ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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E9L011 | MAIEKPVIVACACPLAGHVGPVLSLVRGLLNRGYEVTFVTGNAFKEKVIEAGCTFVPLQGRADYHEYNLPEIAPGLLTIPPGLEQTGYSMNEIFVKAIPEQYDALQTALKQVEAENKSAVVIGETMFLGVHPISLGAPGLKPQGVITLGTIPCMLKAEKAPGVPSLEPMIDTLVRQQVFQPGTDSEKEIMKTLGATKEPEFLLENIYSSPDRFLQLCPPSLEFHLTSPPPGFSFAGSAPHVKSAGLATPPHLPSWWPDVLSAKRLIVVTQGTAAINYEDLLIPALQAFADEEDTLVVGILGVKGASLPDSVKVPANARIVDYFPYDELLPHASVFIYNGGYGGLQHSLSHGVPVIIGGGMLVDKPAVASRAVWAGVGYDLQTLQATSELVSTAVKEVLATPSYHEKAMAVKKELEKYKSLDILESAISELAS | Function: Catalyzes the second glycosylation step of sophorolipid biosynthesis, the further glucosylation of the previoulsy formed glucolipid to give rise to an acidic sophorolipid.
Catalytic Activity: (9Z)-17-hydroxyoctadec-9-enoate 17-O-beta-D-glucoside + UDP-alpha-D-glucose = (9Z)-17-hydroxyoctadec-9-enoate 17-O-sophoroside + H(+) + UDP
Sequence Mass (Da): 46155
Sequence Length: 432
EC: 2.4.1.-
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G3FIN9 | MGSLASEIPPHAVLVPYPAQGHVNPLMQLGKLLHSRGFYITFVNTEHNHRRLIRSRGQEFIDGLPDFKFEAIPDGLPYTDRDATQHVPSLSDSTRKHCLAPFIDLIAKLKASPDVPPITCIISDGVMAFAIDAARHFGIPEIQFWTTSACGFMAYLHHIELVRRGIVPFKDESFLHDGTLDQPVDFIPGMPNMKLRDMPSFIRVTDVNDIMFDFMGSEAHKSLKADAIILNTYDELEQEVLDAIAARYSKNIYTVGPFILLEKGIPEIKSKAFRSSLWKEDLSCIEWLDKREPDSVVYVNYGCVTTITNEQLNEFAWGLANSKHPFLWIVRPDVVMGESAVLPEEFYEAIKDRGLLVSWVPQDRVLQHPAVGVFLSHCGWNSTIECISGGKPMICWPFFAEQQTNCKYACDVWKTGVELSTNLKREELVSIIKEMMETEIGRERRRRAVEWRKKAEEATSVGGVSYNNFDRFIKEAILQHKTK | Function: UDP-glucosyltransferase catalyzing in planta synthesis of cyanogenic glucosides. Able to glucosylate acetone cyanohydrin and 2-hydroxy-2-methylbutyronitrile, forming linamarin and lotaustralin. Accepts also to some extent, a wide range of potential acceptor substrates, including simple alcohols, flavonoids, isoflavonoids and other hydroxynitriles such as p-hydroxymandelonitrile, mandelonitrile, (E)-4-hydroxy-2-methylbut-2-enenitrile and (E)- 2-(hydroxymethyl)but-2-enenitrile.
Catalytic Activity: 2-hydroxy-2-methylpropanenitrile + UDP-alpha-D-glucose = H(+) + linamarin + UDP
Sequence Mass (Da): 54862
Sequence Length: 483
EC: 2.4.1.63
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Q6UDH7 | MATRGRPGAKQVADHSVSDGGEQRRIPQKPPGPERCDVCSAVSAAGAAADLIDVAPLEEDLTKEPQQIVVTIMSNDPAKVCLKVDPALHYRNVELEPYRFLGRGGYGSVFYSRRANVAVKALTHGASFRWELAVSLIVSSAARRQELSDIAKHFLQIYAFSSVEKIIVMEYIRHDLRTYLDEHCKPVTQSALDALVREFRGLAKALAFFHIECGLAHLDVKQNNILVNCDPRTGDPVRMVLADFSLAAINGNSFLNKCCMVCPGRPGVTGVHIIDTEDAVNSLPSNNILLFRMSRRPPEFLLDYCNGVGPRCGEVMGAMTTFAMDVFALGSVVHEVLLLCLSRVLGRDPFPHMTCTDEPMDHKTILSLLAYRLALTDYLSQSWSSAGFVNPAGTREGISSALQWECMRDMFLASAEAWTRTVRRKMNGARSPSMFADILDLSILLCHFDPDVRRTVSALA | Function: Multifunctional serine/threonine kinase that plays a role in several processes including egress of virus particles from the nucleus, modulation of the actin cytoskeleton and regulation of viral and cellular gene expression. Regulates the nuclear localization of viral envelopment factors UL34 and UL31 homologs, by phosphorylating the US3 kinase homolog, indicating a role in nuclear egress. Disrupts host nuclear lamins, including LMNA and LMNB1. Phosphorylates the viral Fc receptor composed of glycoproteins E (gE) and I (gI). Phosphorylation of glycoprotein E (gE) by UL13 homolog alters its subcellular localization, from the host early endosome to the plasma membrane. Participates in the transcriptional regulation of cellular and viral mRNAs mainly by phosphorylating the viral transcriptional regulator ICP22 homolog (By similarity).
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 50687
Sequence Length: 460
Subcellular Location: Virion tegument
EC: 2.7.11.1
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P30662 | MAAGGGGGGVSRAALARPPIHRGTSAPGGAIAAAGGDGDGDEASRLLGRAQPREAPYLIPRPDGDLAVPDDLQYATLDLTGDPVAVGAGSYGSVLVYGSVAVKTLRAGFGHEAVMTLLAAEEARSAGVRGVVRLMGLSAPLRQLMFPAYEMDMDAYRRSLTARPGHVVHALGRVFTELGRALVFLNGRGLSHLDVKGGNIFVRTCGNMVVTAVIGDFSLMALNSRSALADPRFRLARRKALKITSLARSPPTGVLLGHARDRPTRVLMDFINGRPPPPGPLPYEVGLAIDLCALGHVLLDVALGLRPQRGQALTREYAVEVLARRCVLFAALLPPGSGPSAEALAGDILEEELAAGFREGVASSRPGNQPPRTVAPLLELVARFCGEDGGARFAELAA | Function: Multifunctional serine/threonine kinase that plays a role in several processes including egress of virus particles from the nucleus, modulation of the actin cytoskeleton and regulation of viral and cellular gene expression. Regulates the nuclear localization of viral envelopment factors UL34 and UL31, by phosphorylating the US3 kinase, indicating a role in nuclear egress. Disrupts host nuclear lamins, including LMNA and LMNB1. Phosphorylates the viral Fc receptor composed of glycoproteins E (gE) and I (gI). Phosphorylation of glycoprotein E (gE) by UL13 alters its subcellular localization, from the host early endosome to the plasma membrane. Participates in the transcriptional regulation of cellular and viral mRNAs mainly by phosphorylating the viral transcriptional regulator ICP22 (By similarity).
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 41417
Sequence Length: 398
Subcellular Location: Virion tegument
EC: 2.7.11.1
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P09296 | MDADDTPPNLQISPTAGPLRSHHNTDGHEPNATAADQQERESTNPTHGCVNHPWANPSTATCMESPERSQQTSLFLLKHGLTRDPIHQRERVDVFPQFNKPPWVFRISKLSRLIVPIFTLNEQLCFSKLQIRDRPRFAGRGTYGRVHIYPSSKIAVKTMDSRVFNRELINAILASEGSIRAGERLGISSIVCLLGFSLQTKQLLFPAYDMDMDEYIVRLSRRLTIPDHIDRKIAHVFLDLAQALTFLNRTCGLTHLDVKCGNIFLNVDNFASLEITTAVIGDYSLVTLNTYSLCTRAIFEVGNPSHPEHVLRVPRDASQMSFRLVLSHGTNQPPEILLDYINGTGLTKYTGTLPQRVGLAIDLYALGQALLEVILLGRLPGQLPISVHRTPHYHYYGHKLSPDLALDTLAYRCVLAPYILPSDIPGDLNYNPFIHAGELNTRISRNSLRRIFQCHAVRYGVTHSKLFEGIRIPASLYPATVVTSLLCHDNSEIRSDHPLLWHDRDWIGST | Function: Multifunctional serine/threonine kinase that plays a role in several processes including egress of virus particles from the nucleus, modulation of the actin cytoskeleton and regulation of viral and cellular gene expression. Regulates the nuclear localization of viral envelopment factor proteins 24 and 27, by phosphorylating the protein kinase ORF66, indicating a role in nuclear egress. Disrupts host nuclear lamins, including LMNA and LMNB1. Phosphorylates the viral Fc receptor composed of glycoproteins E (gE) and I (gI) (By similarity). Phosphorylation of glycoprotein E (gE) by UL13 alters its subcellular localization, from the host early endosome to the plasma membrane. Participates in the transcriptional regulation of cellular and viral mRNAs mainly by phosphorylating the viral transcriptional regulator IE63.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 57351
Sequence Length: 510
Subcellular Location: Virion tegument
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Q6RJQ3 | MCRRESLRTLPWLFWVLLSCPRLLEYSSSSFPFATADIAEKMWAENYETTSPAPVLVAEGEQVTIPCTVMTHSWPMVSIRARFCRSHDGSDELILDAVKGHRLMNGLQYRLPYATWNFSQLHLGQIFSLTFNVSTDTAGMYECVLRNYSHGLIMQRFVILTQLETLSRPDEPCCTPALGRYSLGDQIWSPTPWRLRNHDCGMYRGFQRNYFYIGRADAEDCWKPACPDEEPDRCWTVIQRYRLPGDCYRSQPHPPKFLPVTPAPPADIDTGMSPWATRGIAAFLGFWSIFTVCFLCYLCYLQCCGRWCPTPGRGRRGGEGYRRLPTYDSYPGVKKMKR | Function: Evasion of NK cell killing. Blocks surface expression of PVR which is a ligand for NK cell-activating receptors. Binds human PVR in the endoplasmic reticulum and prevents its maturation and transport to the cell surface. Targets also the natural killer cell activating ligand NECTIN2 for proteasome-mediated degradation. Additionally promotes intracellular retention of TNFRSF10A/TRAIL-R1 and TNFRSF10B/TRAIL-R2 and thus down-regulates their cell surface expression.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 38918
Sequence Length: 338
Subcellular Location: Host endoplasmic reticulum membrane
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F5HHH2 | MRIEWACWLFGYFVSSVGSERSLSYRYHLESNSSANVVCNGNISVFVNGTLGVRYNITVGISSSLLIGHLTIQTLESWFTPWVQNKSYSKQPLSTTETLYNIDSENIHRVSQYFHTRWIKSLQENHTCDLTNSTPTYTYQANVNNTNYLTLTSSGWQDRLNYTAINSTHFNLTESNITSIHKYLNTTCIERLRNYTLEPVYTTAVPQNVTPEHAITTLYTTPPNAITIKDTTQSHTVQTPSFNDTHNVTEHTLNISYVLSQKTNNTTSPWVYAIPMGATATIGAGLYIGKHFTPVKFVYEVWRGQ | Function: Participates in the inhibition of the host immune response. Prevents host NK cell-mediated lysis of the infected cell by preventing the KLRK1 ligand 3/ULBP3 trafficking to the cell surface. Retains also another KLRK1 ligand, MHC class I-related chain A/MICA, in the Golgi apparatus to avoid its surface expression.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 34626
Sequence Length: 305
Subcellular Location: Host endoplasmic reticulum membrane
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Q68396 | MKPLIMLICFAVILLQLGVTKVCQHNEVQLGNECCPPCGSGQRVTKVCTDYTSVTCTPCPNGTYVSGLYNCTDCTQCNVTQVMIRNCTSTNNTVCAPKNHTYFSTPGVQHHKQRQQNHTAHITVKQGKSGRHTLAWLSLFIFLVGIILLILYLIAAYRSERCQQCCSIGKIFYRTL | Function: Activates NF-kappaB in a tumor necrosis factor receptor (TNFR)-associated factor 6 (TRAF6)-dependent manner, causing the up-regulation of the chemokine CCL22.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19624
Sequence Length: 176
Subcellular Location: Membrane
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F5H8Q3 | MLRLLFTLVLLALYGPSVDASRDYVHVRLLSYRGDPLVFKHTFSGVRRPFTELGWAACRDWDSMHCTPFWSTDLEQMTDSVRRYSTVSPGKEVTLQLHGNQTVQPSFLSFTCRLQLEPVVENVGLYVAYVVNDGERPQQFFTPQVDVVRFALYLETLSRIVEPLESGRLTVEFDTPDLALAPDLVSSLFVAGHGETDFYMNWTLRRSQTHYLEEMALQVEILKPRGVRHRAIIHHPKLQPGVGLWIDFCVYRYNARLTRGYVRYTLSPKARLPAKAEGWLVSLDRFIVQYLNTLLITMMAAIWARVLITYLVSRRR | Function: Chaperone protein that plays an important role in HCMV tropism. Cooperates with UL116 to regulate the abundance of gH-gL complexes in virion. Favors the incorporation of gL into virions once UL116 has regulated the early folding steps of virion assembly. Interacts with the host ERAD machinery and slows gO decay which would otherwise be constitutively degraded. Reorganizes the host endoplasmic reticulum and activates the unfolded protein response. Additionally, plays a role in the evasion of antiviral immune response by down-regulating cell surface expression of host CD58. Mechanistically, interacts with host CD58 and retains its immature form intracellularly. The capacity to cause endoplasmic reticulum reorganization and the intracellular retention of host CD58 are functionally independent properties.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 36504
Sequence Length: 316
Subcellular Location: Host endoplasmic reticulum membrane
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P16757 | MERRRGTVPLGWVFFVLCLSASSSCAVDLGSKSSNSTCRLNVTELASIHPGETWTLHGMCISICYYENVTEDEIIGVAFTWQHNESVVDLWLYQNDTVIRNFSDITTNILQDGLKMRTVPVTKLYTSRMVTNLTVGRYDCLRCENGTTKIIERLYVRLGSLYPRPPGSGLAKHPSVSADEELSATLARDIVLVSAITLFFFLLALRIPQRLCQRLRIRLPHRYQRLRTED | Function: Plays a role in escape from host immune response. Blocks the interaction between the host KLRK1 receptor with the ligands ULBP1 and ULBP2. ULBPs activate multiple signaling pathways in primary NK cells, resulting in the production of cytokines and chemokines. The sequestration of diverse KLRK1 ligands in the endoplasmic reticulum and cis-Golgi apparatus of cells by UL16 inhibits the activation of NK cells.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 26147
Sequence Length: 230
Subcellular Location: Host membrane
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P75294 | MLVIHFKPYNNLKMSFTSTENKHLLGVYEKAINNKFAWKDKIAIAKQASFDFIELSIDESDARLQRLDWSDTEINQLHNELQAQTFCLNSMCLSAHRRFPLGSKNKTTVQQGLTIFEKACVLARKLGIRIIQLAAYDVYYEPHDTETERNFITNMRKVAELAQKYAVTIAFEVMDTPFAGTIVRCLNLIKRIGKANILLYPDIGNLSQFSTAVFDEIALGQDKIVGFHFKDTLPKQFKEVPFGTGTAQFEAALKAIHQYVPTVPILIEMWSKNDPAESTVQNVAQLKQAKQFYEQQWDLALKRVK | Function: Catalyzes the isomerization of L-xylulose-5-phosphate to L-ribulose-5-phosphate. Is involved in the anaerobic L-ascorbate utilization (By similarity).
Catalytic Activity: L-ribulose 5-phosphate = L-xylulose 5-phosphate
Sequence Mass (Da): 34888
Sequence Length: 305
Pathway: Cofactor degradation; L-ascorbate degradation; D-xylulose 5-phosphate from L-ascorbate: step 3/4.
EC: 5.1.3.22
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A0A1X9QDU5 | MILLTIFWDTLLDILPIAAIIFGFQYIVIRKRIQRLPQVLAGFFMVWVGLSLFLVGLEQALFPMGELMASQLTNTDFLPAVEQGVQRHWADYYWVYLFAFAIGASTTIAEPSLIAVSIKAGEISGGTINPFMLRIAVALGMAFGITLGTWRIVMGWPLQWFVFAAYCLVIIQTLRSPKSIIPLAFDSGGVTTSTITVPIIAALGLGLAASIPGRSALMDGFGMIALACLFPIITVMGYAQIAQWKDKRKQTTPHLSYSKAPPPSKGDNNAL | Function: Part of a two-component antiporter that catalyzes the efflux of Na(+), Li(+) and K(+) in exchange for external protons. Shows a preference for Na(+), followed by K(+) and Li(+).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29561
Sequence Length: 271
Subcellular Location: Cell membrane
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P31754 | MAAADALLGSLVTGLYDVQAFKFGNFVLKSGLSSPVYIDLRGIISRPSILNQVAEMLFQTAENAEINFDTVCGVPYTALPLATIVCSTHEIPMLIRRKEKKDYGTKRLIEGAVNPGDTCLIIEDVVSSGSSVWETAEVLQKEGLKVTDAVVLVDREQGGRDNLQARGIRLHSVCTLSTVLCILEQQKKINAETVERVKRFIQENAFVAANPNDSLPSVKKEPKELSFGARAELPGTHPVAAKLLRLMQKKETNLCLSADVSESRELLQLADALGSRICLLKIHVDILNDFTLDVMKELTTLAKRHEFLIFEDRKFADIGNTVKKQYEGGVFKIASWADLVNAHAVPGSGVVKGLEEVGLPLHRACLLVAEMSSAGTLATGSYTEAAVQMAEEHSEFVIGFISGSRVSMKPEFLHLTPGVQLEAGGDNLGQQYHSPQEVIGKRGSDIIIVGRGIIASANQLEAAKMYRKAAWEAYLSRLAV | Function: Bifunctional enzyme catalyzing the last two steps of de novo pyrimidine biosynthesis, orotate phosphoribosyltransferase (OPRT), which converts orotate to orotidine-5'-monophosphate (OMP), and orotidine-5'-monophosphate decarboxylase (ODC), the terminal enzymatic reaction that decarboxylates OMP to uridine monophosphate (UMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 52229
Sequence Length: 480
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
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G5EDZ2 | MSSLTDKTRNGALKRNLLRQMLKASVFKFGEFQLKSGQISPIYIDLRECFGHPGLLMLISEAISKQVEISEVQYAGVLGIPYAALPYASVAAGNYLKKPLLIVRKEAKSYGTKKLIEGLYQPNDRLILIEDVVTTGGSILDVVKVLHTENLVASDVFCILDREQGGRQKLQDAGVTLHSLLDMQTVLTFLYSTGAIGDEQWHGIVQALNLPYTSPTKLEINSELENLSSLPYVENVRTPLAERESLTESALIKKILGIMRRKKSNLCLAVDYTTVEQCLQMIELAGPFVLAIKLHADAITDFNEEFTRKLTTMANDMDFIIFEDRKFGDTGNTNLLQLTGAQKIANWADVVTVHAVQGSDSIAGVFRKLAKDPTYRLSGVLLIAQLSTKGSLTALEGYTETAVKIANENRDVISGFITQTRVSACSDLLNWTPGVNLDAKSDSAGQQWRGVDEAIEVQQNDIIIVGRGVTSSSEPVQQLKRYRQIAWDALTRSDDSI | Function: Bifunctional enzyme which catalyzes the formation of UMP from orotate in the de novo pathway of pyrimidine biosynthesis . May also form UMP from uracil . Regulates the size of gut granules during embryonic development . Involved in resistance to DNA damaging agents including UV-C and X-ray radiation .
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 54805
Sequence Length: 497
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
Subcellular Location: Cytoplasm
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P09556 | MNIKELVLKLNEIDAIKLGEFKLKSGIISPIYIDLRVTVSSPPLLAAIAEMMYQKVYKSGNAQETPALVCGVPYTALPIATGMSIANNIPMVVRRKEAKAYGTKQLIEGRFKEGDNVLVVEDLVTSGASVLETVRDLNSVGLKVTDVVVLLDRQQGARQALEKQGYRLHSVFTMEELINTLIEAGKLTGRTLELVQSFLDANRNVVVPLPPTLAPPAPAPIVINKPFEERAKLASNPMASKLFTLMSSKKTNLAVAADLTDKQQLLDLAESIGSEICVLKTHVDIIDNYDEEFIKSLKCIAAKHNFLIFEDRKFADIGNTVKYQFENGVYKISKWADMVTVHGVAGSSIVDGFKSGLKEYGSGLLLLAQMSSKGSLCVGDYTTQMIEMANNNKEEVMGLICQERLPSMTDGLVLMTPGVQFNSTGDAMGQQYNTPEYIIKEKNTDVIIVGRGIYQSNDPKSVANKYRTAAWETYQSKF | Function: Participates in the last two steps of the pyrimidine biosynthetic pathway leading to UMP synthesis.
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 52519
Sequence Length: 478
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
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P11172 | MAVARAALGPLVTGLYDVQAFKFGDFVLKSGLSSPIYIDLRGIVSRPRLLSQVADILFQTAQNAGISFDTVCGVPYTALPLATVICSTNQIPMLIRRKETKDYGTKRLVEGTINPGETCLIIEDVVTSGSSVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAHGIRLHSVCTLSKMLEILEQQKKVDAETVGRVKRFIQENVFVAANHNGSPLSIKEAPKELSFGARAELPRIHPVASKLLRLMQKKETNLCLSADVSLARELLQLADALGPSICMLKTHVDILNDFTLDVMKELITLAKCHEFLIFEDRKFADIGNTVKKQYEGGIFKIASWADLVNAHVVPGSGVVKGLQEVGLPLHRGCLLIAEMSSTGSLATGDYTRAAVRMAEEHSEFVVGFISGSRVSMKPEFLHLTPGVQLEAGGDNLGQQYNSPQEVIGKRGSDIIIVGRGIISAADRLEAAEMYRKAAWEAYLSRLGV | Function: Bifunctional enzyme catalyzing the last two steps of de novo pyrimidine biosynthesis, orotate phosphoribosyltransferase (OPRT), which converts orotate to orotidine-5'-monophosphate (OMP), and orotidine-5'-monophosphate decarboxylase (ODC), the terminal enzymatic reaction that decarboxylates OMP to uridine monophosphate (UMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 52222
Sequence Length: 480
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
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Q25566 | METTTIDIQALKKELVLDLIQIGALKFGRFTLKSGIVSPFYVDLRIIGPKMLRQFSVLLYHVMTVKGLTNMEKRVICGVPYSALTFSSCMSMTYDLPMVICRKERKQYGTGNMVEGIYTKNETNCILIEDVITSGASIVETAEKLENEGLLVTDALVFLTREQLPLTNGMHILKKGEKVYNVHPCLTMTEVTQVLLDEGKMSQEQREDILQFIGTNTFSETKTTAVPQKKKELTFTERAELTNNEFSKKLFKLMEEKQTNLCVAADITSKDDLLKLADETGPEICMLKTHIDTLDDQPDEQFTQQLKELAKKHNFLIFEDRKLADIGQVVKQQYARGPFKIAQWSDLCNSHLVSGGSATVKALKESLKEENITEPRGLLLIAQMSTEGATTGESTKQEALKVALENPDFVSGFICQSKLRDDLDQFLYCTPGVRLDVKGDSLGQQYNSPEYVVCEKKCDVIIVGRGIYHDKERQNAAKLYRKLGWEAYQKRIQQ | Function: Bifunctional enzyme catalyzing the last two steps of de novo pyrimidine biosynthesis, orotate phosphoribosyltransferase (OPRT), which converts orotate to orotidine-5'-monophosphate (OMP), and orotidine-5'-monophosphate decarboxylase (ODC), the terminal enzymatic reaction that decarboxylates OMP to uridine monophosphate (UMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 55809
Sequence Length: 494
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
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P39615 | MKQLLQDSWWNQLKEEFEKPYYQELREMLKREYAEQTIYPDSRDIFNALHYTSYDDVKVVILGQDPYHGPGQAQGLSFSVKPGVKQPPSLKNIFLELQQDIGCSIPNHGSLVSWAKQGVLLLNTVLTVRRGQANSHKGKGWERLTDRIIDVLSERERPVIFILWGRHAQMKKERIDTSKHFIIESTHPSPFSARNGFFGSRPFSRANAYLEKMGEAPIDWCIKDL | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 26047
Sequence Length: 225
Subcellular Location: Cytoplasm
EC: 3.2.2.27
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Q8A5V6 | MNVQIEESWKTHLQPEFEKDYFRTLTEFVKSEYSQYQIFPPGKLIFNAFNLCPFDKVKVVIIGQDPYHGPGQAHGLCFSVNDGVPFPPSLVNIFKEIKADIGTDAPTTGNLTRWAEQGVLLLNATLTVRAHQAGSHQNRGWEAFTDAAIRALAEEREHLVFILWGAYAQRKGAFIDRNKHLVLSSAHPSPLSAYNGFFGNKHFSRANDYLKANGETEIIW | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 24837
Sequence Length: 220
Subcellular Location: Cytoplasm
EC: 3.2.2.27
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P53764 | MPYTRHALREYERRSRVEQVLPPKADIFAWTRYAAPEDIKVVILGQDPYHSRGQAHGLAFSVNRGVPVPPSLQNIYAAVQKNFPGAPRPSHGCLEDWARRGVLLLNTSLTVRSGAPGSHSSLGWGRLVHAVLARLSAESGPLVFMLWGAHAQRAFGAAGKRHLVLTYSHPSPLSRAPFVHCTHFAEANAFLEQHGRGGVDWSIV | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or deamination of cytosines. Therefore may reduce deleterious uracil incorporation into the viral genome, particularly in terminally differentiated cells which lack DNA repair enzymes.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 22421
Sequence Length: 204
Subcellular Location: Host nucleus
EC: 3.2.2.27
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Q9E6R2 | MAQLDLTGLTETSKMIVGECHVELKRCAEPPLAADEPMPKKCRRPAGPPKGFISTRGDTSPSSDNNHIHSIQSLTNGDSCVQPWDIIANAYNIHENWKQLLLPELCCLRGSEILAEYERRAITEEVYPPKMDIFAWTRYCAPESVKAVIVGQDPYANPGQAHGLAFSVKQGVAIPPSLKNILLAVKACYPSADLGNHGCLEAWSKRGVLLLNSVLTVKRGDPGSHHSVGWQFFIRNILRRLSSTTRGIVFMLWGAQAQTMYFQTDYDDRHLVLKYSHPSPLSRKPFATCTHFKEANDFLSKIGRGCIDWSLTA | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or deamination of cytosines. Therefore may reduce deleterious uracil incorporation into the viral genome, particularly in terminally differentiated cells which lack DNA repair enzymes.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 34805
Sequence Length: 313
Subcellular Location: Host nucleus
EC: 3.2.2.27
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B8F6C3 | MNSWTDAIGEEKTQPYFQHILQYVHQERLVGKVIYPPQNEVFSAFALTEFKDVKVVILGQDPYHGPNQAHGLSFSVKPGIVPPPSLVNMYKELSQDVGFQIPSHGYLIEWAKQGVLLLNTVLTVEQGKAHSHANIGWETFTDKVIHQLNLHRENLVFLLWGSHAQKKGQFIDRSRHCVLTAPHPSPLSAHRGFLGCRHFSKTNDYLRSHGVEEINWQLPL | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 25030
Sequence Length: 220
Subcellular Location: Cytoplasm
EC: 3.2.2.27
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P43731 | MKNWTDVIGTEKAQPYFQHTLQQVHLARASGKTIYPPQEDVFNAFKYTAFEDVKVVILGQDPYHGPNQAHGLAFSVKPEVAIPPSLLNIYKELTQDISGFQMPSNGYLVKWAEQGVLLLNTVLTVERGMAHSHANLGWERFTDKVIAVLNEHREKLVFLLWGSHAQKKGQMIDRTRHLVLTAPHPSPLSAHRGFFGCRHFSKTNSYLESHGIKPIDWQI | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 24848
Sequence Length: 219
Subcellular Location: Cytoplasm
EC: 3.2.2.27
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P16769 | MALKQWMLANIADNKGSLLTPDEQARVFCLSADWIRFLSLPDHDTVLLRDTVAAVEGARQLEMVYPAPEHVHRWSYLCPPEQVRVVIVGQDPYCDGSASGLAFGTLAGRPPPPSLNNVFRELARTVDGFQRPASGCLDAWARRGVLLLNTVFTVVHGQPGSHRHLGWQTLSNHVIRRLSERREHLVFMLWGADAHTCEYLIDRRRHLVLKSCHPSPRNTTRAFVGNDHFILANAYLDTHYRETMDWRLCG | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 28353
Sequence Length: 250
Subcellular Location: Host nucleus
EC: 3.2.2.27
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Q49VD1 | MEWSDVFHEITTRHDFAAMHDFLEKEYTTEIVYPDRKNIYQAFDLTPFEQVKVVILGQDPYHGPNQAHGLAFSVQPDAKFPPSLRNMYKELQDDVGCIRKSPHLQDWAREGVLLLNTVLTVRQGEAHSHKNIGWETFTDEVIQAVSEHLTHVVFILWGKPAQQKIKLIDTSKHHIIQSPHPSPLSAYRGFFGSKPYSQANTYLQANGKQPVNWCESEV | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 25050
Sequence Length: 218
Subcellular Location: Cytoplasm
EC: 3.2.2.27
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Q98NJ1 | MQGITELLPISSTAHMRIVPALLGWQDPGSAFSAAMQLAALAAVISYFWGDVRDLLFGSLDALTRRDFSDRHFRLASWIVLATIPIVIAGVALSGVLNACNSPLRSLTVIGWSCIAMAILLALAEIFARHKRTIAEASLADALLVGVAQIGALIPGVSRSGSTLTAALGLGFKRAEAARFSFLLGLPAIALAGLKELWELHKVHLDAHGWSVLATGLVVASISAFFAIWGLMRVLERFSAWPFVIYRGLLGVVLLLGLAMGWLA | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28109
Sequence Length: 264
Subcellular Location: Cell inner membrane
EC: 3.6.1.27
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A4VNS0 | MDLIQIIVLAIVQGLTEFLPVSSSAHLILFPHLVGWDDQGLAFDVAVHLGTLAAVVWYFRQEVFGMTRDWFASLARRERVGDSRLAWAVILGTIPAGIAGLLFKGFIEEQMRSPLVIAWATIGFGLLLWWSDVVSRRTPQPRDEHSLSWKDILLIGCAQALALIPGTSRSGVTMTAGLLLGLSRSGAARFSFLLSIPIIVLASGLSTLDLVEGEVAVDWTAMGLGVVLSAISAYLCIHFFLKLLERVGMLPFVIYRLILGAVLLVLFSGV | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29371
Sequence Length: 270
Subcellular Location: Cell inner membrane
EC: 3.6.1.27
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Q81V21 | MEQFYYILKYLILGLFQGLTEPIPISSSGHLVLAQHLLGLKIEGFSFELLVNSASLLAVLLIYRNDLIRLTKNGLSYIFTRAEDAKSDFFFIIYLVIATIPAGVIGVLFKDYIDQYLKGVKMVGISLLITAVGLWIIRNLRGRRNDGDLSMKDAIIVGLAQACALIPGISRSGATIVAAMLLGMKQETALRFSFLLYIPVSLGGLLLSITDIAKDPNLDTLFVPYIVAFIATFIMTYISLKWFMNIMAKGNLKYFSFYCIIVGVLTLIFL | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30004
Sequence Length: 270
Subcellular Location: Cell membrane
EC: 3.6.1.27
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Q81CP1 | MNWLEAFILGIIQGLTEFLPISSTGHLYLGRHLFRLDEAGLFLDTMLHIGTLLAVFIYYKKEFIYLIKNPFSKLMLLLIVGTIPAVVIGLLFKDFFEDISKTGITIGWEFLVSGFFLYMADKQKNGRKKMDDITYKDALIIGSFQAAAIFPAISRSGMTIVAALWRKLDRETAAYFSFLLSTPAIVGAIILQFVDVFQGKAESISSTSLIVGTLSAAFFGYIAVSWMIQYLKRHSLKVFAYYVWGLGILILMLQFTDVF | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29187
Sequence Length: 259
Subcellular Location: Cell membrane
EC: 3.6.1.27
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B0C1T8 | MTLLQAIILGIVQGLTEFLPVSSSGHLVLASYYLGWWEKLPLYVDIATNTGTFFAVLVVLRKDVWQALSGFFAGLTSSTARQQEGWRMALLVVLGSIPTAMIGLGLKPIFEELNQPLYVSFALIVTGLVLWFTPKSGLKRNAMSLSWLDATIGGIAQGCAVIPGISRSGSTISTMLWRGATSDLAPRFSFLMYLVVSFGVAILGIDEVREEGLQLAPLLGMIIASFVTGYIALLWLFSVLKKGQFKWFAPYLWVVAAITLIKVAMG | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28929
Sequence Length: 266
Subcellular Location: Cell inner membrane
EC: 3.6.1.27
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B1I2Y8 | MNPFEGIVMGIVQGLTEFLPVSSSAHLVLVPWLFGFETPGLVFDVALHLGTLVAVLVYFWRDWLRLVQAGSRGVGTADGRLFWFLVVATIPGVVVGYFLEDIVETTLRAPLLIGVLLIMMGGVLYLADRYGGQVKRLLDIRFGDAMAIGLSQALAIIPGVSRSGITMATARLRGVERAAAARFSFLLSTPIIFGAGLMQMLKMDPGLLNLSFVLGVFTSAVVGFLAIWFLISWVSRHSFNIFVIYRVLLGLTVIVIALLRG | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28373
Sequence Length: 261
Subcellular Location: Cell membrane
EC: 3.6.1.27
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B8FX50 | MALVEIFKAILLGIVEGITEWLPISSTGHMILVDEFIKLNMSAAFMEMFFVVIQLGAILAVVLLYWKKLNPFTFDRGVSVKQETIEMWFKIIVSCIPAGVIGLLWDDVFNALFYNYQTVAVMLIIFGILFIVIENYNKGKRPRVNHLSQITYTTAFMIGIFQLIAAIFPGTSRSGATIVGGLLLGVSRTVAAEFTFFLAIPVMFGASALKLLKFGFNFTGPELMILLIGMVVAFIVSVISIKFLMGYIKKNDFKIFGWYRIILGVIVLLYFSARTIIG | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31062
Sequence Length: 278
Subcellular Location: Cell membrane
EC: 3.6.1.27
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Q6AKL2 | MDVFQTIILGIIEGITEFLPISSTGHLIVASNWLSIEQNETNKAIEVIIQLAAILAVIANYRDKFTLKHKVLWSKVVLAFIPIGAIGLLFHKEIKTLFTVPMVGTMFIVGGIVFLVLEHFYQERSSHVQEVEAISYRQALWIGIAQVFALIPGTSRAGASIVGALLMGLSRKASAEFSFLLALPVLAAAAGFDLLTHYSDFSRGDMLTLSVGFITSFLIAYLTIRVFIGFLQRFTFVSFGIYRIAFGALLLWLG | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27978
Sequence Length: 254
Subcellular Location: Cell inner membrane
EC: 3.6.1.27
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P62464 | MSDMITAAILGLVEGLTEFLPVSSTGHLIITGELLGFTGPKATTFEVAIQLGAILAVVVLYWDRFWGLLRPQPYVRFAGLRGIMLLLLTSLPASVLGLAAHSTIKAHLFTPSTVAIALAVGAIFMLLVERRTERPRYMTLDEMSPALALGIGCFQCLALWPGFSRSAATIMGGMLLGARRGLAAEYSFIAAVPIMFAATGYDLLKSWTLFTPADLPFFATGFVVSFLSAWAAVKLFIALVGRMTFRPFAWYRLAIAPLVYYFMAY | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28820
Sequence Length: 265
Subcellular Location: Cell inner membrane
EC: 3.6.1.27
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A5EW93 | MTLWQAFILSLIQGITEFLPISSSGHLVITRELLHWQDAGVAFDAFTGLGTLTAVLFYYRKDVCSILYHWFRQFRHCDAPPAPEAKLGNQLIVATLPALLIGFMVKDHIDALTHRPLLIASTTMIFAIFLAAADFWGRKKLSLPETNYRQAFYYGLAQTLALVPGVSRSGITLTAGLAMHFSRESAARFSFLQSIPISAAAGGYGLWKLATNPSDFSWQLIALSYVTATLAAYVCIALFIRFLNTVGMMPHVIYRLLLGAYLFFVFM | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29701
Sequence Length: 267
Subcellular Location: Cell inner membrane
EC: 3.6.1.27
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A8LQR9 | MTLFHLILVAVIQGLTEFLPVSSSGHLILLPELSGMADQGQVIDVAVHVGTLFAVVLYFRADVAVAVAGVGRLIRGRIDTPGAFLALCLLIATVPVMVVGLALNLTGLDQALRSMAVIGWTMLIFGIVLYWADQRGPVTRKAGAWTLRHAAIMGLWQALALIPGTSRSGITITGARLLGYGREDAAKLSMLMSIPTILASGGLLGVEVAAQADWALLKDAAIGAVFAFGAALLALTLMMRLLRTVSFTPYVIYRVCLGTILLIIAYS | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28211
Sequence Length: 267
Subcellular Location: Cell inner membrane
EC: 3.6.1.27
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A1SRC7 | MSELQIVVLALIQGLTEFLPISSSAHLILPSQLLGWQDQGLAFDLILNIGTLSAVLIYFRMEVINMSRAWVGSLRGKGETQDSRLAWWILWSTIPAALIGFFGKSLVETYLRSGYVIAVTTTVFGLLLWWADANAKQVKTEYQTGLKGALFIGFAQVLALIPGTSRSGITITAGLMLGLTRNGAARFSFLMSIPIIAMASGYDLLKFILSDEYVDWGPLFLGAGISFVSAILCIHVFLILLNRVGMMPFVIYRLLLGGFLFYILSGT | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29256
Sequence Length: 267
Subcellular Location: Cell inner membrane
EC: 3.6.1.27
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Q8ZYX0 | MDLGVAAILGVVQGISEWLPISSKTQIMLVSIWLLNASPEYAYSLGLFLEAASVLAALIYFRGVYLKALRGFVGDAEGRRWLVYILVTTLVTAVVGLPLYYVARKWLVVGHSAGFLMIVLGLAVVLNAVFLQRARFSAGLKAFDNMSLRDMAIVGIAQAVSVLPGLSRSGATVTALLLLGYKPEEAFRASFVLVPVAGLGATALAYLSEGGAVATAEALLAMAIGIVISIITIKALLEFAKSKHVVLVNVVIGLLAIAGGLLRIIF | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP).
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28045
Sequence Length: 266
Subcellular Location: Cell membrane
EC: 3.6.1.27
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A5V412 | MEMSLLSIVLLGIVEGVTEFLPVSSTGHLILAGEVMKVPQGTETFDIVIQLGAILAVVVLYRERFAAVLAGLGRRDPAAIRFTRNVLVGFLPSAVIGAVAYGAIKAMLNTPIIVAVALILGGIAILVIERLVRSPTCDSVEGMSLRTSFGVGLVQCLSMIPGVSRSGATIMGALTLGVERRTAAEYSFFLAIPTMLGATTLALWKARHELGDAQATAIAIGFVVSFIVAMLVIRWFLGVVTRHGFAPFAWYRIIAGTAALIWLLAR | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28222
Sequence Length: 266
Subcellular Location: Cell inner membrane
EC: 3.6.1.27
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Q7UNQ8 | MQELIRVVILAIVQGIAEFLPISSSGHLVILGSMLGELGESVTLEIILHAGTLGSILVVFWQRIWALLLKDRRVIGLLVIGTLPAVVIGLTIKTQFPEILRSPLLAGAMLIVTGVMLIVLGRLTPKSGTYDRLGLGAAFLVGCFQAFAILPGISRSGSTILGGRLMGLDRDDSVTFSFLLAIPAILGATVLAIKDLLEDGSSGETSIEVLSIGAAVAFAVGIVALKWLIRWSREDRLHWFAYWCIPAGLLVVLLNLR | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27487
Sequence Length: 257
Subcellular Location: Cell inner membrane
EC: 3.6.1.27
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Q0SIC2 | MGEAMSWLQAIVLGTVQGLTEFLPISSSGHLRIVSEVFFGDDAGASFTAVTQLGTEAAVLIYFARDIGRIIAGWFRGLFHPEHRGDLDYRMGWYVIIGTIPVGVLGFLFKDQIRTGARNLWLIATMLIVFALVIAAAEYYGRKVRPVEDLRAKDGIIMGSAQALALIPGVSRSGGTISAGLFLGLTREAAARYSFLLAIPAVVASGLFSLPDAFEPAGEGLNASGPQLLVATVIAFAIGYASIAWLLRFVVDHSMYWFVGYRIILGVVVLSLLATGVVSAT | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30045
Sequence Length: 281
Subcellular Location: Cell membrane
EC: 3.6.1.27
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P60940 | MLIDIIRAVILGIVEGVTEFLPVSSTGHLLLAERFFNLGEGNFWKSFAVLIQLGAILAILALYFVKLWRIALGMFTDANARRFVIGVLVAFLPAAVIGAAFGGYIKHYLFNPWVVCFSLIVGGAILLWVDQLDLKPRYHDATAFPLLTYFYIGCAQCTAMIPGVSRSGASIVAAMLLGTDKRSAAEFSFFLAIPTMLGAFVYDLYKNHADMTADNLIIVAIGFVVSFITAIIVVKTFLTYVTRHGFELFAWWRVIVGTLGLIALALGL | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29341
Sequence Length: 268
Subcellular Location: Cell inner membrane
EC: 3.6.1.27
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Q89AP0 | MSYSKNNMLFKNVLNFKKNIPSHVAIIMDGNGKWARKRGKSRFFGHFSGFYAARRAISFALFHKLKILTLYAFSSDNWNRSPREIKVLMELFFYALSNETNNLNKYNIRLKVIGNKEKFNTVLKNKIRVVEKETLKNTGLLLNIAANYSGRWEILEAIKKIVVAIKCKNLSLNAITESTVSDFLLINEKIPVDLVIRTGGECRLSNFLVWQISYSELYFTNTLWPDFDRKEFKKAIDEFSNRERRFGRVSH | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di-trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = di-trans,octa-cis-undecaprenyl diphosphate + 8 diphosphate
Sequence Mass (Da): 29311
Sequence Length: 251
EC: 2.5.1.31
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Q5NHX6 | MFILSYHLANLIFFIIFMTSAKENILRHLAIIMDGNGRWAKSRLKPRIFGHRNSVSSVDATIEYCVENNIEMLTLFAFGRDNWLRPAQEVSDLMDLFYKTLKDKTPKLHDNNIVVTVVGDRSRLSNKLIGMIEYSESLTKSNTGLKLRLAVDYAGRWDIVEATRAIAREVDIGKLSVDEIDQNSFAKYLVGGNMPVDLLIRTSGEVRLSDFMLWQLAYAEMYFTDIMWPDFSKQELTRAVEYFYSRQRRFGKSGEQI | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di-trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = di-trans,octa-cis-undecaprenyl diphosphate + 8 diphosphate
Sequence Mass (Da): 29706
Sequence Length: 257
EC: 2.5.1.31
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A8B1Z2 | MIPMHVAVIMDGNGRWARKQLQERTFGHEQGVSVLESIVDECINCGIRFLTVYAFSTENWSRPPTEVSFLFELLSAAIQRVRTTYRERNVKVQFCGERTTQIPETVIAAMNCIEQDTAACTGLILSVCFNYGGHTEIAQACRSVLADCLEGDAVENIKTRLQMPIEQFIQQIDTHLYANLPPVDLLIRTGCEKRLSNFLPWHLAYAEIIFSDLLWPEFSVRAFKDCLDEFASRTRRFGGVQLSPMTGVYSDTHPHSSTNALSNHD | Function: Cis-prenyl transferase involved in the synthesis of dolichol, a long-chain polyprenol that is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER). Catalyzes the sequential condensation of isopentenyl pyrophosphate (IPP) with farnesyl pyrophosphate (FPP) to produce a polyprenyl pyrophosphate which contains 11 (major) and 12 (minor) isoprene units.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = di-trans,octa-cis-undecaprenyl diphosphate + 8 diphosphate
Sequence Mass (Da): 29968
Sequence Length: 265
Pathway: Protein modification; protein glycosylation.
EC: 2.5.1.31
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Q7VM20 | METSVNFDPSNMPQHVAIIMDGNGRWAKKQGKLRVFGHQNGVNAVRAAVHFAAKYGIKVLTLYAFSSENWNRPATEVSALMSLFIQALNTEVSKLHKHNIRLNILGDKTRFSDSLQKRIIESETLTAHNTRLTLNIAANYGSHWDITEATKKLAEKVKLGKISVTDITPEKVQRALVTAEQPPVDLLIRTSGEQRISNFLLWQIAYAELFFSDVLWPDFDETSFSEAIYAYQQRERRFGGCE | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di-trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = di-trans,octa-cis-undecaprenyl diphosphate + 8 diphosphate
Sequence Mass (Da): 27428
Sequence Length: 242
EC: 2.5.1.31
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P44938 | MIELDQTNIPKHVAIIMDGNGRWAKQKNKMRIFGHTNGVTAVRKAVAYARQIGVEVLTLYAFSSENWSRPEQEISALMSLFMQALDREVKKLHKNNICLKIIGDVSRFSETLQEKIKKAENLTEKNTALTLNIAANYGGCWDIIQAAKQIAEKVKKEEMSVSDINNSTFQHHLATQNAPPVDLLIRTSGEQRISNFLLWQIAYAELYFSDVLWPDFNQLEFNRAIASYQQRHRRFGGTE | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di-trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = di-trans,octa-cis-undecaprenyl diphosphate + 8 diphosphate
Sequence Mass (Da): 27343
Sequence Length: 239
EC: 2.5.1.31
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Q5V1I1 | MLSRGKRLGYAAYERLLQWELSGTPDHVAVIMDGNRRYAEKQGTKKQEGHKEGAQTTEALLNWCDELGIREVTLYTFSTENFDRDPEEREHIFDLVEQKLRTFADADRVHEAGVCIRAIGETEMLPERVRDAIDYAEGRTAQYDQLNLNIALAYGGRAELLGAARDVAAAVENETLDPTDVSAETIEERLYEGPTRDVDLIVRTGGDERTSNFLPWHANGNEAATFFCTPYWPEFRKVDFLRAIRTYQNREDSWRTTRAERSLALVRAIEQSELPTAKRMLGRFRDALPSTEREQLDEEYDLAD | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate (tritrans,heptacis-UPP). It is probably the precursor of glycosyl carrier lipids.
Catalytic Activity: geranylgeranyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + tri-trans,hepta-cis-undecaprenyl diphosphate
Sequence Mass (Da): 34830
Sequence Length: 304
EC: 2.5.1.89
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Q8TJQ7 | MKNRTFSMFYQEYEQLLEKEILSSEIPDHIAVIMDGNRRYAGQRGRTRSFGHAMGAEVTEQVIEWCYEIGVKELTLYAFSTENFQRSEEEVDGLFNLINEKFLKLYNDKRTYEKETQIRVIGDRTKLPAFLNKSIEKIEKATETHRKFNLNVAIAYGGRQDIMQAVRDIAACVSSGKLSLEDVDENLISKHLYPAPGVSVPNVDLIVRTGGDERVSNFLPWQANGSECATYFCAPFWPEFRKIDLLRSIRVYQARKDEKKQENSYRVSKVINFLGVGKYGEKSEELGQLLPLKKQGVA | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate (tritrans,heptacis-UPP). It is probably the precursor of glycosyl carrier lipids.
Catalytic Activity: geranylgeranyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + tri-trans,hepta-cis-undecaprenyl diphosphate
Sequence Mass (Da): 34231
Sequence Length: 298
EC: 2.5.1.89
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O26334 | MSPLKPLYKLYEWYISRNLRRDRMPRHVAIIMDGNRRYSKLQGSMNPIEGHKKGIETLEKVLDWCVDLGIEIVTAYAFSTENFKRPEKEVKGLMKLFRENFEAIASNEKIHKNRVRVRAVGKLELLPEDVRRAIEIAEKSTEQYSDRLVNIAIGYDGRQEIVDATRKIAEDVKAGLIDPEDIDEDMINRNLYTAGLEDPHLIIRTSGEERLSGFLLWQSSYSELYFCDSLWPELRKVDFLRAIRSYQQRERRFGV | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate (tritrans,heptacis-UPP). It is probably the precursor of glycosyl carrier lipids.
Catalytic Activity: geranylgeranyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + tri-trans,hepta-cis-undecaprenyl diphosphate
Sequence Mass (Da): 29900
Sequence Length: 255
EC: 2.5.1.89
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Q831G0 | MGKFQVIDHPLIQHKLTMIREKNCGTKVFREVVNEIAMLMAYEVSRDMPLEDVVIETPMGKSTQKTLSGKKVAIIPILRAGIGMVDGILELIPAAKVGHVGLYRDEETLQPHEYFVKLPEDIASRQLFVVDPMLATGGSAIMAIDSLKERGASNIKFVCLVAVPEGVKALQEAHPDVDIYTAALDERLNEDGYIVPGLGDAGDRLFGTK | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Function: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Catalytic Activity: diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil
Sequence Mass (Da): 22885
Sequence Length: 209
Pathway: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1.
EC: 2.4.2.9
|
Q92T49 | MDGVTVIGHPLVQHKLTIMRKKETSTAGFRRLLKEISTLLCYEVTRDLELTTERIETPLVETDAPVLEGKKLVFASILRAGNGLLEGMLELVPSARVAHIGVYRDHETLQAVEYFFKAPDNINERLVIVVDPMLATGNSAIAAIEKLKERGARNIRFLCLLAAPEGIRNFQGAHPDVPIFTASIDSHLNEKGYIVPGLGDAGDRMYGTK | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Function: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Catalytic Activity: diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil
Sequence Mass (Da): 23033
Sequence Length: 209
Pathway: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1.
EC: 2.4.2.9
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A7NRA6 | MKQVFISQHPLVHHKLTLLRRATTEPKKFRELVSELSQFLLYEATLDLPLQERAIDTPLAPYHGHQIAERIGLVPILRAGLGMVDPILDLIPTAHVWHLGLYRDHATLQPVTYYNKLPPEVDVDLCLVLDPMLATGGSAVAAVSILKEWGASRIKFLGLIAAPEGVRALHEAHPNVPIHLAALDDHLNDRGYIVPGLGDAGDRLFGTG | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Function: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Catalytic Activity: diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil
Sequence Mass (Da): 22876
Sequence Length: 208
Pathway: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1.
EC: 2.4.2.9
|
Q980Q4 | MPLYVIDKPITLHILTQLRDKYTDQINFRKNLVRLGRILGYEISNTLDYEIVEVETPLGVKTKGVDITDLNNIVIINILRAAVPLVEGLLKAFPKARQGVIGASRVEVDGKEVPKDMDVYIYYKKIPDIRAKVDNVIIADPMIATASTMLKVLEEVVKANPKRIYIVSIISSEYGVNKILSKYPFIYLFTVAIDPELNNKGYILPGLGDAGDRAFG | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Function: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Catalytic Activity: diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil
Sequence Mass (Da): 24150
Sequence Length: 216
Pathway: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1.
EC: 2.4.2.9
|
Q148G8 | MTTLRKLLLVGALLGAGAGVGTALFALVTPGEERKQAMLKEMPEQYPQRRDEAARTKELLLATLQEAAATQENVAWRKNWMSGGGGGGGGGGRSA | Function: Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex), mediating cytochrome b recruitment and probably stabilization within the complex. Thereby, plays an important role in ATP production by mitochondria. Cardiolipin-binding protein, it may also control the cardiolipin composition of mitochondria membranes and their morphology.
PTM: Probably cleaved by OMA1 under mitochondrial stress conditions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9925
Sequence Length: 95
Subcellular Location: Mitochondrion inner membrane
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B3DFP2 | MSGMRILTGSVALGGLTYAIWIIFSPGEERKKEILKSLPEANPVRMEETRKRNAIMLQVLKDAAETNDNIARGFGSQK | Function: Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex), mediating cytochrome b recruitment and probably stabilization within the complex. Thereby, plays an important role in ATP production by mitochondria. Cardiolipin-binding protein, it may also control the cardiolipin composition of mitochondria membranes and their morphology.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8649
Sequence Length: 78
Subcellular Location: Mitochondrion inner membrane
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Q6UW78 | MDSLRKMLISVAMLGAGAGVGYALLVIVTPGERRKQEMLKEMPLQDPRSREEAARTQQLLLATLQEAATTQENVAWRKNWMVGGEGGAGGRSP | Function: Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex), mediating cytochrome b recruitment and probably stabilization within the complex. Thereby, plays an important role in ATP production by mitochondria. Cardiolipin-binding protein, it may also control the cardiolipin composition of mitochondria membranes and their morphology.
PTM: Probably cleaved by OMA1 under mitochondrial stress conditions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 10081
Sequence Length: 93
Subcellular Location: Mitochondrion inner membrane
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Q8K2T4 | MEVARKALVAVAVLGGGAGVGSILFALVTPGELQKQSMLQEMPERDSRRRDEAVRTTELVMATLKDAAATKENVAWRRNWTVSGDGRSA | Function: Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex), mediating cytochrome b recruitment and probably stabilization within the complex. Thereby, plays an important role in ATP production by mitochondria. Cardiolipin-binding protein, it may also control the cardiolipin composition of mitochondria membranes and their morphology.
PTM: Probably cleaved by OMA1 under mitochondrial stress conditions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9584
Sequence Length: 89
Subcellular Location: Mitochondrion inner membrane
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Q2KP58 | METVRRIVKGTLLLGFCTGIGGDLWVLVAPGQERRLEMRMNYPEANPPMLAEAHKRNEMVLKVIEESAKTNENMARRSPWSS | Function: Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex), mediating cytochrome b recruitment and probably stabilization within the complex. Thereby, plays an important role in ATP production by mitochondria. Cardiolipin-binding protein, it may also control the cardiolipin composition of mitochondria membranes and their morphology.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9313
Sequence Length: 82
Subcellular Location: Mitochondrion inner membrane
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Q4G0I0 | MNRVLCAPAAGAVRALRLIGWASRSLHPLPGSRDRAHPAAEEEDDPDRPIEFSSSKANPHRWSVGHTMGKGHQRPWWKVLPLSCFLVALIIWCYLREESEADQWLRQVWGEVPEPSDRSEEPETPAAYRART | Function: Required for the assembly and stability of the mitochondrial ubiquinol-cytochrome c reductase complex (complex III (CIII) or cytochrome b-c1 complex), a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain (ETC) which drives oxidative phosphorylation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15004
Sequence Length: 132
Subcellular Location: Mitochondrion inner membrane
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Q6RUT7 | MNSVLCSRAAGAVRALRLVGWASRSLHPPPRGRSPAQPADREEEDDDPNLPIQFSGSKATPIRWTVEHSLGKPQQRPWWKVLPLTLTLVALVVWCYQREESGMDLWLRQVLEEEDEEEPEGPPEELEAPALYGART | Function: Required for the assembly and stability of the mitochondrial ubiquinol-cytochrome c reductase complex (complex III (CIII) or cytochrome b-c1 complex), a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain (ETC) which drives oxidative phosphorylation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15348
Sequence Length: 136
Subcellular Location: Mitochondrion inner membrane
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A8WGU8 | MWGSLCKAPLLRLRPTFAAVSNVKTIHIKASPDYNEGIDKSKPLKFSTSKASHRHWTVAKSLGSNQQRPWWKVVPLSVFLTTVLLWAIFRKETDIDEAIYKPIEQLQDESENK | Function: Required for the assembly and stability of the mitochondrial ubiquinol-cytochrome c reductase complex (complex III (CIII) or cytochrome b-c1 complex), a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain (ETC) which drives oxidative phosphorylation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 12964
Sequence Length: 113
Subcellular Location: Mitochondrion inner membrane
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Q8WVI0 | MFTRAQVRRILQRVPGKQRFGIYRFLPFFFVLGGTMEWIMIKVRVGQETFYDVYRRKASERQYQRRLEDE | Function: Required for the assembly and stability of the mitochondrial ubiquinol-cytochrome c reductase complex (complex III (CIII) or cytochrome b-c1 complex), a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain (ETC) which drives oxidative phosphorylation (By similarity). Mediates early complex III biogenesis (By similarity). Participates in regulating the levels of electron transport chain proteins, and therefore energy supply, in response to changes in energy demand (By similarity). Also involved in the first steps of cytochrome c oxidase complex (complex IV) assembly .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8696
Sequence Length: 70
Subcellular Location: Mitochondrion inner membrane
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P18314 | MSNISRQAYADMFGPTVGDKVRLADTELWIEVEDDLTTYGEEVKFGGGKVIRDGMGQGQMLAADCVDLVLTNALIVDHWGIVKADIGVKDGRIFAIGKAGNPDIQPNVTIPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMVGGGTGPAAGTHATTCTPGPWYISRMLQAADSLPVNIGLLGKGNVSQPDALREQVAAGVIGLKIHEDWGATPAAIDCALTVADEMDIQVALHSDTLNESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTLNTIDEHLDMLMVCHHLDPDIAEDVAFAESRIRRETIAAEDVLHDLGAFSLTSSDSQAMGRVGEVILRTWQVAHRMKVQRGALAEETGDNDNFRVKRYIAKYTINPALTHGIAHEVGSIEVGKLADLVVWSPAFFGVKPATVIKGGMIAIAPMGDINASIPTPQPVHYRPMFGALGSARHHCRLTFLSQAAAANGVAERLNLRSAIAVVKGCRTVQKADMVHNSLQPNITVDAQTYEVRVDGELITSEPADVLPMAQRYFLF | Cofactor: Binds 2 nickel ions per subunit.
PTM: Carboxylation allows a single lysine to coordinate two nickel ions.
Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 60305
Sequence Length: 567
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.1.5
|
P17337 | PQISRQEYGGLFGPT | Cofactor: Binds 2 nickel ions per subunit.
Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 1650
Sequence Length: 15
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.1.5
|
Q07398 | MIPGEYVLKKEPILCNQNKQTIKIRVLNRGDRPVQVGSHFHFFEVNQSLQFHREKAFGMRLNIPAGTAVRFEPGDAKEVEIIPFSGERKVYGLNNVTNGSVEMGKRK | Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 12183
Sequence Length: 107
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.1.5
|
P71035 | MKPGAFQIAEGTITINEGREIREVTVKNTGSRSIQVGSHFHFAEANGALLFDRELAIGMRLDVPSGTSVRFEPGEQKTVSLVEIRGRKTIRGLNGMADTFIDERGKEKTLANLKQAGWMEGVIR | Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 13644
Sequence Length: 124
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.1.5
|
Q492E8 | MIPGEFYISHGNIELNVGRQQVLVTIINTGDRPIQIGSHFHFYEVNSALKFNRVITRGFRLNIPSGTAIRFEPGQFRTVELVKYAGACKIYGFCKAIMGKLD | Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 11491
Sequence Length: 102
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.1.5
|
Q89UG2 | MIPGELFIQDGEIELNAGRKTVTLTVANTGDRPIQVGSHYHFFETNPALKFERKKARGMRLDIAAGTAVRFEPGQTRDVQLVALAGKKTIYGFRGDVMGKL | Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 11134
Sequence Length: 101
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.1.5
|
Q55054 | MIPGEYHVASEPIDYNGGYEAISLEVKNVGDRAAQVGSHYHFYEANEAGLQFDREKARGKRLDIPAGTAIRFEPGETKTVQLIDFGGKRRIFGFNNKVNGFLD | Function: Ureolysis may allow urea to be employed as a nitrogen source for growth and produces ammonia which may protect from killing at low pH.
Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 11478
Sequence Length: 103
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.1.5
|
B1W5G8 | MIPGEILHGDGDIPLNAGRPVTRLTVLNAADRPVQVGSHYHFAEANPGLRFDRAAAHGLRLNIAAGTAVRFEPGIPADVELVPLTGRRVVPGLRGETGGALDA | Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 10748
Sequence Length: 103
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.1.5
|
O87401 | MAPFIPGELLPEPGEIELNAGRPVTSLHVANSGDRPVQVGSHFHFAEANAALQFDRTAARGQRLDIPAGTAIRFEPGDSRDVNLIPFAGDRRVIGFNGQINGPLDA | Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 11298
Sequence Length: 106
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.1.5
|
Q3AVR2 | MAPLIPGELIPEPGELELNAGRPVTTISVANGGDRPVQVGSHFHFAEANAALQFDRDAARGQRLDIPAGTAIRFEPGDHRDVNLIPFAGHRRVIGFNGRINGPIDA | Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 11312
Sequence Length: 106
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.1.5
|
P74386 | MATMIPGEIITPEGDIELNVGRSTCTINVANTGDRPIQVGSHYHFYEVNAALQFDRDLAKGMRLDIPAGTAVRFEPGDEKNVNLVAYAGSREIYGFNGLVNGPLE | Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 11382
Sequence Length: 105
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.1.5
|
Q87VP4 | MDLTPREKDKMLIFTAGLVAERRLARGVKLNYPEAMAYISAALLEGARDGQTVADLMHYGTTLLTRDQVMEGIPEMIPEIQVEATFPDGTKLVTVHQPIA | Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 11042
Sequence Length: 100
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.1.5
|
Q49Y49 | MKSTTIIGIAGGSGSGKTSVTNEIMKNLEGHSVALLAQDYYYKDQSHLTFDERLETNYDHPFAFDNDLLIDNLNDLRNGKQVEVPTYDYSNHTRSKETIAFEPKDVIIVEGIFALENKTLRDLMDVKIYVDTDADLRILRRLLRDTEERGRTMESVINQYLNVVRPMHNQFIEPTKRYADIIIPEGGSNKVAIDIMTTKIQTLVSKQ | Catalytic Activity: ATP + uridine = ADP + H(+) + UMP
Sequence Mass (Da): 23645
Sequence Length: 207
Pathway: Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.1.48
|
Q8DTG1 | MRKKPIIIGVTGGSGSGKTSVSRAILANFPNAKIAMIEHDSYYKDQSHLTFEERVTTNYDHPLAFETDLLINHLKELIADRPVDIPIYDYTQHTRSEKSYRQEPQDVFIVEGILVLEDQRLRDLMDIKLFVDTDDDIRIIRRIKRDMQERGRSLDSIIEQYTRVVKPMYHQFIEPTKRYADIVVPEGVSNLVAIDLINTKVASILNETH | Catalytic Activity: ATP + uridine = ADP + H(+) + UMP
Sequence Mass (Da): 24184
Sequence Length: 209
Pathway: Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.1.48
|
Q5T230 | MLLRPRRPPPLAPPAPPSPASPDPEPRTPGDAPGTPPRRPASPSALGELGLPVSPGSAQRTPWSARETELLLGTLLQPAVWRALLLDRRQALPTYRRVSAALAQQQVRRTPAQCRRRYKFLKDKFREAHGQPPGPFDEQIRKLMGLLGDNGRKRPRRRSPGSGRPQRARRPVPNAHAPAPSEPDATPLPTARDRDADPTWTLRFSPSPPKSADASPAPGSPPAPAPTALATCIPEDRAPVRGPGSPPPPPAREDPDSPPGRPEDCAPPPAAPPSLNTALLQTLGHLGDIANILGPLRDQLLTLNQHVEQLRGAFDQTVSLAVGFILGSAAAERGVLRDPCQ | Function: Acts as a transcriptional coactivator of ATF2.
PTM: Phosphorylated.
Sequence Mass (Da): 36439
Sequence Length: 341
Domain: The leucine-zipper domain is required for coactivation activity. When this domain is deleted, the protein is able to stimulate transcription from a number of gene promoters (By similarity).
Subcellular Location: Nucleus
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Q6J1H4 | MLLRPRRLPAFSPPSPASPDAELRSAGDVPVTTSDAFATSGGMAEPGSPKAPVSPDSAQRTPWSARETELLLGTLLQPAMWRSLLLDRRQTLPTYRRVSAALARQQVRRTPAQCRRRYKFLKDKLRDSQGQPSGPFDNQIRQLMGLLGDDGPPRVRRRSTGPGRPQRRGRSSLSALAPAPAPVEQEAELPLAAENDEPAPALRFSSSTTKSAGAHRITSSPPLTSTDTLPPEPGHTFESSPTPTPDHDVETPNEPPGLSQGRASSPQVAPQSLNTALLQTLTHLGDISTVLGPLRDQLSTLNQHVEHLRGSFDQTVSLAVGFILGSAASERGILGDLRQ | Function: Acts as a transcriptional coactivator of ATF2.
PTM: Phosphorylated.
Sequence Mass (Da): 36408
Sequence Length: 339
Domain: The leucine-zipper domain is required for coactivation activity. When this domain is deleted, the protein is able to stimulate transcription from a number of gene promoters.
Subcellular Location: Nucleus
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P36135 | MKLSALLALSASTAVLAAPAVHHSDNHHHNDKRAVVTVTQYVNADGAVVIPAATTATSAAADGKVESVAAATTTLSSTAAAATTSAAASSSSSSSSSSSSSSSVGSGDFEDGTISCSDFPSGQGAVSLDWLGLGGWASIMDMNGNTATSCQDGYYCSYACSPGYAKTQWPSEQPSDGRSVGGLYCKNGKLYRSNTDTNSLCVEGQGSAQAVNKVSGSIAICGTDYPGSENMVVPTVVGAGSSQPINVIKEDSYYQWQGKKTSAQYYVNNAGVSVEDGCIWGTEGSGVGNWAPVVLGAGYTDGITYLSIIPNPNNKEAPNFNIKIVATDGSTVNGACSYENGVYSGSGSDGCTVSVTSGSANFVFY | Function: Involved in aging, oxidative stress response, and in the regulation of mitochondrial biogenesis. Inactivation of UTH1 increases life span, leads to higher resistance to heat stress and against hydrogen peroxide, and increases sensitivity to the superoxide radical-generating drug paraquat and to copper. Also required for the selective autophagic degradation of mitochondria (mitophagy) in response to nitrogen starvation. Involved in the remodeling of the cell wall during the various phases of yeast culture development and under various environmental conditions and plays a role in septation. Involved in cell sensitivity to boric acid.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 36955
Sequence Length: 365
Subcellular Location: Mitochondrion outer membrane
EC: 3.2.1.-
|
Q45978 | MASPARAPVLALKDVRLADGAKPLFDGVDLALEPRVRACLVGRNGAGKSTLLKILAGQGVEADSGERAVQPGAKVVYVSQEPEITGETLLDYATAGGAQDYEAQAALADFGLDPDKSAKGLSGGETRRAALARAFAEQPDVLLLDEPTNHLDIFAIQTLEDELAASKCAALIVSHDRAFLNRVTERCFWLEHRKIRRLDKGFSEFEAWAESIMAADAEEARRLDKVLERENAWLARGVQGRRARNEGRRRALLALRAEKKDRQSELRGTMTMAVESAGTSGKRVVEAKGVTKRFGERTIVENFSTRILRGDRVALVGPNGAGKTTLVKLLLGELERDAGTVQLGTNLEVSYIDQARMALSDKITVWDFLTPGGGDSIIVRGHPKHVAGYAKEFLFTDAQLRQPVTSLSGGERNRLLLARALANPTNLMVLDEPTNDLDMDTLDLLEDLLADFDGTLILVSHDRDFIDRLASSTIALDGKGGVVETPGGWTDLMDQNPDFFKASKGGTAFAPVSKAATKPAPAAPAAPKKSAKLSYKDQRRLEECEALIAKSPAIIAKLEEALADPNLYTRDPATFDKTMKALDKARADLEQAEMEWLELEEKKENLAG | Function: Probably plays a role in ribosome assembly or function. May be involved in resolution of branched DNA intermediates that result from template switching in postreplication gaps. Binds DNA and has ATPase activity.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 66006
Sequence Length: 608
Domain: The C-terminal domain (CTD) helps bind DNA.
Subcellular Location: Cytoplasm
EC: 3.6.1.-
|
P43672 | MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVEGSVYDFVAEGIEEQAEYLKRYHDISRLVMNDPSEKNLNELAKVQEQLDHHNLWQLENRINEVLAQLGLDPNVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQYLLEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKAMRRERGERREVMGTAKMQVEEASRSGKIVFEMEDVCYQVNGKQLVKDFSAQVLRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHVGTKLEVAYFDQHRAELDPDKTVMDNLAEGKQEVMVNGKPRHVLGYLQDFLFHPKRAMTPVRALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELIDSYQGTVLLVSHDRQFVDNTVTECWIFEGGGKIGRYVGGYHDARGQQEQYVALKQPAVKKTEEAAAAKAETVKRSSSKLSYKLQRELEQLPQLLEDLEAKLEALQTQVADASFFSQPHEQTQKVLADMAAAEQELEQAFERWEYLEALKNGG | Function: Probably plays a role in ribosome assembly or function; overexpression suppresses cold-sensitive growth of a bipA deletion (Ref.10) (Probable). May be involved in resolution of branched DNA intermediates that result from template switching in postreplication gaps. Binds DNA at Holliday junctions. May be involved in the correct segregation of nucleoids . Has ATPase activity, binds DNA non-sequence specifically; the presence of DNA does not change the ATPase activity . Mutations in this gene cause an increase in RecA-independent precise excision of transposons and insertion elements, and also reduce bacteriophage Mu growth .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 72067
Sequence Length: 635
Domain: The C-terminal domain (CTD) helps bind DNA, is required to complement a gene deletion.
Subcellular Location: Cytoplasm
EC: 3.6.1.-
|
Q5UNU2 | MNQNLIRLGYACLNSDLRNYDIFTSRKPILKTVKSQGFDYVKETIIRNLRDLFTIIIYNESHGIRFFRISSSIFPHLGNPLLPDSDYDLSFAKNLIKEIGSYAKINGHRLTMHPGQFVQLGSNNEEVVRRSFVELQNHATLLEMLGYSSLDSSVLIVHGGGTFGDKETTLERWKSNFRKLPENIRQLICLENDENSYGILDLLPVCEELNVPFCLDIFHNRVSKNRIPLTKKLMKRIINTWKRRNMTPKMHFSNQEPGLRRGAHSKTINELPEYLFRIPDMFQTSLDIILEVKDKEKSVLKMYFKYFDIETNIDGRNNFILKKDYSLKKN | Function: Endonuclease for the repair of UV-irradiated DNA.
Sequence Mass (Da): 38547
Sequence Length: 330
Subcellular Location: Virion
EC: 3.-.-.-
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O48652 | MQRFCVCSPSSYRLNPITSMATGSGSLIWFRKGLRVHDNPALEYASKGSEFMYPVFVIDPHYMESDPSAFSPGSSRAGVNRIRFLLESLKDLDSSLKKLGSRLLVFKGEPGEVLVRCLQEWKVKRLCFEYDTDPYYQALDVKVKDYASSTGVEVFSPVSHTLFNPAHIIEKNGGKPPLSYQSFLKVAGEPSCAKSELVMSYSSLPPIGDIGNLGISEVPSLEELGYKDDEQADWTPFRGGESEALKRLTKSISDKAWVANFEKPKGDPSAFLKPATTVMSPYLKFGCLSSRYFYQCLQNIYKDVKKHTSPPVSLLGQLLWREFFYTTAFGTPNFDKMKGNRICKQIPWNEDHAMLAAWRDGKTGYPWIDAIMVQLLKWGWMHHLARHCVACFLTRGDLFIHWEQGRDVFERLLIDSDWAINNGNWMWLSCSSFFYQFNRIYSPISFGKKYDPDGKYIRHFLPVLKDMPKQYIYEPWTAPLSVQTKANCIVGKDYPKPMVLHDSASKECKRKMGEAYALNKKMDGKVDEENLRDLRRKLQKDEHEESKIRNQRPKLK | Cofactor: Binds 1 FAD per subunit.
Function: Involved in repair of UV radiation-induced DNA damage. Catalyzes the photoreactivation of pyrimidine [6-4] pyrimidone photoproduct (6-4 products). Binds specifically to DNA containing 6-4 products and repairs these lesions in a visible light-dependent manner. Not required for repair of cyclobutane pyrimidine dimer (CPD).
Catalytic Activity: (6-4) photoproduct (in DNA) = 2 pyrimidine residues (in DNA).
Sequence Mass (Da): 63790
Sequence Length: 556
EC: 4.1.99.13
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Q0E2Y1 | MDAAATAATATAAAAMVWFRKGLRVHDNPALDAARRGGAAARLYPVFVLDPRYLRPDQAAPSPGSARAGVARVRFLLESLSDLDARLRRLGSRLLLLRARDDGDVAGTVCAALKDWNIGKLCFESDTEPYALARDKKVMDFAAASGIDVFSPVSHTLFDPAEIIEKNGGRPPMTYQSFVAIAGEPPEPIMEEYSELPPVGDTGEYELLPVPRVEELGYGDISQEDLSLFRGGETEALKRMRESLHDKEWVAKFEKPKGDPSAFLKPATTVLSPYLKFGCLSSRYFYHCIQDIYRSTKKHTNPPVSLTGQLLWRDFFYTVAFGTPNFDQMKGNKICKQIPWTENEELFPAWRDGRTGYPWIDAIMIQLRKWGWMHHLARHSVACFLTRGDLFIHWEKGRDVFERLLIDSDWAINNGNWMWLSCSSFFYQYHRIYSPTSFGKKYDPNGNYIRHFIPVLKDMPKEYIYEPWTAPLSIQKKANCIIGKDYPKPVVDHAIASKECKKMMGEAYASNRLDDDKPDKGKSSNSSRRKLSAGSQVTPNSSKTKQLKRSS | Cofactor: Binds 1 FAD per subunit.
Function: Involved in repair of UV radiation-induced DNA damage. Catalyzes the photoreactivation of pyrimidine [6-4] pyrimidone photoproduct (6-4 products) (By similarity).
Catalytic Activity: (6-4) photoproduct (in DNA) = 2 pyrimidine residues (in DNA).
Sequence Mass (Da): 62264
Sequence Length: 551
EC: 4.1.99.13
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Q9P2Y5 | MSASASVGGPVPQPPPGPAAALPPGSAARALHVELPSQQRRLRHLRNIAARNIVNRNGHQLLDTYFTLHLCSTEKIYKEFYRSEVIKNSLNPTWRSLDFGIMPDRLDTSVSCFVVKIWGGKENIYQLLIEWKVCLDGLKYLGQQIHARNQNEIIFGLNDGYYGAPFEHKGYSNAQKTILLQVDQNCVRNSYDVFSLLRLHRAQCAIKQTQVTVQKIGKEIEEKLRLTSTSNELKKKSECLQLKILVLQNELERQKKALGREVALLHKQQIALQDKGSAFSAEHLKLQLQKESLNELRKECTAKRELFLKTNAQLTIRCRQLLSELSYIYPIDLNEHKDYFVCGVKLPNSEDFQAKDDGSIAVALGYTAHLVSMISFFLQVPLRYPIIHKGSRSTIKDNINDKLTEKEREFPLYPKGGEKLQFDYGVYLLNKNIAQLRYQHGLGTPDLRQTLPNLKNFMEHGLMVRCDRHHTSSAIPVPKRQSSIFGGADVGFSGGIPSPDKGHRKRASSENERLQYKTPPPSYNSALAQPVTTVPSMGETERKITSLSSSLDTSLDFSKENKKKGEDLVGSLNGGHANVHPSQEQGEALSGHRATVNGTLLPSEQAGSASVQLPGEFHPVSEAELCCTVEQAEEIIGLEATGFASGDQLEAFNCIPVDSAVAVECDEQVLGEFEEFSRRIYALNENVSSFRRPRRSSDK | Function: Versatile protein that is involved in regulation of different cellular pathways implicated in membrane trafficking. Involved in regulation of the COPI-dependent retrograde transport from Golgi and the endoplasmic reticulum by associating with the NRZ complex; the function is dependent on its binding to phosphatidylinositol 3-phosphate (PtdIns(3)P) . During autophagy acts as regulatory subunit of the alternative PI3K complex II (PI3KC3-C2) that mediates formation of phosphatidylinositol 3-phosphate and is believed to be involved in maturation of autophagosomes and endocytosis. Activates lipid kinase activity of PIK3C3 . Involved in the regulation of degradative endocytic trafficking and cytokinesis, and in regulation of ATG9A transport from the Golgi to the autophagosome; the functions seems to implicate its association with PI3KC3-C2 . Involved in maturation of autophagosomes and degradative endocytic trafficking independently of BECN1 but depending on its association with a class C Vps complex (possibly the HOPS complex); the association is also proposed to promote autophagosome recruitment and activation of Rab7 and endosome-endosome fusion events . Enhances class C Vps complex (possibly HOPS complex) association with a SNARE complex and promotes fusogenic SNARE complex formation during late endocytic membrane fusion . In case of negative-strand RNA virus infection is required for efficient virus entry, promotes endocytic transport of virions and is implicated in a VAMP8-specific fusogenic SNARE complex assembly .
PTM: Phosphorylated at Ser-498 by MTOR under basal conditions; increases the interaction with RUBCN implicated in inhibitory effect of RUBCN on PI3KC3 and decreases interaction with RAB7,A and VPS16 and VPS39 (indicative for a class C Vps complex, possibly the HOPS complex) .
Sequence Mass (Da): 78151
Sequence Length: 699
Subcellular Location: Late endosome
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B0JR86 | MTAFQLQAPFQPTGDQPAAIDQLVDSLQNQHRFQTLLGATGTGKTFTIAAVIEKIGRPTLVLAHNKTLAAQLCNELRQFFPNNAVEYFISYYDYYQPEAYIPVSDTYIEKSSSINDEIDMLRHSATRSLFERRDVIVVASISCIYGLGMPAEYLKAAISLTVGQEFDQRQLLRALVSVQYNRNDLELTRGRFRLKGDILEIVPAYEDRVIKIDFFGDEIESIRYLDPLTGEVLQKLERISIYPARHFVTPEERLEVACRDIKTELDNRLLELEKAGKLLEAQRLDQRTRYDLEMLQEVGYCNGVENYSRHLAGRLAGEPPECLVDYFPEDWLLVVDESHVSVPQIRGMYNGDQSRKKVLIDHGFRLPSAADNRPLKSEEFWQKVNQCIFVSATPGDWELEQSENRIVEQIIRPTGVLDPEIFVRPTEGQVDDLLGEIKERVQLNERVLITTLTKRMAEDLTEYLQERGIKVRYLHSEIQSIQRIEIIQDLREGVFDVLIGVNLLREGLDLPEVSLVAILDADKEGFLRATRSLIQTIGRAARHIRGQAILYGDNLTDSMINAIEETKRRRAIQQEYNQKHGIIPQPIVKRSSNSILAFLDISRRLNSQQLEQVCENIEELSLEQIPELIQQLEAQMKEAAKNLEFESAAKYRDRIKQLRDKLLNHVR | Function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Sequence Mass (Da): 76625
Sequence Length: 667
Domain: The beta-hairpin motif is involved in DNA binding.
Subcellular Location: Cytoplasm
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P47319 | MKNQTKSNSLFQLSTNYIPTGDQPEAIKKLSEFKTKQQVLLGATGTGKTFTIANVIQNSQLPTVVIAHNKTLAGQLFNELKQLFPKNAVEYFISYFDFYQPEAYLPSKGIYIEKSATVNEAIKRLRVSTLHSLSTRKDVIVVGSVASIYPTSSPSDFVKYCLWFVVGKDYDLKTIKDRLVSLNYVVNKQQLTPGKFRFQGDVLEVFPGYSDAFVIRISFFDTKVEQICQIDPLTNKILNQLFEIKIGPADEYVVNQSDLDIAIKNIKQELQERVNYFNKQNLVERAQRLATITNHDLNDLKAWGFCSGVENYARHLELRMANSTPYSIFDYFKGDWLLVIDESHQTLPQLNGMYNTDLSRKQSLIDYGFRLPSALDNRPLSFAELQQKMQKVIYVSATPRDKEISLSQNNVIEQLVRPTYLVDPIIVVKPKDNQVEDLIEEIINQRQNNTRTFVTVLTIKMAENLTEYLKERKIKVAYIHKDIKALERLLLINDLRRGEYECLVGINLLREGLDVPEVALVCIFDADIPGLPRDERSLIQIIGRAARNEHGRVVMYANHVTEQMQKAIDETKRRRTVQMEYNKLHNKTPKTVVKPLTFVQPIKLKAKSNAEKNAALIKQLTKEMKKAAANQNYELAIEIRDSIFELEKEIGSKIKV | Function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Sequence Mass (Da): 75202
Sequence Length: 656
Domain: The beta-hairpin motif is involved in DNA binding.
Subcellular Location: Cytoplasm
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P57991 | MRVGGRFEVISPHEPAGDQPAAIDELQRRILAGERDVVLLGATGTGKSATTAWLIERLQRPTLVMAPNKTLAAQLANELRGMLPHNAVEYFVSYYDYYQPEAYIAQTDTYIEKDSSINDDVERLRHSATSSLLSRRDVVVVASVSCIYGLGTPQSYLDRSVELAVSNEVPRDGLLRLLVDVQYTRNDLSFTRGSFRVRGDTVEIIPSYEELAVRIEFFGDEIEALYYLHPLTGEVIRQVDSLRIFPATHYVAGPERMAQAISAIEEELAERLAEFERQGKLLEAQRLRMRTNYDIEMMRQVGFCSGIENYSRHIDGRGPGTPPATLLDYFPEDFLLVIDESHVTVPQIGGMYEGDMSRKRNLVEYGFRLPSACDNRPLTWEEFADRIGQTVYLSATPGPYELSQSGGEFVEQVIRPTGLVDPKVVVKPTKGQIDDLIGEIRKRANADQRVLVTTLTKKMAEDLTDYLLEMGIRVRYLHSEVDTLRRVELLRQLRLGDYDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSARSLIQTIGRAARNVSGEVHMYADTITDSMTEAIDETERRRAKQIAYNNANGIDPQPLRKKIADILDQVYREADDTDTVQVGGSGRNVSRGRRAQSEPVRSVSVGVFEGRDTAGMPRAELADLIKDLTAQMMAAASDLQFELAARFRDEIADLKKELRGMDAAGLK | Function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Sequence Mass (Da): 78159
Sequence Length: 698
Domain: The beta-hairpin motif is involved in DNA binding.
Subcellular Location: Cytoplasm
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Q6MS38 | MLWEKVMFIANNKYKLVTKYKPSGDQNQAIEKLNKAIIENKKHQVLLGATGTGKTFTIANIIAKHNKQALVIAHNKTLAMQLYYELKEMFPENRVEYFVSNFDFFQPEAYIPSKDLYIDKDSRQNMELDMMRLSACNALLTRNDTIVVASVAALFALQNPLEYSSAFIELKVGQKIKRNELLTWLVRSGYTRNDIENQLGSFSAKGDVVKIVPGWVNNIMFRISLFDDEIESIHTLNTITNSILDNITTVTIHPAQSYITPQDKLKTICNNIRNELVQRLAELQSENKLLEAQRLEQRTKYDLESLEEFGFCSGIENYSSHLDFRSKGQRPYVLLDYFNNDFITIVDESHITLPQIRGMYNTDRSRKLTLVEYGFRLPSALDNRPLNFDEFNSLIKQVIYTSATPGDYELDLVNHQVVQQIIRPTGLLDPQIEIRKTTNQIDDIINEIHLRKLQNERVFITTLTIRMSEDLTAFLQEKNIKVAYLHSELKTLERSEILNDLRKGVYDVVVGVNLLREGLDLPEVSLVCILDADKQGFLRNYRSLIQTIGRVARNVNGKAIMYADTVSQAMDEAIKETNRRRKIQEEFNKKHNIVPKTISKAISESILSEQTKKTLAKAKKIKDKKQKLQTIQQTIDNLRQEMLQAAKELDFERAAILRDTIIELENEKNTN | Function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Sequence Mass (Da): 77354
Sequence Length: 671
Domain: The beta-hairpin motif is involved in DNA binding.
Subcellular Location: Cytoplasm
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P58174 | MFKLHSNYSPSGDQPRAIQELAEDIEKNKKHLVLQGVTGSGKTFTIANLIAKFNRTTLVLSHNKTLASQLYSELKEFFPENRVEYFVSYFDFYRPEAYLPSTDTYIDKTSKTNNELDAMRMSSLNALLTRKDTIVVSSVAAIYGAFNPQEYQKNFFSIEVGQELKRKDFFLDLVKRHYKRNDVNLVPGSFSAKGDVVEIAPAWTSDFAIRVEFFGDEIEAIATIDPLNKTLKKRHKNYLIFPANAYSTNKDIVSRVVLQVKEELIDRLDYFEKNNKLLEMQRLEQRVKSDMDSLEEFGICSGIENYARYIDGREQGEKPYTLLDYLPEEALVFIDESHMMVPQLNAMFNGDRSRKQNLVDYGFRLPSALDNRPLTFSEFEEYKFPKIYISATPSEYEIEKADQKITKMIIRPTGLLDPIIETRSKTNQVEDIYDELQKQKAKNERTLILTTTKRFSEELTRYFQEKGEKVAYIHSDHKTFERNEILRKLRKGVYDLVIGINLLREGIDLPEVSLVIILDADKESFLRNTKSLIQIVGRASRNSSGKVIFYADFVSKSMRETIEDNFEKRQIQIQYNKEHGIVPQTIIKDIPEPIEGHGFEHSIEYFLSNEKKSKAQLKEKEKLILDLKKQMLEASQKMNYERAIHLRDLLIELGEKL | Function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Sequence Mass (Da): 76354
Sequence Length: 657
Domain: The beta-hairpin motif is involved in DNA binding.
Subcellular Location: Cytoplasm
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Q9ZD95 | MKDKIQNQNFMHTLNAEQKKAALHTEGPLLLLAGAGTGKTKVLTSRIANIIHQNLALPHNILAVTFTNKAAKEMSERVHNLINCYGLNIGTFHSMAAKILRDQIENLNLGFNNRFTIISHDDQLTLVKDIVKLKKDIDAKKYTPKLIHIIISRWKDQGLLPNKLSTSDTNLPLQKIAKLVYEEYQKNLLISNVLDFGDLLLYNNELFIKNPAVLKYYQEKYRYILIDEYQDTNIAQYLWARMLASLYRNICCVGDDDQSIYGWRGAEVGNILRFEKDFAGATIIKLEQNYRSTLPILAAASNVINNNKNRHSKTLWTDSSSGEKIKIISCLSDKEEARYIACEIDKLVKEERYNAGNIAILVRAGFQTRSFEEAFINSAIPYKIIGGLRFYERMEIRDVLAYIRISLNQNDNLALERIINVPKRAIGAASLNKIRSYALERNISNFAAIKEILEIGNIKAKSYESLKDLLTKIDNWYEQFIIDTPINVVKAILDDSGYLAMLKEEKTEEAFGRIENINEMLRAIAEFNDIHDFIEYSSLVMENEVLETNYGGSVTIMTLHAAKGLEFDVVFLPGWEEGVFPSQRSLDEDGEKGLEEERRIAYVGITRAKKDLYITHAESRKIFYEIVRSCPSRFINEIPDEITIRTSSMKQYNSFYKF | Function: Has both ATPase and helicase activities. Unwinds DNA duplexes with 3' to 5' polarity with respect to the bound strand and initiates unwinding most effectively when a single-stranded region is present. Involved in the post-incision events of nucleotide excision repair and methyl-directed mismatch repair (By similarity).
Catalytic Activity: Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.
Sequence Mass (Da): 75389
Sequence Length: 658
EC: 5.6.2.4
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P0AED5 | MINVLLVDDHELVRAGIRRILEDIKGIKVVGEASCGEDAVKWCRTNAVDVVLMDMSMPGIGGLEATRKIARSTADVKIIMLTVHTENPLPAKVMQAGAAGYLSKGAAPQEVVSAIRSVYSGQRYIASDIAQQMALSQIEPEKTESPFASLSERELQIMLMITKGQKVNEISEQLNLSPKTVNSYRYRMFSKLNIHGDVELTHLAIRHGLCNAETLSSQ | Function: Member of the two-component regulatory system UvrY/BarA involved in the regulation of carbon metabolism via the CsrA/CsrB regulatory system . UvrY activates the transcription of the untranslated csrB RNA and of barA, in an autoregulatory loop. Mediates the effects of CsrA on csrB RNA by BarA-dependent and BarA-independent mechanisms .
PTM: Phosphorylated and activated by BarA.
Sequence Mass (Da): 23893
Sequence Length: 218
Subcellular Location: Cytoplasm
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Q4L320 | MAFINEHFMLNNETGKHLYHDFAKDMPIYDYHCHLDPKQISDNVACDNITDLWLSGDHYKWRAMRAQGIEEQYITGDAAPLDKFKKWTETLENSVGNPLYHWSQLELKMYFDIEDLLTSDNAEAIYHRANDYLKQHHTTTQSLITDSNVNLICTTDNPTDDLNYHDAIKAKDGFNTTVLPAFRPDDVFKVGDPAFTDLLQKLENLTHPITTPSDFIEALYKRIQYFHDKGGRLADHGLEEMHFEAYTDQAIQDIFKKALNHADISTYERFQFQSYMLNELSKAYYERGWVMQIHFGAIRNNNTKMFEKVGKDAGFDSIRDQDNLAYHLNATLDMMEQEGHLPKTILYNLNPIYNDIVGSTIANFQTEPGIKSKVQHGAGWWFNDTKRGMLRQMSSLADQGLLMHFVGMLTDSRSFISYSRHDYFRRILSSFIGDLVEKGEIPNDDQLLKRMIENICYNNAYNYFKLI | Catalytic Activity: D-glucuronate = D-fructuronate
Sequence Mass (Da): 54328
Sequence Length: 467
Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
EC: 5.3.1.12
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B9DSL9 | MTFNDKNFMLKNQAAKQLYTAVQDQPIFDYHCHLDPKEIFEDKVFENIVDLWLGGDHYKWRLMRANGISEEEITGSASQLDKFKAFARTLQRSYGNPVYHWSAMELKNVFGIEEVLTEENAEEIYNRLNTYLLENKVSPRKLIADSKVTFIGTTDHPLDTLEWHQKLAEDKSFETIVAPTFRPDEAFIEHHNFKGFLDKLSQATGKEMTEFKDFISAMEDRIAYFAENGCKASDISFTEIVFEAAEESELNELLAKVKDGYKPNALEVKQWQTAVFAELCQLYKKYGFVTQVHFGALRNNHSKLYQKLGADVGIDSLGDQTALTSNMNKLLDNLVQKDALPKMIWYNLNPSYNIAVANTLANFQANEEGVKSYLQFGAGWWFADTKLGMISQMNALAEQGMLANFVGMLTDSRSFLSYQRHDYFRRILCTYLGEWIEEGEVPEDYEALGHMAKDIAYHNAVNYFKHE | Catalytic Activity: D-glucuronate = D-fructuronate
Sequence Mass (Da): 53730
Sequence Length: 467
Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
EC: 5.3.1.12
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P10379 | MTSNSCLISLGLLLVLIQILAPAKAAEHSVFTHKNASSVLGQLVTSSTLVWESYDPKDATQLQFAVEGGKYVTEDEHYPMYVCRVPIDGIQVSGHTEKILQRHVCLAAHYKHGKYDNFDVLMNKGHLGKVGWRHWRKFDAGVPVGAIRIGDDSYIGRHRAPSQPNKDGVVTHWGADFNLGHLEPVGLGKIRVIEAEREKYYDDGEVLVETEPFRYELRDIKLDRLRTDIQENMTELVTRKLENLEDKYSTVETILSYTFNYNQYWGSHEGVARGLPTKIFEKDEAVPAEINWALKHTEKRSENKAVHTKLWPGTAINVTLRGNYVTLEAPYSGKLFAFYYGSDESVSRKISAEVRKSYLKEVKLEFSPVYWIENGTLVPTTTTTTTTSTSTTTHATTTSTNEPTPINEPPLVHMKDNGVQHSGPDTLEKTLHDSPSSNELNSHEAPENMSSDPGKDVALAGFGVNAAGSTFIAGSALLTLLLTIFLSL | Function: Required for normal axon patterning during neurogenesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 54308
Sequence Length: 488
Subcellular Location: Membrane
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Q9LHA4 | MYGFEALTFNIHGGYLEAIVRGHRAGLLTTADYNNLCQCENLDDIKMHLSATKYGPYLQNEPSPLHTTTIVEKCTLKLVDDYKHMLCQATEPMSTFLEYIRYGHMIDNVVLIVTGTLHERDVQELIEKCHPLGMFDSIATLAVAQNMRELYRLVLVDTPLAPYFSECLTSEDLDDMNIEIMRNTLYKAYLEDFYNFCQKLGGATAEIMSDLLAFEADRRAVNITINSIGTELTREDRKKLYSNFGLLYPYGHEELAICEDIDQVRGVMEKYPPYQAIFSKMSYGESQMLDKAFYEEEVRRLCLAFEQQFHYAVFFAYMRLREQEIRNLMWISECVAQNQKSRIHDSVVYMF | Function: Subunit of the integral membrane V0 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40788
Sequence Length: 351
Subcellular Location: Vacuole membrane
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P53659 | MEGLLFNVNNGYIEGIVRGYRNSLLTSTNYTNMTQCESIDDLKLQLGPAYGDFLASLPPKPSTSALAAKTTDKLVSEFRYVRANAAGSLAKFMDYLTYGYMIDNVALLITGTLHERDTRELLERCHPLGWFETMPVLCVATNIEELYNSVMIETPLAPYFKSSLSLQDLDELNIEIVRNTLYKNYLEDFYHFVNTHPDMAGTPTAEVMSELLEFEADRRAINITLNSFGTELSKADRKKLYPNFGQLYPEGTLMLSRADDFEGVRLAVEGVADYKSFFDAAGLGGGPSGPGNMGGGGTEGKSLEDMFYQKEMEISKMAFTRQFTYAIVYAWVKLREQEIRNITWIAECIAQNQKERINNYISVF | Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity). This subunit is a non-integral membrane component of the membrane pore domain and is required for proper assembly of the V0 sector (By similarity). Might be involved in the regulated assembly of V1 subunits onto the membrane sector or alternatively may prevent the passage of protons through V0 pores (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 41008
Sequence Length: 364
Subcellular Location: Vacuole membrane
|
O13753 | MDALSFNTNSGYIEALVRGYESALLEQHIYSNLSQCESLEDFRLQLSSTDYGGFLANQSKLTSSIISAKATEKLLDEFDLIRRQADETLSKFMDYITYAYMIDNIMLLLTGTVNGQDTHDLLERCHPLGWFETLPALCVATNVEELYSVVLIETPLAPYFKDCLSADDLDEQHIEIIRNTLYKAYLEDFYNFCKKIGACTADTMLPILEFEADRRAITITINSFGTELSKEERAKMYPSFGRLYPFSTSILARAENAGDVENACSLVKEYSDFFDQNSQKSLDDHFNEKEVELNKLAFLQQFHYGIVYAFLKLREQEIRNLTWIAECISQNQRDRALNIVPIL | Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity). This subunit is a non-integral membrane component of the membrane pore domain and is required for proper assembly of the V0 sector (By similarity). Might be involved in the regulated assembly of V1 subunits onto the membrane sector or alternatively may prevent the passage of protons through V0 pores (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39323
Sequence Length: 343
Subcellular Location: Vacuole membrane
|
P32366 | MEGVYFNIDNGFIEGVVRGYRNGLLSNNQYINLTQCDTLEDLKLQLSSTDYGNFLSSVSSESLTTSLIQEYASSKLYHEFNYIRDQSSGSTRKFMDYITYGYMIDNVALMITGTIHDRDKGEILQRCHPLGWFDTLPTLSVATDLESLYETVLVDTPLAPYFKNCFDTAEELDDMNIEIIRNKLYKAYLEDFYNFVTEEIPEPAKECMQTLLGFEADRRSINIALNSLQSSDIDPDLKSDLLPNIGKLYPLATFHLAQAQDFEGVRAALANVYEYRGFLETGNLEDHFYQLEMELCRDAFTQQFAISTVWAWMKSKEQEVRNITWIAECIAQNQRERINNYISVY | Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons . V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments . This subunit is a non-integral membrane component of the membrane pore domain and is required for proper assembly of the V0 sector . Might be involved in the regulated assembly of V1 subunits onto the membrane sector or alternatively may prevent the passage of protons through V0 pores .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39791
Sequence Length: 345
Subcellular Location: Vacuole membrane
|
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