ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P9WEX4 | MSQPAFKIIIVGCSVTGLTLAHCLDKLGVEYTILEKRSAVVLQEGASVAVMPNGGRILDQLGLYDAFEKATVPLDLTDAYLPDQDFRFTSDYPRRVLATFGYPVAFMERRGLLEILYDGIADKSKIHLNKGVTHVEQNDDGAKVHTEDGEVYEGDIVVGADGIHSKTLREMWRMMGEPVVNGIAQSESQNMSVAFSCVFGISHDVPELQPGEQILRMCNGSTIFVMGSKGVVFWFIVTQLNRRYEYHDAPRYTTEEAAAFCEARKDAEIKEGVTFECIWRKQHVFNMLPLQESLFQTWSHGRVVCIGDSVHKMTINLGQG... | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the diterpenoid pyrones subglutinols A and B . The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpasA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA u... |
P9WEX5 | MNRLLASALLVGSAVVAPVSAACIKNATVTEVDVAIIGGGASGVYAAARLIDNNKTVVVLERNADRIGGQTETYYDPTTGTPVNVGVKVFSNTTVTTDFLKRFDFPMGTLNVGQTLATGTQYVDFATGKLIPNFTAVVPAVQAAAMQRYAAELAKYPQIKFGYNLGPQVPEDLVLPFGKFMEKHNLTGMAQTMFEFNSGYTPLLEIPALYILKYLDTYELQSLQSGSFIVAANGDSATLYRNAAKFLGERVVYGVSGMHIQRSSAAGGRVTISVGNSTTGTHMIRAKKLIVAAPPTLDNLRSTGLDLDTTEAGLFGKLSA... | Function: FAD-dependent oxidoreductase; part of the gene cluster that mediates the biosynthesis of the diterpenoid pyrones subglutinols A and B . The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpasA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA ... |
Q9FNY3 | MSMEMELFVTPEKQRQHPSVSVEKTPVRRKLIVDDDSEIGSEKKGQSRTSGGGLRQFSVMVCQKLEAKKITTYKEVADEIISDFATIKQNAEKPLNENEYNEKNIRRRVYDALNVFMALDIIARDKKEIRWKGLPITCKKDVEEVKMDRNKVMSSVQKKAAFLKELREKVSSLESLMSRNQEMVVKTQGPAEGFTLPFILLETNPHAVVEIEISEDMQLVHLDFNSTPFSVHDDAYILKLMQEQKQEQNRVSSSSSTHHQSQHSSAHSSSSSCIASGTSGPVCWNSGSIDTR | Function: Involved in the regulation of the G1/S transition. Increases the DNA binding and the transactivation activities of E2F proteins after heterodimerization. The complex DPA/E2FA promotes cell division and acts as a regulator of the endocycle. Positively regulates the activity of S phase-specific genes.
Sequence ... |
P04440 | MMVLQVSAAPRTVALTALLMVLLTSVVQGRATPENYLFQGRQECYAFNGTQRFLERYIYNREEFARFDSDVGEFRAVTELGRPAAEYWNSQKDILEEKRAVPDRMCRHNYELGGPMTLQRRVQPRVNVSPSKKGPLQHHNLLVCHVTDFYPGSIQVRWFLNGQEETAGVVSTNLIRNGDWTFQILVMLEMTPQQGDVYTCQVEHTSLDSPVTVEWKAQSDSARSKTLTGAGGFVLGLIICGVGIFMHRRSKKVQRGSA | Function: Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mos... |
P24482 | MFGSGNVLPVKIQPPLLRPLAYRVLSRKYGLSIKSDGLSALAEFVGTNIGANWRQGPATIKFLEQFAAVWKQQERGLFIDQSGVKEVIQEMKEREKVEWSHEHPIQHEENILGRTDDDENNSDDEMPIAADSSLQNVSLSSPMRQPTERDEYKQPFKPESSKALDWRDYFKVINASQQQRFSYNPHKMQFIFVPNKKQNGLGGIAGFLPDIEDKVQMFLTRYYLTNDRVMRNENFQNSDMFNPLSSMVSLQNELSNTNRQQQSSSMSITPIKNLLGRDAQNFLLLGLLNKNFKGNWSLEDPSGSVEIDISQTIPTQGHYY... | Function: As accessory component of the DNA polymerase epsilon complex participates in chromosomal DNA replication. It is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofrea... |
Q9USQ7 | MKVLGLISGGKDSCFNLMHCVSLGHEVVALANLHPEDGKDEIDSFMYQSVGHDVIPLYAECFDLPLYREKIGGQSINQNLDYQFTEKDETEDLYRLIKRVLTNHPDLEAVSTGAILSTYQRTRVENVCKRLGLKSLSFLWQKDQEKLLNDMVVSGLNAILIKVAAIGLTRKDLGKSLAEMQDKLLTLNKKFELHPCGEGGEYETLVLDCPLFKKRIVLTDKEVVEHSSGEVCYLKVKACVKDKPEWQPISLKSELVPNEELLGEEYSHIYHTISKKYELIDDQEETPTSLIPIPLRESAFQQKKGSFLVLGNVVATKGSY... | Function: Amidase that catalyzes the last step of diphthamide biosynthesis using ammonium and ATP. Diphthamide biosynthesis consists in the conversion of an L-histidine residue in the translation elongation factor eEF-2 (eft201 or eft202) to diphthamide (By similarity). Has a role in meiosis.
Catalytic Activity: ATP + ... |
Q12429 | MKFIALISGGKDSFYNIFHCLKNNHELIALGNIYPKESEEQELDSFMFQTVGHDLIDYYSKCIGVPLFRRSILRNTSNNVELNYTATQDDEIEELFELLRTVKDKIPDLEAVSVGAILSSYQRTRVENVCSRLGLVVLSYLWQRDQAELMGEMCLMSKDVNNVENDTNSGNKFDARIIKVAAIGLNEKHLGMSLPMMQPVLQKLNQLYQVHICGEGGEFETMVLDAPFFQHGYLELIDIVKCSDGEVHNARLKVKFQPRNLSKSFLLNQLDQLPVPSIFGNNWQDLTQNLPKQQAKTGEQRFENHMSNALPQTTINKTND... | Function: Amidase that catalyzes the last step of diphthamide biosynthesis using ammonium and ATP. Diphthamide biosynthesis consists in the conversion of an L-histidine residue in the translation elongation factor eEF-2 (EFT1 or EFT2) to diphthamide.
Catalytic Activity: ATP + diphthine-[translation elongation factor 2]... |
Q55C80 | MTEIIKNTKYLDYTSDSVEFYPFNNNIFVCGTYEIEKGDTEYKERRKGKLYLFEIEEEQQQKENDNNNENNNNNKLFKEIQNINFNSGILDMKWNNNKDRILGVVMSKGELNIYQYDEVEKKLELKSSTEISLSNDILSLSLDWNKSGDKLICSFSDGNIGLFKVTKDYSKVTEEKRWKAHDYEAWICAFNYHDESIVFSGGDDCKFKIWDLNQLLNHNDDDIGIPPTPKFTKRCDMGVTSIHCHPTIENLIAVGSYDECLRIWDLKSLKQPIITTDSLGGGIWRIKWHPFQKNKLVTACMGGGFHILSTDPENINDFST... | Function: Catalyzes the demethylation of diphthine methyl ester to form diphthine, an intermediate diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (efbA).
Catalytic Activity: diphthine methyl ester-[translation elongation factor 2] + H2O = diphthi... |
Q9BTV6 | MMGCFALQTVDTELTADSVEWCPLQGCRHLLACGTYQLRRPEDRPAGPQNKGGMEVKEPQVRLGRLFLYSFNDNNSIHPLVEVQRKDTSAILDMKWCHIPVAGHALLGLADASGSIQLLRLVESEKSHVLEPLSSLALEEQCLALSLDWSTGKTGRAGDQPLKIISSDSTGQLHLLMVNETRPRLQKVASWQAHQFEAWIAAFNYWHPEIVYSGGDDGLLRGWDTRVPGKFLFTSKRHTMGVCSIQSSPHREHILATGSYDEHILLWDTRNMKQPLADTPVQGGVWRIKWHPFHHHLLLAACMHSGFKILNCQKAMEERQ... | Function: Catalyzes the demethylation of diphthine methyl ester to form diphthine, an intermediate diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) which can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A (Eta).
Catalyt... |
O74865 | MSETGIIPKSTDYTDWPADVCKYSQVFEDVLVVGTYMLDESTKLRHGKLVLYDTKEDVLKRVFDMHCDAILDFKWSPHDASVLAVAHSTGHVSFYRHQFRAELMFLRGIKVADSSVLMLSLDFSDSGKELAVSMSNGSVLIIDIDSGVIKNKWKEHDYEAWTCHYSRQDNNLLYSGGDDAALVCYDQRIPNSCIWRDIQVHHSGVVSILSRAPFGPYIATGEYGDFMHTLDTRNIGKPLFSANLGGGVWRLEHMETTENYHKVLGILMHRGAQVLRISNDFSSIDASKRIFKEHESMCYGGDWRHTDGLLATCSFYDKRV... | Function: Catalyzes the demethylation of diphthine methyl ester to form diphthine, an intermediate in diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (eft201 and eft202).
Catalytic Activity: diphthine methyl ester-[translation elongation factor 2]... |
P38332 | MDSIQESDVLNAVKTKLPPCCLRIFRNKIILVGTYDLDKSTGYRSGSLDVFTMDLKLLCSNNTYGAILDLKLSPFDDTLICTAHSTGNIMLWRIRCTDKDDFQSNELDIHAIANLQLFEKDVLIASCHFSPLDCKKLLVTNTAGEAATIDIRTLSVQFTASAIAQAYSKLDKIDYEVQGATEKVIHVESGQFLKPHELECWTAEFGSLQPFQDVVFTGGDDSRIMAHDLRSKEFIWSNNRIHDAGVVSIKCSQPNFRNNKPTSIITGSYDDNIRSLDLRMMGESIFPGANVPTVNKLACDLGGGVWRFVESPIDQEQSHH... | Function: Catalyzes the demethylation of diphthine methyl ester to form diphthine, an intermediate in diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EFT1 and EFT2). Also plays a role in the regulation of the retromer complex and is required for ... |
Q9YDI2 | MARGREAVTLLLVGWGYAPGMQTLEALDAVRRADVVYVESYTMPGSSWLYKSVVEAAGEARVVEASRRDLEERSREIVSRALDAVVAVVTAGDPMVATTHSSLAAEALEAGVAVRYIPGVSGVQAARGATMLSFYRFGGTVTLPGPWRGVTPISVARRIYLNLCAGLHTTALLDVDERGVQLSPGQGVSLLLEADREYAREAGAPALLARLPSVLVEAGAGGGHRVLYWSSLERLSTADVEGGVYSIVIPARLSGVEEWLLAAASGQRRPLEYDRSVYETVEENCKKGVYMEPV | Function: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphtha... |
O29866 | MLTFVGLGLWDVKDISVKGLEAVREADEVYVEYYTSKLLSSIEEMEEFFGKRVVELERSDLEENSFRLIERAKSKSVVLLVPGDPMVATTHSAIKLEAERKGVKTRIIHGASISTAVCGLTGLHNYRFGKSATVSWHRSQTPVNVIKANRSIDAHTLLFLDLHPEPMTIGHAVENLIAEDAQMKDLYAVGIARAGSGEEVVKCDRLENLKKIDFGKPLHVMVVLAKTLHFMEFECLREFADAPAELERLVA | Function: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphtha... |
Q8TR14 | MLTFIGLGLFDEYDISLKGLEAVREADLVYAEFYTSCLMGTNPEKMEKLYGKKVHLLSREDVEQQPDWLDKAKDKNVAFLTGGDTMVSTTHVDLRLRAEKLGIETHLIHGASIASAVSGLTGLQNYRFGKSASIPYPYESRRGAIIISETPYDTIKQNSELGLHTMIFLDIDKDKGYMTANHALELLLEVEKRRGEGIMERAVAVGIARAGSEKPVVKADYAESLKDFDFGNPLHILVVPGKLHFLEAEALVKLAAGPGKIMEETE | Function: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphtha... |
Q0W085 | MLTFIGLGLYDQKDISVKGLEAIREADVVYAEFYTSRLMGATLEDMQELYGKPVKVLMREDVEQHPKDTVLSDAVDKKVVFLTGGDAMVATTHVDLRLRAKKMGIETRLIHGASIQSAVCGLTGLQNYRFGKSATIAFPYKDIISETPYDTILMNKKNGLHTLLFLDIDREKGYMTVNRGIELLLKVEERRKEGAVAGALCVGIARAGSPSPCVRAGRIEELQAFDFGGPLHIMVMPADLHFLEEEALQDLAGLKLG | Function: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphtha... |
Q9ZHG4 | MIPWVISPYSFDGSVVRFEKLALLLKRKGLKSVILADRNFHAAVKFNTIMRKHGLIPVHGLWKDGRIFVARNREEFDSLVRYYNGETHEIEDIPVFQESELTPVRYLDASEKKASIFMRKIFGLDEDVQGFPEKCEDVADILNAEAYDLRVNHRFPTPPKNWNELLIKKAEPLGEEYISRLKRELEVIKRKGFTPYIYTVEKVVEIAKKMGIKVGPGRGSAVGSLVAYLCGITEVDPIKYDLLFERFLNEERQEPPDIDVDVEDRRRKDLIKELSKSFQVYQVSTFGNLTEKSLKNLINSVLPDASLEEKNEIYKTVYGL... | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diph... |
Q9PQ74 | MFINLNVHSHYSLLNSTLSIDDLIKYALDNKQPYVCLTDLNNMYGCIEFYDKAKAHNLTPIIGLEFEYQNATLVAYAKNYNGYLKLIKWSSWIMTSKEFEIQDDFDDLIIVCKKGTIVFKSPNFYQTHDQNAPNAIALQSVFYANKNDKIVFLAMLAIKNDLKLEDFKNCCDFDNNHFLNDNLAQSFFSPIALNNLNKVLNELKVQIHDLPINIPVYDKQNSIISSEILKQLCISGLKKRLNANDGQVNKIYVQRLKYELDVINEKQFDDYFLIVYDFINFAKSNGIIVGPGRGSAAGSLVAYCLHITDIDPIKHNLIFE... | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diph... |
Q92QM8 | MIDSAAPPSGFCRDCLKEQAAHSRRCLACGSPRLLRHSELYRLTLAHIDCDAFYASVEKRDNPELADKPVIIGGGKRGVVSTACYIARIHGVRSAMPMFKALEACPQAVVIKPDMEKYVRVGREVRAMMQELTPLVQPLSIDEAFLDLSGTERLHHDPPARTLARFAKRVEQEIGITVSVGLSYCKFLAKVASDLQKPRGFSVIGQAEAADFLKAKPVTLIWGVGKAFAATLERDGIRAIGQLQTMEEADLMRRYGTMGRRLYRLSRGLDERSVEIDGEAKSVSSETTFNDDLARQEDLVAHLRGLSEQVAFRLRKSALA... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
Q8UJK7 | MRKIIHVDMDAFYASVEQRDNPELRGRPVAVGSAAARGVVAAASYEAREFGVRSAMPSVTAARRCPDLIFVPPRFDVYKAVSQQIRAIFAEYTRLIEPLSLDEAYLDVTENLKGMEIATEIASEIRERIKQITGLNASAGISYNKFLAKMASDLNKPNGQAVITPKNGPAFVEQLAVKKFHGVGPATAEKMHRFGIETGADLKSKSLQFLAEHFGKSGAYFYGIARGIDERQVRPDRIRKSVGAEDTFSVDINDLDLATAELRPLAEKVWHHCEAQRVSGKTVTVKVKYSDFTQATRSRTSALPVNGIQEILEAASALLA... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
P54560 | MMKEKVIFLVDMQSFYASVEKAENPHLKNRPVIVSGDPEKRGGVVLAACPLAKQKGVVNASRLWEAQEKCPEAVVLRPRMQRYIDVSLQITAILEEYTDLVEPYSIDEQFMDITGSQKLFGTPMEIAKSIQGRIMREIGVYARVGIGPNKALAKIACDNFAKKNKNGIFTLTKENMKTEMWPLPVGSMFGVGSRMKHHLNRMGISTIGGLAAFPLDLLKKKWGINGHVLWMTANGIDYSPVSTSSLDGQKAIGHGMTLPRDYEHFDKEIKVVLLELSEEVCRRSRNAGVMGQTVSVSCRGADFDWPTGFNRQVKLAEPTN... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
Q8PT42 | MMPASNPKKNSSERRIVFHVDMDSFFASVEVRERPELKNLPVIVGSDPKGGSGRGVVSTCSYEARKYGIHSAMPISQAYRFCPDAVFLPVNMKLYAGVSAGVMEILRGFAEKFQQVSVDEAYLIPGSGVRNFEEAALYALRIKDEVQRQQKITCSVGVGPNKLVSKIASGFQKPDGLTVVRPEDVRDFLFPLPVSRIPGVGEKTEETLKKMGINRVEELANCDVQMLSEKLGKMGFRLKQLANGLDFEELVEKESVKSISRHGTFAEDTDDPVKVSGSLDLLIESVHGSLMKHSFLFKTITLTVRFEDFSTYTRSRTLSI... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
P63988 | MPTAAPRWILHVDLDQFLASVELLRHPELAGLPVIVGGNGDPTEPRKVVTCASYEARAYGVRAGMPLRTAARRCPEATFLPSNPAAYNAASEEVVALLRDLGYPVEVWGWDEAYLAVAPGTPDDPIEVAEEIRKVILSQTGLSCSIGISDNKQRAKIATGLAKPAGIYQLTDANWMAIMGDRTVEALWGVGPKTTKRLAKLGINTVYQLAHTDSGLLMSTFGPRTALWLLLAKGGGDTEVSAQAWVPRSRSHAVTFPRDLTCRSEMESAVTELAQRTLNEVVASSRTVTRVAVTVRTATFYTRTKIRKLQAPSTDPDVIT... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
Q98JM5 | METTATILHADLDAFYASVEQLLDPSLRGKPIAVGGGVVLAASYEARAFGVRGGMPGRKARELCPQLIFVGGNFSHYQRLGDAAIKVLDDFTPVVERISIDEAFADVAGCTHLFGQPRDIATAIRHRVRAELGLPISIGVARTKHLAKIASQVAKPDGLVVVDPGTELDFLHDLPVSLMWGVGPATKSRLAEIGIQTIGELARTHSGALTRLLGPAAGEKLAALAWNRDPRKLETRRRAHSAGAQSALGQKPAVARVIVPTLLHLADRVASRLRAKARPGRTVTVRVRFADLSAVTRSITLDQPISATTMLAEIAGDLVR... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
A3DH61 | MKRVILHCDLNNFYASVECLYHPELRDKPVAVCGSIEDRHGIVLAKNYAAKKYKVKTGETVWEAKNKCPGLVVVKANHSLYYKFSKYARQIYEYYTDRVESFGLDECWLDVSESTLLFGDGTKIANEIRERIKRELGVTVSVGVSYNKVFAKLGSDMKKPDAVTVITENDFKEKIWGLPVEALLYVGDSTKKKLNNMAVFTIGDLANCHSEFLVRQLGKWGYTLWSFANGYDTSPVAKNDCEIPIKSIGNSLTAPRDLTNNEDVRILIYVLSESVGERLRSHNLKGRTVQISIKDPELQTLERQAGLDIHTSITSEIAQK... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
Q6FFG4 | MRKIIHIDMDAFYASVELRERPELKTLPVVISSHHPRAVIAAASYPARVYGLRSAMPMGQARKLCPDLIIIEPNFDKYRAVSHQIHQIFQQHTHIIEPLSLDEAYLDVTENLNNLPSATDVAIQIRQQIWEQTSLTASAGVAPNKFLAKIASDWNKPNGLCVIKPHQVMQFIQNLPLKKIPGVGRVTQDKLQQLKLETLGDLQHIEEAVLIQHFGKYGKQLYLYAQGIDHRSVQAERVRQQISKETTFDQDLYLHECSSYWLMLAEKVWQSLQNKNLQARGVNIKLKNKHFQVFQHSKSFKRALQSLDEFKSVLALLLQE... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
A3N148 | MATQRKIIHIDMDCFYAAIEMRENPALIGKPVAVGGSVEGRGVLTTCNYEARKFGLHSAMPTAQALKRCPNLILVPVNMPLYKAVSEQIHQIFRRYTDIVELLSLDEAYLDVTDCRQCSGSATWIAQEIRDAIWNELHLTASAGIAPLKFLAKIASDQNKPNGQFVISPENMTAFIYDLPLKKIPRVGKVTNEKLAQLGLHTCGDIQHSDKAFIYKTFGKFGQRLWEFSHAIDNRKIEANRPRKSLAVENTLPTDIWHLAEAEQIVDELFKKLVFRLQRNWGERSLQEFKKLAIKLKFGDFTQTTLERTTDGLSRERFIE... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
B2UKN1 | MNQRKIIHVDMDAFYASIEQRDHPEYRGKPIAVGRPEMRGVVAAASYEARRFGVRSAMPSMKALKLCPHLIFTRNRMDVYKAVSAQIHAIFHRYTDLVEPLSLDEAFLDVTENKPGIPLAVDIARRIKKEIRRELHLTASAGVSYNKFLAKIASDYRKPDGLFTIHPSRAEKFIAALPIEAFWGVGHATAERMRALSITNGAQLRARDKDFLVRHFGKTGAIFYNFARGVDDRPVEPSRMRKSVGCEETYRENVTRAEALEQRLPLLAEELAGRLARSGFRGNTLTLKVKFPDFVQKTRCATVPEILTEKEGILPLARTL... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
Q0A4X2 | MSQRKIIHVDMDAFYASVEQRDRPGLRGRPVVVGGDPNGRGVVAAASYEARRHGIHSAMPAWRAARLCPDAVFLRPRFDVYRSISAQIQALFREYTPLVEPLSLDEAYLDVSDCPRRGGSATLIAREIRARIHEQTGLTASAGVSCNKFLAKIASDLDKPDGLHVIPPEQAEAFVAALPVGKIHGVGQATRQRMERMGVRTGADLRRLTLLELQRAFGSRARFYYELARGRDERPVRPRRERKSVGAETTFGEDLNNPAEMLERMAPLADKVAASLHRRGLAGRTVTLKVKYHDFRQITRSLSGRPVQSADEIRARLPAL... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
A8MGJ5 | MNPVIFLVDMNAFFISCEMTRNSKLIGIPAAVAGNPQNRTGIVLAANYEARRFGVKTAMTLNNALKLCPTMTVVPPDHRFYRQKSSEVMNLLSKYTPIIEQSSIDEAWLDMTGTENLFGKPADAAKLIMEDIKENLGLWCSIGISEGKFLSKMASDMKKPLGITELWKRDIQTKLWPLSIKSMHGVGAKTYEKLHSLGIETIGDFANLKKDDAHQILGKFGLDLYHHAHGIDTTPVQVISPDDMKSIGRSTTLPEDLVDIEQLKYILLTLCEDIGRSARKHNKRGRTVNLTLKSSDFKVIHRQVTIKATFNTMEIYEAGY... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
Q8CNP3 | MTERRIIHIDMDYFFAQVEMRDNPKLKGKPVIVGGKASHRGVVSTASYEARAYGVHSAMPMTQAHKLCPNGYYVTSRFDTYREVSGQIMKIFRSYTELVEPMSLDEAYLDITHLVRPDLPASTIANYIRRDIYEVTRLTASAGVSYNKFLAKLASGMNKPNGLTVIDYNNVHEILMQLDIGDFPGVGKASKKKMHQHHIYTGQDLYNKDEFELIRLFGKRGRGLYNKARGIDHNEVKASRVRKSVGTERTFSTDVNDDDVILRKIRELSGKTAERLNKIQKSGKTVTVKIKTYQYETISKQKSLRDPIRTETDIYNIAYT... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
Q9AK82 | MRTAPTILHLDMDAFFASVEQASKPSLRGKAVVVGGLGPRGVVATCSYEARVFGVHSAMPMGQARRLAPHAAYLVPRFELYRSISEQVMRLLRELSPLVEPLSLDEAFVDLDAGGAARDAETARLAGTKLRTDIRTVTGLTGSVGLAASKMLAKIASEAAKPDGLVLIPPGTERAMLEPMTVRTLPGVGPATGDHLRRAGITTVGEIAEAGEDELVRLLGKAHGHALYAMALARDERPVVAERETKSVSVEDTYDVDIHDRVRVGVEVGRLADRCVRRLRASGLSGRTIVLKVRRYDFSTLTRSETLRGPTDDPAVVREA... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
B2FLR2 | MTRLRKIIHVDMDAFYASVEQRDDPSLRGKPVVVAWRGARSVVCAASYEARVFGVRSAMPAVRAERLCPDAIFVPPDFARYKAVSQQVRAIFLRHTDLVEPLSLDEAYLDVSEPKSGIELATDIARTIRAQIREETNLTASAGIAPNKFLAKIASDWRKPDGQFVIPPQRVDAFLAPLPVNRVPGVGKVMEGKLAARGIVTCGDLRQWALIDLEEAFGSFGRSLYNRARGIDERPVEPDQQVQSISSEDTFAEDLLLEDLTEAIVQLAGKTWNATRKTERIGHTVVLKLKTAQFRILTRSFTPERPPESMEELRDIALAL... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
Q99Y66 | MLIFPLINDTSRKIIHIDMDAFFAAVEERDNPALKGKPVVIGKDPRETGGRGVVSTCNYEARKYGIHSAMSSKEAYERCPKAIFISGNYEKYRTVGDQIRRIFKRYTDVVEPMSIDEAYLDVTDNKLGIKSAVKIAKLIQHDIWKEVGLTCSAGVSYNKFLAKLASDFEKPHGLTLVLKEDALCFLAKLPIEKFHGVGKKSVKKLHDMGIYTGQDLLAVPEMTLIDHFGRFGFDLYRKARGISNSPVKSDRIRKSIGSERTYAKLLYQETDIKAEISKNVKRVAALLQDHKKLGKTIVLKVRYADFTTLTKRVTLPELTR... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
P06746 | MSKRKAPQETLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVSGIGPSAARKFVDEGIKTLEDLRKNEDKLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEVKKVDSEYIATVCGSFRRGAESSGDMDVLLTHPSFTSESTKQPKLLHQVVEQLQKVHFITDTLSKGETKFMGVCQLPSKNDEKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEKDIF... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Repair polymerase that plays a key role in base-excision repair . During this process, the damaged base is excised by specific DNA glycosylases, the DNA backbone is nicked at the abasic site by an apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxyrib... |
Q8K409 | MSKRKAPQETLNGGITDMLVELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVTGIGPSAARKFVDEGIKTLEDLRKNEDKLNHHQRIGLKYFEDFEKRIPREEMLQMQDIVLNEIKKVDSEYIATVCGSFRRGAESSGDMDVLLTHPNFTSESSKQPKLLHRVVEQLQKVHFITDTLSKGETKFMGVCQLPSEKDGKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEQDIF... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Repair polymerase that plays a key role in base-excision repair. During this process, the damaged base is excised by specific DNA glycosylases, the DNA backbone is nicked at the abasic site by an apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxyribo... |
O57383 | MSKRKAPQESPNEGITDFLVELANYERNVNRAIHKYNAYRKAASVIAKYPTKIKSGTEAKKLDGVGAKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVTGIGPAAARKFFDEGIKTLDDLRNNEHKLNHHQKIGLKHFDDFEKRIPRKEMLQMQEIILDKVNNLDPEYIATVCGSFRRGAESSGDMDILLTHPDFTSESAKQPRLLHQVVQCLEDCNFITDTLVKGDTKFMGVCQLPCESDQDYPYRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRTHALEKGFTLNEYTLRPLGVTGIAGEPLPIDSEKDIFD... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Repair polymerase that plays a key role in base-excision repair. During this process, the damaged base is excised by specific DNA glycosylases, the DNA backbone is nicked at the abasic site by an apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxyribo... |
Q9FNY4 | MAAKRGRNRSPSPDPEGMFAGMVVFMVEIGVQRRRLQIWKQKLVQMGAVIEEDRVTKKVTHVLAMNLEALLHKFGKERLSHFTARLMLYQWLEDSLTSGEKANEDLYVLKIDSEEVDKPKKSLPAISGSEDQSSPQKRTRYSPDAGDFKGVESHSNTQGSPDSPTSCSVPSTSASPGEGIAETPTSPQSESTSVYKPPDLNRNITEIFGKLINIYRALGEDRRSFSYYKAIPVIEKFPTRIESVDQLKHLPGIGKAMRDHIQEIVTTGKLSKLEHFETDEKVRTISLFGEVWGVGPATALKLYEKGHRTLEDLKNEDSLT... | Function: Repair polymerase involved in base excision repair (BER) and responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Has both DNA polymerase and terminal transferase activities. Has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity (By similarity). Involved in the repair of transpo... |
Q9UGP5 | MDPRGILKAFPKRQKIHADASSKVLAKIPRREEGEEAEEWLSSLRAHVVRTGIGRARAELFEKQIVQHGGQLCPAQGPGVTHIVVDEGMDYERALRLLRLPQLPPGAQLVKSAWLSLCLQERRLVDVAGFSIFIPSRYLDHPQPSKAEQDASIPPGTHEALLQTALSPPPPPTRPVSPPQKAKEAPNTQAQPISDDEASDGEETQVSAADLEALISGHYPTSLEGDCEPSPAPAVLDKWVCAQPSSQKATNHNLHITEKLEVLAKAYSVQGDKWRALGYAKAINALKSFHKPVTSYQEACSIPGIGKRMAEKIIEILESG... | Function: DNA polymerase that functions in several pathways of DNA repair . Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA . Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination . Has both templ... |
Q9QXE2 | MDPQGIVKAFPKRKKSHADLSSKALAKIPKREVGEARGWLSSLRAHIMPAGIGRARAELFEKQIIHHGGQVCSAQAPGVTHIVVDEDMDYERALRLLRLPQLPPGAQLVKSTWLSLCLQEGRLTDTEGFSLPMPKRSLDEPQPSKSGQDASAPGTQRDLPRTTLSLSPPHTRAVSPPPTAEKPSRTQAQLSSEDETSDGEGPQVSSADLQALITGHYPTPPEEDGGPDPAPEALDKWVCAQPSSQKATNYNLHITEKLEVLAKAYSVQGDKWRALGYAKAINALKSFHKPVSSYQEACSIPGIGKRMAEKVMEILESGHL... | Function: DNA polymerase that functions in several pathways of DNA repair. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. Has both template... |
Q67VC8 | MAPKRKPPARAAAAKLDPDGMFRGVSAFVVPHAVQSRRLEVWKQRLAQMGGRVQEKLAAKGGGGAVTHVLAADAKALLRELDAAWLHRFRGSVVSFEWLEECLKSGERLPEHKFAINYEEEFKPKKEGGAAGSGVLQSAKRSKISSDGPENRKETAGGNRESRDAIAHPNEDSDVVKGPSTCTSSQSASGDSKETIASQNAFKAEEASSGESSTYAPPDLNRNITEIFGKLINIYRALGDDRRSFSYYKAIPVIEKLPFKIESADQVKDLPAIGKSLKDHINEIVNTGKLSKLEHFENDEKVRTVSLFGEVWGVGPATAL... | Function: Repair polymerase involved in base excision repair (BER) and responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Has both DNA polymerase and terminal transferase activities. Has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-t... |
Q9NP87 | MLPKRRRARVGSPSGDAASSTPPSTRFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSWQERRMAAAPPGCTPPALLDISWLTESLGAGQPVPVECRHRLEVAGPRKGPLSPAWMPAYACQRPTPLTHHNTGLSEALEILAEAAGFEGSEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVCEEVERVRRSERYQTMKLFTQIFGVGVKTADRWYREGLRTLDDLREQPQKLTQQQKAGLQHHQDLSTPVLRSDVDALQQVVEEAVGQALPGATVTLTGG... | Function: Gap-filling polymerase involved in repair of DNA double-strand breaks by non-homologous end joining (NHEJ). Participates in immunoglobulin (Ig) light chain gene rearrangement in V(D)J recombination.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (D... |
Q9JIW4 | MLPKRRRVRAGSPHSAVASSTPPSVVRFPDVAIYLAEPRMGRSRRAFLTRLARSKGFRVLDAYSSKVTHVVMEGTSAKEAICWQKNMDALPTGCPQPALLDISWFTESMAAGQPVPEEGRHHLEVAEPRKEPPVSASMPAYACQRPSPLTHHNTLLSEALETLAEAAGFEANEGRLLSFSRAASVLKSLPCPVASLSQLHGLPYFGEHSTRVIQELLEHGTCEEVKQVRCSERYQTMKLFTQVFGVGVKTANRWYQEGLRTLDELREQPQRLTQQQKAGLQYYQDLSTPVRRADAEALQQLIEAAVRQTLPGATVTLTGG... | Function: Gap-filling polymerase involved in repair of DNA double-strand breaks by non-homologous end joining (NHEJ). Participates in immunoglobulin (Ig) light chain gene rearrangement in V(D)J recombination.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (D... |
Q7Z5Q5 | MENYEALVGFDLCNTPLSSVAQKIMSAMHSGDLVDSKTWGKSTETMEVINKSSVKYSVQLEDRKTQSPEKKDLKSLRSQTSRGSAKLSPQSFSVRLTDQLSADQKQKSISSLTLSSCLIPQYNQEASVLQKKGHKRKHFLMENINNENKGSINLKRKHITYNNLSEKTSKQMALEEDTDDAEGYLNSGNSGALKKHFCDIRHLDDWAKSQLIEMLKQAAALVITVMYTDGSTQLGADQTPVSSVRGIVVLVKRQAEGGHGCPDAPACGPVLEGFVSDDPCIYIQIEHSAIWDQEQEAHQQFARNVLFQTMKCKCPVICFN... | Function: DNA polymerase with very low fidelity that catalyzes considerable misincorporation by inserting dTTP opposite a G template, and dGTP opposite a T template . Is the least accurate of the DNA polymerase A family (i.e. POLG, POLN and POLQ) . Can perform accurate translesion DNA synthesis (TLS) past a 5S-thymine ... |
P42494 | MLTLIQGKKIVNHLRSRLAFEYNGQLIKILSKNIVAVGSLRREEKMLNDVDLLIIVPEKKLLKHVLPNIRIKGLSFSVKVCGERKCVLFIEWEKKTYQLDLFTALAEEKPYAIFHFTGPVSYLIRIRAALKKKNYKLNQYGLFKNQTLVPLKITTEKELIKELGFTYRIPKKRL | Cofactor: In the presence of magnesium, pol X shows a strong preference for the ssDNA gaps having one and two nucleotides.
Function: Error-prone polymerase lacking a proofreading 3'-5' exonuclease which catalyzes the gap-filling reaction during the DNA repair process . Specifically binds intermediates in the single-nuc... |
P80725 | MKTINSVDTKEFLNHQVANLNVFTVKIHQIHWYMRGHNFFTLHEKMDDLYSEFGEQMDEVAERLLAIGGSPFSTLKEFLENASVEEAPYTKPKTMDQLMEDLVGTLELLRDEYKQGIELTDKEGDDVTNDMLIAFKASIDKHIWMFKAFLGKAPLE | Function: Protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction. Does not bind DNA.
Catalytic Activity: 2 Fe(2+) + 2 H(+) + H... |
A0R692 | MTSFTIPGLSDKKASDVADLLQKQLSTYNDLHLTLKHVHWNVVGPNFIGVHEMIDPQVELVRGYADEVAERIATLGKSPKGTPGAIIKDRTWDDYSVERDTVQAHLAALDLVYNGVIEDTRKSIEKLEDLDLVSQDLLIAHAGELEKFQWFVRAHLESAGGQLTHEGQSTEKGAADKARRKSA | Function: Protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction (By similarity). It protects DNA from hydroxyl radical-mediat... |
B2RMG0 | MKKILEVTGLKEQQVAPVVKGLSGLLADLQVYYSNLRGFHWNIRGAEFFVLHEQYEKMYDDLAGKIDEVAERILQLGGKPENRFSEYLKVAEVKEEHELVCAASTLKNVTDTLQIIMAKERAIAEVAGEAGDEVTVDLMIGFLSGQEKLVWMLSAYATK | Function: Responsible for protection of cells against peroxide, especially against hydrogen peroxide. Required for survival in host cells. Although it binds iron, it may not contribute to iron storage. The iron-loaded dps has DNA-binding activity.
Sequence Mass (Da): 17823
Sequence Length: 159
Subcellular Location: Cyt... |
P95855 | MQEKPQEPKVVGVEILEKSGLDIKKLVDKLVKATAAEFTTYYYYTILRMHLTGMEGEGLKEIAEDARLEDRLHFELMTQRIYELGGGLPRDIRQLADISACSDAYLPENWKDPKEILKVLLEAEQCAIRTWKEVCDMTYGKDPRTYDLAQRILQEEIEHEAWFLELLYGRPSGHFRRSSPGNAPYSKK | Function: Protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction (By similarity). In vitro, it efficiently oxidizes Fe(2+) in ... |
B6TB21 | MSAALAVTDEVALPIRAVGDLAAAAEVSREEVAVITQCAALGGKLPFEDASVGAVLAVIKNVESLREQLVAEIRRVLKAGGRVLVQSPAPSSSQKPNTDIERKLLMGGFAEVQSSAASSQDSVQSVTVKAKKASWSMGSSFPLKKTTKALPKIQIDDDSDLIDEDSLLTEEDLKKPQLPVVGDCEVGAAKKACKNCTCGRAEAEEKVGKLELTAEQINNPQSACGSCGLGDAFRCGTCPYRGLPPFKPGEKVSLSGNFLAADI | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosoli... |
A8PS95 | MNNTAHSMSEKVLLVASLEAARYGQYQQAVKGLQAESGLLETHMIDRITDLAYAPPADYFDAVYMMLPSEGVEWAAALPKLRASMIPGAKLRVSVVNENDPSSFLSQVRAELTIAGFTDIQTYENASIESRRPASSSVAEKDSTASSGMGAVKLRRKPNENGGHQQKKALLWATQPETHMDTEAKLQEHARTVSPASRREDCTVDFSAPRTRRKRACKGCTCGLRELEEEDERNSNLVQLDPSEVGGTGGKRTEVTTTVKGPNGEEHTVRRIQVDTRGATSSCGSCFLGDAFRCSSCPYLGLPAFEPGQKVEIPANMDDD... | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold ... |
B7FNA9 | MDAAKMYGAVLACTDEAVLPVSQVFDAIRELGNEGVEKLDPLVITSASSLSKFPVESSSVDLVVLIWKSLDFPIDQLTQEVLRVLKAGGTTLIRKSSQSAVGSGDKMIPDLENKLLLAGFSEIQALQSSVIKAKKPSWKIGSSFALKKVVKSSPKVQIDFDSDLIDENSLLSEEDLKKPELPSGDCEIGPTRKACKNCSCGRAEEEEKVLKLGLTAEQINNPQSACGSCGLGDAFRCSTCPYKGLPAFKMGEKVALSGNFLAADI | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosoli... |
A9V767 | MADLQGKAVLTIAVPEAKADQIEAEILRLRAATTEAGSVQLEQFDRLEQVFLAPSSYDVIFSGHIALPAKSHADSALAKLAAALKPGGRLALRESLNSRNETALRSALTMGGFVNVQVSTSEHALEAHADKPVYEVGAAAPLKLSFAKKKQSGAAAPAAQVAEVWTIATDDFDDDDLLENDGDELLDAEDLALATTAPEGDDCEVGAGGKRRACKNCTCGRADAEAEQAAKPTLTGPLPASSCGNCYLGDAFRCASCPYLGMPAFKPGEKVTLSDRQLKADA | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosoli... |
A7S710 | MEAVVDTNNFVLLLWSGAQLPKDIEAVVGSLTKKVGPNGKVSLEHSDRLHIASHAMSSFDVVLSGVCESPSLIHSMELLSKLAKLLKPDGKLILREPVGSNDSRSPEKIISTLKLSGFVSISQANEVKPSIVEISAQKPSFEVGAKTALSLSFAPKPAQPKAETSAAQIWTLSAQDIDDEDVDLLDSDTLLDEDDLKKPDPLSLKAACGPGSGKKKACKNCTCGLAEQENGDATEKKSVTSSCGSCYLGDAFRCSTCPYLGMPAFKPGEKIALTDRQLKGDL | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosoli... |
A4RS24 | MSVLALDVARDVAAPRRAEILETLRALADGADATTREIASDDDADALERASCDAYFARARDASEARRACARASEKLRAGGALGVVVDDERTATATTEAMVLAGFTTVTREDDGVVRCVKPNWARGTAFALKSRAVRVNATAADAADAWGASAAADDDELIDESALLTELDVNTAPVKYDDCDVGAGKKACKNCTCGRAEAEAAEEATTAASEETFVSACGNCALGDAFRCAGCPYLGQPAFKDQPGTKVELDLGDDL | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosoli... |
C1G2L9 | MPPSQTPAQGSGRFLLLSPPSLSSHPEKLNAILGLHARESTDLQMLDRLALGLVSLPESTYDVVLLLTGADNTLAETYRLVSRGVLQGVVNSLKPGGKLRNRDNQIWGSGSDSAAGLGSSDGDGGGGEKMSSSEQAFRNEAILAGLVFDDRGELAKPDFGAQQAVPLKLGRKKNLGESAFGNGAVELPASNGVRVTTGATSSTTTTTTTTAAAAAATAATPTTTTTTTINSSTPSGVGFIDFSDDFGVPMVEETQDSDEELIDEEELLGEYDMGRHIVQPPECRPKAGKRRRACKDCTCGLSQKLEAEDRAKRANADKAL... | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold ... |
Q0UTA2 | MAAPRTLLLCPPSLSAHPEALNKIYEIHDRSTADLQMLDRIAAGLVQLPAATYDVVLLLTDADGTTRESHKLLARDVASKVAGALKVGGILKAKTEAILAGLSESPNGMVKTEQVESVSIPLKFGKKKTNGVNGTNGAVNPDGSVPLNLNGKRNQPEPVKPVGVGFVDFSDDLDDPIITGEDDDDDLIDEDDLITEEDMARPVIQQCRPKAGKRRRACKDCTCGLKEKMEAEDAAKRTTADKALNTMKLGADDLDELDFTVQGKVGSCGNCALGDAFRCDGCPYIGLPAFKPGEEVRLLNNDIQL | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold ... |
B7G267 | MVPPREDVTVRIVCERRRTAGKEARPPPSAKPTPGNTSSHPNAKETHRSNEPFFRLYTKQSHRRSIMASTLCVVLGSASSTDPAAISAATMTDAAAKTIHDAIYESLELVVVASELADVYDSMELSRFTKILSPNATVSVSVIGDATKSLSPIHTSFLLAGLANNSERRNADGSRTLTATRRNNTTNSVATLNFASNNNNGNDLLIDEDNLLTDASNLLGAPPSMSAAATKSGDDCSGRAPCDDCTCGRAEGAKEGNSEQPKEIKSSSCGKCSLGDAFRCASCPYLGKPAFKPGEEHLVLDLQDDF | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosoli... |
D0N381 | MALQGNVAILTRLQDTASAVQQFKQTNPQVADVTVLAVAEDSDVTQTVTSSSASAKENAFDGIVSFSEQTEELGIELGAVLPLLKTGGVLQLHVANVKEEKKNAILMALMIGGLVDTSDKQESSPFYPEFSDAVSFTSKKQSFESAAIPLAVKSTTTQPIKKWTVLADDFGDDQDDDIIDEDTLLDDTDEVLQAAKADCGDAVGGKKRACKNCTCGLKDENDKPVMSEKDLNSLVSGCGNCFKGDAFRCGSCPFLGKPAFKPGMEKVLLNLDSSDDI | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosoli... |
Q9S0S3 | MMSQQDLPTLFYSGKSNSAVPIISESELQTITAEPWLEISKKGLQLEGLNFDRQGQLFLLDVFEGNIFKINPETKEIKRPFVSHKANPAAIKIHKDGRLFVCYLGDFKSTGGIFAATENGDNLQDIIEDLSTAYCIDDMVFDSKGGFYFTDFRGYSTNPLGGVYYVSPDFRTVTPIIQNISVANGIALSTDEKVLWVTETTAKRLHRIALEDDGVTIQPFGATIPYYFTGHEGPDSCCIDSDDNLYVAMYGQGRVLVFNKRGYPIGQILIPGRDEGHMLRSTHPQFIPGTNQLIICSNDIEMGGGSMLYTVNGFAKGHQS... | Cofactor: Binds 2 Ca(2+) ions per subunit.
Function: Exhibits lactonase activity. Acts in cells with perturbed membrane integrity and is possibly related to the membrane homeostasis. Contributes to bacitracin resistance (By similarity).
Sequence Mass (Da): 35978
Sequence Length: 324
Subcellular Location: Cytoplasm
EC: ... |
P76334 | MEYGSTKMEERLSRSPGGKLALWAFYTWCGYFVWAMARYIWVMSRIPDAPVSGFESDLGSTAGKWLGALVGFLFMALVGALLGSIAWYTRPRPARSRRYE | Function: A non-essential division protein that localizes to the septal ring in low ionic strength medium.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11325
Sequence Length: 100
Subcellular Location: Cell inner membrane
|
A8E5C5 | MAVPSVMVLPLLIVVFAGVYYVYNEVMRFMSKSVVRNKVVVITDAVSGMGSECARLFHAGGARLVLCGPSWDKLESLYDSLCSGSDPSQTFTPKLVLLDFSDMENISDVVSEICECYGCVDVLICNSSMKVKAPVQNLSLEMDKTIMDVNYFGPITLAKGVLPLMITRRTGQFVLVNSIQGKLALPFRTCYAASKHAVQAFFDCLRAEVEEFGISVSTISHTFINAGAENATPTEATPITATPTKATPTNPIWAYVCSKLNTHGVSPQILAQEIVRSVNRQSREVFLAHPVPTVALYIRALMPGCFFSVVSAGVRDGAMA... | Function: Putative oxidoreductase.
Sequence Mass (Da): 35182
Sequence Length: 324
Subcellular Location: Secreted
EC: 1.1.-.-
|
Q21EN9 | MKITKLPSYRQTALIIFAGCVGLILAALYMQEVLGLHPCPLCITQRIFIIGVGLISLIAAIHNPAALGRKVYGCLATLSGVIGAGVSARHVWLQNLPEDQVPACGPDLAYMFDAFPLLDALKLLFAGDGNCADVVASFLGLSIPGWTFVAFVGLIAISVWQGLRKA | Function: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17579
Sequence Length: 166
Subcellular Location: Cell inner membrane
|
Q57NK5 | MLRFLNQCSRGRGAWLLMAFTALALEMVALWFQHVMLLKPCVLCIYERCALFGVMGAGLVGAIAPKTPLRYVAMVIWIYSAWRGLQLAYEHTMIQLHPSPFMTCDFMARFPDWLPLGKWLPQVFVASGDCAERQWSFLTLEMPQWLLGIFAAYLVVAIAVVIAQAFKPKKRDLFGR | Function: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20063
Sequence Length: 176
Subcellular Location: Cell inner membrane
|
Q083H4 | MSQLQQFCHNRFSWGLLLLSAIGLELAALFFQYGMDLAPCVMCIYIRVAVLGIILAALIGILQPKVWLLRLVGMAGWAVSAVWGFKLAYELNQMQVNPSPFATCSFYPEFPSFMPLDTWLPSVFSPTGMCSDSPWSWLSVSMAQWMMLGFAIYGVIWLLMLLPALKSAK | Function: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18913
Sequence Length: 169
Subcellular Location: Cell inner membrane
|
A1RKH3 | MTALTRFAHSRSSWFLLTGTAIGLEAAALYFQYVMKLDPCVMCIYQRLAVFGILVAGLIGMTAPKYRLIRILGASCWAVSATWGLKLALALVNMQNNPSPFATCSFLPEFPTWMPLHEWFPAVMLPTGMCTDLPWRFMDVTMAEWMVVVFSTFLVIWLLFIVPILSGSTKPSLYK | Function: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19672
Sequence Length: 175
Subcellular Location: Cell inner membrane
|
Q6CRM2 | MQFKKSSIVSFLSLLGSLTKAAAEVRLVTMDGVVYSYQVVTSTIKPATTYVETIYYTTTYVEAVTLTNHAVTSTTRESVVTSTLSSTSLLPETTEESTQEDEQTTDFTSTTDVESTTDVTSTTAETATLEPTTSDETYTTELTPTTSVKTTLENDDSTSVITTKSTSKANTQSISRKTSTLTPTVTSETTESTSAETLSSTDKSTSTSSSSVLEPMVTNTDCQVVYEYTDDDEYYSTVEISGTESVDAATTYTKTRTVYATISS | Function: Involved in pseudohyphal growth, cell wall metabolism and required for the separation of the mother and daughter cells.
Location Topology: Lipid-anchor
Sequence Mass (Da): 28409
Sequence Length: 264
Subcellular Location: Secreted
|
P38844 | MKFNFSTIFNILFFLFTLIEANSNGETVKLITSDGIVYSYAVYTKTLAPARVVVKTISYTTTRVYPITLANSVVSSTTEKITEVSTVSASEQVSATQTNSLVSTSTVSTISPTISSGSSTSSSSTYDIESSQSIESSGTSSATAEPSASSGFRLTSSSAFVSSTAPFSSQLSSSSSSETSSSSFSTSSSSAPLSLTSSSSSSSSFATIITLAPSSSKSGNSQLTLASSSSTSAVESSQTGSTIARTTSTLVPSSSVDTTSRATTSMPLESSSTQSISVSSSDGTCYVFYDDDDYYSTVYLTNPSQSVDAATTITSTNTIY... | Function: Involved in pseudohyphal growth, cell wall metabolism and required for the separation of the mother and daughter cells.
Location Topology: Lipid-anchor
Sequence Mass (Da): 33417
Sequence Length: 325
Subcellular Location: Secreted
|
O49523 | MKRKKKEEEEEKLIVTREFAKRWRDLSGQNHWKGMLQPLDQDLREYIIHYGEMAQAGYDTFNINTESQFAGASIYSRKDFFAKVGLEIAHPYTKYKVTKFIYATSDIHVPESFLLFPISREGWSKESNWMGYVAVTDDQGTALLGRRDIVVSWRGSVQPLEWVEDFEFGLVNAIKIFGERNDQVQIHQGWYSIYMSQDERSPFTKTNARDQVLREVGRLLEKYKDEEVSITICGHSLGAALATLSATDIVANGYNRPKSRPDKSCPVTAFVFASPRVGDSDFRKLFSGLEDIRVLRTRNLPDVIPIYPPIGYSEVGDEFP... | Function: Acylhydrolase that catalyzes the hydrolysis of 1,3-diacylglycerol (1,3-DAG) and 1-monoacylglycerol (1-MAG) at the sn-1 position. High activity toward 1,3-DAG and 1-MAG, but low activity toward 1,2-diacylglycerol (1,2-DAG) and 1-lysophosphatidylcholine (1-LPC), and no activity toward phosphatidylcholine (PC), ... |
P0C2H4 | MRTHTRGAPSVFFICLFCFVSACVTDENPEVMIPFTNANYDSHPMLYFSRAEVAELQLRAASSHEHIAARLTEAVNTMLSSPLEYLPPWDPKEYSARWNEIYGNNLGALAMFCVLYPENMEARDMAKDYMERMAAQPSWLVKDAPWDEVPLAHSLVGFATAYDFLYNYLSKTQQEKFLEVIANASGYMYETSYRRGWGFQYLHNHQPTNCMALLTGSLVLMNQGYLQEAYLWTKQVLTIMEKSLVLLREVTDGSLYEGVAYGSYTTRSLFQYMFLVQRHFDINHFGHPWLKQHFAFMYRTILPGFQRTVAIADSNYNWFY... | Cofactor: Also has weak activity in the presence of Mg(2+) or Ca(2+) ions.
Function: Converts D-glucuronic acid to L-iduronic acid (IdoUA) residues. Plays an important role in the biosynthesis of the glycosaminoglycan/mucopolysaccharide dermatan sulfate.
Catalytic Activity: chondroitin 4'-sulfate = dermatan 4'-sulfate
... |
Q9UL01 | MRTHTRGAPSVFFIYLLCFVSAYITDENPEVMIPFTNANYDSHPMLYFSRAEVAELQLRAASSHEHIAARLTEAVHTMLSSPLEYLPPWDPKDYSARWNEIFGNNLGALAMFCVLYPENIEARDMAKDYMERMAAQPSWLVKDAPWDEVPLAHSLVGFATAYDFLYNYLSKTQQEKFLEVIANASGYMYETSYRRGWGFQYLHNHQPTNCMALLTGSLVLMNQGYLQEAYLWTKQVLTIMEKSLVLLREVTDGSLYEGVAYGSYTTRSLFQYMFLVQRHFNINHFGHPWLKQHFAFMYRTILPGFQRTVAIADSNYNWFY... | Cofactor: Also has weak activity in the presence of Mg(2+) or Ca(2+) ions.
Function: Converts D-glucuronic acid to L-iduronic acid (IdoUA) residues. Plays an important role in the biosynthesis of the glycosaminoglycan/mucopolysaccharide dermatan sulfate.
Catalytic Activity: chondroitin 4'-sulfate = dermatan 4'-sulfate
... |
Q8BLI4 | MRTHTRGAPSVFFICLLCCVSAFITDENPEVMIPFTNANYDSHPMLYFSRKDVAELQLRAASSHEHIAARLTEAVHTMLTNPLEYLPPWDPKEYSARWNEIYGNNLGALAMFCVLYPENTEARDMAKDYMERMAAQPSWLVKDAPWDEVPLAHSLVGFATAYDFLYNYLSKTQQETFLEVIANASGYMYETSYRRGWGFQYLHNHQPTNCMALLTGSLILMNQGYLQEAYLWTKQVLSIMEKSLVLLREVTDGSLYEGVAYGSYTTRSLFQYMFLVQRHFDINHFGHPWLKQHFAFMYRTILPGFQRTVAIADSNYNWFY... | Cofactor: Also has weak activity in the presence of Mg(2+) or Ca(2+) ions.
Function: Converts D-glucuronic acid to L-iduronic acid (IdoUA) residues. Plays an important role in the biosynthesis of the glycosaminoglycan/mucopolysaccharide dermatan sulfate.
Catalytic Activity: chondroitin 4'-sulfate = dermatan 4'-sulfate
... |
P0CX08 | MTKSDETTATSLNAKTLKSFESTLPIPTYPREGVKQGIVHLGVGAFHRSHLAVFMHRLMQEHHLKDWSICGVGLMKADALMRDAMKAQDCLYTLVERGIKDTNAYIVGSITAYMYAPDDPRAVIEKMANPDTHIVSLTVTENGYYHSEATNSLMTDAPEIINDLNHPEKPDTLYGYLYEALLLRYKRGLTPFTIMSCDNMPQNGVTVKTMLVAFAKLKKDEKFAAWIEDKVTSPNSMVDRVTPRCTDKERKYVADTWGIKDQCPVVAEPFIQWVLEDNFSDGRPPWELVGVQVVKDVDSYELMKLRLLNGGHSAMGYLGY... | Function: Catalyzes the NAD(H)-dependent interconversion of D-fructose and D-mannitol in the mannitol metabolic pathway.
Catalytic Activity: D-mannitol + NAD(+) = D-fructose + H(+) + NADH
Sequence Mass (Da): 56470
Sequence Length: 502
EC: 1.1.1.67
|
Q9HM47 | MHLIVASRSDPASVRMLDYLTEKYTFSEKGGVLNHGDFDLVIIEDRHIFHDMSLSGKYDYLVVLSRHSSAADVKSLTAHPTGNFGPSADLGGKPRTINISCPRVMSGTLRRMMESYSGSRFEVTFEATHHGPIFDIPNYYVEIGTTENEWNDPEALSTTVDSVMNPDVRDYDAFVGVGGGHYAPKIKEYFRENSVNIGHIISKHDHDALEPWEIDMAVKRTPGCKGFIMDRKGTRGNVREMVKKYADENSLELITI | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-amino... |
Q97CM5 | MKVLIASKSDPASMQMLSYLEDNYDIKENSGRRFVKDFEIFVIEDRHIFHDMNLGNNYEYAVVLSRHSSAADIKSLTAHPTGNFGPKADLGGRPKTINVSCPKYMSGTLRQMLESYSGTKFQVTFEATHHGPIFDLPNYYVEIGTTENEWTDDDAKKTAVDAVINPDAKDFPNFVAVGGGHYAPKILEYFRRNEINIGHIISKHDHDDLEEWQIKDAVEKTPSCKGFLVDRKGTRSRVRDMVKSISDDLGLELIMI | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-amino... |
Q01213 | MSTDYLTLNRTGDKMPIRGFGCWKIDTKDCEETVYQAIKTGYRLFDGACDYGNEVEVGRGINKAINEGLVKREDLFIVTKLWNTFHSKKHVRALFDRQLKDTGLEYFDLYLIHFPVPLQYVDPATVYPPGWYVGDAKSLQFEQSPIHECWAELEKIVDAGLARNIGVANFNCQAILDLLTYARIKPAVLQIELHPYLPQERLVKWVKEQGIQITAYSSFGPTSYVDLTESGKTYTSLLEHASVKSVADKHNVSTGQVLLRWALDREFAVIPKSVNAGRMKANLEILDIKLDAEDNKTLDSLKTNQRFNDPMTYGFGLPLF... | Function: Catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Sequence Mass (Da): 36484
Sequence Length: 321
Pathway: Pheromone biosynthesis; trisporate biosynthesis.
EC: 1.1.1.-
|
Q6F6W0 | MRALIQRVKEAKVIVDDVITGEIRQGLLVFLGLGRDDQLENGKKLIDKILKYRVFDDENGKMGWNLSQAQGGLLLVSQFTLMAQTQKGLRPDFGPAMPPQQAKVLYDQLVEYAQSQFDHVETGIFAADMQVHLINDGPVTFQLEIL | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
Q8FPG8 | MKAVLTRVSSASVTVGDEVVGSIDCPETGGLLALVGVGAADEPDAWETMVRKIAELRILDNEKSVSDVGAPVLLVSQFTLMGKTARGRRPSWSDAAAGGIAEPVMRRIATGLRERGIHVEEGRFGAMMKVASVNEGPFTVLVEC | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
B2HD97 | MRVLVQRVCSAAVTVDGDVVGAVRPPGQGLLAFVGVTHGDDGDKARRLAEKLWYLRILTDEKSASDLGAPILVVSQFTLYADTVKGRRPSWNAAAPRAVAEPLVAAFAEALRALGAHVEAGVFGAHMQVELINDGPVTVMLEL | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
A0R080 | MRVLVQRVSRAQVTVDGEVVGAIDPQPQGLLALVGVTHDDDAAKAQRLAEKLWKLRILDDERSASDVAAPILVISQFTLYANTDKGRRPSWNAAAPGSVAEPLVTEFTEALRRLGATVETGVFGAHMEVELVNDGPVTVLLEL | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
A1TDH1 | MRVLVQRVASARVTVAGETVGEIRPQSQGLLALVGVTHDDDDAKAQRMAEKLWQLRILDDEKSAGDIGAPILVVSQFTLYGNTAKGRRPTWNAAAPGAVAEPLVDAFAAALGRLGADVQTGVFGADMRVELVNDGPVTVLLEL | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
B2A2F7 | MRAVVQRVSKSYVNVNGEKVGEINQGLNVLLGVEDGDGEDDIKYLVDKIVNLRIFEDDQGKMNLSVNDIGGELLVISQFTLLGDCRKGRRPNFMKAASPEIADELYQKFVEKVSKDYGLSLATGSFKEHMEVDILNDGPVTILLDSNKKF | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
B9L8Z4 | MKAVLQRVKHSSVSVEGKLINEINEGLNVLIGFEKDDNDEKLKKMAKKIVSLRIFGERFEKSVADIKGEILLIPNFTIPAITKKGTRPNFQNSMQPSTAKEFYDKMVKELNNYIPTKAGVFGAEMQVEITNNGPVTIILEV | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
Q9K143 | MRAVIQKTVGAKVDVVSEAGTETCGKIDGGFVVLLGVTHSDTEKDARYIADKIAHLRVFEDEAGKLNLSLKDVGGAVLLVSQFTLYADAASGRRPSFSQAAPAEQAQQLYLRTAELLRGHGIHVETGRFRTHMQVSLCNDGPVTILLDSFMTRISPKMKVVPD | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
A6Q128 | MVALIQRVKESWVKIDGTEIAKIGKGYNILLGVMKEDTTKDIEKLIKKIVKLRLFPNESGKMDKNILEVKGSVLVVSQFTLAGNAKKGNRPDFTAAMPPKEAKELYDHFCQKLSLHLPVQTGLFGAMMEVGIINDGPVTLILDSKKL | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
B7IDL6 | MRAVIQRVKNAKVEVEGKTVGKIENGLLVLLGVGKDDNKEDIKYLAEKIINLRIFDDENGKMNLSLLDINGELLIVSQFTLYGDCRKGRRPSYSESAPPDIAKKLYEEFVNACKNYNLKVETGEFGAHMQVSLVNDGPVTLLLDSKKVF | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
A6LML3 | MRAVVQRVNSANVDVNGKIIGKIKKGLLVLLGVGKNDTESDAEYLVNKILNLRIFDDNKGKMNLSLLDIKGDILIVSQFTLYGDCRRGRRPSYSDSASPEKAKKLYEYFVEKIRKEYNIKVETGEFGAYMKVNLENDGPVTLLLDSKKVF | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
B0K971 | MRAVVQRVSRGEVSVGGEMVSSIGKGFVVLVGISIDDNENDVMYMADKIVNLRVFEDEEGKMNLSLLDIGGEVLLVSQFTLLGDVRKGRRPNFMMAQKPQEALKYFNLLVKEIEKRGVSVKTGIFQAMMKVLIENDGPVTILIDSKKVF | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
B9L111 | MRVLLQRVSEASVTVDGTLVSSIGQGVLLLVGVRHGDDRATAEWLAHKVAHLRIFEDEAGKMNRSLLDVGGSALVVSQFTLYADVRKGRRPSFIEAAPPNEARPLVDTFAETLRALGVPVETGVFGAHMDVALVNDGPVTIWLDSAELRGGSLD | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
Q9FJ87 | MSQSNRVRDEVTLPLLQKTSHLKNHSSVLSVFLNEAISICKISYPLVLTGLFLYVRSFVSLSFLGGLGDATLAGGSLAAAFANITGYSLFSGLTMGVESICSQAFGARRYNYVCASVKRGIILLLVTSLPVTLLWMNMEKILLILKQDKKLASEAHIFLLYSVPDLVAQSFLHPLRVYLRTQSKTLPLSICTVIASFLHLPITFFLVSYLGLGIKGIALSGVVSNFNLVAFLFLYICFFEDKLSVNEDEKITEETCEDSVREWKKLLCLAIPSCISVCLEWWCYEIMILLCGFLLDPKASVASMGILIQITSLVYIFPHS... | Function: Functions as a multidrug and toxin extrusion transporter in the export of abscisic acid (ABA) in guard cells. Plays a role in ABA-mediated growth inhibition and responses to drought conditions . May act as a negative regulator of hypocotyl cell elongation in the light .
Location Topology: Multi-pass membrane ... |
Q9SZE2 | MCNPSTTTTTTGSENQESRTGLFLDLFSINSFEPTKRNLRHCENRGSPLMAEAVTEAKSLFTLAFPIAVTALVLYLRSAVSMFFLGQLGDLELAAGSLAIAFANITGYSVLSGLALGMEPLCSQAFGAHRFKLLSLTLHRTVVFLLVCCVPISVLWFNVGKISVYLHQDPDIAKLAQTYLIFSLPDLLTNTLLHPIRIYLRAQGIIHPVTLASLSGAVFHLPANLFLVSYLRLGLTGVAVASSITNIFVVAFLVCYVWASGLHAPTWTDPTRDCFRGWAPLLRLAGPSCVSVCLEWWWYEIMIVLCGLLVNPRSTVAAMG... | Function: Functions as a multidrug and toxin extrusion transporter that negatively regulates plant disease resistance . Plays an important role in maintaining normal plant architecture, possibly by regulating local auxin biosynthesis . May act as a negative regulator of hypocotyl cell elongation in the light .
Location... |
Q4PSF4 | METPNIISHTNLLSKIDLEKQNPAPIFPTITELKSEARSLFSLAFPTILAALILYARSAISMLFLGHIGELELAGGSLAIAFANITGYSVLAGLALGMDPLCSQAFGAGRPKLLSLTLQRTVLFLLTSSVVIVALWLNLGKIMIYLHQDPSISSLAQTYILCSIPDLLTNSFLHPLRIYLRAQGITSPLTLATLAGTIFHIPMNFFLVSYLGWGFMGVSMAAAASNLLVVIFLVAHVWIAGLHQPTWTRPSSECFKDWGPVVTLAIPSCIGVCLEWWWYEIMTVLCGLLIDPSTPVASMGILIQTTSLLYIFPSSLGLAV... | Function: May act as a negative regulator of hypocotyl cell elongation in the light.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54327
Sequence Length: 508
Subcellular Location: Late endosome membrane
|
Q9LE20 | MEDKIQSDDFTSHKNPTLPQVIEELKELWAMVLPITAMNCLVYVRAVVSVLFLGRLGSLELAGGALSIGFTNITGYSVMVGLASGLEPVCSQAYGSKNWDLLTLSLHRMVVILLMASLPISLLWINLGPIMLFMGQNPEITATAAEYCLYALPDLLTNTLLQPLRVYLRSQRVTKPMMWCTLAAVAFHVPLNYWLVMVKHWGVPGVAIASVVTNLIMVVLLVGYVWVSGMLQKRVSGDGDGGSTTMVAVVAQSSSVMELVGGLGPLMRVAVPSCLGICLEWWWYEIVIVMGGYLENPKLAVAATGILIQTTSLMYTVPMA... | Function: May function as a multidrug and toxin extrusion transporter in the export of IAA-conjugates from the cytoplasm into peroxisomes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54793
Sequence Length: 510
Subcellular Location: Peroxisome membrane
|
O49660 | MSETSKSESLDPEVSEGLCSKTLMQSIVHELKLQMRIGLPLVVMNLLWFGKMTTTSVFLGRQGELNLAGGSLGFSFANVTGFSVLYGISAAMEPICGQAFGAKNFKLLHKTLFMAVLLLLLISVPISFLWLNVHKILTGFGQREDISFIAKKYLLYLLPELPILSFLCPLKAYLSSQGVTLPIMFTTAAATSLHIPINIVLSKARGIEGVAMAVWITDFIVVILLTGYVIVVERMKENKWKQGGWLNQSAQDWLTLIKLSGPCCLTVCLEWWCYEILVLLTGRLPNPVQAVSILIIVFNFDYLLYAVMLSLGTCVATRVS... | Function: Could function as a HCO(3)(-) -sensing component in the CO(2) signaling pathway in guard cells. Acts as an upstream repressor of HT1. Plays a role in stomatal response to CO(2).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53702
Sequence Length: 491
Subcellular Location: Cell membrane
|
E9FCP5 | MLRIPGKSLGYHEDISLTPWQAILASVIVLLGLKVATILYTAFYNVFLHPLRRFPGPVTWIAAPWMKSISHIRGQQDHQIVKLHQKLGHIIRVGPDTLSFTEMSAWRDIYGTGHAELPKHIYKGSGMEERPNIITAHSRDHHRFRKAMTPALTPEAITHEEALIKGYVDMLIEHLHKFAKSSDPYVNVSQWYTMTTFDIFGDLCYGESFNSLATGKQHLWLKSMSSMKVLVPLLVFPYISWLLVWWLLSPEQQRSLSDHQKRSYELTMKRIANRDTHPRHDFMTFMLRNRGEDQGVTDHELASNSDIVISAGSETTSTAL... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of destruxins, insecticidal cyclic hexadepsipeptides which induce flaccid paralysis and visceral muscle contraction in insects through targeting the calcium channels and vacuolar-type ATPases . The aldo-keto reductase dtxS3... |
Q7XT07 | MAATAAAAAAAPPADPPDSSPAASSPPRPSPEELVARAVAPVKPAFLRPPLSATPPKDEGKANGGGAVVAEKKSKRQLKRERKQEQKSSSHLCIEVGKSGNVSSCKYGDSCRFSHDIDAYLAQKPADLEGTCPFTNLDQLCPYGLTCRFLGTHKDIHAASGNLSEKHEINALNKDIQKLLWKNKYKFPKASAQIKLLGLKEVIKSKPDAANDDKKVNHDNLDGNDDENKEPLCNPPVNAECDSTLCEELDRSEGEPLIDNSIPCVEPRPTKKSKVESDEIDKHGAGTLNTNTESEDPNLSNGLEPSNNSSSCRTDLITTP... | Function: Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U47 in cytoplasmic tRNAs (By similarity). Catalyzes the synthesis of dihydrouridine in some mRNAs, thereby affecting their translation (By similarity).
Catalytic Activity: 5,6-dihydrouridine(47)... |
Q28BT8 | MAESDGSNNENGNLDTVTQKLDRGVAAIKPQYLTTKEKFHVFIDADGKEVVDKQTCSELSGNDAENTVRAEDAAEPEAKRIKLDDGTGEGQDKPPTSAENKQEKKRARGQNKSRPHMKHSQFEENKLCPSVTQECASKCFFGDKCKFLHDVAKYVSEKPEDIRPNCYLYETFGKCIYGVTCRFAKSHLGDNFKNLINEELMKQWEGQVLVKNSLDKSLKEQLRKRKVVFEKTDKYLKLCNKSGDSLKIKSPVVKEDNAAQVVQKDSPVTTVGAVTDEDLVKLRPCEKKTIDFRNKLYLAPLTTCGNLPFRRLCKRFGADI... | Function: Catalyzes the synthesis of dihydrouridine, a modified base, in various RNAs, such as tRNAs, mRNAs and some long non-coding RNAs (lncRNAs). Mainly modifies the uridine in position 47 (U47) in the D-loop of most cytoplasmic tRNAs. Also able to mediate the formation of dihydrouridine in some mRNAs, thereby regul... |
Q5ALL3 | MITPEKRTLDEPEVGSESKKPNNSTHVKGVAAIKAEYLVPTSSLTVVEYDDDEAEGGDREGESKPRNKKKQKGQNHKRDLKQKKDIIKLCPSLIDPEDDRICQVGADKCRFHHDIASYLESKPQDIDGICPVFEALGYCPTGIKCRWLKSHYNPETSKLIKDGDKMETAKTTNYEVNHIDKDQKMEMQKKKYFFKISQPVIKYLDSRIQNEANLAKQKEERKDNEASYVEAPFTIAEKKKLYLRNAKIVSPLTTVGNLPYRRLMKTLGADVTYSEMALSVPLIQGHNPEWALPKAHVSEYPGFGVQIASSKHWAAAKAAE... | Function: Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U47 in cytoplasmic tRNAs (By similarity). Catalyzes the synthesis of dihydrouridine in some mRNAs, thereby affecting their translation (By similarity).
Catalytic Activity: 5,6-dihydrouridine(47)... |
Q2HDP2 | MEPQDRTKRPQEEDNGVPIDGHNGSNSEPAAKKIKLDSPSSADSRAKGVAPIKAEYLLFPPGQKAKPTQSEAEADDNDDDAAEGRTAPTPQETQQAPQKDGKRKSQRGQNKEREFGTFSDAQRLCNTIAWTPEFSPRPCKHGDRCNALHDLRKYLKEGRRPDITTFGGKCPVWEKYGKCPSGWRCLFVHSHMDEIKHEDGRSELVLVGDASKAPEGGEEAAGEIKPGVVNMVPVGIKYDLSKKRIPLEKSEQYLAWLAKDTKHLAKHYQKHKDDETNPNDYRAQYVEPPFKPSEKRRLYFGRETPVLAPLTTQGNLPFRR... | Function: Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U47 in cytoplasmic tRNAs (By similarity). Catalyzes the synthesis of dihydrouridine in some mRNAs, thereby affecting their translation (By similarity).
Catalytic Activity: 5,6-dihydrouridine(47)... |
P0CN28 | MTDDPAATPRPETSVNARPAFSGQAPIKAEYLINTTPIVESASASELNNIHPDDAAEGRTDSRDSRDGRDRPDNKRRKPNKQDKKDKKGQNKGRHFPVIREASVRICRAWETTGICDRADKGDCRYAHSWEGYFEVKPNDISYRPDWSLVGEAPFVVEGERVVGGEDVVGKTLDLDTVCPVLKDLGYCPFGWRCRFLGAHVKRVAAAVDGEKEKEAGPEKRMGEWQVENWVQSEVENGWKQKETNWPEHEVLNALRRSTASFPFSEAYLKKVDPDKPFTLQNKKPTKQQPHKRKNNVLDEEEAANGPTGIPSAGDDEENA... | Function: Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U47 in cytoplasmic tRNAs (By similarity). Catalyzes the synthesis of dihydrouridine in some mRNAs, thereby affecting their translation (By similarity).
Catalytic Activity: 5,6-dihydrouridine(47)... |
P07239 | MDKKSLYKYLLLRSTGDMHKAKSPTIMTRVTNNVYLGNYKNAMDAPSSEVKFKYVLNLTMDKYTLPNSNINIIHIPLVDDTTTDISKYFDDVTAFLSKCDQRNEPVLVHCAAGVNRSGAMILAYLMSKNKESLPMLYFLYVYHSMRDLRGAFVENPSFKRQIIEKYVIDKN | Function: Serine/tyrosine phosphatase which down-regulates cellular antiviral response by dephosphorylating activated host STAT1 and blocking interferon (IFN)-stimulated innate immune responses. Dephosphorylates the OPG144 protein.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphat... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.