ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
B1A0U4 | MALSGLGSGPEGNPNNHQGKAIPTLNPSHGQGPSFLFSWVSFLVPFWSWYPFSPLPLKGIPGENSSSPNGLKNFHGIGLNGTERGMGHFHPISGNRLGLRLTLVAGWFLEPFPTFLAVLIRTQGDSTPSRSFVAFFVGTLGLGQEGITGSFNRKIAGPATIDPQDWAMEEGVLTNFLWPPFTTFFRTTKGFPVQWHGEGSFVVPGIFSLPQPLPWWLLLPDTPTGAGKPPESRQHQPSHSMNGAIVDIPGGLTQTPSSPDRSSSTNSIADEEKKLDYKPTSPTSDTEKGESLPLTASQSEIIASPTFSEMIRVIFSGPTLVLGACYFCTFGAELSINSVLGTFYQRQLGLGLQNAGNLAAIFGLLNIVMRPLGGMASDLLYRKTGSVWSKKALLHTYCVMTGVFCIAIGLARSRSQATLVGLVSGGLAFFLEGANGLTYSHVHPYANGVVSGFTGACGNLGGIVFAIVFRYNSLDYSKVFWIIGAIIIGLQVATCWIKPVPKSVI | Function: Major facilitator-type transporter; part of the gene cluster that mediates the biosynthesis of elsinochromes, pigments consisting of at least four interconvertible tautomers (A, B, C and D) that have a core phenolic quinone to which various side chains are attached and which play an important role in fungal pathogenesis . Once elsinochrome is synthesized, it must be exported outside the fungal cells, which is probably accomplished by the ECT1 transporter, to avoid toxicity .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54058
Sequence Length: 505
Subcellular Location: Cell membrane
|
Q8SQW6 | MASHEIQKVWADGCFDMFHYGHANALRQSKALGDYLIAGVHSSLSINQEKGLPVMEDEERYEVVEGCRYVDEVVRDAPFVTQTSMIKEYGVSIVAHGNDIVLDSSGQDSYCQVRRMGIFREVERTFGISTTEIVGRMMLKNRGSWLDGENGESSKDSGYHDRLLSLFMSSMGREKRGKVVFMDGNFDLFHAGHVASLRIARGMGDYLIVGIHDDETTKEYTRSYPVLSTKERMLTLMACRYVDEIVVSPYLVGSEFIKRHGIDVVAPSFDSKDLSRYDGIKDVVEHSYAENRFNYLSAEHIVNRIISNYQDYANRQKKRTGK | Catalytic Activity: CTP + H(+) + phosphoethanolamine = CDP-ethanolamine + diphosphate
Sequence Mass (Da): 36594
Sequence Length: 322
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 2/3.
EC: 2.7.7.14
|
Q9UTI6 | MASSSNIKHRLWLDGCMDFFHYGHSNAILQAKQLGETLVIGIHSDEEITLNKGPPVMTLEERCLSANTCKWVDEVVPSAPYVFDLEWMRRYGCQYVVHGDDISTDANGDDCYRFAKAADQYLEVKRTEGVSTTELLDRLLSSVPLEIYSTPVSVLSSQIDLLRRFATDSDGLTPFTDVFIYNTEKPETLISGTTLLRLNPEKNIIYIDGDWDLFTEKHISALELCTRMFPGIPIMAGIFADEKCFEKPMLNLLERILNLLQCKYISSILVGPPPASLFASSKYIKLCFDEQISKVYYPIFSTDVSIPALDISLSNTPNNSFYKFDKLGSDLIKQRVMLRRQHYEERQRRKMGKNATEQTTIKTYA | Catalytic Activity: CTP + H(+) + phosphoethanolamine = CDP-ethanolamine + diphosphate
Sequence Mass (Da): 41557
Sequence Length: 365
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 2/3.
EC: 2.7.7.14
|
P33412 | MTVNLDPDKVWIDGCFDFTHHGHAGAILQARRTVSKENGKLFCGVHTDEDIQHNKGTPVMNSSERYEHTRSNRWCSEVVEAAPYVTDPNWMDKYQCQYVVHGDDITIDANGEDCYKLVKEMGRFKVVKRTYGVSTTEIIHRILTKKSLPPTHPDYYPTTQELSFYSVAQDAVSKHCYVFQRDLDNVLVNGGYKFDAEDCVYVDGDFDLFHMGDIDQLRKLKMDLHPDKKLIVGITTSDYSSTIMTMKERVLSVLSCKYVDAVIIDADATSMSQYNCEKYHIGTAVLTAAGKFSEYLTKELIVKRVESQREVYIARNQKKGMSI | Function: Ethanolamine-phosphate cytidylyltransferase which catalyzes the second step of phosphatidylethanolamine biosynthesis. Involved in the maintenance of plasma membrane and required for proper sporulation.
Catalytic Activity: CTP + H(+) + phosphoethanolamine = CDP-ethanolamine + diphosphate
Sequence Mass (Da): 36863
Sequence Length: 323
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 2/3.
Subcellular Location: Cytoplasm
EC: 2.7.7.14
|
Q9H8V3 | MAENSVLTSTTGRTSLADSSIFDSKVTEISKENLLIGSTSYVEEEMPQIETRVILVQEAGKQEELIKALKTIKIMEVPVIKIKESCPGKSDEKLIKSVINMDIKVGFVKMESVEEFEGLDSPEFENVFVVTDFQDSVFNDLYKADCRVIGPPVVLNCSQKGEPLPFSCRPLYCTSMMNLVLCFTGFRKKEELVRLVTLVHHMGGVIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIYKAWERRNEQDFYAAVDDFRNEFKVPPFQDCILSFLGFSDEEKTNMEEMTEMQGGKYLPLGDERCTHLVVEENIVKDLPFEPSKKLYVVKQEWFWGSIQMDARAGETMYLYEKANTPELKKSVSMLSLNTPNSNRKRRRLKETLAQLSRETDVSPFPPRKRPSAEHSLSIGSLLDISNTPESSINYGDTPKSCTKSSKSSTPVPSKQSARWQVAKELYQTESNYVNILATIIQLFQVPLEEEGQRGGPILAPEEIKTIFGSIPDIFDVHTKIKDDLEDLIVNWDESKSIGDIFLKYSKDLVKTYPPFVNFFEMSKETIIKCEKQKPRFHAFLKINQAKPECGRQSLVELLIRPVQRLPSVALLLNDLKKHTADENPDKSTLEKAIGSLKEVMTHINEDKRKTEAQKQIFDVVYEVDGCPANLLSSHRSLVQRVETISLGEHPCDRGEQVTLFLFNDCLEIARKRHKVIGTFRSPHGQTRPPASLKHIHLMPLSQIKKVLDIRETEDCHNAFALLVRPPTEQANVLLSFQMTSDELPKENWLKMLCRHVANTICKADAENLIYTADPESFEVNTKDMDSTLSRASRAIKKTSKKVTRAFSFSKTPKRALRRALMTSHGSVEGRSPSSNDKHVMSRLSSTSSLAGIPSPSLVSLPSFFERRSHTLSRSTTHLI | Function: Guanine nucleotide exchange factor (GEF) that catalyzes the exchange of GDP for GTP. Promotes guanine nucleotide exchange on the Rho family members of small GTPases, like RHOA, RHOC, RAC1 and CDC42. Required for signal transduction pathways involved in the regulation of cytokinesis. Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Regulates the translocation of RHOA from the central spindle to the equatorial region. Plays a role in the control of mitotic spindle assembly; regulates the activation of CDC42 in metaphase for the process of spindle fibers attachment to kinetochores before chromosome congression. Involved in the regulation of epithelial cell polarity; participates in the formation of epithelial tight junctions in a polarity complex PARD3-PARD6-protein kinase PRKCQ-dependent manner. Plays a role in the regulation of neurite outgrowth. Inhibits phenobarbital (PB)-induced NR1I3 nuclear translocation. Stimulates the activity of RAC1 through its association with the oncogenic PARD6A-PRKCI complex in cancer cells, thereby acting to coordinately drive tumor cell proliferation and invasion. Also stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death.
PTM: Phosphorylated by PLK1 in vitro. Hyperphosphorylated during the G2 phase of the cell cycle. Phosphorylation at Thr-373 occurs during the G2/M phase, relieves its auto-inhibition status and stimulates its GEF activity. Phosphorylation at Thr-444 in G2/M phase is required for subsequent binding with PLK1 and Rho exchange activation. Dephosphorylated at the time of cytokinesis. Phosphorylation at Thr-359 is required for its transformation activity in cancer cells.
Sequence Mass (Da): 103505
Sequence Length: 914
Domain: The BRCT domains 1 and 2 are required for intramolecular interaction, but not for intermolecular oligomerization . The BRCT domains negatively inhibit its GEF activity in interphase cells . The same BRCT domains may act as a positive regulatory motif for the completion of cytokinesis after the breakdown of nuclear membrane during mitosis .
Subcellular Location: Nucleus
|
Q07139 | MADDSVLPSPSEITSLADSSVFDSKVAEMSKENLCLASTSNVDEEMPQVEARVIMVQDAGKQEELLKALKTIKIMEVPVIKIKESCPGKSEEKLIKSIINMEMKVPCVKMDSMEEFESLDSPEFENIFVVTDFQNSVFNDLYKADCRIVGPPVILNCAQRGEPLPFSCRPLYCTSMLNLVLCFTGFRKKEELVKLVTLVHHMGGVIRKECNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIYKAWERRNEQCFCAAVDDFRNEFKVPPFQDCILSFLGFSDEEKHSMEEMTEMQGGSYLPVGDERCTHLIVEENTVKDLPFEPSKKLFVVKQEWFWGSIQMDARAGETMYLYEKANTPELKKSVSLLSLSTPNSNRKRRRLKETLAQLSRETDLSPFPPRKRPSAEHSLSIGSLLDISNTPESSIHYGETPKSCAKSSRSSTPVPPKQSARWQVAKELYQTESNYVNILATIIQLFQVPLEEEGQRGGPILAPEEIKTIFGSIPDIFDVHMKIKDDLEDLIANWDESRSIGDIFLKYAKDLVKTYPPFVNFFEMSKEMIIKCEKQKPRFHAFLKINQAKPECGRQSLVELLIRPVQRLPSVALLLNDLKKHTADENPDKSTLEKAIGSLKEVMTHINEDKRKTEAQKQIFDVVYEVDGCPANLLSSHRSLVQRVETVSLGEHPCDRGEQVTLFLFNDCLEIARKRHKVIGTFRSPHDRTRPPASLKHIHLMPLSQIKKVLDIRETEDCHNAFALLVRPPTEQANVLLSFQMTSEELPKESWLKMLCRHVANTICKADAENLMYVADPESFEVNTKDMDSTLSRASRAIKKTSKKVTRAFSFSKTPKRALRMALSSSHSSEGRSPPSSGKLAVSRLSSTSSLAGIPSPSLVSLPSFFERRSHTLSRSTTHLI | Function: Guanine nucleotide exchange factor (GEF) that catalyzes the exchange of GDP for GTP. Promotes guanine nucleotide exchange on the Rho family members of small GTPases, like RHOA, RHOC, RAC1 and CDC42. Required for signal transduction pathways involved in the regulation of cytokinesis. Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Regulates the translocation of RHOA from the central spindle to the equatorial region. Plays a role in the control of mitotic spindle assembly; regulates the activation of CDC42 in metaphase for the process of spindle fibers attachment to kinetochores before chromosome congression. Involved in the regulation of epithelial cell polarity; participates in the formation of epithelial tight junctions in a polarity complex PARD3-PARD6-protein kinase PRKCQ-dependent manner. Plays a role in the regulation of neurite outgrowth. Inhibits phenobarbital (PB)-induced NR1I3 nuclear translocation. Stimulates the activity of RAC1 through its association with the oncogenic PARD6A-PRKCI complex in cancer cells, thereby acting to coordinately drive tumor cell proliferation and invasion. Also stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death.
PTM: Phosphorylated by PLK1 in vitro. Hyperphosphorylated during the G2 phase of the cell cycle. Phosphorylation at Thr-373 occurs during the G2/M phase, relieves its auto-inhibition status and stimulates its GEF activity. Phosphorylation at Thr-444 in G2/M phase is required for subsequent binding with PLK1 and Rho exchange activation. Dephosphorylated at the time of cytokinesis. Phosphorylation at Thr-359 is required for its transformation activity in cancer cells (By similarity).
Sequence Mass (Da): 103131
Sequence Length: 913
Domain: The BRCT domain 1 and 2 are required for the intramolecular interaction, but not for the intermolecular oligomerization. The BRCT domains negatively inhibit its GEF activity in interphase cells. The same BRCT domains may act as a positive regulatory motif for the completion of cytokinesis after the breakdown of nuclear membrane during mitosis (By similarity).
Subcellular Location: Nucleus
|
Q7W980 | MRKDETSNTSPDISVAQPASALRYHLRPPRRNDGAAIHQLVSECPPLDLNSLYAYLLLCEHHAHTCVVAESPGGRIDGFVSAYLLPTRPDVLFVWQVAVHSRARGHRLGRAMLGHILERQECRHVRHLETTVGPDNQASRRTFAGLAGERGAHVSEQPFFDRQAFGGADHDDEMLLRIGPFTHPPH | Function: Catalyzes the acetylation of L-2,4-diaminobutyrate (DABA) to gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) with acetyl coenzyme A.
Catalytic Activity: acetyl-CoA + L-2,4-diaminobutanoate = (2S)-4-acetamido-2-aminobutanoate + CoA + H(+)
Sequence Mass (Da): 20729
Sequence Length: 186
Pathway: Amine and polyamine biosynthesis; ectoine biosynthesis; L-ectoine from L-aspartate 4-semialdehyde: step 2/3.
EC: 2.3.1.178
|
O52249 | MNATTEPFTPSADLAKPSVADAVVGHEASPLFIRKPSPDDGWGIYELVKSCPPLDVNSAYAYLLLATQFRDSCAVATNEEGEIVGFVSGYVKSNAPDTYFLWQVAVGEKARGTGLARRLVEAVMTRPEMAEVHHLETTITPDNQASWGLFRRLADRWQAPLNSREYFSTDQLGGEHDPENLVRIGPFQTDQI | Function: Catalyzes the acetylation of L-2,4-diaminobutyrate (DABA) to gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) with acetyl coenzyme A. Does not acetylate amino acids like GABA, L-ornithine, L-lysine and L-aspartate.
Catalytic Activity: acetyl-CoA + L-2,4-diaminobutanoate = (2S)-4-acetamido-2-aminobutanoate + CoA + H(+)
Sequence Mass (Da): 21170
Sequence Length: 192
Pathway: Amine and polyamine biosynthesis; ectoine biosynthesis; L-ectoine from L-aspartate 4-semialdehyde: step 2/3.
EC: 2.3.1.178
|
P68104 | MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGNASGTTLLEALDCILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQKAQKAK | Function: Translation elongation factor that catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of ribosomes during the elongation phase of protein synthesis . Base pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing its accommodation into the ribosome . The growing protein chain is subsequently transferred from the P-site peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid through ribosome-catalyzed peptide bond formation . Also plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and PARP1 .
PTM: ISGylated.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 50141
Sequence Length: 462
Subcellular Location: Cytoplasm
EC: 3.6.5.-
|
P86934 | MGKEKVHMNLVVVGHVDAGKSTATGHLIYKCGGIDKRTIEKFEKEAADIGKASFKYAWVLDKLKAERERGITIDIALWKFESPKSVFTIIDAPGHRDFIKNMITGTSQADAAILIIASAQGEFEAGISKDGQTREHALLAFTLGVKQMVVCCNKMDDKTVNYGQERYDEIVKEVSAYIKKVGYNVEKVRFVPISGWQGDNMIEKSEKMPWYKGPTLLEALDMLEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVMKPGDVVTFAPANVTTEVKSIEMHHEQLAEATPGDNVGFNVKNVSVKDIRRGNVCGNTKNDPPKEAADFTAQVIILNHPGQIGNGYAPVLDCHTSHIACKFAEIESKIDRRSGKELEKAPKSIKSGDAAIVRMVPQKPMCVEVFNDYAPLGRFAVRDMRQTVAVGIIKAVTKKDGSGGKVTKAAVKASKK | Function: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
PTM: Phosphatidylethanolamine (PE) is a direct precursor of the ethanolamine-phosphoglycerol (EPG) moiety.
Sequence Mass (Da): 49106
Sequence Length: 449
Subcellular Location: Cytoplasm
|
Q05639 | MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETTKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPAYSEKRYDEIVKEVSAYIKKIGYNPATVPFVPISGWHGDNMLEPSPNMPWFKGWKVERKEGNASGVSLLEALDTILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDIRRGNVCGDSKSDPPQEAAQFTSQVIILNHPGQISAGYSPVIDCHTAHIACKFAELKEKIDRRSGKKLEDNPKSLKSGDAAIVEMVPGKPMCVESFSQYPPLGRFAVRDMRQTVAVGVIKNVEKKSGGAGKVTKSAQKAQKAGK | Function: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
PTM: Trimethylated at Lys-165 by EEF1AKMT3 . Mono-, di-, and trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is predominant. Methylation by EEF1AKMT4 contributes to the fine-tuning of translation rates for a subset of tRNAs . Trimethylated at the N-terminus by METTL13 . Mono- and dimethylated at Lys-55 by METTL13; dimethylated form is predominant .
Sequence Mass (Da): 50470
Sequence Length: 463
Subcellular Location: Nucleus
|
P60608 | MNSPCDRLQQFIQVLLEESWSFPSFANTLHWPENLLSYIDELVWQGSLQNFHQHEVRFDKPPLRLPLTGFSSLTENWSSRQAVSSRLVATAASPPAGCQAPIAFLGLKFSSLGPARKNPALCFLYDQSNSKCNTSWVKENVGCPWHWCNIHEALIRTEKGSDPMFYVNTSTGGRDGFNGFNLQISDPWDPRWASGVDGGLYEHKTFMYPVAKIRIARTLKTTVTGLSDLASSIQSAEKELTSQLQPAADQAKSSRFSWLTLISEGAQLLQSTGVQNLSHCFLCAALRRPPLVAVPLPTPFNYTINSSTPIPPVPKGQVPLFSDPIRHKFPFCYSTPNASWCNQTRMLTSTPAPPRGYFWCNSTLTKVLNSTGNHTLCLPISLIPGLTLYSQDELSHLLAWTEPRPQNKSKWAIFLPLVLGISLASSLVASGLGKGALTHSIQTSQDLSTHLQLAIEASAESLDSLQRQITTVAQVAAQNRQALDLLMAEKGRTCLFLQEECCYYLNESGVVENSLQTLKKKKSSKRS | Function: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has lost its original fusogenic properties.
PTM: The CXXC motif is highly conserved across a broad range of retroviral envelope proteins. It is thought to participate in the formation of a labile disulfide bond possibly with the CX6CC motif present in the transmembrane domain (By similarity).
Sequence Mass (Da): 58319
Sequence Length: 527
Domain: The CKS-17 immunosuppressive domain is present in many retroviral envelope proteins. As a synthetic peptide, it inhibits immune function in vitro and in vivo (By similarity).
Subcellular Location: Virion
|
A7RR04 | MGIITLLANRRGLHAILSNAQRIVGCRFVSSSIIPDASRLRNIGISAHIDSGKTTLTERLLFYTGRISHMHEVKGKDNVGATMDSMELERQRGITIQSAATYVNWKDHNINIIDTPGHVDFTVEVERALRVLDGAVLVLCAVGGVQSQTLTVNRQMKRYNVPCIAFINKLDRMGANHNRVLSQLRAKLNHNAALLQLPVGLEGNNTGVVDIIRWKAYYFDGDNGEIVREDVIPEDMVDECRKRRQELIEVVADVDPELGDLFLEEVKPSESQIIAAIRRATIERTFTPVFVGSALKNKGVQPLLDGVLDYLPNPTEVKNYALDAESLDTKVLMDSRRSGEAPFVGLAFKLEAGRYGQLTYLRVYQGALKRGGFIVNTRTGKRVKVPRIVRMHSDIMEDIQEGYAGDICALFGIECASGDTFTAEGAPLVSMESIFVPEPVISLAVEPKNKNDLDQFSKAINRFTREDPTFRVRFDDESKETIISGMGELHLDVYTERMRLEYNCPVICGKPKVAFRETIGKEASLDFRPKSRVAAAGQYGKVVGKIEPMPPESITKNEFVDATVGMNIPKNFIPAIEKGFYEACERGFITGHKVAGVRFVLEDGAAHAVDSSEMAFRMATIGAFREAFNKAAPMILEPIMSVEVNAPQEFQGTVIAGVNRRHGQVTGTDANEGYFTLFAEVPLNDMFGYATELRSQTQGKGEFTMEYCRYLPALAQVQAELMDRFNVEKLKKAKR | Function: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Sequence Mass (Da): 81675
Sequence Length: 735
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Mitochondrion
|
Q07803 | MRLLRITAGLGRGPLPRVPAILGWQGKQANWKTYRWCSSGSIPNEKIRNIGISAHIDSGKTTLTERVLYYTGRIATMHEVKGKDGVGAVMDSMELERQRGITIQSAATYTMWRDVNINIIDTPGHVDFTIEVERALRVLDGAVLVLCAVGGVQCQTMTVSRQMKRYNVPFLTFINKLDRMGSNPARALQQMRSKLNHNAAFVQIPIGLEGDFKGIIDLIEERAIYFDGDFGQIVRYDEIPADLRAAAADHRQELIECVANSDEQLGELFLEEKIPSVSDLKLAIRRATLSRSFTPVFLGSALKNKGVQPLLDAVLEFLPNPSEVQNYALLNQNDSKEKNKILMNPKRDDSHPFVGLAFKLEAGRFGQLTYVRNYQGELKKGSTIYNTRTGKKVRVQRLVRMHADMMEDVEEVYAGDICALFGIDCASGDTFTNKDNSDLSMESIHVPDPVISVAMKPSNKNDLEKFSKGIARFTREDPTFKVHFDTESKETIVSGMGELHLEIYAQRMEREYGCPCITGKPKVAFRETVTAPVPFDFTHKKQSGGAGQYGKVIGVLEPLAPEDYTKLEFSDETFGANVPKQFVPAVEKGFLDACEKGPLSGHKLSGLRFVLQDGAHHMVDSNEISFIRAGEGALKQALASATLCIIEPIMSVEVIAPNEFQGAVFAGINRRHGVITGQDGIEDYFTLYADVPLNNMFGYSTELRSCTEGKGEYTMEYNRYQPCSPSTQEELVNKYLEATGQLPVKKGKAKN | Function: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis.
Sequence Mass (Da): 83457
Sequence Length: 751
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Mitochondrion
|
Q9USZ1 | MLKLSFRSLTSRLPRLSTLVVRGYASVANTGIEASNTSENNLNIQEQLNDNDKKRLKQIRNIGISAHIDSGKTTFTERVLYYTGRIKDIHEVRGKDNVGAKMDFMELEREKGITIQSAATHCTWERTVDQIEANEKQKTDFEKSYNINIIDTPGHIDFTIEVERALRVLDGAVLVLCAVSGVQSQTITVDRQMRRYNVPRISFVNKMDRMGADPWKVIQQINTKLKIPAAAVQIPIGQEDKLEGVVDLIQMRAIYNRGSKGEKIEISQQVPENLIELAKEKRSALIEKLADLDEEIADIYVMEEDPTPEQLMGAIRRTTLARKFTPVLMGSALSNVGVQSVLDAVCDYLPNPSEVENIALNAADSEKPVSLVPSSEKPLVALAFKLEEGRFGQLTYLRIYQGTLKRGNYIYNVNSTKKIKVSRLVRMHSNDMEEIEKVEAGGICALFGIECASGDTFTDGSVSYTMTSMFVPEPVISLSLKPKSKDTTSFSKALNRFQREDPTFRVQLDNESKETIISGMGELHLEVYVERMRREYKVDCETGKPRVAFRETLSKKVPFSYLHKKQSGGAGQYAKVEGYIEYMDGVEDESGNVVDCEFINKVTGGTVPTQYIPACEKAFYEALKKGFLIGHPIKNCRFVLEDGAYHPVDSSELAFRLATISAFRTAFLQANPMVLEPIMNVSITAPVEHQGGVIGNLDKRKATIVDSDTDEDEFTLQAEVPLNSMFSYSSDIRALTKGKGEFSMEFLKYLPAPKYVQKELVDAYNKQQQK | Function: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Sequence Mass (Da): 86325
Sequence Length: 770
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Mitochondrion
|
A7EVV9 | MSMHRVARAVASSEACAGALRGSVSRTRFLCLNAPVQRFGARNALLGAGLGAKRHFFQSPIIRSGVAQAVLEKAAADPSALTQEAIVDNLNAAERDRLRRVRNIGIAAHIDSGKTTATERVLFYTGRINAIHEVRGKDAVGAKMDSMELEREKGITIQSAATFCDWMKVENGKEEKYHINLIDTPGHIDFTIEVERALRVLDGAVMILCAVSGVQSQTITVDRQMRRYNVPRISFINKMDRMGANPFKAVEQINQKLRIPAAALQVPIGSEDSFNGVVDLIRMKAIYNDGPKGEIIRETDEIPEELKQLCKEKRALLIETLADVDDEIAEIFLDEKTPSIEQMKAAIRRATINLKFTPVLMGSALADKSVQPMLDAVCDYLPNPAEVENLALDKRRAEAPVKLVSYNELPFVGLAFKLEESNYGQLTYIRVYQGSLRKGMNVFNARTDKRVKIPRIVRMHSNEMEEVPEIGAGEICAVFGVDCASGDTFTDGGLPYSMSSMFVPDPVISLSIKPKTTKDGSNFSKAMNRFQREDPTFRVHVDAESQETIISGMGELHLDIYVERMRREYKVEVETGKPQVAYRETITEHVTFDHTLKKQTGGAGDYARVVGFLEPIEAGPNGYAPSTFKEEVTGGSISDKFLFACEKGFLASCEKGPLLGHPVLGTHMVVNDGATHMTDSSEMAFKNATQQAFRKAFKEGKPQVLEPLMKTTITAPNEFQGNIVGLLNKRNAIISDTEIGPEDFTLIADCSLNAMFGFSSQLRAATQGKGEFGMEFSHYAPAPGQLQKELISNYEKAQADRHKK | Function: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Sequence Mass (Da): 88744
Sequence Length: 804
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Mitochondrion
|
B8MJJ5 | MVRPAQVRALSGLARSATFVRLLPSQSQNALRCASLPVSRLGALPLRATTQITSAPLRQWHQIRNSSATATASLAEQAAADPEGLSQAEIISNIDAEEWKRISKVRNIGIAAHIDSGKTTATERVLFYTGRINAIHEVRGRDSVGAKMDSMDLEREKGITIQSAATFCDWVKKENGKEEKYHFNLIDTPGHIDFTIEVERALRVLDGAVMILCAVSGVQSQTITVDRQMKRYNVPRISFVNKMDRMGANPFKAIDQINNKLKLPAAAVQVPIGAEDEFQGVVDLIRMKAIYNEGPRGETIVEKDEIPEHIKPLAEERRRILIETLADVDDEIAEIFLDEREPTIEQIKAAIRRATIALKFTPVFMGSALADKSIQPMLDGVCDYLPNPSEVTNLALDQKRKEAQVKLLPYGSQPFVGLAFKLEESNFGQLTYIRVYQGTLRKGANVFNARNDKKVKVPRIVRMHSNEMEEVQEIGAGEICAVFGVDCASGDTFTDGQLAYTMSSMFVPEPVISLSIKPKNNKDSANFSKAMARFQREDPTFRVSYDTESEQTIISGMGELHLDIYVERMRREYKVDCETGQPQVAYRETIGRRVEFDHLLKKQSGGPGDYARVVGWMEPSESLEENKFEEQIVGGAISEKFLFACEKGFNLACEKGPLIGHKVLGTKMVINDGATHMTDSSEMSFKNATQQAFRKAFMESQPHVLEPLMKTVVTAPIEFQGDVIGLLNKRNATINDSEIGVDEFTVYADCSLNGMFGFSSHLRAATQGKGEYTMEFSHYEKAPGQLQKELVQKYLKAQADRHKK | Function: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Sequence Mass (Da): 89606
Sequence Length: 804
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Mitochondrion
|
Q4P257 | MVAIPRVAAARSLARQLARQSLRTTSFASAPVRIAIASTPLARSPSSFRSLSSSTRRSAAAAAAAAAAKATPAHDDSHTPMAVLTEADLGRLVRQRNVGISAHIDSGKTTLTERVLFYTGRIKDIHEVRGRDAVGAKMDHMELEREKGITIQSAATYCSWKATPPTEKASVSGDAANVESKELMEKKQDFHINIIDTPGHVDFTIEVERALRVLDGAVLVLCAVSGVQSQTITVDRQMRRYSVPRISFINKMDRAGANPWRVIGQIRNKLKMPAAAVQIPIGAEDDFNGVIDLIRWKAVYNEGHKGIDIRETDEIPAEYLELAKQKRAELIEQLAEVDDEMTEMFIEEREPTIEELAAAIRRTTIRCQFSPVFLGSAIKNKGVQAMLDGVCSYLPNPAEVPATAMDMSSAATKKAAEEAAQAAGEDQEAAAEARKNAAPPVLPLSPASEAPLVGLAFKLEEGKYGQLTYMRVYQGTLKRGNLIFNARTGKKVKVPRLVRMHSNDMEDVDEIGAGEICAMFGVECSSGDTFTDGTTQLSMTSMFVPEPVISLAITPEGKESQNFSRALNRFQKEDPTFRVHVDKESNETIISGMGELHLEIYVERMRREYNVPCTTGKPRVAFRETIEKKATFAYTHKKQTGGAGQFGRVMGYIEPMEVDPETGVDTAFDNRVVGGSIPNGYISACEKGFYDALEKGALSGHAVTGVRFVLEDGAAHSVDSSELAFRLATAGAFREAYQKANPVILEPKMTVEVVAPIEFQGAVIGALNQRKGTISDTEVREDEFTLTAEVSLNDMFGYSSQLRGLTQGKGEFSMEYKCHTPVMMNIQKEMHEAYRKKQTEKK | Function: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Sequence Mass (Da): 92219
Sequence Length: 842
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Mitochondrion
|
P38732 | MITQTELDNCLQWAQNNGAFIDPKISFRITEDAGVSAFVNEKFSPKPDQALIRVPETLLITSQQALSEFSQAANERSLLNSVTQLYLSKLKFGTDAVHLKSFYKPYLDVLPLHLPQPYFWSTDEVMNLHGTDVYLTMRDTLNKLVKEWRMLFQALSIEHSSQDKQFLSLFQENKDSAVVPLEQFCAHINGCKLEDSEWNSFVAYLWSYCIFNSRAFPRVILGRAGTDRTNLNEGFLYPIVDLLNHKNDVPVRWEMNEQNELCFMSQTTTFSAQDELFNNYGNISNEKCLLNYGFWDSSNKFDFSRLTLKLPSTLVSGLPVDFNKSGNFVTDDGETTILQFSLKISEPLPPVLLALFAYLSKLKSEETPTVRSVLEGIDQLTSVVSQRLLFYKNFKIKTSSTQKLRPHVIKLIKLYYQDNKKILNATTEKLSVLQKKIYSNNKEFSLSFKTIFKNDKIFANSLLLVFGAINYEDLITKDCLNDALLLWIVKLINDKSNNQGGFIKQTFKEVSDSIVIEKEDVMEFLPFYKKYFPNLSERIPEIYSVGDWGIRQFIVADTAIDRLVWIRKSNKEPIFLMKKAYDLQI | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that monomethylates elongation factor 1-alpha (TEF1/TEF2) at 'Lys-30'.
Sequence Mass (Da): 67452
Sequence Length: 585
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
P38347 | MFDPLDLYTPDDIQVEALQFNLAEREPKDPCSPQRDEILTAVDEEESDDDDTIIDNLDLPSVKYAPPEVILCILILLKPDRQVNFNQETGKNKSVLEVCKSHGLEPDLLKRLLTWYTEEWPNKRLNSLEKICNKIPMLRFTVSKELLLGYYTSVLKKYNNSCGLNEEIIQELLKELSSRISENCGRTAQPSIVRYFELRNLSTSIPLHEPSLTADNLGWKTWGSSLILSQLVVDHLDYLHTTNVNMLANSDIKQIKVLELGAGTGLVGLSWALKWKELYGTENIEIFVTDLPEIVTNLKKNVSLNNLGDFVQAEILDWTNPHDFIDKFGHENEFDVILIADPIYSPQHPEWVVNMISKFLAASGTCHLEIPLRAKYAKEREVLKLLLKESDLKVVEERHSEGVDDWGAVKYLYRQIVRN | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that mono- and dimethylates elongation factor 2 (EFT1/EFT2) at 'Lys-613' and methylates elongation factor 3A (YEF3).
Sequence Mass (Da): 47977
Sequence Length: 419
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
P0CU27 | MVASRNPQTARFCWQYLQLEQSLDFPDGELLRDEAVQETIYQQLFAPNAPTPLPPARYRLRVLKELTSRIESAIEDWETHGISDNLMDAMAELVAQPLPSEAEAAQERCYVTYYLSLLEGGLEKPHITLLESRSLISASGTTGLRTWEAALHLGQFLSVNSGLVKDKRVLELGTGTGYLAVLCAKYLGTSHVIASDGSEEVVEKLSDNLFVNGLQDSDKVQPMELKWGHALLGTEEEHWNGGRKIDVVLGADITYDVSVIPALIATLEELVDLYPGISIIIAATERNRETYETFLAACGRRGFSVTPESFPVPSRAEQKGPFYKDGTPIHICQLRR | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates elongation factor 2.
Sequence Mass (Da): 37265
Sequence Length: 336
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
O14118 | MHGAPEFLTKVKQQYLQQVDLYRFQWVSKPTDWPILFNDYAQVFLSEIVTPSAYTRAFLKSYFRFLDSIDSGHNERNEALLYTYIESLSSTYIPPVQYSLGEYDILIRESRHVLLREGTTGARTWEAGMALAEYIYQHPVQSGMRVLELGAGTGLVSILCAKMGSIVLATDGDTKVCDGVRENARLNNCDINVKKLLWGVDPPEFSDIVFASDVTYDCDLRCLATTLTQIITINPNCKIILSASLRRQETFFNFLKLIQNLYARQLEVWDSPKILYYDSPPIVFYEVSK | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates elongation factor 2.
Sequence Mass (Da): 33051
Sequence Length: 289
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
P47163 | MNEDLFYDRLHQRCPGKYLLEELETSKSNDVLHASRFVCEMELVQKTNAYYCKTIVKMLLDHEWIFAKAFTIVNDGEDEIEIYDYLYEKYIKLLSTGKPDPMMKDVVRYRFDEDVKIKIEETPNLISAASTTGFRTWEAALYMGDFLIHKPLQELAPVQGQDDGKKKLNVLEVGAGTGIVSLVILQKYHEFVNKMYVTDGDSNLVETQLKRNFELNNEVRENEPDIKLQRLWWGSDRVPEDIDLVVGADVTYDPTILPDLCECLAECLALDRCKLCLLSATIRSESTVQLFSQECNKLGLKCTIVTSTEYDANNEIRAMKALQFKPLIAPIRIYKITKQ | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that mono-, di- and trimethylates elongation factor 2 (EFT1/EFT2) at 'Lys-509'.
Sequence Mass (Da): 39024
Sequence Length: 339
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q9P7Z3 | MSGLPESKLGTKQYWDNVYEREVSNFTEFNDEGEVWFGEEAEERIVQWLEDHISTSFREVSEAAPFRVLDLGTGNGHLLFRLLEEEDTLLPSPCQLVGVDYSEAAIVLAKNIARHRQFSDKVKFQQLDIIKDSKFCSKDWDLILDKGTFDAISLSGELLDGRPLNSVYVDRVRGMLSPNGIFLITSCNWTIQELEERFTKNGFIVHSTVPVPVFEFQGSTGSSTSVIAFQIDPSFNRK | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that mono- and dimethylates elongation factor 1-alpha at 'Lys-316'. May play a role in intracellular transport.
Sequence Mass (Da): 27011
Sequence Length: 238
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
P40516 | MKRSEKKSMSSALKNGIMERTQPEKVVQMQGTADLSTSKLGTKKYWDELYALELENFRRNPQDTGDCWFSDSDAEQKMIDFLVDNIGAYRISENASVVDLGTGNGHMLFELHQTEFQGKLVGIDYSEESVKLASNIAEATGVDNFISFQQADIFSGDWKPGKYDIVLDKGTLDAISLSGMKINGKLDVVDVYAGVVERILKKDGIFLITSCNFTQDELVKIIETDNLKMWKTIKYPVFQFGGVQGATICSVAFVKQN | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that mono- and dimethylates elongation factor 1-alpha (TEF1 and TEF2) at 'Lys-316'. May play a role in intracellular transport.
Sequence Mass (Da): 28690
Sequence Length: 257
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q5WRN3 | MSDTDDIPQLSADTLAALSMFQAEQQEKIEQLQSGIIEKIDEDWQLSQFWYDDETSRKLVAEGVAAALEGSEARPARIGCVSSPTLVKFFHETEEYKTGQIQLTLFEFDDRFGLKFPTEFVHYDYKHPTDLPAELLAKFDVIIADPPFLAAECLIKTAHSIRLLGKSDVKVLLCTGAIMEDYASRLMAMHRTSFEPRHANNLANDFSCFANYQTLTFC | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates elongation factor 1-alpha.
Sequence Mass (Da): 24660
Sequence Length: 218
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q86A24 | MSDSSDDEITLSKESLSALQDFYKSREVEQQDKFEISEDWQLSQFWYEEETSKFVANVIEQETIGGNVVVCLSTPSIYKVLHKNNNLLLNNNLFEYDKRFDVYGEKFHFYDYNNPEDGISEQLKGNVDYICLDPPFLSEECIEKVAKTIALLRKPTTRLLLLTGRIQWNNIQKYLPEMMICEFEPKHPRLQNDFFCCSNYHSKLLGLENKK | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates elongation factor 1-alpha.
Sequence Mass (Da): 24823
Sequence Length: 211
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q9VMH7 | MDDDISLPADTLAILNEFLLERSKREAEEENQIANKTGKDAQFEEDWQLSQFWYSTETKHALRDVVRKLLAERTEDSGDFSIALLSCPSLYKDIREIHDTVHIFEFDKRFEAYGTDFVHYDLNCVGSNPDYLKEHHQQYDLIVADPPFLSQECIAKTCEIITRLQRNQKESKVILCSGEVVEPWLTARLPVLKCSFRPEHERNLGNKFVSYANFNLDEYIENK | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates elongation factor 1-alpha.
Sequence Mass (Da): 26043
Sequence Length: 223
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
P53200 | MSDSDSDSDYELTLSANALAALEEFKREEQQHQEAFQKLYDETDEDFQKKKKEEGMKLFKEDWQLSQFWYSDDTAAILADAILEGADENTVIAIVSAPSVYAAIQKKPTNEIPTEHIYLFEFDKRFELLAGRDHFFFYDYNKPLDFSDEIKGKVDRLLIDPPFLNEDCQTKSSITAKCLLAPNDNSKTKKGVFKHRLISCTGERMSEVISKVYSDTRITTFLPEHSNGLSNEFRCYANFECSSWKFAS | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that trimethylates elongation factor 1-alpha (TEF1 and TEF2) at 'Lys-79' . Required for replication of Brome mosaic virus (BMV) .
Sequence Mass (Da): 28582
Sequence Length: 248
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
P53970 | MESIFGGFGDLVVPRPKEHLGQTDLSFGGKLLPALKICEDGGESGCGGKVWIAGELLCEYILEKSVDHLLSKTVNGTKQFKKVLELGSGTGLVGLCVGLLEKNTFHDGTKVYVTDIDKLIPLLKRNIELDEVQYEVLARELWWGEPLSADFSPQEGAMQANNVDLVLAADCVYLEEAFPLLEKTLLDLTHCINPPVILMAYKKRRKADKHFFNKIKRNFDVLEITDFSKFEHYLKERTHLFQLIRK | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates elongation factor 1-alpha (TEF1 and TEF2) at 'Lys-390'.
Sequence Mass (Da): 27738
Sequence Length: 246
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
P49778 | MISVNDFRTGLTIEVDGGIWRVVDFQHVKPGKGAAFVRSKLRNLRTGAIQEKTFRAGEKVAKAQIETKTMQYLYANGDQHVFMDTSSYEQLELSATQIEEELKYLLENMSVHIMMYQDETLGIELPNTVELKVVETEPGIKGDTASGGTKPAKTETGLVVNVPFFVNEGDTLVVNTSDGSYVSRA | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase (By similarity).
Sequence Mass (Da): 20468
Sequence Length: 185
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Cytoplasm
|
Q8A1F7 | MINAQDIKNGTCIRMDGKLYFCIEFLHVKPGKGNTFMRTKLKDVVSGYVLERRFNIGEKLEDVRVERRPYQFLYKEGEDYIFMNQETFDQHPIAHDLINGVDFLLEGAVLDVVSDASTETVLYADMPIKVQMKVTYTEPGMKGDTATNTLKPATVESGATVRVPLFISEGETIEIDTRDGSYVGRVKA | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Sequence Mass (Da): 21227
Sequence Length: 188
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Cytoplasm
|
A1UR93 | MKINGNEIRPGNVIEHQGSLWVAVKCNAVKPGKGGAFNQVELKNVIDGTKLNERFRAAETVEKVRLEQKDFTFLYQQGEALVFMDTESYEQLELQRDFVGDRAAFLQDGMTVTVELHEEKPLGISLPDQVTVTIAEADPAIKGQTVTSSYKPAILENGIRILVPPFVQAGERIIVDTNELTYIRRVSEKG | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Sequence Mass (Da): 21175
Sequence Length: 190
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Cytoplasm
|
B2KCP2 | MISTTDFKEGLIFENENGEIVEIVDYQHHRKSQARAVVRVKLRKLGSGSYVETSYRPEDKFKEVSVEKRPFMYLYSEGDMAHFMNNESYDQVAVPLDKLENQRKYLIENMECTGLYINDQLFDIVLPIKVVLTIKSTVPGVKGDTVSNLTKEAELETGVTIKVPLFINEGDKVIMDTRYCTYVERA | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Sequence Mass (Da): 21388
Sequence Length: 186
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Cytoplasm
|
B1GZJ0 | MISTSDFKNGTNILVDGEPYQIAWFQNHKPGKGGAVMRVKLRHLKKGGIIERTFKSGEKFKALTITRQKKRFLYKESNNFNFMDMDTYEQITVHPELLGKMVNFLKENLEVEAIYLENELIGIDLPVIIEMTIAEAEHGIKGDSVSNTTKTAKLETGADIHVPLFIKEGDRIKVDTRTGEYVERA | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Sequence Mass (Da): 21033
Sequence Length: 185
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Cytoplasm
|
Q2NAZ6 | MKISGVDIRPGNIIEYEGGIWKVAKIQHTQPGKGGAYMQVEMKNLQDGRKTNVRFRSADTVEKVRLDTQDYQFLYEDGDQLVFMDQDTYEQINLDSDLLGDARPFLQDGMTVQLELWEEKPISVQLPQQVEADIVEADAVVKGQTASSSYKPAVLDNGVRIMVPPHIESGTRIVVDVYEQTYVGKAG | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Sequence Mass (Da): 20967
Sequence Length: 187
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Cytoplasm
|
Q885R6 | MKTGKELKPGTVIRLENDPWLVQKAEFTKSGRNSAIMKTKLKNLLTGYKTEIVYSADDKLDDVILDRKEATLSFISGDTYTFMDTTDYTMYELNAEDIESVLPFVEEGMTDVCEAVFFDERLVSVELPTTIVRQVDYTEGSARGDTSGKVMKPAKLKNGTELSVADFIEIGDMIEIDTREGGSYKGRAK | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Sequence Mass (Da): 21138
Sequence Length: 189
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Cytoplasm
|
Q8D2R7 | MIIYYSANQSKSGLKILLKNEPCLILENQFVKPGKGQPFNRIKIKKLISGKIFTKIFKSNEKLIYADVLDVKVKSLYKDKKYWNFIKKENFEQFKISKKNLGEKYKWIIEQLECIVTFWDENPINITLPRFVDIKVCNANFDIKGDTIKSGNKYIILTTGAIIKAPIFIRSEEIVRVDTNLGEYVSRIK | Function: Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-35 is required for alleviation.
PTM: May be beta-lysylated on the epsilon-amino group of Lys-35 by the combined action of EpmA and EpmB, and then hydroxylated on the C5 position of the same residue by EpmC (if this protein is present). Lysylation is critical for the stimulatory effect of EF-P on peptide-bond formation. The lysylation moiety may extend toward the peptidyltransferase center and stabilize the terminal 3-CCA end of the tRNA. Hydroxylation of the C5 position on Lys-35 may allow additional potential stabilizing hydrogen-bond interactions with the P-tRNA.
Sequence Mass (Da): 22050
Sequence Length: 189
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Cytoplasm
|
Q73FP5 | MAERANDIRPGQVLEHNGGLFLVVGIMHTQPGKGGAYIQAEMKNIKTGAKHYERFRSDATIRRAILDEEEYVYLFTEGNIVNLMHPSNYEQITINLDLLGEKKIYLQDNMKIKVVAYQDKIISAHVPDYVTLAVKETESVIKGQTATASYKPAILENGMRVNVPQFIKEEDKIVVYTPGDSYYERVKE | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Sequence Mass (Da): 21353
Sequence Length: 188
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Cytoplasm
|
Q0C7P6 | MQLTQLLALALSLATSEAAYKGFNYGDKKPDGSSKYQADFASEFETAQNLVGAPGFTSARLYTMIQAGTANDPISAIPAAIAQNTSLLLGLWASGNNMNNELTALKAAISQYGEDLSKLVVGISVGSEDLYRNSVLGQKVNAGVGVDPHVLASYIEEVRSTISGTPLSGAPLGHVDTWNDWVNGSNAAVIDAVDWVGFDGYPYFQNTMANSIDDAKALFNEAVAKTKSAAGNKEVWITETGWPVSGKTENLAVASIPNAKRFWDEVGCPLFDNTNTWWYTLQDAFGASVPNPSFGIVGSTLTTQPLFDLSCSKSNTTSSSAIASPTSTAAAAGGVAGGSTGSASGSSTGTGSSSGSGSNSNTGAASGAVGAADRETSGTSGSANTNGTSGSGSGSNSTSGHGSNVTVPTRPTSVSNVSPSKSSSALFTGAATSMGASPSSVGNVGPSKSSGAASPSSTTMFTGAATSVSAPVVHVVLLALMMVIAA | Function: Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation and also function biosynthetically as a transglycosylase (By similarity).
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By similarity).
Location Topology: Lipid-anchor
Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Sequence Mass (Da): 48753
Sequence Length: 486
Subcellular Location: Cell membrane
EC: 3.2.1.39
|
Q5AUT0 | MFTKTQILALALSIASAEAVSKGFNYGANKPDGTLKVQADFEAEFRTAKNLETTSGFNSARLYTMIQGTGSTPISAIPAAIAEETTLLLGLWASGGNMDNEIAALKAAINQYGDEFAKLVVGISVGSEDLYRNSEIGVQANAGIGIEPEELVSYIQRVREAIAGTALSGAPIGHVDTWNAWTNGSNAAVAEAVDWLGFDGYPFFQNTMQNSIDDAKALFDESVQKTKAVAGNKEVWITETGWPVSGDSQNLAIASVENAKQFWDEVGCPLFDNVNTWWYILQDASGSSVPNPSFGIVGNTLSTTPLFDLSCSASSKKNSSSASASASGSSAQSTGFVSTTKPAASPSGSSGLGHGGSLGSSGSFSGGHYAGVGSSSVIASPSATPSGSAVPGSSSGPGSSSGSASGSSSGFGSGAAADSTSGTSTSGDSTSSTSATPADFTGAGSRLSGSIFGAAMLVAALAVAL | Function: Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation and also function biosynthetically as a transglycosylase.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By similarity).
Location Topology: Lipid-anchor
Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Sequence Mass (Da): 46685
Sequence Length: 465
Subcellular Location: Cell membrane
EC: 3.2.1.39
|
A1DJ47 | MQFTQLVALALALATSEAAHQGFNYGNTKSDGSAKSQSDFQAEFSTAKNLVGTSGFTSARLYTMIQGGTANTPISAIPAAVAEETSLLLGLWASGGNFANEIAALKTAIADYGDDLAKLVVGISVGSEDLYRNSVDGVKAKAGLGTNPDEIVSYINQVRSTIAGTKLSGAPIGHVDTWTAWVNGSNSAVIDACDWLGFDGYPYFQNTMANSISDAKALFDESVAKTEAVAKGKEVWITETGWPVSGNTENLAVANLANAKTYWDEVGCPLFGKTNTWWYILQDANPVTPNPSFGIVGSTLSTTPLFDLSCSASSSAAASSTAVPSASSVAGAKASGFATAAASSGAAGSAKPTFTVGKGPGGSYNGTGFWNSTSSARPSSTAISGSSSGSASGSSGSSGSGASGASGQSSSSTGSSSAPSSSNILSNAASGLSGSIFGAVVAVCLALAAL | Function: Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation and also function biosynthetically as a transglycosylase (By similarity).
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By similarity).
Location Topology: Lipid-anchor
Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Sequence Mass (Da): 44878
Sequence Length: 450
Subcellular Location: Cell membrane
EC: 3.2.1.39
|
Q5BCX8 | MKFSSVLALAASAKLVASHATVFAVWINDEDQGLGNTADGYIRTPPNNSPVTDVTSTDLTCNVNGDQAAAKTLEVAAGDKITFEWHHNSRDSSDDIIADSHKGPVLVYMAPTEAGSAGKNWVKIYEDGYNDGTWAVDTLIANKGKHSVTVPDVPAGNYLFRPEIIALHEGNREGGAQLYMECVQFKVTSDGTTQLPEGVSLPGAYTATDEGILFDIYSSFDSYPIPGPAVWDGASSGSGSSGSGSSSSAAATSSAEKTATSTTAAATTTAVATSTSSATQVQPTSVATFTTSVRPTTSAAPTTSAPTSSAAPTGGTGTGSIQIYQQCGGMNYKGATGCASGLTCKQWNPYYHQCVQA | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 36732
Sequence Length: 357
Domain: Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.
Subcellular Location: Secreted
EC: 3.2.1.4
|
Q9GZT9 | MANDSGGPGGPSPSERDRQYCELCGKMENLLRCSRCRSSFYCCKEHQRQDWKKHKLVCQGSEGALGHGVGPHQHSGPAPPAAVPPPRAGAREPRKAAARRDNASGDAAKGKVKAKPPADPAAAASPCRAAAGGQGSAVAAEAEPGKEEPPARSSLFQEKANLYPPSNTPGDALSPGGGLRPNGQTKPLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQLVSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKINGRTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKYLTGEKGVRVELNKPSDSVGKDVF | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized via a LXXLAP motif.
PTM: S-nitrosylation inhibits the enzyme activity up to 60% under aerobic conditions. Chelation of Fe(2+) has no effect on the S-nitrosylation. It is uncertain whether nitrosylation occurs on Cys-323 or Cys-326.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[hypoxia-inducible factor alpha subunit] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[hypoxia-inducible factor alpha subunit]
Sequence Mass (Da): 46021
Sequence Length: 426
Domain: The beta(2)beta(3) 'finger-like' loop domain is important for substrate (HIFs' CODD/NODD) selectivity.
Subcellular Location: Cytoplasm
EC: 1.14.11.29
|
Q96KS0 | MDSPCQPQPLSQALPQLPGSSSEPLEPEPGRARMGVESYLPCPLLPSYHCPGVPSEASAGSGTPRATATSTTASPLRDGFGGQDGGELRPLQSEGAAALVTKGCQRLAAQGARPEAPKRKWAEDGGDAPSPSKRPWARQENQEAEREGGMSCSCSSGSGEASAGLMEEALPSAPERLALDYIVPCMRYYGICVKDSFLGAALGGRVLAEVEALKRGGRLRDGQLVSQRAIPPRSIRGDQIAWVEGHEPGCRSIGALMAHVDAVIRHCAGRLGSYVINGRTKAMVACYPGNGLGYVRHVDNPHGDGRCITCIYYLNQNWDVKVHGGLLQIFPEGRPVVANIEPLFDRLLIFWSDRRNPHEVKPAYATRYAITVWYFDAKERAAAKDKYQLASGQKGVQVPVSQPPTPT | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Prolyl hydroxylase that mediates hydroxylation of proline residues in target proteins, such as ATF4, IKBKB, CEP192 and HIF1A . Target proteins are preferentially recognized via a LXXLAP motif . Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins . Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A . Also hydroxylates HIF2A . Has a preference for the CODD site for both HIF1A and HIF2A . Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex . Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes . EGLN2 is involved in regulating hypoxia tolerance and apoptosis in cardiac and skeletal muscle . Also regulates susceptibility to normoxic oxidative neuronal death . Links oxygen sensing to cell cycle and primary cilia formation by hydroxylating the critical centrosome component CEP192 which promotes its ubiquitination and subsequent proteasomal degradation . Hydroxylates IKBKB, mediating NF-kappa-B activation in hypoxic conditions . Also mediates hydroxylation of ATF4, leading to decreased protein stability of ATF4 (By similarity).
PTM: Ubiquitinated by SIAH1 and/or SIAH2 in response to the unfolded protein response (UPR), leading to its degradation.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[protein] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[protein]
Sequence Mass (Da): 43650
Sequence Length: 407
Domain: The Beta(2)beta(3) 'finger-like' loop domain is important for substrate (HIFs' CODD/NODD) selectivity.
Subcellular Location: Nucleus
EC: 1.14.11.-
|
Q91YE2 | MDSPCQPQALNQALPQLPGSVSESLESSRARMGVESYLPCPLLPAYHRPGASGEASAGNGTPRTTATATTTTASPLREGFGGQDGGELWPLQSEGAAALVTKECQRLAAQGARPEAPKRKWAKDGGDAPSPSKRPWARQENQEAKGESGMGCDSGASNSSSSSSNTTSSSGEASARLREEVQPSAPERLALDYIVPCMRYYGICVKDNFLGAVLGGRVLAEVEALKWGGRLRDGQLVSQRAIPPRSIRGDQIAWVEGHEPGCRSIGALMAHVDAVIRHCAGRLGNYVINGRTKAMVACYPGNGLGYVRHVDNPHGDGRCITCIYYLNQNWDVKVHGGLLQIFPEGRPVVANIEPLFDRLLIFWSDRRNPHEVKPAYATRYAITVWYFDAKERAAARDKYQLASGQKGVQVPVSQPTTPT | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Prolyl hydroxylase that mediates hydroxylation of proline residues in target proteins, such as ATF4, IKBKB, CEP192 and HIF1A . Target proteins are preferentially recognized via a LXXLAP motif (By similarity). Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins . Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A . Also hydroxylates HIF2A . Has a preference for the CODD site for both HIF1A and HIF2A . Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex . Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes . EGLN2 is involved in regulating hypoxia tolerance and apoptosis in cardiac and skeletal muscle . Also regulates susceptibility to normoxic oxidative neuronal death . Links oxygen sensing to cell cycle and primary cilia formation by hydroxylating the critical centrosome component CEP192 which promotes its ubiquitination and subsequent proteasomal degradation (By similarity). Hydroxylates IKBKB, mediating NF-kappa-B activation in hypoxic conditions (By similarity). Also mediates hydroxylation of ATF4, leading to decreased protein stability of ATF4 .
PTM: Ubiquitinated by SIAH1 and/or SIAH2 in response to the unfolded protein response (UPR), leading to its degradation.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[protein] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[protein]
Sequence Mass (Da): 45109
Sequence Length: 419
Domain: The Beta(2)beta(3) 'finger-like' loop domain is important for substrate (HIFs' CODD/NODD) selectivity.
Subcellular Location: Nucleus
EC: 1.14.11.-
|
Q7QBW3 | MSDTISCTPETATFEAPQLQFNEDGWGPCELPDAFKDIPYQPFSKSDRLGKISDWTGTAQTDKKFSNKYASQFGGGSQYAYFHEEDETTFHLVDSARIQKPPHQRGRFRGNMRNNRSGRGRGARGGVQVGGMTTLSKSANKMRDQRRGTTRKWGMRGPPPKIRDASVTVRPDWVTIEEMDFPRLAKLSLPSVKEGEDIMTCGTLEYYDKTYDRVNVKNERPLQSVDRIFHTVTTTDDPIIRQLSKTHGNVYATDAILATIMCCTRSNYSWDIVIDKIGGKLFMDKRDNTEFDLLTVNETASEPPQEDGNSLNSPRNLAIEATFINHNFSQQVLKSGEKEPKYKFQQPNPFIGDDEDGEVASVAYRYRKWDLNNGITLVARCEHDAVLKMPQGDTQFLTIKALNEWDSKIANAVEWRQKLDTQRGAILANELRNNSCKLAKWTVQALLAGSDQLKFGYVSRAHVRDSSKHVILGTQQFKPQEFANQINLSMDNAWGILRCIIDICMKQKDGKYLIMKDPNKPMVRLYDIPDNTFDSDGEGEEGDDGEAFQPMYGYSAAASTSANVTAAQSNTSATVPDQSEKASA | Function: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.
Sequence Mass (Da): 65600
Sequence Length: 584
Domain: The RNA gate region regulates mRNA cap recognition to prevent promiscuous mRNA-binding before assembly of eif3d into the full eukaryotic translation initiation factor 3 (eIF-3) complex.
Subcellular Location: Cytoplasm
|
P56820 | MVTEAFEFVAVPFNSDGWGPPDASDVSSSASPTSVAAANLLPNVPFASFSRSDKLGRVADWTRNLSNPSARPNTGSKSDPSAVFDFSAFAIDEGFGLASSGGNPDEDAAFRLVDGKPPPRPKFGPKWRFNPHHNRNQLPQRRDEEVEAKKRDAEKERARRDRLYNNNRNNIHHQRREAAAFKSSVDIQPEWNMLEQIPFSTFSKLSYTVQEPEDLLLCGGLEYYNRLFDRITPKNERRLERFKNRNFFKVTTSDDPVIRRLAKEDKATVFATDAILAALMCAPRSVYSWDIVIQRVGNKLFFDKRDGSQLDLLSVHETSQEPLPESKDDINSAHSLGVEAAYINQNFSQQVLVRDGKKETFDEANPFANEGEEIASVAYRYRRWKLDDNMHLVARCELQSVADLNNQRSFLTLNALNEFDPKYSGVDWRQKLETQRGAVLATELKNNGNKLAKWTAQALLANADMMKIGFVSRVHPRDHFNHVILSVLGYKPKDFAGQINLNTSNMWGIVKSIVDLCMKLSEGKYVLVKDPSKPQVRIYEVPPDAFENDYVEEPLPEDEQVQPTEENTEGAEASVAATKETEEKKADDAQA | Function: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.
Sequence Mass (Da): 66725
Sequence Length: 591
Domain: The RNA gate region regulates mRNA cap recognition to prevent promiscuous mRNA-binding before assembly of eif3d into the full eukaryotic translation initiation factor 3 (eIF-3) complex.
Subcellular Location: Cytoplasm
|
Q3T122 | MAKFMTPVIQDNPSGWGPCAVPEQFRDMPYQPFSKGDRLGKVADWTGATYQDKRYTNKYSSQFGGGSQYAYFHEEDETSFQLVDTARTQKTAYQRNRMRFAQRNLRRDKDRRNMLQFNLQTLPKSAKQKERERIRLQKKFQKQFGVRQKWDQKSQKPRDSSVEVRSDWEVKEEMDFPQLMKMRYLEVSEPQDIECCGALEYYDKAFDRITTRSEKPLRSIKRIFHTVTTTDDPVIRKLAKTQGNVFATDAILATLMSCTRSVYSWDIVVQRVGSKLFFDKRDNSDFDLLTVSETANEPPQDEGNSFNSPRNLAMEATYINHNFSQQCLRMGKERYNFPNPNPFVEDDMDKNEIASVAYRYRRWKLGDDIDLIVRCEHDGVMTGANGEVSFINIKTLNEWDSRHCNGVDWRQKLDSQRGAVIATELKNNSYKLARWTCCALLAGSEYLKLGYVSRYHVKDSSRHVILGTQQFKPNEFASQINLSVENAWGILRCVIDICMKLEEGKYLILKDPNKQVIRVYSLPDGTFSSDEDDEEEEEEEEEEEEEEA | Function: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, a complex required for several steps in the initiation of protein synthesis of a specialized repertoire of mRNAs. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. In the eIF-3 complex, EIF3D specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.
Sequence Mass (Da): 63931
Sequence Length: 548
Domain: The RNA gate region regulates mRNA cap recognition to prevent promiscuous mRNA-binding before assembly of eif3d into the full eukaryotic translation initiation factor 3 (eIF-3) complex.
Subcellular Location: Cytoplasm
|
P30642 | MALPKFELLSLADNTVGWGPLASSSSADEPVPFQQFNKADRIGRVADWIGVDRFYRRGNERYNERVYGSAANAGSQFDYIHGMDEHNFQLVDTSKPMARNPQRNFRVRQMHLRKMMQKENEKREMVNQSTNLRMKRSIAKEQQRAFKMWQRRGGNARQGQRGQGGRFGGDRPKERLPSVQVRPEWVVLEEMNLSAFSKLALPNIPGGDDIGDHQYGSLQYYDKTIDRVSVKNSIPLQRCAGVFYNVTTTEDPVIQELAQGGAGNVFGTDIILATLMTAPRSVYSWDIVAYRVGDKLFFDKRNTRDILNPVETLTVSETSAEPPSFDGNGINNAKDLATEAFYINQNFRRQVVKRNDAGFTFKNARAPFEDEETGESGTAYKYRKWNLGNGVDGKPVELVCRTELDGVIHGLGNETQTLTIKAFNEWDSTQSGGVDWRTKLDVQKGAVMATEIKNNSAKVAKWTLQALLAGSDTMKLGYVSRNNARSTQNHSILLTQYVKPTEFASNIALNMDNCWGILRCVIDSCMKQKPGKYLLMKDPQSPVIRLYSLPEGTFESERESSDEENSDDDQ | Function: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.
Sequence Mass (Da): 64289
Sequence Length: 570
Domain: The RNA gate region regulates mRNA cap recognition to prevent promiscuous mRNA-binding before assembly of eif3d into the full eukaryotic translation initiation factor 3 (eIF-3) complex.
Subcellular Location: Cytoplasm
|
Q9C5Z2 | MATMARSFLQAISKDEAVAPPLRVVQIEGLAVLKIIKHCKEFSPTLVTGQLLGLDVGSVLEVTNCFPFPVRDDDEEIEADGANYQLEMMRCLREVNVDNNTVGWYQSTVLGSYQTVELIETFMNYQENIKRCVCIIYDPSKADLGVLALKALKLSDSFMELYRGGNFTGEKLREKNFSWMDIFEEIPIKVSNSALVSAFMTELETDTPVSQGDYDRLHSSTTPFLENNMEFLIKCMDDLSMEQQKFQYYYRNLSRQQAQQQAWLQKRRTENMARKSAGEEPLPEEDPSNPIFKAIPEPSRLESFLITNQVSNFCGQINGVAGQNFSRLYLTKALHDN | Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation (Potential). Regulates translation initiation of specific 5' mRNAs harboring multiple upstream open reading frames (uORFs) in their 5' leader sequence (e.g. BETA-OHASE 2 and LHY) .
PTM: In response to auxin (NAA), phosphorylated at Ser-178 by ATPK1 and binds to polysomes via TOR signaling. This phosphorylation is repressed by Torin-1.
Sequence Mass (Da): 38373
Sequence Length: 337
Subcellular Location: Cytoplasm
|
P26378 | MEWNGLKMIISTMEPQVSNGPTSNTSNGPSSNNRNCPSPMQTGATTDDSKTNLIVNYLPQNMTQEEFRSLFGSIGEIESCKLVRDKITGQSLGYGFVNYIDPKDAEKAINTLNGLRLQTKTIKVSYARPSSASIRDANLYVSGLPKTMTQKELEQLFSQYGRIITSRILVDQVTGVSRGVGFIRFDKRIEAEEAIKGLNGQKPSGATEPITVKFANNPSQKSSQALLSQLYQSPNRRYPGPLHHQAQRFRLDNLLNMAYGVKRLMSGPVPPSACPPRFSPITIDGMTSLVGMNIPGHTGTGWCIFVYNLSPDSDESVLWQLFGPFGAVNNVKVIRDFNTNKCKGFGFVTMTNYDEAAMAIASLNGYRLGDRVLQVSFKTNKAHKS | Function: RNA-binding protein that is involved in the post-transcriptional regulation of mRNAs . Plays a role in the regulation of mRNA stability, alternative splicing and translation . Binds to AU-rich element (ARE) sequences in the 3' untranslated region (UTR) of target mRNAs, including GAP43, VEGF, FOS, CDKN1A and ACHE mRNA . Many of the target mRNAs are coding for RNA-binding proteins, transcription factors and proteins involved in RNA processing and/or neuronal development and function (By similarity). By binding to the mRNA 3'UTR, decreases mRNA deadenylation and thereby contributes to the stabilization of mRNA molecules and their protection from decay . Also binds to the polyadenylated (poly(A)) tail in the 3'UTR of mRNA, thereby increasing its affinity for mRNA binding . Mainly plays a role in neuron-specific RNA processing by stabilization of mRNAs such as GAP43, ACHE and mRNAs of other neuronal proteins, thereby contributing to the differentiation of neural progenitor cells, nervous system development, learning and memory mechanisms . Involved in the negative regulation of the proliferative activity of neuronal stem cells and in the positive regulation of neuronal differentiation of neural progenitor cells (By similarity). Promotes neuronal differentiation of neural stem/progenitor cells in the adult subventricular zone of the hippocampus by binding to and stabilizing SATB1 mRNA (By similarity). Binds and stabilizes MSI1 mRNA in neural stem cells (By similarity). Exhibits increased binding to ACHE mRNA during neuronal differentiation, thereby stabilizing ACHE mRNA and enhancing its expression . Protects CDKN1A mRNA from decay by binding to its 3'-UTR (By similarity). May bind to APP and BACE1 mRNAS and the BACE1AS lncRNA and enhance their stabilization . Plays a role in neurite outgrowth and in the establishment and maturation of dendritic arbors, thereby contributing to neocortical and hippocampal circuitry function (By similarity). Stabilizes GAP43 mRNA and protects it from decay during postembryonic development in the brain . By promoting the stabilization of GAP43 mRNA, plays a role in NGF-mediated neurite outgrowth (By similarity). Binds to BDNF long 3'UTR mRNA, thereby leading to its stabilization and increased dendritic translation after activation of PKC (By similarity). By increasing translation of BDNF after nerve injury, may contribute to nerve regeneration (By similarity). Acts as a stabilizing factor by binding to the 3'UTR of NOVA1 mRNA, thereby increasing its translation and enhancing its functional activity in neuron-specific splicing . Stimulates translation of mRNA in a poly(A)- and cap-dependent manner, possibly by associating with the EIF4F cap-binding complex (By similarity). May also negatively regulate translation by binding to the 5'UTR of Ins2 mRNA, thereby repressing its translation (By similarity). Upon glucose stimulation, Ins2 mRNA is released from ELAVL4 and translational inhibition is abolished (By similarity). Also plays a role in the regulation of alternative splicing . May regulate alternative splicing of CALCA pre-mRNA into Calcitonin and Calcitonin gene-related peptide 1 (CGRP) by competing with splicing regulator TIAR for binding to U-rich intronic sequences of CALCA pre-mRNA .
PTM: Methylated by CARM1, which leads to reduced RNA-binding activity and enhanced interaction with SMN . Methylation at Arg-248 by CARM1 weakens protective binding to the 3'UTR of CDKN1A mRNA and down-regulates CDKN1A protein expression, thereby maintaining cells in a proliferative state (By similarity). Methylation is inhibited by NGF, which facilitates neurite outgrowth (By similarity).
Sequence Mass (Da): 42398
Sequence Length: 385
Domain: The RRM 3 domain is required for binding to poly(A) RNA, for the association with polysomes and with the EIF4F cap-binding complex and for the stimulation of translation (By similarity). The RRM 1 and RRM 2 domains may contribute to polysome association and stimulation of translation (By similarity).
Subcellular Location: Cytoplasm
|
O94533 | MFQYEALHVGCNRIPTAATWSSNLGLIYGAERLIAVADPFKEINYLMAGHSGRINCVCELATNSEYRSPFILSGASDKTLRLWQLEEEYFTCIKTIELEATVNCLCVNENLVVCGCSNSSCIVYSWNAEQRNLTEISRFTCSEIIPLEFAIVKLDHGIILTVCGSSKKIMVYGSDSAISSFKLKAVLRGHLDWVRTLSFKKTSGSTATLASGSQDRYIRLWNISLWGSEDEKVSEEFFESVLSNKPVRFTLGKIDLKIVFDALLMGHEDWVMSVDWHPTKEMILSSSADSSMIVWEPDTNTGIWVVTGRMGEMASSHGSTTATGSAGGFWGGLWNPNGNCVVCWGRTGGWRLWKQDAGQWLQLPSISGHTKSVKGVAWDPEGKFYLSAGTDQTTRLFARFKKDNAWHEMARPQIHGYDLTSISCMPSRIGFLSCADEKVSRVFKFPKTIVRLLYRLCDTNIGEESLPDAANVPLLGLSNKATTASETGTVNAEEVQTPVADVIGSLNHPPFEEHLQRLLLFPEVEKLFGHGYEVYACAISNNGNIAATSCKSQTPEHAVIRLYETQSWNQQQVLKGHSLTVTTIKFSPDDRYILSAGRDRLVCLHEQAENLLDYNNFASIKAHSRIIWDASWAPKEMGYFFATASRDKFVKFWKINDNKKICDVAALQFSDAVTAVDFAPFFHNDELLLAVGTEAGKIFIWRCPRENLTKWYPTRLPDHMAPMESINQILWKPTFETMGLYSLLIAGEDTSVRLLNVTLG | Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) . The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs .
Sequence Mass (Da): 84949
Sequence Length: 760
Domain: Folds into a two seven-bladed beta-propeller structure which is required for elongator complex assembly.
Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Subcellular Location: Cytoplasm
|
Q5EBD9 | MSAPIVQLAHAAFSVNRCPSCVSWSRTGILACATCHSIALYDPQKNVVISTLNGHTGRVNCVHWVQKNDCSAETELVSGGSDKKVIIWAIEKNKCEQPVAAEGHTEVVNAVHAVYTQRSENELLIVSAASDCTVRLWLRRNVKTECLQTLSFGKGFVLDVCISFLPGSLVPVLACGADDSRIHLYVLQNEQFEKTQVLHGHEDWIRGVEWAVTGQNLFLASCAQDCLIRIWKIFRKTAKENSKTEDENSIKLKENIFKVKEKDTETSYAVTLETVLTGHENSIYAVHWQPSFSRDGSIVQPMSLLSASMDKTMILWEPDEESGVWLEQVRVGEVGGNTLGFLGCQFSPDKSMILAHAFHGALHLWSRAPNKQNEWIPMVIISGHFDSVQDMRWDPDGQFVITVSADQTTRLFGPWKKKGQSHVTWHEIARPQIHGYDMQCLAMIGRFQFVSGADEKVLRVFAAPRNFIENFSNISCISVEKLLLNEDTNLPEGATVPALGLSNKAVFHGEILIQSTQEEGKYNSVSEQYSQPNFQPLNLTEPPTEDHLLQNTLWPEVQKLYGHGYEIFAVACNSAKTVIASACKASKREHAAIILWSTTSWKQLQSLSYHNLTVTQMAFSPDDEFLLVVSRDRNWSLWKKQEGIPEQTEPTFTLYASTDKNSCVHSRIIWACDWTPDSKYFVTGSRDKKVIVWGDCSLPSMNEEKSSALIRPCSSLLDTGDSITAVSVSQVLALDGSYIIAVGLDCGIIQLYKWKHSGTVNDWLKCLAMDQSLLSHTLTVKQLCWRSCLGRAGHDDRDNGDWIQLASCGADHCVKIFDVYRKAL | Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). The elongator complex catalyzes the formation of carboxymethyluridine in the wobble base at position 34 in tRNAs.
Sequence Mass (Da): 92123
Sequence Length: 824
Domain: Folds into a two seven-bladed beta-propeller structure which is required for elongator complex assembly.
Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Subcellular Location: Cytoplasm
|
P42935 | MVECITPEAIFIGANKQTQVSDIHKVKKIVAFGAGKTIALWDPIEPNNKGVYATLKGHEAEVTCVRFVPDSDFMVSASEDHHVKIWKFTDYSHLQCIQTIQHYSKTIVALSALPSLISVGCADGTISIWRQNIQNDEFGLAHEFTIKKGFFYPLCLSLSKVEEKKYLLAIGGTNVNVFIASFILSDSGIEKCRVVAELEGHEDWVKSLAFRHQETPGDYLLCSGSQDRYIRLWRIRINDLIDDSEEDSKKLTLLSNKQYKFQIDDELRVGINFEALIMGHDDWISSLQWHESRLQLLAATADTSLMVWEPDETSGIWVCSLRLGEMSSKGASTATGSSGGFWSCLWFTHERMDFFLTNGKTGSWRMWATKDNIICDQRLGISGATKDVTDIAWSPSGEYLLATSLDQTTRLFAPWIYDASGRKREIATWHEFSRPQIHGYDMICVETVTDTRFVSGGDEKILRSFDLPKGVAGMLQKFVGIQFEEKSEMPDSATVPVLGLSNKAGEDDANEDDEEEEGGNKETPDITDPLSLLECPPMEDQLQRHLLWPEVEKLYGHGFEITCLDISPDQKLIASACRSNNVQNAVIRIFSTENWLEIKPALPFHSLTITRLKFSKDGKFLLSVCRDRKWALWERNMEDNTFELRFKNEKPHTRIIWDADWAPLEFGNVFVTASRDKTVKVWRHQKEPADDYVLEASIKHTKAVTAISIHDSMIREKILISVGLENGEIYLYSYTLGKFELITQLNEDITPADKITRLRWSHLKRNGKLFLGVGSSDLSTRIYSLAYE | Function: Component of the elongator complex, a multiprotein complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) . The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs . It functions as a gamma-toxin target (TOT); disruption of the complex confers resistance to Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin) . May also be involved in sensitivity to Pichia inositovora toxin . ELP2 binds to microtubules . Independently, ELP2 may be involved in polarized exocytosis .
Sequence Mass (Da): 89411
Sequence Length: 788
Domain: Folds into a two seven-bladed beta-propeller structure which is required for elongator complex assembly and association with microtubules.
Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Subcellular Location: Cytoplasm
|
Q23651 | MDQKGSQRALLAQTINEIVKLLIEAHNQKKDVNLNRLKCIVAQKNGLSFQPKLVDIIAGVPSDYKDSLLPKLKAKPVRTASGIAVVAVMSKPHRCPHINFTGNICVYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYNPYLQTRGRLNQLMQLGHSVDKVEFIVMGGTFMSLPEDYRDFFIRNLHDALSGHTSASVEEAVAYSERSKMKCIGITIETRPDYCLPRHLNDMLLYGCTRLEIGVQSTYEDVARDTNRGHTVKSVCETFHMAKDTGYKVVIHMMPDLPNVGLERDKEQFLELFESPAFRPDGLKLYPTLVIRGTGLYELWKTGRYQSYPPSVLVDLIATILSLVPPWTRVYRVQRDIPMPLVSSGVEHGNLREHAMAKMKELGLKCRDVRTREVGIQEIHNKVRPEDVELIRRDYTANGGWETFISYEDPKQDILIGLLRLRKISDKAHRPELKGNVSVVRELHVYGSVVSVADRDPKKFQHQGYGSLLMEEAERIAREEHGSDKIAVISGVGTREYYRKLGYELDGPYMSKMLDSAAA | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalytic tRNA acetyltransferase subunit of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). In the elongator complex, acts as a tRNA uridine(34) acetyltransferase by mediating formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity).
Catalytic Activity: acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in tRNA = 5'-deoxyadenosine + 5-(carboxymethyl)uridine(34) in tRNA + CoA + 2 H(+) + L-methionine
Sequence Mass (Da): 61910
Sequence Length: 547
Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
EC: 2.3.1.-
|
A0A1C7D1B7 | MKKLSRTISGVTPVAVMTKPLPCPGKCIYCPTFAATPQSYTPESPAVLRAKSCEYQAYKQVALRLRIIQDMGHPTDKVELIIMGGTFLSADITYQYGFIKDCYDALNGVVAGSLEEAKTINETAQHRCVGLCIETRPDICGKAEIQRMIDFGTTRVELGVQMLDDDIYKLVERGHRVSDVAEATCLLREYGLKVHYHWMPGLPGSSPEKDLALSRMVFEDPRFCPDGLKLYPTMVVEGTILEQWWKEGRYTPYPNGTMTGLIADIKALVPPYVRISRVLRDIPAVFISAGLKDSLRDGVRQILESRHQKCRCIRCREYGHRQRKGQTSGEPTLRRLDYPASGGKEIFLSFEDASDTLYGLLRLRIPCASLPVLGQKYGAKTGLVRELHVYGTELSLGEQGDQSAQHRGLGRKLLAEAECLARDEFGLDSLAILSGVGAREYYRSLGYELVAGYMCKHLD | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs . The proposed mechanism is the following: (i) recruits S-adenosyl-L-methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'-dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule. Does not show protein lysine acetyltransferase activity (By similarity).
Catalytic Activity: acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in tRNA = 5'-deoxyadenosine + 5-(carboxymethyl)uridine(34) in tRNA + CoA + 2 H(+) + L-methionine
Sequence Mass (Da): 51188
Sequence Length: 459
Pathway: tRNA modification.
EC: 2.3.1.-
|
Q1ZXC6 | MSLMNDPRPVSKKAGAKPVYGKNTPQFTKTVGEIVNALINAYKEGKKVNLLKIKTELAAKNSLSDQPKSVDIISAIPESYKNTLLPLLKAKPVRTASGIAVVAVMCKPHRCPHLAMTGNICVYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYNPFLQTRHRIDQLKRLGHNVEKVEFIIMGGTFMSLPSDYRDYFIRNLHDALSGHTSNNVAEAVKYSEQSNVKCVGITIETRPDHCLKLHLSNMLTYGCTRLEIGVQSVFEDIARDTNRGHTVRAVLESFQLAKDSGFKVVAHMMPDLPNMGMERDIYGFMEFFENPAFRADGLKIYPTLVIRGTGLYELWKTGTYKNYSPDSLVDLIAKVLALVPPWTRIYRIQRDIPMPLVTSGVEYGNLRELCLARMKDFGTKCRDVRTREVGIQEVHHKIKPDQVELIRRDYVANGGWETFLSFEDPKQDILIGLLRLRKCSETSFRPELKENCSIVRELHVYGSVVGIHNRDPTKFQHQGYGTLLMEEAERIAREEHGSIKLAVIAGVGTRHYYRKLGYELDGVYVSKYLG | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalytic tRNA acetyltransferase subunit of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). In the elongator complex, acts as a tRNA uridine(34) acetyltransferase by mediating formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity).
Catalytic Activity: acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in tRNA = 5'-deoxyadenosine + 5-(carboxymethyl)uridine(34) in tRNA + CoA + 2 H(+) + L-methionine
Sequence Mass (Da): 63210
Sequence Length: 559
Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
EC: 2.3.1.-
|
Q9H9T3 | MRQKRKGDLSPAELMMLTIGDVIKQLIEAHEQGKDIDLNKVKTKTAAKYGLSAQPRLVDIIAAVPPQYRKVLMPKLKAKPIRTASGIAVVAVMCKPHRCPHISFTGNICVYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRNLHDALSGHTSNNIYEAVKYSERSLTKCIGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCESFHLAKDSGFKVVAHMMPDLPNVGLERDIEQFTEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYKSYSPSDLVELVARILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELALARMKDLGIQCRDVRTREVGIQEIHHKVRPYQVELVRRDYVANGGWETFLSYEDPDQDILIGLLRLRKCSEETFRFELGGGVSIVRELHVYGSVVPVSSRDPTKFQHQGFGMLLMEEAERIAREEHGSGKIAVISGVGTRNYYRKIGYRLQGPYMVKMLK | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalytic tRNA acetyltransferase subunit of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) . In the elongator complex, acts as a tRNA uridine(34) acetyltransferase by mediating formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity). May also act as a protein lysine acetyltransferase by mediating acetylation of target proteins; such activity is however unclear in vivo and recent evidences suggest that ELP3 primarily acts as a tRNA acetyltransferase . Involved in neurogenesis: regulates the migration and branching of projection neurons in the developing cerebral cortex, through a process depending on alpha-tubulin acetylation . Required for acetylation of GJA1 in the developing cerebral cortex (By similarity).
PTM: Tyrosine-phosphorylated; phosphorylation on Tyr-202 does not affect elongator complex integrity or ELP3 protein stability . Also serine/threonine-phosphorylated .
Catalytic Activity: acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in tRNA = 5'-deoxyadenosine + 5-(carboxymethyl)uridine(34) in tRNA + CoA + 2 H(+) + L-methionine
Sequence Mass (Da): 62259
Sequence Length: 547
Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.-
|
D5VRB9 | MKEKLMRCIIERILKEYKEGKTLDKKRIEQIKSECLRIYRIGIGHPSNSEILKYATEEEKKILIPILRKKPVRTISGVAVVAVMTSPAKCPHGKCIFCPGGLDSVFGDVPQSYTGREPATMRGLMFNFDPYLQTRARIEQLEKVGHPTDKIELIIMGGTFPAREIEYQDWFIKRCLDAMNERESKSLEEAQKINETAKHRCVALCIETRPDYCSEKEINQMLKLGATRVELGVQSIYNEILKLCKRGHSVEDTIKATQLLKDSGLKVSYHLMPGMPGSSIEMDKKMFKEIFTNPDFMPDMVKIYPCLVIEGTELYEMWKRGEFKPYREEEAIEVISYAKSIMPKWVRTSRIQRDIPATVIVDGVKKSNLGELVYKYMEKKGLRCRCIRCREVGHVYYKKGILPDPEHIKLVREDYEASGGTEIFLSFEDVKNDILIAFLRLRDPYKPFRKEIDDKTMLVRQLHVFGWEKALTRDIKEVSWQHMGYGRMLMKEAERIAKEEFGKKKILVTSGIGVREYYRKLGYKRVGAYMGKEL | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs . The proposed mechanism is the following: (i) recruits S-adenosyl-L-methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'-dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule . Does not show protein lysine acetyltransferase activity .
Catalytic Activity: acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in tRNA = 5'-deoxyadenosine + 5-(carboxymethyl)uridine(34) in tRNA + CoA + 2 H(+) + L-methionine
Sequence Mass (Da): 61939
Sequence Length: 534
Pathway: tRNA modification.
EC: 2.3.1.-
|
O14023 | MSTSSLAFLKAKACAEIVAELIASENQNKVINLNALKMRISKKHQLSESPRLTDIIAAIPPDAYLKESLMRKLRAKPVRTASGIAVVAVMCKPHRCPHIAMTGNVCVYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYDPYEQARGRVEQLRSLGHTVDKVEYIIMGGTFMSLPESYRHTFIANLHNALSGATTEDLDEAVKFSEQSETKCVGITIETRPDYCLDQHLDEMLRYGCTRLEIGVQSVYEDVARDTNRGHTVKAVCETFQLAKDTGYKVVTHMMPDLPNVGMERDIFQFQEYFENPAFRTDGLKLYPTLVIRGTGLYELWKTGRYKNYTPNALVDLIARILALVPPWTRIYRIQRDIPMPLVSSGVETGNLRELALNRMRDLGTKCRDIRAREVGMQEVHHKIHPEQVELLRRDYTANGGWETFLSYEDPKQDILIGLLRLRQCSDKTYRPEFTSQPTSLVRELHVYGSAVPVHSRDPKKFQHQGFGTLLLEEAERIAKYEHGSKKISVISGVGVRKYYQKLGYTLDGPYMSKWL | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalytic tRNA acetyltransferase subunit of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) . In the elongator complex, acts as a tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity).
Catalytic Activity: acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in tRNA = 5'-deoxyadenosine + 5-(carboxymethyl)uridine(34) in tRNA + CoA + 2 H(+) + L-methionine
Sequence Mass (Da): 61850
Sequence Length: 544
Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.-
|
Q6GLC5 | MAGVALKREGPQFISEAAVRGNAAVLDYCRTSVSALSGATAGILGLTALYGFIFYFLASFLLSLLLVLKSGRKWNKYFKSRKPLFTGGLIGGLFTYVLFWTFLYGMVHVY | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12090
Sequence Length: 110
Subcellular Location: Endoplasmic reticulum membrane
|
Q12431 | MSSNEEVFTQINATANVVDNKKRLLFVQDSSALVLGLVAGFLQIESVHGFIWFLILYNLINVIYIVWICQLQPGKFYQSPLHDIFFESFFREITGFVMAWTFGYALIG | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins . Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues . Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices . It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12404
Sequence Length: 108
Subcellular Location: Endoplasmic reticulum membrane
|
Q9NPA0 | MAAALWGFFPVLLLLLLSGDVQSSEVPGAAAEGSGGSGVGIGDRFKIEGRAVVPGVKPQDWISAARVLVDGEEHVGFLKTDGSFVVHDIPSGSYVVEVVSPAYRFDPVRVDITSKGKMRARYVNYIKTSEVVRLPYPLQMKSSGPPSYFIKRESWGWTDFLMNPMVMMMVLPLLIFVLLPKVVNTSDPDMRREMEQSMNMLNSNHELPDVSEFMTRLFSSKSSGKSSSGSSKTGKSGAGKRR | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins . Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues . Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices . It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes . By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors . By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (Probable).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 26471
Sequence Length: 242
Subcellular Location: Endoplasmic reticulum membrane
|
Q0IHY5 | MPAVALGVSVGWRSLSLWLLALLQLCSADLDVLSPGSGSDKFKVEGRAVVPGVRPQDWVNTARVLVDGEEHVGFLRTDGSFVVHDVPSGSYVVEVISPAHRFEPVRVDITSKGKMRARYVNHIKTSEVVRLPYPLQMKSSGPPSYFIKRETWGWTDFLMNPMVMMMVLPLLIFVLLPKVVNTSDPEMRREMEQSMNMLNTNPELPDVSEFMTRLFTSKSSSKSSGSGKAGKSVGKRR | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 26341
Sequence Length: 237
Subcellular Location: Endoplasmic reticulum membrane
|
Q9W1Y1 | MCDYKVSERAYAKLIFHAAKYPHQAVNGLLLAEKTSKGSQVEIVDAIPLFHQCLYVTPMAEVALMLIDAHAEREGLVIAGYYAAPENFYDNQVDKTPAAKIADKIQENFKNACFVVVDNKLMTLQHDRAAIQVFNCPGDSGARWSKAKFTLSQASDTLEGVSLLLKRGAMRDLVDFDNHLDNPDKNWTNDFLNQPLNDLQKLY | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized multi-pass membrane proteins like rhodopsins.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22781
Sequence Length: 203
Subcellular Location: Endoplasmic reticulum membrane
|
O43402 | MPGVKLTTQAYCKMVLHGAKYPHCAVNGLLVAEKQKPRKEHLPLGGPGAHHTLFVDCIPLFHGTLALAPMLEVALTLIDSWCKDHSYVIAGYYQANERVKDASPNQVAEKVASRIAEGFSDTALIMVDNTKFTMDCVAPTIHVYEHHENRWRCRDPHHDYCEDWPEAQRISASLLDSRSYETLVDFDNHLDDIRNDWTNPEINKAVLHLC | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins . Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues . Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices . It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes . By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors . By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (Probable).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 23773
Sequence Length: 210
Subcellular Location: Endoplasmic reticulum membrane
|
O70378 | MPGVKLTTQAYCKMVLHGAKYPHCAVNGLLVAERQRPRKEHPPGAGSHTLFVDCIPLFHGTLALTPMLEVALTLIDSWCKDNSYVIAGYYQANERVKDASPNQVAEKVASRIAEGFGDAALIMVDNAKFTMDCAAPTIHVYEQHENRWRCRDPHHDYCEDWPEAQRISASLLDSRSYETLVDFDNHLDDIRSDWTNPEINKAVLHLC | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 23348
Sequence Length: 207
Subcellular Location: Endoplasmic reticulum membrane
|
Q9Y3B6 | MGEVEISALAYVKMCLHAARYPHAAVNGLFLAPAPRSGECLCLTDCVPLFHSHLALSVMLEVALNQVDVWGAQAGLVVAGYYHANAAVNDQSPGPLALKIAGRIAEFFPDAVLIMLDNQKLVPQPRVPPVIVLENQGLRWVPKDKNLVMWRDWEESRQMVGALLEDRAHQHLVDFDCHLDDIRQDWTNQRLNTQITQWVGPTNGNGNA | Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins . Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues . Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices . It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes . By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors . By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (Probable).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 23061
Sequence Length: 208
Subcellular Location: Endoplasmic reticulum membrane
|
Q9WZP2 | MEFLKRSFAPLTEKQWQEIDNRAREIFKTQLYGRKFVDVEGPYGWEYAAHPLGEVEVLSDENEVVKWGLRKSLPLIELRATFTLDLWELDNLERGKPNVDLSSLEETVRKVAEFEDEVIFRGCEKSGVKGLLSFEERKIECGSTPKDLLEAIVRALSIFSKDGIEGPYTLVINTDRWINFLKEEAGHYPLEKRVEECLRGGKIITTPRIEDALVVSERGGDFKLILGQDLSIGYEDREKDAVRLFITETFTFQVVNPEALILLKF | Cofactor: A flavin ligand is bound near the 3-fold axis channel; FMN is consistent with the observed density, absorbance data and mass spectrometry.
Function: Shell component of a type 1 encapsulin nanocompartment. Assembles into proteinaceous shells 23-24 nm in diameter with 2-2.5 nm thick walls. Cargo protein Flp (ferritin-like protein, probably stores iron) is targeted to the interior via its C-terminal extension; empty intact shells can be isolated in the absence of cargo protein . Fe(2+) may be able to pass though the 5-fold and dimer channels in the protein shell (Probable).
Sequence Mass (Da): 30478
Sequence Length: 265
Domain: Has 3 domains; a discontinuous peripheral domain (P, 13-39, 76-133, 221-254), an elongated loop (E, 53-73) and the discontinuous axial domain (A, 137-216 and 259-263). The E-loop forms contacts between two subunits, while the A domain mediates contacts in the 5-fold interface . Pores are formed by residues 184-189, pore size can be modified by mutagenesis .
Subcellular Location: Encapsulin nanocompartment
|
Q4W945 | MDQYSNLFAFEDYLGAQARSIPDLPEVDVLSPRVVRVLGGNPGQMQLQGTNTYILGTGAERLLIDSGQGRARWEQLMASLAAEHKFRISTVLLTHWHLDHTGGVPHLFRIFPELRGANAIYKYHPDPSQQAIVDGQVFSVEGATVRAVFTPGHSTDHMCFLLQEEEAIFTGDTVLGHGTTGVEDLEEYMQSLRKIQSLGCRIGYPGHGAVIENMQQKVQQEIDRKQRRERQVLLALQNIQREKRTVGDANGAATQAELIEAIFGRLPADVADRFFAPYMKDILMKMARDKQVGFRFKGGQKHWFANVSQENPVCR | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Atrochrysone carboxyl ACP thioesterase; part of the gene cluster that mediates the biosynthesis of endocrocin, a simple anthraquinone interesting for many biotechnological applications . The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) encA . The atrochrysone carboxyl ACP thioesterase encB then breaks the thioester bond and releases the atrochrysone carboxylic acid from encA . The atrochrysone carboxylic acid is then converted to endocrocin anthrone which is further oxidized into endocrocin by the anthrone oxygenase encC . The exact function of encD has not been identified yet, but it negatively regulates endocrocin production, likely through the modification of endocrocin itself .
Catalytic Activity: atrochrysone carboxyl-[ACP] + H2O = atrochrysone carboxylate + H(+) + holo-[ACP]
Sequence Mass (Da): 35346
Sequence Length: 315
EC: 3.1.2.-
|
A4DA85 | MASVQGLIKIVAITGGVWLSGKITAHSLVSVPALLQTRSADGLSPCTILRVWRRIYEQGHRHSPQIAACTSTAFAYLAWCASDRTPRLLYGTAACSVMGIVPYTLLFMGPTNSRLLERSAAEEEKVPGATRGEDMVNVPSEMTTEELLSHWRFLAGIRGLLPLAGGILGLFAALYSNEGAR | Function: Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of endocrocin, a simple anthraquinone interesting for many biotechnological applications . The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) encA . The atrochrysone carboxyl ACP thioesterase encB then breaks the thioester bond and releases the atrochrysone carboxylic acid from encA . The atrochrysone carboxylic acid is then converted to endocrocin anthrone which is further oxidized into endocrocin by the anthrone oxygenase encC . The exact function of encD has not been identified yet, but it negatively regulates endocrocin production, likely through the modification of endocrocin itself .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19473
Sequence Length: 181
Subcellular Location: Membrane
EC: 1.-.-.-
|
Q4W946 | MTKPQPPPILDFSVFYGHDSQAKAQLVQRVRECCLNNGFFQITGHKVSPELQRRTFDCAKRFFDLPLIEKKKIERSPDAFNRGYEAFQSHMSQPGSAPDRKEGLFLGPDLAEDHPYCVQKKLNCGPNRWPQGLDDLEEFKLVSMEYYAALFQLAKDVVAVLALTMDYEETFFDPLTEGAIATLRYLHYPPQPVGDAEAGLGTGAHRDYSCITLLLQDGTGGLQVLDEPTGQWLDVKPVPGAYIVNLANVFARMTNGHYKSALHRVVNKSGMERYSIPFFFTGNPDYVCECLSRFRKEGEPVRHPPATVHEVVAEAVRGTVERANRYNAERQGIHAAQ | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 2-oxoglutarate-Fe(II) type oxidoreductase; part of the gene cluster that mediates the biosynthesis of endocrocin, a simple anthraquinone interesting for many biotechnological applications . The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) encA . The atrochrysone carboxyl ACP thioesterase encB then breaks the thioester bond and releases the atrochrysone carboxylic acid from encA . The atrochrysone carboxylic acid is then converted to endocrocin anthrone which is further oxidized into endocrocin by encC . The exact function of encD has not been identified yet, but it negatively regulates endocrocin production, likely through the modification of endocrocin itself .
Sequence Mass (Da): 37912
Sequence Length: 337
Pathway: Secondary metabolite biosynthesis.
EC: 1.14.11.-
|
Q8U1L4 | MLSINPTLINRDKPYTKEELMEILRLAIIAELDAINLYEQMARYSEDENVRKILLDVAREEKAHVGEFMALLLNLDPEQVTELKGGFEEVKELTGIEAHINDNKKEESNVEYFEKLRSALLDGVNKGRSLLKHLPVTRIEGQSFRVDIIKFEDGVRVVKQEYKPIPLLKKKFYVGIRELNDGTYDVSIATKAGELLVKDEESLVIREILSTEGIKKMKLSSWDNPEEALNDLMNALQEASNASAGPFGLIINPKRYAKLLKIYEKSGKMLVEVLKEIFRGGIIVTLNIDENKVIIFANTPAVLDVVVGQDVTLQELGPEGDDVAFLVSEAIGIRIKNPEAIVVLE | Function: Fusion of the shell and cargo protein of a type 1 encapsulin nanocompartment . The nanocompartment is probably involved in iron storage (Probable). Expression in E.coli generates spherical particles (PfSPs) about 30 nm in diameter . The purified N-terminus has ferroxidase activity .
Catalytic Activity: 4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O
Sequence Mass (Da): 38802
Sequence Length: 345
Domain: The ferritin-like domain N-terminal 109 disordered residues are located inside the organelle in the crystal. The rest of the protein has 3 structural domains; a discontinuous peripheral domain (P, 110-138, 167-210, 304-334), an elongated loop (E, 139-166) and the discontinuous axial domain (A, 211-303 and 335-345). The E loop is highly flexible and allows formation of the pentamers and hexamers from the same protein . The N-terminal domain decamer has negatively charged patches on its exterior, and a negatively charged tunnel at the center, the charges are probably metal-binding sites .
Subcellular Location: Encapsulin nanocompartment
EC: 1.16.3.1
|
P46841 | MTSAQNESQALGDLAAGQLANATKTVPQLSTITPRWLLHLLNWVPVEAGVYRVNRVVNPERVAVKAEAGAGTEAPLPETFVDYETSPREYTLRTISTLLDIHTRVSDLYSSPHDQITQQLRLTIETIKERQECELVNSPEFGLLAQVTPEQTIRTFAGAPTPDDLDALITKVWKMPSFFLTHPQGIAAFGREATYRGVPPVVVSLFGAQFITWRGIPLIPSDKVPVQDGETKFILVRTGEERQGVVGLFQPGLVGEQAPGLSVRFTGINQAAIATYLVTLYTSLAVLTDDALAVLDNVAVDQFHEYK | Function: Shell component of a type 2A encapsulin nanocompartment. Forms encapsulin nanocompartments about 24 nm in diameter from 60 monomers. Probably encapsulates at least cysteine desulfurase (CyD, AC O32975) and allows passage of cysteine into its interior, probably involved in sulfur metabolism (By similarity). Expression in M.smegmatis generates a multimeric protein, whereas expression in E.coli does not .
PTM: The N-terminus is blocked.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33651
Sequence Length: 307
Domain: Has 4 domains; an N-terminal arm not found in the type 1 subfamily, a discontinuous peripheral domain (P), an elongated loop (E) and the discontinuous axial domain (A).
Subcellular Location: Encapsulin nanocompartment
|
I3NID5 | MTSAQNESQALGDLAARQLANATKTVPQLSTITPRWLLHLLNWVPVEAGIYRVNRVVNPEQVAIKAEAGAGSEEPLPQTYVDYETSPREYTLRSISTLVDIHTRVSDLYSSPHDQIAQQLRLTIETIKERQELELINSPEYGLLAQATPEQTIQTLAGAPTPDDLDALITKVWKTPSFFLTHPLGIAAFGREATYRGVPPPVVSLFGAQFITWRGIPLIPSDKVPVEDGKTKFILVRTGEERQGVVGLFQPGLVGEQAPGLSVRFTGINQSAIATYLVTLYTSLAVLTDDALAVLDDVAVDQFHEYK | Function: Shell component of a type 2A encapsulin nanocompartment. Forms encapsulin nanocompartments about 24 nm in diameter from 60 monomers, probably involved in sulfur metabolism (By similarity). Probably encapsulates cysteine desulfurase (Probable).
Sequence Mass (Da): 33671
Sequence Length: 307
Domain: Has 4 domains; an N-terminal arm not found in the type 1 subfamily, a discontinuous peripheral domain (P), an elongated loop (E) and the discontinuous axial domain (A).
Subcellular Location: Encapsulin nanocompartment
|
Q55032 | MTDNAPQLALRDVAARQLANATKTVPQLRTITPRWLVRLLHWTPVEAGIYRVNQVKDASQITVACSERDESELPETFVDYIDNPREYLLSAVNTVVDVHTRISDLYSNPHDQIREQLRLTIEIMKERQESELINSREYGLLNNVAPGQLVHTRNGAPTPDDLDELLIRVWKEPAFFLAHPQAIAAFGRECTRRGVPPATVSLFGSSFITWRGVPLIPSDKVPLENGKTKILLLRVGESRQGVVGLYQPNLPGEQGMGLSVRFMGINRKALASYLVSLYCSLAVLTDDALAVLDNVDVTQYHTYRYN | Function: Shell component of a type 2A encapsulin nanocompartment. Expression in E.coli generates nanocompartments with an average diameter of 25 nm. They can be disassembled by treatment with 6M guanidine hydrochloride and reassembled with cargo. The nanocompartment is probably involved in sulfur metabolism . Probably allows passage of cysteine into its interior; during growth in light the physiological pH is 8-8.4, about 30-54% of free cysteine (charge -1) would be able to pass through the shell (Probable).
Sequence Mass (Da): 34360
Sequence Length: 306
Domain: Has 4 domains; an N-terminal arm not found in the type 1 subfamily, a discontinuous peripheral domain (P), an elongated loop (E) and the discontinuous axial domain (A).
Subcellular Location: Encapsulin nanocompartment
|
B8GKX5 | MVKIGVHVSIAGSIARAVERAMAIDCDTFQIFSRNPRGWTFKPLAEEDAALFQGALGTSGIGPAVVHMPYLPNLASPKEEIWRKSVEALTEELHRCSMLDVPYLVTHLGHHMGEGIGAGEGRVQQAIDAAFSQSDPGSSRVMLLLENTAGEKNSVGSRFEEIGRIRESCSDPDRIGVCMDTCHAFAAGYDLRNEVGLSRTLEAFEDGIGIEHLHVIHLNDAKADIGSHLDRHTHIGLGMIGEEGCSGILTHPTLASLPFICETPEDAVRDNAANIRAVRRLAVPRA | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence Mass (Da): 30890
Sequence Length: 286
EC: 3.1.21.2
|
Q5UPY4 | MQSNINICTLSIFIIESMTTRIGRHINISKGFVSAPEYAKNIGCSVFQIFLGAPQQILSKARQKDELIEFGKQLIKHDLIMVVHGSYTINLCHPPGSKKFETSIKSLVKDLNATNLIGDRCLGVIIHMGKNISENKLTVDQAIDNYVTGIKTALSQTPDNTTIVLETGASQGSEVASHIDGLAQIYWCLNDAERERVYFCIDTCHIWATGYDISSPTGVKKFFKEFDKKIGVEKISCIHFNDSKTGLESKVDRHADLCYGEIGSNGLKAIAKFAKEYKIHLIMETPLDAINPETNQEISYNEEYNKVKSWLK | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues (By similarity).
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence Mass (Da): 34857
Sequence Length: 312
EC: 3.1.21.2
|
Q2RJF1 | MRLGAHLSIAKGLPRTAAMATSIGANTFQYFTRNPRGGAARQIPGKEIQAWREARRRADLYPIAGHLPYTVNLGAAAERQQEFTRMVLHDDTLRVAAIDGEYLISHPGHYEGERQAGLDRIIQLIEEAYLSITPPGPMLLLETMAGQGKEVGTIDDLCYILEGLGWPDRVGVCLDSAHLFAAGWDLRTPAGCQQLVQELAAKIGLDRVKAMHLNDSAAPLGSHRDRHAGIGKGELGREGIAAVVNDPFLGELPLFLETPVANYEEYGEEIALIQKLKSV | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence Mass (Da): 30409
Sequence Length: 279
EC: 3.1.21.2
|
P63536 | MLIGSHVSPTDPLAAAEAEGADVVQIFLGNPQSWKAPKPRDDAAALKAATLPIYVHAPYLINLASANNRVRIPSRKILQETCAAAADIGAAAVIVHGGHVADDNDIDKGFQRWRKALDRLETEVPVYLENTAGGDHAMARRFDTIARLWDVIGDTGIGFCLDTCHTWAAGEALTDAVDRIKAITGRIDLVHCNDSRDEAGSGRDRHANLGSGQIDPDLLVAAVKAAGAPVICETADQGRKDDIAFLRERTGS | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence Mass (Da): 26845
Sequence Length: 252
EC: 3.1.21.2
|
Q7NBA9 | MKSNKIKYLGCFVGATKPDFMLGMVKTVVDYGATSFMFYSGPPQSFRRTPTAQFKLDLAKAYLAKHNLGDLGDNYVVHAPYLINLANGDSTKRERSFNFFLDELKRTNELGAKYFVLHPGSALNVKDKTQALDHLATELNRAISMTKDTIICLETMADKGQQICSKFEELRYVIDQISDKSRIGVCFDTCHVHDAGYDLAKTQELIDHFDQVIGLKYLYVIHLNDSKNPMGARKDRHANIGYGKIGFENLLNFIYHKEICNKIIILETPWIDDPIRGEVPLYKEEIEMIRNKKFVEGLVNEES | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence Mass (Da): 34550
Sequence Length: 303
EC: 3.1.21.2
|
P47477 | MPKLLGSFISFKAPNYFVQSAQDAIAIDATALMVFLGPPHSAYRVPFNKMQFSLGYELLKTKNINSNGLVVHAPYIINCASKDPLKQQNAISVLTNEIQLCNLAGAHYLVLHPGSAVAQTTNEALDNLVKVLNQVINKTKTTVICLETMAGKGNEIGRDLTELKYVIDRIVDKDRIGVCLDTCHFHDSGIDFSDLTGVFNTITTKLGFEFLKVIHLNESKNNCGSKKDRHANINAGMIGFENLMKFISHPQIKDLPIILETPSTSLNYPTIYREEISQIRSWFKTYQPDAN | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence Mass (Da): 32391
Sequence Length: 291
EC: 3.1.21.2
|
B8ZSC5 | MLIGSHVSSTDPLAAAEVEGADVVQIFLGNPQSWKAPTLRSDADVLKATALPVYVHAPYLINVASANSRVRIPSRKILQQTCDAAADIGAAAVVVHGGYVADDNDLEDGFQRWRKALDQLQTDVPVYLENTAGGDHAMARRFDTIARLWDVIGETGIGFCLDTCHAWAAGEGLIHVVDRIKAITGRIDLVHCNDSKDEAGSGRDRHANLGSGQIDAELLVAAVKVAGAPVICETAEEGRKDDIAFLREKTSG | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence Mass (Da): 26861
Sequence Length: 252
EC: 3.1.21.2
|
Q6MUC7 | MDKILLGCHVSMNKQNNYLVGSVNEAISYKANTFMIFTGPPQSTLRTNTNHLYINQMHELMNSYKIDAKDLVVHAPYIINIANSVDQNKWKFTVDFLIQEIKRCEEIKIPTLVLHPGSYTTGNYKDSLNQIIKALNIVSNYQVNVKIALETMSGKGTEVCSRLEDFKYILDNVKNKDKVGVCLDTCHLHDAGYDLSKWTEFKEQMKQNFSLDKVLCIHLNDSKNMISSHKDRHANIGYGYVGFDTLVNVVFDKDFSNISKILETPYIDKTPPYKIEIEDLLNKTFTNRL | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence Mass (Da): 33160
Sequence Length: 289
EC: 3.1.21.2
|
Q98PU8 | MIKLGSHVSFKSPNYLYDSIKESIKNGANCAMIFLGAPQNTKRVDFEKYQYEKYLKDFSNLIKPEDIVVHAPYIINPASLEKADFAISFLSSEIKRMDKAKFKYLVLHPGFYGKNNVKDSLDQLARSIQKIFEITKDSNVEIMLETMSGKGSEVGKSYEEILYVIDKVKSPRLGACLDTCHVWDAGYNINDYQVFKDELIKTGILKHIKVIHLNDSKNELGSHKDRHANIDKGLIGLKNLKRIVHDPIFENIPIILETPWTEKGPIYDQEIAMLLEK | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence Mass (Da): 31685
Sequence Length: 277
EC: 3.1.21.2
|
Q9YBF1 | MGDRCAPIKASGVLIGDSVLVTDVEQARSLYSCGYYGQPLDVEKPRGADFEGPLRLSLIESLYLAEKGVLEVAKPDGSSVGVEDLRTAVRGNPRFSMLYNIYRDLRERGFVVRSGLKFGSDFAVYRLGPGIDHAPFIVHAYSPEDNIDPVEIVRAGRLSHSVRKKFVFAVTRGGDVSYLMIDWFRP | Function: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a stem of 4 bp.
Catalytic Activity: pretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.
Sequence Mass (Da): 20602
Sequence Length: 186
EC: 4.6.1.16
|
O29362 | MIGGDFAVVKAKKSLERRGFGVKRGDKIYLHPLEVVYLQIKGIESFGELEDVLSWAESRMEDFSTYYFVYEDLRDRGNKVKIQGEFLLTKKPYLPISERKTIRMEEIAEKARNFDELRLAVVDEESEITYFRVYEPDMMGEQKEELPEIAGILSDEYVITKQTEIFSRYFYGSEKGDLVTLSLIESLYLLDLGKLNLLNADREELVKRAREVERNFDRRYEVYRNLKERGFVVKTGFKFGSEFRVYRKVESVDDLPHSEYLVDIADSREIRLIDLARAVRLAQNVRKRMVFAYGKNYLCFERVKV | Function: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a stem of 4 bp.
Catalytic Activity: pretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.
Sequence Mass (Da): 35959
Sequence Length: 305
EC: 4.6.1.16
|
O07118 | MQGRLEDGVVHLPGDARQRFHDSRGYGRPTGGDDLEVAPVEAAHLLSRDDIDGVDGMGLRELLARTGTTLDFVVYKDLRDRGFYLSPAREGWPGVADAADADFLVYPRGKGPWDGEVEHRVRVVGERESIPVSSLGEVVLAIVDEDGDLTYFDTEGDDPEGTAAEDLPADLDAELLSDRALVWDGVDRLYQRGFFGQRLYGRNADSGPLQLSLLEAAYLARADALAIDEADVVSRGRDVEGDRFDRRLAVYAALREAKTVPKSGFKFGSDFRVYTEFESVDDLSHSEFLVRVVAPDHTFVPRDLSLDVRLAGGVRKRMVFALTDDNGEIDWLSVSRLTP | Cofactor: Divalent cations; Ca(2+) better than Mg(2+).
Function: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a stem of 4 bp.
PTM: The N-terminus is blocked.
Catalytic Activity: pretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.
Sequence Mass (Da): 37418
Sequence Length: 339
EC: 4.6.1.16
|
Q8TGX1 | MKTQLEGDRVLAGKEAVAELYKTGYFGRPREDGLELSLVEAAYLQFRGKIEIELEGRKLDFRALFEQASLRQPNFELKYIVYKDLKERGYYVQPSAADFRVYPRGSHPGKSAAKIFVHVLSERQPLPVKLLQDSVISAENVHKQFILAVVDEESDLTFYEIKTASPQGEMPEPYPEVKTDATFLEDRVIAWDAEASGALYAGGFYGKMLDPERLQLSLVESLYLFSRGIIVVRDRKDRIFSFDEFVEKASEIESSFLRKYGAYKALRDSGHVVKTGFKFGTHFRVYRKVESIEKIPHSEYLVNVIPSDYEFRLPVMSGAVRLANSVRKRMLFAVEKEEGVEYLDISRVKM | Function: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a stem of 4 bp (By similarity).
Catalytic Activity: pretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.
Sequence Mass (Da): 40133
Sequence Length: 350
EC: 4.6.1.16
|
Q58819 | MVRDKMGKKITGLLDGDRVIVFDKNGISKLSARHYGNVEGNFLSLSLVEALYLINLGWLEVKYKDNKPLSFEELYEYARNVEERLCLKYLVYKDLRTRGYIVKTGLKYGADFRLYERGANIDKEHSVYLVKVFPEDSSFLLSELTGFVRVAHSVRKKLLIAIVDADGDIVYYNMTYVKP | Function: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a stem of 4 bp.
Catalytic Activity: pretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.
Sequence Mass (Da): 20664
Sequence Length: 179
EC: 4.6.1.16
|
Q8TGZ7 | MLCAGNGGKELPRAKVFEGGSLVSKDYEDLKRRYFGTEHGNVLFLDPFETVYLTEKGEIDPETPEGEPMSVEELLSFFERRRPGFRAGYVVYRDLTERGYVVKSGFKYGGRFRVYEEDPDREHSKYVVRVVEPDTELSTRDVLRATRLAHSVRKDFVLAVVEDVEEPRIEYVMWRWKRL | Function: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a stem of 4 bp.
Catalytic Activity: pretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.
Sequence Mass (Da): 20939
Sequence Length: 179
EC: 4.6.1.16
|
O07165 | MRVEGQLGDEVVTIKATSIARRLHGKSHYGKMYEDRLQLSLIEAAYLMERGKLKLMKDDDEVSPEEFISLLGERGLYSKYLVYRDLRNRGYIVKTGFKYGAEFRLYERGGAPGRTHSAYLVRVISENDTIHALDFSSYVRVAHGVNKKLLMAFLDDEEDITYYLVDWIRP | Function: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a stem of 4 bp.
Catalytic Activity: pretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.
Sequence Mass (Da): 19693
Sequence Length: 170
EC: 4.6.1.16
|
Q7Q9C0 | MAAVVALGANVLSAKSIICDIEGTTTSISFVKDTLFPYALKHVEGYLKNNWNEEATKTVVTALREQAEEDKKAEVEGVVPIPTGDSEDIIPEIVKNVEWQMSLDRKTGSLKTLQGLVWAKGYKDGSIKGHVYDDVQKAFEQWTENGRKIYIYSSGSVDAQKLLFEHSEQGDLLKYLSGHYDTKIGAKREKESYTSILKNIESSPEEALFLTDVYAEAKAAKEAGLNVVLLDRPGNSELSEEERKDFPVIATFSDLSFAAETKEENGGATNGKRKIEETNDDVAEEDKAQVYPNKK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 32682
Sequence Length: 295
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
Subcellular Location: Cytoplasm
EC: 3.1.3.77
|
Q753F5 | MEEDYGVFILDVEGTVCPIAFVREQLFPYFLDKVEELINNADETERDLLADMQSRHGGAAAASLLRQLVAEDVKDPALKALQGRVWERGYASGEITAPVYADAVRFIQRNAGRVYIYSSGSVQAQRLLFGHVSNPSGDGVLDLTGHLAGFFDIPAAGRKTEAKSYERILAAIGLERQPGAAIFVSDSVAELDAASASGLSVRLAVRPGNERVSGARYTTLTDFEGL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 24411
Sequence Length: 226
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
Subcellular Location: Cytoplasm
EC: 3.1.3.77
|
Q0VD27 | MVVLSVPAEVTVILLDIEGTTTPIAFVKDILFPYVKENVEEYLQAHWEEEECQQDVRLLRKQAEEDSHLDGAVPIPAASGNGADDPQWMIQAVVDNVYWQMSLDRKTTALKQLQGHMWRAAFKAGHMKAEFFEDVVPAVRKWREAGMKVYVYSSGSVEAQKLLFGHSTEGDILELVDGHFDTKIGHKVESESYQKIASSIGCSTNNILFLTDVSREASAAEEAGVHVAVVVRPGNAGLTDDEKTHFSLITSFSELYLPSST | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 28930
Sequence Length: 261
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
Subcellular Location: Cytoplasm
EC: 3.1.3.77
|
C3XR70 | MSDSRLRRRQGTAGTDNKRRADGPHDISGLLDGVSVVLLDIEGTTTPITFVKDELFPYVCSHVRQHLEEHWKEEECQEDIAALRKQAKEDKEMDGVVLIPECTTKDDDEEARKKVLSAVVDNVLLNMDADRKVTALKQLQGHMWRAAYQTGKIKGEYVKLTFADVVPAIRGWLETGRQVYIYSSGSVEAQKLLFGFSTEGDLLELFSGHFDTTTGLKVETESYRRIAKTVGCDPANILFLTDVVREAKPSREAGMKTCLTVRPGNAPLTEEDWANYPVIKSFSELACDVSPTKMRSRGKAAT | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 33701
Sequence Length: 302
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
Subcellular Location: Cytoplasm
EC: 3.1.3.77
|
A8Y461 | MTNTTTIQFNALLLDIEGTITSISFVKDELFPYAFENVGKYLEEHYDKPATQIIIEDLRRLAEQQLETDADVVKIRERKQECIEDVTKNVRHWIKRDKKLTPMKALQGLIWEEAYQRGYVKGHVYPDVLPILKIIESRQIPIYIYSSGSVHAQKLLFANSVEGDMTKILYGYFDTNIGLKGETSSYTKISEQIGVPEKDILFLTDVEAEAAAASKAGLQTRLVIRPGNATLTQEAKNAYGTIHTLEEIL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 28242
Sequence Length: 249
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
Subcellular Location: Cytoplasm
EC: 3.1.3.77
|
Q21012 | MTTTTIQFNALLLDIEGTITSISFVKDELFPYAFENVGNYLEEHYDNPATQIIVEDLRHIADQQAENDVAVVRIREPRKECIEDVTKNVRHWIKRDKKLTPMKALQGLIWEEAYQRGDVKGHVYPDVLPVLKIVENRKIPIYIYSSGSVHAQKLLFANSIEGDMTKILYGYFDTNIGLKGESNSYTKISERIKIPPSEILFLTDVEAEAAAAKKAGLQTKLVVRPGNAGLTQEAINAYGTIESLEEIL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 27955
Sequence Length: 248
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
Subcellular Location: Cytoplasm
EC: 3.1.3.77
|
Q5AM80 | MTTTAKTDDIPIDTVILDIEGTVCPITFVKDTLFPYFIEKLPSILDKFQYPLSNTSASSDDQVLNILKQLPDNITKSSESIYKHFKNLVDQDIKDPILKSLQGLIWKQGYEKNELQAPIYQDSIEFIESFPTKSSTNNKIYIYSSGSIKAQILLFGHVKSTTTTITNEVIDLNPKLNGYFDITTAGFKNQSNSYKKILQEINKSSTPKSVLFLSDNINEVNAAIEAGMKSYIVIRPGNPPIDDDDDGNDDKINHKIIYSLDELDL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 29786
Sequence Length: 265
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
Subcellular Location: Cytoplasm
EC: 3.1.3.77
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.