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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P0C6Y0 | R1AB_CVMJH | MAKMGKYGLGFKWAPEFPWMLPNASEKLGNPERSEEDGFCPSAAQEPKVKGKTLVNHVRVDCSRLPALECCVQSAIIRDIFVDEDPQKVEASTMMALQFGSAVLVKPSKRLSVQAWAKLGVLPKTPAMGLFKRFCLCNTRECVCDAHVAFQLFTVQPDGVCLGNGRFIGWFVPVTAIPEYAKQWLQPWSILLRKGGNKGSVTSGHFRRAVTMPVYDFNVEDACEEVHLNPRGKYSCKAYALLRGYRGVKPILFVDQYGCDYTGCLAKGLEDYGDLTLSEMKELSPVWRDSLDNEVVVAWHVDRDPRAVMRLQTLATVRSI... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 2.7.7.50; 3.1.13.-; 3.4.19.12; 3.4.22.-; 3.6.4.12; 3.6.4.13; 4.6.1.- | COFACTOR: [Uridylate-specific endoribonuclease nsp15]: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P0C6X7}; Note=Likely affects Nsp15 binding to RNA. {ECO:0000250|UniProtKB:P0C6X7}; COFACTOR: [RNA-directed RNA polymerase nsp12]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProt... | DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont-mediated degradation of host mRNA [GO:0039595]; symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]; symbiont-mediated suppression of host ISG15-protein conjugation [GO:... | host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell membrane [GO:0033644]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020] | 3'-5'-RNA exonuclease activity [GO:0000175]; 5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; endonuclease activity [GO:0004519]; lyase activity [GO:0016829]; m... | PF13087;PF13245;PF11963;PF16251;PF06471;PF06460;PF09401;PF20631;PF20633;PF20632;PF19215;PF19216;PF19219;PF19218;PF16348;PF19217;PF19213;PF08716;PF08717;PF08710;PF08715;PF06478;PF01661;PF01831;PF05409;PF00680; | 1.10.8.1190;2.60.120.1680;3.10.20.350;3.10.20.540;3.40.50.11580;6.10.140.2090;1.10.150.420;3.40.220.10;1.10.1840.10;3.30.160.820;1.10.8.370;3.30.70.3540;3.40.50.300;2.40.10.250;3.40.50.11020;2.40.10.10;3.40.50.150; | Coronaviruses polyprotein 1ab family | PTM: Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: [Papain-like proteinase nsp3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Non-structural protein 6]: Host membrane {ECO:00... | CATALYTIC ACTIVITY: [RNA-directed RNA polymerase nsp12]: 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: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {EC... | Murine coronavirus (strain JHM) (MHV-JHM) (Murine hepatitis virus) |
P0C6Y1 | R1AB_IBVB | MASSLKQGVSPKPRDVILVSKDIPEQLCDALFFYTSHNPKDYADAFAVRQKFDRSLQTGKQFKFETVCGLFLLKGVDKITPGVPAKVLKATSKLADLEDIFGVSPLARKYRELLKTACQWSLTVEALDVRAQTLDEIFDPTEILWLQVAAKIHVSSMAMRRLVGEVTAKVMDALGSNLSALFQIVKQQIARIFQKALAIFENVNELPQRIAALKMAFAKCARSITVVVVERTLVVKEFAGTCLASINGAVAKFFEELPNGFMGSKIFTTLAFFKEAAVRVVENIPNAPRGTKGFEVVGNAKGTQVVVRGMRNDLTLLDQK... | 2.1.1.-; 2.1.1.57; 2.7.7.48; 2.7.7.50; 3.1.13.-; 3.4.19.12; 3.4.22.-; 3.6.4.12; 3.6.4.13; 4.6.1.- | COFACTOR: [Uridylate-specific endoribonuclease]: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P0C6X7}; Note=Likely affects Nsp15 binding to RNA. {ECO:0000250|UniProtKB:P0C6X7}; COFACTOR: [Papain-like protease]: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P0C6X7}; | DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; viral protein processing [GO:0019082]; viral RNA genome replication [GO:0039694] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020] | 3'-5'-RNA exonuclease activity [GO:0000175]; 5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; endonuclease activity [GO:0004519]; lyase activity [GO:0016829]; mRNA (nucleoside-2'-O-)-methyltransferase activity [G... | PF06471;PF06460;PF09401;PF20631;PF20633;PF20632;PF19215;PF19216;PF19219;PF19218;PF16348;PF19217;PF19213;PF08716;PF08717;PF08710;PF08715;PF06478;PF01661;PF17896;PF05409;PF00680;PF01443; | 1.10.8.1190;2.60.120.1680;3.40.50.11580;6.10.250.2820;1.10.150.420;3.40.220.10;1.10.1840.10;3.30.160.820;1.10.8.370;3.30.70.3540;3.40.50.300;2.40.10.250;2.40.10.10;3.40.50.150; | Coronaviruses polyprotein 1ab family | PTM: [Isoform Replicase polyprotein 1ab]: Specific enzymatic cleavages in vivo by its own proteases yield mature proteins (By similarity). 3C-like proteinase nsp5 liberates nsps 6-16 from the polyprotein (By similarity). Papain-like and 3C-like proteinases are autocatalytically processed. {ECO:0000250|UniProtKB:P0C6X7}... | SUBCELLULAR LOCATION: [Papain-like protease]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {ECO:0000250|UniProt... | CATALYTIC ACTIVITY: [Papain-like protease]: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:25609249}; CATA... | null | null | null | null | FUNCTION: [Isoform Replicase polyprotein 1ab]: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. {ECO:0000305}.; FUNCTION: [Non-structural protein 2]: May play a role in the modulation of host cell survival sig... | Avian infectious bronchitis virus (strain Beaudette) (IBV) |
P0C6Y2 | R1AB_IBVBC | MASSLKQGVSPKPRDVILVSKDIPEQLCDALFFYTSHNPKDYADAFAVRQKFDRSLQTGKQFKFETVCGLFLLKGVDKITPGVPAKVLKATSKLADLEDIFGVSPLARKYRELLKTACQWSLTVEALDVRAQTLDEIFDPTEILWLQVAAKIHVSSMAMRRLVGEVTAKVMDALGSNLSALFQIVKQQIARIFQKALAIFENVNELPQRIAALKMAFAKCARSITVVVVERTLVVKEFAGTCLASINGAVAKFFEELPNGFMGSKIFTTLAFFKEAAVRVVENIPNAPRGTKGFEVVGNAKGTQVVVRGMRNDLTLLDQK... | 2.1.1.-; 2.1.1.57; 2.7.7.48; 2.7.7.50; 3.1.13.-; 3.4.19.12; 3.4.22.-; 3.6.4.12; 3.6.4.13; 4.6.1.- | COFACTOR: [Uridylate-specific endoribonuclease]: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P0C6X7}; Note=Likely affects Nsp15 binding to RNA. {ECO:0000250|UniProtKB:P0C6X7}; COFACTOR: [Papain-like protease]: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P0C6X7}; | DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; viral protein processing [GO:0019082]; viral RNA genome replication [GO:0039694] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020] | 3'-5'-RNA exonuclease activity [GO:0000175]; 5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; endonuclease activity [GO:0004519]; lyase activity [GO:0016829]; mRNA (nucleoside-2'-O-)-methyltransferase activity [G... | PF06471;PF06460;PF09401;PF20631;PF20633;PF20632;PF19215;PF19216;PF19219;PF19218;PF16348;PF19217;PF19213;PF08716;PF08717;PF08710;PF08715;PF06478;PF01661;PF17896;PF05409;PF00680;PF01443; | 1.10.8.1190;2.60.120.1680;3.40.50.11580;6.10.250.2820;1.10.150.420;3.40.220.10;1.10.1840.10;3.30.160.820;1.10.8.370;3.30.70.3540;3.40.50.300;2.40.10.250;2.40.10.10;3.40.50.150; | Coronaviruses polyprotein 1ab family | PTM: [Isoform Replicase polyprotein 1ab]: Specific enzymatic cleavages in vivo by its own proteases yield mature proteins (By similarity). 3C-like proteinase nsp5 liberates nsps 6-16 from the polyprotein (By similarity). Papain-like and 3C-like proteinases are autocatalytically processed. {ECO:0000250|UniProtKB:P0C6X7}... | SUBCELLULAR LOCATION: [Papain-like protease]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {ECO:0000250|UniProt... | CATALYTIC ACTIVITY: [RNA-directed RNA polymerase nsp12]: 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: [Isoform Replicase polyprotein 1ab]: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. {ECO:0000305}.; FUNCTION: [Non-structural protein 2]: May play a role in the modulation of host cell survival sig... | Avian infectious bronchitis virus (strain Beaudette CK) (IBV) |
P0C6Y3 | R1AB_IBVM | MASSLKQGVSPKLRDVILVSKDIPEQLCDALFFYTSHNPKDYADAFAVRQKFDRNLQTGKQFKFETVCGLFLLKGVDKITPGVPAKVLKATSKLADLEDIFGVSPFARKYRELLKTACQWSLTVETLDARAQTLDEIFDPTEILWLQVAAKIQVSAMAMRRLVGEVTAKVMDALGSNMSALFQIFKQQIVRIFQKALAIFENVSELPQRIAALKMAFAKCAKSITVVVMERTLVVREFAGTCLASINGAVAKFFEELPNGFMGAKIFTTLAFFREAAVKIVDNIPNAPRGTKGFEVVGNAKGTQVVVRGMRNDLTLLDQK... | 2.1.1.-; 2.1.1.57; 2.7.7.48; 2.7.7.50; 3.1.13.-; 3.4.19.12; 3.4.22.-; 3.6.4.12; 3.6.4.13; 4.6.1.- | COFACTOR: [Uridylate-specific endoribonuclease]: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P0C6X7}; Note=Likely affects Nsp15 binding to RNA. {ECO:0000250|UniProtKB:P0C6X7}; COFACTOR: [Papain-like protease]: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P0C6X7}; | DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; viral protein processing [GO:0019082]; viral RNA genome replication [GO:0039694] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020] | 3'-5'-RNA exonuclease activity [GO:0000175]; 5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; endonuclease activity [GO:0004519]; lyase activity [GO:0016829]; mRNA (nucleoside-2'-O-)-methyltransferase activity [G... | PF06471;PF06460;PF09401;PF20631;PF20633;PF20632;PF19215;PF19216;PF19219;PF19218;PF16348;PF19217;PF19213;PF08716;PF08717;PF08710;PF08715;PF06478;PF01661;PF17896;PF05409;PF00680;PF01443; | 1.10.8.1190;2.60.120.1680;3.40.50.11580;6.10.250.2820;1.10.150.420;3.40.220.10;1.10.1840.10;3.30.160.820;1.10.8.370;3.30.70.3540;3.40.50.300;2.40.10.250;2.40.10.10;3.40.50.150; | Coronaviruses polyprotein 1ab family | PTM: [Isoform Replicase polyprotein 1ab]: Specific enzymatic cleavages in vivo by its own proteases yield mature proteins (By similarity). 3C-like proteinase nsp5 liberates nsps 6-16 from the polyprotein (By similarity). Papain-like and 3C-like proteinases are autocatalytically processed. {ECO:0000250|UniProtKB:P0C6X7}... | SUBCELLULAR LOCATION: [Papain-like protease]: Host endoplasmic reticulum membrane {ECO:0000305|PubMed:30200673}; Multi-pass membrane protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {ECO:0000305|PubMed:3... | CATALYTIC ACTIVITY: [Papain-like protease]: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:P0C6Y1}; CAT... | null | null | null | null | FUNCTION: [Isoform Replicase polyprotein 1ab]: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. {ECO:0000305}.; FUNCTION: [Non-structural protein 2]: May play a role in the modulation of host cell survival sig... | Avian infectious bronchitis virus (strain M41) (IBV) |
P0C6Y4 | R1AB_PEDV7 | MASNHVTLAFANDAEISAFGFCTASEAVSYYSEAAASGFMQCRFVSLDLADTVEGLLPEDYVMVVIGTTKLSAYVDTFGSRPRNICGWLLFSNCNYFLEELELTFGRRGGNIVPVDQYMCGADGKPVLQESEWEYTDFFADSEDGQLNIAGITYVKAWIVERSDVSYASQNLTSIKSITYCSTYEHTFLDGTAMKVARTPKIKKNVVLSEPLATIYREIGSPFVDNGSDARSIIRRPVFLHAFVKCKCGSYHWTVGDWTSYVSTCCGFKCKPVLVASCSAMPGSVVVTRAGAGTGVKYYNNMFLRHVADIDGLAFWRILK... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 2.7.7.50; 3.1.13.-; 3.4.19.12; 3.4.22.-; 3.6.4.12; 3.6.4.13; 4.6.1.- | COFACTOR: [Uridylate-specific endoribonuclease nsp15]: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P0C6X7}; Note=Likely affects Nsp15 binding to RNA. {ECO:0000250|UniProtKB:P0C6X7}; | DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activ... | host cell endoplasmic reticulum [GO:0044165]; host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell membrane [GO:0033644]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020] | 3'-5'-RNA exonuclease activity [GO:0000175]; 5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; lyas... | PF13087;PF13604;PF06471;PF06460;PF09401;PF20631;PF20633;PF20632;PF19215;PF19216;PF19219;PF19212;PF19211;PF19218;PF16348;PF19217;PF19213;PF08716;PF08717;PF08710;PF08715;PF06478;PF01661;PF05409;PF00680; | 1.10.8.1190;3.40.50.11580;6.10.140.2090;1.10.150.420;3.40.220.10;1.10.1840.10;3.30.160.820;1.10.8.370;3.30.70.3540;3.40.50.300;2.40.10.250;2.40.10.10;3.40.50.150; | Coronaviruses polyprotein 1ab family | PTM: [Replicase polyprotein 1ab]: Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: [Non-structural protein 1]: Host cytoplasm {ECO:0000269|PubMed:26773386}. Host nucleus {ECO:0000269|PubMed:26773386}.; SUBCELLULAR LOCATION: [Papain-like protease nsp3]: Host membrane {ECO:0000250|UniProtKB:P0C6X7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0C6X7}.; SUBCELLULAR LOCATION:... | CATALYTIC ACTIVITY: [Papain-like protease nsp3]: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; CATALYTIC ACTIVITY: [RNA-directed RNA p... | null | null | null | null | FUNCTION: [Replicase polyprotein 1ab]: Multifunctional protein responsible for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.; FUNCTION: [Non-structural protein 1]: Plays a r... | Porcine epidemic diarrhea virus (strain CV777) (PEDV) |
P0C6Y5 | R1AB_CVPPU | MSSKQFKILVNEDYQVNVPSLPIRDVLQEIKYCYRNGFEGYVFVPEYCRDLVDCDRKDHYVIGVLGNGVSDLKPVLLTEPSVMLQGFIVRANCNGVLEDFDLKIARTGRGAIYVDQYMCGADGKPVIEGDFKDYFGDEDIIEFEGEEYHCAWTTVRDEKPLNQQTLFTIQEIQYNLDIPHKLPNCATRHVAPPVKKNSKIVLSEDYKKLYDIFGSPFMGNGDCLSKCFDTLHFIAATLRCPCGSESSGVGDWTGFKTACCGLSGKVKGVTLGDIKPGDAVVTSMSAGKGVKFFANCVLQYAGDVEGVSIWKVIKTFTVDE... | 2.1.1.57; 2.7.7.48; 2.7.7.50; 3.1.13.-; 3.4.19.12; 3.4.22.-; 3.6.4.12; 3.6.4.13; 4.6.1.- | COFACTOR: [Uridylate-specific endoribonuclease]: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P0C6X7}; Note=Likely affects Nsp15 binding to RNA. {ECO:0000250|UniProtKB:P0C6X7}; | DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activ... | host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell membrane [GO:0033644]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020] | 3'-5'-RNA exonuclease activity [GO:0000175]; 5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; endonuclease activity [GO:0004519]; lyase activity [GO:0016829]; m... | PF13087;PF13245;PF16688;PF06471;PF06460;PF09401;PF20631;PF20633;PF20632;PF19215;PF19216;PF19219;PF19212;PF19211;PF19218;PF16348;PF19217;PF19213;PF08716;PF08717;PF08710;PF08715;PF06478;PF01661;PF05409;PF00680; | 1.10.8.1190;3.10.20.540;3.40.50.11580;6.10.140.2090;1.10.150.420;3.40.220.10;1.10.1840.10;3.30.160.820;1.10.8.370;3.30.70.3540;3.40.50.300;2.40.10.250;2.30.30.1000;2.40.10.10;3.40.50.150; | Coronaviruses polyprotein 1ab family | PTM: Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO is autocatalytically processed. {ECO:0000269|PubMed:11842254}. | SUBCELLULAR LOCATION: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Non-structural protein 6]: Host membrane {ECO:00003... | CATALYTIC ACTIVITY: [Non-structural protein 3]: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; CATALYTIC ACTIVITY: [RNA-directed RNA po... | null | null | null | null | FUNCTION: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {EC... | Porcine transmissible gastroenteritis coronavirus (strain Purdue) (TGEV) |
P0C6Y6 | E_PRRSL | MGSLWSKISQLFVDAFTEFLVSVVDIAIFLAILFGFTVAGWLLVFLLRVVCSALLRSRSAIHSPELSKVL | null | null | protein complex oligomerization [GO:0051259] | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | monoatomic ion channel activity [GO:0005216] | PF07069; | null | Arteriviridae E protein family | PTM: Myristoylated. {ECO:0000269|PubMed:19951726}.; PTM: Not glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:16160177}; Single-pass type I membrane protein {ECO:0000269|PubMed:16160177}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:16160177}; Single-pass type I membrane protein {ECO:0000269|PubMed:16160177}. Host Golgi apparatus membrane {ECO:0000269|PubMed:... | null | null | null | null | null | FUNCTION: Minor envelope protein. May function as a viroporin in the virion envelope that facilitates uncoating of the virus in order to release the genomic RNA into the cytoplasm for subsequent replication. {ECO:0000269|PubMed:16904148}. | Porcine reproductive and respiratory syndrome virus (strain Lelystad) (PRRSV) |
P0C6Y7 | PRDM9_RAT | MSRTMNTNKPEENSTEGDAGKLEWKPKVKDEFKDISIYFSKEEWAEMGEWEKIRYRNVKRNYKMLISIGLRAPRPAFMCYQRQAIKPQINDNEDSDEEWTPKQQVSSPWVPFRVKHSKQQKETPRMPLSDKSSVKEVFGIENLLNTSGSEHAQKPVCSPEEGNTSGQHFGKKLKLRRKNVEVNRYRLRERKDLAYEEVSEPQDDDYLYCEKCQNFFIDSCPNHGPPVFVKDSVVDRGHPNHSVLSLPPGLRIGPSGIPEAGLGVWNEASDLPVGLHFGPYKGQITEDEEAANSGYSWLITKGRNCYEYVDGQDESQANWM... | 2.1.1.-; 2.1.1.354; 2.1.1.355; 2.1.1.359; 2.1.1.361; 2.1.1.362 | null | double-strand break repair involved in meiotic recombination [GO:1990918]; female gamete generation [GO:0007292]; homologous chromosome pairing at meiosis [GO:0007129]; male gamete generation [GO:0048232]; meiosis I [GO:0007127]; meiotic gene conversion [GO:0006311]; methylation [GO:0032259]; negative regulation of apo... | chromatin [GO:0000785]; nucleus [GO:0005634] | histone H3K36 methyltransferase activity [GO:0046975]; histone H3K36 trimethyltransferase activity [GO:0140955]; histone H3K4 methyltransferase activity [GO:0042800]; histone H3K4 trimethyltransferase activity [GO:0140999]; histone H3K9 trimethyltransferase activity [GO:0140949]; histone H4K20 monomethyltransferase act... | PF01352;PF21549;PF09514;PF00096;PF21225; | 6.10.140.140;3.30.160.60;2.170.270.10; | Class V-like SAM-binding methyltransferase superfamily | PTM: Mono-methylated; automethylated. Tri-methylated; automethylated. Mono-methylation is predominant; automethylation is lower and slower than H3 peptide methylation and is in a highest S-adenosyl-L-methionine concentration-dependent. There are two major sites for automethylation at Lys-372 and Lys-378. Lysines can be... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96EQ9}. Chromosome {ECO:0000250|UniProtKB:Q96EQ9}. Note=Localizes in nuclei of pre-leptotene, leptotene, and early to mid-zygotene spermatocytes. {ECO:0000250|UniProtKB:Q96EQ9}. | CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; Evidence={ECO:00002... | null | null | null | null | FUNCTION: Histone methyltransferase that sequentially mono-, di-, and tri-methylates both 'Lys-4' (H3K4) and 'Lys-36' (H3K36) of histone H3 to produce respectively trimethylated 'Lys-4' (H3K4me3) and trimethylated 'Lys-36' (H3K36me3) histone H3 and plays a key role in meiotic prophase by determining hotspot localizatio... | Rattus norvegicus (Rat) |
P0C746 | HBZ_HTL1A | MVNFVSAGLFRCLPVSCPEDLLVEELVDGLLSLEEELKDKEEEEAVLDGLLSLEEESRGRLRRGPPGEKAPPRGETHRDRQRRAEEKRKRKKEREKEEEKQTAEYLKRKEEEKARRRRRAEKKAADVARRKQEEQERRERKWRQGAEKAKQHSARKEKMQELGIDGYTRQLEGEVESLEAERRKLLQEKEDLMGEVNYWQGRLEAMWLQ | null | null | viral process [GO:0016032] | host cell nucleus [GO:0042025] | DNA binding [GO:0003677] | null | null | HTLV-1 HBZ protein family | null | SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:12438606}. | null | null | null | null | null | FUNCTION: Contributes to the regulation of viral RNA transcription by interacting with host proteins involved in transcriptional activation such as ATF4, or CREB1, and by inhibiting their activity. Additionally, HBZ suppresses host NF-kappa-B-driven transcription mediated by host RELA as well as transcription of some c... | Human T-cell leukemia virus 1 (strain Japan ATK-1 subtype A) (HTLV-1) |
P0C767 | HBEAG_HBVCJ | MQLFPLCLIISCSCPTVQASKLCLGWLWGMDIDPYKEFGASVELLSFLPSDFFPSIRDLLDTASALYREALESPEHCSPHHTALRQAILCWGELMNLATWVGSNLEDPASRELVVSYVNVNMGLKIRQLLWFHISCLTFGRETVLEYLVSFGVWIRTPPAYRPPNAPILSTLPETTVVRRRGRSPRRRTPSPRRRRSQSPRRRRSQSRESQC | null | null | microtubule-dependent intracellular transport of viral material towards nucleus [GO:0075521]; symbiont entry into host cell [GO:0046718]; viral penetration into host nucleus [GO:0075732]; virus-mediated perturbation of host defense response [GO:0019049] | extracellular region [GO:0005576]; host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; T=4 icosahedral viral capsid [GO:0039619] | DNA binding [GO:0003677]; RNA binding [GO:0003723]; structural molecule activity [GO:0005198] | PF08290;PF00906; | 1.10.4090.10; | Orthohepadnavirus precore antigen family | PTM: Phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04076}.; PTM: Cleaved by host furin. {ECO:0000255|HAMAP-Rule:MF_04076}. | SUBCELLULAR LOCATION: Secreted {ECO:0000255|HAMAP-Rule:MF_04076}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04076}. | null | null | null | null | null | FUNCTION: May regulate immune response to the intracellular capsid in acting as a T-cell tolerogen, by having an immunoregulatory effect which prevents destruction of infected cells by cytotoxic T-cells. This immune regulation may predispose to chronicity during perinatal infections and prevent severe liver injury duri... | Hepatitis B virus genotype C subtype ayr (isolate Human/Japan/Okamoto/-) (HBV-C) |
P0C776 | GAG_ALVA | MEAVIKVISSACKTYCGKISPSKKEIGAMLSLLQKEGLLMSPSDLYSPGSWDPITAALSQRAMVLGKSGELKTWGLVLGALKAAREEQVTSEQAKFWLGLGGGRVSPPGPECIEKPATERRIDKGEEVGETTAQRDAKMAPEKMATPKTVGTSCYQCGTATGCNCATASAPPPPYVGSGLYPSLAGVGEQQGQGGDTPWGAEQPRAEPGHAGLAPGPALTDWARIREELASTGPPVVAMPVVIKTEGPAWTPLEPKLITRLADTVRTKGLRSPITMAEVEALMSSPLLPHDVTNLMRVILGPAPYALWMDAWGVQLQTVI... | 3.4.23.- | null | proteolysis [GO:0006508]; viral procapsid maturation [GO:0046797] | host cell nucleolus [GO:0044196]; host cell nucleoplasm [GO:0044095]; viral capsid [GO:0019028] | aspartic-type endopeptidase activity [GO:0004190]; nucleic acid binding [GO:0003676]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270] | PF00607;PF02813;PF00077;PF00098; | 1.10.1200.30;2.40.70.10;1.10.375.10;1.10.150.90;4.10.60.10; | null | PTM: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. The cleavage at the C-terminus of the Capsid protein p27 is slowly trimmed by the viral protease, sometimes being cut internally thereby generating the short version of the capsid protein and a capsid protein C-terminally extended by 3 ... | SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000250|UniProtKB:P03322}.; SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 1]: Virion {ECO:0000250|UniProtKB:P03322}.; SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 2]: Virion {ECO:0000250|UniProtKB:P03322}.; SUBCELLULAR LOCATION: [Nuc... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: The p10 domain folds back and interacts with the capsid protein domain during Gag polyprotein assembly in the immature particle (before the maturation cleavage thatz splits the 2 domains). {ECO:0000250|UniProtKB:P03322}.; FUNCTION: [Capsid protein p27, alternate cleaved 1]: Self-associates ... | Avian leukosis virus subgroup A (isolate RSA) (ALV-A RSA) |
P0C797 | NCAP_BDVV | MPPKRRLVDDADAMEDQDLYEPPASLPKLPGKFLQYTVGGSDPHPGIGHEKDIRQNAVALLDQSRRDMFHTVTPSLVFLCLLIPGLHAAFVHGGVPRESYLSTPVTRGEQTVVKTAKFYGEKTTQRDLTELEISSIFSHCCSLLIGVVIGSSSKIKAGAEQIKKRFKTMMAALNRPSHGETATLLQMFNPHEAIDWINGQPWVGSFVLSLLTTDFESPGKEFMDQIKLVASYAQMTTYTTIKEYLAECMDATLTIPVVAYEIRDFLEVSAKLKEDHADLFPFLGAIRHPDAIKLAPRSFPNLASAAFYWSKKENPTMAGY... | null | null | symbiont entry into host cell [GO:0046718]; symbiont-mediated arrest of host cell cycle during G2/M transition [GO:0039592]; symbiont-mediated suppression of host NF-kappaB cascade [GO:0085034]; viral penetration into host nucleus [GO:0075732] | helical viral capsid [GO:0019029]; host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; viral nucleocapsid [GO:0019013] | null | PF06407; | 1.10.3040.10;1.10.3050.10; | null | null | SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host nucleus {ECO:0000269|PubMed:11238866}. Host cytoplasm {ECO:0000269|PubMed:11238866}. Note=Shuttles between the host nucleus and cytoplasm. {ECO:0000269|PubMed:11238866}. | null | null | null | null | null | FUNCTION: Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. Plays a critical role in the nucleocytoplasmic transport of viral RNP by interaction with other viral proteins. The nuclear export signal is masked by ... | Borna disease virus (strain V) (BDV) |
P0C7A3 | MBOA4_MOUSE | MDWLQLFFLHPLSFYQGAAFPFALLFNYLCILDTFSTRARYLFLLAGGGVLAFAAMGPYSLLIFIPALCAVALVSFLSPQEVHRLTFFFQMGWQTLCHLGLHYTEYYLGEPPPVRFYITLSSLMLLTQRVTSLSLDICEGKVEAPRRGIRSKSSFSEHLWDALPHFSYLLFFPALLGGSLCSFRRFQACVQRSSSLYPSISFRALTWRGLQILGLECLKVALRSAVSAGAGLDDCQRLECIYLMWSTAWLFKLTYYSHWILDDSLLHAAGFGAEAGQGPGEEGYVPDVDIWTLETTHRISLFARQWNRSTALWLRRLVFR... | 2.3.1.- | null | lipid modification [GO:0030258]; peptidyl-serine octanoylation [GO:0018191]; protein acylation [GO:0043543]; protein decanoylation [GO:0051366]; protein octanoylation [GO:0018190] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020] | acyltransferase activity, transferring groups other than amino-acyl groups [GO:0016747]; serine O-acyltransferase activity [GO:0016412] | PF03062; | null | Membrane-bound acyltransferase family | PTM: Not glycosylated. {ECO:0000269|PubMed:24045953}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18267071, ECO:0000269|PubMed:24045953}; Multi-pass membrane protein {ECO:0000269|PubMed:18267071}. | CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + octanoyl-CoA = CoA + O-octanoyl-L-seryl-[protein]; Xref=Rhea:RHEA:59964, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15484, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386, ChEBI:CHEBI:143548; Evidence={ECO:0000269|PubMed:18443287, ECO:0000269|PubMed:18669668, ECO:000026... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=294 uM for n-hexanoyl-CoA {ECO:0000269|PubMed:19501572}; KM=13.6 uM for n-octanoyl-CoA {ECO:0000269|PubMed:19501572}; KM=0.6 uM for octanoyl CoA {ECO:0000269|PubMed:18669668}; KM=6 uM for proghrelin {ECO:0000269|PubMed:18669668}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:19501572}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37-50 degrees Celsius. {ECO:0000269|PubMed:19501572}; | FUNCTION: Catalyzes ghrelin acylation at 'Ser-3' using preferentially octanoyl-CoA, hexanoyl-CoA and decanoyl-CoA as acyl-CoA donors leading to ghrelin activity (PubMed:18267071, PubMed:18443287, PubMed:18669668, PubMed:19501572, PubMed:24045953, PubMed:28134508). In vitro uses also acyl-CoA donors of different lengths... | Mus musculus (Mouse) |
P0C7B0 | VM3H6_GLOBR | MIQVLLVTICLAAFPYQGSSIILESGNVNDYEVVYPRKVTALPKGAVQPKYEDAMQYEFKVNGEPVVLHLGKNKQLFSKDYSETHYSPDGREITTNPPVEDHCYYHGRIENDADSTRSISACNGLKGHFKLQGETYLIEPLKLSDSEAHAVYKYENILKEDEAPKMCGVTQNWESYEPIKKASQLNLTPEQQRYNPFRFVELVLVADKGMVTKNNGDLNKIKTRMYELANNLNDIYRYMYIHVALVGVEIWSDGDKITVTPNVDDTLSSFAEWRKTHLLTRKKHDNAQLLTAIDFNGPTIGYAYIASMCHPKRSVGIVQD... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729] | PF08516;PF00200;PF01562;PF01421; | 3.40.390.10;4.10.70.10; | Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIb sub-subfamily | PTM: In the absence of calcium ions, is autocatalytically degraded giving 29 (p29K) and 45 kDa (p45K) fragments. In presence of calcium ions, the p45K is not detected (PubMed:10920250). {ECO:0000269|PubMed:10920250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10920250}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8 in the absence of calcium ions. Optimum pH is 5.6-8.5 in the presence of calcium ions.; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: The activity is markedly reduced above 40 degrees Celsius. Calcium ions increases the thermal stability by 10 degrees Celsius.; | FUNCTION: Shows weak hemorrhagic activity. Rapidly degrades the alpha-chain of fibrinogen (FGA). {ECO:0000269|PubMed:10920250}. | Gloydius brevicaudus (Korean slamosa snake) (Agkistrodon halys brevicaudus) |
P0C7B1 | VM3BG_BOTAL | SISACNGLKGHFLIEPLKLSDSEKTDLLNRSHDNAQLSPINLVVAVIMAHEMGHGMVLPGTK | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | proteolysis [GO:0006508] | extracellular region [GO:0005576] | metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237]; toxin activity [GO:0090729] | null | null | Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIc sub-subfamily | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12893294}. | null | null | null | null | null | FUNCTION: Snake venom Zinc metalloproteinase that inhibits ADP-induced platelet aggregation and inhibits the alpha-5/beta-1 (ITGA5/ITGB1) integrin, a fibronectin receptor. Has caseinolytic activity. Induces the detachment of cells that are bound to fibronectin. {ECO:0000269|PubMed:12893294}. | Bothrops alternatus (Urutu) (Rhinocerophis alternatus) |
P0C7I4 | PAND_ECOLW | MIRTMLQGKLHRVKVTHADLHYEGSCAIDQDFLDAAGILENEAIDIWNVTNGKRFSTYAIAAERGSRIISVNGAAAHCASVGDIVIIASFVTMPDEEARTWRPNVAYFEGDNEMKRTAKAIPVQVA | 4.1.1.11 | COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000269|PubMed:381298}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000269|PubMed:381298}; | alanine biosynthetic process [GO:0006523]; pantothenate biosynthetic process [GO:0015940] | cytosol [GO:0005829] | aspartate 1-decarboxylase activity [GO:0004068] | PF02261; | 2.40.40.20; | PanD family | PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=H(+) + L-aspartate = beta-alanine + CO2; Xref=Rhea:RHEA:19497, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29991, ChEBI:CHEBI:57966; EC=4.1.1.11; Evidence={ECO:0000269|PubMed:381298}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=80 uM for L-aspartate (at pH 6.8 and 37 degrees Celsius) {ECO:0000269|PubMed:381298}; KM=160 uM for L-aspartate (at pH 7.5) {ECO:0000269|PubMed:381298}; | PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is about 7.5. The reaction rates at the pH values of 6.8 and 8.0 are about 60% of the pH 7.5 rate. {ECO:0000269|PubMed:381298}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. The half-maximal activity is reached at 26 degrees Celsius and 78 degrees Celsius. {ECO:0000269|PubMed:381298}; | FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. {ECO:0000269|PubMed:381298}. | Escherichia coli (strain ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 / NCIMB 8666 / NRRL B-766 / W) |
P0C7J6 | LRFN1_RAT | MAPGPFSSGLLSPPPAALPFLLLLWAGASRGQPCPGRCICQNVAPTLTMLCAKTGLLFVPPAIDRRVVELRLTDNFIAAVRRRDFANMTSLVHLTLSRNTIGQVAAGAFADLRALRALHLDSNRLAEVRGDQLRGLGNLRHLILGNNQIRKVESAAFDAFLSTVEDLDLSYNNLEALPWEAVGQMVNLNTLTLDHNLIDHIAEGTFVQLHKLVRLDMTSNRLHKLPPDGLFLRSQGGGPKPPTPLTVSFGGNPLHCNCELLWLRRLTREDDLETCATPEHLTDRYFWSIPEEEFLCEPPLITRQAGGRALVVEGQAVSLR... | null | null | regulation of postsynaptic density assembly [GO:0099151] | cell surface [GO:0009986]; postsynaptic density membrane [GO:0098839] | null | PF00041;PF07679;PF13855; | 2.60.40.10;3.80.10.10; | LRFN family | PTM: Glycosylated. {ECO:0000269|PubMed:16630835}. | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16630835}; Single-pass type I membrane protein {ECO:0000269|PubMed:16630835}. Synapse {ECO:0000269|PubMed:16630835}. Postsynaptic density membrane {ECO:0000269|PubMed:16630835}. Note=Detected in excitatory, but not inhibitory, synaptic plasma membrane. | null | null | null | null | null | FUNCTION: Promotes neurite outgrowth in hippocampal neurons (By similarity). Involved in the regulation of the differentiation and maintenance of excitatory synapses. Induces the clustering of excitatory postsynaptic proteins, including DLG4, DLGAP1, GRIA1 and GRIN1. {ECO:0000250, ECO:0000269|PubMed:16630835}. | Rattus norvegicus (Rat) |
P0C7L0 | WIPF3_MOUSE | MPVPPPPPPPPPPPPPPPPPLGAPPPPPLGAPPPPPPPGPPVSTDTPSLRKPDLKGRSALLADIQQGTRLRKVTQINDRSAPQIEGSKGTSKEGGAAGSNARGGNTPPALGDLFAGGFPVLRPAGQRDVSGGKSGQGPGSRAPSPRLPIKAISGPLPAPASPRLGNASETHSSARPVPPRPSVPAPPPPTPPPPPPPPLPPASPIKAQLVSPPAPPTKVNPSVVPPPLPCAPPLPPPPPTPPPLPPASALSDKAVRPQLAPLHLPPIPPPLPLLPPCGYPGLHSEPNSPAQEVREPPAPPPPPPPPPPPPLPTYASCSSR... | null | null | Arp2/3 complex-mediated actin nucleation [GO:0034314]; cell differentiation [GO:0030154]; endocytic recycling [GO:0032456]; exocytosis [GO:0006887]; retrograde transport, endosome to Golgi [GO:0042147]; spermatogenesis [GO:0007283] | early endosome [GO:0005769]; recycling endosome [GO:0055037]; WASH complex [GO:0071203] | actin binding [GO:0003779]; alpha-tubulin binding [GO:0043014]; gamma-tubulin binding [GO:0043015]; SH3 domain binding [GO:0017124] | PF02205; | null | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17573773}. Note=In hippocampal neurons colocalizes with WASL in the cell body, axons and the growth cone (By similarity). Localizes to the actin filaments at the Sertoli cell-spermatid junctions. {ECO:0000250}. | null | null | null | null | null | FUNCTION: May be a regulator of cytoskeletal organization (Potential). May have a role in spermatogenesis. {ECO:0000269|PubMed:17573773, ECO:0000305}. | Mus musculus (Mouse) |
P0C7L2 | PAAJ_ECOLI | MREAFICDGIRTPIGRYGGALSSVRADDLAAIPLRELLVRNPRLDAECIDDVILGCANQAGEDNRNVARMATLLAGLPQSVSGTTINRLCGSGLDALGFAARAIKAGDGDLLIAGGVESMSRAPFVMGKAASAFSRQAEMFDTTIGWRFVNPLMAQQFGTDSMPETAENVAELLKISREDQDSFALRSQQRTAKAQSSGILAEEIVPVVLKNKKGVVTEIQHDEHLRPETTLEQLRGLKAPFRANGVITAGNASGVNDGAAALIIASEQMAAAQGLTPRARIVAMATAGVEPRLMGLGPVPATRRVLERAGLSIHDMDVI... | 2.3.1.174; 2.3.1.223 | null | 3,4-dihydroxybenzoate catabolic process [GO:0019619]; DNA damage response [GO:0006974]; fatty acid beta-oxidation [GO:0006635]; phenylacetate catabolic process [GO:0010124] | null | 3-oxoadipyl-CoA thiolase activity [GO:0033812]; acetyl-CoA C-acyltransferase activity [GO:0003988]; transferase activity [GO:0016740] | PF02803;PF00108; | 3.40.47.10; | Thiolase-like superfamily, Thiolase family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + succinyl-CoA = 3-oxoadipyl-CoA + CoA; Xref=Rhea:RHEA:19481, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57292, ChEBI:CHEBI:57348; EC=2.3.1.174; Evidence={ECO:0000269|PubMed:17259607, ECO:0000269|PubMed:20660314}; CATALYTIC ACTIVITY: Reaction=2,3-didehydroadipoyl-CoA + ace... | null | PATHWAY: Aromatic compound metabolism; phenylacetate degradation. | null | null | FUNCTION: Catalyzes the thiolytic cleavage of the beta-keto C8 intermediate 3-oxo-5,6-dehydrosuberyl-CoA with CoA to yield the C6 intermediate 2,3-dehydroadipyl-CoA and acetyl-CoA. Besides it catalyzes also the last step of the pathway, in which 3-oxoadipyl-CoA similarly is cleaved to acetyl-CoA and succinyl-CoA. {ECO:... | Escherichia coli (strain K12) |
P0C7P0 | CISD3_HUMAN | MRGAGAILRPAARGARDLNPRRDISSWLAQWFPRTPARSVVALKTPIKVELVAGKTYRWCVCGRSKKQPFCDGSHFFQRTGLSPLKFKAQETRMVALCTCKATQRPPYCDGTHRSERVQKAEVGSPL | null | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:29259115, ECO:0000305|PubMed:17376863}; Note=Binds 2 [2Fe-2S] clusters per subunit. {ECO:0000269|PubMed:29259115, ECO:0000305|PubMed:17376863}; | protein maturation by [2Fe-2S] cluster transfer [GO:0106034] | mitochondrion [GO:0005739] | 2 iron, 2 sulfur cluster binding [GO:0051537]; metal ion binding [GO:0046872] | PF09360; | 3.40.5.90; | CISD protein family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17376863}. | null | null | null | null | null | FUNCTION: Can transfer its iron-sulfur clusters to the apoferrodoxins FDX1 and FDX2. Contributes to mitochondrial iron homeostasis and in maintaining normal levels of free iron and reactive oxygen species, and thereby contributes to normal mitochondrial function. {ECO:0000269|PubMed:29259115}. | Homo sapiens (Human) |
P0C7P3 | SLN14_HUMAN | MESLKTDTEMPYPEVIVDVGRVIFGEENRKKMTNSCLKRSENSRIIRAICALLNSGGGVIKAEIDDKTYSYQCHGLGQDLETSFQKLLPSGSQKYLDYMQQGHNLLIFVKSWSPDVFSLPLRICSLRSNLYRRDVTSAINLSASSALELLREKGFRAQRGRPRVKKLHPQQVLNRCIQEEEDMRILASEFFKKDKLMYKEKLNFTESTHVEFKRFTTKKVIPRIKEMLPHYVSAFANTQGGYVLIGVDDKSKEVVGCKWEKVNPDLLKKEIENCIEKLPTFHFCCEKPKVNFTTKILNVYQKDVLDGYVCVIQVEPFCCV... | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:G1SRW8}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:G1SRW8}; Note=C-terminally truncated SLFN14 endoribonuclease requires manganese and magnesium for its endoribonuclease activity. {ECO:0000250|UniProtKB:G1SRW8}; | cellular response to magnesium ion [GO:0071286]; cellular response to manganese ion [GO:0071287]; mRNA catabolic process [GO:0006402]; platelet maturation [GO:0036345]; rRNA catabolic process [GO:0016075] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ribosome binding [GO:0043022]; RNA endonuclease activity [GO:0004521] | PF17057;PF04326;PF21026; | 3.30.950.30; | Schlafen family, Subgroup III subfamily | null | SUBCELLULAR LOCATION: [Protein SLFN14]: Nucleus {ECO:0000269|PubMed:25996083, ECO:0000269|PubMed:26280575}. | null | null | null | null | null | FUNCTION: [Protein SLFN14]: Shows no ribosome-associated and endoribonuclease activities. {ECO:0000269|PubMed:25996083}.; FUNCTION: [C-terminally truncated SLFN14 endoribonuclease]: Displays polysome-associated endoribonuclease activity towards mRNAs and rRNAs (PubMed:25996083). May play a role in RNA surveillance path... | Homo sapiens (Human) |
P0C7P5 | BNP_PROFL | MFVSRLAASGLLLLALLALSLDGKPVHQSKPGRSPPISPLSAQQWMPEGRPPHPIPPLSVQQWSQGRPRSEVPPVVVQPHESPAGGTTAFREELSPGPEAASGPAAPHRLPKSKGASATSAASRPMRDLRTDGKQERQKWGRMVQPDHHAAPGGGGGGGGGARRMKGLAKKAMGKGCFGHKLDRIGSTSGLGC | null | null | cGMP biosynthetic process [GO:0006182]; receptor guanylyl cyclase signaling pathway [GO:0007168]; regulation of blood pressure [GO:0008217]; vasodilation [GO:0042311] | extracellular region [GO:0005576] | hormone activity [GO:0005179]; peptidase inhibitor activity [GO:0030414]; toxin activity [GO:0090729] | PF00212; | null | Bradykinin-potentiating peptide family; Natriuretic peptide family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10876042}. | null | null | null | null | null | FUNCTION: Bradykinin-potentiating peptide both inhibits the activity of the angiotensin-converting enzyme (ACE) and enhances the action of bradykinin by inhibiting the peptidases that inactivate it. It acts as an indirect hypotensive agent (By similarity). Neither synthetic Tf1, nor synthetic Tf2 show bradykinin-potent... | Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis) |
P0C7Q4 | GNAT3_BOVIN | MGIGISSESKESAKRSKELEKKLQEDAERDARTVKLLLLGAGESGKSTIVKQMKIIHKNGYSEQECMEFKAVIYSNTLQSILAIVKAMATLEIDYVNPRSAEDQQQLCAMANTLEDGSMTPELAEIIKRLWRDPGVQACFERASEYQLNDSAAYYLNDLDRIAAPGYVPNEQDVLHSRVKTTGIIETQFSFKDLHFRMFDVGGQRSERKKWIHCFEGVTCIIFCAALSAYDMVLVEDEEVNRMHESLHLFNSICNHKYFATTSIVLFLNKKDLFQEKVTKVHLSICFPEYTGPNTFEDAGNYIKNQFLDLNLKKEDKEIY... | null | null | adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; detection of chemical stimulus involved in sensory perception of bitter taste [GO:0001580]; sensory perception of sweet taste [GO:0050916] | cytoplasm [GO:0005737]; heterotrimeric G-protein complex [GO:0005834]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750] | G protein-coupled receptor binding [GO:0001664]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872] | PF00503; | 1.10.400.10;3.40.50.300; | G-alpha family, G(i/o/t/z) subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Guanine nucleotide-binding protein (G protein) alpha subunit playing a prominent role in bitter and sweet taste transduction as well as in umami (monosodium glutamate, monopotassium glutamate, and inosine monophosphate) taste transduction. | Bos taurus (Bovine) |
P0C7Q8 | DA1_ARATH | MGWFNKIFKGSNQRLRVGNNKHNHNVYYDNYPTASHDDEPSAADTDADNDEPHHTQEPSTSEDNTSNDQENEDIDRAIALSLLEENQEQTSISGKYSMPVDEDEQLARALQESMVVGNSPRHKSGSTYDNGNAYGAGDLYGNGHMYGGGNVYANGDIYYPRPITFQMDFRICAGCNMEIGHGRFLNCLNSLWHPECFRCYGCSQPISEYEFSTSGNYPFHKACYRERYHPKCDVCSHFIPTNHAGLIEYRAHPFWVQKYCPSHEHDATPRCCSCERMEPRNTRYVELNDGRKLCLECLDSAVMDTMQCQPLYLQIQNFYE... | null | null | negative regulation of cell population proliferation [GO:0008285]; negative regulation of organ growth [GO:0046621]; plant ovule morphogenesis [GO:0048482]; positive regulation of leaf senescence [GO:1900057]; regulation of DNA endoreduplication [GO:0032875]; regulation of organ growth [GO:0046620]; regulation of seed ... | null | metal ion binding [GO:0046872]; peptidase activity [GO:0008233]; ubiquitin binding [GO:0043130] | PF12315;PF00412; | 2.10.110.10; | null | PTM: Ubiquitinated at Lys-95, Lys-221, Lys-348, Lys-376, Lys-381, Lys-391, Lys-474, Lys-475 and Lys-519 by the E3 ubiquitin-protein ligases BB and DA2. {ECO:0000269|PubMed:28167503}. | null | null | null | null | null | null | FUNCTION: Ubiquitin receptor that limits final seed and organ size by restricting the period of cell proliferation. May act maternally to control seed mass (PubMed:18483219, PubMed:24045020). Acts synergistically with DA2 to regulate seed size. Functions synergistically with DA2 to restrict cell proliferation in the ma... | Arabidopsis thaliana (Mouse-ear cress) |
P0C7R1 | PPR74_ARATH | MALEAAFSMSFCSFSVPKAIFCERETSSFQRITSRAKGIAGESQVQSSDGVETQVKETSPKVFDKLPERNLDTWSGGRETARGLSGSVVRNTVRKDTTLRHISPSSHSTKVRGDKPEISGGEKKAIVDRSKAYVKLKSLGKEVRDAGYVPETKYVLHDIDEEAKEKALMHHSERLAIAFGIINTPPGTTIRVMKNLRICGDCHNFIKILSSIEDREIIVRDNKRFHHFRDGNCSCGDYW | null | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:24194514, ECO:0000269|PubMed:25041347}; Note=Binds 2 zinc ions per subunit. {ECO:0000269|PubMed:24194514}; | chloroplast mRNA modification [GO:1900871]; chloroplast RNA modification [GO:1900865]; mRNA processing [GO:0006397] | chloroplast [GO:0009507]; plastid [GO:0009536] | zinc ion binding [GO:0008270] | PF14432; | null | PPR family, PCMP-H subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:23001034}. | null | null | null | null | null | FUNCTION: Plays a major role in single RNA editing events in chloroplasts. Acts as a site-recognition transacting factor involved in the edition of the site 1 of ndhD (ndhD-1 site corresponding to cytidine-2), which is a plastid-encoded subunit of the NADH-plastoquinone oxidoreductase. The interaction with CRR4 is requ... | Arabidopsis thaliana (Mouse-ear cress) |
P0C7R2 | LI2P2_ARATH | MVFSVATSSVTNPKLHHHHHLSDFNRNRVSTSLKIMNSKNHTNPRKCECFDLYDQLIPYKKAWSWQKSILNEKKALIDKNQECSDSLIILQHPSVYTMGTGSSENYLNFDIKNAPFDVYRTERGGEVTYHGPGQLVMYPIINLRNHKMDLHWYLRKLEEVVIRVLSSAFAINASRLDGFTGVWVGNKKMAAIGIRVSKWMTYHGLALNVTTDLTPFNSIVPCGIRNRGVGSVKGLIEDGEHYNKLEDLQLLDIAHESLLKEFSEVFQLQMEKQTVFKLEC | 2.3.1.181 | null | protein modification process [GO:0036211]; rRNA processing [GO:0006364]; tRNA processing [GO:0008033] | chloroplast [GO:0009507]; nucleolar ribonuclease P complex [GO:0005655]; ribonuclease MRP complex [GO:0000172] | lipoyl(octanoyl) transferase activity [GO:0033819] | null | null | LipB family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:23581459}. | CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:17665, Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:9928, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479, ChEBI:CHEBI:78463, ChEBI:CHEBI:78809; ... | null | PATHWAY: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00013}. | null | null | FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity) (PubMed:23581459). Together with LIP1P... | Arabidopsis thaliana (Mouse-ear cress) |
P0C7T5 | ATX1L_HUMAN | MKPVHERSQECLPPKKRDLPVTSEDMGRTTSCSTNHTPSSDASEWSRGVVVAGQSQAGARVSLGGDGAEAITGLTVDQYGMLYKVAVPPATFSPTGLPSVVNMSPLPPTFNVASSLIQHPGIHYPPLHYAQLPSTSLQFIGSPYSLPYAVPPNFLPSPLLSPSANLATSHLPHFVPYASLLAEGATPPPQAPSPAHSFNKAPSATSPSGQLPHHSSTQPLDLAPGRMPIYYQMSRLPAGYTLHETPPAGASPVLTPQESQSALEAAAANGGQRPRERNLVRRESEALDSPNSKGEGQGLVPVVECVVDGQLFSGSQTPRV... | null | null | brain development [GO:0007420]; extracellular matrix organization [GO:0030198]; learning [GO:0007612]; lung alveolus development [GO:0048286]; memory [GO:0007613]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of hematopoietic stem cell proliferation [GO:1902035]; regulatio... | dendrite [GO:0030425]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; POZ domain binding [GO:0031208]; RNA binding [GO:0003723] | PF12547;PF08517; | 2.170.16.10; | ATXN1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16121196}. Cell projection, dendrite {ECO:0000269|PubMed:16121196}. Note=Forms nuclear foci. Colocalizes with NCOR2 and HDAC3. Distributed beyond the nucleus into the cell body and dendrites in Purkinje cells and in inferior olive cells. | null | null | null | null | null | FUNCTION: Chromatin-binding factor that repress Notch signaling in the absence of Notch intracellular domain by acting as a CBF1 corepressor. Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-mediated repression (PubMed:21475249). Can suppress ATXN1 cytotoxicity in spinocerebellar ataxia type 1 (SCA1).... | Homo sapiens (Human) |
P0C7T6 | ATX1L_MOUSE | MKPVHERSQECLPPKKRDLPVTSEDMGRTTSCSTNHTPSSDASEWSRGVVVAGQSQTGARVSLGGDGTEAITGLTVDQYGMLYKVAVPPATFSPTGLPSVVNMSPLPPTFNVASSLIQHPGIHYPPVHYAQLPSTSLQFIGSPYSLPYAVPPNFLPSPLLSPSANLATTHLPHFVPYASLLAEEATPPPQAASPAQSFNKSSSATSPPGQLPHHSNTQPLDLAPGRMPIYYQMSRLPAGYTLHETSTAGASPILTPQEGQSALEAAAANGQRQRERNVRRESEALDSASSKGESQGLVPVVECMADGQLFSGSQTPRVEV... | null | null | brain development [GO:0007420]; extracellular matrix organization [GO:0030198]; learning [GO:0007612]; lung alveolus development [GO:0048286]; memory [GO:0007613]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of hematopoietic stem cell proliferation [GO:1902035]; regulatio... | dendrite [GO:0030425]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; POZ domain binding [GO:0031208]; RNA binding [GO:0003723] | PF12547;PF08517; | 2.170.16.10; | ATXN1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16121196}. Cell projection, dendrite {ECO:0000269|PubMed:16121196}. Note=Forms nuclear foci. Colocalizes with NCOR2 and HDAC3. Distributed beyond the nucleus into the cell body and dendrites in Purkinje cells and in inferior olive cells. | null | null | null | null | null | FUNCTION: Chromatin-binding factor that repress Notch signaling in the absence of Notch intracellular domain by acting as a CBF1 corepressor. Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-mediated repression (By similarity). Can suppress the cytotoxicity of ATXN1 in spinocerebellar ataxia type 1 (S... | Mus musculus (Mouse) |
P0C7W6 | CC172_HUMAN | MSLESLFQHIIFTEHQAEESRRLMREVRSEITRCREKIKKATEELNEEKIKLESKVQQFFEKSFFLQLLKAHENALEKQYSEITNHRNMLLQTFEAIKKQMIEEEDKFIKEITDFNNDYEITKKRELLMKENVKIEISDLENQANMLKSEMKSMEHDSSQLNELQKQKSELIQELFTLQRKLKVFEDEENESICTTKYLEAEKIKISEKPQNDTECLRLKKELELYKEDDMESVYEALQTEIEFLELTLAQKDLQESK | null | null | null | cytoplasm [GO:0005737]; sperm midpiece [GO:0097225] | null | null | null | CCDC172 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q810N9}. Cell projection, cilium {ECO:0000250|UniProtKB:Q6AXT4}. Note=In spermatozoa, localized in the middle piece, predominantly concentrated at the mitochondrial sheath of the flagella and to a lesser extent with outer dense fibers (ODF) (By similarity). Colocal... | null | null | null | null | null | null | Homo sapiens (Human) |
P0C7X2 | ZN688_HUMAN | MAPPPAPLLAPRPGETRPGCRKPGTVSFADVAVYFSPEEWGCLRPAQRALYRDVMQETYGHLGALGFPGPKPALISWMEQESEAWSPAAQDPEKGERLGGARRGDVPNRKEEEPEEVPRAKGPRKAPVKESPEVLVERNPDPAISVAPARAQPPKNAAWDPTTGAQPPAPIPSMDAQAGQRRHVCTDCGRRFTYPSLLVSHRRMHSGERPFPCPECGMRFKRKFAVEAHQWIHRSCSGGRRGRRPGIRAVPRAPVRGDRDPPVLFRHYPDIFEECG | null | null | null | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; metal ion binding [GO:0046872] | PF01352;PF00096; | 6.10.140.140;3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: May be involved in transcriptional regulation. | Homo sapiens (Human) |
P0C828 | CA4A_CONST | MGMRMMFTVFLLVVLATTVVSTPSDRASDGRNAAVHERQKSLVPSVITTCCGYDPGTMCPPCRCTNSCG | null | null | null | extracellular region [GO:0005576] | acetylcholine receptor inhibitor activity [GO:0030550]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07365; | null | Conotoxin A superfamily | PTM: Contains 3 disulfide bonds. {ECO:0000305|PubMed:17115716}.; PTM: O-linked glycan consists of Hex3-HexNAc2 pentasaccharide. {ECO:0000269|PubMed:17115716, ECO:0000305|PubMed:9819194}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9819194}. | null | null | null | null | null | FUNCTION: Neurotoxin with probable activity on sodium channel (Probable). Induces intense repetitive firing of the frog neuromuscular junction, leading to a tetanic contracture in muscle fiber (spastic paralysis) (PubMed:17115716). In vivo, shows the same effect as the whole venom when injected on fish (PubMed:17115716... | Conus striatus (Striated cone) |
P0C829 | CA4B_CONST | MGMRMMFTVFLSVVLATTVVSTPSDRASDGRNAAVHERQKELVPSVITTCCGYDPGTMCPPCRCTNSCPTKPKKPGRRND | null | null | null | extracellular region [GO:0005576] | acetylcholine receptor inhibitor activity [GO:0030550]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07365; | null | Conotoxin A superfamily | PTM: Contains 3 disulfide bonds. {ECO:0000305|PubMed:17115716}.; PTM: O-linked glycan consists of Hex3-HexNAc2 pentasaccharide. {ECO:0000269|PubMed:17115716}. | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:14701840}. | null | null | null | null | null | FUNCTION: Neurotoxin with probable activity on sodium channel (Probable). Induces intense repetitive firing of the frog neuromuscular junction, leading to a tetanic contracture in muscle fiber (spastic paralysis) (PubMed:17115716). In vivo, shows the same effect as the whole venom when injected on fish prey (PubMed:171... | Conus striatus (Striated cone) |
P0C865 | MK07_RAT | MAEPLKEEDGEDGSGEPPGRVKAEPVHTAASVVAKNLALLKARSFDVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYGEFRSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVGAERVRAYIQSLPPRQPVPWETVYPGADRQA... | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | calcineurin-NFAT signaling cascade [GO:0033173]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cellular response to growth factor stimulus [GO:0071363]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to laminar fluid shear stress [GO:0071499]; cellular response to transforming grow... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; PML body [GO:0016605] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; mitogen-activated protein kinase binding [GO:0051019]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | PTM: Dually phosphorylated on Thr-219 and Tyr-221, which activates the enzyme. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, PML body {ECO:0000250}. Note=Translocates to the nucleus upon activation. {ECO:0000250}. | 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=2.7.11.24; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Plays a role in various cellular processes such as proliferation, differentiation and cell survival. The upstream activator of MAPK7 is the MAPK kinase MAP2K5. Upon activation, it translocates to the nucleus and phosphorylates various downstream targets including MEF2C. EGF activates MAPK7 through a Ras-indep... | Rattus norvegicus (Rat) |
P0C869 | PA24B_HUMAN | MAVAEVSRTCLLTVRVLQAHRLPSKDLVTPSDCYVTLWLPTACSHRLQTRTVKNSSSPVWNQSFHFRIHRQLKNVMELKVFDQDLVTGDDPVLSVLFDAGTLRAGEFRRESFSLSPQGEGRLEVEFRLQSLADRGEWLVSNGVLVARELSCLHVQLEETGDQKSSEHRVQLVVPGSCEGPQEASVGTGTFRFHCPACWEQELSIRLQDAPEEQLKAPLSALPSGQVVRLVFPTSQEPLMRVELKKEAGLRELAVRLGFGPCAEEQAFLSRRKQVVAAALRQALQLDGDLQEDEIPVVAIMATGGGIRAMTSLYGQLAGLK... | 3.1.1.4; 3.1.1.5 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; | arachidonic acid metabolic process [GO:0019369]; calcium-mediated signaling [GO:0019722]; glycerophospholipid catabolic process [GO:0046475]; inflammatory response [GO:0006954]; parturition [GO:0007567]; phosphatidylcholine acyl-chain remodeling [GO:0036151]; phosphatidylethanolamine acyl-chain remodeling [GO:0036152];... | cytosol [GO:0005829]; early endosome membrane [GO:0031901]; extracellular region [GO:0005576]; mitochondrial inner membrane [GO:0005743] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; calcium-dependent phospholipid binding [GO:0005544]; lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; phospholipase A1 activity [GO:0008970]; phospholipase A2 activity [GO:0004623] | PF00168;PF18695;PF01735; | 2.60.40.150;3.40.1090.10; | null | null | SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytosol {ECO:0000269|PubMed:16617059}. Mitochondrion membrane {ECO:0000269|PubMed:16617059}; Peripheral membrane protein. Early endosome membrane {ECO:0000269|PubMed:16617059}; Peripheral membrane protein. Note=Translocates to membrane vesicles in a calcium-dependent fashio... | CATALYTIC ACTIVITY: [Isoform 5]: 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:0000269|PubMed:10085124, E... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=The specific activity is 0.8 nmol/min/ug enzyme with 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine as substrate. The specific activity is 0.3 nmol/min/ug enzyme with 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosp... | null | null | null | FUNCTION: Calcium-dependent phospholipase A1 and A2 and lysophospholipase that may play a role in membrane phospholipid remodeling. {ECO:0000269|PubMed:10085124, ECO:0000269|PubMed:10358058, ECO:0000269|PubMed:16617059}.; FUNCTION: [Isoform 3]: Calcium-dependent phospholipase A2 and lysophospholipase. Cleaves the ester... | Homo sapiens (Human) |
P0C870 | JMJD7_HUMAN | MAEAALEAVRSELREFPAAARELCVPLAVPYLDKPPTPLHFYRDWVCPNRPCIIRNALQHWPALQKWSLPYFRATVGSTEVSVAVTPDGYADAVRGDRFMMPAERRLPLSFVLDVLEGRAQHPGVLYVQKQCSNLPSELPQLLPDLESHVPWASEALGKMPDAVNFWLGEAAAVTSLHKDHYENLYCVVSGEKHFLFHPPSDRPFIPYELYTPATYQLTEEGTFKVVDEEAMEKVPWIPLDPLAPDLARYPSYSQAQALRCTVRAGEMLYLPALWFHHVQQSQGCIAVNFWYDMEYDLKYSYFQLLDSLTKASGLD | 1.14.11.63; 3.4.-.- | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:29915238}; | protein hydroxylation [GO:0018126]; proteolysis [GO:0006508]; wybutosine biosynthetic process [GO:0031591] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; aminopeptidase activity [GO:0004177]; endopeptidase activity [GO:0004175]; histone H3K36 demethylase activity [GO:0051864]; metal ion binding [GO:0046872]; methylated histone binding [GO:0035064]; monooxygenase activity [GO:0004497]; peptidyl-lysine 3-dioxygen... | PF13621; | 2.60.120.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29915238}. Cytoplasm {ECO:0000269|PubMed:29915238}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-lysyl-[protein] + O2 = (3S)-3-hydroxy-L-lysyl-[protein] + CO2 + succinate; Xref=Rhea:RHEA:57152, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15133, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, ChEBI:CHEBI:141492; EC=1.14.11.63; Ev... | null | null | null | null | FUNCTION: Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monooxygenase (PubMed:28847961, PubMed:29915238). Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger trans... | Homo sapiens (Human) |
P0C871 | PA24B_MOUSE | MQAKVPETCLLTVRVLRASGLPSKDLVTSSDCYVTLNLPTASSHTLQTRTVKNSRNPVWNQNFHFRIHRQLKNVMELKVFDHDLVTRDDPVLSVLFDVGTLQIGTQRQSFSLGTQEKGCLEVEFRLQTLTDCEEQLISNGIVVARELSCLHVELKRTGDPKRSERKVQLVVAGACEGPQDASAGTGSFHFHYPACWEQELNVHLQDDPHEQLKVPLRTLPSSQLVRLVFPTSQEPLMRLELKKEEGPKELAVRLGCGPCPEEQAFLSKRKQVVAAALKKALQLDQDLHEDEIPVIAVMATGGGIRAMTSLYGQLAGLQEL... | 3.1.1.4; 3.1.1.5 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; | glycerophospholipid catabolic process [GO:0046475] | cytosol [GO:0005829]; early endosome membrane [GO:0031901]; mitochondrial membrane [GO:0031966] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; calcium-dependent phospholipid binding [GO:0005544]; lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; phospholipase A2 activity [GO:0004623] | PF00168;PF18695;PF01735; | 2.60.40.150;3.40.1090.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P0C869}. Mitochondrion membrane {ECO:0000250|UniProtKB:P0C869}; Peripheral membrane protein {ECO:0000250|UniProtKB:P0C869}. Early endosome membrane {ECO:0000250|UniProtKB:P0C869}; Peripheral membrane protein {ECO:0000250|UniProtKB:P0C869}. Note=Translocate... | 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:0000269|PubMed:20705608}; Physiological... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=The specific activity is 394 nmol/min/ug enzyme with 1-hexadecanoyl-sn-glycero-3-phosphocholine. The specific PLA2 activity is 11 nmol/min/ug enzyme with 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine (in the presence of cardiolipin... | null | null | null | FUNCTION: Calcium-dependent phospholipase A1 and A2 and lysophospholipase that may play a role in membrane phospholipid remodeling. Cleaves the ester bond of the fatty acyl group attached to the sn-1 or sn-2 position of phospholipids (phospholipase A1 and A2 activity, respectively), producing lysophospholipids that may... | Mus musculus (Mouse) |
P0C872 | JMJD7_MOUSE | MAEAALEAVRRALQEFPAAARDLNVPRVVPYLDEPPSPLCFYRDWVCPNRPCIIRNALQHWPALQKWSLSYLRATVGSTEVSVAVTPDGYADAVRGDRFVMPAERRLPISHVLDVLEGRAQHPGVLYVQKQCSNLPTELPQLLSDIESHVPWASESLGKMPDAVNFWLGDASAVTSLHKDHYENLYCVVSGEKHFLLHPPSDRPFIPYNLYTPATYQLTEEGTFRVVDEEAMEKVPWIPLDPLAPDLTQYPSYSQAQALHCTVRAGEMLYLPALWFHHVQQSHGCIAVNFWYDMEYDLKYSYFQLMDTLTRATGLD | 1.14.11.63; 3.4.-.- | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:P0C870}; | proteolysis [GO:0006508]; wybutosine biosynthetic process [GO:0031591] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; aminopeptidase activity [GO:0004177]; endopeptidase activity [GO:0004175]; histone H3K36 demethylase activity [GO:0051864]; metal ion binding [GO:0046872]; methylated histone binding [GO:0035064]; monooxygenase activity [GO:0004497]; peptidyl-lysine 3-dioxygen... | PF13621; | 2.60.120.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P0C870}. Cytoplasm {ECO:0000250|UniProtKB:P0C870}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-lysyl-[protein] + O2 = (3S)-3-hydroxy-L-lysyl-[protein] + CO2 + succinate; Xref=Rhea:RHEA:57152, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15133, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, ChEBI:CHEBI:141492; EC=1.14.11.63; Ev... | null | null | null | null | FUNCTION: Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monooxygenase (By similarity) (PubMed:28847961). Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transc... | Mus musculus (Mouse) |
P0C882 | GGGPS_METTM | MKVEDYFHDILGERKIHLTLIDPEEQTPEEAVEIAEAAIRGGTDGIMLGGSTTDSSELDATAGALRENIDVPIILFPGNTTGVSRHADAIFFMSLLNSNNPYWIIGAQALGAPAVKKMGIEALPMGYLVVEPGGTVGWVGDTKPVPRNKPDIAAAYAMAAEFLGMRLFYLEAGSGAPQHVPEEMISLVKRCTDQILIVGGGIRTGADAARVAGAGADIIVTGTVVENSSNVEDKIREIVEGMGSL | 2.5.1.41 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00112, ECO:0000269|PubMed:8408023, ECO:0000269|Ref.3}; | glycerophospholipid biosynthetic process [GO:0046474] | cytoplasm [GO:0005737] | imidazoleglycerol-phosphate synthase activity [GO:0000107]; magnesium ion binding [GO:0000287]; phosphoglycerol geranylgeranyltransferase activity [GO:0047294] | PF01884; | 3.20.20.390; | GGGP/HepGP synthase family, Group II subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00112, ECO:0000269|PubMed:8408023}. | CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + sn-glycerol 1-phosphate = diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate; Xref=Rhea:RHEA:23404, ChEBI:CHEBI:33019, ChEBI:CHEBI:57677, ChEBI:CHEBI:57685, ChEBI:CHEBI:58756; EC=2.5.1.41; Evidence={ECO:0000255|HAMAP-Rule:MF_00112, ECO:0000269... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13.5 uM for G1P (at 55 degrees Celsius and pH 8) {ECO:0000269|PubMed:11732904}; KM=506 nM for GGPP (at 55 degrees Celsius and pH 8) {ECO:0000269|PubMed:11732904}; Vmax=4 umol/min/mg enzyme (at 55 degrees Celsius and pH 8) {ECO:0000269|PubMed:11732904}; | PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism. {ECO:0000255|HAMAP-Rule:MF_00112}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-9.0. {ECO:0000269|PubMed:11732904}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius at pH 8.0. {ECO:0000269|PubMed:11732904}; | FUNCTION: Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids. Cannot use sn-glycerol-3-phosphate (G3P) or... | Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum) |
P0C8E4 | M3K7_RAT | MSTASAASSSSSSSASEMIEAPSQVLNFEEIDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFPGADEPLQYPCQYSDEGQSNSATSTGSFM... | 2.7.11.25 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O43318}; | angiogenesis [GO:0001525]; anoikis [GO:0043276]; apoptotic signaling pathway [GO:0097190]; bone development [GO:0060348]; canonical NF-kappaB signal transduction [GO:0007249]; cellular response to angiotensin [GO:1904385]; cellular response to hypoxia [GO:0071456]; cellular response to transforming growth factor beta s... | ATAC complex [GO:0140672]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069] | ATP binding [GO:0005524]; DNA-binding transcription factor binding [GO:0140297]; histone kinase activity [GO:0035173]; identical protein binding [GO:0042802]; linear polyubiquitin binding [GO:1990450]; magnesium ion binding [GO:0000287]; MAP kinase activity [GO:0004707]; MAP kinase kinase activity [GO:0004708]; MAP kin... | PF07714; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily | PTM: Association with TAB1/MAP3K7IP1 promotes autophosphorylation at Ser-192 and subsequent activation. Association with TAB2/MAP3K7IP2, itself associated with free unanchored Lys-63 polyubiquitin chain, promotes autophosphorylation and subsequent activation of MAP3K7. Dephosphorylation at Ser-192 by PPM1B/PP2CB and at... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Although the majority of MAP3K7/TAK1 is found in the cytosol, when complexed with TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2, it is also localized at the cell membrane. {ECO... | 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=2.7.11.25; Evidence={ECO:0000250|UniProtKB:O43318}; CATALYT... | null | null | null | null | FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signal transduction of TRAF6, various cytokines including interleukin-1 (IL-1), transforming ... | Rattus norvegicus (Rat) |
P0C8E7 | EVA1_RHISA | MTFKACIAIITALCAMQVICEDDEDYGDLGGCPFLVAENKTGYPTIVACKQDCNGTTETAPNGTRCFSIGDEGLRRMTANLPYDCPLGQCSNGDCIPKETYEVCYRRNWRDKKN | null | null | negative regulation of chemokine activity [GO:1900137] | extracellular region [GO:0005576] | C-C chemokine binding [GO:0019957]; chemokine binding [GO:0019956] | PF19429; | 2.30.130.100; | Evasin C8 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Salivary chemokine-binding protein which shows chemokine neutralizing activity and binds to host chemokines CCL3, CCL4 and CCL18 (PubMed:17640866, PubMed:18678732, PubMed:20041127, PubMed:25266725). Binds to CCL3 with 1:1 stoichiometry (PubMed:20041127). {ECO:0000269|PubMed:17640866, ECO:0000269|PubMed:186787... | Rhipicephalus sanguineus (Brown dog tick) (Ixodes sanguineus) |
P0C8E9 | EVA4_RHISA | MAFKYWFVFAAVLYARQWLSTKCEVPQMTSSSAPDLEEEDDYTAYAPLTCYFTNSTLGLLAPPNCSVLCNSTTTWFNETSPNNASCLLTVDFLTQDAILQENQPYNCSVGHCDNGTCAGPPRHAQCW | null | null | negative regulation of chemokine activity [GO:1900137] | extracellular region [GO:0005576] | C-C chemokine binding [GO:0019957] | PF19429; | 2.30.130.100; | Evasin C8 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Salivary chemokine-binding protein which has chemokine-neutralizing activity and binds to host chemokines CCL1, CCL3, CCL5, CCL7, CCL8, CCL11, CCL14, CCL15, CCL16, CCL17, CCL18, CCL19, CCL21, CCL22, CCL23, CCL24, CCL25 and CCL26 with nanomolar affinity (PubMed:18678732, PubMed:23910450, PubMed:25266725). Bind... | Rhipicephalus sanguineus (Brown dog tick) (Ixodes sanguineus) |
P0C8G6 | PV21_POMCA | MSQLRWWVVSQLLLLIVVCILDHSEGARVCPKIVPGLDKLRVGVDITKLDLLPLFDLGDNGFRSAVADYTCDRGQTTVVDGESFDVPDQVDSVVIESSGQQTSSVTTIKSESQISQALSISAGISVDTAKAGFSSSASYAEMQEAITKYGRTVSQMSAVYTTCSANLSPNLLLGQNPLQTLSRLPSDFTADTEGYYDFIKTYGTHYFNKGKLGGMFLFTSETDMSYFQNKNSQQVEANIKATFASILSTETGGSSDQSKEVIEFKESSLITAKFFGGRTNLAADGLTKWQPTIAKLPYFMSGTLSTISSLIADTTKRASM... | null | null | complement activation [GO:0006956] | extracellular space [GO:0005615]; membrane attack complex [GO:0005579]; other organism cell membrane [GO:0044218] | nutrient reservoir activity [GO:0045735]; toxin activity [GO:0090729] | PF01823; | null | null | PTM: Glycosylated. Contains four O-linked and one N-linked oligosaccharide bonds. The protein contains 2.5% of carbohydrates (high levels of mannose, galactose, and NAcGlucosamine, and small amounts of NacGalactosamine). {ECO:0000269|PubMed:15112330}.; PTM: PV2 is a very high density lipoprotein (VHDL). It contains 3.7... | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Target cell membrane {ECO:0000269|PubMed:23737950}. | null | null | null | null | null | FUNCTION: The egg defensive protein perivitellin-2 is a pore-forming two-subunit glycoprotein that affects both the nervous and digestive systems of mammals (PubMed:18640143, PubMed:23737950). In addition, it is a source of both structural and energetic molecules during embryonic development (Probable). The tachylectin... | Pomacea canaliculata (Golden apple snail) |
P0C8G7 | PV22_POMCA | MVKKIHFIMERHASIVAFLLAVLALTESQAFTSVKLPRDEHWPYNYVSIGPAGVWAVNRQNKLFYRTGTYGDNANMGSGWQFKQDGVGQVDVGKDKVGYINLSGGSLFRIDGISQGNPVGGSPKSWEWWTKYIGMSLREDTRFSSRIENQNKVLTFTFRTCFWASRITNWCFADSSYTETVTAGGSGTWITKSQLKYKSGTFGNPDTEGGDWITVDSGSFQHVSSGSGVVLAVRSNGELVKRTGITCSLPQGSGWTSMLNGMSRVDTYGTVAWAVDTYGDLYFINL | null | null | autophagosome maturation [GO:0097352] | autophagosome membrane [GO:0000421]; extracellular region [GO:0005576]; lysosomal membrane [GO:0005765]; other organism cell membrane [GO:0044218] | carbohydrate binding [GO:0030246]; nutrient reservoir activity [GO:0045735]; phosphatidylinositol-3-phosphate binding [GO:0032266]; toxin activity [GO:0090729] | PF19193; | null | Tectonin family | PTM: Glycosylated. PV2 contains four O-linked and one N-linked oligosaccharide bonds. The protein contains 2.5% of carbohydrates (high levels of mannose, galactose, and NAcGlucosamine, and small amounts of NacGalactosamine). {ECO:0000269|PubMed:15112330}.; PTM: PV2 is a very high density lipoprotein (VHDL). It contains... | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Target cell membrane {ECO:0000269|PubMed:23737950}. | null | null | null | null | null | FUNCTION: The egg defensive protein perivitellin-2 is a pore-forming two-subunit glycoprotein that affects both the nervous and digestive systems of mammals (PubMed:18640143, PubMed:23737950). In addition, it is a source of both structural and energetic molecules during embryonic development (Probable). The tachylectin... | Pomacea canaliculata (Golden apple snail) |
P0C8M1 | PA2B1_BOTMO | DLWQFNKMIKKEVGKLPFPFYGAYGCYCGWGGRGEKPKDGTDRCCFVHDCCYKKLTGCPKWDDRYSYSWKDITIVCGEDLPCEEICECDRAAAVCFYENLGTYNKKYMKHLKPCKKADYPC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:18501940}; Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:18501940}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18501940}. | 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:0... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:18501940}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35-45 degrees Celsius. {ECO:0000269|PubMed:18501940}; | FUNCTION: Snake venom phospholipase A2 (PLA2) that shows enzymatic activity in the presence of a synthetic substrate. In vitro, blocks the neuromuscular transmission in young chick biventer cervicis preparations. In mice, induces myonecrosis and a systemic interleukin-6 response upon intramuscular injection. Also induc... | Bothrops moojeni (Lance-headed viper) (Caissaca) |
P0C8P8 | THCL_STRAJ | MDATAIHERWSVMSNASIGQEIGVEGLTGLDVDALEISDYVDETLLDGEDLTVTMIASASCTTCICTCSCSS | null | null | defense response to bacterium [GO:0042742] | extracellular region [GO:0005576] | null | null | null | Thiocillin family | PTM: Maturation of thiazole and oxazole containing antibiotics involves the enzymatic condensation of a Cys, Ser or Thr with the alpha-carbonyl of the preceding amino acid to form a thioether or ether bond, then dehydration to form a double bond with the alpha-amino nitrogen. Thiazoline or oxazoline ring are dehydrogen... | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Has bacteriocidal activity. Inhibits bacterial protein biosynthesis by acting on the elongation factor Tu (EF-Tu) (By similarity). {ECO:0000250}. | Streptomyces azureus |
P0C8P9 | THCL_STRSQ | MGNNEEYFIDVNDLSIDVFDVVEQGGAVTALTADHGMPEVGASTNCFCYICCSCSSN | null | null | defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640]; negative regulation of translation [GO:0017148] | extracellular region [GO:0005576] | translation repressor activity [GO:0030371] | PF19409; | null | Thiocillin family | PTM: Maturation of thiazole and oxazole containing antibiotics involves the enzymatic condensation of a Cys, Ser or Thr with the alpha-carbonyl of the preceding amino acid to form a thioether or ether bond, then dehydration to form a double bond with the alpha-amino nitrogen. Thiazoline or oxazoline ring are dehydrogen... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7592021}. | null | null | null | null | null | FUNCTION: Has bacteriocidal activity against both aerobic and anaerobic Gram-positive bacteria. Inhibits growth of B.subtilis (MIC=0.047 ug/ml) and methicillin-resistant S.aureus (MRSA) (MIC=0.047 ug/ml). Has poor activity against Gram-negative bacteria, with the exception of B.fragilis. Inhibits bacterial protein bios... | Streptomyces sp |
P0C942 | PA2B1_LACMU | HLLKFNKMIKFETRKNAIPFYAFYGCYCGWGGRXXXXXXXXXCCFVHDCCYGKXXXXXXXWDLYRYSLKSGYLTCGKGTWCEEQICECDRVAAECLRRSLSTYKYGYMFYPDSRCRGPSETC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:16005152}; Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:16005152}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | 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:0... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:16005152}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35-45 degrees Celsius. {ECO:0000269|PubMed:16005152}; | FUNCTION: Snake venom phospholipase A2 (PLA2) that displays neurotoxic and myotoxic activities. Induces inflammatory edema by mechanisms involving mast cell activation and arachidonic acid metabolites. Increases plasma creatine kinase activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-s... | Lachesis muta muta (Bushmaster) |
P0C9E0 | TPRT_ASFP4 | MLHLIYISIIVVLIIILISYTRKPKYFRITAPRSVALFHGIHPLKPKNYKTFSEEFETILNNAIEDGDFKGQLTEPCSYALRGGKYIRPIILMEIVRACQLQHSFGAPIYPAEAALAVEYFHVASLIIDDMPSFDNDVKRRNKDTVWARFGVAKAQMSALALTMQGFQNICRQIDWIKEHCPRFPDPNQLGALLCTFVSHSLNSAGSGQLVDTPEKTIPFFKIAFIMGWVLGTGTIEDIGMIERAAHCFGNAFQLADDIKDHDTDTGWNYAKIHGKRKTFDDVAQSLQECKKILHGKKIYTSIWNEIFQKVINVALGT | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250}; | farnesyl diphosphate biosynthetic process [GO:0045337]; geranyl diphosphate biosynthetic process [GO:0033384]; geranylgeranyl diphosphate biosynthetic process [GO:0033386] | host cell endoplasmic reticulum [GO:0044165]; host cell membrane [GO:0033644]; membrane [GO:0016020] | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranylfarnesyl diphosphate synthase activity [GO:0044687]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family, Asfivirus trans-prenyltransferase subfamily | null | SUBCELLULAR LOCATION: Host endoplasmic reticulum. Host membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,... | null | PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWA... | null | null | FUNCTION: Trans-prenyltransferase that catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with different allylic diphosphates, such as dimethylallyl diphosphate (DMAPP), geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylgeranyl diphosphate (GGPP), farnesyl diphosphate being the best a... | African swine fever virus (isolate Tick/South Africa/Pretoriuskop Pr4/1996) (ASFV) |
P0C9E1 | TPRT_ASFWA | MLHLIYISIIVVLIIILISYTRKPKYFRITAPRSVALFHGIHPLNPKNYKTFSEEFETILNNAIEDGDFKGQLTEPCSYALRGGKYIRPIILMEIVRACQLQHSFGAPIYPAEAALAVEYFHVASLIIDDMPSFDNDVKRRNKDTVWARFGVAKAQMSALALTMQGFQNICRQIDWIKEHCPRFPDPNQLGALLCTFVSHSLNSAGSGQLVDTPEKTIPFFKIAFIMGWVLGTGSVEDIGMIERAAHCFGNAFQLADDIKDHDTDTGWNYAKIHGKRKTFDDVAQFLQECKKILHGKKIYTSIWNEIFQKVINVALGT | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250}; | farnesyl diphosphate biosynthetic process [GO:0045337]; geranyl diphosphate biosynthetic process [GO:0033384]; geranylgeranyl diphosphate biosynthetic process [GO:0033386] | host cell endoplasmic reticulum [GO:0044165]; host cell membrane [GO:0033644]; membrane [GO:0016020] | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranylfarnesyl diphosphate synthase activity [GO:0044687]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family, Asfivirus trans-prenyltransferase subfamily | null | SUBCELLULAR LOCATION: Host endoplasmic reticulum. Host membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,... | null | PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWA... | null | null | FUNCTION: Trans-prenyltransferase that catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with different allylic diphosphates, such as dimethylallyl diphosphate (DMAPP), geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylgeranyl diphosphate (GGPP), farnesyl diphosphate being the best a... | African swine fever virus (isolate Warthog/Namibia/Wart80/1980) (ASFV) |
P0C9E2 | TPRT_ASFK5 | MLHLIYISIIVVLIIILISYTRKPQYFRITAPRSVALFHGIHPLNPKNYKTFSEEFETILNNAIEDGDFKGQLTEPCSYALRGGKYIRPIILMEIVRACQLQHSFGAPIYPAEAALAVEYFHVASLIIDDMPSFDNDVKRRNKDTVWARFGVAKAQMSALALTMQGFQNICRQVDWIKENCPRFPDPNQLGALLCTFVSHSLNSAGSGQLVDTPEKTIPFFKIAFIMGWVLGTGTIEDIGAIERAAHCFGNAFQLADDIKDHDTDTGRNYAKIHGKRKTFDVVAQSLQECKKILHEKKIYTSIWNEIFQKVINVALGT | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250}; | farnesyl diphosphate biosynthetic process [GO:0045337]; geranyl diphosphate biosynthetic process [GO:0033384]; geranylgeranyl diphosphate biosynthetic process [GO:0033386] | host cell endoplasmic reticulum [GO:0044165]; host cell membrane [GO:0033644]; membrane [GO:0016020] | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranylfarnesyl diphosphate synthase activity [GO:0044687]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family, Asfivirus trans-prenyltransferase subfamily | null | SUBCELLULAR LOCATION: Host endoplasmic reticulum. Host membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,... | null | PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWA... | null | null | FUNCTION: Trans-prenyltransferase that catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with different allylic diphosphates, such as dimethylallyl diphosphate (DMAPP), geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylgeranyl diphosphate (GGPP), farnesyl diphosphate being the best a... | African swine fever virus (isolate Pig/Kenya/KEN-50/1950) (ASFV) |
P0CAP1 | MYZAP_HUMAN | MLRSTSTVTLLSGGAARTPGAPSRRANVCRLRLTVPPESPVPEQCEKKIERKEQLLDLSNGEPTRKLPQGVVYGVVRRSDQNQQKEMVVYGWSTSQLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQKTLVDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQL... | null | null | intracellular signal transduction [GO:0035556]; maintenance of ER location [GO:0051685] | anchoring junction [GO:0070161]; cortical actin cytoskeleton [GO:0030864]; cytoplasmic side of plasma membrane [GO:0009898]; I band [GO:0031674]; nuclear envelope [GO:0005635]; RNA polymerase II, holoenzyme [GO:0016591]; Z disc [GO:0030018] | null | null | null | MYZAP family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q5EB94}. Cell membrane {ECO:0000250|UniProtKB:Q5EB94}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5EB94}; Cytoplasmic side {ECO:0000250|UniProtKB:Q5EB94}. Cytoplasm, myofibril, sarcomere, I band {ECO:0000250|UniProtKB:Q5EB94}. Cytoplasm, myof... | null | null | null | null | null | FUNCTION: Plays a role in cellular signaling via Rho-related GTP-binding proteins and subsequent activation of transcription factor SRF (By similarity). Targets TJP1 to cell junctions. In cortical neurons, may play a role in glutaminergic signal transduction through interaction with the NMDA receptor subunit GRIN1 (By ... | Homo sapiens (Human) |
P0CAP2 | GRL1A_HUMAN | MCSLPRGFEPQAPEDLAQRSLVELREMLKRQERLLRNEKFICKLPDKGKKIFDSFAKLKAAIAECEEVRRKSELFNPVSLDCKLRQKAIAEVDVGTDKAQNSDPILDTSSLVPGCSSVDNIKSSQTSQNQGLGRPTLEGDEETSEVEYTVNKGPASSNRDRVPPSSEASEHHPRHRVSSQAEDTSSSFDNLFIDRLQRITIADQGEQQSEENASTKNLTGLSSGTEKKPHYMEVLEMRAKNPVPQLRKFKTNVLPFRQNDSSSHCQKSGSPISSEERRRRDKQHLDDITAARLLPLHHMPTQLLSIEESLALQKQQKQNY... | null | null | intracellular signal transduction [GO:0035556]; maintenance of ER location [GO:0051685]; transcription elongation by RNA polymerase II [GO:0006368] | I band [GO:0031674]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635]; RNA polymerase II, core complex [GO:0005665]; RNA polymerase II, holoenzyme [GO:0016591]; transcription preinitiation complex [GO:0097550] | RNA polymerase II complex binding [GO:0000993]; transcription elongation factor activity [GO:0003711] | PF15328; | null | GRINL1 family | null | SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: [Isoform 1]: Appears to be a stable component of the Pol II(G) complex form of RNA polymerase II (Pol II). Pol II synthesizes mRNA precursors and many functional non-coding RNAs and is the central component of the basal RNA polymerase II transcription machinery. May play a role in the Mediator complex-depende... | Homo sapiens (Human) |
P0CAR9 | PA2A1_CERCE | MRTLWIVAVWLMGVEGNLYQFGKMIKHKTGKSALLSYSAYGCYCGWGGQGKPQDATDHCCFVHDCCYGEVSGCYPKTAFTLKFENQDIICGDEDPCNRAVCECDRVAAICFGENVNTSDKKYLFYSSSYCEEESEQC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|Ref.2}; Note=Binds 1 Ca(2+) ion. {ECO:0000269|Ref.2}; | angiogenesis [GO:0001525]; arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | PTM: Glycosylated (2.5%). | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}. | 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:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits blood coagulation and platelet aggregation induced by ADP and arachidonic acid. Inhibits tumor cell adhesion and migration in a dose-dependent manner. Abolishes the attachment of human brain microvascular endothelial cells (HBMEC) to fibrinogen (IC(50)=0.12 uM... | Cerastes cerastes (Horned desert viper) |
P0CAS0 | PA2A2_CERCE | MRTLWIVAVWLMGVEGNLFQFGKMIKHKTGKSALLSYSGNPCYCGWGGQGPPQDATDHCCFVHDCCYGEENACYPKTAFTLKFENQIIICDEDPCNYAVCMCDRVAAICGGENVATSDAKYLFYRSMGCEEESVQC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|Ref.2}; Note=Binds 1 Ca(2+) ion. {ECO:0000269|Ref.2}; | angiogenesis [GO:0001525]; arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | PTM: Glycosylated (2.5%). | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}. | 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:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 that inhibits blood coagulation and platelet aggregation induced by ADP and arachidonic acid. Inhibits tumor cell adhesion and migration in a dose-dependent manner. Abolishes the attachment of human brain microvascular endothelial cells (HBMEC) to fibrinogen (IC(50)=0.2 uM) and dr... | Cerastes cerastes (Horned desert viper) |
P0CAS2 | PA2B6_CRODO | HLLQFNKMIKFETRRNAIPPYAFYGCYCGWGGRGRPKDATDRCCFVHDCCYGKLAKCNTKWDFYRYSLKSGYITCGKGTWCEEQICECDRVAAECLRRSLSTYRYGYMIYPDSRCRGPSETC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | 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:0... | null | null | null | null | FUNCTION: Heterodimer CA-CB: Crotoxin is a potent presynaptic neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission (PubMed:16003952, PubMed:17203389). It consists of a non-covalent association of a basic and weakly toxic PLA2 subunit (CB), with a s... | Crotalus durissus collilineatus (Brazilian rattlesnake) |
P0CAS5 | PA2BE_CRODU | HLLQFNKMIKFETRKNAVPFYAFYGCYCGWGGQRRPKDATDRCCFVHDCCYGKLTKCNTKWDIYRYSLKSGYITCGKGTWCKEQICECDRVAAECLRRSLSTYKNEYMFYPKSRCRRPSETC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12875878}; Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:12875878}; | arachidonic acid secretion [GO:0050482]; defense response to bacterium [GO:0042742]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | 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:0... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=38.5 mM for 4-nitro-3-(octanoyloxy)benzoic acid {ECO:0000269|PubMed:12875878}; Vmax=8.5 nmol/min/mg enzyme {ECO:0000269|PubMed:12875878}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:12875878}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 18 degrees Celsius. {ECO:0000269|PubMed:12875878}; | FUNCTION: Snake venom phospholipase A2 (PLA2) that shows moderate neurotoxic activity in isolated mouse phrenic nerve diaphragm but shows high neurotoxic activity in a chick biventer cervis preparation. Also shows a high bactericidal effect against both Gram-negative and Gram-positive bacteria. PLA2 catalyzes the calci... | Crotalus durissus terrificus (South American rattlesnake) |
P0CAS7 | PA2BG_CRODU | HLLQFNKMLKFETRKNAVPFYAFGCYCGWGGQRRPKDATDRCCFVHDCCYEKVTKCNTKWDFYRYSLKSGYITCGKGTWCKEQICECDRVAAECLRRSLSTYKNEYMFYPDSRCREPSETC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12018617}; Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:12018617}; | arachidonic acid secretion [GO:0050482]; defense response to bacterium [GO:0042742]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | 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:0... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=31.2 mM for 4-nitro-3-(octanoyloxy)benzoic acid {ECO:0000269|PubMed:12018617}; Vmax=8.2 nmol/min/mg enzyme {ECO:0000269|PubMed:12018617}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.9. {ECO:0000269|PubMed:12018617}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 10-30 degrees Celsius. {ECO:0000269|PubMed:12018617}; | FUNCTION: Snake venom phospholipase A2 (PLA2) that has anticoagulant activity and inhibits bactericial growth of the Gram-negative bacteria Xanthomonas axonopodis pv. passiflorae (in monomeric form). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:1201... | Crotalus durissus terrificus (South American rattlesnake) |
P0CAW2 | CCRM_CAUVC | MKFGPETIIHGDCIEQMNALPEKSVDLIFADPPYNLQLGGDLLRPDNSKVDAVDDHWDQFESFAAYDKFTREWLKAARRVLKDDGAIWVIGSYHNIFRVGVAVQDLGFWILNDIVWRKSNPMPNFKGTRFANAHETLIWASKSQNAKRYTFNYDALKMANDEVQMRSDWTIPLCTGEERIKGADGQKAHPTQKPEALLYRVILSTTKPGDVILDPFFGVGTTGAAAKRLGRKFIGIEREAEYLEHAKARIAKVVPIAPEDLDVMGSKRAEPRVPFGTIVEAGLLSPGDTLYCSKGTHVAKVRPDGSITVGDLSGSIHKIG... | 2.1.1.72 | null | DNA replication [GO:0006260]; macromolecule modification [GO:0043412]; methylation [GO:0032259] | cytoplasm [GO:0005737] | DNA binding [GO:0003677]; N-methyltransferase activity [GO:0008170]; site-specific DNA-methyltransferase (adenine-specific) activity [GO:0009007] | PF01555;PF18755; | 3.40.50.150; | N(4)/N(6)-methyltransferase family | PTM: Rapidly degraded by Lon protease prior to cell division. {ECO:0000250|UniProtKB:B8GZ33}. | null | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90615, ChEBI:CHEBI:90616;... | null | null | null | null | FUNCTION: A beta subtype methylase that recognizes the double-stranded sequence 5'-GANTC-3' and methylates non-modifed A-2 on the hemimethylated, post-replicative DNA (Probable) (PubMed:12654995) (By similarity). Opens a bubble in the DNA at the recognition site, allowing precise recognition of the sequence and ensurin... | Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus) |
P0CAX5 | OPHN1_RAT | MGHPPLEFSDCYLDSPDFRERLKCYEQELERTNKFIKDVIKDGSALISAMRSYSSAVQKFSQTLQSFQFDFIGDTLTDDEINIAESFKEFAELLNEVENERMMMVQNASDLLIKPLETFRKEQIGFTKERKKKFEKDGERFYSLLDRHLHLSSKKKESQLLEADLQVDKERHNFFESSLDYVYQIQEVQESKKFNIVEPVLAFLHSLFISNSLTVELTQDFLPYKQQLQLSLQNTRNHFSSTREEMEELKKRMKEAPQTCKLPGQPTIEGYLYTQEKWALGISWVKYYCRYEKETRTLTMTPTEQKPGAKQGPVDLTLKY... | null | null | actin cytoskeleton organization [GO:0030036]; cell junction assembly [GO:0034329]; cell morphogenesis involved in neuron differentiation [GO:0048667]; cerebellar granule cell differentiation [GO:0021707]; cerebral cortex neuron differentiation [GO:0021895]; establishment of epithelial cell apical/basal polarity [GO:004... | actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; presynapse [GO:0098793]; terminal bouton [GO:0043195] | actin binding [GO:0003779]; GTPase activator activity [GO:0005096]; ionotropic glutamate receptor binding [GO:0035255]; phospholipid binding [GO:0005543] | PF16746;PF00169;PF00620; | 1.20.1270.60;2.30.29.30;1.10.555.10; | null | null | SUBCELLULAR LOCATION: Postsynapse {ECO:0000269|PubMed:15034583, ECO:0000269|PubMed:19487570}. Presynapse {ECO:0000269|PubMed:15034583, ECO:0000305|PubMed:19481455}. Cell projection, axon {ECO:0000269|PubMed:15034583}. Cell projection, dendritic spine {ECO:0000269|PubMed:15034583}. Cell projection, dendrite {ECO:0000250... | null | null | null | null | null | FUNCTION: Stimulates GTP hydrolysis of members of the Rho family. Its action on RHOA activity and signaling is implicated in growth and stabilization of dendritic spines, and therefore in synaptic function, in hippocampal neurons. Critical for the stabilization of AMPA receptors at postsynaptic sites. Critical for the ... | Rattus norvegicus (Rat) |
P0CAX7 | MP83_MYCBO | MINVQAKPAAAASLAAIAIAFLAGCSSTKPVSQDTSPKPATSPAAPVTTAAMADPAADLIGRGCAQYAAQNPTGPGSVAGMAQDPVATAASNNPMLSTLTSALSGKLNPDVNLVDTLNGGEYTVFAPTNAAFDKLPAATIDQLKTDAKLLSSILTYHVIAGQASPSRIDGTHQTLQGADLTVIGARDDLMVNNAGLVCGGVHTANATVYMIDTVLMPPAQ | null | null | cell adhesion [GO:0007155]; extracellular matrix organization [GO:0030198] | extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | cell adhesion molecule binding [GO:0050839] | PF02469; | 2.30.180.10; | null | PTM: O-glycosylated. Contains 0-3 mannose residues attached to residues 48-49 in various configurations; the dominant glycoform is Thr-48(Man)/Thr-49(Man2) with an unusual Man(1->3)Man linkage, but Thr48(Man3)/Thr49(Man0) through to Thr48(Man0/)Thr49(Man3) are also seen (PubMed:12517764). {ECO:0000269|PubMed:12517764}.... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Secreted, cell wall {ECO:0000250|UniProtKB:P9WNF3}. Secreted {ECO:0000269|PubMed:12517764, ECO:0000269|PubMed:20800577}. | null | null | null | null | null | FUNCTION: Induces expression of human (host) matrix metalloproteinase-9 (MMP9) in a TLR1/TLR2-dependent fashion; the acylated 20 first mature residues (residues 25-40) induce the most expression, but whole recombinant protein (non-acylated and non-glycosylated), and mannosylated but not acylated protein (residues 26-22... | Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) |
P0CAZ0 | TTL3B_TETTS | MFSIDIQGKSMSLCDPTSKIKQMQQQQQQLQQGTNNGIQKDQQLPNMIINGNSNSYLNNGSNLQQQAVIQQSNHKQSQIKYNSPLSHQQHHQFKIGHQNKLEYLRQQQAQKYNQIYQLDPQLQQQNQMFQQHQYMQNVQMQQQLLYQGNQEVFPPFNQIANGSAQNSILLQQYLSNNKGQTNNSNRENGGNFHSEQSPKSAAGSVVSGNGSNTQFAANILRNSNIIQQQNEFRFQQIQQTHQLLHSLVQQQPQPLSQQHSNQSSQSSNPQSQSPLPLSISSQQPVISMANYFNQPSQQSNSLFNGQQPTMFNSSENFQQK... | 6.3.2.- | null | axoneme assembly [GO:0035082]; cilium assembly [GO:0060271]; cilium movement [GO:0003341]; protein polyglycylation [GO:0018094] | axoneme [GO:0005930]; cilium [GO:0005929]; microtubule cytoskeleton [GO:0015630] | ATP binding [GO:0005524]; protein-glycine ligase activity [GO:0070735]; protein-glycine ligase activity, elongating [GO:0070737]; protein-glycine ligase activity, initiating [GO:0070736] | PF03133; | 3.30.470.20; | null | null | SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:19531357}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:19531357}. Note=Mainly present in oral cilia. | null | null | null | null | null | FUNCTION: Polyglycylase which modifies tubulin, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of tubulin. Polyglycylates tubulin, with a preference for alpha-tubulin toward beta-tubulin. {ECO:0000269|PubMed:19531357}. | Tetrahymena thermophila (strain SB210) |
P0CB14 | VM1K_CALRH | MIEVLLVTICLAAFPYQGSSIILESGNVNDYEVVYPRKITALSEGAAQQKYEDTMQYEFKVNGEPVVLHLEKNKELFAKDYSETHYSPDGTRITTYPSVEDHCYYQGRIHNDADSTASISTCNGLKGHFKFHGERYFIEPLKLPGSEAHAVYKYENIEKEDETPKMCGVIQKWKSDELIKKPFRLNLTPQQQESPQAKVYLVIVADKSMVDKHNGNIKKIEEQGHQMVNTMNECYRPMGIIIIMAGIECWTTNDFFEVKSSAKETLYSFAKWRVEDLSKRKPHNDAQFLTNKDFDGNTVGLAFVGGICNEKYCAGVVQDH... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | proteolysis [GO:0006508]; suppression of platelet aggregation in another organism [GO:0035893] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; peptidase activity [GO:0008233]; toxin activity [GO:0090729] | PF01562;PF01421; | 3.40.390.10; | Venom metalloproteinase (M12B) family, P-I subfamily | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Snake venom zinc metalloprotease that inhibits platelet aggregation by binding specifically to platelet glycoprotein VI (GP6) and platelet glycoprotein Ib alpha (GP1BA). It inhibits the interaction between collagen and platelet GP6 by cleaving GP6 (at '225-Glu-|-Ala-226' and '238-Val-|-Phe-239' bonds), and in... | Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma) |
P0CB20 | CONII_CONST | MAMNMSMTLCMFVMVVVAATVIDSTQLQEPDLSRMRRSGPADCCRMKECCTDRVNECLQRYSGREDKFVSFCYQEATVTCGSFNEIVGCCYGYQMCMIRVVKPNSLSGAHEACKTVSCGNPCA | null | null | null | extracellular region [GO:0005576]; host cell postsynaptic membrane [GO:0035792] | identical protein binding [GO:0042802]; ion channel regulator activity [GO:0099106]; toxin activity [GO:0090729] | null | 1.20.120.1800; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19481459}. | null | null | null | null | null | FUNCTION: Potently and selectively blocks the desensitization of ionotropic glutamate AMPA receptors (GRIA1, GRIA2, GRIA3 and GRIA4) (PubMed:19481459, PubMed:35377397). Binds to a different site than does the drug cyclothiazide (PubMed:19481459). The toxin acts like a straitjacket on the 'gating ring' of the ligand-bin... | Conus striatus (Striated cone) |
P0CB22 | ATX2_ARATH | MISMSCVPKEEEGEDTQIKTELHDHAADNPVRYASLESVYSVSSSSSSLCCKTAAGSHKKVNALKLPMSDSFELQPHRRPEIVHVYCRRKRRRRRRRESFLELAILQNEGVERDDRIVKIESAELDDEKEEENKKKKQKKRRIGNGELMKLGVDSTTLSVSATPPLRGCRIKAVCSGNKQDGSSRSKRNTVKNQEKVVTASATAKKWVRLSYDGVDPKHFIGLQCKVFWPLDAVWYPGSIVGYNVETKHHIVKYGDGDGEELALRREKIKFLISRDDMELLNMKFGTNDVVVDGQDYDELVILAASFEECQDFEPRDIIW... | 2.1.1.- | null | epigenetic regulation of gene expression [GO:0040029]; methylation [GO:0032259]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; vegetative to reproductive phase transition of meristem [GO:0010228] | chromatin [GO:0000785]; Set1C/COMPASS complex [GO:0048188] | histone H3K4 dimethyltransferase activity [GO:0140946]; histone H3K4 methyltransferase activity [GO:0042800]; metal ion binding [GO:0046872] | PF05965;PF05964;PF00855;PF00856;PF13832; | 2.30.30.140;3.30.160.360;2.170.270.10;3.30.40.10; | Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, TRX/MLL subfamily | PTM: Activated via O-glycosylation. {ECO:0000250|UniProtKB:Q9C5X4}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. | CATALYTIC ACTIVITY: Reaction=N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:21696, Rhea:RHEA-COMP:9846, Rhea:RHEA-COMP:15914, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; ... | null | null | null | null | FUNCTION: Histone methyltransferase (PubMed:18375658). Dimethylates 'Lys-4' of histone H3 (H3K4me2) (PubMed:18375658, PubMed:24102415). H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation (PubMed:18375658). Methylates only a limited fraction of nucleosomes of target genes (e.g. NA... | Arabidopsis thaliana (Mouse-ear cress) |
P0CB42 | ALKB1_MOUSE | MGKMAAAVASLATLAAEPREDAFRKLFRFYRQSRPGTADLGAVIDFSEAHLARSPKPGVPQVVRFPLNVSSVTERDAERVGLEPVSKWRAYGLEGYPGFIFIPNPFLPGCQRHWVKQCLKLYSQKPNVCNLDKHMTKEETQGLWEQSKEVLRSKEVTKRRPRSLLERLRWVTLGYHYNWDSKKYSADHYTPFPSDLAFLSEQVATACGFQGFQAEAGILNYYRLDSTLGIHVDRSELDHSKPLLSFSFGQSAIFLLGGLKRDEAPTAMFMHSGDIMVMSGFSRLLNHAVPRVLPHPDGECLPHCLETPLPAVLPSNSLVE... | 1.14.11.-; 1.14.11.33; 1.14.11.51; 4.2.99.18 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:27027282}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805}; | cell differentiation [GO:0030154]; developmental growth [GO:0048589]; DNA dealkylation involved in DNA repair [GO:0006307]; in utero embryonic development [GO:0001701]; negative regulation of neuron apoptotic process [GO:0043524]; neuron migration [GO:0001764]; neuron projection development [GO:0031175]; oxidative RNA ... | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; euchromatin [GO:0000791]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; broad specificity oxidative DNA demethylase activity [GO:0035516]; chemoattractant activity [GO:0042056]; class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; DNA N6-methyladenine demethylase activity [GO:0141131]; ferrous iron bindi... | PF13532; | 2.60.120.590; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18163532}. Note=Mainly localizes in euchromatin, largely excluded from heterochromatin and nucleoli. {ECO:0000269|PubMed:18163532}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + an N(6)-methyl-2'-deoxyadenosine in DNA + O2 = a 2'-deoxyadenosine in DNA + CO2 + formaldehyde + succinate; Xref=Rhea:RHEA:49524, Rhea:RHEA-COMP:12418, Rhea:RHEA-COMP:12419, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI... | null | null | null | null | FUNCTION: Dioxygenase that acts as on nucleic acids, such as DNA and tRNA (PubMed:27027282, PubMed:27745969). Requires molecular oxygen, alpha-ketoglutarate and iron (PubMed:27027282). A number of activities have been described for this dioxygenase, but recent results suggest that it mainly acts as on tRNAs and mediate... | Mus musculus (Mouse) |
P0CB47 | UBFL1_HUMAN | MALPRSQGHWSNKDILRLLECMENNRPSDDNSTFSSTQSHMDWGKVAFKNFSGEMCRLKWLEISCNLRKFGTLKELVLEAKKCVKKMNKSQKYRNGPDFPKRPLTAYNRFFKESWPQYSQMYPGMRSQELTKILSKKYRELPEQMKQKYIQDFRKEKQEFEEKLARFREEHPDLVQKAKKSSVSKRTQNKVQKKFQKNIEEVRSLPKTDRFFKKVKFHGEPQKPPMNGYHKFHQDSWSSKEMQHLSVRERMVEIGRRWQRIPQSQKDHFKSQAEELQKQYKVKLDLWLKTLSPENYAAYKESTYAKGKNMAMTGGPDPRL... | null | null | blastocyst growth [GO:0001832]; embryo implantation [GO:0007566]; positive regulation of transcription by RNA polymerase I [GO:0045943]; transcription by RNA polymerase I [GO:0006360] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | RNA polymerase I core promoter sequence-specific DNA binding [GO:0001164]; RNA polymerase I general transcription initiation factor activity [GO:0001181] | PF00505; | 1.10.30.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q3USZ2}. Nucleus {ECO:0000250|UniProtKB:Q3USZ2, ECO:0000255|PROSITE-ProRule:PRU00267}. Note=Mainly cytoplasmic from the 4-cell stage to the morula stage. Becomes nuclear at the blastocyst stage. {ECO:0000250|UniProtKB:Q3USZ2}. | null | null | null | null | null | FUNCTION: Essential for proliferation of the inner cell mass and trophectodermal cells in peri-implantation development. {ECO:0000250|UniProtKB:Q3USZ2}. | Homo sapiens (Human) |
P0CB51 | CHI1_COCPS | MRFLIGALLTLQTLVQASSMSSMPNYYPVPEAPAEGGFRSVVYFVNWAIYGRGHNPQDLKADQFTHILYAFANIRPSGEVYLSDTWADTDKHYPGDKWDEPGNNVYGCIKQMYLLKKNNRNLKTLLSIGGWTYSPNFKTPASTEEGRKKFADTSLKLMKDLGFDGIDIDWEYPEDEKQANDFVLLLKACREALDAYSAKHPNGKKFLLTIASPAGPQNYNKLKLAEMDKYLDFWNLMAYDFSGSWDKVSGHMSNVFPSTTKPESTPFSSDKAVKDYIKAGVPANKIVLGMPLYGRAFASTDGIGTSFNGVGGGSWENGVW... | 3.2.1.14 | null | chitin catabolic process [GO:0006032]; polysaccharide catabolic process [GO:0000272] | extracellular region [GO:0005576] | chitin binding [GO:0008061]; chitinase activity [GO:0004568] | PF00704; | 3.10.50.10;3.20.20.80; | Glycosyl hydrolase 18 family, Chitinase class V subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. Active from pH 4 to 8. {ECO:0000269|PubMed:11327866}; | null | null | Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus) |
P0CB53 | DPS_STRSU | MMKQKYYQSPAEIASFSPRPSLADSKAVLNQAVADLSVAHSILHQVHWYMRGRGFMIWHPKMDEYMEEIDGYLDEMSERLITLGGAPFSTLKEFSENSQLKEVLGDYNVTIEEQLARVVEVFRYLAALFQKGFDVSDEEGDSVTNDIFNVAKASIEKHIWMLQAELGQAPKL | 1.16.-.- | null | intracellular iron ion homeostasis [GO:0006879] | cytoplasm [GO:0005737] | ferric iron binding [GO:0008199]; oxidoreductase activity [GO:0016491] | PF00210; | 1.20.1260.10; | Dps family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=2 Fe(2+) + 2 H(+) + H2O2 = 2 Fe(3+) + 2 H2O; Xref=Rhea:RHEA:48712, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; | null | null | null | null | FUNCTION: Protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction (By similarity). It binds and incorporates Fe(2+) iron. Is re... | Streptococcus suis |
P0CC10 | LRC4B_RAT | MAQAHIQGSPCPLLPPGRMSWPQGALLLLWLFSPPLRAGGGGVAVTSAAGGGSPPATSCPAACSCSNQASRVICTRRELAEVPASIPVNTRYLNLQENSIQVIRTDTFKHLRHLEILQLSKNLVRKIEVGAFNGLPSLNTLELFDNRLTTVPTQAFEYLSKLRELWLRNNPIESIPSYAFNRVPSLRRLDLGELKRLEYISEAAFEGLVNLRYLNLGMCNLKDIPNLTALVRLEELELSGNRLDLIRPGSFQGLTSLRKLWLMHAQVATIERNAFDDLKSLEELNLSHNNLMSLPHDLFTPLHRLERVHLNHNPWHCNCD... | null | null | positive regulation of synapse assembly [GO:0051965]; regulation of postsynaptic density assembly [GO:0099151]; regulation of presynapse assembly [GO:1905606]; synaptic membrane adhesion [GO:0099560] | cerebellar mossy fiber [GO:0044300]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; presynaptic membrane [GO:0042734] | signaling receptor binding [GO:0005102] | PF07679;PF00560;PF13855; | 2.60.40.10;3.80.10.10; | null | PTM: N-glycosylated. O-glycosylated; contains sialic acid. {ECO:0000269|PubMed:16980967, ECO:0000269|PubMed:19252495}. | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:19252495}; Single-pass membrane protein {ECO:0000269|PubMed:19252495}. Presynaptic cell membrane {ECO:0000269|PubMed:19252495}. | null | null | null | null | null | FUNCTION: Synaptic adhesion protein. Regulates the formation of excitatory synapses. The trans-synaptic adhesion between LRRC4B and PTPRF regulates the formation of excitatory synapses in a bidirectional manner. {ECO:0000269|PubMed:19252495}. | Rattus norvegicus (Rat) |
P0CC16 | OXLA_AGKCL | ADSRNPLEEEFRETNYEEF | 1.4.3.2 | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:10441379}; Note=Does not use FAD as a cofactor. {ECO:0000269|PubMed:10441379}; | apoptotic process [GO:0006915]; defense response to bacterium [GO:0042742]; envenomation resulting in hemorrhagic damage in another organism [GO:0044358]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | FMN binding [GO:0010181]; L-amino-acid oxidase activity [GO:0001716]; L-phenylalaine oxidase activity [GO:0106329]; protein homodimerization activity [GO:0042803]; toxin activity [GO:0090729] | null | null | Flavin monoamine oxidase family, FIG1 subfamily | PTM: Contains 2 disulfide bonds. {ECO:0000250|UniProtKB:P81382}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:P81382}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10441379}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:10441379}; CATALYTIC ACTIVITY: Reaction=H2O... | null | null | null | null | FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:10441379). Is active on L-Ile followed by L-Phe, L-Met, L-Val, L-Arg, L-Leu (PubMed:10441379). Exhibits diverse b... | Agkistrodon contortrix laticinctus (Broad-banded copperhead) (Agkistrodon mokasen laticinctus) |
P0CC17 | OXLA_BOTAT | MNVFFTFSLLFLAALGSCADDRNPLEECFRETDYEEFLEIAKNGLSTTSNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYRNEKEGWYANLGPMRLPEKHRIVREYIRKFDLQLNEFSQENENAWYFIKNIRKRVGEVNKDPGVLEYPVKPSEVGKSAGQLYEESLQKAVEELRRTNCSYMLNKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVGGMDKLPTSMYQAIQEKVHLNARVIKIQQDVKEVTVTYQTSEKETLSVTADYVIVCTTSRAARRI... | 1.4.3.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:28137621}; | amino acid catabolic process [GO:0009063]; apoptotic process [GO:0006915]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; envenomation resulting in positive regulation of platelet aggregation in another organism [GO:0044478]; killing of cells of anoth... | extracellular region [GO:0005576] | L-amino-acid oxidase activity [GO:0001716]; L-phenylalaine oxidase activity [GO:0106329]; metal ion binding [GO:0046872]; toxin activity [GO:0090729] | PF01593; | 3.90.660.10;3.50.50.60;1.10.405.10; | Flavin monoamine oxidase family, FIG1 subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18804547}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:18804547}; CATALYTIC ACTIVITY: Reaction=H2O... | null | null | null | null | FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:18804547). Shows high catalytic activity against L-Met, L-Leu, L-Phe, L-Trp, L-Tyr, L-Ile (PubMed:18804547). Show... | Bothrops atrox (Barba amarilla) (Fer-de-lance) |
P0CD91 | AQY1_YEAST | MSSNDSNDTDKQHTRLDPTGVDDAYIPPEQPETKHHRFKISRDTLRDHFIAAVGEFCGTFMFLWCAYVICNVANHDVALVAAPDGSHPGQLIMIAIGFGFSVMFSIWCFAGVSGGALNPAMSLSLCLARAVSPTRCVVMWVSQIVAGMAAGGAASAMTPGEVLFANSLGLGCSRTRGLFLEMFGTAILCLTVLMTAVEKRETNFMAALPIGISLFIAHVALTAYTGTGVNPARSLGAAVAARYFPHYHWIYWIGTLLGSILAWSVWQLLQILDYTTYVTAEKAASTKEKAQKKGETSSSSAVAEV | null | null | ascospore formation [GO:0030437]; transmembrane transport [GO:0055085]; water transport [GO:0006833] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886] | water channel activity [GO:0015250] | PF00230; | 1.20.1080.10; | MIP/aquaporin (TC 1.A.8) family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein. Cell membrane {ECO:0000250}; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Water channel required to facilitate the transport of water across membranes. Involved in sporulation, freeze tolerance and osmotolerance (By similarity). Is non-functional in most laboratory strains. {ECO:0000250, ECO:0000269|PubMed:10092523, ECO:0000269|PubMed:10870101, ECO:0000269|PubMed:9765289}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P0CE12 | SSPH2_SALTY | MPFHIGSGCLPATISNRRIYRIAWSDTPPEMSSWEKMKEFFCSTHQTEALECIWTICHPPAGTTREDVINRFELLRTLAYAGWEESIHSGQHGENYFCILDEDSQEILSVTLDDAGNYTVNCQGYSETHRLTLDTAQGEEGTGHAEGASGTFRTSFLPATTAPQTPAEYDAVWSAWRRAAPAEESRGRAAVVQKMRACLNNGNAVLNVGESGLTTLPDCLPAHITTLVIPDNNLTSLPALPPELRTLEVSGNQLTSLPVLPPGLLELSIFSNPLTHLPALPSGLCKLWIFGNQLTSLPVLPPGLQELSVSDNQLASLPAL... | 2.3.2.27 | null | positive regulation of interleukin-8 production [GO:0032757]; positive regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway [GO:0070430]; positive regulation of plant-type hypersensitive response [GO:0034052]; protein secretion by the type III secretion system [GO:0030254]; protein ubi... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | catalytic activity [GO:0003824]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF14496; | 1.20.58.90;3.80.10.10;3.30.2440.10;1.20.58.360;1.20.1270.130; | LRR-containing bacterial E3 ligase family | PTM: Ubiquitinated in the presence of host E1 ubiquitin-activating enzyme UBA1, E2 ubiquitin-conjugating enzyme UBE2D2 and ubiquitin. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Host cytoplasm {ECO:0000250}. Host apical cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Secreted via type III secretion system 2 (SPI-2 T3SS), and delivered into the host cytoplasm. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | null | null | null | FUNCTION: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. {ECO:0000250}. | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P0CE41 | HAP1_YEAST | MSNTPYNSSVPSIASMTQSSVSRSPNMHTATTPGANTSSNSPPLHMSSDSSKIKRKRNRIPLSCTICRKRKVKCDKLRPHCQQCTKTGVAHLCHYMEQTWAEEAEKELLKDNELKKLRERVKSLEKTLSKVHSSPSSNSLKSYNTPESSNLFMGSDEHTTLVNANTGSASSASHMHQQQQQQQQQEQQQDFSRSANANANSSSLSISNKYDNDELDLTKDFDLLHIKSNGTIHLGATHWLSIMKGDPYLKLLWGHIFAMREKLNEWYYQKNSYSKLKSSKCPINHAQAPPSAAAAATRKCPVDHSAFSSGMVAPKEETPL... | null | null | carbon catabolite activation of transcription from RNA polymerase II promoter [GO:0000436]; DNA-templated transcription [GO:0006351]; establishment of protein localization to chromatin [GO:0071169]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase I... | mitochondrion [GO:0005739]; nucleus [GO:0005634]; transcription repressor complex [GO:0017053] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; zinc ion binding [GO:0008270] | PF00172; | 1.20.5.170;4.10.240.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}. | null | null | null | null | null | FUNCTION: Regulation of oxygen dependent gene expression. It modulates the expression of Iso-1 (CYP1) and Iso-2 (CYP3) cytochrome c. In response to heme, promotes transcription of genes encoding functions required for respiration, controlling oxidative damage and repression of anaerobic genes. Binds to the sequence 5'-... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P0CE43 | GRB10_RAT | MNNDINSSVESLNSACNMQSDTDTVPLLENGQSASNQPSASSSRGQPQASPRQKMQRSQPVHIQPLRRLQEEDQQLRTSSLPAIPNPFPELAGGAPGSPPSVAPSSLPPPPSQPPAKHFPPGFQLAKLTRPGLWTKTTARFSKRQPKNQCQTDTANAVSRIPTSQMEKLRLRKDVKVFSEDGTSKVVEILTDMTARDLCQLLVYKSHCVDDNSWTLVEHHPQLGLERCLEDHEIVVQVESTMPSESKFLFRKNYAKYEFFKNPVNFFPDQMVTWCQQSNGGQAQLLQNFLNSSSCPEIQGFLQVKEVGRKSWKKLYVCLR... | null | null | ERK1 and ERK2 cascade [GO:0070371]; gene expression [GO:0010467]; insulin receptor signaling pathway [GO:0008286]; insulin-like growth factor receptor signaling pathway [GO:0048009]; negative regulation of glucose import [GO:0046325]; negative regulation of glycogen biosynthetic process [GO:0045719]; negative regulatio... | cytoplasm [GO:0005737]; protein-containing complex [GO:0032991] | insulin receptor binding [GO:0005158]; protein-macromolecule adaptor activity [GO:0030674]; signaling receptor complex adaptor activity [GO:0030159] | PF08947;PF00169;PF00788;PF00017; | 2.30.29.30;3.30.505.10; | GRB7/10/14 family | PTM: Phosphorylated on serine residues upon EGF, FGF and PDGF stimulation. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=When complexed with NEDD4 and IGF1R, follows IGF1R internalization, remaining associated with early endosomes. Uncouples from IGF1R-containing endosomes before the sorting of the receptor to the lysosomal compartment (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Adapter protein which modulates coupling of a number of cell surface receptor kinases with specific signaling pathways. Binds to, and suppress signals from, activated receptors tyrosine kinases, including the insulin (INSR) and insulin-like growth factor (IGF1R) receptors. The inhibitory effect can be achieve... | Rattus norvegicus (Rat) |
P0CE46 | ZNT8_RAT | MEFLERTYLVNDQATKMYAFTSDRERGQKPVNKDQCPGDGPERPEAGAIYHCHNSFKATGNRSSKQVHAKWRLCAASAICFFFMVAEVVGGHVAGSLAVLTDAAHLLIDLTSFLLSLFSLWLSSRPPSKRLTFGWYRAEILGALLSVLCIWVVTGVLVYLACERLLYPDYQIQAGIMITVSGCAVAANIVLTLILHQRHLGHNHKDAQANASVRAAFVHALGDVFQSTSVLISALIIYFKPDYKMADPVCTFISSVLALASTVMILKDFSILLMEGVPKGLSYNSVKELLLTVDGVISVHNLHIWSLTVNQVILSVHVAT... | null | null | insulin processing [GO:0030070]; insulin secretion [GO:0030073]; intracellular zinc ion homeostasis [GO:0006882]; positive regulation of insulin secretion [GO:0032024]; regulation of vesicle-mediated transport [GO:0060627]; response to glucose [GO:0009749]; response to interleukin-1 [GO:0070555]; response to type II in... | cytoplasmic vesicle [GO:0031410]; plasma membrane [GO:0005886]; secretory granule [GO:0030141]; secretory granule membrane [GO:0030667]; transport vesicle membrane [GO:0030658] | metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; zinc ion transmembrane transporter activity [GO:0005385]; zinc:proton antiporter activity [GO:0140826] | PF01545; | 1.20.1510.10; | Cation diffusion facilitator (CDF) transporter (TC 2.A.4) family, SLC30A subfamily | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:19095428}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q8IWU4}; Multi-pass membrane protein {ECO:0000255}. Note=Associated with insulin and glucagon secretory granules. {ECO:0000250|UniProtKB:Q8... | CATALYTIC ACTIVITY: Reaction=2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out); Xref=Rhea:RHEA:72627, ChEBI:CHEBI:15378, ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q8IWU4}; | null | null | null | null | FUNCTION: Proton-coupled zinc ion antiporter mediating the entry of zinc into the lumen of pancreatic beta cell secretory granules, thereby regulating insulin secretion. {ECO:0000269|PubMed:19479076}. | Rattus norvegicus (Rat) |
P0CE47 | EFTU1_ECOLI | MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGGRH... | null | null | response to antibiotic [GO:0046677]; translational elongation [GO:0006414] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; guanyl-nucleotide exchange factor complex [GO:0032045]; plasma membrane [GO:0005886] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; guanosine tetraphosphate binding [GO:0097216]; RNA binding [GO:0003723]; translation elongation factor activity [GO:0003746] | PF00009;PF03144;PF03143; | 3.40.50.300;2.40.30.10; | TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, EF-Tu/EF-1A subfamily | PTM: The N-terminus is blocked.; PTM: Methylated in vivo on Lys-57 in response to nutrient starvation. {ECO:0000269|PubMed:2022614, ECO:0000269|PubMed:389663, ECO:0000269|PubMed:6997043, ECO:0000269|PubMed:7021545}.; PTM: Phosphorylated in vitro by phage protein doc on Thr-383. {ECO:0000269|PubMed:19150849, ECO:0000269... | SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral membrane protein. Note=Between 50-80% of the protein is associated with the cell inner membrane. Localization to the membrane has been suggested to follow nutrient stress. | null | null | null | null | null | FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.; FUNCTION: May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.; FUNCTION: Plays a stimulatory role in trans-translation; binds tmRNA... | Escherichia coli (strain K12) |
P0CE48 | EFTU2_ECOLI | MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGGRH... | null | null | response to antibiotic [GO:0046677]; translational elongation [GO:0006414] | cytosol [GO:0005829]; guanyl-nucleotide exchange factor complex [GO:0032045]; plasma membrane [GO:0005886] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; guanosine tetraphosphate binding [GO:0097216]; RNA binding [GO:0003723]; translation elongation factor activity [GO:0003746] | PF00009;PF03144;PF03143; | 3.40.50.300;2.40.30.10; | TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, EF-Tu/EF-1A subfamily | PTM: The N-terminus is blocked.; PTM: Methylated in vivo on Lys-57 in response to nutrient starvation. {ECO:0000269|PubMed:2022614, ECO:0000269|PubMed:389663, ECO:0000269|PubMed:6997043, ECO:0000269|PubMed:7021545}.; PTM: Phosphorylated in vitro by phage protein doc on Thr-383. {ECO:0000269|PubMed:19150849, ECO:0000269... | SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral membrane protein. Note=Between 50-80% of the protein is associated with the cell inner membrane. Localization to the membrane has been suggested to follow nutrient stress. | null | null | null | null | null | FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.; FUNCTION: May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.; FUNCTION: Plays a stimulatory role in trans-translation, binds tmRNA... | Escherichia coli (strain K12) |
P0CE79 | A1H2_LOXRE | MLLYVTLILGCWSAFSESAETDVAERANKRPIWIMGHMVNAIYQIDEFVNLGANSIETDVSFDKDANPEYTYHGVPCDCGRSCLKWEYFSDFLKGLRKATTPGDSKYHAKLVLVVFDLKTGSLYDNQAYDAGKKLAKNLLKHYWNNGNNGGRAYIVLSIPDLNHYKLITGFKETLKSEGHPELMDKVGHDFSGNDAIGDVGNAYKKAGVTGHVWQSDGITNCLLRGLSRVKEAVKNRDSSNGFINKVYYWTVDKRATTREALDAGVDGVMTNYPDVITDVLNESAYKAKFRIATYDDNPWETFKN | 4.6.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8I914}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8I914}; | killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042] | extracellular region [GO:0005576] | lyase activity [GO:0016829]; metal ion binding [GO:0046872]; phosphoric diester hydrolase activity [GO:0008081]; toxin activity [GO:0090729] | PF13653; | 3.20.20.190; | Arthropod phospholipase D family, Class II subfamily, Class IIa sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:15926888}. | CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60652, ChEBI:CHEBI:15354, ChEBI:CHEBI:64583, ChEBI:CHEBI:143892; Evidence={ECO:0000305|PubMed:15926888}; CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphoethanolamine = an N... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=436 uM for LPC (12:0) {ECO:0000269|PubMed:15926888}; KM=219 uM for LPC (14:0) {ECO:0000269|PubMed:15926888}; KM=220 uM for LPC (16:0) {ECO:0000269|PubMed:15926888}; KM=104 uM for LPC (18:0) {ECO:0000269|PubMed:15926888}; KM=98 uM for LPC (18:1) {ECO:0000269|PubMed:... | null | null | null | FUNCTION: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (PubMed:15926888). It also acts on a bro... | Loxosceles reclusa (Brown recluse spider) |
P0CE80 | A1HA_LOXIN | MLPYIVLVLGCWSVLSQAAQTDDEERAGNRRPIWIMGHMVNAIGQIDEFVNLGANSIETDVSFDDNANPEYTYHGIPCDCGRNCKKYENFNDFLKGLRSATTPGNSKYQEKLVLVVFDLKTGSLYDNQANDAGKKLAKNLLQHYWNNGNNGGRAYIVLSIPDLNHYPLIKGFKDQLTKDGHPELMDKVGHDFSGNDDIGDVGKAYKKAGITGHIWQSDGITNCLPRGLSRVNAAVANRDSANGFINKVYYWTVDKRSTTRDALDAGVDGIMTNYPDVITDVLNEAAYKKKFRVATYDENPWVTFKK | 4.6.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:21301094, ECO:0000269|PubMed:21616057, ECO:0000312|PDB:3RLG, ECO:0000312|PDB:3RLH}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:21301094, ECO:0000269|PubMed:21616057, ECO:0000312|PDB:3RLG, ECO:0000312|PDB:3RLH}; | killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042] | extracellular region [GO:0005576] | lyase activity [GO:0016829]; metal ion binding [GO:0046872]; phosphoric diester hydrolase activity [GO:0008081]; toxin activity [GO:0090729] | PF13653; | 3.20.20.190; | Arthropod phospholipase D family, Class II subfamily, Class IIa sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9790962}. | CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60652, ChEBI:CHEBI:15354, ChEBI:CHEBI:64583, ChEBI:CHEBI:143892; Evidence={ECO:0000305|PubMed:16581177, ECO:0000305|PubMed:21590705, ECO:0000305|PubMed:27233517, ECO:0000305|PubMed:9... | null | null | null | null | FUNCTION: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) with high activity (PubMed:16581177, Pub... | Loxosceles intermedia (Brown spider) |
P0CE81 | A1HB1_LOXIN | MLPYIVLVLGCWSVLSQAAQTDDEERAGNRRPIWIMGHMVNAIGQIDEFVNLGANSIETDVSFDDNANPEYTYHGIPCDCGRNCKKYENFNDFLKGLRSATTPGNSKYQEKLVLVVFDLKTGSLYDNQANDAGKKLAKNLLQHYWNNGNNGGRAYIVLSIPDLNHYPLIKGFKDQLTKDGHPELMEKVGHDFSGNDDIGDVGKAYKKAGITGHIWQSDGITNCLPRGLSRVNAAVANRDSANGFINKVYYWTVDKRSTTRDALDAGVDGIMTNYPDVITDVLNEAAYKKKFRVATYDDNPWVTFKK | 4.6.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8I914}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8I914}; | killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042] | extracellular region [GO:0005576] | lyase activity [GO:0016829]; metal ion binding [GO:0046872]; phosphoric diester hydrolase activity [GO:0008081]; toxin activity [GO:0090729] | PF13653; | 3.20.20.190; | Arthropod phospholipase D family, Class II subfamily, Class IIa sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9790962}. | CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60652, ChEBI:CHEBI:15354, ChEBI:CHEBI:64583, ChEBI:CHEBI:143892; Evidence={ECO:0000305|PubMed:9790962}; CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphoethanolamine = an N-... | null | null | null | null | FUNCTION: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (PubMed:15234562, PubMed:16934304, PubMe... | Loxosceles intermedia (Brown spider) |
P0CE82 | A1HB2_LOXIN | ARVVLGCWSVLSQAAQTDDEERAGNRRPIWIMGHMVNAIGQIDEFVNLGANSIETDVSFDDNANPEYTYHGIPCDCGRNCKKYENFNDFLKGLRSATTPGNSKYQEKLVLVVFDLKTGSLYDNQANDAGKKLAKNLLQHYWNNGNNGGRAYIVLSIPDLNHYPLIKGFKDQLTKDGHPELMDKVGHDFSGNDDIGDVGKAYKKAGITGHIWQSDGITNCLPRGLSRVNAAVANRDSANGFINKVYYWTVDKRSTTRDALDAGVDGIMTNYPDVITDVLNEAAYKKKFRVATYDDNPWVTFKK | 4.6.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:25961401, ECO:0000312|PDB:4RW3, ECO:0000312|PDB:4RW5}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:25961401, ECO:0000312|PDB:4RW3, ECO:0000312|PDB:4RW5}; | killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042] | extracellular region [GO:0005576] | lyase activity [GO:0016829]; metal ion binding [GO:0046872]; phosphoric diester hydrolase activity [GO:0008081]; toxin activity [GO:0090729] | PF13653; | 3.20.20.190; | Arthropod phospholipase D family, Class II subfamily, Class IIa sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9790962}. | CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60652, ChEBI:CHEBI:15354, ChEBI:CHEBI:64583, ChEBI:CHEBI:143892; Evidence={ECO:0000305|PubMed:9790962}; CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphoethanolamine = an N-... | null | null | null | null | FUNCTION: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (PubMed:9790962). It may also act on cer... | Loxosceles intermedia (Brown spider) |
P0CE83 | A1IA1_LOXIN | MLPYIALILVCWSVLSQAAQTDVEGRADKRRPIWIMGHMVNAIAQIDEFVNLGANSIETDVSFDDNANPEYTYHGIPCDCGRSCLKWENFNDFLKGLRSATTPGNAKYQAKLILVVFDLKTGSLYDNQANEAGKKLAKNLLKHYWNNGNNGGRAYIVLSIPDLNHYPLIKGFKDQLTQDGHPELMDKVGHDFSGNDAIGDVGNAYKKAGISGHVWQSDGITNCLLRGLDRVKQATANRDSANGFINKVYYWTVDKRATTRDALDAGVDGVMTNYPDVITDVLNESAYKNKFRVASYEDNPWETFKK | 4.6.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8I914}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8I914}; | killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042] | extracellular region [GO:0005576] | lyase activity [GO:0016829]; metal ion binding [GO:0046872]; phosphoric diester hydrolase activity [GO:0008081]; toxin activity [GO:0090729] | PF13653; | 3.20.20.190; | Arthropod phospholipase D family, Class II subfamily, Class IIa sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9790962}. | CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60652, ChEBI:CHEBI:15354, ChEBI:CHEBI:64583, ChEBI:CHEBI:143892; Evidence={ECO:0000305|PubMed:9790962}; CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphoethanolamine = an N-... | null | null | null | null | FUNCTION: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (PubMed:15234562, PubMed:9790962). It ma... | Loxosceles intermedia (Brown spider) |
P0CE84 | A1IA2_LOXIN | DVEERADKRRPIWIMGHMVNAIAQIDEFVNLGANSIETDVSFDDNANPEYTYHGIPCDCGRSCLKWENFNDFLKGLRSATTPGNAKYQAKLILVVFDLKTGSLYDNQANEAGKKLAKNLLKHYWNNGNNGGRAYIVLSIPDLNHYPLIKGFKDQLTQDGHPELMDKVGHDFSGNDAIGDVGNAYKKAGISGHVWQSDGITNCLLRGLDRVKQAIANRDSANGFINKVYYWTVDKRATTRDALDAGVDGVMTNYPDVITDVLNESAYKNKFRVASYEDNPWETFKK | 4.6.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8I914}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8I914}; | killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042] | extracellular region [GO:0005576] | lyase activity [GO:0016829]; metal ion binding [GO:0046872]; phosphoric diester hydrolase activity [GO:0008081]; toxin activity [GO:0090729] | PF13653; | 3.20.20.190; | Arthropod phospholipase D family, Class II subfamily, Class IIa sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9790962}. | CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60652, ChEBI:CHEBI:15354, ChEBI:CHEBI:64583, ChEBI:CHEBI:143892; Evidence={ECO:0000305|PubMed:16581177, ECO:0000305|PubMed:9790962}; CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingos... | null | null | null | null | FUNCTION: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) with high activity (PubMed:16581177, Pub... | Loxosceles intermedia (Brown spider) |
P0CE94 | TALA_DICDI | MSISLKINIVGANTVKTLRFAPDMCIQECCTHIFEKTNEGGPDHGLYQAHIEGKQSARWLAMEKTLQFYDINSDQQLDYKKKHRPQKFKLLDGTIKTQLVDESQNVSEIVNSICKKMGIKNPEEYSLMNSAGAWLNNTQILSEQGISENDITVLMKKFFFNDANIDRNDPVQLHLLFVQCRDGIIEGKYPTQREESLALSALQCQVQLGDYNPTKHVPGFLTLKDYLPLQWLKSKGVEKDIFKEHKKLVSMTEVNAKYRYVQLCRSLKTYGMTSFDVKIREYGKKKMVDHILGITREQMLLMLTETKEVIMTHPLKHIKR... | null | null | actomyosin contractile ring contraction [GO:0000916]; cell morphogenesis [GO:0000902]; cell-cell adhesion [GO:0098609]; cell-substrate adhesion [GO:0031589]; cleavage furrow ingression [GO:0036090]; mitotic cytokinesis [GO:0000281]; phagocytosis [GO:0006909]; sorocarp development [GO:0030587]; uropod retraction [GO:003... | cell cortex [GO:0005938]; cell trailing edge [GO:0031254]; cleavage furrow [GO:0032154]; cytoskeleton [GO:0005856]; filopodium tip [GO:0032433]; focal adhesion [GO:0005925]; membrane [GO:0016020]; pseudopodium [GO:0031143] | actin binding [GO:0003779]; integrin binding [GO:0005178]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546] | PF16511;PF00373;PF21692; | 1.20.80.10;1.20.120.230;2.30.29.30;1.20.1420.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex {ECO:0000250}. | null | null | null | null | null | FUNCTION: Actin-binding protein that may be involved in the control of cell motility and chemotaxis. {ECO:0000250}. | Dictyostelium discoideum (Social amoeba) |
P0CF24 | FOXP2_RAT | MMQESATETISNSSMNQNGMSTLSSQLDAGSRDGRSSGDTSSEVSTVELLHLQQQQALQAARQLLLQQQTSGLKSPKSSDKQRPLQVPVSVAMMTPQVITPQQMQQILQQQVLSPQQLQALLQQQQAVMLQQQQLQEFYKKQQEQLHLQLLQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQHPGKQAKEQQQQQQQQQLAAQQLVFQQQLLQMQQLQQQQHLLSLQCQGLISIPPGQAALPVQSLPQAGLSPAEIQQLWKEVTGVHSQEDNGIKHGGLDLTTNNSSSTTSSTTSKASPPITHHSIVNGQSSVLN... | null | null | camera-type eye development [GO:0043010]; caudate nucleus development [GO:0021757]; cerebellar Purkinje cell differentiation [GO:0021702]; cerebellum development [GO:0021549]; cerebral cortex development [GO:0021987]; epithelial cell proliferation involved in lung morphogenesis [GO:0060502]; forebrain development [GO:0... | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; nuclear androgen receptor binding [GO:0050681]; protein homodimerization activi... | PF00250;PF16159; | 1.20.5.340;1.10.10.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Transcriptional repressor that may play a role in the specification and differentiation of lung epithelium. May also play a role in developing neural, gastrointestinal and cardiovascular tissues. Can act with CTBP1 to synergistically repress transcription but CTPBP1 is not essential (By similarity). Plays a r... | Rattus norvegicus (Rat) |
P0CF52 | KDM7B_DANRE | MATAQLYCVCRQPYDVSRFMIECDICKDWFHGSCVEVEEHYAVDIDVYHCPNCDVHHGPSLMKKRRNWHRHDYTEPDDGSKPVQAGTSVFVRELQARTFPSGDEILQPMHGGQVTQRYLERHGFRYPIIVSKREELGLRLPPPDFSIKDVERYVGGNKVIDVIDVARQADSKMKLKAFVKYYYSPQRPKVLNVISLEFSDTKMAELVVVPDIAQKMSWVENYWPDDSYFPKPFVQKYCLMGVKDSYTDFHIDFGGTSVWYHVLWGEKIFYLIKPTPANLALYEEWSSSPNQSEVFFGEKVDKCYKCVVRQGTTLLIPTGW... | 1.14.11.- | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250}; | midbrain development [GO:0030901]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; histone demethylase activity [GO:0032452]; histone H3K27me2/H3K27me3 demethylase activity [GO:0071558]; histone H3K36 demethylase activity [GO:0051864]; histone H3K9 demethylase activity [GO:0032454]; histone H4K20 demethylase activity [GO:0035575]; metal ion ... | PF17811;PF02373;PF00628; | 1.20.58.1360;2.60.120.650; | JHDM1 histone demethylase family, JHDM1D subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Histone demethylase required for brain development. Specifically demethylates dimethylated 'Lys-9' and 'Lys-27' (H3K9me2 and H3K27me2, respectively) of histone H3 and monomethylated histone H4 'Lys-20' residue (H4K20Me1), thereby playing a central role in histone code (By similarity). {ECO:0000250, ECO:000026... | Danio rerio (Zebrafish) (Brachydanio rerio) |
P0CF96 | MZT1_SCHPO | MSESTKETIEVLYEIGTLLGTELDKTTLSLCISLCENNVHPEAIAQIIREIRMAQEQTVDTEPS | null | null | gamma-tubulin complex localization [GO:0033566]; microtubule nucleation by interphase microtubule organizing center [GO:0051415]; microtubule nucleation by spindle pole body [GO:0051417]; mitotic spindle assembly [GO:0090307] | cytoplasm [GO:0005737]; equatorial microtubule organizing center [GO:0000923]; gamma-tubulin complex [GO:0000930]; gamma-tubulin ring complex [GO:0000931]; gamma-tubulin small complex [GO:0008275]; inner plaque of mitotic spindle pole body [GO:0061497]; interphase microtubule organizing center [GO:0031021]; mitotic spi... | spindle pole body anchor activity [GO:0140475] | PF12554; | null | MOZART1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:23885124, ECO:0000269|PubMed:24006493}. Note=Localizes to all the MTOCs, including the SPB and interphase and equatorial MTOCs. | null | null | null | null | null | FUNCTION: Required for gamma-tubulin complex recruitment to the microtubule organizing center (MTOC). {ECO:0000269|PubMed:23885124, ECO:0000269|PubMed:24006493}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P0CG03 | VSPBH_BOTAL | MVLIRVLANLLILQLSYAQKASELVIGGDECNINEHRSLVVLFNSSGFLCAGTLINQEWVLTAANCDRKNIRIKLGMHSKNVTNEDEQTRVPKRSTFVSVAKTSHQTLGTRTSMLIRLKRPVNDSPHIAPLSLPSSPPSVGSVCRVMGWGTISPTKVSYPDVPHCANINLLDYEVCREAHGGLPATSRTLCAGILEGGKDSCQGDSGGPLICNGQFQGILSWGVHPCGQPHKPGVYTKVSDYSEWIQSIIAGNTDVTCPP | 3.4.21.- | null | killing of cells of another organism [GO:0031640]; proteolysis [GO:0006508] | extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00089; | 2.40.10.10; | Peptidase S1 family, Snake venom subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20184912}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:20184912}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-40 degrees Celsius. {ECO:0000269|PubMed:20184912}; | FUNCTION: Thrombin-like snake venom serine protease that induces blood clotting in vitro, defibrinogenation in vivo (by intraperitoneal injection into mice), albuminolytic and fibrinogenolytic activities. Preferentially cleaves the alpha chain of fibrinogen (FGA). Causes hemolysis in the heart, causes apparent hyperemi... | Bothrops alternatus (Urutu) (Rhinocerophis alternatus) |
P0CG04 | IGLC1_HUMAN | GQPKANPTVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADGSPVKAGVETTKPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS | null | null | adaptive immune response [GO:0002250]; B cell receptor signaling pathway [GO:0050853]; immune response [GO:0006955]; immunoglobulin mediated immune response [GO:0016064] | blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; IgA immunoglobulin complex [GO:0071745]; IgD immunoglobulin complex [GO:0071738]; IgE immunoglobulin complex [GO:0071742]; IgG immunoglobulin complex [GO:0071735]; IgM immunoglobuli... | antigen binding [GO:0003823] | PF07654; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. | null | null | null | null | null | FUNCTION: Constant region of immunoglobulin light chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trig... | Homo sapiens (Human) |
P0CG08 | GPHRB_HUMAN | MSFLIDSSIMITSQILFFGFGWLFFMRQLFKDYEIRQYVVQVIFSVTFAFSCTMFELIIFEILGVLNSSSRYFHWKMNLCVILLILVFMVPFYIGYFIVSNIRLLHKQRLLFSCLLWLTFMYFFWKLGDPFPILSPKHGILSIEQLISRVGVIGVTLMALLSGFGAVNCPYTYMSYFLRNVTDTDILALERRLLQTMDMIISKKKRMAMARRTMFQKGEVHNKPSGFWGMIKSVTTSASGSENLTLIQQEVDALEELSRQLFLETADLYATKERIEYSKTFKGKYFNFLGYFFSIYCVWKIFMATINIVFDRVGKTDPVT... | null | null | intracellular pH reduction [GO:0051452]; protein transport [GO:0015031]; response to abscisic acid [GO:0009737]; T cell differentiation [GO:0030217] | Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; monoatomic ion channel complex [GO:0034702] | abscisic acid binding [GO:0010427]; voltage-gated monoatomic anion channel activity [GO:0008308] | PF12430;PF12537; | null | Golgi pH regulator (TC 1.A.38) family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:18794847}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=iodide(out) = iodide(in); Xref=Rhea:RHEA:66324, ChEBI:CHEBI:16382; Evidence={ECO:0000269|PubMed:18794847}; CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:18794847}; CATALYTIC ACTIVITY: Reaction=bromide(in) = b... | null | null | null | null | FUNCTION: Voltage-gated channel that enables the transfer of anions such as iodide, chloride, bromide and fluoride which may function in counter-ion conductance and participates in Golgi acidification (PubMed:18794847). Plays a role in lymphocyte development, probably by acting as a RABL3 effector in hematopoietic cell... | Homo sapiens (Human) |
P0CG18 | RNPH_ECOBW | MRPAGRSNNQVRPVTLTRNYTKHAEGSVLVEFGDTKVLCTASIEEGVPRFLKGQGQGWITAEYGMLPRSTHTRNAREAAKGKQGGRTMEIQRLIARALRAAVDLKALGEFTITLDCDVLQADGGTRTASITGACVALVDALQKLVENGKLKTNPMKGMVAAVSVGIVNGEAVCDLEYVEDSAAETDMNVVMTEDGRIIEVQGTAEGEPFTHEELLILLALARGGIESIVATQKAALAN | 2.7.7.56 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:1512253}; Note=Can also use Mn(2+) or Co(2+) with reduced efficiency. K(+) simulates the degradative reaction. {ECO:0000269|PubMed:1512253}; | nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' [GO:0034427]; polyadenylation-dependent snoRNA 3'-end processing [GO:0071051]; rRNA catabolic process [GO:0016075]; rRNA processing [GO:0006364]; tRNA processing [GO:0008033]; U4 snRNA 3'-end processing [GO:0034475] | cytoplasmic exosome (RNase complex) [GO:0000177] | 3'-5'-RNA exonuclease activity [GO:0000175]; tRNA binding [GO:0000049]; tRNA nucleotidyltransferase activity [GO:0009022] | PF01138;PF03725; | 3.30.230.70; | RNase PH family | null | null | CATALYTIC ACTIVITY: Reaction=phosphate + tRNA(n+1) = a ribonucleoside 5'-diphosphate + tRNA(n); Xref=Rhea:RHEA:10628, Rhea:RHEA-COMP:17343, Rhea:RHEA-COMP:17344, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:173114; EC=2.7.7.56; Evidence={ECO:0000255|HAMAP-Rule:MF_00564, ECO:0000269|PubMed:1512253}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 mM for phosphate in the degradative reaction {ECO:0000269|PubMed:1512253}; KM=1 uM for tRNA-CCA-C2-3 in the degradative reaction {ECO:0000269|PubMed:1512253}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-9 for degradation (PubMed:1512253). {ECO:0000269|PubMed:1512253}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius activity drops off quickly from 45 degrees Celsius (PubMed:1512253). {ECO:0000269|PubMed:1512253}; | FUNCTION: Phosphorolytic exoribonuclease that plays an important role in tRNA 3'-end maturation; has no activity on a tRNA precursor with a 3'-terminal phosphate group (PubMed:1512253). In vitro is freely reversible, adds nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this ... | Escherichia coli (strain K12 / MC4100 / BW2952) |
P0CG19 | RNPH_ECOLI | MRPAGRSNNQVRPVTLTRNYTKHAEGSVLVEFGDTKVLCTASIEEGVPRFLKGQGQGWITAEYGMLPRSTHTRNAREAAKGKQGGRTMEIQRLIARALRAAVDLKALGEFTITLDCDVLQADGGTRTASITGACVALVDALQKLVENGKLKTNPMKGMVAAVSVGIVNGEAVCDLEYVEDSAAETDMNVVMTEDGRIIEVQGTAEGEPFTHEELLILLALARGESNPL | null | null | nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' [GO:0034427]; polyadenylation-dependent snoRNA 3'-end processing [GO:0071051]; rRNA catabolic process [GO:0016075]; rRNA processing [GO:0006364]; tRNA processing [GO:0008033]; U4 snRNA 3'-end processing [GO:0034475] | cytoplasmic exosome (RNase complex) [GO:0000177]; cytosol [GO:0005829] | 3'-5'-RNA exonuclease activity [GO:0000175]; tRNA binding [GO:0000049]; tRNA nucleotidyltransferase activity [GO:0009022] | PF01138;PF03725; | 3.30.230.70; | RNase PH family | null | null | null | null | null | null | null | FUNCTION: This an expressed but non-active exoribonuclease allele (PubMed:8501045). The catalytically inactive protein translated in strain K12 MG1655 inhibits the 5'-processing of primary pre-tRNAs with short (<5 nucleotide) leaders in a dominant-negative effect when RNA pyrophosphohydrolase (rppH) is also inactive; p... | Escherichia coli (strain K12) |
P0CG20 | PRR35_HUMAN | MSREAGSCRVGTGARARSRKPKKPHYIPRPWGKPYNYKCFQCPFTCLEKSHLYNHMKYSLCKDSLSLLLDSPDWACRRGSTTPRPHAPTPDRPGESDPGRQPQGARPTGAAPAPDLVVADIHSLHCGGGPKSRAKGSPGPPPPVARATRKGPGPSGLLPESWKPGMGGDPRGVGAGDMASAGPEGSVPCYPPPAPGEFPEAHSLHLSLLGVNYPLSPGLFSYLGPSLAAAAHVPFLASASPLLPPATAFPAVQPPQRPTPAPRLYYPLLLEHTLGLPAGKAALAKAPVSPRSPSGTPAPGLLKVPVPGLGPWPRVTPRDP... | null | null | null | null | null | PF15269; | null | null | null | null | null | null | null | null | null | null | Homo sapiens (Human) |
P0CG30 | GSTT2_HUMAN | MGLELFLDLVSQPSRAVYIFAKKNGIPLELRTVDLVKGQHKSKEFLQINSLGKLPTLKDGDFILTESSAILIYLSCKYQTPDHWYPSDLQARARVHEYLGWHADCIRGTFGIPLWVQVLGPLIGVQVPEEKVERNRTAMDQALQWLEDKFLGDRPFLAGQQVTLADLMALEELMQPVALGYELFEGRPRLAAWRGRVEAFLGAELCQEAHSIILSILEQAAKKTLPTPSPEAYQAMLLRIARIP | 2.5.1.18 | null | glutathione metabolic process [GO:0006749] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062] | glutathione transferase activity [GO:0004364] | PF00043;PF02798; | 1.20.1050.10;3.40.30.10; | GST superfamily, Theta family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:1417752}. | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:1417752}; | null | null | null | null | FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles (PubMed:1417752). Has a sulfatase activity (PubMed:1417752). {ECO:0000269|PubMed:1417752}. | Homo sapiens (Human) |
P0CG37 | CFC1_HUMAN | MTWRHHVRLLFTVSLALQIINLGNSYQREKHNGGREEVTKVATQKHRQSPLNWTSSHFGEVTGSAEGWGPEEPLPYSRAFGEGASARPRCCRNGGTCVLGSFCVCPAHFTGRYCEHDQRRSECGALEHGAWTLRACHLCRCIFGALHCLPLQTPDRCDPKDFLASHAHGPSAGGAPSLLLLLPCALLHRLLRPDAPAHPRSLVPSVLQRERRPCGRPGLGHRL | null | null | anterior/posterior pattern specification [GO:0009952]; blood vessel development [GO:0001568]; determination of left/right symmetry [GO:0007368]; gastrulation [GO:0007369]; heart development [GO:0007507]; nodal signaling pathway [GO:0038092] | cell surface [GO:0009986]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | activin receptor binding [GO:0070697]; nodal binding [GO:0038100] | PF09443; | 2.10.25.10; | EGF-CFC (Cripto-1/FRL1/Cryptic) family | PTM: N-glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18930707}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:18930707}. Secreted {ECO:0000269|PubMed:18930707}. Note=Does not exhibit a typical GPI-signal sequence. The C-ter hydrophilic extension of the GPI-signal sequence reduces the efficiency of processing and coul... | null | null | null | null | null | FUNCTION: NODAL coreceptor involved in the correct establishment of the left-right axis. May play a role in mesoderm and/or neural patterning during gastrulation. {ECO:0000269|PubMed:11062482}. | Homo sapiens (Human) |
P0CG47 | UBB_HUMAN | MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGC | null | null | energy homeostasis [GO:0097009]; fat pad development [GO:0060613]; female gonad development [GO:0008585]; female meiosis I [GO:0007144]; hypothalamus gonadotrophin-releasing hormone neuron development [GO:0021888]; male meiosis I [GO:0007141]; mitochondrion transport along microtubule [GO:0047497]; modification-depende... | cytosol [GO:0005829]; endocytic vesicle membrane [GO:0030666]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; neurona... | protein tag activity [GO:0031386]; RNA binding [GO:0003723]; ubiquitin protein ligase binding [GO:0031625] | PF00240; | null | Ubiquitin family | PTM: [Ubiquitin]: Phosphorylated at Ser-65 by PINK1 during mitophagy (PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:25527291, PubMed:26161729). Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy (PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:25527291, P... | SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion outer membrane {ECO:0000269|PubMed:24751536}; Peripheral membrane protein {ECO:0000305|PubMed:24751536}. | null | null | null | null | null | FUNCTION: [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polyme... | Homo sapiens (Human) |
P0CG48 | UBC_HUMAN | MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLE... | null | null | modification-dependent protein catabolic process [GO:0019941]; protein ubiquitination [GO:0016567] | cytosol [GO:0005829]; endocytic vesicle membrane [GO:0030666]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; mitochondrial outer membrane [GO:0005741]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO... | protease binding [GO:0002020]; protein tag activity [GO:0031386]; RNA binding [GO:0003723]; ubiquitin protein ligase binding [GO:0031625] | PF00240; | null | Ubiquitin family | PTM: [Ubiquitin]: Phosphorylated at Ser-65 by PINK1 during mitophagy. Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy (PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:25527291). Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects disch... | SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion outer membrane {ECO:0000269|PubMed:24751536}; Peripheral membrane protein {ECO:0000305|PubMed:24751536}. | null | null | null | null | null | FUNCTION: [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polyme... | Homo sapiens (Human) |
P0CG49 | UBB_MOUSE | MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGY | null | null | adipose tissue development [GO:0060612]; energy homeostasis [GO:0097009]; fat pad development [GO:0060613]; female gonad development [GO:0008585]; female meiosis I [GO:0007144]; hypothalamus gonadotrophin-releasing hormone neuron development [GO:0021888]; male gonad development [GO:0008584]; male meiosis I [GO:0007141]... | cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654] | protein tag activity [GO:0031386]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]; ubiquitin protein ligase binding [GO:0031625] | PF00240; | null | Ubiquitin family | PTM: [Ubiquitin]: Phosphorylated at Ser-65 by PINK1 during mitophagy. Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy. Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyubiquitin chains. It also affects de... | SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P0CG47}; Peripheral membrane protein {ECO:0000250|UniProtKB:P0CG47}. | null | null | null | null | null | FUNCTION: [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polyme... | Mus musculus (Mouse) |
P0CG51 | UBB_RAT | MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGY | null | null | adipose tissue development [GO:0060612]; energy homeostasis [GO:0097009]; fat pad development [GO:0060613]; female gonad development [GO:0008585]; female meiosis I [GO:0007144]; hypothalamus gonadotrophin-releasing hormone neuron development [GO:0021888]; male gonad development [GO:0008584]; male meiosis I [GO:0007141]... | cytosol [GO:0005829]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; nucleus [GO:0005634] | protein tag activity [GO:0031386]; RNA binding [GO:0003723]; ubiquitin protein ligase binding [GO:0031625] | PF00240; | null | Ubiquitin family | PTM: [Ubiquitin]: Phosphorylated at Ser-65 by PINK1 during mitophagy (PubMed:29475881). Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy (By similarity). Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyub... | SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P0CG47}; Peripheral membrane protein {ECO:0000250|UniProtKB:P0CG47}. | null | null | null | null | null | FUNCTION: [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polyme... | Rattus norvegicus (Rat) |
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