTDDVTGTNLFLVAAHELGHSLGLFHSANAEALMYPVYKSSTDLARFHLSQDDVDGIQSLYGPPTESPDVLVVPTKSNSLDPETLPMCSSALSFDAVSTLRGEVLFFKDRHFWRKSLRTPEPGFYLISSFWPSLPSNMDAAYEVTNRDTVFILKGNQIWAIRGHEELAGYPKSIHTLGLPETVQKIDAAISLKDQKKTYFFVEDKFWRFDEKKQSMDPEFPRKIAENFPGIGTKVDAVFEAFGFLYFFSGSSQLEFDPNAGKVTHILKSNSWFNC
|
3.4.24.17
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:1963430}; Note=Binds 4 Ca(2+) ions per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
|
cellular response to amino acid stimulus [GO:0071230]; cellular response to cell-matrix adhesion [GO:0071460]; cellular response to interleukin-1 [GO:0071347]; cellular response to reactive oxygen species [GO:0034614]; cellular response to UV-A [GO:0071492]; collagen catabolic process [GO:0030574]; extracellular matrix organization [GO:0030198]; female pregnancy [GO:0007565]; innate immune response [GO:0045087]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; positive regulation of cell migration [GO:0030335]; positive regulation of protein-containing complex assembly [GO:0031334]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508]; regulation of cell migration [GO:0030334]; response to amino acid [GO:0043200]; response to cytokine [GO:0034097]; response to estradiol [GO:0032355]; response to hypoxia [GO:0001666]; response to interleukin-1 [GO:0070555]; response to lipopolysaccharide [GO:0032496]; response to mechanical stimulus [GO:0009612]; response to tumor necrosis factor [GO:0034612]
|
cell body [GO:0044297]; cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; protein-containing complex [GO:0032991]
|
endopeptidase activity [GO:0004175]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; peptidase activity [GO:0008233]; protein-containing complex binding [GO:0044877]; zinc ion binding [GO:0008270]
|
PF00045;PF00413;PF01471;
|
3.40.390.10;2.110.10.10;
|
Peptidase M10A family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:1963430, ECO:0000269|PubMed:1988438, ECO:0000269|PubMed:2841336}.
|
CATALYTIC ACTIVITY: Reaction=Preferential cleavage where P1', P2' and P3' are hydrophobic residues.; EC=3.4.24.17; Evidence={ECO:0000269|PubMed:1963430, ECO:0000269|PubMed:1988438, ECO:0000269|PubMed:2841336};
| null | null | null | null |
FUNCTION: Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase. {ECO:0000269|PubMed:1963430}.; FUNCTION: Metalloproteinase with a rather broad substrate specificity that can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates different molecules including growth factors, plasminogen or other matrix metalloproteinases such as MMP9. Once released into the extracellular matrix (ECM), the inactive pro-enzyme is activated by the plasmin cascade signaling pathway. Acts also intracellularly. For example, in dopaminergic neurons, gets activated by the serine protease HTRA2 upon stress and plays a pivotal role in DA neuronal degeneration by mediating microglial activation and alpha-synuclein/SNCA cleavage. In addition, plays a role in immune response and possesses antiviral activity against various viruses. Mechanistically, translocates from the cytoplasm into the cell nucleus upon virus infection to influence NF-kappa-B activities. {ECO:0000250|UniProtKB:P08254}.
|
Rattus norvegicus (Rat)
|
P03958
|
ADA_MOUSE
|
MAQTPAFNKPKVELHVHLDGAIKPETILYFGKKRGIALPADTVEELRNIIGMDKPLSLPGFLAKFDYYMPVIAGCREAIKRIAYEFVEMKAKEGVVYVEVRYSPHLLANSKVDPMPWNQTEGDVTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMRHQPSWSLEVLELCKKYNQKTVVAMDLAGDETIEGSSLFPGHVEAYEGAVKNGIHRTVHAGEVGSPEVVREAVDILKTERVGHGYHTIEDEALYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRFKNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFKRLNINAAKSSFLPEEEKKELLERLYREYQ
|
3.5.4.4
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8634299, ECO:0000269|PubMed:9622483}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8634299, ECO:0000269|PubMed:9622483};
|
adenosine catabolic process [GO:0006154]; adenosine metabolic process [GO:0046085]; allantoin metabolic process [GO:0000255]; alpha-beta T cell differentiation [GO:0046632]; amide catabolic process [GO:0043605]; AMP catabolic process [GO:0006196]; AMP salvage [GO:0044209]; apoptotic process [GO:0006915]; B cell proliferation [GO:0042100]; calcium-mediated signaling [GO:0019722]; cell adhesion [GO:0007155]; dAMP catabolic process [GO:0046059]; dATP catabolic process [GO:0046061]; deoxyadenosine catabolic process [GO:0006157]; embryonic digestive tract development [GO:0048566]; germinal center B cell differentiation [GO:0002314]; germinal center formation [GO:0002467]; GMP salvage [GO:0032263]; histamine secretion [GO:0001821]; hypoxanthine biosynthetic process [GO:0046101]; hypoxanthine salvage [GO:0043103]; IMP salvage [GO:0032264]; in utero embryonic development [GO:0001701]; inhibition of non-skeletal tissue mineralization [GO:0140928]; inosine biosynthetic process [GO:0046103]; leukocyte migration [GO:0050900]; liver development [GO:0001889]; lung alveolus development [GO:0048286]; lung development [GO:0030324]; mature B cell apoptotic process [GO:0002901]; mucus secretion [GO:0070254]; negative regulation of adenosine receptor signaling pathway [GO:0060169]; negative regulation of apoptotic process [GO:0043066]; negative regulation of circadian sleep/wake cycle, non-REM sleep [GO:0042323]; negative regulation of inflammatory response [GO:0050728]; negative regulation of leukocyte migration [GO:0002686]; negative regulation of mature B cell apoptotic process [GO:0002906]; negative regulation of mucus secretion [GO:0070256]; negative regulation of penile erection [GO:0060407]; negative regulation of thymocyte apoptotic process [GO:0070244]; penile erection [GO:0043084]; Peyer's patch development [GO:0048541]; placenta development [GO:0001890]; positive regulation of alpha-beta T cell differentiation [GO:0046638]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of calcium-mediated signaling [GO:0050850]; positive regulation of germinal center formation [GO:0002636]; positive regulation of heart rate [GO:0010460]; positive regulation of smooth muscle contraction [GO:0045987]; positive regulation of T cell activation [GO:0050870]; positive regulation of T cell differentiation [GO:0045582]; positive regulation of T cell differentiation in thymus [GO:0033089]; positive regulation of T cell receptor signaling pathway [GO:0050862]; regulation of cell-cell adhesion mediated by integrin [GO:0033632]; regulation of T cell differentiation [GO:0045580]; regulation of T cell differentiation in thymus [GO:0033081]; response to hypoxia [GO:0001666]; response to inorganic substance [GO:0010035]; response to purine-containing compound [GO:0014074]; response to vitamin E [GO:0033197]; smooth muscle contraction [GO:0006939]; T cell activation [GO:0042110]; T cell differentiation [GO:0030217]; T cell differentiation in thymus [GO:0033077]; T cell receptor signaling pathway [GO:0050852]; thymocyte apoptotic process [GO:0070242]; trophectodermal cell differentiation [GO:0001829]; xanthine biosynthetic process [GO:0046111]
|
anchoring junction [GO:0070161]; cytoplasm [GO:0005737]; cytoplasmic vesicle lumen [GO:0060205]; cytosol [GO:0005829]; dendrite cytoplasm [GO:0032839]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lysosome [GO:0005764]; neuronal cell body [GO:0043025]
|
2'-deoxyadenosine deaminase activity [GO:0046936]; adenosine deaminase activity [GO:0004000]; purine nucleoside binding [GO:0001883]; zinc ion binding [GO:0008270]
|
PF00962;
|
3.20.20.140;
|
Metallo-dependent hydrolases superfamily, Adenosine and AMP deaminases family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P00813}; Peripheral membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}. Cell junction {ECO:0000250|UniProtKB:P00813}. Cytoplasmic vesicle lumen {ECO:0000269|PubMed:8783262}. Cytoplasm {ECO:0000250}. Lysosome {ECO:0000250|UniProtKB:P00813}. Note=Colocalized with DPP4 at the cell surface. {ECO:0000250|UniProtKB:P00813}.
|
CATALYTIC ACTIVITY: Reaction=adenosine + H(+) + H2O = inosine + NH4(+); Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; Evidence={ECO:0000269|PubMed:10720488, ECO:0000269|PubMed:8634299, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9272950}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409; Evidence={ECO:0000305|PubMed:10720488}; CATALYTIC ACTIVITY: Reaction=2'-deoxyadenosine + H(+) + H2O = 2'-deoxyinosine + NH4(+); Xref=Rhea:RHEA:28190, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17256, ChEBI:CHEBI:28938, ChEBI:CHEBI:28997; EC=3.5.4.4; Evidence={ECO:0000269|PubMed:10720488}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28191; Evidence={ECO:0000305|PubMed:10720488};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20 uM for adenosine {ECO:0000269|PubMed:8634299, ECO:0000269|PubMed:8672487};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-8.5. {ECO:0000269|PubMed:8634299, ECO:0000269|PubMed:8672487};
| null |
FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine (PubMed:10720488, PubMed:8634299, PubMed:8672487, PubMed:8942668, PubMed:9272950). Plays an important role in purine metabolism and in adenosine homeostasis (PubMed:10720488, PubMed:9272950). Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events (PubMed:11435465). Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (By similarity). Enhances dendritic cell immunogenicity by affecting dendritic cell costimulatory molecule expression and cytokines and chemokines secretion (By similarity). Enhances CD4+ T-cell differentiation and proliferation (By similarity). Acts as a positive modulator of adenosine receptors ADORA1 and ADORA2A, by enhancing their ligand affinity via conformational change (By similarity). Stimulates plasminogen activation (By similarity). Plays a role in male fertility (By similarity). Plays a protective role in early postimplantation embryonic development (PubMed:9272950). {ECO:0000250|UniProtKB:P00813, ECO:0000250|UniProtKB:P56658, ECO:0000269|PubMed:10720488, ECO:0000269|PubMed:11435465, ECO:0000269|PubMed:8634299, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9272950}.
|
Mus musculus (Mouse)
|
P03959
|
KDPA_ECOLI
|
MAAQGFLLIATFLLVLMVLARPLGSGLARLINDIPLPGTTGVERVLFRALGVSDREMNWKQYLCAILGLNMLGLAVLFFMLLGQHYLPLNPQQLPGLSWDLALNTAVSFVTNTNWQSYSGETTLSYFSQMAGLTVQNFLSAASGIAVIFALIRAFTRQSMSTLGNAWVDLLRITLWVLVPVALLIALFFIQQGALQNFLPYQAVNTVEGAQQLLPMGPVASQEAIKMLGTNGGGFFNANSSHPFENPTALTNFVQMLAIFLIPTALCFAFGEVMGDRRQGRMLLWAMSVIFVICVGVVMWAEVQGNPHLLALGTDSSINMEGKESRFGVLVSSLFAVVTTAASCGAVIAMHDSFTALGGMVPMWLMQIGEVVFGGVGSGLYGMMLFVLLAVFIAGLMIGRTPEYLGKKIDVREMKLTALAILVTPTLVLMGAALAMMTDAGRSAMLNPGPHGFSEVLYAVSSAANNNGSAFAGLSANSPFWNCLLAFCMFVGRFGVIIPVMAIAGSLVSKKSQAASSGTLPTHGPLFVGLLIGTVLLVGALTFIPALALGPVAEYLS
| null | null |
monoatomic cation transmembrane transport [GO:0098655]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]
|
plasma membrane [GO:0005886]; potassium ion-transporting ATPase complex [GO:0031004]; potassium:proton antiporter complex [GO:1903103]
|
P-type potassium transmembrane transporter activity [GO:0008556]; potassium ion binding [GO:0030955]
|
PF03814;
| null |
KdpA family
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00275, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2849541, ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378, ECO:0000269|PubMed:7896809}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00275, ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378, ECO:0000269|PubMed:7896809}.
| null | null | null | null | null |
FUNCTION: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm (PubMed:23930894, PubMed:2849541, PubMed:8499455). This subunit binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel (PubMed:30478378, PubMed:34272288, PubMed:7896809). {ECO:0000269|PubMed:23930894, ECO:0000269|PubMed:2849541, ECO:0000269|PubMed:30478378, ECO:0000269|PubMed:34272288, ECO:0000269|PubMed:7896809, ECO:0000269|PubMed:8499455}.
|
Escherichia coli (strain K12)
|
P03960
|
KDPB_ECOLI
|
MSRKQLALFEPTLVVQALKEAVKKLNPQAQWRNPVMFIVWIGSLLTTCISIAMASGAMPGNALFSAAISGWLWITVLFANFAEALAEGRSKAQANSLKGVKKTAFARKLREPKYGAAADKVPADQLRKGDIVLVEAGDIIPCDGEVIEGGASVDESAITGESAPVIRESGGDFASVTGGTRILSDWLVIECSVNPGETFLDRMIAMVEGAQRRKTPNEIALTILLIALTIVFLLATATLWPFSAWGGNAVSVTVLVALLVCLIPTTIGGLLSAIGVAGMSRMLGANVIATSGRAVEAAGDVDVLLLDKTGTITLGNRQASEFIPAQGVDEKTLADAAQLASLADETPEGRSIVILAKQRFNLRERDVQSLHATFVPFTAQSRMSGINIDNRMIRKGSVDAIRRHVEANGGHFPTDVDQKVDQVARQGATPLVVVEGSRVLGVIALKDIVKGGIKERFAQLRKMGIKTVMITGDNRLTAAAIAAEAGVDDFLAEATPEAKLALIRQYQAEGRLVAMTGDGTNDAPALAQADVAVAMNSGTQAAKEAGNMVDLDSNPTKLIEVVHIGKQMLMTRGSLTTFSIANDVAKYFAIIPAAFAATYPQLNALNIMCLHSPDSAILSAVIFNALIIVFLIPLALKGVSYKPLTASAMLRRNLWIYGLGGLLVPFIGIKVIDLLLTVCGLV
|
7.2.2.6
| null |
monoatomic cation transmembrane transport [GO:0098655]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]
|
plasma membrane [GO:0005886]; potassium ion-transporting ATPase complex [GO:0031004]; potassium:proton antiporter complex [GO:1903103]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; magnesium ion binding [GO:0000287]; P-type potassium transmembrane transporter activity [GO:0008556]
|
PF00122;PF00702;
|
3.40.1110.10;2.70.150.10;3.40.50.1000;
|
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IA subfamily
|
PTM: Phosphorylated at Ser-162, which leads to the inhibition of the ATPase activity. {ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378}.
|
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00285, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2849541, ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00285, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + K(+)(out) = ADP + H(+) + K(+)(in) + phosphate; Xref=Rhea:RHEA:16777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00285, ECO:0000269|PubMed:2849541, ECO:0000269|PubMed:34272288}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16778; Evidence={ECO:0000255|HAMAP-Rule:MF_00285, ECO:0000269|PubMed:2849541, ECO:0000269|PubMed:34272288};
| null | null | null | null |
FUNCTION: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm (PubMed:23930894, PubMed:2849541, PubMed:8499455). This subunit is responsible for energy coupling to the transport system and for the release of the potassium ions to the cytoplasm (PubMed:16354672, PubMed:30478378, PubMed:34272288). {ECO:0000269|PubMed:16354672, ECO:0000269|PubMed:23930894, ECO:0000269|PubMed:2849541, ECO:0000269|PubMed:30478378, ECO:0000269|PubMed:34272288, ECO:0000269|PubMed:8499455}.
|
Escherichia coli (strain K12)
|
P03961
|
KDPC_ECOLI
|
MSGLRPALSTFIFLLLITGGVYPLLTTVLGQWWFPWQANGSLIREGDTVRGSALIGQNFTGNGYFHGRPSATAEMPYNPQASGGSNLAVSNPELDKLIAARVAALRAANPDASASVPVELVTASASGLDNNITPQAAAWQIPRVAKARNLSVEQLTQLIAKYSQQPLVKYIGQPVVNIVELNLALDKLDE
| null | null |
monoatomic cation transmembrane transport [GO:0098655]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]
|
plasma membrane [GO:0005886]; potassium ion-transporting ATPase complex [GO:0031004]; potassium:proton antiporter complex [GO:1903103]
|
ATP binding [GO:0005524]; P-type potassium transmembrane transporter activity [GO:0008556]
|
PF02669;
| null |
KdpC family
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00276, ECO:0000269|PubMed:2849541, ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00276, ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378}.
| null | null | null | null | null |
FUNCTION: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm (PubMed:23930894, PubMed:2849541, PubMed:8499455). This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex (PubMed:21711450). {ECO:0000269|PubMed:21711450, ECO:0000269|PubMed:23930894, ECO:0000269|PubMed:2849541, ECO:0000269|PubMed:8499455}.
|
Escherichia coli (strain K12)
|
P03962
|
PYRF_YEAST
|
MSKATYKERAATHPSPVAAKLFNIMHEKQTNLCASLDVRTTKELLELVEALGPKICLLKTHVDILTDFSMEGTVKPLKALSAKYNFLLFEDRKFADIGNTVKLQYSAGVYRIAEWADITNAHGVVGPGIVSGLKQAAEEVTKEPRGLLMLAELSCKGSLATGEYTKGTVDIAKSDKDFVIGFIAQRDMGGRDEGYDWLIMTPGVGLDDKGDALGQQYRTVDDVVSTGSDIIIVGRGLFAKGRDAKVEGERYRKAGWEAYLRRCGQQN
|
4.1.1.23
| null |
'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; UMP biosynthetic process [GO:0006222]
|
cytosol [GO:0005829]
|
orotate phosphoribosyltransferase activity [GO:0004588]; orotidine-5'-phosphate decarboxylase activity [GO:0004590]
|
PF00215;
|
3.20.20.70;
|
OMP decarboxylase family
| null | null |
CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU10110};
| null |
PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
| null | null | null |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P03965
|
CARB_YEAST
|
MTSIYTSTEPTNSAFTTEDYKPQLVEGVNSVLVIGSGGLSIGQAGEFDYSGSQAIKALKEDNKFTILVNPNIATNQTSHSLADKIYYLPVTPEYITYIIELERPDAILLTFGGQTGLNCGVALDESGVLAKYNVKVLGTPIKTLITSEDRDLFASALKDINIPIAESFACETVDEALEAAERVKYPVIVRSAYALGGLGSGFANNASEMKELAAQSLSLAPQILVEKSLKGWKEVEYEVVRDRVGNCITVCNMENFDPLGVHTGDSMVFAPSQTLSDEEFHMLRSAAIKIIRHLGVIGECNVQYALQPDGLDYRVIEVNARLSRSSALASKATGYPLAYTAAKIGLGYTLPELPNPITKTTVANFEPSLDYIVAKIPKWDLSKFQYVDRSIGSSMKSVGEVMAIGRNYEEAFQKALRQVDPSLLGFQGSTEFGDQLDEALRTPTDRRVLAIGQALIHENYTVERVNELSKIDKWFLYKCMNIVNIYKELESVKSLSDLSKDLLQRAKKLGFSDKQIAVTINKHASTNINELEIRSLRKTLGIIPFVKRIDTLAAEFPAQTNYLYTTYNATKNDVEFNENGMLVLGSGVYRIGSSVEFDWCAVNTAKTLRDQGKKTIMINYNPETVSTDFDEVDRLYFEELSYERVMDIYELEQSEGCIISVGGQLPQNIALKLYDNGCNIMGTNPNDIDRAENRHKFSSILDSIDVDQPEWSELTSVEEAKLFASKVNYPVLIRPSYVLSGAAMSVVNNEEELKAKLTLASDVSPDHPVVMSKFIEGAQEIDVDAVAYNGNVLVHAISEHVENAGVHSGDASLVLPPQHLSDDVKIALKDIADKVAKAWKITGPFNMQIIKDGEHTLKVIECNIRASRSFPFVSKVLGVNFIEIAVKAFLGGDIVPKPVDLMLNKKYDYVATKVPQFSFTRLAGADPFLGVEMASTGEVASFGRDLIESYWTAIQSTMNFHVPLPPSGILFGGDTSREYLGQVASIVATIGYRIYTTNETTKTYLQEHIKEKNAKVSLIKFPKNDKRKLRELFQEYDIKAVFNLASKRAESTDDVDYIMRRNAIDFAIPLFNEPQTALLFAKCLKAKIAEKIKILESHDVIVPPEVRSWDEFIGFKAY
|
6.3.4.16; 6.3.5.5
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00409};
|
'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; arginine biosynthetic process [GO:0006526]; citrulline biosynthetic process [GO:0019240]; glutamine metabolic process [GO:0006541]; pyrimidine nucleotide biosynthetic process [GO:0006221]; UTP biosynthetic process [GO:0006228]
|
carbamoyl-phosphate synthase complex [GO:0005951]; cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
aspartate carbamoyltransferase activity [GO:0004070]; ATP binding [GO:0005524]; carbamoyl-phosphate synthase (ammonia) activity [GO:0004087]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; dihydroorotase activity [GO:0004151]; metal ion binding [GO:0046872]
|
PF02786;PF02787;PF02142;
|
3.40.50.20;3.30.1490.20;3.30.470.20;1.10.1030.10;3.40.50.1380;
|
CarB family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:200419, ECO:0000269|PubMed:205532}.
|
CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000269|PubMed:206535, ECO:0000269|PubMed:206652, ECO:0000269|PubMed:5856369}; CATALYTIC ACTIVITY: [Carbamoyl phosphate synthase arginine-specific large chain]: Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:456216; EC=6.3.4.16; Evidence={ECO:0000269|PubMed:206535, ECO:0000269|PubMed:206652, ECO:0000269|PubMed:5856369};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.3 mM for hydrogencarbonate {ECO:0000269|PubMed:206535}; KM=75 mM for NH4(+) {ECO:0000269|PubMed:206535}; KM=0.2 mM for ATP {ECO:0000269|PubMed:206652}; KM=6.08 mM for ATP (for the ammonia-dependent ATPase reaction) {ECO:0000269|PubMed:12392708}; Vmax=0.64 umol/min/mg enzyme (for the ammonia-dependent ATPase reaction) {ECO:0000269|PubMed:12392708};
|
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. {ECO:0000305|PubMed:5856369}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:206652};
| null |
FUNCTION: Large subunit of the arginine-specific carbamoyl phosphate synthase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, hydrogencarbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate. {ECO:0000269|PubMed:206535, ECO:0000269|PubMed:4594376, ECO:0000269|PubMed:5856369, ECO:0000269|Ref.6}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P03966
|
MYCN_MOUSE
|
MPSCTASTMPGMICKNPDLEFDSLQPCFYPDEDDFYFGGPDSTPPGEDIWKKFELLPTPPLSPSRAFPEHSPEPSNWATEMLLPEADLWGNPAEEDAFGLGGLGGLTPNPVILQDCMWSGFSAREKLERAVNEKLQHGHGPPGVSSACSAPGVGASSPGGRALGGSSSASHTGATLPTDLSHPAAECVDPAVVFPFPVNKRESASVPAAPTSAPATSAAVTSVSVPATAPVAAPARAGGRPASSGEAKALSTSGEDTLSDSDDEDDEEEDEEEEIDVVTVEKRRSSSNNKAVTTFTITVRPKTSALGLGRAQPGELILKRCVPIHQQHNYAAPSPYVESEDAPPQKKIKSEASPRPLKSVVPAKAKSLSPRNSDSEDSERRRNHNILERQRRNDLRSSFLTLRDHVPELVKNEKAAKVVILKKATEYVHALQANEHQLLLEKEKLQARQQQLLKKIEHARTC
| null | null |
astrocyte differentiation [GO:0048708]; autosome genomic imprinting [GO:0141068]; branching morphogenesis of an epithelial tube [GO:0048754]; cartilage condensation [GO:0001502]; cell population proliferation [GO:0008283]; embryonic digit morphogenesis [GO:0042733]; embryonic skeletal system morphogenesis [GO:0048704]; epithelial cell proliferation [GO:0050673]; lung development [GO:0030324]; negative regulation of astrocyte differentiation [GO:0048712]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of mesenchymal cell proliferation [GO:0002053]; positive regulation of programmed cell death [GO:0043068]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of inner ear auditory receptor cell differentiation [GO:0045607]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00010;PF01056;
|
4.10.280.10;
| null |
PTM: Phosphorylated by GSK3-beta which may promote its degradation. Phosphorylated by AURKA. {ECO:0000250|UniProtKB:P04198}.
|
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Positively regulates the transcription of MYCNOS in neuroblastoma cells. {ECO:0000250|UniProtKB:P04198}.
|
Mus musculus (Mouse)
|
P03967
|
RASD_DICDI
|
MTEYKLVIVGGGGVGKSALTIQLIQNHFIDEYDPTIEDSYRKQVSIDDETCLLDILDTAGQEEYSAMRDQYMRTGQGFLCVYSITSRSSYDEIASFREQILRVKDKDRVPLILVGNKADLDHERQVSVNEGQELAKGFNCPFMESSAKSRINVEEAFYSLVREIRKELKGDQSSGKAQKKKKQCLIL
|
3.6.5.2
| null |
adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway [GO:0140582]; chemotaxis [GO:0006935]; ERK1 and ERK2 cascade [GO:0070371]; mitotic cytokinesis [GO:0000281]; phototaxis [GO:0042331]; Ras protein signal transduction [GO:0007265]; response to bacterium [GO:0009617]; thermotaxis [GO:0043052]
|
cytosol [GO:0005829]; lipid droplet [GO:0005811]; plasma membrane [GO:0005886]
|
filamin binding [GO:0031005]; G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; mitogen-activated protein kinase binding [GO:0051019]; protein kinase B binding [GO:0043422]; protein kinase inhibitor activity [GO:0004860]; protein kinase regulator activity [GO:0019887]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Ras family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000305|PubMed:18948008};
| null | null | null | null |
FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. {ECO:0000269|PubMed:18948008}.
|
Dictyostelium discoideum (Social amoeba)
|
P03968
|
FGF1_BOVIN
|
MAEGETTTFTALTEKFNLPLGNYKKPKLLYCSNGGYFLRILPDGTVDGTKDRSDQHIQLQLCAESIGEVYIKSTETGQFLAMDTDGLLYGSQTPNEECLFLERLEENHYNTYISKKHAEKHWFVGLKKNGRSKLGPRTHFGQKAILFLPLPVSSD
| null | null |
activation of protein kinase B activity [GO:0032148]; angiogenesis [GO:0001525]; animal organ morphogenesis [GO:0009887]; branch elongation involved in ureteric bud branching [GO:0060681]; cell differentiation [GO:0030154]; cellular response to heat [GO:0034605]; fibroblast growth factor receptor signaling pathway [GO:0008543]; lung development [GO:0030324]; mesonephric epithelium development [GO:0072163]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cell division [GO:0051781]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cholesterol biosynthetic process [GO:0045542]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of gene expression [GO:0010628]; positive regulation of intracellular signal transduction [GO:1902533]; positive regulation of sprouting angiogenesis [GO:1903672]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of endothelial tube morphogenesis [GO:1901509]; wound healing [GO:0042060]
|
cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634]
|
fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; integrin binding [GO:0005178]; S100 protein binding [GO:0044548]
|
PF00167;
|
2.80.10.50;
|
Heparin-binding growth factors family
|
PTM: In the nucleus, phosphorylated by PKC/PRKCD. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted. Cytoplasm {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytosol. Nucleus. Note=Lacks a cleavable signal sequence. Within the cytoplasm, it is transported to the cell membrane and then secreted by a non-classical pathway that requires Cu(2+) ions and S100A13. Secreted in a complex with SYT1. Binding of exogenous FGF1 to FGFR facilitates endocytosis followed by translocation of FGF1 across endosomal membrane into the cytosol. Nuclear import from the cytosol requires the classical nuclear import machinery, involving proteins KPNA1 and KPNB1, as well as LRRC59 (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as a potent mitogen in vitro. Acts as a ligand for FGFR1 and integrins. Binds to FGFR1 in the presence of heparin leading to FGFR1 dimerization and activation via sequential autophosphorylation on tyrosine residues which act as docking sites for interacting proteins, leading to the activation of several signaling cascades. Binds to integrin ITGAV:ITGB3. Its binding to integrin, subsequent ternary complex formation with integrin and FGFR1, and the recruitment of PTPN11 to the complex are essential for FGF1 signaling. Induces the phosphorylation and activation of FGFR1, FRS2, MAPK3/ERK1, MAPK1/ERK2 and AKT1. Can induce angiogenesis (By similarity). {ECO:0000250|UniProtKB:P05230, ECO:0000269|PubMed:11039909, ECO:0000269|PubMed:9712834}.
|
Bos taurus (Bovine)
|
P03969
|
FGF2_BOVIN
|
MAAGSITTLPALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYSSWYVALKRTGQYKLGPKTGPGQKAILFLPMSAKS
| null | null |
angiogenesis [GO:0001525]; animal organ morphogenesis [GO:0009887]; branching involved in ureteric bud morphogenesis [GO:0001658]; cell differentiation [GO:0030154]; fibroblast growth factor receptor signaling pathway [GO:0008543]; lung development [GO:0030324]; positive regulation of angiogenesis [GO:0045766]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of cell division [GO:0051781]; positive regulation of cell migration involved in sprouting angiogenesis [GO:0090050]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of gene expression [GO:0010628]; positive regulation of lens fiber cell differentiation [GO:1902748]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of sprouting angiogenesis [GO:1903672]; positive regulation of transcription by RNA polymerase II [GO:0045944]; signal transduction [GO:0007165]; wound healing [GO:0042060]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]
|
fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; integrin binding [GO:0005178]
|
PF00167;
|
2.80.10.50;
|
Heparin-binding growth factors family
|
PTM: Phosphorylation at Tyr-82 regulates FGF2 unconventional secretion. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P09038}. Nucleus {ECO:0000250|UniProtKB:P09038}. Note=Exported from cells by an endoplasmic reticulum (ER)/Golgi-independent mechanism (By similarity). Unconventional secretion of FGF2 occurs by direct translocation across the plasma membrane (By similarity). Binding of exogenous FGF2 to FGFR facilitates endocytosis followed by translocation of FGF2 across endosomal membrane into the cytosol (By similarity). Nuclear import from the cytosol requires the classical nuclear import machinery, involving proteins KPNA1 and KPNB1, as well as CEP57 (By similarity). {ECO:0000250|UniProtKB:P09038}.
| null | null | null | null | null |
FUNCTION: Acts as a ligand for FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Also acts as an integrin ligand which is required for FGF2 signaling (By similarity). Binds to integrin ITGAV:ITGB3 (By similarity). Plays an important role in the regulation of cell survival, cell division, cell differentiation and cell migration (By similarity). Functions as a potent mitogen in vitro (By similarity). Can induce angiogenesis (By similarity). Mediates phosphorylation of ERK1/2 and thereby promotes retinal lens fiber differentiation (By similarity). {ECO:0000250|UniProtKB:P09038}.
|
Bos taurus (Bovine)
|
P03970
|
INHBA_PIG
|
MPLLWLRGFLLASCWIIVRSSPTPGSGGHSAAPDCPSCALATLPKDVPNSQPEMVEAVKKHILNMLHLKKRPDVTQPVPKAALLNAIRKLHVGKVGENGYVELEDDIGRRAEMNELMEQTSEIITFAEAGTARKTLRFEISKEGSDLSVVERAEIWLFLKVPKANRTRTKVSIRLFQQQRRPQGSADAGEEAEDVGFPEEKSEVLISEKVVDARKSTWHIFPVSSSIQRLLDQGKSALDIRTACEQCHETGASLVLLGKKKKKEEEAEGRKRDGEGAGVDEEKEQSHRPFLMLQARQSEEHPHRRRRRGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS
| null | null |
activin receptor signaling pathway [GO:0032924]; eyelid development in camera-type eye [GO:0061029]; hair follicle development [GO:0001942]; hematopoietic progenitor cell differentiation [GO:0002244]; hemoglobin biosynthetic process [GO:0042541]; male gonad development [GO:0008584]; negative regulation of cell growth [GO:0030308]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; odontogenesis [GO:0042476]; ovarian follicle development [GO:0001541]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of erythrocyte differentiation [GO:0045648]; positive regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001241]; positive regulation of ovulation [GO:0060279]; positive regulation of transcription by RNA polymerase II [GO:0045944]; progesterone secretion [GO:0042701]; regulation of follicle-stimulating hormone secretion [GO:0046880]; regulation of transcription by RNA polymerase II [GO:0006357]; roof of mouth development [GO:0060021]
|
activin A complex [GO:0043509]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; inhibin A complex [GO:0043512]
|
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; hormone activity [GO:0005179]
|
PF00019;PF00688;
|
2.60.120.970;2.10.90.10;
|
TGF-beta family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.
|
Sus scrofa (Pig)
|
P03971
|
MIS_HUMAN
|
MRDLPLTSLALVLSALGALLGTEALRAEEPAVGTSGLIFREDLDWPPGSPQEPLCLVALGGDSNGSSSPLRVVGALSAYEQAFLGAVQRARWGPRDLATFGVCNTGDRQAALPSLRRLGAWLRDPGGQRLVVLHLEEVTWEPTPSLRFQEPPPGGAGPPELALLVLYPGPGPEVTVTRAGLPGAQSLCPSRDTRYLVLAVDRPAGAWRGSGLALTLQPRGEDSRLSTARLQALLFGDDHRCFTRMTPALLLLPRSEPAPLPAHGQLDTVPFPPPRPSAELEESPPSADPFLETLTRLVRALRVPPARASAPRLALDPDALAGFPQGLVNLSDPAALERLLDGEEPLLLLLRPTAATTGDPAPLHDPTSAPWATALARRVAAELQAAAAELRSLPGLPPATAPLLARLLALCPGGPGGLGDPLRALLLLKALQGLRVEWRGRDPRGPGRAQRSAGATAADGPCALRELSVDLRAERSVLIPETYQANNCQGVCGWPQSDRNPRYGNHVVLLLKMQVRGAALARPPCCVPTAYAGKLLISLSEERISAHHVPNMVATECGCR
| null | null |
anti-Mullerian hormone signaling pathway [GO:1990262]; cell-cell signaling [GO:0007267]; gonadal mesoderm development [GO:0007506]; Leydig cell differentiation [GO:0033327]; Mullerian duct regression [GO:0001880]; negative regulation of ovarian follicle development [GO:2000355]; ovarian follicle development [GO:0001541]; positive regulation of gene expression [GO:0010628]; positive regulation of SMAD protein signal transduction [GO:0060391]; preantral ovarian follicle growth [GO:0001546]; response to organic cyclic compound [GO:0014070]; response to xenobiotic stimulus [GO:0009410]; sex determination [GO:0007530]; sex differentiation [GO:0007548]; urogenital system development [GO:0001655]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
growth factor activity [GO:0008083]; hormone activity [GO:0005179]; signaling receptor binding [GO:0005102]; type II transforming growth factor beta receptor binding [GO:0005114]
|
PF04709;PF00019;
|
2.10.90.10;
|
TGF-beta family
|
PTM: Preproprotein is proteolytically processed to generate N- and C-terminal cleavage products that homodimerize and associate to form a biologically active non-covalent complex (PubMed:2974034, PubMed:8469238). Binding of the non-covalent complex to AMHR2 induces dissociation of the pro-region from the mature C-terminal dimer (PubMed:20861221). The N-terminal portion of the protein, despite having no intrinsic activity, has the role of amplifying the activity of the C-terminus (PubMed:20861221, PubMed:8469238). {ECO:0000269|PubMed:20861221, ECO:0000269|PubMed:2974034, ECO:0000269|PubMed:8469238}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2974034, ECO:0000269|PubMed:3754790}.
| null | null | null | null | null |
FUNCTION: Plays an important role in several reproductive functions. Induces Muellerian duct regression during male fetal sexual differentiation (PubMed:34155118, PubMed:3754790, PubMed:8469238). Also plays a role in Leydig cell differentiation and function (By similarity). In female acts as a negative regulator of the primordial to primary follicle transition and decreases FSH sensitivity of growing follicles (PubMed:14742691). AMH signals by binding to a specific type-II receptor, AMHR2, that heterodimerizes with type-I receptors (ACVR1 and BMPR1A), and recruiting SMAD proteins that are translocated to the nucleus to regulate target gene expression (PubMed:20861221, PubMed:34155118). {ECO:0000250|UniProtKB:P27106, ECO:0000269|PubMed:14742691, ECO:0000269|PubMed:20861221, ECO:0000269|PubMed:34155118, ECO:0000269|PubMed:3754790, ECO:0000269|PubMed:8469238}.
|
Homo sapiens (Human)
|
P03973
|
SLPI_HUMAN
|
MKSSGLFPFLVLLALGTLAPWAVEGSGKSFKAGVCPPKKSAQCLRYKKPECQSDWQCPGKKRCCPDTCGIKCLDPVDTPNPTRRKPGKCPVTYGQCLMLNPPNFCEMDGQCKRDLKCCMGMCGKSCVSPVKA
| null | null |
antibacterial humoral response [GO:0019731]; immune response [GO:0006955]; innate immune response [GO:0045087]; modulation of process of another organism [GO:0035821]; negative regulation of protein binding [GO:0032091]; negative regulation of viral genome replication [GO:0045071]; response to lipopolysaccharide [GO:0032496]
|
collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; specific granule lumen [GO:0035580]
|
DNA binding [GO:0003677]; endopeptidase inhibitor activity [GO:0004866]; enzyme binding [GO:0019899]; mRNA binding [GO:0003729]; serine-type endopeptidase inhibitor activity [GO:0004867]
|
PF00095;
|
4.10.75.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2039600, ECO:0000269|PubMed:24352879, ECO:0000269|PubMed:3462719, ECO:0000269|PubMed:3485543}.
| null | null | null | null | null |
FUNCTION: Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G (PubMed:10702419, PubMed:2039600, PubMed:2110563, PubMed:24121345, PubMed:3462719, PubMed:3533531). Modulates the inflammatory and immune responses after bacterial infection, and after infection by the intracellular parasite L.major. Down-regulates responses to bacterial lipopolysaccharide (LPS) (By similarity). Plays a role in regulating the activation of NF-kappa-B and inflammatory responses (PubMed:10702419, PubMed:24352879). Has antimicrobial activity against mycobacteria, but not against salmonella. Contributes to normal resistance against infection by M.tuberculosis. Required for normal resistance to infection by L.major. Required for normal wound healing, probably by preventing tissue damage by limiting protease activity (By similarity). Together with ELANE, required for normal differentiation and proliferation of bone marrow myeloid cells (PubMed:24352879). {ECO:0000250|UniProtKB:P97430, ECO:0000269|PubMed:10702419, ECO:0000269|PubMed:2039600, ECO:0000269|PubMed:2110563, ECO:0000269|PubMed:24121345, ECO:0000269|PubMed:24352879, ECO:0000269|PubMed:3462719, ECO:0000269|PubMed:3533531, ECO:0000305}.
|
Homo sapiens (Human)
|
P03974
|
TERA_PIG
|
MASGADSKGDDLSTAILKQKNRPNRLIVDEAINEDNSVVSLSQPKMDELQLFRGDTVLLKGKKRREAVCIVLSDDTCSDEKIRMNRVVRNNLRVHLGDVISIQPCPDVKYGKRIHVLPIDDTVEGITGNLFEVYLKPYFLEAYRPIRKGDIFLVRGGMRAVEFKVVETDPSPYCIVAPDTVIHCEGEPIKREDEEESLNEVGYDDIGGCRKQLAQIKEMVELPLRHPALFKAIGVKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAIIFIDELDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFDREVDIGIPDATGRLEILQIHTKNMKLADDVDLEQVANETHGHVGADLAALCSEAALQAIRKKMDLIDLEDETIDAEVMNSLAVTMDDFRWALSQSNPSALRETVVEVPQVTWEDIGGLEDVKRELQDLVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLAIRESIESEIRRERERQTNPSAMEVEEDDPVPEIRRDHFEEAMRFARRSVSDNDIRKYEMFAQTLQQSRGFGSFRFPSGNQGGAGPSQGSGGGTGGSVYTEDNDDDLYG
|
3.6.4.6
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
autophagosome maturation [GO:0097352]; autophagy [GO:0006914]; cellular response to arsenite ion [GO:1903843]; cellular response to heat [GO:0034605]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; endoplasmic reticulum stress-induced pre-emptive quality control [GO:0061857]; endosome to lysosome transport via multivesicular body sorting pathway [GO:0032510]; ERAD pathway [GO:0036503]; interstrand cross-link repair [GO:0036297]; macroautophagy [GO:0016236]; mitotic spindle disassembly [GO:0051228]; proteasomal protein catabolic process [GO:0010498]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination [GO:0016567]; protein-DNA covalent cross-linking repair [GO:0106300]; regulation of protein localization to chromatin [GO:1905634]; retrograde protein transport, ER to cytosol [GO:0030970]; stress granule disassembly [GO:0035617]; translesion synthesis [GO:0019985]
|
cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]; VCP-NPL4-UFD1 AAA ATPase complex [GO:0034098]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; lipid binding [GO:0008289]; polyubiquitin modification-dependent protein binding [GO:0031593]
|
PF00004;PF17862;PF02933;PF02359;
|
1.10.8.60;2.40.40.20;3.10.330.10;6.10.20.150;3.40.50.300;
|
AAA ATPase family
|
PTM: ISGylated. {ECO:0000250|UniProtKB:P55072}.; PTM: Methylation at Lys-315 catalyzed by VCPKMT is increased in the presence of ASPSCR1. Lys-315 methylation may decrease ATPase activity. {ECO:0000250|UniProtKB:P55072}.; PTM: Phosphorylated by tyrosine kinases in response to T-cell antigen receptor activation. Phosphorylated in mitotic cells. {ECO:0000250|UniProtKB:P46462}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P55072}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P55072}. Nucleus {ECO:0000250|UniProtKB:P55072}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P55072}. Note=Recruited to the cytoplasmic surface of the endoplasmic reticulum via interaction with AMFR/gp78. Following DNA double-strand breaks, recruited to the sites of damage. Recruited to stalled replication forks via interaction with SPRTN. Recruited to damaged lysosomes decorated with K48-linked ubiquitin chains. Colocalizes with TIA1, ZFAND1 and G3BP1 in cytoplasmic stress granules (SGs) in response to arsenite-induced stress treatment (By similarity). {ECO:0000250|UniProtKB:P55072}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6; Evidence={ECO:0000250|UniProtKB:P55072};
| null | null | null | null |
FUNCTION: Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. Regulates E3 ubiquitin-protein ligase activity of RNF19A. Component of the VCP/p97-AMFR/gp78 complex that participates in the final step of the sterol-mediated ubiquitination and endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Mediates the endoplasmic reticulum-associated degradation of CHRNA3 in cortical neurons as part of the STUB1-VCP-UBXN2A complex (By similarity). Involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. Involved in clearance process by mediating G3BP1 extraction from stress granules. Also involved in DNA damage response: recruited to double-strand breaks (DSBs) sites in a RNF8- and RNF168-dependent manner and promotes the recruitment of TP53BP1 at DNA damage sites. Recruited to stalled replication forks by SPRTN: may act by mediating extraction of DNA polymerase eta (POLH) to prevent excessive translesion DNA synthesis and limit the incidence of mutations induced by DNA damage. Together with SPRTN metalloprotease, involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis. Involved in interstrand cross-link repair in response to replication stress by mediating unloading of the ubiquitinated CMG helicase complex. Mediates extraction of PARP1 trapped to chromatin: recognizes and binds ubiquitinated PARP1 and promotes its removal. Required for cytoplasmic retrotranslocation of stressed/damaged mitochondrial outer-membrane proteins and their subsequent proteasomal degradation. Essential for the maturation of ubiquitin-containing autophagosomes and the clearance of ubiquitinated protein by autophagy. Acts as a negative regulator of type I interferon production by interacting with RIGI: interaction takes place when RIGI is ubiquitinated via 'Lys-63'-linked ubiquitin on its CARD domains, leading to recruit RNF125 and promote ubiquitination and degradation of RIGI. May play a role in the ubiquitin-dependent sorting of membrane proteins to lysosomes where they undergo degradation. May more particularly play a role in caveolins sorting in cells. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (By similarity). {ECO:0000250|UniProtKB:P23787, ECO:0000250|UniProtKB:P46462, ECO:0000250|UniProtKB:P55072}.
|
Sus scrofa (Pig)
|
P03991
|
HA1W_MOUSE
|
MAPCMLLLLLAAALAPTQTRAGPHSLRYFHTAVSRPGLGKPRFISVGYVDDTEFVRFDSDAENPRYEPRARWMEQVEPEYWERNTQIAKDNEQSSRVDLRTLLRYYNQSAGGSHTIQRMYGCDVGSDGRLLRGYEQVAYDGCDYIALNEDLKTWTAADMAALITKHKWEQAGAAERRRAYLEGACVEWLSRHLKNGNATLLRTDSPKAHVTHHSRPEDKVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQYYTCHVYHQGLPKPLTLRWEPPPSAVSNTVIIAVLVVLGAAIVTGAVVAFVMMRRRNTGGKGGDYALAPGSQTSDLSLPDCKVMVHDPHSLA
| null | null |
antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent [GO:0002485]; antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; defense response to bacterium [GO:0042742]; immune response [GO:0006955]; inner ear development [GO:0048839]; negative regulation of neuron projection development [GO:0010977]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; T cell mediated cytotoxicity [GO:0001913]
|
external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]
|
beta-2-microglobulin binding [GO:0030881]; peptide antigen binding [GO:0042605]; peptide binding [GO:0042277]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102]
|
PF07654;PF00129;PF06623;
|
2.60.40.10;3.30.500.10;
|
MHC class I family
| null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Involved in the presentation of foreign antigens to the immune system.
|
Mus musculus (Mouse)
|
P03994
|
HPLN1_RAT
|
MRSLLFLVLISVCRADHLSDSYTPDQDRVIHIQAENGPRLLVEAEQAKVFSHRGGNVTLPCKFYRDPTAFGSGIHKIRIKWTKLTSDYLREVDVFVSMGYHKKTYGGYQGRVFLKGGSDNDASLIITDLTLEDYGRYKCEVIEGLEDDTAVVALELQGVVFPYFPRLGRYNLNFHEARQACLDQDAVIASFDQLYDAWRGGLDWCNAGWLSDGSVQYPITKPREPCGGQNTVPGVRNYGFWDKDKSRYDVFCFTSNFNGRFYYLIHPTKLTYDEAVQACLNDGAQIAKVGQIFAAWKLLGYDRCDAGWLADGSVRYPISRPRRRCSPTEAAVRFVGFPDKKHKLYGVYCFRAYN
| null | null |
cell adhesion [GO:0007155]; central nervous system development [GO:0007417]; glial cell differentiation [GO:0010001]; positive regulation of neuroblast proliferation [GO:0002052]; skeletal system development [GO:0001501]
|
extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; perineuronal net [GO:0072534]; synapse [GO:0045202]
|
hyaluronic acid binding [GO:0005540]; structural molecule activity [GO:0005198]
|
PF07686;PF00193;
|
2.60.40.10;3.10.100.10;
|
HAPLN family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix.
| null | null | null | null | null |
FUNCTION: Stabilizes the aggregates of proteoglycan monomers with hyaluronic acid in the extracellular cartilage matrix.
|
Rattus norvegicus (Rat)
|
P03995
|
GFAP_MOUSE
|
MERRRITSARRSYASETVVRGLGPSRQLGTMPRFSLSRMTPPLPARVDFSLAGALNAGFKETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELREQLAQQQVHVEMDVAKPDLTAALREIRTQYEAVATSNMQETEEWYRSKFADLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLRGTNESLERQMREQEERHARESASYQEALARLEEEGQSLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEENRITIPVQTFSNLQIRETSLDTKSVSEGHLKRNIVVKTVEMRDGEVIKDSKQEHKDVVM
| null | null |
astrocyte development [GO:0014002]; Bergmann glial cell differentiation [GO:0060020]; D-aspartate import across plasma membrane [GO:0070779]; extracellular matrix organization [GO:0030198]; gene expression [GO:0010467]; intermediate filament organization [GO:0045109]; intermediate filament-based process [GO:0045103]; intracellular protein transport [GO:0006886]; long-term synaptic potentiation [GO:0060291]; negative regulation of neuron projection development [GO:0010977]; neuron projection development [GO:0031175]; neuron projection regeneration [GO:0031102]; positive regulation of glial cell proliferation [GO:0060252]; positive regulation of Schwann cell proliferation [GO:0010625]; regulation of chaperone-mediated autophagy [GO:1904714]; regulation of neurotransmitter uptake [GO:0051580]; Schwann cell proliferation [GO:0014010]
|
astrocyte end-foot [GO:0097450]; astrocyte projection [GO:0097449]; cell body [GO:0044297]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytoplasmic side of lysosomal membrane [GO:0098574]; cytoskeleton [GO:0005856]; glial cell projection [GO:0097386]; intermediate filament [GO:0005882]; membrane [GO:0016020]; myelin sheath [GO:0043209]
|
identical protein binding [GO:0042802]; integrin binding [GO:0005178]; kinase binding [GO:0019900]; structural constituent of cytoskeleton [GO:0005200]
|
PF00038;PF04732;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
|
PTM: Phosphorylated by PKN1. {ECO:0000250|UniProtKB:P14136}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P14136}. Note=Associated with intermediate filaments. {ECO:0000250|UniProtKB:P14136}.
| null | null | null | null | null |
FUNCTION: GFAP, a class-III intermediate filament, is a cell-specific marker that, during the development of the central nervous system, distinguishes astrocytes from other glial cells.
|
Mus musculus (Mouse)
|
P03999
|
OPSB_HUMAN
|
MSEEEFYLFKNISSVGPWDGPQYHIAPVWAFYLQAAFMGTVFLIGFPLNAMVLVATLRYKKLRQPLNYILVNVSFGGFLLCIFSVFPVFVASCNGYFVFGRHVCALEGFLGTVAGLVTGWSLAFLAFERYIVICKPFGNFRFSSKHALTVVLATWTIGIGVSIPPFFGWSRFIPEGLQCSCGPDWYTVGTKYRSESYTWFLFIFCFIVPLSLICFSYTQLLRALKAVAAQQQESATTQKAEREVSRMVVVMVGSFCVCYVPYAAFAMYMVNNRNHGLDLRLVTIPSFFSKSACIYNPIIYCFMNKQFQACIMKMVCGKAMTDESDTCSSQKTEVSTVSSTQVGPN
| null | null |
cellular response to light stimulus [GO:0071482]; cellular response to UV-A [GO:0071492]; G protein-coupled receptor signaling pathway [GO:0007186]; phototransduction [GO:0007602]; signal transduction [GO:0007165]; visual perception [GO:0007601]
|
cone photoreceptor outer segment [GO:0120199]; cytosol [GO:0005829]; intercellular bridge [GO:0045171]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; photoreceptor disc membrane [GO:0097381]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]
|
G protein-coupled photoreceptor activity [GO:0008020]; signaling receptor activity [GO:0038023]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family, Opsin subfamily
|
PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2937147, ECO:0000269|PubMed:31380578, ECO:0000269|PubMed:31730232}; Multi-pass membrane protein {ECO:0000255}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P51491}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P51491}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:30168605}.
| null | null | null | null | null |
FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal (Probable). Required for the maintenance of cone outer segment organization in the ventral retina, but not essential for the maintenance of functioning cone photoreceptors (By similarity). Involved in ensuring correct abundance and localization of retinal membrane proteins (By similarity). May increase spectral sensitivity in dim light (By similarity). {ECO:0000250|UniProtKB:P51491, ECO:0000305|PubMed:2937147}.
|
Homo sapiens (Human)
|
P04000
|
OPSR_HUMAN
|
MAQQWSLQRLAGRHPQDSYEDSTQSSIFTYTNSNSTRGPFEGPNYHIAPRWVYHLTSVWMIFVVTASVFTNGLVLAATMKFKKLRHPLNWILVNLAVADLAETVIASTISIVNQVSGYFVLGHPMCVLEGYTVSLCGITGLWSLAIISWERWMVVCKPFGNVRFDAKLAIVGIAFSWIWAAVWTAPPIFGWSRYWPHGLKTSCGPDVFSGSSYPGVQSYMIVLMVTCCIIPLAIIMLCYLQVWLAIRAVAKQQKESESTQKAEKEVTRMVVVMIFAYCVCWGPYTFFACFAAANPGYAFHPLMAALPAYFAKSATIYNPVIYVFMNRQFRNCILQLFGKKVDDGSELSSASKTEVSSVSSVSPA
| null | null |
cellular response to light stimulus [GO:0071482]; G protein-coupled receptor signaling pathway [GO:0007186]; phototransduction [GO:0007602]; positive regulation of cytokinesis [GO:0032467]; signal transduction [GO:0007165]; visual perception [GO:0007601]
|
photoreceptor disc membrane [GO:0097381]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]
|
G protein-coupled photoreceptor activity [GO:0008020]; photoreceptor activity [GO:0009881]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family, Opsin subfamily
|
PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.
|
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal.
|
Homo sapiens (Human)
|
P04001
|
OPSG_HUMAN
|
MAQQWSLQRLAGRHPQDSYEDSTQSSIFTYTNSNSTRGPFEGPNYHIAPRWVYHLTSVWMIFVVIASVFTNGLVLAATMKFKKLRHPLNWILVNLAVADLAETVIASTISVVNQVYGYFVLGHPMCVLEGYTVSLCGITGLWSLAIISWERWMVVCKPFGNVRFDAKLAIVGIAFSWIWAAVWTAPPIFGWSRYWPHGLKTSCGPDVFSGSSYPGVQSYMIVLMVTCCITPLSIIVLCYLQVWLAIRAVAKQQKESESTQKAEKEVTRMVVVMVLAFCFCWGPYAFFACFAAANPGYPFHPLMAALPAFFAKSATIYNPVIYVFMNRQFRNCILQLFGKKVDDGSELSSASKTEVSSVSSVSPA
| null | null |
cellular response to light stimulus [GO:0071482]; G protein-coupled receptor signaling pathway [GO:0007186]; phototransduction [GO:0007602]; positive regulation of cytokinesis [GO:0032467]; visual perception [GO:0007601]
|
photoreceptor disc membrane [GO:0097381]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]
|
G protein-coupled photoreceptor activity [GO:0008020]; identical protein binding [GO:0042802]; photoreceptor activity [GO:0009881]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family, Opsin subfamily
|
PTM: N-glycosylated (PubMed:30948514). O-glycosylated (PubMed:30948514). {ECO:0000269|PubMed:30948514}.; PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region. {ECO:0000305|PubMed:2937147}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20579627}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. {ECO:0000305|PubMed:12051694, ECO:0000305|PubMed:1302020, ECO:0000305|PubMed:2937147}.
|
Homo sapiens (Human)
|
P04002
|
ANPA_PSEAM
|
MALSLFTVGQLIFLFWTMRITEASPDPAAKAAPAAAAAPAAAAPDTASDAAAAAALTAANAKAAAELTAANAAAAAAATARG
| null | null | null |
extracellular space [GO:0005615]
|
ice binding [GO:0050825]; identical protein binding [GO:0042802]
| null | null |
Type-I AFP family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6952188}.
| null | null | null | null | null |
FUNCTION: Contributes to protect fish blood from freezing at subzero sea water temperatures. Lowers the blood freezing point. Binds to nascent ice crystals and prevents further growth. {ECO:0000269|PubMed:3769927, ECO:0000269|PubMed:6952188}.
|
Pseudopleuronectes americanus (Winter flounder) (Pleuronectes americanus)
|
P04003
|
C4BPA_HUMAN
|
MHPPKTPSGALHRKRKMAAWPFSRLWKVSDPILFQMTLIAALLPAVLGNCGPPPTLSFAAPMDITLTETRFKTGTTLKYTCLPGYVRSHSTQTLTCNSDGEWVYNTFCIYKRCRHPGELRNGQVEIKTDLSFGSQIEFSCSEGFFLIGSTTSRCEVQDRGVGWSHPLPQCEIVKCKPPPDIRNGRHSGEENFYAYGFSVTYSCDPRFSLLGHASISCTVENETIGVWRPSPPTCEKITCRKPDVSHGEMVSGFGPIYNYKDTIVFKCQKGFVLRGSSVIHCDADSKWNPSPPACEPNSCINLPDIPHASWETYPRPTKEDVYVVGTVLRYRCHPGYKPTTDEPTTVICQKNLRWTPYQGCEALCCPEPKLNNGEITQHRKSRPANHCVYFYGDEISFSCHETSRFSAICQGDGTWSPRTPSCGDICNFPPKIAHGHYKQSSSYSFFKEEIIYECDKGYILVGQAKLSCSYSHWSAPAPQCKALCRKPELVNGRLSVDKDQYVEPENVTIQCDSGYGVVGPQSITCSGNRTWYPEVPKCEWETPEGCEQVLTGKRLMQCLPNPEDVKMALEVYKLSLEIEQLELQRDSARQSTLDKEL
| null | null |
complement activation, classical pathway [GO:0006958]; innate immune response [GO:0045087]; negative regulation of complement activation, classical pathway [GO:0045959]; positive regulation of protein catabolic process [GO:0045732]; regulation of opsonization [GO:1903027]; response to symbiotic bacterium [GO:0009609]; T cell mediated immunity [GO:0002456]
|
blood microparticle [GO:0072562]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
RNA binding [GO:0003723]
|
PF18453;PF00084;
|
1.20.5.3730;2.10.70.10;
| null | null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Controls the classical pathway of complement activation. It binds as a cofactor to C3b/C4b inactivator (C3bINA), which then hydrolyzes the complement fragment C4b. It also accelerates the degradation of the C4bC2a complex (C3 convertase) by dissociating the complement fragment C2a. Alpha chain binds C4b. It interacts also with anticoagulant protein S and with serum amyloid P component.
|
Homo sapiens (Human)
|
P04004
|
VTNC_HUMAN
|
MAPLRPLLILALLAWVALADQESCKGRCTEGFNVDKKCQCDELCSYYQSCCTDYTAECKPQVTRGDVFTMPEDEYTVYDDGEEKNNATVHEQVGGPSLTSDLQAQSKGNPEQTPVLKPEEEAPAPEVGASKPEGIDSRPETLHPGRPQPPAEEELCSGKPFDAFTDLKNGSLFAFRGQYCYELDEKAVRPGYPKLIRDVWGIEGPIDAAFTRINCQGKTYLFKGSQYWRFEDGVLDPDYPRNISDGFDGIPDNVDAALALPAHSYSGRERVYFFKGKQYWEYQFQHQPSQEECEGSSLSAVFEHFAMMQRDSWEDIFELLFWGRTSAGTRQPQFISRDWHGVPGQVDAAMAGRIYISGMAPRPSLAKKQRFRHRNRKGYRSQRGHSRGRNQNSRRPSRATWLSLFSSEESNLGANNYDDYRMDWLVPATCEPIQSVFFFSGDKYYRVNLRTRRVDTVDPPYPRSIAQYWLGCPAPGHL
| null | null |
cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell migration [GO:0016477]; cell-matrix adhesion [GO:0007160]; endodermal cell differentiation [GO:0035987]; extracellular matrix organization [GO:0030198]; immune response [GO:0006955]; liver regeneration [GO:0097421]; negative regulation of blood coagulation [GO:0030195]; negative regulation of endopeptidase activity [GO:0010951]; negative regulation of fibrinolysis [GO:0051918]; oligodendrocyte differentiation [GO:0048709]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of protein binding [GO:0032092]; positive regulation of receptor-mediated endocytosis [GO:0048260]; positive regulation of smooth muscle cell migration [GO:0014911]; positive regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030949]; positive regulation of wound healing [GO:0090303]; protein polymerization [GO:0051258]; regulation of cell adhesion [GO:0030155]; smooth muscle cell-matrix adhesion [GO:0061302]
|
alphav-beta3 integrin-vitronectin complex [GO:0071062]; basement membrane [GO:0005604]; blood microparticle [GO:0072562]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; intracellular membrane-bounded organelle [GO:0043231]; peptidase inhibitor complex [GO:1904090]; protein complex involved in cell-matrix adhesion [GO:0098637]; rough endoplasmic reticulum lumen [GO:0048237]
|
collagen binding [GO:0005518]; extracellular matrix binding [GO:0050840]; extracellular matrix structural constituent [GO:0005201]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; integrin binding [GO:0005178]; polysaccharide binding [GO:0030247]; scavenger receptor activity [GO:0005044]
|
PF00045;PF01033;
|
4.10.410.20;2.110.10.10;
| null |
PTM: Sulfated on tyrosine residues. {ECO:0000269|PubMed:17558413, ECO:0000269|PubMed:2479556, ECO:0000269|PubMed:25136834}.; PTM: N- and O-glycosylated. {ECO:0000250}.; PTM: Phosphorylation on Thr-69 and Thr-76 favors cell adhesion and spreading. {ECO:0000269|PubMed:9733784}.; PTM: It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both.; PTM: Phosphorylation sites are present in the extracellular medium.
|
SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:2448300, ECO:0000269|PubMed:29567995}.; SUBCELLULAR LOCATION: Parasitophorous vacuole {ECO:0000269|PubMed:29567995}. Note=(Microbial infection) In P.falciparum-infected red blood cells, VTN internalization is detected at the early trophozoite stage (PubMed:29567995). Colocalizes with SERA5 at the schizont stage and with SERA5 P47 at the merozoite surface (PubMed:29567995). {ECO:0000269|PubMed:29567995}.
| null | null | null | null | null |
FUNCTION: Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.; FUNCTION: Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity.
|
Homo sapiens (Human)
|
P04011
|
VP2_POVLY
|
MGGVLSLLFNISEIAAELSLSTGFTVDAILTGEAFAAVSTEAAWLIEIEAVDLAGLSTLEALSLTGLTTEQFSLLSAIPTALNNAIGIGVFFQTVSGASAVVAAGVTTFGYSKEVPVVNMALVPWFPQVDYLFPGFTSFSYYLNAVLDWGESLFHAVGREVWRHLMRQATLQIGQATRAVAVRSTNELSHTLAQIAENARWALTSGPVHIYSSVQDYYRYLPARNPIQLRQEYRNRGEPPPSRADFEYQENREGQRARRELGYDEPRSGQYVEHYTAPGGAHQRVTQDWMLPLILGLYGDITPTWEVELNKLEKEEDGPSKKKARRSMQKNMPYSRSRPQAPSKRRSRGARSKNRA
| null | null |
symbiont entry into host cell [GO:0046718]; viral penetration into host nucleus [GO:0075732]
|
host cell [GO:0043657]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; viral capsid [GO:0019028]
|
DNA binding [GO:0003677]; structural molecule activity [GO:0005198]
|
PF00761;
| null |
Polyomaviruses capsid protein VP2 family
| null |
SUBCELLULAR LOCATION: [Isoform VP2]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform VP3]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: [Isoform VP2]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus in particular through a DNA-binding domain located in the C-terminal region. A N-terminal myristoylation suggests a scaffold function for virion assembly. The viral progenies exit the cells by lytic release (By similarity). {ECO:0000250}.; FUNCTION: [Isoform VP3]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus (By similarity). {ECO:0000250}.
|
B-lymphotropic polyomavirus (LPV)
|
P04014
|
VE1_HPV11
|
MADDSGTENEGSGCTGWFMVEAIVEHTTGTQISEDEEEEVEDSGYDMVDFIDDRHITQNSVEAQALFNRQEADAHYATVQDLKRKYLGSPYVSPISNVANAVESEISPRLDAIKLTTQPKKVKRRLFETRELTDSGYGYSEVEAATQVEKHGDPENGGDGQERDTGRDIEGEGVEHREAEAVDDSTREHADTSGILELLKCKDIRSTLHGKFKDCFGLSFVDLIRPFKSDRTTCADWVVAGFGIHHSIADAFQKLIEPLSLYAHIQWLTNAWGMVLLVLIRFKVNKSRCTVARTLGTLLNIPENHMLIEPPKIQSGVRALYWFRTGISNASTVIGEAPEWITRQTVIEHSLADSQFKLTEMVQWAYDNDICEESEIAFEYAQRGDFDSNARAFLNSNMQAKYVKDCAIMCRHYKHAEMKKMSIKQWIKYRGTKVDSVGNWKPIVQFLRHQNIEFIPFLSKLKLWLHGTPKKNCIAIVGPPDTGKSCFCMSLIKFLGGTVISYVNSCSHFWLQPLTDAKVALLDDATQPCWTYMDTYMRNLLDGNPMSIDRKHRALTLIKCPPLLVTSNIDISKEEKYKYLHSRVTTFTFPNPFPFDRNGNAVYELSDANWKCFFERLSSSLDIEDSEDEEDGSNSQAFRCVPGSVVRTL
|
3.6.4.12
| null |
bidirectional double-stranded viral DNA replication [GO:0039686]; DNA duplex unwinding [GO:0032508]; DNA replication [GO:0006260]; protein hexamerization [GO:0034214]; viral DNA genome replication [GO:0039693]
|
host cell nucleus [GO:0042025]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; TPR domain binding [GO:0030911]
|
PF00519;PF20450;PF00524;
|
3.40.1310.10;3.40.50.300;1.10.10.510;
|
Papillomaviridae E1 protein family
|
PTM: Phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04000}.; PTM: Sumoylated. {ECO:0000255|HAMAP-Rule:MF_04000}.
|
SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04000, ECO:0000269|PubMed:15564503}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000255|HAMAP-Rule:MF_04000};
| null | null | null | null |
FUNCTION: ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins. During the initial step, a dimer of E1 interacts with a dimer of protein E2 leading to a complex that binds the viral origin of replication with high specificity. Then, a second dimer of E1 displaces the E2 dimer in an ATP-dependent manner to form the E1 tetramer. Following this, two E1 monomers are added to each half of the site, which results in the formation of two E1 trimers on the viral ori. Subsequently, two hexamers will be created. The double hexamer acts as a bi-directional helicase machinery and unwinds the viral DNA and then recruits the host DNA polymerase to start replication. {ECO:0000255|HAMAP-Rule:MF_04000}.
|
Human papillomavirus 11
|
P04021
|
PG057_VACCW
|
MWPFASVPAGAKCRLVETLPENMDFRSDHLTTFECFNEIITLAKKYIYIASFCCNPLSTTRGALIFDKLKEASEKGIKIIVLLDERGKRNLGELQSHCPDINFITVNIDKKNNVGLLLGCFWVSDDERCYVGNASFTGGSIHTIKTLGVYSDYPPLATDLRRRFDTFKAFNSAKNSWLNLCSAACCLPVSTAYHIKNPIGGVFFTDSPEHLLGYSRDLDTDVVIDKLKSAKTSIDIEHLAIVPTTRVDGNSYYWPDIYNSIIEAAINRGVKIRLLVGNWDKNDVYSMATARSLDALCVQNDLSVKVFTIQNNTKLLIVDDEYVHITSANFDGTHYQNHGFVSFNSIDKQLVSEAKKIFERDWVSSHSKSLKI
|
3.1.1.-; 3.1.4.4
| null |
viral budding from Golgi membrane [GO:0046760]; viral budding via host ESCRT complex [GO:0039702]
|
host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi apparatus [GO:0044177]; membrane [GO:0016020]; viral envelope [GO:0019031]; viral membrane [GO:0036338]; virion membrane [GO:0055036]
|
phospholipase D activity [GO:0004630]
|
PF13918;
|
3.30.870.10;
|
Orthopoxvirus OPG057 family
|
PTM: Palmitoylated. Attachment of the palmitate moiety is essential for correct intracellular targeting and protein function. {ECO:0000269|PubMed:11017799, ECO:0000269|PubMed:8999886}.
|
SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:12706074}; Lipid-anchor {ECO:0000269|PubMed:12706074}. Host Golgi apparatus, host trans-Golgi network {ECO:0000269|PubMed:27466413, ECO:0000269|PubMed:29540596}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:12706074}; Lipid-anchor {ECO:0000269|PubMed:12706074}; Cytoplasmic side {ECO:0000269|PubMed:12706074}. Note=Component of the inner side of the enveloped virion (EV) membrane. F13 is associated post-translationally with membranes.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4; Evidence={ECO:0000269|PubMed:9405398}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14446; Evidence={ECO:0000269|PubMed:9405398};
| null | null | null | null |
FUNCTION: Major envelope protein that plays a role in the biogenesis of the viral double membrane and in egress of virus from the host cell (PubMed:17475658, PubMed:27466413, PubMed:8999886). Produces the wrapped form of virus that is required for cell-to-cell spread (PubMed:27466413, PubMed:29540596). Acts as a lipase with broad specificity including phospholipase C, phospholipase A, and triacylglycerol lipase activities (PubMed:9405398). {ECO:0000269|PubMed:17475658, ECO:0000269|PubMed:27466413, ECO:0000269|PubMed:29540596, ECO:0000269|PubMed:8999886, ECO:0000269|PubMed:9405398}.
|
Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
|
P04022
|
GAG_SRV1
|
MGQELSQHERYVEQLKQALKTRGVKVKYADLLKFFDFVKDTCPWFPQEGTIDIKRWRRVGDCFQDYYNTFGPEKVPVTAFSYWNLIKELIDKKEVNPQVMAAVAQTEEILKTSSHTELTTKPSQNPDLDLISLDSDDEGAKGSSLKDKNLSCTKKPKRFPVLLTAQTSADPEDPNPSEVDWDGLEDEAAKYHNPDWPPFLTRPPPYNKATPSAPTVMAVVNPKEELKEKIAQLEEQIKLEELHQALISKLQKLKTGNETVTSPETAGGFSRTPHWPGQHIPKGKCCASREKEEQTPKDIFPVTETVDGQGQAWRHHNGFDFTVIKELKTAASQYGATAPYTLAIVESVADNWLTPTDWNTLVRAVLSGGDHLLWKSEFFENCRETAKRNQQAGNGWDFDMLTGSGNYSSTDAQMQYDPGLFAQIQAAATKAWRKLPVKGDPGASLTGVKQGPDEPFADFVHRLITTAGRIFGSAEAGVDYVKQLAYENANPACQAAIRPYRKKTDLTGYIRLCSDIGPSYQQGLAMAAAFSGQTVKDFLNNKNKEKGGCCFKCGRKGHFAKNCHEHIHNNSETKAPGLCPRCKRGKHWANECKSKTDSQGNPLPPHQGNGLRGQPQAPKQAYGAVSFVPANKNNPFQSLPEPPQEVQDWTSVPPPTQY
| null | null |
viral budding via host ESCRT complex [GO:0039702]
|
viral nucleocapsid [GO:0019013]
|
nucleic acid binding [GO:0003676]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270]
|
PF02337;PF00607;PF19317;PF14787;
|
1.10.1200.30;1.10.375.10;1.10.150.490;4.10.60.10;
| null |
PTM: [Gag polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and is required for the assembly of viral particles. {ECO:0000250|UniProtKB:P10258}.; PTM: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. {ECO:0000250|UniProtKB:P07567}.
|
SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p14]: Virion {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.; FUNCTION: [Nucleocapsid protein p14]: Nucleocapsid protein. {ECO:0000305}.; FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000305}.
|
Simian retrovirus SRV-1
|
P04024
|
PRO_SRV1
|
MGQELSQHERYVEQLKQALKTRGVKVKYADLLKFFDFVKDTCPWFPQEGTIDIKRWRRVGDCFQDYYNTFGPEKVPVTAFSYWNLIKELIDKKEVNPQVMAAVAQTEEILKTSSHTELTTKPSQNPDLDLISLDSDDEGAKGSSLKDKNLSCTKKPKRFPVLLTAQTSADPEDPNPSEVDWDGLEDEAAKYHNPDWPPFLTRPPPYNKATPSAPTVMAVVNPKEELKEKIAQLEEQIKLEELHQALISKLQKLKTGNETVTSPETAGGFSRTPHWPGQHIPKGKCCASREKEEQTPKDIFPVTETVDGQGQAWRHHNGFDFTVIKELKTAASQYGATAPYTLAIVESVADNWLTPTDWNTLVRAVLSGGDHLLWKSEFFENCRETAKRNQQAGNGWDFDMLTGSGNYSSTDAQMQYDPGLFAQIQAAATKAWRKLPVKGDPGASLTGVKQGPDEPFADFVHRLITTAGRIFGSAEAGVDYVKQLAYENANPACQAAIRPYRKKTDLTGYIRLCSDIGPSYQQGLAMAAAFSGQTVKDFLNNKNKEKGGCCFKCGRKGHFAKNCHEHIHNNSETKAPGLCPRCKRGKHWANECKSKTDSQGNPLPPHQGNRTEGPAPGPETSLWGGQLCSSQQKQPISKLTRATPGSAGLDLSSTSHTVLTPEMGPQALSTGIYGPLPPNTFGLILGRSSITIKGLQVYPGVIDNDYTGEIKIMAKAVNNIVTVPQGNRIAQLILLPLIETDNKVQQPYRGQGSFGSSDIYWVQPITCQKPSLTLWLDDKMFTGLIDTGADVTIIKLEDWPPNWPITDTLTNLRGIGQSNNPKQSSKYLTWRDKENNSGLIKPFVIPNLPVNLWGRDLLSQMKIMMCSPSDIVTAQMLAQGYSPGKGLGKNENGILHPIPNQGQFDKKGFGNF
|
3.4.23.-; 3.6.1.23
| null |
nucleotide metabolic process [GO:0009117]; proteolysis [GO:0006508]; viral process [GO:0016032]
|
viral nucleocapsid [GO:0019013]
|
aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; dUTP diphosphatase activity [GO:0004170]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270]
|
PF00692;PF01585;PF02337;PF00607;PF19317;PF00077;PF14787;
|
1.10.1200.30;2.70.40.10;2.40.70.10;1.10.375.10;1.10.150.490;4.10.60.10;
| null |
PTM: [Protease 17 kDa]: Released by autocatalytic processing. The protease can undergo further autoprocessing to yield 2 shorter but enzymatically active forms of 12 kDa and 13 kDa without the GDP domain. {ECO:0000250|UniProtKB:P07570}.; PTM: [Gag-Pro polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and is required for the assembly of viral particles. {ECO:0000250|UniProtKB:P10258}.; PTM: [Gag-Pro polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. {ECO:0000250|UniProtKB:P07570}.
|
SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein-dUTPase]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Protease 13 kDa]: Virion {ECO:0000250|UniProtKB:P07570}.; SUBCELLULAR LOCATION: [Protease 17 kDa]: Virion {ECO:0000250|UniProtKB:P07570}.
|
CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={ECO:0000250|UniProtKB:P07570};
| null | null | null | null |
FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.; FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein. {ECO:0000305}.; FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000305}.; FUNCTION: [Protease 17 kDa]: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. {ECO:0000250|UniProtKB:P07570, ECO:0000255|PROSITE-ProRule:PRU00275}.; FUNCTION: [Protease 13 kDa]: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. {ECO:0000250|UniProtKB:P07570, ECO:0000255|PROSITE-ProRule:PRU00275}.; FUNCTION: [G-patch peptide]: Enhances the activity of the reverse transcriptase. May be part of the mature RT. {ECO:0000250|UniProtKB:P07570}.
|
Simian retrovirus SRV-1
|
P04025
|
POL_SRV1
|
MGQELSQHERYVEQLKQALKTRGVKVKYADLLKFFDFVKDTCPWFPQEGTIDIKRWRRVGDCFQDYYNTFGPEKVPVTAFSYWNLIKELIDKKEVNPQVMAAVAQTEEILKTSSHTELTTKPSQNPDLDLISLDSDDEGAKGSSLKDKNLSCTKKPKRFPVLLTAQTSADPEDPNPSEVDWDGLEDEAAKYHNPDWPPFLTRPPPYNKATPSAPTVMAVVNPKEELKEKIAQLEEQIKLEELHQALISKLQKLKTGNETVTSPETAGGFSRTPHWPGQHIPKGKCCASREKEEQTPKDIFPVTETVDGQGQAWRHHNGFDFTVIKELKTAASQYGATAPYTLAIVESVADNWLTPTDWNTLVRAVLSGGDHLLWKSEFFENCRETAKRNQQAGNGWDFDMLTGSGNYSSTDAQMQYDPGLFAQIQAAATKAWRKLPVKGDPGASLTGVKQGPDEPFADFVHRLITTAGRIFGSAEAGVDYVKQLAYENANPACQAAIRPYRKKTDLTGYIRLCSDIGPSYQQGLAMAAAFSGQTVKDFLNNKNKEKGGCCFKCGRKGHFAKNCHEHIHNNSETKAPGLCPRCKRGKHWANECKSKTDSQGNPLPPHQGNRTEGPAPGPETSLWGGQLCSSQQKQPISKLTRATPGSAGLDLSSTSHTVLTPEMGPQALSTGIYGPLPPNTFGLILGRSSITIKGLQVYPGVIDNDYTGEIKIMAKAVNNIVTVPQGNRIAQLILLPLIETDNKVQQPYRGQGSFGSSDIYWVQPITCQKPSLTLWLDDKMFTGLIDTGADVTIIKLEDWPPNWPITDTLTNLRGIGQSNNPKQSSKYLTWRDKENNSGLIKPFVIPNLPVNLWGRDLLSQMKIMMCSPSDIVTAQMLAQGYSPGKGLGKNENGILHPIPNQGQFDKKGFGNFLTAAIDMLAPQQCAEPITWKSDEPVWVDQWPLTSEKLAAAQQLVQEQLEAGHITESNSPWNTPIFVIKKKSGKWRLLQDLRAVNATMVLMGALQPGLPSPVAIPQGYLKIIIDLKDCFFSIPLHPSDQKRFAFSLPSTNFKEPMQRFQWKVLPQRMANSPTLCQKYVATAIHKVRHAWKQMYIIHYMDDILIAGKDGQQVLQCFDQLKQELTIAGLHIAPEKIQLQDPYTYLGFELNGPKITNQKAVIRKDKLQTLNDFQKLLGDINWLRPYLKLTTADLKPLFDTLKGDSNPNSHRSLSKEALALLDKVETAIAEQFVTHINYSLPLMFLIFNTALTPTGLFWQNNPIMWVHLPASPKKVLLPYYDAIADLIILGRDHSKKYFGIEPSVIIQPYSKSQIDWLMQNTEMWPIACASYVGILDNHYPPNKLIQFCKLHAFIFPQIISKTPLNNALLVFTDGSSTGMAAYTLADTTIKFQTNLNSAQLVELQALIAVLSAFPNQPLNIYTDSAYLAHSIPLLETVAQIKHISETAKLFLQCQQLIYNRSIPFYIGHVRAHSGLPGPIAHGNQKADLATKTVASNINTNLESAQNAHTLHHLNAQTLKLMFNIPREQARQIVRQCPICATYLPVPHLGVNPRGLLPNMIWQMDVTHYSEFGNLKYIHVSIDTFSGFLLATLQTGETTKHVITHLLHCFSIIGLPKQIKTDNGPGYTSKNFQEFCSTLQIKHVTGIPYNPQGQGIVERAHLSLKTTIEKIKKGEWYPTKGTPRNILNHALFILNFLNLDDQNHSAADRFWHSNPRKQFAMVKWKDPLDNTWPWPDPVIIWGRGSVCVYSQTHDAARWLPERLVKQIPNNNQSRE
|
2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.-; 3.6.1.23
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; Note=The RT polymerase active site binds 2 magnesium ions. {ECO:0000255|PROSITE-ProRule:PRU00405};
|
DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; viral genome integration into host DNA [GO:0044826]
|
viral nucleocapsid [GO:0019013]
|
aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; dUTP diphosphatase activity [GO:0004170]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270]
|
PF00692;PF01585;PF02337;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06817;PF14787;
|
1.10.10.200;1.10.1200.30;2.70.40.10;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;2.30.30.10;1.10.150.490;3.30.420.10;4.10.60.10;
|
Retroviral Pol polyprotein family
|
PTM: [Protease 17 kDa]: Released by autocatalytic processing. The protease can undergo further autoprocessing to yield 2 shorter but enzymatically active forms of 12 kDa and 13 kDa. {ECO:0000250|UniProtKB:P07572}.; PTM: [Gag-Pro-Pol polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and is required for the assembly of viral particles. {ECO:0000250|UniProtKB:P10258}.; PTM: [Gag-Pro-Pol polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. {ECO:0000250|UniProtKB:P07572}.
|
SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein-dUTPase]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Protease 13 kDa]: Virion {ECO:0000250|UniProtKB:P07572}.; SUBCELLULAR LOCATION: [Protease 17 kDa]: Virion {ECO:0000250|UniProtKB:P07572}.
|
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU00408}; CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={ECO:0000250|UniProtKB:P07570};
| null | null | null | null |
FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000250|UniProtKB:P07572}.; FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein. {ECO:0000250|UniProtKB:P07572}.; FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000250|UniProtKB:P07572}.; FUNCTION: [Protease 17 kDa]: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. {ECO:0000255|PROSITE-ProRule:PRU00275}.; FUNCTION: [Protease 13 kDa]: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. {ECO:0000255|PROSITE-ProRule:PRU00275}.; FUNCTION: [G-patch peptide]: Enhances the activity of the reverse transcriptase. May be part of the mature RT. {ECO:0000250|UniProtKB:P07572}.; FUNCTION: [Reverse transcriptase/ribonuclease H]: RT is a multifunctional enzyme that converts the viral dimeric RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA binds to the primer-binding site (PBS) situated at the 5' end of the viral RNA. RT uses the 3' end of the tRNA primer to perfom a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perfom the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for a polypurine tract (PPT) situated at the 5' end of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPT that has not been removed by RNase H as primers. PPT and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends. {ECO:0000255|PROSITE-ProRule:PRU00405}.; FUNCTION: [Integrase]: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. {ECO:0000305|PubMed:28458055}.
|
Simian retrovirus SRV-1
|
P04035
|
HMDH_HUMAN
|
MLSRLFRMHGLFVASHPWEVIVGTVTLTICMMSMNMFTGNNKICGWNYECPKFEEDVLSSDIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTGLNEALPFFLLLIDLSRASTLAKFALSSNSQDEVRENIARGMAILGPTFTLDALVECLVIGVGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFARVLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADPSPQNSTADTSKVSLGLDENVSKRIEPSVSLWQFYLSKMISMDIEQVITLSLALLLAVKYIFFEQTETESTLSLKNPITSPVVTQKKVPDNCCRREPMLVRNNQKCDSVEEETGINRERKVEVIKPLVAETDTPNRATFVVGNSSLLDTSSVLVTQEPEIELPREPRPNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYKLETLMETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGVAGPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRACDSAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMISKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREVLKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAAGHLVKSHMIHNRSKINLQDLQGACTKKTA
|
1.1.1.34
| null |
cholesterol biosynthetic process [GO:0006695]; coenzyme A metabolic process [GO:0015936]; ergosterol biosynthetic process [GO:0006696]; isoprenoid biosynthetic process [GO:0008299]; long-term synaptic potentiation [GO:0060291]; negative regulation of amyloid-beta clearance [GO:1900222]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of protein secretion [GO:0050709]; regulation of ERK1 and ERK2 cascade [GO:0070372]; sterol biosynthetic process [GO:0016126]; visual learning [GO:0008542]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; peroxisomal membrane [GO:0005778]
|
coenzyme A binding [GO:0120225]; GTPase regulator activity [GO:0030695]; hydroxymethylglutaryl-CoA reductase (NADPH) activity [GO:0004420]; NADPH binding [GO:0070402]
|
PF00368;PF12349;
|
1.10.3270.10;3.30.70.420;
|
HMG-CoA reductase family
|
PTM: N-glycosylated. Deglycosylated by NGLY1 on release from the endoplasmic reticulum (ER) in a sterol-mediated manner. {ECO:0000269|PubMed:19458199}.; PTM: Undergoes sterol-mediated ubiquitination and ER-associated degradation (ERAD) (PubMed:12535518, PubMed:19458199, PubMed:21778231). Accumulation of sterols in the endoplasmic reticulum (ER) membrane, triggers binding of the reductase to the ER membrane protein INSIG1 or INSIG2 (PubMed:12535518, PubMed:19458199, PubMed:21778231, PubMed:22143767). The INSIG1 binding leads to the recruitment of the ubiquitin ligase, AMFR/gp78, RNF139 or RNF145, initiating ubiquitination of the reductase (PubMed:12535518, PubMed:19458199, PubMed:21778231). The ubiquitinated reductase is then extracted from the ER membrane and delivered to cytosolic 26S proteosomes by a mechanism probably mediated by the ATPase Valosin-containing protein VCP/p97 (PubMed:12535518, PubMed:19458199, PubMed:21778231). The INSIG2-binding leads to the recruitment of the ubiquitin ligase RNF139, initiating ubiquitination of the reductase (PubMed:22143767). Lys-248 is the main site of ubiquitination (PubMed:19458199). Ubiquitination is enhanced by the presence of a geranylgeranylated protein (PubMed:21778231). {ECO:0000269|PubMed:12535518, ECO:0000269|PubMed:19458199, ECO:0000269|PubMed:21778231, ECO:0000269|PubMed:22143767}.; PTM: Phosphorylated. Phosphorylation at Ser-872 reduces the catalytic activity. {ECO:0000250|UniProtKB:P00347}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17180682, ECO:0000305|PubMed:2991281}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00347}. Peroxisome membrane {ECO:0000269|PubMed:17180682}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00347}.
|
CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34; Evidence={ECO:0000269|PubMed:21357570, ECO:0000269|PubMed:2991281, ECO:0000269|PubMed:36745799, ECO:0000269|PubMed:6995544}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15991; Evidence={ECO:0000269|PubMed:36745799};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13.73 uM for (3S)-hydroxy-3-methylglutaryl-CoA {ECO:0000269|PubMed:36745799};
|
PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
| null | null |
FUNCTION: Catalyzes the conversion of (3S)-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to mevalonic acid, the rate-limiting step in the synthesis of cholesterol and other isoprenoids, thus plays a critical role in cellular cholesterol homeostasis (PubMed:21357570, PubMed:2991281, PubMed:36745799, PubMed:6995544). HMGCR is the main target of statins, a class of cholesterol-lowering drugs (PubMed:11349148, PubMed:18540668, PubMed:36745799). {ECO:0000269|PubMed:11349148, ECO:0000269|PubMed:18540668, ECO:0000269|PubMed:21357570, ECO:0000269|PubMed:2991281, ECO:0000269|PubMed:36745799, ECO:0000269|PubMed:6995544}.
|
Homo sapiens (Human)
|
P04036
|
DAPB_ECOLI
|
MHDANIRVAIAGAGGRMGRQLIQAALALEGVQLGAALEREGSSLLGSDAGELAGAGKTGVTVQSSLDAVKDDFDVFIDFTRPEGTLNHLAFCRQHGKGMVIGTTGFDEAGKQAIRDAAADIAIVFAANFSVGVNVMLKLLEKAAKVMGDYTDIEIIEAHHRHKVDAPSGTALAMGEAIAHALDKDLKDCAVYSREGHTGERVPGTIGFATVRAGDIVGEHTAMFADIGERLEITHKASSRMTFANGAVRSALWLSGKESGLFDMRDVLDLNNL
|
1.17.1.8
| null |
amino acid biosynthetic process [GO:0008652]; diaminopimelate biosynthetic process [GO:0019877]; lysine biosynthetic process via diaminopimelate [GO:0009089]
|
cytosol [GO:0005829]
|
4-hydroxy-tetrahydrodipicolinate reductase [GO:0008839]; identical protein binding [GO:0042802]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor [GO:0016726]
|
PF05173;PF01113;
|
3.40.50.720;
|
DapB family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102, ECO:0000269|PubMed:20503968}; CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH; Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00102, ECO:0000269|PubMed:20503968};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.6 uM for NADH {ECO:0000269|PubMed:7893644, ECO:0000269|PubMed:9398235}; KM=8 uM for NADPH {ECO:0000269|PubMed:7893644, ECO:0000269|PubMed:9398235};
|
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. {ECO:0000255|HAMAP-Rule:MF_00102}.
| null | null |
FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. Can use both NADH and NADPH as a reductant, with NADH being twice as effective as NADPH. {ECO:0000255|HAMAP-Rule:MF_00102, ECO:0000269|PubMed:20503968, ECO:0000269|PubMed:7893644}.
|
Escherichia coli (strain K12)
|
P04037
|
COX4_YEAST
|
MLSLRQSIRFFKPATRTLCSSRYLLQQKPVVKTAQNLAEVNGPETLIGPGAKEGTVPTDLDQETGLARLELLGKLEGIDVFDTKPLDSSRKGTMKDPIIIESYDDYRYVGCTGSPAGSHTIMWLKPTVNEVARCWECGSVYKLNPVGVPNDDHHH
| null | null |
mitochondrial cytochrome c oxidase assembly [GO:0033617]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; proton transmembrane transport [GO:1902600]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739]
|
oxidoreductase activity [GO:0016491]; zinc ion binding [GO:0008270]
|
PF01215;
|
2.60.11.10;
|
Cytochrome c oxidase subunit 5B family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:30598554}; Peripheral membrane protein {ECO:0000269|PubMed:30598554}; Matrix side {ECO:0000269|PubMed:30598554}.
| null | null |
PATHWAY: Energy metabolism; oxidative phosphorylation.
| null | null |
FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. {ECO:0000305|PubMed:30598554}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P04039
|
COX8_YEAST
|
MLCQQMIRTTAKRSSNIMTRPIIMKRSVHFKDGVYENIPFKVKGRKTPYALSHFGFFAIGFAVPFVACYVQLKKSGAF
| null | null |
mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; proton transmembrane transport [GO:1902600]
|
mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739]
|
oxidoreductase activity [GO:0016491]
|
PF02935;
|
4.10.49.10;
|
Cytochrome c oxidase VIIc family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:30598554}; Single-pass membrane protein {ECO:0000269|PubMed:30598554}.
| null | null |
PATHWAY: Energy metabolism; oxidative phosphorylation.
| null | null |
FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. {ECO:0000305|PubMed:30598554}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P04040
|
CATA_HUMAN
|
MADSRDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPDTHRHRLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNYYPNSFGAPEQQPSALEHSIQYSGEVRRFNTANDDNVTQVRAFYVNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVKNFTEVHPDYGSHIQALLDKYNAEKPKNAIHTFVQSGSHLAAREKANL
|
1.11.1.6
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:10656833, ECO:0000269|PubMed:10666617}; COFACTOR: Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:10656833};
|
aerobic respiration [GO:0009060]; cellular detoxification of hydrogen peroxide [GO:0061692]; cellular response to growth factor stimulus [GO:0071363]; cholesterol metabolic process [GO:0008203]; hemoglobin metabolic process [GO:0020027]; hydrogen peroxide catabolic process [GO:0042744]; negative regulation of apoptotic process [GO:0043066]; osteoblast differentiation [GO:0001649]; positive regulation of cell division [GO:0051781]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; response to activity [GO:0014823]; response to cadmium ion [GO:0046686]; response to estradiol [GO:0032355]; response to ethanol [GO:0045471]; response to fatty acid [GO:0070542]; response to hydrogen peroxide [GO:0042542]; response to hyperoxia [GO:0055093]; response to hypoxia [GO:0001666]; response to inactivity [GO:0014854]; response to insulin [GO:0032868]; response to L-ascorbic acid [GO:0033591]; response to lead ion [GO:0010288]; response to light intensity [GO:0009642]; response to ozone [GO:0010193]; response to phenylpropanoid [GO:0080184]; response to reactive oxygen species [GO:0000302]; response to vitamin A [GO:0033189]; response to vitamin E [GO:0033197]; response to xenobiotic stimulus [GO:0009410]; triglyceride metabolic process [GO:0006641]; ureteric bud development [GO:0001657]; UV protection [GO:0009650]
|
catalase complex [GO:0062151]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; focal adhesion [GO:0005925]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; protein-containing complex [GO:0032991]; secretory granule lumen [GO:0034774]
|
aminoacylase activity [GO:0004046]; antioxidant activity [GO:0016209]; catalase activity [GO:0004096]; enzyme binding [GO:0019899]; heme binding [GO:0020037]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; NADP binding [GO:0050661]; oxidoreductase activity, acting on peroxide as acceptor [GO:0016684]; protein homodimerization activity [GO:0042803]
|
PF00199;PF06628;
|
2.40.180.10;
|
Catalase family
| null |
SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:21976670, ECO:0000269|PubMed:8769411}.
|
CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10013, ECO:0000269|PubMed:7882369};
| null | null | null | null |
FUNCTION: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide (PubMed:7882369). Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells (PubMed:7882369). {ECO:0000269|PubMed:7882369}.
|
Homo sapiens (Human)
|
P04041
|
GPX1_RAT
|
MSAARLSAVAQSTVYAFSARPLAGGEPVSLGSLRGKVLLIENVASLUGTTTRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEILNSLKYVRPGGGFEPNFTLFEKCEVNGEKAHPLFTFLRNALPAPSDDPTALMTDPKYIIWSPVCRNDISWNFEKFLVGPDGVPVRRYSRRFRTIDIEPDIEALLSKQPSNP
|
1.11.1.12; 1.11.1.9
| null |
angiogenesis involved in wound healing [GO:0060055]; apoptotic process [GO:0006915]; arachidonic acid metabolic process [GO:0019369]; biological process involved in interaction with symbiont [GO:0051702]; blood vessel endothelial cell migration [GO:0043534]; cell redox homeostasis [GO:0045454]; cellular response to glucose stimulus [GO:0071333]; endothelial cell development [GO:0001885]; epigenetic regulation of gene expression [GO:0040029]; fat cell differentiation [GO:0045444]; fibroblast proliferation [GO:0048144]; glutathione metabolic process [GO:0006749]; heart contraction [GO:0060047]; hydrogen peroxide catabolic process [GO:0042744]; intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0008631]; lipid metabolic process [GO:0006629]; lipoxygenase pathway [GO:0019372]; myoblast differentiation [GO:0045445]; myoblast proliferation [GO:0051450]; myotube differentiation [GO:0014902]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; negative regulation of inflammatory response to antigenic stimulus [GO:0002862]; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902176]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; neuron apoptotic process [GO:0051402]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; regulation of mammary gland epithelial cell proliferation [GO:0033599]; regulation of proteasomal protein catabolic process [GO:0061136]; response to estradiol [GO:0032355]; response to folic acid [GO:0051593]; response to gamma radiation [GO:0010332]; response to glucose [GO:0009749]; response to hormone [GO:0009725]; response to hydrogen peroxide [GO:0042542]; response to hydroperoxide [GO:0033194]; response to nicotine [GO:0035094]; response to organic cyclic compound [GO:0014070]; response to oxidative stress [GO:0006979]; response to reactive oxygen species [GO:0000302]; response to selenium ion [GO:0010269]; response to symbiotic bacterium [GO:0009609]; response to toxic substance [GO:0009636]; response to vitamin E [GO:0033197]; response to wounding [GO:0009611]; response to xenobiotic stimulus [GO:0009410]; sensory perception of sound [GO:0007605]; skeletal muscle fiber development [GO:0048741]; skeletal muscle tissue regeneration [GO:0043403]; temperature homeostasis [GO:0001659]; triglyceride metabolic process [GO:0006641]; UV protection [GO:0009650]; vasodilation [GO:0042311]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; Lewy body [GO:0097413]; mitochondrion [GO:0005739]
|
glutathione peroxidase activity [GO:0004602]; peroxidase activity [GO:0004601]; phospholipid-hydroperoxide glutathione peroxidase activity [GO:0047066]; SH3 domain binding [GO:0017124]
|
PF00255;
|
3.40.30.10;
|
Glutathione peroxidase family
|
PTM: During periods of oxidative stress, Sec-47 may react with a superoxide radical, irreversibly lose hydroselenide and be converted to dehydroalanine. {ECO:0000250|UniProtKB:P11352}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11352}. Mitochondrion {ECO:0000250|UniProtKB:P11352}.
|
CATALYTIC ACTIVITY: Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O; Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9; Evidence={ECO:0000250|UniProtKB:P11352}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16834; Evidence={ECO:0000250|UniProtKB:P11352}; CATALYTIC ACTIVITY: Reaction=a hydroperoxy polyunsaturated fatty acid + 2 glutathione = a hydroxy polyunsaturated fatty acid + glutathione disulfide + H2O; Xref=Rhea:RHEA:19057, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:131871, ChEBI:CHEBI:134019; EC=1.11.1.12; Evidence={ECO:0000250|UniProtKB:P07203}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19058; Evidence={ECO:0000250|UniProtKB:P07203}; CATALYTIC ACTIVITY: Reaction=2 glutathione + tert-butyl hydroperoxide = glutathione disulfide + H2O + tert-butanol; Xref=Rhea:RHEA:69412, ChEBI:CHEBI:15377, ChEBI:CHEBI:45895, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:64090; Evidence={ECO:0000250|UniProtKB:P07203}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69413; Evidence={ECO:0000250|UniProtKB:P07203}; CATALYTIC ACTIVITY: Reaction=cumene hydroperoxide + 2 glutathione = 2-phenylpropan-2-ol + glutathione disulfide + H2O; Xref=Rhea:RHEA:69651, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:78673, ChEBI:CHEBI:131607; Evidence={ECO:0000250|UniProtKB:P07203}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69652; Evidence={ECO:0000250|UniProtKB:P07203}; CATALYTIC ACTIVITY: Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate + 2 glutathione = (13S)-hydroxy-(9Z,11E)-octadecadienoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:48888, ChEBI:CHEBI:15377, ChEBI:CHEBI:57466, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90850; Evidence={ECO:0000250|UniProtKB:P07203}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48889; Evidence={ECO:0000250|UniProtKB:P07203}; CATALYTIC ACTIVITY: Reaction=(9S)-hydroperoxy-(10E,12Z)-octadecadienoate + 2 glutathione = (9S)-hydroxy-(10E,12Z)-octadecadienoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76687, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:60955, ChEBI:CHEBI:77852; Evidence={ECO:0000250|UniProtKB:P07203}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76688; Evidence={ECO:0000250|UniProtKB:P07203}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + 2 glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:48620, ChEBI:CHEBI:15377, ChEBI:CHEBI:57450, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90632; Evidence={ECO:0000250|UniProtKB:P07203}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48621; Evidence={ECO:0000250|UniProtKB:P07203}; CATALYTIC ACTIVITY: Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + 2 glutathione = (12S)-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:50708, ChEBI:CHEBI:15377, ChEBI:CHEBI:57444, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90680; Evidence={ECO:0000250|UniProtKB:P11352}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50709; Evidence={ECO:0000250|UniProtKB:P11352}; CATALYTIC ACTIVITY: Reaction=(12R)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + 2 glutathione = (12R)-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76691, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:75230, ChEBI:CHEBI:83343; Evidence={ECO:0000250|UniProtKB:P07203}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76692; Evidence={ECO:0000250|UniProtKB:P07203}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + 2 glutathione = (15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76695, ChEBI:CHEBI:15377, ChEBI:CHEBI:57409, ChEBI:CHEBI:57446, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; Evidence={ECO:0000250|UniProtKB:P07203}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76696; Evidence={ECO:0000250|UniProtKB:P07203}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z,17Z)-eicosapentaenoate + 2 glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z,17Z)-eicosapentaenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76699, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:195399, ChEBI:CHEBI:195400; Evidence={ECO:0000250|UniProtKB:P07203}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76700; Evidence={ECO:0000250|UniProtKB:P07203}; CATALYTIC ACTIVITY: Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z,17Z)-eicosapentaenoate + 2 glutathione = (12S)-hydroxy-(5Z,8Z,10E,14Z,17Z)-eicosapentaenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76703, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90772, ChEBI:CHEBI:195401; Evidence={ECO:0000250|UniProtKB:P07203}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76704; Evidence={ECO:0000250|UniProtKB:P07203}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + 2 glutathione = (15S)-hydroxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76707, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:132087, ChEBI:CHEBI:194369; Evidence={ECO:0000250|UniProtKB:P07203}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76708; Evidence={ECO:0000250|UniProtKB:P07203}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(11Z,13E)-eicosadienoate + 2 glutathione = (15S)-hydroxy-(11Z,13E)-eicosadienoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76711, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:144832, ChEBI:CHEBI:195402; Evidence={ECO:0000250|UniProtKB:P07203}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76712; Evidence={ECO:0000250|UniProtKB:P07203}; CATALYTIC ACTIVITY: Reaction=(17S)-hydroperoxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate + 2 glutathione = (17S)-hydroxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76715, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:133795, ChEBI:CHEBI:195403; Evidence={ECO:0000250|UniProtKB:P07203}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76716; Evidence={ECO:0000250|UniProtKB:P07203};
| null | null | null | null |
FUNCTION: Catalyzes the reduction of hydroperoxides in a glutathione-dependent manner thus regulating cellular redox homeostasis. Can reduce small soluble hydroperoxides such as H2O2, cumene hydroperoxide and tert-butyl hydroperoxide, as well as several fatty acid-derived hydroperoxides. In platelets catalyzes the reduction of 12-hydroperoxyeicosatetraenoic acid, the primary product of the arachidonate 12-lipoxygenase pathway. {ECO:0000250|UniProtKB:P11352}.
|
Rattus norvegicus (Rat)
|
P04042
|
CHEB_SALTY
|
MSKIRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVSSLTGKGSEVTLRALELGAIDFVTKPQLGIREGMLAYSEMIAEKVRTAARARIAAHKPMAAPTTLKAGPLLSSEKLIAIGASTGGTEAIRHVLQPLPLSSPAVIITQHMPPGFTRSFAERLNKLCQISVKEAEDGERVLPGHAYIAPGDKHMELARSGANYQIKIHDGPPVNRHRPSVDVLFHSVAKHAGRNAVGVILTGMGNDGAAGMLAMYQAGAWTIAQNEASCVVFGMPREAINMGGVSEVVDLSQVSQQMLAKISAGQAIRI
|
3.1.1.61; 3.5.1.44
| null |
chemotaxis [GO:0006935]
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cytoplasm [GO:0005737]
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phosphorelay response regulator activity [GO:0000156]; protein-glutamate methylesterase activity [GO:0008984]; protein-glutamine glutaminase activity [GO:0050568]
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PF01339;PF00072;
|
3.40.50.2300;3.40.50.180;
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CheB family
|
PTM: Phosphorylated by CheA (PubMed:2677005, PubMed:3280143, PubMed:9465023). Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity (PubMed:2677005, PubMed:9760239). {ECO:0000269|PubMed:2677005, ECO:0000269|PubMed:3280143, ECO:0000269|PubMed:9465023, ECO:0000269|PubMed:9760239}.; PTM: Two forms were isolated, the intact protein and a proteolytic fragment (147-349) that is 15-fold more active than its precursor. {ECO:0000269|PubMed:2991277}.
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SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07330, ECO:0000255|HAMAP-Rule:MF_00099}.
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CATALYTIC ACTIVITY: Reaction=[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol; Xref=Rhea:RHEA:23236, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:10311, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:29973, ChEBI:CHEBI:82795; EC=3.1.1.61; Evidence={ECO:0000255|HAMAP-Rule:MF_00099, ECO:0000269|PubMed:2677005, ECO:0000269|PubMed:2991277, ECO:0000269|PubMed:9760239}; CATALYTIC ACTIVITY: Reaction=H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:16441, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:10208, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29973, ChEBI:CHEBI:30011; EC=3.5.1.44; Evidence={ECO:0000250|UniProtKB:P07330, ECO:0000255|HAMAP-Rule:MF_00099};
| null | null | null | null |
FUNCTION: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR (PubMed:2677005, PubMed:2991277, PubMed:9760239). Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid (By similarity). {ECO:0000250|UniProtKB:P07330, ECO:0000269|PubMed:2677005, ECO:0000269|PubMed:2991277, ECO:0000269|PubMed:9760239}.
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Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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P04049
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RAF1_HUMAN
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MEHIQGAWKTISNGFGFKDAVFDGSSCISPTIVQQFGYQRRASDDGKLTDPSKTSNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDWSNIRQLLLFPNSTIGDSGVPALPSLTMRRMRESVSRMPVSSQHRYSTPHAFTFNTSSPSSEGSLSQRQRSTSTPNVHMVSTTLPVDSRMIEDAIRSHSESASPSALSSSPNNLSPTGWSQPKTPVPAQRERAPVSGTQEKNKIRPRGQRDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYKNCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQHSLPKINRSASEPSLHRAAHTEDINACTLTTSPRLPVF
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2.7.11.1
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COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.;
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activation of adenylate cyclase activity [GO:0007190]; apoptotic process [GO:0006915]; death-inducing signaling complex assembly [GO:0071550]; ERBB2-ERBB3 signaling pathway [GO:0038133]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; face development [GO:0060324]; insulin receptor signaling pathway [GO:0008286]; insulin secretion involved in cellular response to glucose stimulus [GO:0035773]; insulin-like growth factor receptor signaling pathway [GO:0048009]; intermediate filament cytoskeleton organization [GO:0045104]; MAPK cascade [GO:0000165]; myelination [GO:0042552]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; negative regulation of protein-containing complex assembly [GO:0031333]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein phosphorylation [GO:0006468]; Ras protein signal transduction [GO:0007265]; regulation of apoptotic process [GO:0042981]; regulation of cell differentiation [GO:0045595]; regulation of cell motility [GO:2000145]; regulation of Rho protein signal transduction [GO:0035023]; response to muscle stretch [GO:0035994]; Schwann cell development [GO:0014044]; signal transduction [GO:0007165]; somatic stem cell population maintenance [GO:0035019]; thymus development [GO:0048538]; thyroid gland development [GO:0030878]; type B pancreatic cell proliferation [GO:0044342]; type II interferon-mediated signaling pathway [GO:0060333]; wound healing [GO:0042060]
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cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; pseudopodium [GO:0031143]
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ATP binding [GO:0005524]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
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PF00130;PF00069;PF02196;
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3.30.60.20;1.10.510.10;
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Protein kinase superfamily, TKL Ser/Thr protein kinase family, RAF subfamily
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PTM: Phosphorylation at Thr-269, Ser-338, Tyr-341, Thr-491 and Ser-494 results in its activation. Phosphorylation at Ser-29, Ser-43, Ser-289, Ser-296, Ser-301 and Ser-642 by MAPK1/ERK2 results in its inactivation. Phosphorylation at Ser-259 induces the interaction with YWHAZ and inactivates kinase activity. Dephosphorylation of Ser-259 by the complex containing protein phosphatase 1, SHOC2 and M-Ras/MRAS relieves inactivation, leading to stimulate RAF1 activity. Phosphorylation at Ser-338 by PAK1 and PAK5 and Ser-339 by PAK1 is required for its mitochondrial localization. Phosphorylation at Ser-621 in response to growth factor treatment stabilizes the protein, possibly by preventing proteasomal degradation. Phosphorylation at Ser-289, Ser-296, Ser-301, Ser-338 and Ser-621 are somehow linked to the methylation potential of cells. Treatment of cells with HGF in the presence of the methylation inhibitor 5'-methylthioadenosine (MTA) results in increased phosphorylation at Ser-338 and Ser-621 and decreased phosphorylation at Ser-296, Ser-301 and Ser-338. Dephosphorylation at Ser-338 by PPP5C results in an activity decrease. {ECO:0000269|PubMed:10576742, ECO:0000269|PubMed:10801873, ECO:0000269|PubMed:11447113, ECO:0000269|PubMed:11733498, ECO:0000269|PubMed:11756411, ECO:0000269|PubMed:15047712, ECO:0000269|PubMed:15849194, ECO:0000269|PubMed:16093354, ECO:0000269|PubMed:16630891, ECO:0000269|PubMed:16892053, ECO:0000269|PubMed:18465753, ECO:0000269|PubMed:21917714, ECO:0000269|PubMed:7477354, ECO:0000269|PubMed:8349614, ECO:0000269|PubMed:9823899}.; PTM: Methylated at Arg-563 in response to EGF treatment. This modification leads to destabilization of the protein, possibly through proteasomal degradation. {ECO:0000269|PubMed:21917714}.
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SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Mitochondrion. Nucleus. Note=Colocalizes with RGS14 and BRAF in both the cytoplasm and membranes. Phosphorylation at Ser-259 impairs its membrane accumulation. Recruited to the cell membrane by the active Ras protein. Phosphorylation at Ser-338 and Ser-339 by PAK1 is required for its mitochondrial localization. Retinoic acid-induced Ser-621 phosphorylated form of RAF1 is predominantly localized at the nucleus.
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CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:17603483}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000269|PubMed:17603483}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:17603483}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000269|PubMed:17603483};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation. {ECO:0000269|PubMed:11427728, ECO:0000269|PubMed:11719507, ECO:0000269|PubMed:15385642, ECO:0000269|PubMed:15618521, ECO:0000269|PubMed:15849194, ECO:0000269|PubMed:16892053, ECO:0000269|PubMed:16924233, ECO:0000269|PubMed:9360956}.
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Homo sapiens (Human)
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P04050
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RPB1_YEAST
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MVGQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETMDETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHFGHIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNELMRQALAIKDSKKRFAAIWTLCKTKMVCETDVPSEDDPTQLVSRGGCGNTQPTIRKDGLKLVGSWKKDRATGDADEPELRVLSTEEILNIFKHISVKDFTSLGFNEVFSRPEWMILTCLPVPPPPVRPSISFNESQRGEDDLTFKLADILKANISLETLEHNGAPHHAIEEAESLLQFHVATYMDNDIAGQPQALQKSGRPVKSIRARLKGKEGRIRGNLMGKRVDFSARTVISGDPNLELDQVGVPKSIAKTLTYPEVVTPYNIDRLTQLVRNGPNEHPGAKYVIRDSGDRIDLRYSKRAGDIQLQYGWKVERHIMDNDPVLFNRQPSLHKMSMMAHRVKVIPYSTFRLNLSVTSPYNADFDGDEMNLHVPQSEETRAELSQLCAVPLQIVSPQSNKPCMGIVQDTLCGIRKLTLRDTFIELDQVLNMLYWVPDWDGVIPTPAIIKPKPLWSGKQILSVAIPNGIHLQRFDEGTTLLSPKDNGMLIIDGQIIFGVVEKKTVGSSNGGLIHVVTREKGPQVCAKLFGNIQKVVNFWLLHNGFSTGIGDTIADGPTMREITETIAEAKKKVLDVTKEAQANLLTAKHGMTLRESFEDNVVRFLNEARDKAGRLAEVNLKDLNNVKQMVMAGSKGSFINIAQMSACVGQQSVEGKRIAFGFVDRTLPHFSKDDYSPESKGFVENSYLRGLTPQEFFFHAMGGREGLIDTAVKTAETGYIQRRLVKALEDIMVHYDNTTRNSLGNVIQFIYGEDGMDAAHIEKQSLDTIGGSDAAFEKRYRVDLLNTDHTLDPSLLESGSEILGDLKLQVLLDEEYKQLVKDRKFLREVFVDGEANWPLPVNIRRIIQNAQQTFHIDHTKPSDLTIKDIVLGVKDLQENLLVLRGKNEIIQNAQRDAVTLFCCLLRSRLATRRVLQEYRLTKQAFDWVLSNIEAQFLRSVVHPGEMVGVLAAQSIGEPATQMTLNTFHFAGVASKKVTSGVPRLKEILNVAKNMKTPSLTVYLEPGHAADQEQAKLIRSAIEHTTLKSVTIASEIYYDPDPRSTVIPEDEEIIQLHFSLLDEEAEQSFDQQSPWLLRLELDRAAMNDKDLTMGQVGERIKQTFKNDLFVIWSEDNDEKLIIRCRVVRPKSLDAETEAEEDHMLKKIENTMLENITLRGVENIERVVMMKYDRKVPSPTGEYVKEPEWVLETDGVNLSEVMTVPGIDPTRIYTNSFIDIMEVLGIEAGRAALYKEVYNVIASDGSYVNYRHMALLVDVMTTQGGLTSVTRHGFNRSNTGALMRCSFEETVEILFEAGASAELDDCRGVSENVILGQMAPIGTGAFDVMIDEESLVKYMPEQKITEIEDGQDGGVTPYSNESGLVNADLDVKDELMFSPLVDSGSNDAMAGGFTAYGGADYGEATSPFGAYGEAPTSPGFGVSSPGFSPTSPTYSPTSPAYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPAYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPSYSPTSPGYSPGSPAYSPKQDEQKHNENENSR
|
2.7.7.6
| null |
RNA-templated transcription [GO:0001172]; transcription by RNA polymerase II [GO:0006366]; transcription elongation by RNA polymerase II [GO:0006368]; transcription initiation at RNA polymerase II promoter [GO:0006367]; translesion synthesis [GO:0019985]
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cytoplasmic stress granule [GO:0010494]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; RNA polymerase II, core complex [GO:0005665]
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DNA binding [GO:0003677]; metal ion binding [GO:0046872]; RNA polymerase II activity [GO:0001055]
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PF04997;PF00623;PF04983;PF05000;PF04998;PF04992;PF04990;PF05001;
|
1.10.132.30;1.10.150.390;2.40.40.20;3.30.1360.140;6.10.250.2940;6.20.50.80;3.30.1490.180;4.10.860.120;1.10.274.100;
|
RNA polymerase beta' chain family
|
PTM: The tandem 7 residues repeats in the C-terminal domain (CTD) can be highly phosphorylated. The phosphorylation activates Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat. The phosphorylated form of Pol II appears to carry, on average, one phosphate per repeat. The phosphorylation state is believed to result from the balanced action of site-specific CTD kinases and phosphatases, and a 'CTD code' that specifies the position of Pol II within the transcription cycle has been proposed. Phosphorylation at 'Ser-5' occurs in promoter-proximal regions in early elongation. Phosphorylation at 'Ser-2' predominates in regions more distal to the promoter and triggers binding of the 3' RNA processing machinery. CTD kinases include KIN28 (as part of the TFKII complex, a subcomplex of the TFIIH holo complex), SSN3/SRB10 (as part of the SRB8-11 complex, a module of the Mediator complex), CTK1 (as part of CTD kinase), and probably BUR1 (as part of the BUR1-BUR2 kinase complex). Phosphatases include FCP1 and SSU72. {ECO:0000269|PubMed:11390638, ECO:0000269|PubMed:15047695, ECO:0000269|PubMed:9702190}.; PTM: Following transcription stress, the elongating form of RNA polymerase II (RNA pol IIo) is polyubiquitinated via 'Lys-63'-linkages on Lys-1246 by the RSP5-UBA1-UBC5 complex at DNA damage sites without leading to degradation: ubiquitination promotes RNA pol IIo backtracking to allow access by the transcription-coupled nucleotide excision repair (TC-NER) machinery (PubMed:15166235, PubMed:15960978, PubMed:19920177, PubMed:32142654). Subsequent DEF1-dependent polyubiquitination by the elongin complex via 'Lys-48'-linkages may lead to proteasome-mediated degradation; presumably at stalled RNA pol II where TC-NER has failed, to halt global transcription and enable 'last resort' DNA repair pathways (PubMed:11859374, PubMed:15166235, PubMed:19920177, PubMed:32142654). {ECO:0000269|PubMed:11859374, ECO:0000269|PubMed:15166235, ECO:0000269|PubMed:15960978, ECO:0000269|PubMed:19920177, ECO:0000269|PubMed:32142654}.
|
SUBCELLULAR LOCATION: Nucleus.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6;
| null | null | null | null |
FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. During a transcription cycle, Pol II, general transcription factors and the Mediator complex assemble as the preinitiation complex (PIC) at the promoter. 11-15 base pairs of DNA surrounding the transcription start site are melted and the single-stranded DNA template strand of the promoter is positioned deeply within the central active site cleft of Pol II to form the open complex. After synthesis of about 30 bases of RNA, Pol II releases its contacts with the core promoter and the rest of the transcription machinery (promoter clearance) and enters the stage of transcription elongation in which it moves on the template as the transcript elongates. Pol II appears to oscillate between inactive and active conformations at each step of nucleotide addition. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing. Pol II is composed of mobile elements that move relative to each other. The core element with the central large cleft comprises RPB3, RBP10, RPB11, RPB12 and regions of RPB1 and RPB2 forming the active center. The clamp element (portions of RPB1, RPB2 and RPB3) is connected to the core through a set of flexible switches and moves to open and close the cleft. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. In elongating Pol II, the lid loop (RPB1) appears to act as a wedge to drive apart the DNA and RNA strands at the upstream end of the transcription bubble and guide the RNA strand toward the RNA exit groove located near the base of the largely unstructured CTD domain of RPB1. The rudder loop (RPB1) interacts with single-stranded DNA after separation from the RNA strand, likely preventing reassociation with the exiting RNA. The cleft is surrounded by jaws: an upper jaw formed by portions of RBP1, RPB2 and RPB9, and a lower jaw, formed by RPB5 and portions of RBP1. The jaws are thought to grab the incoming DNA template, mainly by RPB5 direct contacts to DNA.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P04051
|
RPC1_YEAST
|
MKEVVVSETPKRIKGLEFSALSAADIVAQSEVEVSTRDLFDLEKDRAPKANGALDPKMGVSSSSLECATCHGNLASCHGHFGHLKLALPVFHIGYFKATIQILQGICKNCSAILLSETDKRQFLHELRRPGVDNLRRMGILKKILDQCKKQRRCLHCGALNGVVKKAAAGAGSAALKIIHDTFRWVGKKSAPEKDIWVGEWKEVLAHNPELERYVKRCMDDLNPLKTLNLFKQIKSADCELLGIDATVPSGRPETYIWRYLPAPPVCIRPSVMMQDSPASNEDDLTVKLTEIVWTSSLIKAGLDKGISINNMMEHWDYLQLTVAMYINSDSVNPAMLPGSSNGGGKVKPIRGFCQRLKGKQGRFRGNLSGKRVDFSGRTVISPDPNLSIDEVAVPDRVAKVLTYPEKVTRYNRHKLQELIVNGPNVHPGANYLLKRNEDARRNLRYGDRMKLAKNLQIGDVVERHLEDGDVVLFNRQPSLHRLSILSHYAKIRPWRTFRLNECVCTPYNADFDGDEMNLHVPQTEEARAEAINLMGVKNNLLTPKSGEPIIAATQDFITGSYLISHKDSFYDRATLTQLLSMMSDGIEHFDIPPPAIMKPYYLWTGKQVFSLLIKPNHNSPVVINLDAKNKVFVPPKSKSLPNEMSQNDGFVIIRGSQILSGVMDKSVLGDGKKHSVFYTILRDYGPQEAANAMNRMAKLCARFLGNRGFSIGINDVTPADDLKQKKEELVEIAYHKCDELITLFNKGELETQPGCNEEQTLEAKIGGLLSKVREEVGDVCINELDNWNAPLIMATCGSKGSTLNVSQMVAVVGQQIISGNRVPDGFQDRSLPHFPKNSKTPQSKGFVRNSFFSGLSPPEFLFHAISGREGLVDTAVKTAETGYMSRRLMKSLEDLSCQYDNTVRTSANGIVQFTYGGDGLDPLEMEGNAQPVNFNRSWDHAYNITFNNQDKGLLPYAIMETANEILGPLEERLVRYDNSGCLVKREDLNKAEYVDQYDAERDFYHSLREYINGKATALANLRKSRGMLGLLEPPAKELQGIDPDETVPDNVKTSVSQLYRISEKSVRKFLEIALFKYRKARLEPGTAIGAIGAQSIGEPGTQMTLKTFHFAGVASMNVTLGVPRIKEIINASKVISTPIINAVLVNDNDERAARVVKGRVEKTLLSDVAFYVQDVYKDNLSFIQVRIDLGTIDKLQLELTIEDIAVAITRASKLKIQASDVNIIGKDRIAINVFPEGYKAKSISTSAKEPSENDVFYRMQQLRRALPDVVVKGLPDISRAVINIRDDGKRELLVEGYGLRDVMCTDGVIGSRTTTNHVLEVFSVLGIEAARYSIIREINYTMSNHGMSVDPRHIQLLGDVMTYKGEVLGITRFGLSKMRDSVLQLASFEKTTDHLFDAAFYMKKDAVEGVSECIILGQTMSIGTGSFKVVKGTNISEKDLVPKRCLFESLSNEAALKAN
|
2.7.7.6
| null |
termination of RNA polymerase III transcription [GO:0006386]; transcription by RNA polymerase III [GO:0006383]; transcription initiation at RNA polymerase III promoter [GO:0006384]; tRNA transcription by RNA polymerase III [GO:0042797]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase III complex [GO:0005666]
|
DNA binding [GO:0003677]; metal ion binding [GO:0046872]; RNA polymerase III activity [GO:0001056]
|
PF04997;PF00623;PF04983;PF05000;PF04998;
|
1.10.132.30;1.10.150.390;2.40.40.20;6.10.250.2940;6.20.50.80;3.30.1490.180;4.10.860.120;1.10.274.100;
|
RNA polymerase beta' chain family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6;
| null | null | null | null |
FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase active center together with the second largest subunit. A single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol III. A bridging helix emanates from RPC1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol III by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition (By similarity). {ECO:0000250}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P04052
|
RPB1_DROME
|
MSTPTDSKAPLRQVKRVQFGILSPDEIRRMSVTEGGVQFAETMEGGRPKLGGLMDPRQGVIDRTSRCQTCAGNMTECPGHFGHIDLAKPVFHIGFITKTIKILRCVCFYCSKMLVSPHNPKIKEIVMKSRGQPRKRLAYVYDLCKGKTICEGGEDMDLTKENQQPDPNKKPGHGGCGHYQPSIRRTGLDLTAEWKHQNEDSQEKKIVVSAERVWEILKHITDEECFILGMDPKYARPDWMIVTVLPVPPLAVRPAVVMFGAAKNQDDLTHKLSDIIKANNELRKNEASGAAAHVIQENIKMLQFHVATLVDNDMPGMPRAMQKSGKPLKAIKARLKGKEGRIRGNLMGKRVDFSARTVITPDPNLRIDQVGVPRSIAQNLTFPELVTPFNIDRMQELVRRGNSQYPGAKYIVRDNGERIDLRFHPKSSDLHLQCGYKVERHLRDDDLVIFNRQPTLHKMSMMGHRVKVLPWSTFRMNLSCTSPYNADFDGDEMNLHVPQSMETRAEVENIHITPRQIITPQANKPVMGIVQDTLTAVRKMTKRDVFITREQVMNLLMFLPTWDAKMPQPCILKPRPLWTGKQIFSLIIPGNVNMIRTHSTHPDEEDEGPYKWISPGDTKVMVEHGELIMGILCKKSLGTSAGSLLHICFLELGHDIAGRFYGNIQTVINNWLLFEGHSIGIGDTIADPQTYNEIQQAIKKAKDDVINVIQKAHNMELEPTPGNTLRQTFENKVNRILNDARDKTGGSAKKSLTEYNNLKAMVVSGSKGSNINISQVIACVGQQNVEGKRIPYGFRKRTLPHFIKDDYGPESRGFVENSYLAGLTPSEFYFHAMGGREGLIDTAVKTAETGYIQRRLIKAMESVMVNYDGTVRNSVGQLIQLRYGEDGLCGELVEFQNMPTVKLSNKSFEKRFKFDWSNERLMKKVFTDDVIKEMTDSSEAIQELEAEWDRLVSDRDSLRQIFPNGESKVVLPCNLQRMIWNVQKIFHINKRLPTDLSPIRVIKGVKTLLERCVIVTGNDRISKQANENATLLFQCLIRSTLCTKYVSEEFRLSTEAFEWLVGEIETRFQQAQANPGEMVGALAAQSLGEPATQMTLNTFHFAGVSSKNVTLGVPRLKEIINISKKPKAPSLTVFLTGGAARDAEKAKNVLCRLEHTTLRKVTANTAIYYDPDPQRTVISEDQEFVNVYYEMPDFDPTRISPWLLRIELDRKRMTDKKLTMEQIAEKINVGFGEDLNCIFNDDNADKLVLRIRIMNNEENKFQDEDEAVDKMEDDMFLRCIEANMLSDMTLQGIEAIGKVYMHLPQTDSKKRIVITETGEFKAIGEWLLETDGTSMMKVLSERDVDPIRTSSNDICEIFQVLGIEAVRKSVEKEMNAVLQFYGLYVNYRHLALLCDVMTAKGHLMAITRHGINRQDTGALMRCSFEETVDVLMDAAAHAETDPMRGVSENIIMGQLPKMGTGCFDLLLDAEKCRFGIEIPNTLGNSMLGGAAMFIGGGSTPSMTPPMTPWANCNTPRYFSPPGHVSAMTPGGPSFSPSAASDASGMSPSWSPAHPGSSPSSPGPSMSPYFPASPSVSPSYSPTSPNYTASSPGGASPNYSPSSPNYSPTSPLYASPRYASTTPNFNPQSTGYSPSSSGYSPTSPVYSPTVQFQSSPSFAGSGSNIYSPGNAYSPSSSNYSPNSPSYSPTSPSYSPSSPSYSPTSPCYSPTSPSYSPTSPNYTPVTPSYSPTSPNYSASPQYSPASPAYSQTGVKYSPTSPTYSPPSPSYDGSPGSPQYTPGSPQYSPASPKYSPTSPLYSPSSPQHSPSNQYSPTGSTYSATSPRYSPNMSIYSPSSTKYSPTSPTYTPTARNYSPTSPMYSPTAPSHYSPTSPAYSPSSPTFEESED
|
2.7.7.6
| null |
transcription by RNA polymerase II [GO:0006366]
|
nucleus [GO:0005634]; polytene chromosome [GO:0005700]; polytene chromosome puff [GO:0005703]; RNA polymerase II, core complex [GO:0005665]
|
DNA binding [GO:0003677]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; metal ion binding [GO:0046872]; RNA polymerase II activity [GO:0001055]
|
PF04997;PF00623;PF04983;PF05000;PF04998;PF04992;PF04990;
|
1.10.132.30;1.10.150.390;2.40.40.20;3.30.1360.140;6.10.250.2940;6.20.50.80;3.30.1490.180;4.10.860.120;1.10.274.100;
|
RNA polymerase beta' chain family
|
PTM: The tandem 7 residues repeats in the C-terminal domain (CTD) can be highly phosphorylated. The phosphorylation activates Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat. The phosphorylation state is believed to result from the balanced action of site-specific CTD kinases and phosphatase, and a 'CTD code' that specifies the position of Pol II within the transcription cycle has been proposed. {ECO:0000250|UniProtKB:P04050}.; PTM: Following transcription stress, the elongating form of RNA polymerase II (RNA pol IIo) is polyubiquitinated via 'Lys-63'-linkages on Lys-1260 at DNA damage sites without leading to degradation: ubiquitination promotes RNA pol IIo backtracking to allow access by the transcription-coupled nucleotide excision repair (TC-NER) machinery. Subsequent DEF1-dependent polyubiquitination by the elongin complex via 'Lys-48'-linkages may lead to proteasome-mediated degradation; presumably at stalled RNA pol II where TC-NER has failed, to halt global transcription and enable 'last resort' DNA repair pathways. {ECO:0000250|UniProtKB:P04050}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P04050}.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6;
| null | null | null | null |
FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing (By similarity). {ECO:0000250}.
|
Drosophila melanogaster (Fruit fly)
|
P04053
|
TDT_HUMAN
|
MDPPRASHLSPRKKRPRQTGALMASSPQDIKFQDLVVFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQAQKVQVSSQPELLDVSWLIECIRAGKPVEMTGKHQLVVRRDYSDSTNPGPPKTPPIAVQKISQYACQRRTTLNNCNQIFTDAFDILAENCEFRENEDSCVTFMRAASVLKSLPFTIISMKDTEGIPCLGSKVKGIIEEIIEDGESSEVKAVLNDERYQSFKLFTSVFGVGLKTSEKWFRMGFRTLSKVRSDKSLKFTRMQKAGFLYYEDLVSCVTRAEAEAVSVLVKEAVWAFLPDAFVTMTGGFRRGKKMGHDVDFLITSPGSTEDEEQLLQKVMNLWEKKGLLLYYDLVESTFEKLRLPSRKVDALDHFQKCFLIFKLPRQRVDSDQSSWQEGKTWKAIRVDLVLCPYERRAFALLGWTGSRQFERDLRRYATHERKMILDNHALYDKTKRIFLKAESEEEIFAHLGLDYIEPWERNA
|
2.7.7.31
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:11473582}; Note=Can also utilize other divalent cations, such as Mn(2+) and Co(2+) (in vitro). {ECO:0000250|UniProtKB:P09838, ECO:0000305};
|
DNA metabolic process [GO:0006259]; DNA modification [GO:0006304]; double-strand break repair via nonhomologous end joining [GO:0006303]; response to ATP [GO:0033198]
|
cytosol [GO:0005829]; euchromatin [GO:0000791]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA nucleotidylexotransferase activity [GO:0003912]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]
|
PF00533;PF14791;PF10391;PF14716;PF01909;
|
1.10.150.20;3.30.460.10;3.40.50.10190;1.10.150.110;3.30.210.10;
|
DNA polymerase type-X family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16371131}.
|
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.31; Evidence={ECO:0000269|PubMed:11473582, ECO:0000269|PubMed:16371131, ECO:0000269|PubMed:8163485};
| null | null | null | null |
FUNCTION: Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells. {ECO:0000250|UniProtKB:P09838}.
|
Homo sapiens (Human)
|
P04054
|
PA21B_HUMAN
|
MKLLVLAVLLTVAAADSGISPRAVWQFRKMIKCVIPGSDPFLEYNNYGCYCGLGGSGTPVDELDKCCQTHDNCYDQAKKLDSCKFLLDNPYTHTYSYSCSGSAITCSSKNKECEAFICNCDRNAAICFSKAPYNKAHKNLDTKKYCQS
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P00593}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P00593};
|
actin filament organization [GO:0007015]; activation of phospholipase A2 activity [GO:0032431]; antibacterial humoral response [GO:0019731]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; arachidonic acid secretion [GO:0050482]; cellular response to insulin stimulus [GO:0032869]; defense response to Gram-positive bacterium [GO:0050830]; fatty acid biosynthetic process [GO:0006633]; innate immune response in mucosa [GO:0002227]; intracellular signal transduction [GO:0035556]; leukotriene biosynthetic process [GO:0019370]; lipid catabolic process [GO:0016042]; neutrophil chemotaxis [GO:0030593]; neutrophil mediated immunity [GO:0002446]; phosphatidylcholine metabolic process [GO:0046470]; phosphatidylglycerol metabolic process [GO:0046471]; phospholipid metabolic process [GO:0006644]; positive regulation of calcium ion transport into cytosol [GO:0010524]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of immune response [GO:0050778]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of podocyte apoptotic process [GO:1904635]; positive regulation of protein secretion [GO:0050714]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of glucose import [GO:0046324]; signal transduction [GO:0007165]
|
cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
bile acid binding [GO:0032052]; calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipase A2 activity [GO:0004623]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family
|
PTM: Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically. {ECO:0000269|PubMed:19297324, ECO:0000269|PubMed:6349696}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19297324}. Note=Secreted from pancreatic acinar cells in its inactive form.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036, ECO:0000269|PubMed:10681567, ECO:0000269|PubMed:17603006}; CATALYTIC ACTIVITY: Reaction=1,2-ditetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1-tetradecanoyl-sn-glycero-3-phosphocholine + H(+) + tetradecanoate; Xref=Rhea:RHEA:54456, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:45240, ChEBI:CHEBI:64489; Evidence={ECO:0000269|PubMed:17603006}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000250|UniProtKB:P04055}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001; Evidence={ECO:0000269|PubMed:10681567}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; Evidence={ECO:0000305|PubMed:10681567}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428; Evidence={ECO:0000250|UniProtKB:P04055}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72841, ChEBI:CHEBI:75158; Evidence={ECO:0000269|PubMed:1420353}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920; Evidence={ECO:0000305|PubMed:1420353}; CATALYTIC ACTIVITY: Reaction=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:78097, ChEBI:CHEBI:85217; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425; Evidence={ECO:0000250|UniProtKB:P04055}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816; Evidence={ECO:0000250|UniProtKB:P04055}; CATALYTIC ACTIVITY: Reaction=H2O + N,1-dihexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = (9Z,12Z)-octadecadienoate + H(+) + N,1-dihexadecanoyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:56424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:85334, ChEBI:CHEBI:85335; Evidence={ECO:0000250|UniProtKB:P04055}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56425; Evidence={ECO:0000250|UniProtKB:P04055};
| null | null | null | null |
FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract (PubMed:10681567, PubMed:1420353, PubMed:17603006). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines (PubMed:10681567, PubMed:1420353, PubMed:17603006). May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation in the intestinal tract. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines (By similarity). May act in an autocrine and paracrine manner (PubMed:25335547, PubMed:7721806). Upon binding to the PLA2R1 receptor can regulate podocyte survival and glomerular homeostasis (PubMed:25335547). Has anti-helminth activity in a process regulated by gut microbiota. Upon helminth infection of intestinal epithelia, directly affects phosphatidylethanolamine contents in the membrane of helminth larvae, likely controlling an array of phospholipid-mediated cellular processes such as membrane fusion and cell division while providing for better immune recognition, ultimately reducing larvae integrity and infectivity (By similarity). {ECO:0000250|UniProtKB:P04055, ECO:0000250|UniProtKB:Q9Z0Y2, ECO:0000269|PubMed:10681567, ECO:0000269|PubMed:1420353, ECO:0000269|PubMed:17603006, ECO:0000269|PubMed:25335547, ECO:0000269|PubMed:7721806}.
|
Homo sapiens (Human)
|
P04055
|
PA21B_RAT
|
MKLLLLAALLTAGVTAHSISTRAVWQFRNMIKCTIPGSDPLREYNNYGCYCGLGGSGTPVDDLDRCCQTHDHCYNQAKKLESCKFLIDNPYTNTYSYKCSGNVITCSDKNNDCESFICNCDRQAAICFSKVPYNKEYKDLDTKKHC
|
3.1.1.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P00593}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P00593};
|
antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; arachidonic acid secretion [GO:0050482]; cellular response to insulin stimulus [GO:0032869]; fatty acid biosynthetic process [GO:0006633]; innate immune response in mucosa [GO:0002227]; lipid catabolic process [GO:0016042]; phosphatidylcholine metabolic process [GO:0046470]; phosphatidylglycerol metabolic process [GO:0046471]; phospholipid metabolic process [GO:0006644]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of podocyte apoptotic process [GO:1904635]; regulation of glucose import [GO:0046324]
|
cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; secretory granule [GO:0030141]
|
bile acid binding [GO:0032052]; calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipase A2 activity [GO:0004623]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102]
|
PF00068;
|
1.20.90.10;
|
Phospholipase A2 family
|
PTM: Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically. {ECO:0000250|UniProtKB:P04054}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04054}. Note=Secreted from pancreatic acinar cells in its inactive form. {ECO:0000250|UniProtKB:P04054}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036, ECO:0000269|PubMed:17158102}; CATALYTIC ACTIVITY: Reaction=1,2-ditetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1-tetradecanoyl-sn-glycero-3-phosphocholine + H(+) + tetradecanoate; Xref=Rhea:RHEA:54456, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:45240, ChEBI:CHEBI:64489; Evidence={ECO:0000250|UniProtKB:P04054}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000269|PubMed:17158102}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000305|PubMed:17158102}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001; Evidence={ECO:0000269|PubMed:17158102}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; Evidence={ECO:0000305|PubMed:17158102}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003; Evidence={ECO:0000269|PubMed:17158102}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428; Evidence={ECO:0000305|PubMed:17158102}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72841, ChEBI:CHEBI:75158; Evidence={ECO:0000269|PubMed:1420353}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920; Evidence={ECO:0000305|PubMed:1420353}; CATALYTIC ACTIVITY: Reaction=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:78097, ChEBI:CHEBI:85217; Evidence={ECO:0000269|PubMed:14998370}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425; Evidence={ECO:0000305|PubMed:14998370}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008; Evidence={ECO:0000269|PubMed:14998370}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816; Evidence={ECO:0000305|PubMed:14998370}; CATALYTIC ACTIVITY: Reaction=H2O + N,1-dihexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine = (9Z,12Z)-octadecadienoate + H(+) + N,1-dihexadecanoyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:56424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:85334, ChEBI:CHEBI:85335; Evidence={ECO:0000269|PubMed:14998370}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56425; Evidence={ECO:0000305|PubMed:14998370};
| null | null | null | null |
FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract (PubMed:1420353, PubMed:17158102). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines (PubMed:1420353, PubMed:17158102). May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation in the intestinal tract (PubMed:14998370). Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines (PubMed:14998370). May act in an autocrine and paracrine manner (By similarity). Has anti-helminth activity in a process regulated by gut microbiota. Upon helminth infection of intestinal epithelia, directly affects phosphatidylethanolamine contents in the membrane of helminth larvae, likely controlling an array of phospholipid-mediated cellular processes such as membrane fusion and cell division while providing for better immune recognition, ultimately reducing larvae integrity and infectivity (By similarity). {ECO:0000250|UniProtKB:P04054, ECO:0000250|UniProtKB:Q9Z0Y2, ECO:0000269|PubMed:1420353, ECO:0000269|PubMed:14998370, ECO:0000269|PubMed:17158102}.
|
Rattus norvegicus (Rat)
|
P04058
|
ACES_TETCF
|
MNLLVTSSLGVLLHLVVLCQADDHSELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGSEMWNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGGASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRRRAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQILLGVNKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTGNPNEPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVFWNQFLPKLLNATACDGELSSSGTSSSKGIIFYVLFSILYLIF
|
3.1.1.7
| null |
acetylcholine catabolic process in synaptic cleft [GO:0001507]; choline metabolic process [GO:0019695]
|
extracellular space [GO:0005615]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; synapse [GO:0045202]; synaptic cleft [GO:0043083]
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acetylcholinesterase activity [GO:0003990]
|
PF00135;
|
3.40.50.1820;
|
Type-B carboxylesterase/lipase family
|
PTM: An interchain disulfide bond is present in what becomes position 593 of the T isoform.
|
SUBCELLULAR LOCATION: [Isoform H]: Cell membrane; Lipid-anchor, GPI-anchor. Synapse.; SUBCELLULAR LOCATION: [Isoform T]: Cell membrane; Peripheral membrane protein. Synapse. Note=Attached to the membrane through disulfide linkage with the collagenic subunit, itself bound to the membrane.
|
CATALYTIC ACTIVITY: Reaction=acetylcholine + H2O = acetate + choline + H(+); Xref=Rhea:RHEA:17561, ChEBI:CHEBI:15354, ChEBI:CHEBI:15355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089; EC=3.1.1.7;
| null | null | null | null |
FUNCTION: Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions.
|
Tetronarce californica (Pacific electric ray) (Torpedo californica)
|
P04062
|
GBA1_HUMAN
|
MEFSSPSREECPKPLSRVSIMAGSLTGLLLLQAVSWASGARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANHTGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPEAAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVVGWTDWNLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQKNDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ
|
2.4.1.-; 3.2.1.-; 3.2.1.45; 3.2.1.46
| null |
antigen processing and presentation [GO:0019882]; autophagosome organization [GO:1905037]; autophagy [GO:0006914]; beta-glucoside catabolic process [GO:1901805]; brain morphogenesis [GO:0048854]; cell maturation [GO:0048469]; cellular response to starvation [GO:0009267]; cellular response to tumor necrosis factor [GO:0071356]; ceramide biosynthetic process [GO:0046513]; cerebellar Purkinje cell layer formation [GO:0021694]; cholesterol metabolic process [GO:0008203]; determination of adult lifespan [GO:0008340]; establishment of skin barrier [GO:0061436]; glucosylceramide catabolic process [GO:0006680]; hematopoietic stem cell proliferation [GO:0071425]; homeostasis of number of cells [GO:0048872]; lipid glycosylation [GO:0030259]; lipid storage [GO:0019915]; lymphocyte migration [GO:0072676]; lysosome organization [GO:0007040]; microglia differentiation [GO:0014004]; microglial cell proliferation [GO:0061518]; motor behavior [GO:0061744]; negative regulation of inflammatory response [GO:0050728]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of MAP kinase activity [GO:0043407]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of protein-containing complex assembly [GO:0031333]; neuromuscular process [GO:0050905]; neuron apoptotic process [GO:0051402]; positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization [GO:1904925]; positive regulation of neuronal action potential [GO:1904457]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein dephosphorylation [GO:0035307]; positive regulation of protein lipidation [GO:1903061]; positive regulation of protein-containing complex disassembly [GO:0043243]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; pyramidal neuron differentiation [GO:0021859]; regulation of lysosomal protein catabolic process [GO:1905165]; regulation of macroautophagy [GO:0016241]; regulation of TOR signaling [GO:0032006]; respiratory electron transport chain [GO:0022904]; response to dexamethasone [GO:0071548]; response to estrogen [GO:0043627]; response to pH [GO:0009268]; response to testosterone [GO:0033574]; response to thyroid hormone [GO:0097066]; sphingosine biosynthetic process [GO:0046512]; T cell differentiation in thymus [GO:0033077]; termination of signal transduction [GO:0023021]
|
endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; trans-Golgi network [GO:0005802]
|
galactosylceramidase activity [GO:0004336]; glucosylceramidase activity [GO:0004348]; glucosyltransferase activity [GO:0046527]; scavenger receptor binding [GO:0005124]; signaling receptor binding [GO:0005102]; steryl-beta-glucosidase activity [GO:0050295]
|
PF02055;PF17189;
|
3.20.20.80;
|
Glycosyl hydrolase 30 family
| null |
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:17187079, ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:18022370}; Peripheral membrane protein {ECO:0000269|PubMed:10781797, ECO:0000269|PubMed:18022370, ECO:0000269|PubMed:1848227}; Lumenal side {ECO:0000269|PubMed:18022370}. Note=Interaction with saposin-C promotes membrane association (PubMed:10781797). Targeting to lysosomes occurs through an alternative MPR-independent mechanism via SCARB2 (PubMed:18022370). {ECO:0000269|PubMed:10781797, ECO:0000269|PubMed:18022370}.
|
CATALYTIC ACTIVITY: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + H2O = an N-acylsphing-4-enine + D-glucose; Xref=Rhea:RHEA:13269, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:22801, ChEBI:CHEBI:52639; EC=3.2.1.45; Evidence={ECO:0000269|PubMed:15916907, ECO:0000269|PubMed:16293621, ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:32144204, ECO:0000269|PubMed:9201993}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13270; Evidence={ECO:0000269|PubMed:16293621, ECO:0000269|PubMed:32144204}; CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine + H2O = an N-acylsphing-4-enine + D-galactose; Xref=Rhea:RHEA:14297, ChEBI:CHEBI:4139, ChEBI:CHEBI:15377, ChEBI:CHEBI:18390, ChEBI:CHEBI:52639; EC=3.2.1.46; Evidence={ECO:0000269|PubMed:32144204}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14298; Evidence={ECO:0000305|PubMed:32144204}; CATALYTIC ACTIVITY: Reaction=cholesteryl 3-beta-D-glucoside + H2O = cholesterol + D-glucose; Xref=Rhea:RHEA:11956, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495; Evidence={ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:33361282}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11957; Evidence={ECO:0000269|PubMed:33361282, ECO:0000305|PubMed:24211208}; CATALYTIC ACTIVITY: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + cholesterol = an N-acylsphing-4-enine + cholesteryl 3-beta-D-glucoside; Xref=Rhea:RHEA:58264, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495, ChEBI:CHEBI:22801, ChEBI:CHEBI:52639; Evidence={ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:26724485, ECO:0000269|PubMed:32144204}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58265; Evidence={ECO:0000269|PubMed:32144204, ECO:0000305|PubMed:24211208}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:58266; Evidence={ECO:0000305|PubMed:32144204}; CATALYTIC ACTIVITY: Reaction=beta-D-glucosyl-N-(9Z-octadecenoyl)-sphing-4E-enine + cholesterol = cholesteryl 3-beta-D-glucoside + N-(9Z-octadecenoyl)-sphing-4-enine; Xref=Rhea:RHEA:58324, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495, ChEBI:CHEBI:77996, ChEBI:CHEBI:139140; Evidence={ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:32144204}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58325; Evidence={ECO:0000269|PubMed:32144204, ECO:0000305|PubMed:24211208}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:58326; Evidence={ECO:0000305|PubMed:32144204}; CATALYTIC ACTIVITY: Reaction=beta-D-glucosyl-(1<->1')-N-hexadecanoylsphing-4-enine + cholesterol = cholesteryl 3-beta-D-glucoside + N-hexadecanoylsphing-4-enine; Xref=Rhea:RHEA:58316, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495, ChEBI:CHEBI:72959, ChEBI:CHEBI:84716; Evidence={ECO:0000269|PubMed:24211208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58317; Evidence={ECO:0000305|PubMed:24211208}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:58318; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=beta-D-glucosyl-N-octanoylsphing-4E-enine + cholesterol = cholesteryl 3-beta-D-glucoside + N-octanoylsphing-4-enine; Xref=Rhea:RHEA:70303, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495, ChEBI:CHEBI:45815, ChEBI:CHEBI:65222; Evidence={ECO:0000269|PubMed:24211208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70304; Evidence={ECO:0000305|PubMed:24211208}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70305; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=beta-D-glucosyl-N-dodecanoylsphing-4-enine + cholesterol = cholesteryl 3-beta-D-glucoside + N-dodecanoylsphing-4-enine; Xref=Rhea:RHEA:70307, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495, ChEBI:CHEBI:72956, ChEBI:CHEBI:76297; Evidence={ECO:0000269|PubMed:24211208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70308; Evidence={ECO:0000305|PubMed:24211208}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70309; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=beta-D-glucosyl-(1<->1)-N-octadecanoylsphing-4-enine + cholesterol = cholesteryl 3-beta-D-glucoside + N-octadecanoylsphing-4-enine; Xref=Rhea:RHEA:70311, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495, ChEBI:CHEBI:72961, ChEBI:CHEBI:84719; Evidence={ECO:0000269|PubMed:24211208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70312; Evidence={ECO:0000305|PubMed:24211208}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70313; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=beta-D-glucosyl-(1<->1')-N-(15Z-tetracosenoyl)-sphing-4-enine + cholesterol = cholesteryl 3-beta-D-glucoside + N-(15Z-tetracosenoyl)-sphing-4-enine; Xref=Rhea:RHEA:70315, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495, ChEBI:CHEBI:74450, ChEBI:CHEBI:76302; Evidence={ECO:0000269|PubMed:24211208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70316; Evidence={ECO:0000305|PubMed:24211208}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70317; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine + cholesterol = an N-acylsphing-4-enine + cholesteryl 3-beta-D-galactoside; Xref=Rhea:RHEA:70235, ChEBI:CHEBI:16113, ChEBI:CHEBI:18390, ChEBI:CHEBI:52639, ChEBI:CHEBI:189066; Evidence={ECO:0000269|PubMed:32144204}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70236; Evidence={ECO:0000269|PubMed:32144204}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70237; Evidence={ECO:0000305|PubMed:32144204}; CATALYTIC ACTIVITY: Reaction=1-(beta-D-galactosyl)-N-dodecanoylsphing-4-enine + cholesterol = cholesteryl 3-beta-D-galactoside + N-dodecanoylsphing-4-enine; Xref=Rhea:RHEA:70255, ChEBI:CHEBI:16113, ChEBI:CHEBI:72956, ChEBI:CHEBI:73432, ChEBI:CHEBI:189066; Evidence={ECO:0000269|PubMed:32144204}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70256; Evidence={ECO:0000269|PubMed:32144204}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70257; Evidence={ECO:0000305|PubMed:32144204}; CATALYTIC ACTIVITY: Reaction=a beta-D-xylosyl-(1<->1')-N-acylsphing-4-enine + cholesterol = an N-acylsphing-4-enine + cholesteryl 3-beta-D-xyloside; Xref=Rhea:RHEA:70239, ChEBI:CHEBI:16113, ChEBI:CHEBI:52639, ChEBI:CHEBI:189067, ChEBI:CHEBI:189068; Evidence={ECO:0000269|PubMed:33361282}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70240; Evidence={ECO:0000269|PubMed:33361282}; CATALYTIC ACTIVITY: Reaction=beta-D-xylosyl-(1<->1')-N-(9Z-octadecenoyl)-sphing-4-enine + cholesterol = cholesteryl 3-beta-D-xyloside + N-(9Z-octadecenoyl)-sphing-4-enine; Xref=Rhea:RHEA:70251, ChEBI:CHEBI:16113, ChEBI:CHEBI:77996, ChEBI:CHEBI:189067, ChEBI:CHEBI:189081; Evidence={ECO:0000269|PubMed:33361282}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70252; Evidence={ECO:0000269|PubMed:33361282};
| null |
PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:26724485}.; PATHWAY: Sphingolipid metabolism. {ECO:0000269|PubMed:16293621, ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:26724485, ECO:0000269|PubMed:9201993}.
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BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.3. {ECO:0000269|PubMed:24211208};
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BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 43 degrees Celsius. {ECO:0000269|PubMed:24211208};
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FUNCTION: Glucosylceramidase that catalyzes, within the lysosomal compartment, the hydrolysis of glucosylceramides/GlcCers (such as beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine) into free ceramides (such as N-acylsphing-4-enine) and glucose (PubMed:15916907, PubMed:24211208, PubMed:32144204, PubMed:9201993). Plays a central role in the degradation of complex lipids and the turnover of cellular membranes (PubMed:27378698). Through the production of ceramides, participates in the PKC-activated salvage pathway of ceramide formation (PubMed:19279011). Catalyzes the glucosylation of cholesterol, through a transglucosylation reaction where glucose is transferred from GlcCer to cholesterol (PubMed:24211208, PubMed:26724485, PubMed:32144204). GlcCer containing mono-unsaturated fatty acids (such as beta-D-glucosyl-N-(9Z-octadecenoyl)-sphing-4-enine) are preferred as glucose donors for cholesterol glucosylation when compared with GlcCer containing same chain length of saturated fatty acids (such as beta-D-glucosyl-N-octadecanoyl-sphing-4-enine) (PubMed:24211208). Under specific conditions, may alternatively catalyze the reverse reaction, transferring glucose from cholesteryl 3-beta-D-glucoside to ceramide (Probable) (PubMed:26724485). Can also hydrolyze cholesteryl 3-beta-D-glucoside producing glucose and cholesterol (PubMed:24211208, PubMed:26724485). Catalyzes the hydrolysis of galactosylceramides/GalCers (such as beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine), as well as the transfer of galactose between GalCers and cholesterol in vitro, but with lower activity than with GlcCers (PubMed:32144204). Contrary to GlcCer and GalCer, xylosylceramide/XylCer (such as beta-D-xyosyl-(1<->1')-N-acylsphing-4-enine) is not a good substrate for hydrolysis, however it is a good xylose donor for transxylosylation activity to form cholesteryl 3-beta-D-xyloside (PubMed:33361282). {ECO:0000269|PubMed:15916907, ECO:0000269|PubMed:19279011, ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:26724485, ECO:0000269|PubMed:27378698, ECO:0000269|PubMed:32144204, ECO:0000269|PubMed:33361282, ECO:0000269|PubMed:9201993, ECO:0000305|PubMed:32144204}.
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Homo sapiens (Human)
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