ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
E9L011 | MAIEKPVIVACACPLAGHVGPVLSLVRGLLNRGYEVTFVTGNAFKEKVIEAGCTFVPLQGRADYHEYNLPEIAPGLLTIPPGLEQTGYSMNEIFVKAIPEQYDALQTALKQVEAENKSAVVIGETMFLGVHPISLGAPGLKPQGVITLGTIPCMLKAEKAPGVPSLEPMIDTLVRQQVFQPGTDSEKEIMKTLGATKEPEFLLENIYSSPDRFLQLCPPSLEFHLTSPPPGFSFAGSAPHVKSAGLATPPHLPSWWPDVLSAKRLIVVTQGTAAINYEDLLIPALQAFADEEDTLVVGILGVKGASLPDSVKVPANARIV... | 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-sop... |
G3FIN9 | MGSLASEIPPHAVLVPYPAQGHVNPLMQLGKLLHSRGFYITFVNTEHNHRRLIRSRGQEFIDGLPDFKFEAIPDGLPYTDRDATQHVPSLSDSTRKHCLAPFIDLIAKLKASPDVPPITCIISDGVMAFAIDAARHFGIPEIQFWTTSACGFMAYLHHIELVRRGIVPFKDESFLHDGTLDQPVDFIPGMPNMKLRDMPSFIRVTDVNDIMFDFMGSEAHKSLKADAIILNTYDELEQEVLDAIAARYSKNIYTVGPFILLEKGIPEIKSKAFRSSLWKEDLSCIEWLDKREPDSVVYVNYGCVTTITNEQLNEFAWGLA... | 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, i... |
Q6UDH7 | MATRGRPGAKQVADHSVSDGGEQRRIPQKPPGPERCDVCSAVSAAGAAADLIDVAPLEEDLTKEPQQIVVTIMSNDPAKVCLKVDPALHYRNVELEPYRFLGRGGYGSVFYSRRANVAVKALTHGASFRWELAVSLIVSSAARRQELSDIAKHFLQIYAFSSVEKIIVMEYIRHDLRTYLDEHCKPVTQSALDALVREFRGLAKALAFFHIECGLAHLDVKQNNILVNCDPRTGDPVRMVLADFSLAAINGNSFLNKCCMVCPGRPGVTGVHIIDTEDAVNSLPSNNILLFRMSRRPPEFLLDYCNGVGPRCGEVMGAMT... | 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... |
P30662 | MAAGGGGGGVSRAALARPPIHRGTSAPGGAIAAAGGDGDGDEASRLLGRAQPREAPYLIPRPDGDLAVPDDLQYATLDLTGDPVAVGAGSYGSVLVYGSVAVKTLRAGFGHEAVMTLLAAEEARSAGVRGVVRLMGLSAPLRQLMFPAYEMDMDAYRRSLTARPGHVVHALGRVFTELGRALVFLNGRGLSHLDVKGGNIFVRTCGNMVVTAVIGDFSLMALNSRSALADPRFRLARRKALKITSLARSPPTGVLLGHARDRPTRVLMDFINGRPPPPGPLPYEVGLAIDLCALGHVLLDVALGLRPQRGQALTREYAVE... | 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 phos... |
P09296 | MDADDTPPNLQISPTAGPLRSHHNTDGHEPNATAADQQERESTNPTHGCVNHPWANPSTATCMESPERSQQTSLFLLKHGLTRDPIHQRERVDVFPQFNKPPWVFRISKLSRLIVPIFTLNEQLCFSKLQIRDRPRFAGRGTYGRVHIYPSSKIAVKTMDSRVFNRELINAILASEGSIRAGERLGISSIVCLLGFSLQTKQLLFPAYDMDMDEYIVRLSRRLTIPDHIDRKIAHVFLDLAQALTFLNRTCGLTHLDVKCGNIFLNVDNFASLEITTAVIGDYSLVTLNTYSLCTRAIFEVGNPSHPEHVLRVPRDASQM... | 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 ... |
Q6RJQ3 | MCRRESLRTLPWLFWVLLSCPRLLEYSSSSFPFATADIAEKMWAENYETTSPAPVLVAEGEQVTIPCTVMTHSWPMVSIRARFCRSHDGSDELILDAVKGHRLMNGLQYRLPYATWNFSQLHLGQIFSLTFNVSTDTAGMYECVLRNYSHGLIMQRFVILTQLETLSRPDEPCCTPALGRYSLGDQIWSPTPWRLRNHDCGMYRGFQRNYFYIGRADAEDCWKPACPDEEPDRCWTVIQRYRLPGDCYRSQPHPPKFLPVTPAPPADIDTGMSPWATRGIAAFLGFWSIFTVCFLCYLCYLQCCGRWCPTPGRGRRGGEG... | 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 de... |
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 express... |
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 dec... |
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 ... |
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 d... |
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 | MAAADALLGSLVTGLYDVQAFKFGNFVLKSGLSSPVYIDLRGIISRPSILNQVAEMLFQTAENAEINFDTVCGVPYTALPLATIVCSTHEIPMLIRRKEKKDYGTKRLIEGAVNPGDTCLIIEDVVSSGSSVWETAEVLQKEGLKVTDAVVLVDREQGGRDNLQARGIRLHSVCTLSTVLCILEQQKKINAETVERVKRFIQENAFVAANPNDSLPSVKKEPKELSFGARAELPGTHPVAAKLLRLMQKKETNLCLSADVSESRELLQLADALGSRICLLKIHVDILNDFTLDVMKELTTLAKRHEFLIFEDRKFADIGN... | 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 mon... |
G5EDZ2 | MSSLTDKTRNGALKRNLLRQMLKASVFKFGEFQLKSGQISPIYIDLRECFGHPGLLMLISEAISKQVEISEVQYAGVLGIPYAALPYASVAAGNYLKKPLLIVRKEAKSYGTKKLIEGLYQPNDRLILIEDVVTTGGSILDVVKVLHTENLVASDVFCILDREQGGRQKLQDAGVTLHSLLDMQTVLTFLYSTGAIGDEQWHGIVQALNLPYTSPTKLEINSELENLSSLPYVENVRTPLAERESLTESALIKKILGIMRRKKSNLCLAVDYTTVEQCLQMIELAGPFVLAIKLHADAITDFNEEFTRKLTTMANDMDFI... | 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 .
Catalyt... |
P09556 | MNIKELVLKLNEIDAIKLGEFKLKSGIISPIYIDLRVTVSSPPLLAAIAEMMYQKVYKSGNAQETPALVCGVPYTALPIATGMSIANNIPMVVRRKEAKAYGTKQLIEGRFKEGDNVLVVEDLVTSGASVLETVRDLNSVGLKVTDVVVLLDRQQGARQALEKQGYRLHSVFTMEELINTLIEAGKLTGRTLELVQSFLDANRNVVVPLPPTLAPPAPAPIVINKPFEERAKLASNPMASKLFTLMSSKKTNLAVAADLTDKQQLLDLAESIGSEICVLKTHVDIIDNYDEEFIKSLKCIAAKHNFLIFEDRKFADIGNT... | 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... |
P11172 | MAVARAALGPLVTGLYDVQAFKFGDFVLKSGLSSPIYIDLRGIVSRPRLLSQVADILFQTAQNAGISFDTVCGVPYTALPLATVICSTNQIPMLIRRKETKDYGTKRLVEGTINPGETCLIIEDVVTSGSSVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAHGIRLHSVCTLSKMLEILEQQKKVDAETVGRVKRFIQENVFVAANHNGSPLSIKEAPKELSFGARAELPRIHPVASKLLRLMQKKETNLCLSADVSLARELLQLADALGPSICMLKTHVDILNDFTLDVMKELITLAKCHEFLIFEDRKFADIGN... | 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 mon... |
Q25566 | METTTIDIQALKKELVLDLIQIGALKFGRFTLKSGIVSPFYVDLRIIGPKMLRQFSVLLYHVMTVKGLTNMEKRVICGVPYSALTFSSCMSMTYDLPMVICRKERKQYGTGNMVEGIYTKNETNCILIEDVITSGASIVETAEKLENEGLLVTDALVFLTREQLPLTNGMHILKKGEKVYNVHPCLTMTEVTQVLLDEGKMSQEQREDILQFIGTNTFSETKTTAVPQKKKELTFTERAELTNNEFSKKLFKLMEEKQTNLCVAADITSKDDLLKLADETGPEICMLKTHIDTLDDQPDEQFTQQLKELAKKHNFLIFED... | 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 mon... |
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
... |
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
... |
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.
Catal... |
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.
Catal... |
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
... |
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
... |
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
... |
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
... |
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
Seque... |
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
Seque... |
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
Seque... |
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
Seque... |
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
Seque... |
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
Seque... |
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
Seque... |
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
Seque... |
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
Seque... |
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
Seque... |
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
Seque... |
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
Seque... |
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 Locati... |
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
Seque... |
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
Seque... |
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
Seque... |
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
Seque... |
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 ... |
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 ... |
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 polypren... |
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 ... |
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 ... |
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... |
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... |
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... |
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 L... |
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 L... |
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 L... |
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 L... |
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-... |
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-... |
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-... |
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-... |
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-... |
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... |
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... |
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... |
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). M... |
P18314 | MSNISRQAYADMFGPTVGDKVRLADTELWIEVEDDLTTYGEEVKFGGGKVIRDGMGQGQMLAADCVDLVLTNALIVDHWGIVKADIGVKDGRIFAIGKAGNPDIQPNVTIPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMVGGGTGPAAGTHATTCTPGPWYISRMLQAADSLPVNIGLLGKGNVSQPDALREQVAAGVIGLKIHEDWGATPAAIDCALTVADEMDIQVALHSDTLNESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTLNTIDEHLDMLMVCH... | 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.
... |
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 ur... |
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 | MLLRPRRPPPLAPPAPPSPASPDPEPRTPGDAPGTPPRRPASPSALGELGLPVSPGSAQRTPWSARETELLLGTLLQPAVWRALLLDRRQALPTYRRVSAALAQQQVRRTPAQCRRRYKFLKDKFREAHGQPPGPFDEQIRKLMGLLGDNGRKRPRRRSPGSGRPQRARRPVPNAHAPAPSEPDATPLPTARDRDADPTWTLRFSPSPPKSADASPAPGSPPAPAPTALATCIPEDRAPVRGPGSPPPPPAREDPDSPPGRPEDCAPPPAAPPSLNTALLQTLGHLGDIANILGPLRDQLLTLNQHVEQLRGAFDQTVSL... | 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... |
Q6J1H4 | MLLRPRRLPAFSPPSPASPDAELRSAGDVPVTTSDAFATSGGMAEPGSPKAPVSPDSAQRTPWSARETELLLGTLLQPAMWRSLLLDRRQTLPTYRRVSAALARQQVRRTPAQCRRRYKFLKDKLRDSQGQPSGPFDNQIRQLMGLLGDDGPPRVRRRSTGPGRPQRRGRSSLSALAPAPAPVEQEAELPLAAENDEPAPALRFSSSTTKSAGAHRITSSPPLTSTDTLPPEPGHTFESSPTPTPDHDVETPNEPPGLSQGRASSPQVAPQSLNTALLQTLTHLGDISTVLGPLRDQLSTLNQHVEHLRGSFDQTVSLAV... | 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 L... |
P36135 | MKLSALLALSASTAVLAAPAVHHSDNHHHNDKRAVVTVTQYVNADGAVVIPAATTATSAAADGKVESVAAATTTLSSTAAAATTSAAASSSSSSSSSSSSSSSVGSGDFEDGTISCSDFPSGQGAVSLDWLGLGGWASIMDMNGNTATSCQDGYYCSYACSPGYAKTQWPSEQPSDGRSVGGLYCKNGKLYRSNTDTNSLCVEGQGSAQAVNKVSGSIAICGTDYPGSENMVVPTVVGAGSSQPINVIKEDSYYQWQGKKTSAQYYVNNAGVSVEDGCIWGTEGSGVGNWAPVVLGAGYTDGITYLSIIPNPNNKEAPNF... | 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 r... |
Q45978 | MASPARAPVLALKDVRLADGAKPLFDGVDLALEPRVRACLVGRNGAGKSTLLKILAGQGVEADSGERAVQPGAKVVYVSQEPEITGETLLDYATAGGAQDYEAQAALADFGLDPDKSAKGLSGGETRRAALARAFAEQPDVLLLDEPTNHLDIFAIQTLEDELAASKCAALIVSHDRAFLNRVTERCFWLEHRKIRRLDKGFSEFEAWAESIMAADAEEARRLDKVLERENAWLARGVQGRRARNEGRRRALLALRAEKKDRQSELRGTMTMAVESAGTSGKRVVEAKGVTKRFGERTIVENFSTRILRGDRVALVGPNG... | 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: ... |
P43672 | MSLISMHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNREQGLDDGRIIYEQDLIVARLQQDPPRNVEGSVYDFVAEGIEEQAEYLKRYHDISRLVMNDPSEKNLNELAKVQEQLDHHNLWQLENRINEVLAQLGLDPNVALSSLSGGWLRKAALGRALVSNPRVLLLDEPTNHLDIETIDWLEGFLKTFNGTIIFISHDRSFIRNMATRIVDLDRGKLVTYPGNYDQYLLEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKAMRRERGERREVMGTAKMQVEEASRSGKIVF... | 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 invol... |
Q5UNU2 | MNQNLIRLGYACLNSDLRNYDIFTSRKPILKTVKSQGFDYVKETIIRNLRDLFTIIIYNESHGIRFFRISSSIFPHLGNPLLPDSDYDLSFAKNLIKEIGSYAKINGHRLTMHPGQFVQLGSNNEEVVRRSFVELQNHATLLEMLGYSSLDSSVLIVHGGGTFGDKETTLERWKSNFRKLPENIRQLICLENDENSYGILDLLPVCEELNVPFCLDIFHNRVSKNRIPLTKKLMKRIINTWKRRNMTPKMHFSNQEPGLRRGAHSKTINELPEYLFRIPDMFQTSLDIILEVKDKEKSVLKMYFKYFDIETNIDGRNNFI... | Function: Endonuclease for the repair of UV-irradiated DNA.
Sequence Mass (Da): 38547
Sequence Length: 330
Subcellular Location: Virion
EC: 3.-.-.-
|
O48652 | MQRFCVCSPSSYRLNPITSMATGSGSLIWFRKGLRVHDNPALEYASKGSEFMYPVFVIDPHYMESDPSAFSPGSSRAGVNRIRFLLESLKDLDSSLKKLGSRLLVFKGEPGEVLVRCLQEWKVKRLCFEYDTDPYYQALDVKVKDYASSTGVEVFSPVSHTLFNPAHIIEKNGGKPPLSYQSFLKVAGEPSCAKSELVMSYSSLPPIGDIGNLGISEVPSLEELGYKDDEQADWTPFRGGESEALKRLTKSISDKAWVANFEKPKGDPSAFLKPATTVMSPYLKFGCLSSRYFYQCLQNIYKDVKKHTSPPVSLLGQLLW... | 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 fo... |
Q0E2Y1 | MDAAATAATATAAAAMVWFRKGLRVHDNPALDAARRGGAAARLYPVFVLDPRYLRPDQAAPSPGSARAGVARVRFLLESLSDLDARLRRLGSRLLLLRARDDGDVAGTVCAALKDWNIGKLCFESDTEPYALARDKKVMDFAAASGIDVFSPVSHTLFDPAEIIEKNGGRPPMTYQSFVAIAGEPPEPIMEEYSELPPVGDTGEYELLPVPRVEELGYGDISQEDLSLFRGGETEALKRMRESLHDKEWVAKFEKPKGDPSAFLKPATTVLSPYLKFGCLSSRYFYHCIQDIYRSTKKHTNPPVSLTGQLLWRDFFYTVA... | 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
Sequ... |
Q9P2Y5 | MSASASVGGPVPQPPPGPAAALPPGSAARALHVELPSQQRRLRHLRNIAARNIVNRNGHQLLDTYFTLHLCSTEKIYKEFYRSEVIKNSLNPTWRSLDFGIMPDRLDTSVSCFVVKIWGGKENIYQLLIEWKVCLDGLKYLGQQIHARNQNEIIFGLNDGYYGAPFEHKGYSNAQKTILLQVDQNCVRNSYDVFSLLRLHRAQCAIKQTQVTVQKIGKEIEEKLRLTSTSNELKKKSECLQLKILVLQNELERQKKALGREVALLHKQQIALQDKGSAFSAEHLKLQLQKESLNELRKECTAKRELFLKTNAQLTIRCRQ... | 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 phosph... |
B0JR86 | MTAFQLQAPFQPTGDQPAAIDQLVDSLQNQHRFQTLLGATGTGKTFTIAAVIEKIGRPTLVLAHNKTLAAQLCNELRQFFPNNAVEYFISYYDYYQPEAYIPVSDTYIEKSSSINDEIDMLRHSATRSLFERRDVIVVASISCIYGLGMPAEYLKAAISLTVGQEFDQRQLLRALVSVQYNRNDLELTRGRFRLKGDILEIVPAYEDRVIKIDFFGDEIESIRYLDPLTGEVLQKLERISIYPARHFVTPEERLEVACRDIKTELDNRLLELEKAGKLLEAQRLDQRTRYDLEMLQEVGYCNGVENYSRHLAGRLAGEPP... | 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... |
P47319 | MKNQTKSNSLFQLSTNYIPTGDQPEAIKKLSEFKTKQQVLLGATGTGKTFTIANVIQNSQLPTVVIAHNKTLAGQLFNELKQLFPKNAVEYFISYFDFYQPEAYLPSKGIYIEKSATVNEAIKRLRVSTLHSLSTRKDVIVVGSVASIYPTSSPSDFVKYCLWFVVGKDYDLKTIKDRLVSLNYVVNKQQLTPGKFRFQGDVLEVFPGYSDAFVIRISFFDTKVEQICQIDPLTNKILNQLFEIKIGPADEYVVNQSDLDIAIKNIKQELQERVNYFNKQNLVERAQRLATITNHDLNDLKAWGFCSGVENYARHLELRM... | 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... |
P57991 | MRVGGRFEVISPHEPAGDQPAAIDELQRRILAGERDVVLLGATGTGKSATTAWLIERLQRPTLVMAPNKTLAAQLANELRGMLPHNAVEYFVSYYDYYQPEAYIAQTDTYIEKDSSINDDVERLRHSATSSLLSRRDVVVVASVSCIYGLGTPQSYLDRSVELAVSNEVPRDGLLRLLVDVQYTRNDLSFTRGSFRVRGDTVEIIPSYEELAVRIEFFGDEIEALYYLHPLTGEVIRQVDSLRIFPATHYVAGPERMAQAISAIEEELAERLAEFERQGKLLEAQRLRMRTNYDIEMMRQVGFCSGIENYSRHIDGRGPG... | 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... |
Q6MS38 | MLWEKVMFIANNKYKLVTKYKPSGDQNQAIEKLNKAIIENKKHQVLLGATGTGKTFTIANIIAKHNKQALVIAHNKTLAMQLYYELKEMFPENRVEYFVSNFDFFQPEAYIPSKDLYIDKDSRQNMELDMMRLSACNALLTRNDTIVVASVAALFALQNPLEYSSAFIELKVGQKIKRNELLTWLVRSGYTRNDIENQLGSFSAKGDVVKIVPGWVNNIMFRISLFDDEIESIHTLNTITNSILDNITTVTIHPAQSYITPQDKLKTICNNIRNELVQRLAELQSENKLLEAQRLEQRTKYDLESLEEFGFCSGIENYSS... | 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... |
P58174 | MFKLHSNYSPSGDQPRAIQELAEDIEKNKKHLVLQGVTGSGKTFTIANLIAKFNRTTLVLSHNKTLASQLYSELKEFFPENRVEYFVSYFDFYRPEAYLPSTDTYIDKTSKTNNELDAMRMSSLNALLTRKDTIVVSSVAAIYGAFNPQEYQKNFFSIEVGQELKRKDFFLDLVKRHYKRNDVNLVPGSFSAKGDVVEIAPAWTSDFAIRVEFFGDEIEAIATIDPLNKTLKKRHKNYLIFPANAYSTNKDIVSRVVLQVKEELIDRLDYFEKNNKLLEMQRLEQRVKSDMDSLEEFGICSGIENYARYIDGREQGEKPY... | 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... |
Q9ZD95 | MKDKIQNQNFMHTLNAEQKKAALHTEGPLLLLAGAGTGKTKVLTSRIANIIHQNLALPHNILAVTFTNKAAKEMSERVHNLINCYGLNIGTFHSMAAKILRDQIENLNLGFNNRFTIISHDDQLTLVKDIVKLKKDIDAKKYTPKLIHIIISRWKDQGLLPNKLSTSDTNLPLQKIAKLVYEEYQKNLLISNVLDFGDLLLYNNELFIKNPAVLKYYQEKYRYILIDEYQDTNIAQYLWARMLASLYRNICCVGDDDQSIYGWRGAEVGNILRFEKDFAGATIIKLEQNYRSTLPILAAASNVINNNKNRHSKTLWTDSS... | 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 si... |
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 Bar... |
Q4L320 | MAFINEHFMLNNETGKHLYHDFAKDMPIYDYHCHLDPKQISDNVACDNITDLWLSGDHYKWRAMRAQGIEEQYITGDAAPLDKFKKWTETLENSVGNPLYHWSQLELKMYFDIEDLLTSDNAEAIYHRANDYLKQHHTTTQSLITDSNVNLICTTDNPTDDLNYHDAIKAKDGFNTTVLPAFRPDDVFKVGDPAFTDLLQKLENLTHPITTPSDFIEALYKRIQYFHDKGGRLADHGLEEMHFEAYTDQAIQDIFKKALNHADISTYERFQFQSYMLNELSKAYYERGWVMQIHFGAIRNNNTKMFEKVGKDAGFDSIRD... | 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
|
B9DSL9 | MTFNDKNFMLKNQAAKQLYTAVQDQPIFDYHCHLDPKEIFEDKVFENIVDLWLGGDHYKWRLMRANGISEEEITGSASQLDKFKAFARTLQRSYGNPVYHWSAMELKNVFGIEEVLTEENAEEIYNRLNTYLLENKVSPRKLIADSKVTFIGTTDHPLDTLEWHQKLAEDKSFETIVAPTFRPDEAFIEHHNFKGFLDKLSQATGKEMTEFKDFISAMEDRIAYFAENGCKASDISFTEIVFEAAEESELNELLAKVKDGYKPNALEVKQWQTAVFAELCQLYKKYGFVTQVHFGALRNNHSKLYQKLGADVGIDSLGDQ... | 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
|
P10379 | MTSNSCLISLGLLLVLIQILAPAKAAEHSVFTHKNASSVLGQLVTSSTLVWESYDPKDATQLQFAVEGGKYVTEDEHYPMYVCRVPIDGIQVSGHTEKILQRHVCLAAHYKHGKYDNFDVLMNKGHLGKVGWRHWRKFDAGVPVGAIRIGDDSYIGRHRAPSQPNKDGVVTHWGADFNLGHLEPVGLGKIRVIEAEREKYYDDGEVLVETEPFRYELRDIKLDRLRTDIQENMTELVTRKLENLEDKYSTVETILSYTFNYNQYWGSHEGVARGLPTKIFEKDEAVPAEINWALKHTEKRSENKAVHTKLWPGTAINVTL... | 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
|
Q9LHA4 | MYGFEALTFNIHGGYLEAIVRGHRAGLLTTADYNNLCQCENLDDIKMHLSATKYGPYLQNEPSPLHTTTIVEKCTLKLVDDYKHMLCQATEPMSTFLEYIRYGHMIDNVVLIVTGTLHERDVQELIEKCHPLGMFDSIATLAVAQNMRELYRLVLVDTPLAPYFSECLTSEDLDDMNIEIMRNTLYKAYLEDFYNFCQKLGGATAEIMSDLLAFEADRRAVNITINSIGTELTREDRKKLYSNFGLLYPYGHEELAICEDIDQVRGVMEKYPPYQAIFSKMSYGESQMLDKAFYEEEVRRLCLAFEQQFHYAVFFAYMRL... | 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
S... |
P53659 | MEGLLFNVNNGYIEGIVRGYRNSLLTSTNYTNMTQCESIDDLKLQLGPAYGDFLASLPPKPSTSALAAKTTDKLVSEFRYVRANAAGSLAKFMDYLTYGYMIDNVALLITGTLHERDTRELLERCHPLGWFETMPVLCVATNIEELYNSVMIETPLAPYFKSSLSLQDLDELNIEIVRNTLYKNYLEDFYHFVNTHPDMAGTPTAEVMSELLEFEADRRAINITLNSFGTELSKADRKKLYPNFGQLYPEGTLMLSRADDFEGVRLAVEGVADYKSFFDAAGLGGGPSGPGNMGGGGTEGKSLEDMFYQKEMEISKMAFT... | 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 compartmen... |
O13753 | MDALSFNTNSGYIEALVRGYESALLEQHIYSNLSQCESLEDFRLQLSSTDYGGFLANQSKLTSSIISAKATEKLLDEFDLIRRQADETLSKFMDYITYAYMIDNIMLLLTGTVNGQDTHDLLERCHPLGWFETLPALCVATNVEELYSVVLIETPLAPYFKDCLSADDLDEQHIEIIRNTLYKAYLEDFYNFCKKIGACTADTMLPILEFEADRRAITITINSFGTELSKEERAKMYPSFGRLYPFSTSILARAENAGDVENACSLVKEYSDFFDQNSQKSLDDHFNEKEVELNKLAFLQQFHYGIVYAFLKLREQEIRN... | 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 compartmen... |
P32366 | MEGVYFNIDNGFIEGVVRGYRNGLLSNNQYINLTQCDTLEDLKLQLSSTDYGNFLSSVSSESLTTSLIQEYASSKLYHEFNYIRDQSSGSTRKFMDYITYGYMIDNVALMITGTIHDRDKGEILQRCHPLGWFDTLPTLSVATDLESLYETVLVDTPLAPYFKNCFDTAEELDDMNIEIIRNKLYKAYLEDFYNFVTEEIPEPAKECMQTLLGFEADRRSINIALNSLQSSDIDPDLKSDLLPNIGKLYPLATFHLAQAQDFEGVRAALANVYEYRGFLETGNLEDHFYQLEMELCRDAFTQQFAISTVWAWMKSKEQEV... | 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 subun... |
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