ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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P9WEX4 | MSQPAFKIIIVGCSVTGLTLAHCLDKLGVEYTILEKRSAVVLQEGASVAVMPNGGRILDQLGLYDAFEKATVPLDLTDAYLPDQDFRFTSDYPRRVLATFGYPVAFMERRGLLEILYDGIADKSKIHLNKGVTHVEQNDDGAKVHTEDGEVYEGDIVVGADGIHSKTLREMWRMMGEPVVNGIAQSESQNMSVAFSCVFGISHDVPELQPGEQILRMCNGSTIFVMGSKGVVFWFIVTQLNRRYEYHDAPRYTTEEAAAFCEARKDAEIKEGVTFECIWRKQHVFNMLPLQESLFQTWSHGRVVCIGDSVHKMTINLGQGANCAIEDVTVLCNMLRAFLAEKREKKPSYSEIDTLLRRFNKEHLPRASTIVETSRLTTRVHAQVGISQRIMTRWVVPYFGKFLQGKPLGLIASGPVLDFLPLKRASYPGWERYRVKKSSRGAGFWITAFLSLSLLAVAATMYGWGNSQIWADWNIL | 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 units and 2 methylations . The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpasD through the action of the prenyltransferase dpasC to yield a linear alpha-pyrone diterpenoid . Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpasE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpasB . The FAD-linked oxidoreductase dpasF is then involved in tetrahydrofuran (THF) ring formation at the C5 unit to complete the formation of subglutinols A and B . DpasF possesses also an additional catalytic ability of multi-step oxidations to generate a new DDP analog with an enone system at the C5 named FDDP A .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 53436
Sequence Length: 476
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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P9WEX5 | MNRLLASALLVGSAVVAPVSAACIKNATVTEVDVAIIGGGASGVYAAARLIDNNKTVVVLERNADRIGGQTETYYDPTTGTPVNVGVKVFSNTTVTTDFLKRFDFPMGTLNVGQTLATGTQYVDFATGKLIPNFTAVVPAVQAAAMQRYAAELAKYPQIKFGYNLGPQVPEDLVLPFGKFMEKHNLTGMAQTMFEFNSGYTPLLEIPALYILKYLDTYELQSLQSGSFIVAANGDSATLYRNAAKFLGERVVYGVSGMHIQRSSAAGGRVTISVGNSTTGTHMIRAKKLIVAAPPTLDNLRSTGLDLDTTEAGLFGKLSAGVFYSLVVKDTGVAKANLRNRHPANPYGFPDQPFIYSVIPLPKTSGLAQVLLGSASPLTASQVEARVAADIGRLPASLRGNATSVPKVVTMAAHTWNVMAPVADIKAGFYDKLEGLQGLKDTWYIGAAWATQSSTTIWEGLEQEFLPKLLAAL | 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 units and 2 methylations . The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpasD through the action of the prenyltransferase dpasC to yield a linear alpha-pyrone diterpenoid . Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpasE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpasB . The FAD-linked oxidoreductase dpasF is then involved in tetrahydrofuran (THF) ring formation at the C5 unit to complete the formation of subglutinols A and B . DpasF possesses also an additional catalytic ability of multi-step oxidations to generate a new DDP analog with an enone system at the C5 named FDDP A .
Sequence Mass (Da): 50300
Sequence Length: 473
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 1.1.1.-
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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 Mass (Da): 33038
Sequence Length: 292
Domain: The DIM domain (143-214) is necessary but not sufficient for heterodimerization.
Subcellular Location: Cytoplasm
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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 mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 29159
Sequence Length: 258
Subcellular Location: Cell membrane
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P24482 | MFGSGNVLPVKIQPPLLRPLAYRVLSRKYGLSIKSDGLSALAEFVGTNIGANWRQGPATIKFLEQFAAVWKQQERGLFIDQSGVKEVIQEMKEREKVEWSHEHPIQHEENILGRTDDDENNSDDEMPIAADSSLQNVSLSSPMRQPTERDEYKQPFKPESSKALDWRDYFKVINASQQQRFSYNPHKMQFIFVPNKKQNGLGGIAGFLPDIEDKVQMFLTRYYLTNDRVMRNENFQNSDMFNPLSSMVSLQNELSNTNRQQQSSSMSITPIKNLLGRDAQNFLLLGLLNKNFKGNWSLEDPSGSVEIDISQTIPTQGHYYVPGCMVLVEGIYYSVGNKFHVTSMTLPPGERREITLETIGNLDLLGIHGISNNNFIARLDKDLKIRLHLLEKELTDHKFVILGANLFLDDLKIMTALSKILQKLNDDPPTLLIWQGSFTSVPVFASMSSRNISSSTQFKNNFDALATLLSRFDNLTENTTMIFIPGPNDLWGSMVSLGASGTLPQDPIPSAFTKKINKVCKNVVWSSNPTRIAYLSQEIVIFRDDLSGRFKRHRLEFPFNESEDVYTENDNMMSKDTDIVPIDELVKEPDQLPQKVQETRKLVKTILDQGHLSPFLDSLRPISWDLDHTLTLCPIPSTMVLCDTTSAQFDLTYNGCKVINPGSFIHNRRARYMEYVPSSKKTIQEEIYI | 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' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair.
PTM: Phosphorylated in a cell cycle dependent manner during late G1 phase. Phosphorylation may facilitate the interaction with POL2 or the activity of DNA polymerase II. Phosphorylation is independent of DNA replication but dependent upon CDC28 in vivo. Both Ser-141 and Ser-613 are phosphorylated in vivo, but in vitro only Ser-141 is phosphorylated by CDC28.
Sequence Mass (Da): 78340
Sequence Length: 689
Subcellular Location: Cytoplasm
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Q9USQ7 | MKVLGLISGGKDSCFNLMHCVSLGHEVVALANLHPEDGKDEIDSFMYQSVGHDVIPLYAECFDLPLYREKIGGQSINQNLDYQFTEKDETEDLYRLIKRVLTNHPDLEAVSTGAILSTYQRTRVENVCKRLGLKSLSFLWQKDQEKLLNDMVVSGLNAILIKVAAIGLTRKDLGKSLAEMQDKLLTLNKKFELHPCGEGGEYETLVLDCPLFKKRIVLTDKEVVEHSSGEVCYLKVKACVKDKPEWQPISLKSELVPNEELLGEEYSHIYHTISKKYELIDDQEETPTSLIPIPLRESAFQQKKGSFLVLGNVVATKGSYNTFQGEAESAINNLNELLGTYGYSNKNVYFVTVILSSMSKFAEFNSVYNKYFDFTNPPSRSCVAAPLASEYRIVMSCIVGDVTEKRALHVQGQSYWAPANIGPYSQSICANGVVFISGQIGLIPSVMELKLHDKIFEMVLALQHANRVAKAMRVGSLIACLAYVCDSRDADCVVKIWSEYTKNTGESSPVLVALVDALPRNASVEWQLLYNDSSCDVPLLSSLVTNQTLFGSDTAWDVALLNQNGLRMESSFIHHEHPSAYAIVLNNAFPNSQLLHVRYTARDQNV | 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 + diphthine-[translation elongation factor 2] + NH4(+) = AMP + diphosphate + diphthamide-[translation elongation factor 2] + H(+)
Sequence Mass (Da): 67624
Sequence Length: 606
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.1.14
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Q12429 | MKFIALISGGKDSFYNIFHCLKNNHELIALGNIYPKESEEQELDSFMFQTVGHDLIDYYSKCIGVPLFRRSILRNTSNNVELNYTATQDDEIEELFELLRTVKDKIPDLEAVSVGAILSSYQRTRVENVCSRLGLVVLSYLWQRDQAELMGEMCLMSKDVNNVENDTNSGNKFDARIIKVAAIGLNEKHLGMSLPMMQPVLQKLNQLYQVHICGEGGEFETMVLDAPFFQHGYLELIDIVKCSDGEVHNARLKVKFQPRNLSKSFLLNQLDQLPVPSIFGNNWQDLTQNLPKQQAKTGEQRFENHMSNALPQTTINKTNDKLYISNLQSRKSETVEKQSEDIFTELADILHSNQIPRNHILSASLLIRDMSNFGKINKIYNEFLDLSKYGPLPPSRACVGSKCLPEDCHVQLSVVVDVKNTGKEKINKNKGGLHVQGRSYWAPCNIGPYSQSTWLNDDANQVSFISGQIGLVPQSMEILGTPLTDQIVLALQHFDTLCETIGAQEKLLMTCYISDESVLDSVIKTWAFYCSNMNHRSDLWMDKSDDVEKCLVLVKISELPRGAVAEFGGVTCKRLIVDDNDSDKKEREENDDVSTVFQKLNLNIEGFHNTTVSAFGYNRNFITGFVDSREELELILEKTPKSAQITLYYNPKEIITFHHHIGYYPVEKLFDYRGKEHRFGLHIRS | 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] + NH4(+) = AMP + diphosphate + diphthamide-[translation elongation factor 2] + H(+)
Sequence Mass (Da): 77941
Sequence Length: 685
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.1.14
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Q55C80 | MTEIIKNTKYLDYTSDSVEFYPFNNNIFVCGTYEIEKGDTEYKERRKGKLYLFEIEEEQQQKENDNNNENNNNNKLFKEIQNINFNSGILDMKWNNNKDRILGVVMSKGELNIYQYDEVEKKLELKSSTEISLSNDILSLSLDWNKSGDKLICSFSDGNIGLFKVTKDYSKVTEEKRWKAHDYEAWICAFNYHDESIVFSGGDDCKFKIWDLNQLLNHNDDDIGIPPTPKFTKRCDMGVTSIHCHPTIENLIAVGSYDECLRIWDLKSLKQPIITTDSLGGGIWRIKWHPFQKNKLVTACMGGGFHILSTDPENINDFSTLQIEQSYNGPHKSIAYGVDWSFNKNNFDKQFIGCCSFYDKCLSIWIP | 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 = diphthine-[translation elongation factor 2] + H(+) + methanol
Sequence Mass (Da): 42561
Sequence Length: 367
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
EC: 3.1.1.97
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Q9BTV6 | MMGCFALQTVDTELTADSVEWCPLQGCRHLLACGTYQLRRPEDRPAGPQNKGGMEVKEPQVRLGRLFLYSFNDNNSIHPLVEVQRKDTSAILDMKWCHIPVAGHALLGLADASGSIQLLRLVESEKSHVLEPLSSLALEEQCLALSLDWSTGKTGRAGDQPLKIISSDSTGQLHLLMVNETRPRLQKVASWQAHQFEAWIAAFNYWHPEIVYSGGDDGLLRGWDTRVPGKFLFTSKRHTMGVCSIQSSPHREHILATGSYDEHILLWDTRNMKQPLADTPVQGGVWRIKWHPFHHHLLLAACMHSGFKILNCQKAMEERQEATVLTSHTLPDSLVYGADWSWLLFRSLQRAPSWSFPSNLGTKTADLKGASELPTPCHECREDNDGEGHARPQSGMKPLTEGMRKNGTWLQATAATTRDCGVNPEEADSAFSLLATCSFYDHALHLWEWEGN | 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).
Catalytic Activity: diphthine methyl ester-[translation elongation factor 2] + H2O = diphthine-[translation elongation factor 2] + H(+) + methanol
Sequence Mass (Da): 50575
Sequence Length: 452
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
EC: 3.1.1.97
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O74865 | MSETGIIPKSTDYTDWPADVCKYSQVFEDVLVVGTYMLDESTKLRHGKLVLYDTKEDVLKRVFDMHCDAILDFKWSPHDASVLAVAHSTGHVSFYRHQFRAELMFLRGIKVADSSVLMLSLDFSDSGKELAVSMSNGSVLIIDIDSGVIKNKWKEHDYEAWTCHYSRQDNNLLYSGGDDAALVCYDQRIPNSCIWRDIQVHHSGVVSILSRAPFGPYIATGEYGDFMHTLDTRNIGKPLFSANLGGGVWRLEHMETTENYHKVLGILMHRGAQVLRISNDFSSIDASKRIFKEHESMCYGGDWRHTDGLLATCSFYDKRVCLWEDI | 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] + H2O = diphthine-[translation elongation factor 2] + H(+) + methanol
Sequence Mass (Da): 37040
Sequence Length: 326
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Subcellular Location: Cytoplasm
EC: 3.1.1.97
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P38332 | MDSIQESDVLNAVKTKLPPCCLRIFRNKIILVGTYDLDKSTGYRSGSLDVFTMDLKLLCSNNTYGAILDLKLSPFDDTLICTAHSTGNIMLWRIRCTDKDDFQSNELDIHAIANLQLFEKDVLIASCHFSPLDCKKLLVTNTAGEAATIDIRTLSVQFTASAIAQAYSKLDKIDYEVQGATEKVIHVESGQFLKPHELECWTAEFGSLQPFQDVVFTGGDDSRIMAHDLRSKEFIWSNNRIHDAGVVSIKCSQPNFRNNKPTSIITGSYDDNIRSLDLRMMGESIFPGANVPTVNKLACDLGGGVWRFVESPIDQEQSHHNGSDRLLVCCMYNGAKVVTMNDNSDEYFQIQHYLKKGHDSMCYGGDWSNSLIATCSFYDNSLQTWIV | 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 the recycling from endosomes of plasma membrane proteins like CAN1 and MUP1. Identified in a screen for mutants with decreased levels of rDNA transcription.
Catalytic Activity: diphthine methyl ester-[translation elongation factor 2] + H2O = diphthine-[translation elongation factor 2] + H(+) + methanol
Sequence Mass (Da): 43308
Sequence Length: 387
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Subcellular Location: Cytoplasm
EC: 3.1.1.97
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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 diphthamide biosynthesis (By similarity).
Catalytic Activity: 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 31451
Sequence Length: 294
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
EC: 2.1.1.98
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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 diphthamide biosynthesis.
Catalytic Activity: 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 28008
Sequence Length: 251
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
EC: 2.1.1.98
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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 diphthamide biosynthesis.
Catalytic Activity: 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 29432
Sequence Length: 266
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
EC: 2.1.1.98
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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 diphthamide biosynthesis.
Catalytic Activity: 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 3 S-adenosyl-L-methionine = diphthine-[translation elongation factor 2] + 3 H(+) + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 28332
Sequence Length: 257
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
EC: 2.1.1.98
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Q9ZHG4 | MIPWVISPYSFDGSVVRFEKLALLLKRKGLKSVILADRNFHAAVKFNTIMRKHGLIPVHGLWKDGRIFVARNREEFDSLVRYYNGETHEIEDIPVFQESELTPVRYLDASEKKASIFMRKIFGLDEDVQGFPEKCEDVADILNAEAYDLRVNHRFPTPPKNWNELLIKKAEPLGEEYISRLKRELEVIKRKGFTPYIYTVEKVVEIAKKMGIKVGPGRGSAVGSLVAYLCGITEVDPIKYDLLFERFLNEERQEPPDIDVDVEDRRRKDLIKELSKSFQVYQVSTFGNLTEKSLKNLINSVLPDASLEEKNEIYKTVYGLPHHPSVHAAGVVISENPLPLPTRTEEDIPITDYDMYDLQEIGVVKIDILGLKTLSFIKDFKKEIFDYSDEKTYHLISKGKTLGVFQLEGLQARKLCRRISPRNMDELSILLALNRPGPLRSGLDVMFSNSKNVPAFFRKMFPETRGVLIYQEQIMRLAMFAGLSGTEADILRRAIAKKEREKMEPLLEKMKKGLLEKGMENAEQILEILLNFSSYAFNKSHSVAYAHITYQTAYLKAHHLEEFFKLYFAYNSSDAGKIFLAVQELRNEGYRVHPPDINISGKDLVFHGKDVYLPLTVVKGVGVTLVEQIEKIRPVSSVRELQERVTGVPRNVVESLITAGAFDKLYENRKLALEELNKRVEKDILEIRSLFGEKVEQESSNIKIGDITELEEKSMGFPLTPVHEVPTGLFARIDDVFTYGRILPVLVKRVSRNIVTDGLSVCRVRTDVPDGVHLVLLSPLQKIIKIWPFNENTRFVYRVDFTATLEKAGQNEITEVLKNGAVVRYEGYRPLTDEYRYRVVPR | 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) = diphosphate + DNA(n+1)
Sequence Mass (Da): 96500
Sequence Length: 842
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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Q9PQ74 | MFINLNVHSHYSLLNSTLSIDDLIKYALDNKQPYVCLTDLNNMYGCIEFYDKAKAHNLTPIIGLEFEYQNATLVAYAKNYNGYLKLIKWSSWIMTSKEFEIQDDFDDLIIVCKKGTIVFKSPNFYQTHDQNAPNAIALQSVFYANKNDKIVFLAMLAIKNDLKLEDFKNCCDFDNNHFLNDNLAQSFFSPIALNNLNKVLNELKVQIHDLPINIPVYDKQNSIISSEILKQLCISGLKKRLNANDGQVNKIYVQRLKYELDVINEKQFDDYFLIVYDFINFAKSNGIIVGPGRGSAAGSLVAYCLHITDIDPIKHNLIFERFLNPTRKSMPDIDTDIMDEKRDLVIEYLFEKYGNDHVAYILTFQRLKAKMAIRDVGRILGIDLKVIDKICKNIKPEYDEDLDLAIKKNTILKEMYLLHKELFEISKKLINAPRQIGTHAAGIILSDSLISNIIPIQLGINDRPLSQYSMEYLERFGLIKMDLLGLKNLTIIDNVLKMIYENQNKKIDLFNINYNDKFVFEDLAKARTNGIFQLESPGMKKVLLKVKPQNIEDISIVSALFRPGPQQNIKTFVERRFKREEFSYWNEATRKILEPTYGIIVYQEQVIELVKTIANFDIATSDNFRRAISKKDEKILIQLKDDFINGALNNNYKQPLVNQIFEYIFSFAHYGFNHSHSLAYSYISYWLAYLKHYYTLEFLSVLLSHTSASKDKLLSYLNEAKEFNISIKGPDIQYFSNDFVIDTQKQIIRFGFKTIKGFGDELLKKIKSALQKSTLSDYISYIDALKKGNVSLKNIEILIRVGTFDSFGINRLFLLNNLNEIFEKTGLNGHFFDLNLVGLDYAKDMSVNDRYLDDEIQYLGIDLNSLNYANYKTEIDYNKLKYTIKDFYEINTNYETNILAQVLNIKQSKTKNGNDIFYLETLIDNKKQTLTIFQNSKYLIDEISIGGIYVFGVKLLNHFNFIVNIKQRI | 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) = diphosphate + DNA(n+1)
Sequence Mass (Da): 112344
Sequence Length: 969
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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Q92QM8 | MIDSAAPPSGFCRDCLKEQAAHSRRCLACGSPRLLRHSELYRLTLAHIDCDAFYASVEKRDNPELADKPVIIGGGKRGVVSTACYIARIHGVRSAMPMFKALEACPQAVVIKPDMEKYVRVGREVRAMMQELTPLVQPLSIDEAFLDLSGTERLHHDPPARTLARFAKRVEQEIGITVSVGLSYCKFLAKVASDLQKPRGFSVIGQAEAADFLKAKPVTLIWGVGKAFAATLERDGIRAIGQLQTMEEADLMRRYGTMGRRLYRLSRGLDERSVEIDGEAKSVSSETTFNDDLARQEDLVAHLRGLSEQVAFRLRKSALAGQTVVLKLKTADFKTRTRNRRLESPTRLADRIFRTGLQLLEKEVDGTKYRLIGIGVSDLVDPDLADPPDLVDPQASRRAAAEDAINRLRDKFGKTSVETGYTFGKGRRGQ | 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' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 47656
Sequence Length: 430
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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Q8UJK7 | MRKIIHVDMDAFYASVEQRDNPELRGRPVAVGSAAARGVVAAASYEAREFGVRSAMPSVTAARRCPDLIFVPPRFDVYKAVSQQIRAIFAEYTRLIEPLSLDEAYLDVTENLKGMEIATEIASEIRERIKQITGLNASAGISYNKFLAKMASDLNKPNGQAVITPKNGPAFVEQLAVKKFHGVGPATAEKMHRFGIETGADLKSKSLQFLAEHFGKSGAYFYGIARGIDERQVRPDRIRKSVGAEDTFSVDINDLDLATAELRPLAEKVWHHCEAQRVSGKTVTVKVKYSDFTQATRSRTSALPVNGIQEILEAASALLATVYPFRRSVRLLGVTLSSLTNDQEAEDEEQPQLDLAL | 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' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 39301
Sequence Length: 357
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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P54560 | MMKEKVIFLVDMQSFYASVEKAENPHLKNRPVIVSGDPEKRGGVVLAACPLAKQKGVVNASRLWEAQEKCPEAVVLRPRMQRYIDVSLQITAILEEYTDLVEPYSIDEQFMDITGSQKLFGTPMEIAKSIQGRIMREIGVYARVGIGPNKALAKIACDNFAKKNKNGIFTLTKENMKTEMWPLPVGSMFGVGSRMKHHLNRMGISTIGGLAAFPLDLLKKKWGINGHVLWMTANGIDYSPVSTSSLDGQKAIGHGMTLPRDYEHFDKEIKVVLLELSEEVCRRSRNAGVMGQTVSVSCRGADFDWPTGFNRQVKLAEPTNSTQDVYEAVRRLFLTFWDGKPVRRLGVNLSQLSSDDIWQLNLFQDYAKKMSLGYVMDGIKNRFGDTAIIRAASLTAAGQAFERAAKIGGHYK | 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' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 45944
Sequence Length: 412
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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Q8PT42 | MMPASNPKKNSSERRIVFHVDMDSFFASVEVRERPELKNLPVIVGSDPKGGSGRGVVSTCSYEARKYGIHSAMPISQAYRFCPDAVFLPVNMKLYAGVSAGVMEILRGFAEKFQQVSVDEAYLIPGSGVRNFEEAALYALRIKDEVQRQQKITCSVGVGPNKLVSKIASGFQKPDGLTVVRPEDVRDFLFPLPVSRIPGVGEKTEETLKKMGINRVEELANCDVQMLSEKLGKMGFRLKQLANGLDFEELVEKESVKSISRHGTFAEDTDDPVKVSGSLDLLIESVHGSLMKHSFLFKTITLTVRFEDFSTYTRSRTLSIWTSDVFVIKRTAMQLLSEFTGRRKFRLVGVGVTKLRERDERQTLITDFP | 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' exonuclease (proofreading) activity. May be involved in translesional synthesis (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 41305
Sequence Length: 369
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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P63988 | MPTAAPRWILHVDLDQFLASVELLRHPELAGLPVIVGGNGDPTEPRKVVTCASYEARAYGVRAGMPLRTAARRCPEATFLPSNPAAYNAASEEVVALLRDLGYPVEVWGWDEAYLAVAPGTPDDPIEVAEEIRKVILSQTGLSCSIGISDNKQRAKIATGLAKPAGIYQLTDANWMAIMGDRTVEALWGVGPKTTKRLAKLGINTVYQLAHTDSGLLMSTFGPRTALWLLLAKGGGDTEVSAQAWVPRSRSHAVTFPRDLTCRSEMESAVTELAQRTLNEVVASSRTVTRVAVTVRTATFYTRTKIRKLQAPSTDPDVITAAARHVLDLFELDRPVRLLGVRLELA | 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' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 37562
Sequence Length: 346
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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Q98JM5 | METTATILHADLDAFYASVEQLLDPSLRGKPIAVGGGVVLAASYEARAFGVRGGMPGRKARELCPQLIFVGGNFSHYQRLGDAAIKVLDDFTPVVERISIDEAFADVAGCTHLFGQPRDIATAIRHRVRAELGLPISIGVARTKHLAKIASQVAKPDGLVVVDPGTELDFLHDLPVSLMWGVGPATKSRLAEIGIQTIGELARTHSGALTRLLGPAAGEKLAALAWNRDPRKLETRRRAHSAGAQSALGQKPAVARVIVPTLLHLADRVASRLRAKARPGRTVTVRVRFADLSAVTRSITLDQPISATTMLAEIAGDLVRGVLADHPREKTISLLAISVSHLEESAELQLDLPLGLADEKRRPGSKKGLARFGADRAIDKIRERFGKQAVGYGTVALEAARSVPDEFRELAEKEL | 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' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 44508
Sequence Length: 415
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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A3DH61 | MKRVILHCDLNNFYASVECLYHPELRDKPVAVCGSIEDRHGIVLAKNYAAKKYKVKTGETVWEAKNKCPGLVVVKANHSLYYKFSKYARQIYEYYTDRVESFGLDECWLDVSESTLLFGDGTKIANEIRERIKRELGVTVSVGVSYNKVFAKLGSDMKKPDAVTVITENDFKEKIWGLPVEALLYVGDSTKKKLNNMAVFTIGDLANCHSEFLVRQLGKWGYTLWSFANGYDTSPVAKNDCEIPIKSIGNSLTAPRDLTNNEDVRILIYVLSESVGERLRSHNLKGRTVQISIKDPELQTLERQAGLDIHTSITSEIAQKAYEIFLKSWNWSKNVRALGVRVTDLVESDTCTQISLFSDDIKRQKLEILDECVDRVRERFGYYSVRRGILLQDRGLNRI | 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' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 45491
Sequence Length: 399
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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Q6FFG4 | MRKIIHIDMDAFYASVELRERPELKTLPVVISSHHPRAVIAAASYPARVYGLRSAMPMGQARKLCPDLIIIEPNFDKYRAVSHQIHQIFQQHTHIIEPLSLDEAYLDVTENLNNLPSATDVAIQIRQQIWEQTSLTASAGVAPNKFLAKIASDWNKPNGLCVIKPHQVMQFIQNLPLKKIPGVGRVTQDKLQQLKLETLGDLQHIEEAVLIQHFGKYGKQLYLYAQGIDHRSVQAERVRQQISKETTFDQDLYLHECSSYWLMLAEKVWQSLQNKNLQARGVNIKLKNKHFQVFQHSKSFKRALQSLDEFKSVLALLLQEISLTLDDQYRLIGVGLYQLSPSASESQLTLW | 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' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 40192
Sequence Length: 351
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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A3N148 | MATQRKIIHIDMDCFYAAIEMRENPALIGKPVAVGGSVEGRGVLTTCNYEARKFGLHSAMPTAQALKRCPNLILVPVNMPLYKAVSEQIHQIFRRYTDIVELLSLDEAYLDVTDCRQCSGSATWIAQEIRDAIWNELHLTASAGIAPLKFLAKIASDQNKPNGQFVISPENMTAFIYDLPLKKIPRVGKVTNEKLAQLGLHTCGDIQHSDKAFIYKTFGKFGQRLWEFSHAIDNRKIEANRPRKSLAVENTLPTDIWHLAEAEQIVDELFKKLVFRLQRNWGERSLQEFKKLAIKLKFGDFTQTTLERTTDGLSRERFIELLQQVWQRTNRRSVRLIGLSVHYPTEKVKKQLNLWE | 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' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 40808
Sequence Length: 356
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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B2UKN1 | MNQRKIIHVDMDAFYASIEQRDHPEYRGKPIAVGRPEMRGVVAAASYEARRFGVRSAMPSMKALKLCPHLIFTRNRMDVYKAVSAQIHAIFHRYTDLVEPLSLDEAFLDVTENKPGIPLAVDIARRIKKEIRRELHLTASAGVSYNKFLAKIASDYRKPDGLFTIHPSRAEKFIAALPIEAFWGVGHATAERMRALSITNGAQLRARDKDFLVRHFGKTGAIFYNFARGVDDRPVEPSRMRKSVGCEETYRENVTRAEALEQRLPLLAEELAGRLARSGFRGNTLTLKVKFPDFVQKTRCATVPEILTEKEGILPLARTLMEELDSGDRTFRLLGLSVSHPQEEQRQGIWEQLWLELEY | 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' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 40891
Sequence Length: 359
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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Q0A4X2 | MSQRKIIHVDMDAFYASVEQRDRPGLRGRPVVVGGDPNGRGVVAAASYEARRHGIHSAMPAWRAARLCPDAVFLRPRFDVYRSISAQIQALFREYTPLVEPLSLDEAYLDVSDCPRRGGSATLIAREIRARIHEQTGLTASAGVSCNKFLAKIASDLDKPDGLHVIPPEQAEAFVAALPVGKIHGVGQATRQRMERMGVRTGADLRRLTLLELQRAFGSRARFYYELARGRDERPVRPRRERKSVGAETTFGEDLNNPAEMLERMAPLADKVAASLHRRGLAGRTVTLKVKYHDFRQITRSLSGRPVQSADEIRARLPALLQDTEAGDRPVRLLGVTVSGLVTVTPDQARQLALF | 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' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 39313
Sequence Length: 355
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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A8MGJ5 | MNPVIFLVDMNAFFISCEMTRNSKLIGIPAAVAGNPQNRTGIVLAANYEARRFGVKTAMTLNNALKLCPTMTVVPPDHRFYRQKSSEVMNLLSKYTPIIEQSSIDEAWLDMTGTENLFGKPADAAKLIMEDIKENLGLWCSIGISEGKFLSKMASDMKKPLGITELWKRDIQTKLWPLSIKSMHGVGAKTYEKLHSLGIETIGDFANLKKDDAHQILGKFGLDLYHHAHGIDTTPVQVISPDDMKSIGRSTTLPEDLVDIEQLKYILLTLCEDIGRSARKHNKRGRTVNLTLKSSDFKVIHRQVTIKATFNTMEIYEAGYHLLKLHLNPKIPIRLIGVSISGFEDTSVPEQISIFNMDEFNKRDTIGNNRNEKIDMVMDSIRNKYGSDKISRASLIIK | 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' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 44741
Sequence Length: 398
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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Q8CNP3 | MTERRIIHIDMDYFFAQVEMRDNPKLKGKPVIVGGKASHRGVVSTASYEARAYGVHSAMPMTQAHKLCPNGYYVTSRFDTYREVSGQIMKIFRSYTELVEPMSLDEAYLDITHLVRPDLPASTIANYIRRDIYEVTRLTASAGVSYNKFLAKLASGMNKPNGLTVIDYNNVHEILMQLDIGDFPGVGKASKKKMHQHHIYTGQDLYNKDEFELIRLFGKRGRGLYNKARGIDHNEVKASRVRKSVGTERTFSTDVNDDDVILRKIRELSGKTAERLNKIQKSGKTVTVKIKTYQYETISKQKSLRDPIRTETDIYNIAYTLYNDLKDPEIPIRLIGVTVGSLEQSDFKNLTIYDFI | 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' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 40669
Sequence Length: 356
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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Q9AK82 | MRTAPTILHLDMDAFFASVEQASKPSLRGKAVVVGGLGPRGVVATCSYEARVFGVHSAMPMGQARRLAPHAAYLVPRFELYRSISEQVMRLLRELSPLVEPLSLDEAFVDLDAGGAARDAETARLAGTKLRTDIRTVTGLTGSVGLAASKMLAKIASEAAKPDGLVLIPPGTERAMLEPMTVRTLPGVGPATGDHLRRAGITTVGEIAEAGEDELVRLLGKAHGHALYAMALARDERPVVAERETKSVSVEDTYDVDIHDRVRVGVEVGRLADRCVRRLRASGLSGRTIVLKVRRYDFSTLTRSETLRGPTDDPAVVREAAARLLDSVDTTGGVRLLGVGVSGLADYTQEDLFAQAAGDRAEEPAEEPGTEPAEAHSPSPAERRWPSGHDVRHTELGHGWVQGSGLGRVTVRFETPYSGVGRVRTFLVDDPELTPADPLPLVADTEGGAGQPSSGPLPLPASLPKSWSGGGGAAATSRP | 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' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 50700
Sequence Length: 479
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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B2FLR2 | MTRLRKIIHVDMDAFYASVEQRDDPSLRGKPVVVAWRGARSVVCAASYEARVFGVRSAMPAVRAERLCPDAIFVPPDFARYKAVSQQVRAIFLRHTDLVEPLSLDEAYLDVSEPKSGIELATDIARTIRAQIREETNLTASAGIAPNKFLAKIASDWRKPDGQFVIPPQRVDAFLAPLPVNRVPGVGKVMEGKLAARGIVTCGDLRQWALIDLEEAFGSFGRSLYNRARGIDERPVEPDQQVQSISSEDTFAEDLLLEDLTEAIVQLAGKTWNATRKTERIGHTVVLKLKTAQFRILTRSFTPERPPESMEELRDIALALRARVDLPAETRYRLVGVGLGGFREKEAVVQGELFEQGPNDSPRS | 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' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 40489
Sequence Length: 364
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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Q99Y66 | MLIFPLINDTSRKIIHIDMDAFFAAVEERDNPALKGKPVVIGKDPRETGGRGVVSTCNYEARKYGIHSAMSSKEAYERCPKAIFISGNYEKYRTVGDQIRRIFKRYTDVVEPMSIDEAYLDVTDNKLGIKSAVKIAKLIQHDIWKEVGLTCSAGVSYNKFLAKLASDFEKPHGLTLVLKEDALCFLAKLPIEKFHGVGKKSVKKLHDMGIYTGQDLLAVPEMTLIDHFGRFGFDLYRKARGISNSPVKSDRIRKSIGSERTYAKLLYQETDIKAEISKNVKRVAALLQDHKKLGKTIVLKVRYADFTTLTKRVTLPELTRNAAQIEQVAGDIFDSLSENPAGIRLLGVTMTNLEDKVADISLDL | 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' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 40788
Sequence Length: 364
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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P06746 | MSKRKAPQETLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVSGIGPSAARKFVDEGIKTLEDLRKNEDKLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEVKKVDSEYIATVCGSFRRGAESSGDMDVLLTHPSFTSESTKQPKLLHQVVEQLQKVHFITDTLSKGETKFMGVCQLPSKNDEKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEKDIFDYIQWKYREPKDRSE | 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'-deoxyribose-phosphate from the preincised AP site acting as a 5'-deoxyribose-phosphate lyase (5'-dRP lyase); through its DNA polymerase activity, it adds one nucleotide to the 3' end of the arising single-nucleotide gap . Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. It is also able to cleave sugar-phosphate bonds 3' to an intact AP site, acting as an AP lyase .
PTM: Methylation by PRMT6 stimulates the polymerase activity by enhancing DNA binding and processivity.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 38178
Sequence Length: 335
Domain: Residues 239-252 form a flexible loop which appears to affect the polymerase fidelity.
Subcellular Location: Nucleus
EC: 2.7.7.7
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Q8K409 | MSKRKAPQETLNGGITDMLVELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVTGIGPSAARKFVDEGIKTLEDLRKNEDKLNHHQRIGLKYFEDFEKRIPREEMLQMQDIVLNEIKKVDSEYIATVCGSFRRGAESSGDMDVLLTHPNFTSESSKQPKLLHRVVEQLQKVHFITDTLSKGETKFMGVCQLPSEKDGKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEQDIFDYIQWRYREPKDRSE | 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'-deoxyribose-phosphate from the preincised AP site acting as a 5'-deoxyribose-phosphate lyase (5'-dRP lyase); through its DNA polymerase activity, it adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. It is also able to cleave sugar-phosphate bonds 3' to an intact AP site, acting as an AP lyase.
PTM: Methylation by PRMT6 stimulates the polymerase activity by enhancing DNA binding and processivity.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 38288
Sequence Length: 335
Domain: Residues 239-252 form a flexible loop which appears to affect the polymerase fidelity.
Subcellular Location: Nucleus
EC: 2.7.7.7
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O57383 | MSKRKAPQESPNEGITDFLVELANYERNVNRAIHKYNAYRKAASVIAKYPTKIKSGTEAKKLDGVGAKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVTGIGPAAARKFFDEGIKTLDDLRNNEHKLNHHQKIGLKHFDDFEKRIPRKEMLQMQEIILDKVNNLDPEYIATVCGSFRRGAESSGDMDILLTHPDFTSESAKQPRLLHQVVQCLEDCNFITDTLVKGDTKFMGVCQLPCESDQDYPYRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRTHALEKGFTLNEYTLRPLGVTGIAGEPLPIDSEKDIFDYIQWKYREPKDRSE | 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'-deoxyribose-phosphate from the preincised AP site acting as a 5'-deoxyribose-phosphate lyase (5'-dRP lyase); through its DNA polymerase activity, it adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. It is also able to cleave sugar-phosphate bonds 3' to an intact AP site, acting as an AP lyase.
PTM: Methylation by PRMT6 stimulates the polymerase activity by enhancing DNA binding and processivity.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 38294
Sequence Length: 334
Subcellular Location: Nucleus
EC: 2.7.7.7
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Q9FNY4 | MAAKRGRNRSPSPDPEGMFAGMVVFMVEIGVQRRRLQIWKQKLVQMGAVIEEDRVTKKVTHVLAMNLEALLHKFGKERLSHFTARLMLYQWLEDSLTSGEKANEDLYVLKIDSEEVDKPKKSLPAISGSEDQSSPQKRTRYSPDAGDFKGVESHSNTQGSPDSPTSCSVPSTSASPGEGIAETPTSPQSESTSVYKPPDLNRNITEIFGKLINIYRALGEDRRSFSYYKAIPVIEKFPTRIESVDQLKHLPGIGKAMRDHIQEIVTTGKLSKLEHFETDEKVRTISLFGEVWGVGPATALKLYEKGHRTLEDLKNEDSLTHAQKLGLKYFDDIKTRIPRQEVQEMEQLLQRVGEETLPGVNIVCGGSYRRGKATCGDLDIVVTHPDGQSHKGFLTKFVKRLKEMNFLREDLIFSTHSEEGTDSGVDTYFGLCTYPGQELRRRIDFKVYPRDIYSFGLIAWTGNDVLNRRLRLLAESKGYRLDDTGLFPATHSSSGNRGARGTASLKLSTEKQVFDFLGFPWLEPHERNL | 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 transposon-induced DNA double strand breaks (DSBs) . Involved in repair of UV-B-mediated DNA damage during seedling development through an excision repair mechanism . Involved the repair of DSBs induced by high salinity and DNA cross-linking agent. Functions via the DNA non-homologous end joining (NHEJ) pathway.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 59588
Sequence Length: 529
Subcellular Location: Nucleus
EC: 2.7.7.7
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Q9UGP5 | MDPRGILKAFPKRQKIHADASSKVLAKIPRREEGEEAEEWLSSLRAHVVRTGIGRARAELFEKQIVQHGGQLCPAQGPGVTHIVVDEGMDYERALRLLRLPQLPPGAQLVKSAWLSLCLQERRLVDVAGFSIFIPSRYLDHPQPSKAEQDASIPPGTHEALLQTALSPPPPPTRPVSPPQKAKEAPNTQAQPISDDEASDGEETQVSAADLEALISGHYPTSLEGDCEPSPAPAVLDKWVCAQPSSQKATNHNLHITEKLEVLAKAYSVQGDKWRALGYAKAINALKSFHKPVTSYQEACSIPGIGKRMAEKIIEILESGHLRKLDHISESVPVLELFSNIWGAGTKTAQMWYQQGFRSLEDIRSQASLTTQQAIGLKHYSDFLERMPREEATEIEQTVQKAAQAFNSGLLCVACGSYRRGKATCGDVDVLITHPDGRSHRGIFSRLLDSLRQEGFLTDDLVSQEENGQQQKYLGVCRLPGPGRRHRRLDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKGMSLSEHALSTAVVRNTHGCKVGPGRVLPTPTEKDVFRLLGLPYREPAERDW | 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-dependent and template-independent (terminal transferase) DNA polymerase activities . Has also a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity .
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 63482
Sequence Length: 575
Subcellular Location: Nucleus
EC: 2.7.7.7
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Q9QXE2 | MDPQGIVKAFPKRKKSHADLSSKALAKIPKREVGEARGWLSSLRAHIMPAGIGRARAELFEKQIIHHGGQVCSAQAPGVTHIVVDEDMDYERALRLLRLPQLPPGAQLVKSTWLSLCLQEGRLTDTEGFSLPMPKRSLDEPQPSKSGQDASAPGTQRDLPRTTLSLSPPHTRAVSPPPTAEKPSRTQAQLSSEDETSDGEGPQVSSADLQALITGHYPTPPEEDGGPDPAPEALDKWVCAQPSSQKATNYNLHITEKLEVLAKAYSVQGDKWRALGYAKAINALKSFHKPVSSYQEACSIPGIGKRMAEKVMEILESGHLRKLDHISDSVPVLELFSNIWGAGTKTAQMWYHQGFRNLEDLQSLGSLTAQQAIGLKHYDDFLDRMPREEAAEIEQTVRISAQAFNPGLLCVACGSYRRGKMTCGDVDVLITHPDGRSHRGIFSCLLDSLRQQGFLTDDLVSQEENGQQQKYLGVCRLPGPGKRHRRLDIIVVPYCEFACALLYFTGSAHFNRSMRALAKTKGMSLSEHALSAAVVRNSQGVKVGPGQVLPTPTEKDVFKHLGLPYREPAERDW | 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-dependent and template-independent (terminal transferase) DNA polymerase activities. Has also a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 62943
Sequence Length: 573
Subcellular Location: Nucleus
EC: 2.7.7.7
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Q67VC8 | MAPKRKPPARAAAAKLDPDGMFRGVSAFVVPHAVQSRRLEVWKQRLAQMGGRVQEKLAAKGGGGAVTHVLAADAKALLRELDAAWLHRFRGSVVSFEWLEECLKSGERLPEHKFAINYEEEFKPKKEGGAAGSGVLQSAKRSKISSDGPENRKETAGGNRESRDAIAHPNEDSDVVKGPSTCTSSQSASGDSKETIASQNAFKAEEASSGESSTYAPPDLNRNITEIFGKLINIYRALGDDRRSFSYYKAIPVIEKLPFKIESADQVKDLPAIGKSLKDHINEIVNTGKLSKLEHFENDEKVRTVSLFGEVWGVGPATALKLYDKGHRTLDDLQKDDSLTSAQRIGLKFFDDIKQRIPRHEVSEMEKLLQEVGTDILPGVIIVCGGSYRRGKSSCGDMDIIITHPDGESHVGFLPKFVQRLKGINFLREDLIFSIHSIEGTDCGVDTYFGLCTYPGRELRHRIDLKVYPRNRHAFGLLAWTGNDVLNRRLRILADSKGYILDDTGLYLATPGSGGKRGGRSDAIINCDTEKDVFDTLGFPWLEPHERNL | 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'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 60628
Sequence Length: 549
Subcellular Location: Nucleus
EC: 2.7.7.7
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Q9NP87 | MLPKRRRARVGSPSGDAASSTPPSTRFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSWQERRMAAAPPGCTPPALLDISWLTESLGAGQPVPVECRHRLEVAGPRKGPLSPAWMPAYACQRPTPLTHHNTGLSEALEILAEAAGFEGSEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVCEEVERVRRSERYQTMKLFTQIFGVGVKTADRWYREGLRTLDDLREQPQKLTQQQKAGLQHHQDLSTPVLRSDVDALQQVVEEAVGQALPGATVTLTGGFRRGKLQGHDVDFLITHPKEGQEAGLLPRVMCRLQDQGLILYHQHQHSCCESPTRLAQQSHMDAFERSFCIFRLPQPPGAAVGGSTRPCPSWKAVRVDLVVAPVSQFPFALLGWTGSKLFQRELRRFSRKEKGLWLNSHGLFDPEQKTFFQAASEEDIFRHLGLEYLPPEQRNA | 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 (Da): 54816
Sequence Length: 494
Subcellular Location: Nucleus
EC: 2.7.7.7
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Q9JIW4 | MLPKRRRVRAGSPHSAVASSTPPSVVRFPDVAIYLAEPRMGRSRRAFLTRLARSKGFRVLDAYSSKVTHVVMEGTSAKEAICWQKNMDALPTGCPQPALLDISWFTESMAAGQPVPEEGRHHLEVAEPRKEPPVSASMPAYACQRPSPLTHHNTLLSEALETLAEAAGFEANEGRLLSFSRAASVLKSLPCPVASLSQLHGLPYFGEHSTRVIQELLEHGTCEEVKQVRCSERYQTMKLFTQVFGVGVKTANRWYQEGLRTLDELREQPQRLTQQQKAGLQYYQDLSTPVRRADAEALQQLIEAAVRQTLPGATVTLTGGFRRGKLQGHDVDFLITHPEEGQEVGLLPKVMSCLQSQGLVLYHQYHRSHLADSAHNLRQRSSTMDAFERSFCILGLPQPQQAALAGALPPCPTWKAVRVDLVVTPSSQFPFALLGWTGSQFFERELRRFSRQEKGLWLNSHGLFDPEQKRVFHATSEEDVFRLLGLKYLPPEQRNA | 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 (Da): 55490
Sequence Length: 496
Subcellular Location: Nucleus
EC: 2.7.7.7
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Q7Z5Q5 | MENYEALVGFDLCNTPLSSVAQKIMSAMHSGDLVDSKTWGKSTETMEVINKSSVKYSVQLEDRKTQSPEKKDLKSLRSQTSRGSAKLSPQSFSVRLTDQLSADQKQKSISSLTLSSCLIPQYNQEASVLQKKGHKRKHFLMENINNENKGSINLKRKHITYNNLSEKTSKQMALEEDTDDAEGYLNSGNSGALKKHFCDIRHLDDWAKSQLIEMLKQAAALVITVMYTDGSTQLGADQTPVSSVRGIVVLVKRQAEGGHGCPDAPACGPVLEGFVSDDPCIYIQIEHSAIWDQEQEAHQQFARNVLFQTMKCKCPVICFNAKDFVRIVLQFFGNDGSWKHVADFIGLDPRIAAWLIDPSDATPSFEDLVEKYCEKSITVKVNSTYGNSSRNIVNQNVRENLKTLYRLTMDLCSKLKDYGLWQLFRTLELPLIPILAVMESHAIQVNKEEMEKTSALLGARLKELEQEAHFVAGERFLITSNNQLREILFGKLKLHLLSQRNSLPRTGLQKYPSTSEAVLNALRDLHPLPKIILEYRQVHKIKSTFVDGLLACMKKGSISSTWNQTGTVTGRLSAKHPNIQGISKHPIQITTPKNFKGKEDKILTISPRAMFVSSKGHTFLAADFSQIELRILTHLSGDPELLKLFQESERDDVFSTLTSQWKDVPVEQVTHADREQTKKVVYAVVYGAGKERLAACLGVPIQEAAQFLESFLQKYKKIKDFARAAIAQCHQTGCVVSIMGRRRPLPRIHAHDQQLRAQAERQAVNFVVQGSAADLCKLAMIHVFTAVAASHTLTARLVAQIHDELLFEVEDPQIPECAALVRRTMESLEQVQALELQLQVPLKVSLSAGRSWGHLVPLQEAWGPPPGPCRTESPSNSLAAPGSPASTQPPPLHFSPSFCL | 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 glycol. Can perform efficient strand displacement past a nick or a gap and gives rise to an amount of product similar to that on non-damaged template. Has no exonuclease activity . Error-prone DNA polymerase that preferentially misincorporates dT regardless of template sequence . May play a role in TLS during interstrand cross-link (ICL) repair . May be involved in TLS when genomic replication is blocked by extremely large major groove DNA lesions. May function in the bypass of some DNA-protein and DNA-DNA cross-links. May have a role in cellular tolerance to DNA cross-linking agents . Involved in the repair of DNA cross-links and double-strand break (DSB) resistance. Participates in FANCD2-mediated repair. Forms a complex with HELQ helicase that participates in homologous recombination (HR) repair and is essential for cellular protection against DNA cross-links .
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 100307
Sequence Length: 900
Subcellular Location: Nucleus
EC: 2.7.7.7
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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-nucleotide base-excision repair process . Also catalyzes DNA polymerization with low nucleotide-insertion fidelity . Probably acts as a strategic DNA mutase, which gives rise to a rapid emergence of variants . Generates mismatched G-G pairs, in that case, the polymerase first binds the deoxynucleotide followed by mismatch formation . Together with the viral DNA ligase, fills the single nucleotide gaps generated by the AP endonuclease (Probable). Binds DNA with high affinity via the helix alphaE .
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 20314
Sequence Length: 174
Domain: Small DNA polymerase formed from only a palm and a C-terminal subdomain . Unlike other polymerases, binds DNA via the helix alphaE . The total DNA-binding site of pol X is composed of two DNA-binding subsites.
Subcellular Location: Virion
EC: 2.7.7.7
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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(+) + H2O2 = 2 Fe(3+) + 2 H2O
Sequence Mass (Da): 18049
Sequence Length: 156
Domain: 12 di-nuclear ferroxidase centers are located at the interfaces between subunits related by 2-fold symmetry axes.
Subcellular Location: Cytoplasm
EC: 1.16.-.-
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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-mediated cleavage. Binds DNA with no apparent sequence specificity without self-aggregation nor promotion of DNA condensation. Is unable to protect DNA from DNase-mediated cleavage (By similarity).
Catalytic Activity: 2 Fe(2+) + 2 H(+) + H2O2 = 2 Fe(3+) + 2 H2O
Sequence Mass (Da): 20270
Sequence Length: 183
Subcellular Location: Cytoplasm
EC: 1.16.-.-
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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: Cytoplasm
EC: 1.16.-.-
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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 the presence of hydrogen peroxide and stores it as a mineral core.
Catalytic Activity: 2 Fe(2+) + 2 H(+) + H2O2 = 2 Fe(3+) + 2 H2O
Sequence Mass (Da): 21770
Sequence Length: 188
Subcellular Location: Cytoplasm
EC: 1.16.-.-
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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 cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
Sequence Mass (Da): 27487
Sequence Length: 263
Domain: The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
Subcellular Location: Cytoplasm
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A8PS95 | MNNTAHSMSEKVLLVASLEAARYGQYQQAVKGLQAESGLLETHMIDRITDLAYAPPADYFDAVYMMLPSEGVEWAAALPKLRASMIPGAKLRVSVVNENDPSSFLSQVRAELTIAGFTDIQTYENASIESRRPASSSVAEKDSTASSGMGAVKLRRKPNENGGHQQKKALLWATQPETHMDTEAKLQEHARTVSPASRREDCTVDFSAPRTRRKRACKGCTCGLRELEEEDERNSNLVQLDPSEVGGTGGKRTEVTTTVKGPNGEEHTVRRIQVDTRGATSSCGSCFLGDAFRCSSCPYLGLPAFEPGQKVEIPANMDDDL | 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 complex CFD1-NBP35. Electrons are transferred to DRE2 from NADPH via the FAD- and FMN-containing protein TAH18. TAH18-DRE2 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit RNR2.
Sequence Mass (Da): 34958
Sequence Length: 321
Domain: The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
Subcellular Location: Cytoplasm
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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 cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
Sequence Mass (Da): 28305
Sequence Length: 265
Domain: The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
Subcellular Location: Cytoplasm
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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 cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
Sequence Mass (Da): 29474
Sequence Length: 282
Domain: The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
Subcellular Location: Cytoplasm
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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 cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
Sequence Mass (Da): 29931
Sequence Length: 282
Domain: The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
Subcellular Location: Cytoplasm
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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 cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
Sequence Mass (Da): 26725
Sequence Length: 257
Domain: The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
Subcellular Location: Cytoplasm
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C1G2L9 | MPPSQTPAQGSGRFLLLSPPSLSSHPEKLNAILGLHARESTDLQMLDRLALGLVSLPESTYDVVLLLTGADNTLAETYRLVSRGVLQGVVNSLKPGGKLRNRDNQIWGSGSDSAAGLGSSDGDGGGGEKMSSSEQAFRNEAILAGLVFDDRGELAKPDFGAQQAVPLKLGRKKNLGESAFGNGAVELPASNGVRVTTGATSSTTTTTTTTAAAAAATAATPTTTTTTTINSSTPSGVGFIDFSDDFGVPMVEETQDSDEELIDEEELLGEYDMGRHIVQPPECRPKAGKRRRACKDCTCGLSQKLEAEDRAKRANADKALETLKLRTNDLAEVDFTVQGKVGSCGNCALGDAFRCDGCPYIGLPAFKPGEEVRLLNNDVQL | 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 complex CFD1-NBP35. Electrons are transferred to DRE2 from NADPH via the FAD- and FMN-containing protein TAH18. TAH18-DRE2 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit RNR2.
Sequence Mass (Da): 40037
Sequence Length: 381
Domain: The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
Subcellular Location: Cytoplasm
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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 complex CFD1-NBP35. Electrons are transferred to DRE2 from NADPH via the FAD- and FMN-containing protein TAH18. TAH18-DRE2 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit RNR2.
Sequence Mass (Da): 32596
Sequence Length: 305
Domain: The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
Subcellular Location: Cytoplasm
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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 cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
Sequence Mass (Da): 32481
Sequence Length: 306
Domain: The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
Subcellular Location: Cytoplasm
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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 cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
Sequence Mass (Da): 29487
Sequence Length: 277
Domain: The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
Subcellular Location: Cytoplasm
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Q9S0S3 | MMSQQDLPTLFYSGKSNSAVPIISESELQTITAEPWLEISKKGLQLEGLNFDRQGQLFLLDVFEGNIFKINPETKEIKRPFVSHKANPAAIKIHKDGRLFVCYLGDFKSTGGIFAATENGDNLQDIIEDLSTAYCIDDMVFDSKGGFYFTDFRGYSTNPLGGVYYVSPDFRTVTPIIQNISVANGIALSTDEKVLWVTETTAKRLHRIALEDDGVTIQPFGATIPYYFTGHEGPDSCCIDSDDNLYVAMYGQGRVLVFNKRGYPIGQILIPGRDEGHMLRSTHPQFIPGTNQLIICSNDIEMGGGSMLYTVNGFAKGHQSFQFQ | 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: 3.1.1.-
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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
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A8E5C5 | MAVPSVMVLPLLIVVFAGVYYVYNEVMRFMSKSVVRNKVVVITDAVSGMGSECARLFHAGGARLVLCGPSWDKLESLYDSLCSGSDPSQTFTPKLVLLDFSDMENISDVVSEICECYGCVDVLICNSSMKVKAPVQNLSLEMDKTIMDVNYFGPITLAKGVLPLMITRRTGQFVLVNSIQGKLALPFRTCYAASKHAVQAFFDCLRAEVEEFGISVSTISHTFINAGAENATPTEATPITATPTKATPTNPIWAYVCSKLNTHGVSPQILAQEIVRSVNRQSREVFLAHPVPTVALYIRALMPGCFFSVVSAGVRDGAMAEQLK | Function: Putative oxidoreductase.
Sequence Mass (Da): 35182
Sequence Length: 324
Subcellular Location: Secreted
EC: 1.1.-.-
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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
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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
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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
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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
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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
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P38844 | MKFNFSTIFNILFFLFTLIEANSNGETVKLITSDGIVYSYAVYTKTLAPARVVVKTISYTTTRVYPITLANSVVSSTTEKITEVSTVSASEQVSATQTNSLVSTSTVSTISPTISSGSSTSSSSTYDIESSQSIESSGTSSATAEPSASSGFRLTSSSAFVSSTAPFSSQLSSSSSSETSSSSFSTSSSSAPLSLTSSSSSSSSFATIITLAPSSSKSGNSQLTLASSSSTSAVESSQTGSTIARTTSTLVPSSSVDTTSRATTSMPLESSSTQSISVSSSDGTCYVFYDDDDYYSTVYLTNPSQSVDAATTITSTNTIYATVTI | 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
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O49523 | MKRKKKEEEEEKLIVTREFAKRWRDLSGQNHWKGMLQPLDQDLREYIIHYGEMAQAGYDTFNINTESQFAGASIYSRKDFFAKVGLEIAHPYTKYKVTKFIYATSDIHVPESFLLFPISREGWSKESNWMGYVAVTDDQGTALLGRRDIVVSWRGSVQPLEWVEDFEFGLVNAIKIFGERNDQVQIHQGWYSIYMSQDERSPFTKTNARDQVLREVGRLLEKYKDEEVSITICGHSLGAALATLSATDIVANGYNRPKSRPDKSCPVTAFVFASPRVGDSDFRKLFSGLEDIRVLRTRNLPDVIPIYPPIGYSEVGDEFPIDTRKSPYMKSPGNLATFHCLEGYLHGVAGTQGTNKADLFRLDVERAIGLVNKSVDGLKDECMVPGKWRVLKNKGMAQQDDGSWELVDHEIDDNEDLDF | 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), monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG), triacylglycerol (TAG) and 2-monoacylglycerol (2-MAG). May be involved in the negative regulation of seedling establishment by inhibiting the breakdown, beta-oxidation and mobilization of seed storage oils.
Sequence Mass (Da): 47792
Sequence Length: 419
Subcellular Location: Cytoplasm
EC: 3.1.1.-
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P0C2H4 | MRTHTRGAPSVFFICLFCFVSACVTDENPEVMIPFTNANYDSHPMLYFSRAEVAELQLRAASSHEHIAARLTEAVNTMLSSPLEYLPPWDPKEYSARWNEIYGNNLGALAMFCVLYPENMEARDMAKDYMERMAAQPSWLVKDAPWDEVPLAHSLVGFATAYDFLYNYLSKTQQEKFLEVIANASGYMYETSYRRGWGFQYLHNHQPTNCMALLTGSLVLMNQGYLQEAYLWTKQVLTIMEKSLVLLREVTDGSLYEGVAYGSYTTRSLFQYMFLVQRHFDINHFGHPWLKQHFAFMYRTILPGFQRTVAIADSNYNWFYGPESQLVFLDKFVMRNGSGNWLADQIRRNRVVEGPGTPSKGQRWCTLHTEFLWYDASLKSVPPPDFGTPTLHYFEDWGVVTYGSALPAEINRSFLSFKSGKLGGRAIYDIVHRNKYKDWIKGWRNFNAGHEHPDQNSFTFAPNGVPFITEALYGPKYTFFNNVLMFSPAASKSCFSPWEGQVTEDCSSKWSKYKHDPAASCQGRVVAAVEKNGVVFIRGEGVGAYNPQLHLRNVQRNLILLHPQLLLLVDQIHLGEDSPLERAASFFHNVDFPFEETVVDGVHGALIRQRDGLYKMYWMDDTGYSEKGTFASVTYPRGYPYNGTNYVNVTTHLRSPVTRAAYLFIGPSIDVQSFSIHGDAQQLDVFVATSEHAYATYLWTGETAGQSAFAQVIADRQKILFDRSSAIRSSVVPEVKDYAALVEQNLQHFKPVFQLLEKQILSRVRNTASFRKTAERLLRFSDKRQTEEAIDRIFAISQQQQQQQSKSKKNRRGGKRYKFVDAVPDIFAQIEVNERKVRQKAQILAQKELPVDEDEEMKDLLDFADITYEKHKNGDVMNGRFGQARMVTTHSRAPALSASYTRLFLILNIAIFFVMLAMQLTYFQRAQSLHGQRCLYAVLLIDSCILLWLYSSCSQSQC | 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
PTM: N-glycosylated. Glycosylation is important for enzymatic activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 109725
Sequence Length: 958
Pathway: Glycan metabolism; chondroitin sulfate biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 5.1.3.19
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Q9UL01 | MRTHTRGAPSVFFIYLLCFVSAYITDENPEVMIPFTNANYDSHPMLYFSRAEVAELQLRAASSHEHIAARLTEAVHTMLSSPLEYLPPWDPKDYSARWNEIFGNNLGALAMFCVLYPENIEARDMAKDYMERMAAQPSWLVKDAPWDEVPLAHSLVGFATAYDFLYNYLSKTQQEKFLEVIANASGYMYETSYRRGWGFQYLHNHQPTNCMALLTGSLVLMNQGYLQEAYLWTKQVLTIMEKSLVLLREVTDGSLYEGVAYGSYTTRSLFQYMFLVQRHFNINHFGHPWLKQHFAFMYRTILPGFQRTVAIADSNYNWFYGPESQLVFLDKFVMRNGSGNWLADQIRRNRVVEGPGTPSKGQRWCTLHTEFLWYDGSLKSVPPPDFGTPTLHYFEDWGVVTYGSALPAEINRSFLSFKSGKLGGRAIYDIVHRNKYKDWIKGWRNFNAGHEHPDQNSFTFAPNGVPFITEALYGPKYTFFNNVLMFSPAVSKSCFSPWVGQVTEDCSSKWSKYKHDLAASCQGRVVAAEEKNGVVFIRGEGVGAYNPQLNLKNVQRNLILLHPQLLLLVDQIHLGEESPLETAASFFHNVDVPFEETVVDGVHGAFIRQRDGLYKMYWMDDTGYSEKATFASVTYPRGYPYNGTNYVNVTMHLRSPITRAAYLFIGPSIDVQSFTVHGDSQQLDVFIATSKHAYATYLWTGEATGQSAFAQVIADRHKILFDRNSAIKSSIVPEVKDYAAIVEQNLQHFKPVFQLLEKQILSRVRNTASFRKTAERLLRFSDKRQTEEAIDRIFAISQQQQQQSKSKKNRRAGKRYKFVDAVPDIFAQIEVNEKKIRQKAQILAQKELPIDEDEEMKDLLDFADVTYEKHKNGGLIKGRFGQARMVTTTHSRAPSLSASYTRLFLILNIAIFFVMLAMQLTYFQRAQSLHGQRCLYAVLLIDSCILLWLYSSCSQSQC | 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
PTM: N-glycosylated . Glycosylation is important for enzymatic activity .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 109773
Sequence Length: 958
Pathway: Glycan metabolism; chondroitin sulfate biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 5.1.3.19
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Q8BLI4 | MRTHTRGAPSVFFICLLCCVSAFITDENPEVMIPFTNANYDSHPMLYFSRKDVAELQLRAASSHEHIAARLTEAVHTMLTNPLEYLPPWDPKEYSARWNEIYGNNLGALAMFCVLYPENTEARDMAKDYMERMAAQPSWLVKDAPWDEVPLAHSLVGFATAYDFLYNYLSKTQQETFLEVIANASGYMYETSYRRGWGFQYLHNHQPTNCMALLTGSLILMNQGYLQEAYLWTKQVLSIMEKSLVLLREVTDGSLYEGVAYGSYTTRSLFQYMFLVQRHFDINHFGHPWLKQHFAFMYRTILPGFQRTVAIADSNYNWFYGPESQLVFLDKFVMRNGSGNWLADQIRRNRVVEGPGTPSKGQRWCTLHTEFLWYDASLKPVPPPDFGTPTLHYFEDWGVVTYGSALPAEINRSFLSFKSGKLGGRAIYDIVHRNKYKDWIKGWRNFNAGHEHPDQNSFTFAPNGVPFITEALYGPKYTYFNNVLMFSPAVSKSCFSPWEGQVTEDCSSKWSKYKHDLAASCQGRVIAADEKDGVVFIRGEGVGAYNPMLNLKHIQRNLILLHPQLLLLVDQIHLGEESPLETAASFFHNVDVPFEETVVDGVHGALIRQRDGLYKMYWMDDTGYSEKANFASVMYPRGYPYNGTNYVNVTMHLRSPITRAAYLFIGPSVDVQSFSIHGDPQRLDVFIATSEHAYATYLWTGENTGHSAFAQVIADHQKILFDQSSAIKSTAVPEVKDYAAIVEQNLQHFKPVFQLLEKQILSRVQNTASFRKTAERLLRFSDKRQTEEAIDRIFAISQQQRQQRGKSKKSRKAGKHYKFVDAVPDIFAQIEVNEKKIRQKAQVLAQREQPIDEDEEMKDLLDFADVTYEKHKNEGSVKGGFGQVRMVTSHNRAPSLSASYTRLFLILNIAIFFVMLAMQLTYFQRAQSLHGQRCLYAVLLIDSCVLLWLYSSCSQSQC | 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
PTM: N-glycosylated. Glycosylation is important for enzymatic activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 109755
Sequence Length: 958
Pathway: Glycan metabolism; chondroitin sulfate biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 5.1.3.19
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P0CX08 | MTKSDETTATSLNAKTLKSFESTLPIPTYPREGVKQGIVHLGVGAFHRSHLAVFMHRLMQEHHLKDWSICGVGLMKADALMRDAMKAQDCLYTLVERGIKDTNAYIVGSITAYMYAPDDPRAVIEKMANPDTHIVSLTVTENGYYHSEATNSLMTDAPEIINDLNHPEKPDTLYGYLYEALLLRYKRGLTPFTIMSCDNMPQNGVTVKTMLVAFAKLKKDEKFAAWIEDKVTSPNSMVDRVTPRCTDKERKYVADTWGIKDQCPVVAEPFIQWVLEDNFSDGRPPWELVGVQVVKDVDSYELMKLRLLNGGHSAMGYLGYLAGYTYIHEVVNDPTINKYIRVLMREEVIPLLPKVPGVDFEEYTASVLERFSNPAIQDTVARICLMGSGKMPKYVLPSIYEQLRKPDGKYKLLAVCVAGWFRYLTGVDMNGKPFEIEDPMAPTLKAAAVKGGKDPHELLNIEVLFSPEIRDNKEFVAQLTHSLETVYDKGPIAAIKEILDQV | 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
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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-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)
Sequence Mass (Da): 28719
Sequence Length: 256
EC: 3.1.1.96
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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-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)
Sequence Mass (Da): 28967
Sequence Length: 256
EC: 3.1.1.96
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Q01213 | MSTDYLTLNRTGDKMPIRGFGCWKIDTKDCEETVYQAIKTGYRLFDGACDYGNEVEVGRGINKAINEGLVKREDLFIVTKLWNTFHSKKHVRALFDRQLKDTGLEYFDLYLIHFPVPLQYVDPATVYPPGWYVGDAKSLQFEQSPIHECWAELEKIVDAGLARNIGVANFNCQAILDLLTYARIKPAVLQIELHPYLPQERLVKWVKEQGIQITAYSSFGPTSYVDLTESGKTYTSLLEHASVKSVADKHNVSTGQVLLRWALDREFAVIPKSVNAGRMKANLEILDIKLDAEDNKTLDSLKTNQRFNDPMTYGFGLPLFD | 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.-
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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 site. 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 and helps enforce protein L-homochirality.
Catalytic Activity: glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)
Sequence Mass (Da): 16400
Sequence Length: 146
Domain: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Subcellular Location: Cytoplasm
EC: 3.1.1.96
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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 site. 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 and helps enforce protein L-homochirality.
Catalytic Activity: glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)
Sequence Mass (Da): 15152
Sequence Length: 144
Domain: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Subcellular Location: Cytoplasm
EC: 3.1.1.96
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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 site. 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 and helps enforce protein L-homochirality.
Catalytic Activity: glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)
Sequence Mass (Da): 15128
Sequence Length: 143
Domain: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Subcellular Location: Cytoplasm
EC: 3.1.1.96
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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 site. 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 and helps enforce protein L-homochirality.
Catalytic Activity: glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)
Sequence Mass (Da): 15382
Sequence Length: 143
Domain: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Subcellular Location: Cytoplasm
EC: 3.1.1.96
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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 site. 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 and helps enforce protein L-homochirality.
Catalytic Activity: glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)
Sequence Mass (Da): 15088
Sequence Length: 143
Domain: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Subcellular Location: Cytoplasm
EC: 3.1.1.96
|
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 site. 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 and helps enforce protein L-homochirality.
Catalytic Activity: glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)
Sequence Mass (Da): 16683
Sequence Length: 150
Domain: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Subcellular Location: Cytoplasm
EC: 3.1.1.96
|
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 site. 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 and helps enforce protein L-homochirality.
Catalytic Activity: glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)
Sequence Mass (Da): 15809
Sequence Length: 141
Domain: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Subcellular Location: Cytoplasm
EC: 3.1.1.96
|
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 site. 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 and helps enforce protein L-homochirality.
Catalytic Activity: glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)
Sequence Mass (Da): 17639
Sequence Length: 163
Domain: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Subcellular Location: Cytoplasm
EC: 3.1.1.96
|
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 site. 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 and helps enforce protein L-homochirality.
Catalytic Activity: glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)
Sequence Mass (Da): 16280
Sequence Length: 147
Domain: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Subcellular Location: Cytoplasm
EC: 3.1.1.96
|
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 site. 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 and helps enforce protein L-homochirality.
Catalytic Activity: glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)
Sequence Mass (Da): 16662
Sequence Length: 149
Domain: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Subcellular Location: Cytoplasm
EC: 3.1.1.96
|
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 site. 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 and helps enforce protein L-homochirality.
Catalytic Activity: glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)
Sequence Mass (Da): 16923
Sequence Length: 150
Domain: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Subcellular Location: Cytoplasm
EC: 3.1.1.96
|
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 site. 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 and helps enforce protein L-homochirality.
Catalytic Activity: glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)
Sequence Mass (Da): 16568
Sequence Length: 149
Domain: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Subcellular Location: Cytoplasm
EC: 3.1.1.96
|
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 site. 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 and helps enforce protein L-homochirality.
Catalytic Activity: glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)
Sequence Mass (Da): 16486
Sequence Length: 154
Domain: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Subcellular Location: Cytoplasm
EC: 3.1.1.96
|
Q9FJ87 | MSQSNRVRDEVTLPLLQKTSHLKNHSSVLSVFLNEAISICKISYPLVLTGLFLYVRSFVSLSFLGGLGDATLAGGSLAAAFANITGYSLFSGLTMGVESICSQAFGARRYNYVCASVKRGIILLLVTSLPVTLLWMNMEKILLILKQDKKLASEAHIFLLYSVPDLVAQSFLHPLRVYLRTQSKTLPLSICTVIASFLHLPITFFLVSYLGLGIKGIALSGVVSNFNLVAFLFLYICFFEDKLSVNEDEKITEETCEDSVREWKKLLCLAIPSCISVCLEWWCYEIMILLCGFLLDPKASVASMGILIQITSLVYIFPHSLSLGVSTRVGNELGSNQPKRARRAAIVGLGLSIALGFTAFAFTVSVRNTWAMFFTDDKEIMKLTAMALPIVGLCELGNCPQTTGCGVLRGSARPKIGANINGVAFYAVGIPVGAVLAFWFGFGFKGLWLGMLAAQITCVIGMMAATCRTDWELEAERAKVLTTAVDCGSSDDDAKEDMEAGMVDK | 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 protein
Sequence Mass (Da): 54970
Sequence Length: 505
Subcellular Location: Cell membrane
|
Q9SZE2 | MCNPSTTTTTTGSENQESRTGLFLDLFSINSFEPTKRNLRHCENRGSPLMAEAVTEAKSLFTLAFPIAVTALVLYLRSAVSMFFLGQLGDLELAAGSLAIAFANITGYSVLSGLALGMEPLCSQAFGAHRFKLLSLTLHRTVVFLLVCCVPISVLWFNVGKISVYLHQDPDIAKLAQTYLIFSLPDLLTNTLLHPIRIYLRAQGIIHPVTLASLSGAVFHLPANLFLVSYLRLGLTGVAVASSITNIFVVAFLVCYVWASGLHAPTWTDPTRDCFRGWAPLLRLAGPSCVSVCLEWWWYEIMIVLCGLLVNPRSTVAAMGVLIQTTSFLYVFPSSLSFAVSTRVGNELGANRPKTAKLTATVAIVFAAVTGIIAAAFAYSVRNAWGRIFTGDKEILQLTAAALPILGLCEIGNCPQTVGCGVVRGTARPSTAANVNLGAFYLVGMPVAVGLGFWAGIGFNGLWVGLLAAQISCAGLMMYVVGTTDWESEAKKAQTLTCAETVENDIIKAVVASTIDGECDEAEPLIRITVLY | 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 Topology: Multi-pass membrane protein
Sequence Mass (Da): 57054
Sequence Length: 532
Subcellular Location: Endosome membrane
|
Q4PSF4 | METPNIISHTNLLSKIDLEKQNPAPIFPTITELKSEARSLFSLAFPTILAALILYARSAISMLFLGHIGELELAGGSLAIAFANITGYSVLAGLALGMDPLCSQAFGAGRPKLLSLTLQRTVLFLLTSSVVIVALWLNLGKIMIYLHQDPSISSLAQTYILCSIPDLLTNSFLHPLRIYLRAQGITSPLTLATLAGTIFHIPMNFFLVSYLGWGFMGVSMAAAASNLLVVIFLVAHVWIAGLHQPTWTRPSSECFKDWGPVVTLAIPSCIGVCLEWWWYEIMTVLCGLLIDPSTPVASMGILIQTTSLLYIFPSSLGLAVSTRVGNELGSNRPNKARLSAIVAVSFAGVMGLTASAFAWGVSDVWGWIFTNDVAIIKLTAAALPILGLCELGNCPQTVGCGVVRGTARPSMAANINLGAFYLVGTPVAVGLTFWAAYGFCGLWVGLLAAQICCAAMMLYVVATTDWEKEAIRARKLTCTEGVDVVITTTQTNGDLSEPLIYVVTVATD | 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 | MEDKIQSDDFTSHKNPTLPQVIEELKELWAMVLPITAMNCLVYVRAVVSVLFLGRLGSLELAGGALSIGFTNITGYSVMVGLASGLEPVCSQAYGSKNWDLLTLSLHRMVVILLMASLPISLLWINLGPIMLFMGQNPEITATAAEYCLYALPDLLTNTLLQPLRVYLRSQRVTKPMMWCTLAAVAFHVPLNYWLVMVKHWGVPGVAIASVVTNLIMVVLLVGYVWVSGMLQKRVSGDGDGGSTTMVAVVAQSSSVMELVGGLGPLMRVAVPSCLGICLEWWWYEIVIVMGGYLENPKLAVAATGILIQTTSLMYTVPMALAGCVSARVGNELGAGRPYKARLAANVALACAFVVGALNVAWTVILKERWAGLFTGYEPLKVLVASVMPIVGLCELGNCPQTTGCGILRGTGRPAVGAHVNLGSFYFVGTPVAVGLAFWLKIGFSGLWFGLLSAQAACVVSILYAVLARTDWEGEAVKAMRLTSLEMRKVGQDEESSLLLLDDEKLGDVL | 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 | MSETSKSESLDPEVSEGLCSKTLMQSIVHELKLQMRIGLPLVVMNLLWFGKMTTTSVFLGRQGELNLAGGSLGFSFANVTGFSVLYGISAAMEPICGQAFGAKNFKLLHKTLFMAVLLLLLISVPISFLWLNVHKILTGFGQREDISFIAKKYLLYLLPELPILSFLCPLKAYLSSQGVTLPIMFTTAAATSLHIPINIVLSKARGIEGVAMAVWITDFIVVILLTGYVIVVERMKENKWKQGGWLNQSAQDWLTLIKLSGPCCLTVCLEWWCYEILVLLTGRLPNPVQAVSILIIVFNFDYLLYAVMLSLGTCVATRVSNELGANNPKGAYRAAYTTLIVGIISGCIGALVMIAFRGFWGSLYTHHDQLILNGVKKMMLIMAVIEVVNFPLMVCGEIVRGTAKPSLGMYANLSGFYLLALPLGATLAFKAKQGLQGFLIGLFVGISLCLSILLIFIARIDWEKEAGKAQILTCNTEDEQTSQGSGQDSHS | 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 | MLRIPGKSLGYHEDISLTPWQAILASVIVLLGLKVATILYTAFYNVFLHPLRRFPGPVTWIAAPWMKSISHIRGQQDHQIVKLHQKLGHIIRVGPDTLSFTEMSAWRDIYGTGHAELPKHIYKGSGMEERPNIITAHSRDHHRFRKAMTPALTPEAITHEEALIKGYVDMLIEHLHKFAKSSDPYVNVSQWYTMTTFDIFGDLCYGESFNSLATGKQHLWLKSMSSMKVLVPLLVFPYISWLLVWWLLSPEQQRSLSDHQKRSYELTMKRIANRDTHPRHDFMTFMLRNRGEDQGVTDHELASNSDIVISAGSETTSTALTGITFFLCSNPDAMARCAKEVREAFKSDDEITFKATAELPFMLACIEETLRMYPPVPTSLIRRTLPGRPTLIAGELIPENTIVGVHHLATYRSERNFFDAKAFRPERWLAETRNDPKSPFKDDRLDAVRPFSYGPRNCIGRNLAYHEMRLILAKLLWHFDLKLKPGYEDWGFKQRTFQLWEKPKLVVEFKERQFQV | 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 converts alpha-ketoisocaproic acid from deaminated leucine into alpha-hydroxyisocaproic acid (HIC), which is the first substrate for destruxin assembly by dtxS1 . L-aspartate decarboxylase dtxS4 converts aspartic acid into beta-alanine, the last substrate for the destruxin assembly line performed by dtxS1 . The nonribosomal peptide synthetase dtxS1 synthesizes destruxins B and B2, whereas the cytochrome P450 monooxygenase dtxS2 is required to convert destruxin B into other destruxin derivatives, including destructins C, D, A and E . Destruxin E-diol (ED) is further produced in a non-enzymatic manner from destruxin E . Destruxins play an important role in virulence and escape from insect host immune defenses .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59594
Sequence Length: 516
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
|
Q7XT07 | MAATAAAAAAAPPADPPDSSPAASSPPRPSPEELVARAVAPVKPAFLRPPLSATPPKDEGKANGGGAVVAEKKSKRQLKRERKQEQKSSSHLCIEVGKSGNVSSCKYGDSCRFSHDIDAYLAQKPADLEGTCPFTNLDQLCPYGLTCRFLGTHKDIHAASGNLSEKHEINALNKDIQKLLWKNKYKFPKASAQIKLLGLKEVIKSKPDAANDDKKVNHDNLDGNDDENKEPLCNPPVNAECDSTLCEELDRSEGEPLIDNSIPCVEPRPTKKSKVESDEIDKHGAGTLNTNTESEDPNLSNGLEPSNNSSSCRTDLITTPHLREKKIIDFREKLYLAPLTTVGNLPFRRLCKTLGADITCGEMAMCTNLLQGQASEWALLRRHSSEDLFGVQICGAYPDTVARTVELVDNECSVDFIDINMGCPIDIVVNKGAGSSLLTKPMRIKSIVQAASTVTEKPLTVKVRTAFFEGRNRADSIVSDIYDWGASAITVHGRSRQQRYSKLADWDYIYQCAQKAPDQLHVVGNGDVFSFTDWNKHVSGCSKISTSMIARGALIKPWIFTEVKEQRHWDITSGERFNILKDFVSFGLEHWGSDSKGVETTRYFLLEWLSYTCRYIPVGLLDVIPQRLNWRPPSYCGRDDLETLMISDSAADWIRISEMLLGKVPEGFTFTPKHKSNAYDRAENG | 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) in tRNA + NAD(+) = H(+) + NADH + uridine(47) in tRNA
Sequence Mass (Da): 75572
Sequence Length: 685
EC: 1.3.1.89
|
Q28BT8 | MAESDGSNNENGNLDTVTQKLDRGVAAIKPQYLTTKEKFHVFIDADGKEVVDKQTCSELSGNDAENTVRAEDAAEPEAKRIKLDDGTGEGQDKPPTSAENKQEKKRARGQNKSRPHMKHSQFEENKLCPSVTQECASKCFFGDKCKFLHDVAKYVSEKPEDIRPNCYLYETFGKCIYGVTCRFAKSHLGDNFKNLINEELMKQWEGQVLVKNSLDKSLKEQLRKRKVVFEKTDKYLKLCNKSGDSLKIKSPVVKEDNAAQVVQKDSPVTTVGAVTDEDLVKLRPCEKKTIDFRNKLYLAPLTTCGNLPFRRLCKRFGADITCGEMAMCTNLLQGQPSEWALLKRHHSEDIFGVQLEGAFPDTMTKCAELLNRTIDVDFVDINVGCPIDLVYKKGGGCGLMNRTNKFEQIVKGMNSVLDVPLTVKIRTGVQEKINIAHKLIPNLRDWGVSLVTLHGRSREQRYTKLADWEYIAQCADIASPLPLFGNGDIISYEDANRALQTGVSGIMLARGALLKPWLFTEIKEQRHWDISSTERFDILKDFTNYGLEHWGSDCQGVEKTRRFMLEWLSFLCRYIPIGLLEHVPQKINERPPYYMGRDYMETLMASQNVTDWIKISEMLLGPVPPNFSFLPKHKANSYK | 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 regulating their translation.
Catalytic Activity: 5,6-dihydrouridine(47) in tRNA + NAD(+) = H(+) + NADH + uridine(47) in tRNA
Sequence Mass (Da): 72480
Sequence Length: 639
EC: 1.3.1.89
|
Q5ALL3 | MITPEKRTLDEPEVGSESKKPNNSTHVKGVAAIKAEYLVPTSSLTVVEYDDDEAEGGDREGESKPRNKKKQKGQNHKRDLKQKKDIIKLCPSLIDPEDDRICQVGADKCRFHHDIASYLESKPQDIDGICPVFEALGYCPTGIKCRWLKSHYNPETSKLIKDGDKMETAKTTNYEVNHIDKDQKMEMQKKKYFFKISQPVIKYLDSRIQNEANLAKQKEERKDNEASYVEAPFTIAEKKKLYLRNAKIVSPLTTVGNLPYRRLMKTLGADVTYSEMALSVPLIQGHNPEWALPKAHVSEYPGFGVQIASSKHWAAAKAAEAIYRNTTHVSELNLNCGCPIDLLYKQGQGSALLDQPSKLLRILSGMNASSGDIPVTVKIRTGIKEGKNTAVNLVSRVLEEGNAAAITLHGRSRQQRYSKEADWNYIAEVGTVVKNWNEQQKEDKEGRDRDPVYFVGNGDVYSHEDWYEHVNTDGIDSVMVARGALIKPWIFEEVEAQQYLDKSSSERLDILGKFAKYAIEHWGSDEYGVGLSRRFMCEFLSFTHRYIPVGIMERLPPKLNERPPKWVGRNDLETLLASTDYKDWIKITEMFLGKATDDFQFTPKHKSNAYENK | 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) in tRNA + NAD(+) = H(+) + NADH + uridine(47) in tRNA
Sequence Mass (Da): 69618
Sequence Length: 613
Subcellular Location: Cytoplasm
EC: 1.3.1.89
|
Q2HDP2 | MEPQDRTKRPQEEDNGVPIDGHNGSNSEPAAKKIKLDSPSSADSRAKGVAPIKAEYLLFPPGQKAKPTQSEAEADDNDDDAAEGRTAPTPQETQQAPQKDGKRKSQRGQNKEREFGTFSDAQRLCNTIAWTPEFSPRPCKHGDRCNALHDLRKYLKEGRRPDITTFGGKCPVWEKYGKCPSGWRCLFVHSHMDEIKHEDGRSELVLVGDASKAPEGGEEAAGEIKPGVVNMVPVGIKYDLSKKRIPLEKSEQYLAWLAKDTKHLAKHYQKHKDDETNPNDYRAQYVEPPFKPSEKRRLYFGRETPVLAPLTTQGNLPFRRLCVELGAQVTYSEMALGLPLLQGLKADWTLMRAHESEIVPPRFNPGGPIVQGYDNSKDVKFGAQIAANAPWVAVKATEALSQLLPHLRLVDLNCGCPVDAVFKSGSGSALLDSHSKLERMIRGMNAVSGEVPITAKIRMGSRDGKLTAQKLVERLALGSEDLRDMIGAPGCAAVTLHGRTRLQRYTKAADWGYIAECAALIKQFNEKSNDLADTIREADENTLPNGGKMYFLGNGDCYSHVEYFDHVDNAKVDSVMIGRGALVKPWVFEEIEKGQYLDKSSSERLTYIEKFVRYGMEAWGSDELGLNYTRRFLLEFLSFFCRYVPIGLLERLPPNLNERPPAYRGRDDLETLFASKNYKDWIKISEMFLGPAPPGFKFQPKHKSNSYEIEAEG | 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) in tRNA + NAD(+) = H(+) + NADH + uridine(47) in tRNA
Sequence Mass (Da): 79704
Sequence Length: 713
Subcellular Location: Cytoplasm
EC: 1.3.1.89
|
P0CN28 | MTDDPAATPRPETSVNARPAFSGQAPIKAEYLINTTPIVESASASELNNIHPDDAAEGRTDSRDSRDGRDRPDNKRRKPNKQDKKDKKGQNKGRHFPVIREASVRICRAWETTGICDRADKGDCRYAHSWEGYFEVKPNDISYRPDWSLVGEAPFVVEGERVVGGEDVVGKTLDLDTVCPVLKDLGYCPFGWRCRFLGAHVKRVAAAVDGEKEKEAGPEKRMGEWQVENWVQSEVENGWKQKETNWPEHEVLNALRRSTASFPFSEAYLKKVDPDKPFTLQNKKPTKQQPHKRKNNVLDEEEAANGPTGIPSAGDDEENAMNATENERNEEKGKVYGEPEAIDVPLRPEEKRRLNWEGGRYLAPLTTVGNLPFRRLCVDYGATITVSEMALAQPLVYGAKEEWALVRRHESEKMFGVQVAGGFPNRMVPAAEVIANTIGKGGGVDFVDVNMGCPIDLVFNQGAGSALMDSPGRLGKLLVGMNRALGDIPLTVKFRTGVAHGKPNAHKLIPRFVTEWGAGALTIHGRSRQQRYSKPADWEYIKTCVTALRESVADANLPPVPIFGNGDCFSAASYYEEMDRSGVDGVMVARGALIKPWIFTEIKERREWDISAVERLEGIKKFAEFGLSHWGSDTQGVNTTRRFLCEALSFQHRYIPIGLLERLPAKLNERPPAYRGRNELETLLASPFAGDWVKISEMFLGKVDEGFSFVPKHKSNAYGGEEAQG | 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) in tRNA + NAD(+) = H(+) + NADH + uridine(47) in tRNA
Sequence Mass (Da): 80723
Sequence Length: 725
Subcellular Location: Cytoplasm
EC: 1.3.1.89
|
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] + phosphate
Sequence Mass (Da): 19698
Sequence Length: 171
Subcellular Location: Virion
EC: 3.1.3.-
|
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