ids
stringlengths 6
10
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stringlengths 16
1.02k
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stringlengths 117
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A0A8D8SQ05 | MSNHAVVVWEWLNRNRRWRPFTPDVSQLIERAHSKNLTSVILSDADPSLQNYFINLHTLQQCSEIDGAITSVRRSFYPPDSPAGKGAKWEWEGDVTGEWHAYDMQAQCLIEYSWAKGDQTIDISKTYLGFPYILNFCNLTQVRNTTGNVRNIRRAQQAPYPLIKLSANQMAEIQGQVNGAGVSSSVAVATTMTPGKKCKHTTSSNITRTLRNIFHGHSNSNSHGSTSSSSSNIQPSHHCSNSSNHCSNSRSNNNTSSRHHNKCDATSRCNCRPACNRTCAGCNECNIRCSNSSCSKATCCSKSSVCSSGVGCNSKSPNSCNASAKSATVCSGCNSSCKPNCNGCNKCSLSCNGCNACPGVACHSNCNGRNACNKSNALSQSDLRTTLSQADRRTHSHSRVANSIRSSNTSLNSSTHSVVSSTHSMISNSQASTTSNSDLRSKKSRRPSIDTVSTYLSHDSHLNNSTHDLLDCSTSSDDPFDQKGGGSIIGMDPASETISKYVAIVKNCTDGSCPICLEPFVHSNGLVVSLIYCHHKLHLDCLNSLLTRQTSTESLYIQCPLCMKIYGERIGNQPPGTMEWSILRGVPLPGFPGTRTIQITYQISSGVQTYEHPNPGKPYYAVGFPRVCYLPDTDKGRRVLRLLGVAFKRRLIFTIGRSVTTGREDVVTWNDIHHRTSLHGDSTEPWFLDNCLDELSRHGVDDTDLTGHL | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Cytoplasm
Sequence Length: 709
Sequence Mass (Da): 77434
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A0A132HK16 | MLLTRVITAVCLLLLILPILFLAPPAALAGLVAVIVLLGGWEFGRLIGLRGAWPYVYAVACLLVLIGWHDAPQRDAVTWLLEASLIAWGVALVLMARGVRTATPAFTALGVVLGLIMLPAFGHAVMVLRAAGIGVLLTAAVLVWAADIGAYFVGKAIGKRKLAPTISPGKSWEGAIGGWLLAMIVALSLAATHTFAPTWYSLVADKGGLRLVVILTTLLVAASIVGDLFESLLKRQVGMKDSSRLLPGHGGILDRIDALIPVFPLAALLLAWI | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 273
Sequence Mass (Da): 28697
Location Topology: Multi-pass membrane protein
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A0A1C3JZ59 | MKTIDINSDLGEGYGRYRVADDEALMPRITSANIACGFHAGDPVIMRRTAELAVANGVRIGAHIGYPDVQGFGRRAVSFDAKELSALTLYQLGAMRAMADAAGGTLGHVNFHGALGNLSFADEDVARAVLQAVKDYDPTLKYVTLPFTAAARVAESLGLQTVNSFLADRAYTPEGLLASRKQPGAMVTDTARIRARVARLLSDGEIETVDGSVRKMPVDSILVHSDTAGALDIATAVREAIDAAGYAVRAF | Function: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
EC: 3.5.2.9
Catalytic Activity: 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate
Sequence Length: 251
Sequence Mass (Da): 26584
|
A0A3F2RQ48 | MGCILTKVCLGEDLLQLGDAAAPEQQQELQPSSHRLSRAKTTLLVLDPNDVSSAAGLPHTEDFHAKEVPTEVRNDTLVYGGGVPGVALDAERVELPEFTGIRDGGYRSRKDTSATFFSVFDGHGPQGAFVSHFVRENYHRAIAEAYLELIPRASSGAASGVARNASVTCDVIAEVFQTAARTTVNRLGASNIDISVSGTTAVGMLVCEKDVFIANIGDSRAIIARYSEDESTYVLHCETKDHKPNLPEERARIERSNGRVFEWGSYRVWLQDVDMPGLAMSRSFGDSVAKTVGVTAEPDVSTVEKLDFSSSRKKGERPTAFAVLASDGIWEFMTTDECIDFVAVCIAEPGMSAQEACTALVEEAYDRWDAEEDVVDDITVALVYF | Function: Enzyme with a broad specificity.
Subcellular Location: Membrane
Sequence Length: 385
Sequence Mass (Da): 41803
Location Topology: Peripheral membrane protein
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A0A6A3DBE4 | MRLCYVLLVAASAFVASSDAKTLTADRTATHATRQRHLRSYNMNDLESEDEERFQLLGNGINNLAQRVPRTINVDAILRLDSRTNALARIDTFFETSDGALGGWLQKSVLDDLLGSSVTQKREEFTQWQSQGRTAEEVKALLGANTWVEQRYKPLAVIRDPQK | Function: Effector that suppresses plant defense responses during the early stages of pathogen infection.
Subcellular Location: Secreted
Sequence Length: 163
Domain: The RxLR-dEER motif is required for the delivery of the effector to the host cell cytoplasm.
Sequence Mass (Da): 18354
|
A0A3F2RRF5 | MRLGFVVIALIFLASGEVLSATGPKISVAASANTPLQIRDELNDSSKKRFLRSKETTGDEEERKFQVQGLQKIIKKQQALSKALSKKFTEKELVVFKEWFSLS | Function: Effector that suppresses plant defense responses during the early stages of pathogen infection.
Subcellular Location: Secreted
Sequence Length: 103
Domain: The RxLR-dEER motif is required for the delivery of the effector to the host cell cytoplasm.
Sequence Mass (Da): 11559
|
A0A8D8VLC2 | MAQIRYTRNLFLRTVCLVYVFAFASLYIQIPGLYGDNGILPARSQLEGDESLPLQKKLHRKPTLLWLAPFISLSTEYMMDVISLVGIFLGFTGFVSQKFCCKPNFFALWSLYYSLFQVGQTFMTFQWDSLLLETGFLCILVAPFGINKDSYRKGSSPSDQVKFWLVSWLLFRLILTSPINKLSSGDPSWWTLKALGIHFQSMALPTPLAWFCHHIPAWGLRLTTAFSLAVELILPPLFLLPLSGAKKIAFYFQMFLQFTIIITGNFNWYNLLTIALCFSLLDDSYFYPELNRKKNKLLSILSWVVSLVVFGAACFVFYKLFGLKIDQKPFTVQTQITFSKIQYDDFLGQGLVIAIFLGVVSFLWTALAALWQTFRAPSKNGTLSSLVVTFFYIATALMVFSINTVPLANLHPFANKTSHPLLKSWHSQLAHLHISNSYGLFRVMTGVDGRPEVIIEGANNRQGPWTEIPFRYKPGNVNRTLPIVAPHQPRLDWQMWFAALGTYHQNPWISSLAYRLLTHQPEVLALLDVANYPFKSKAPAFVRAVSYKYYYSPAATKTPQWWIRNRQEEYFPEFEANHQPLIAYLTQFGILKKRKPEYVEPRVKNALDALRKYSATLEPAHLLWSLFITGLAIIYLRGGSKQAAPSANNNQGTQGKKQQQQQGQGLSKNKSRKK | Function: Involved in the maturation of specific proteins in the endoplasmic reticulum.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 674
Sequence Mass (Da): 76926
Location Topology: Multi-pass membrane protein
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A0A3F2REJ9 | MLLNCDRPRPTTMRLTNFLLVAAAAVLASCEAVSAVTDSTQTKLSTMTSPDAVQSTDVVHDGKRFLRTTKTEKYEVDDDEDDENDSYDVEEEERANLLQPYINRYGTAWVDKWAGKANDWASAGKKLGQIKEKLQGLGSSLSPEAKDKYDLFNAAYLKKHPGGI | Function: Effector that suppresses plant defense responses during the early stages of pathogen infection.
Subcellular Location: Secreted
Sequence Length: 164
Domain: The RxLR-dEER motif is required for the delivery of the effector to the host cell cytoplasm.
Sequence Mass (Da): 18178
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A0A149TX54 | MSSIPSPRRRRSRFSPVTRQVLLYLFFLLPAAMDIAQGMAGTLGPNPTSACLHDFGRYAFRFLLVSLAVTPLKRFVGVDIMLYRRPLGLLAFTYAALHVFFYVVVARHLDTHILWQDFSSRPFLTFGVLTFLILAALASTSTRRAIRALGRKWSPLHKLAYLAMIFACIHYSIAFKTWHVEPFIYTVIAICVLALRMVPRSARRKV | Cofactor: Binds 1 FMN per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.
Subcellular Location: Cell membrane
Sequence Length: 206
Sequence Mass (Da): 23479
Location Topology: Multi-pass membrane protein
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A0A7S3E343 | GRAGQERKSAEERRREASGLRDALEGAMSQQRAWELLRKEARKLESEIDSKLAAYANDKGLSYVPGSGSESVLGSAVQAAEIEDLLSKLDRTNVEMVSSASGSDSRKHTLARHRDILQEYKQEFKRLKAIHSSMQDRAELLRDHDVESGHAPLLPLSSNSSAILRERANIGSVDNALDDVIGQAQSVASSLMQQRRMFDGINSKLNVLGARFPVVNSLLTSIRRRKAKDTIVMSLVVAFCLVVMLMYMFR | Function: Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 250
Sequence Mass (Da): 27744
Location Topology: Single-pass type IV membrane protein
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B9X156 | HPEVYILILPGFGLISHIISQESNKNETFGNISMIYAMLTIGLLGFIVWAHHMFTIGMDIDTRAYFTSATMIIAIPTGIKIFSWLATIYGSKINFSPSTIWSLGFIFLFTIGGLTGVILANSSIDIIL | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 128
Sequence Mass (Da): 14090
Location Topology: Multi-pass membrane protein
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A0A1B6I1K7 | RVQDLHTDNMLESRICRLVSAVSIRVRCQSTANSPSPQTNEAEKETTGLHKIQTKYTNPFSLFKEWYQDNKVPNKVVSNALTFSTSNRSGKLSSRTLILRRLDEDGFVIMTDGRSRKCKDLEENPYASMVFLWLNMTDGVLLSRQVRAEGPVNQLTPKDMEELYEVEPLFCKIRAHICHQGRPVDWQQHKENHDKVHRLWEEGQYNLDRPDHVVAYKLVPEGIEFYEANGLTIGDRLLYQKQGKEWEVTRIAA | Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
EC: 1.4.3.5
Sequence Length: 253
Sequence Mass (Da): 29333
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A0A6A3WEU9 | MRVNSLLLLAAVVIFASAHAASATLNADQTKMVSSREASTVSRLLRKHEAYKKQDDDDEERAFNLEMIGNVFKFDSKKIDDLAPKMEIEMTNLNKLDNVVVDAKKSTTSLISRSWRSWKSKKTSLSQARLEMLNGCVKDEQAIDAVLAWYKFYAKHVVD | Function: Effector that suppresses plant defense responses during the early stages of pathogen infection.
Subcellular Location: Secreted
Sequence Length: 159
Domain: The RxLR-dEER motif is required for the delivery of the effector to the host cell cytoplasm.
Sequence Mass (Da): 17986
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A0A6A3W7R6 | MHEEDFGTPLKHTDVLASPPIGTVRRQRRFVVSCFVTIDYYDYGFYWYFYLDGRIELECKATGIVSTSRRPEGLTSTRRRWLRVSVRRATCTCSRPAWMSPSTAPRAMSTSKDRKKVVPCDYHDRTIKNM | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
EC: 1.4.3.-
Sequence Length: 130
Sequence Mass (Da): 15193
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A0A3F2RZ87 | MTSPFDRHLIDIYAGRAPDGLVFFSEHGYYDVSDTTNTVQMFRDNVGRDDFWHDRESYDEFDPFERPTVYPFGSQSKVPSSRMRSELHRTNSGRFTLLDDDGNPVSEDDLLEMEREDRLKVKSLELDDDDLAELESEQATVESAIEVIRVEKYRFQRVLFRAFYEPENGVDPDSPTGTFVSSVHDFMELPPLLSPVALLDLPPYCGNLFDRSSSFANLKHSKHSKQKDNEKITMMEQLKEQSKKASDKLEEIANKGHEAIDKVTKQTKDSINKSTKKKDSKENTDSSFLNSAKEAFHIDIKEDKKDKKKPKRKDSSDSDSDEEEGLLHGIGDEFDDLTLNQRMLGAVGCYILSGLFAFAATVMLFTGVHHVRFYALFYSLSNIATFCSLIFIMGQERLQKRMLSRKRSTSGSTWMGALALTVIVAFLWPSHWFIVILLLIAQFCGMIWYSASYIPFGRKFLHKYAAKRVILVDAMDGKIDGK | Function: May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex.
Subcellular Location: Membrane
Sequence Length: 482
Sequence Mass (Da): 55067
Location Topology: Multi-pass membrane protein
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A0A6A3JCC5 | MVHVPPRLPSDDALRLHLGRWLGLHLRSAQMLLGQALQRRLLGRDWRVPALFEAEIDARLPDKYVTLLRWFADLPDVECCGTW | Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins.
EC: 3.4.22.-
Subcellular Location: Cytoplasm
Sequence Length: 83
Sequence Mass (Da): 9642
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A0A8D8VTI3 | MHVSEMEPMKGSVSWTGRPVSYYLHVIDRTKLERYFQRHRNPRTRAAVQQIANGNVNDLEAISAAVNADLSSKQGRDRARRDLTKQMNESSSSSDEETHSDETDNRPRVTTRRAWSDYCTNKSVRTSSEEENNNSTNLVEESPPPKPKPRAKKKLRSRNDTRRRSNNKTAAPPVTAQHNISANSTPCASPPPRSAAQKQRAGKAAVGRVKRGKNKRPIKITGLDLLHSETLASTTQDVGKKLPPARGCVDQTLTSLSSSQALTVGCDVHTELEIPPTPSETPFALQMLLDILRNQYLGMIERLKSEKYKKEVEDQIEMEKKKKEQTKKRIEALDKQISHLIQDSVELLKTRMSELDIHANTPKELLSKANDIVVRHRELQAKTVKYQKEVMSLEETKNNLVMERVQELKLMPQKTEKLTKDVVIKEITATLHHQKKLKNTVNKLQSETSSLEDSQKQIIANNNNKYAHMNGNSKVSRKSREHRSRSQEWPDVPDVGKIDEKNPEVLAQKILETGRQLEARKLHETALPPARNPHLPSAASKVPLPKMSPKLKPEPCFTANRVQEPPRVDYFEDRLKLIITNVLNEDKDSRHKQSKPSPVPHHNHVPDYTQVSPAKLALRRHLSNEKPPGLMSSSGFGPMGARTIGDLVNTEIERSLEISNQSLINAAVDSAVTMCTPTSLINSILPPRPDRISPSQCPRPNVYSPIGRRSSSPPSHHPSPPKPSPLASSGPLPLSTTSKPLSQNSSSRYTHVQLPRAEMKPYHESYFTDLPSEEPVEGLAATLHSRLLSSQQQQSSTPNSLVQQPPISPRNVDDMELVESVSSRKRYSSSPLREHLALPPVKKMFSPDLPPLPNMSRPDEGKVSLFNGCHTSALILAANKHLPACYGLR | Catalytic Activity: L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.360
Subcellular Location: Nucleus
Sequence Length: 889
Sequence Mass (Da): 99481
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A0A118WLY4 | MTFVFPPEAPVALPVAGSDARFAVRRVYCVGRNYAAHAREMGFDPDREPPFFFCKPADSIVPVAYGETLDLAYPSQTQNYHYEAELVAVIGKGGADIPLERALEHVWGYAVGLDMTRRDLQMKMREMGRPWEIGKAFDRSAPIGPVHPASDVGHFEQGGLWLTVNGTTKQKSDVSHLIWSVAETVADLSKFFRLEPGDVIFTGTPEGVGAVVAGDVMKVGVERLGELAVRVV | Pathway: Purine metabolism; urate degradation.
EC: 4.3.2.3
Catalytic Activity: (S)-ureidoglycolate = glyoxylate + urea
Sequence Length: 232
Sequence Mass (Da): 25376
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A0A078G1S4 | MYSEVFQEHFISRKLLQQLPFDHNMHQQEAHVPDKNNLSGNVLMVLSILVCGIIGSLGLHYVIGCIFRRSSSFMIADPISSPSTPRGSATANKGIKKKALKMFPVTKYSPEMNLSGLGEECVICLSDFVAGEQVRLLPKCNHGFHVRCIDKWLKQHVTCPKCRHCLVETCQKILGDEADQVVATPTEMIYVMIAPLEREARVNTYRENS | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Membrane
Sequence Length: 209
Sequence Mass (Da): 23490
Location Topology: Single-pass membrane protein
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A0A8D8SX10 | MKESGEYFVSVIEDTRTQQVVGTATLVLEQKFIHECALKGKIEDVVVDNTYRGKELGKLLIAILVKLAKHFKCYKLALDCADHMIPFYETFGFEKKHNLMLNYF | Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
EC: 2.3.1.4
Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Length: 104
Sequence Mass (Da): 12006
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A0A8D9FHT0 | RPTNHSLSHGDDVTFSEFANFLIKNGSDGAEMNEHWRPVHHLCQPCKINYDFIGKHETLYEDANLLLKEMGVPDVKFPSPPVSETRQRITKQFLNLSHTTIAQLYKLFQMDFKLFNYDLKAVSNSITYVYVDEFDSSDKEWNKTSTMPVSNEPHGLVNSSTESTETVASSKNKSLPLVR | EC: 2.8.2.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 179
Sequence Mass (Da): 20444
Location Topology: Single-pass type II membrane protein
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A0A166EGH6 | MNAHTAPTAQRYAQACNDNHPAHIQSEVIYMPGPEPTNKVAIVTCMDARLDVFKMFGLKVGEAHVIRVGGGRTPDALRSLVASEHILETKEIMVVHHTDCGFMRAPTDEEAHTHIEQSLQKANGVKLSTRHLPIQVIQQGDLNRSVCEDVQFLHSSPYIRNDAVLTGWIYDTMLGTIKEVREASAISQEGKGAPAAGDRIARQTGQGILSTEHEVAASQRSLQQASA | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 227
Sequence Mass (Da): 24765
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A0A8D9A6F5 | MAVEETEFYATKFEETTFLVPVRYANLKPKGLGAQGMVCSAYDTIRKQTVAIKKMTNPFNNFVYAKRAYREIKLMKLFNHKNIMGLLNAFTPQRSLEEFKDVYLVMEHMDTDLNKIIRNEMDHEVISFLMYQMLCGIKHLHSAGIIHRDLKPSNIVVNSNCTLKILDFGLARSVAQTFSMTAYVVTRYYRAPEVILEMGYKENVDIWSIGCIMGEMIRNGILFPGTDHIDQWFKITQQLGTPSNEFLSKLEPMIQDYIMKRRHNPGYSFERLFPNNLFPPNSTKHGDLNASQARDLLSKMLVIEELAAEKKAAASSLLEAQMSKTKESISPALGNAEPHASSAAEDAKKAAIDSFDEEIKKAEGA | Function: Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating a number of transcription factors, and thus regulates transcriptional activity.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.24
Subcellular Location: Cytoplasm
Sequence Length: 365
Sequence Mass (Da): 41401
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A0A078FV14 | MDSSTTAFDNIYYKMLMQGQSLFSTDQALLTTPSTKKLVAKYASSMEEYERAFVKSMIKMSSISGNGNEVRLSCRRVR | Cofactor: Binds 2 calcium ions per subunit.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Length: 78
Sequence Mass (Da): 8831
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Q9T3C1 | TQMSGYSPPMLWTLGFVFLFTIGGLTGVILANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGLIQWFPLFTGLSLNKFLLKIHFLIMFIGVNLTFFPQHFLGLSGMPRRYSDYPDIFLKWNLVSSIGSLISLVGVIFMLFIIWESFSTQ | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 151
Sequence Mass (Da): 17088
Location Topology: Multi-pass membrane protein
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A0A2X3GTM1 | MTTTPLAADNWEGIEPIYETMPGWSETTFGVKERSGLPQAALNYIQRIEELTGVPVDIISTGPDRTETMILRDPFDA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
EC: 6.3.4.4
Subcellular Location: Cytoplasm
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Length: 77
Sequence Mass (Da): 8556
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A0A8D8Q4Z7 | MEESRLPRQSRVREFAQLLTAPSEDARDILVTRFPMPRYIETEHGGSQARFLLSKVNPSQTHANSYGYGGMLVVSPDSNSSEGGAPVLTEDVSLQVFMEHLKKLAVSSAT | Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
Subcellular Location: Cytoplasmic vesicle
Sequence Length: 110
Sequence Mass (Da): 12109
Location Topology: Peripheral membrane protein
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A0A332L6U2 | MMILNRIKLAVDRTIAAFSVVVMIALVVCVVWQVFSRYVLNQPSTLTDELARFLMIWVGLLGAAYTVGAQRHLAIDLLTLMLSSRKQALLSVIINLLIFLFAGSVIVTGGVKLIEKTLSTAQVSAAMQIPMGYVYLILPLTGIMMMFYALCFISNGLKNMKHSEAGAN | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 168
Sequence Mass (Da): 18414
Location Topology: Multi-pass membrane protein
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A0A078GFV1 | MREKRRDPNRKTLDPVVDDDEPRVVTGKGFFACYILTSLSPRHKGHTYIGFTVNPKRRIRQHNGEIRSGAYRTKKKRPWEMVLCIFGFPTNVSALQFEWAWQHPRESRALREAAAAFKSFSGLARKIKLAYTMLTLPAWNSLNLTVNYFSSKYAHHGGLSPSLPPHMKVQVCAMDDLQCFTKGDNGPEDEESSDSNEEEDDYISNQIQPRNPTTSSLDGFYPGEKVKEPEAVLDDRLANFTGFGLLDESDEDEVSGSTVEKELETDRIANFNGFGLEEIIDDEVSHITMGTDCWRRRSLITSNTEVEVIDLMTPSPTCRVGSSMKRPRISEFIDLTRSPCFIELRRMNTPMSMLNPRGRVLPFSEKERTEEETETLESSLLQLIEDNRRSSLQLREKTERSRKEAIRHAARTADLLVKAVNGGVEECFVNEKRIEAEIRSLAVTVARFGKQTDQWLAATHAVNSAVKEIGDFENWMKTMEFDCKKITAAIRNIHEDH | Function: Catalytic subunit of a heterodimeric structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
EC: 3.1.-.-
Subcellular Location: Nucleus
Sequence Length: 497
Sequence Mass (Da): 56676
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A0A078FGU9 | MSLLLKDDSIQIREVWHDNLESEMALIRDIVDDFPFVAMDTEFPGIVCRPVGTFKTNTEYHYETLRTNVNLLKMIQLGLTFSDERGNLPTCGPDDKKYCIWQFNFREFDLSSDIFAHDSIELLRQSGIDFDNNKRNGVDSRRFAELLMSSGIVLNENVHWVTFHSGYDFGYLLKLLTCQDLPETQVGFFEMIRVYFPRVYDIKHLMKFCNSLHGGLNKLAELLEVERVGICHQAGSDSLLTSCTFRKLQENFFIGSMEKYSGVLYGLGVENVQSVH | Function: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression.
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
EC: 3.1.13.4
Subcellular Location: Nucleus
Sequence Length: 276
Sequence Mass (Da): 31813
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K9KU55 | QESGKKETFGSLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQISYSPSLLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAILAGFIQWFPLFTGLTLNSKLLTIQFIIMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTSWNVISSIGSTISFIGILMLIYIIWEAFISQWMVIFSNQMSTS | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 232
Sequence Mass (Da): 25842
Location Topology: Multi-pass membrane protein
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A0A8D8QIW1 | MVDSSLLGAVEKKDSFRGDPGAILTRKQILELSKQKLEEKVFVQKCPQCHTIDAGGAHKVEPNLHGLVGRKTGQAAGYTYTEANIKKKKKKKNMKRRRKIIIGRRKKKEAEERKRKRRRRKEKKRRRKKTSRILPLLTSRRYNL | PTM: Binds 1 heme group per subunit.
Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
Subcellular Location: Mitochondrion intermembrane space
Sequence Length: 144
Sequence Mass (Da): 16859
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A0A078H021 | MYALLWSWSFTGLFLLSILANGVMGYDEMDLFNGTYVFHKQDDDDGDVLVVGLTLVQAATAEGAVCLDGSMPGYHLYRGYGSGANNWIIQLQGGAWCDSIEDCQNRKRSSYGSSTLMEKQLNFTGLLSNKAAENPDFYNWNKVKVRYCDGASFSGDSENKTAQLQFRGKRIFLAVMEDLMAKGMCHAKKALLNGCSSGGLSAILRCDDFSSLFPPTTKVKCMSDAGFFLDAVDISGAHSIRRMYSGVVNTQGLQNTLPRTCTSHLEPTSCLFPQNIINQVKTPLFILNSAFDSWQIENSIAPPSADPSGSWHNCSSSFKCNTSQMQFLEGFKMSMLDALKTFSMSSKNGMYISSRWAHCLAERKDTWSPGNSQPGEDTGMAVAVGDWYFERAKK | Function: Hydrolyzes acetyl esters in homogalacturonan regions of pectin. In type I primary cell wall, galacturonic acid residues of pectin can be acetylated at the O-2 and O-3 positions. Decreasing the degree of acetylation of pectin gels in vitro alters their physical properties.
EC: 3.1.1.-
Subcellular Location: Secreted
Sequence Length: 394
Sequence Mass (Da): 43439
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C4WUN1 | MDNFGDNFDDGDVDPAAEFLAREQTQLAGLEDDLSTPNVPIGVTQTLSNGSGSSFEIIDSAENQLTNPVIENGLTNGFTVTNSDDDTSSPIIAPKIEREEPEKIKKWREEQKTRLEEKDADEEKKKEELRLVAKANWKNGTRFTRNKLQKLKMLIEMQRNNLLLNLMKLSQALNGIASQNSAILTPNRVVLVKMLHV | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Subcellular Location: Cytoplasmic vesicle membrane
Sequence Length: 197
Sequence Mass (Da): 22080
Location Topology: Peripheral membrane protein
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J7MH70 | KSSLLWALGFIYLFSIGGFTGIVLANASIDTILHDTYYVVAHFHYVLSMGAMFSIFGGFIYWYPIMTNLSLNENLLIIQFWLSFVSVNLTFFPQHMLGLLGMPRRYSDYPIHYLSWNIVSSIGAIGSTLSSLLLIYIIYESFY | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 143
Sequence Mass (Da): 16337
Location Topology: Multi-pass membrane protein
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A0A967SYZ9 | ENHLIIRVSWLCGQFGSNFVKTMLQLGQERDELQVVDDQWGSPTFAENVVANCLNLLGKDIAGTYHITSKGLISWYDFAKAIFEMSGIDVSLETVDSDAFSTKAKRPYFS | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 110
Sequence Mass (Da): 12326
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A0A078JUD2 | MLADLCHLRPLMDPLFLLLAPANPKVFFYMTVDAKPAGMIVMELFADTTPRTAENFRALCTGEKCTGKLGKPLHYKGSIIHHVDPCYMIAGGDIIDGGKGNRGECIYGSRFFEVENFIKKHTGPGILSKWNRGRNSTGSQFMIHAKANSDLDNECVVFGQVVQGMYVVTSIMALSTNTSIPVAVISNCGQIS | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 192
Sequence Mass (Da): 20933
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S5X4Q9 | TLYFIFGIWAGMLGTSLSLLIRAELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWMLPPSITLLISSSIV | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 102
Sequence Mass (Da): 11233
Location Topology: Multi-pass membrane protein
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A0A8R2JR53 | MASAPYLDELKNSLNNLPDELHRNFSLMQELDLRSQKVMNNIDKMANNYMSNVKEYSVDKKKETMASIKHHFDAAKAYSDDKVQLSIQTYELVDKHIRKLDTELLKFKGKIQLQTDMRNAAIKAKINLPPKKEGLKTTSALPSVSAVITPSNPTNSLDDVAVGTGCLSGPSVDHGIAHSAYVDMPIDPNEPTFCLCKQVSFGEMIGCDNPDCEIEWFHFACLNLTTKPKGKWFCPNCVKDKKKK | Function: Component of an histone acetyltransferase complex.
Subcellular Location: Nucleus
Sequence Length: 244
Domain: The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence Mass (Da): 27354
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A0A1A8VTX3 | MKEVTRRKDKLNMEQNDTKNDLTIGHIIVKNKDNVVKKNNSGYSRKSGKKNKNSVDAKRKKRLIDKKQVKKKRKINKVKNEEDKKECKQFANSNSMVEYNINKVVYDINKNDLIRGDDNNYKNVYLERNKQKYKKKKKIEKTPEDIVNSSLFRYINEFMYTNKSETVQKKLNETKNVFNIYHMGYKNQKDKWPNNPINDIIKYLRKNFTKIDKIADLGCGEAEIAKTLSGWSISSFDLIKFNEYVTACNITHLPLSNNSQDCVIICLSLMNTDWPKIIFESVRCLKKKATLIIADVVSRFTNYKAFVKFMSNVGCTLSNQVNLDNFFYIFFFENNKKDNVSLTVNEGKVKKFSKLLAPCFYKRR | Function: Probable methyltransferase required to silence rDNA.
EC: 2.1.1.-
Subcellular Location: Nucleus
Sequence Length: 364
Sequence Mass (Da): 42753
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A0A8D8UE29 | SYQAILENANVLARYASICQANRIVPIVEPEVLPDGPHDLERAQKVTETVLAAVYKALNDHHVYLEGTLLKPNMVTAGQSCTKKFTAQEIAQAPVTALNRTVPAAVTGITFLAGGQSEEENE | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
EC: 4.1.2.13
Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Length: 122
Sequence Mass (Da): 13144
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A0A4T0S3R6 | MLSTLSAIQVLAIHDAIQESGIDTDKVINYILSLRPKNEGFFTGDEWGESDTRFTYCAVSALSLLGALHKLDEKENGVAIKDRIVDWFKQCMNFDGGFGNNISAETHSGQAALAILDRLDIIDRDNLSWWLSERQVESGGLNGRPQKLEDVCYSWWVLSGLSILHRLHWINKEKLMSFILSSQDPDNGGIADRPGDVADVYHTLFGVADTPPPPYENNQRASTSATPRVSDEFAPEDAPLLRQHEEYDEEEELVDDDRTVWERYWAGTFSTFQWKALAHLSVISFPLALFAWIFCFVGSVITASLLITLPIGLGFGWVLLLQSYHFQYF | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX.
EC: 2.5.1.60
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Length: 329
Sequence Mass (Da): 37099
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A0A132H7Y4 | MRKLIMGIVEFREKMLPRYAEQFSKLALAQTPDALFITCSDSRVVPDLLASTHPGDLFTMRNVGNLIPPATAEGVSTGDLSEASAIEYAVLVLKVANIVVCGHSECGAMKAVYSRNPKLKAPNLDKWLYHASNAAFRLEHEGALDESLKPHDQLSQLNVLVQIEHLMTYPIVRRQVMAGALVLSGWWFDIATGDMYAYERASRSFEVIDRALAERLASRLASRAR | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 225
Sequence Mass (Da): 24975
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A0A1A8VW09 | MKSVSIKQLEAILILDTDGNRIAVKYYNDKLTPKGDDKLNNTGCSKESLNYPYDGTLYNNLKTSEQQKLFESDITDKAKKLGCNSNETEILVINKYIILYLSINDVSIYIVGDENDNEIILNEIIQTVEQSLNNITNNQIGKKQLIDKLDSVYLILDEIADSGIIMETNSDVIINRLYMHEGDLQEHTPLNQAISSAKENIIRSLLSGT | Function: The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.
Subcellular Location: Cytoplasm
Sequence Length: 209
Sequence Mass (Da): 23535
Location Topology: Peripheral membrane protein
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A0A0S3I0A0 | TLYFMFGAWAGMVGTSLSVIIRAELGHPGTLIGNDQIYNVIVTSHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLMASSMIENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRTTGITFDRMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDP | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 206
Sequence Mass (Da): 22175
Location Topology: Multi-pass membrane protein
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A0A6A3VSX7 | MRHIQTVFLVAATFLAVCTTSSATPNNSKLEAPNLFQSGDAQQDDRNARRFLRTDENAAATEERAIDLKKIFDARIFSTTYLNLMKYNEAFRLKMFKKWDQYSMEQIKVATGQAKLRNPRLAKVMVEYVQDHRVYGQWNKLRKH | Function: Effector that suppresses plant defense responses during the early stages of pathogen infection.
Subcellular Location: Secreted
Sequence Length: 144
Domain: The RxLR-dEER motif is required for the delivery of the effector to the host cell cytoplasm.
Sequence Mass (Da): 16821
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A0A069B544 | MSHATVHPSGALKGTVTLPASKPHVQRALLVALLNGATTRIENVSWCAETELQFAALRQFGLTVVERGDASLTLRGAGAGVEATGTIDAAGSGMLFRMSAALASLSERPVTIRCNDSLFSRDSVFDDGFFSHLGIDARRRAGNLVTISRKPHPERIALTTRKSTQFISFALFVAPFSADRTLRVADDGSQAGYIDMTIKAMSLLHATVTRAPGRLLAGEYRADDIVIGIPTDFTSLSYLASAALSVGARSAIDIANYRPGDTLNEAALFDVYRALGVRLTRDDARHALRIECERDRAARRAPRELSLRELPSAATNIIAAASNLGDSIRFGGVDGINNHKCQRAFVIHENLRAMGGRSALVFNDVGRFDKIDVMSDGPLQGGAELPSYRDHRICAANIVAALGARRKTVVCDTDKLDDGFPKFIDTLRALGAEIA | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
EC: 2.5.1.19
Catalytic Activity: 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate
Sequence Length: 435
Sequence Mass (Da): 46690
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A0A087SRN9 | MIDSDRHIEVTRSGNAFLYTTEQNIQAQKFLRELKQLQRHQKVMSFSELVQGYMKSTGVTDGDEASRNCAALSTAGLILKHGDLVYLEPGEVALAVLGALPQQPQLLRAKLEETRRELAVLEDRRRHIERSVARKHHLARWGGLAFLTLPWAILFRLTYWELSWDVVEPIGFFLTGLTTILSYLWYMHHRAEFTWSEMHQRMISGWEQQAFKRANFDVARYEQLRRAAERQEQALRLTTPTQPLSPHAEPP | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes a pore-forming and calcium-conducting subunit. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways.
Subcellular Location: Membrane
Sequence Length: 251
Sequence Mass (Da): 29121
Location Topology: Multi-pass membrane protein
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A0A9E4XX75 | MDPAVSSTSVAWNSRSTLAIRTFVAIEIPEPLKAKLDRSVEALRSGVVDDLVRWVRPDSMHLTLKFLGEIEQLQVHAIEQILDQVAGGFAEFALEMAGFGCFPNKKRPRVIWVGFDAAAAELLRLQAELTSHLELIGFEGDRRDYHPHMTLGRVRKELSAAHSRILSDWAKEAQIGTIGKFQVESISLIHSVLEPGGAVYTRLHSARFAP | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 210
Sequence Mass (Da): 23322
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A0A520XVB5 | MIALLIAVTFAFGFAFAAMPVVIHALRRHDVGQFIQEDVSEHSHKRGTPTMGGTVIIVATVLAYGIAHLRIWSPEAGFGLDPRPFSAEGGLALLALIGMGVIGFIDDYQKYARKQNLGLSKRWKFGGQLLVAGLFAWGAVAAEVSTELSFTRELGFDLAWAYPLWVLFLLTAAANATNLTDGLDGLAAGSSALVFGAFVIIGFWQFRNPSVYAVDGALDLGILAAALLGSVMAFLWYNAAPAELFMGDVGSQALGGAMAALALLTNTHLLLAVLGGLYVMEATSVILQVGSFRLFGKRIFRMAPIHHHFELRGWPETTVIIRFWIIAGICVALGLGIFYGDFISMEGGLS | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Catalytic Activity: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP
EC: 2.7.8.13
Subcellular Location: Cell membrane
Sequence Length: 350
Sequence Mass (Da): 37457
Location Topology: Multi-pass membrane protein
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A0A6L7JF64 | MIVARNVNYRYPAGELALRTVNLTIRRGEFVFLVGSSGAGKTTLIHLLNRDLVPSSGSIYIDGVNTARLTRSEIPRLRRRVGVIFQDYKLLTRYTVGENVAFALRVTGGYDGAAQRRVREALATVSLADRANDYPFQLSGGEQQRVAIARCLVTKPPIVIADEPTGNLDPEIARETISLLLRISELGTTVIVATHNRELVNSLRQRVIELSGGRLARDEIRAGYTADLLDADAFTSAQSPAEDPSDD | Function: Part of the ABC transporter FtsEX involved in cellular division.
Subcellular Location: Cell membrane
Sequence Length: 247
Sequence Mass (Da): 27064
Location Topology: Peripheral membrane protein
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A0A2E9GVA4 | MRIAKGLHWILPLGLAALAFALRAAGHETVFAGDELAPTVGDAWYHLRRIVYDAARFPHLLGFDPFVQFPRGASAAWPPLFDALVAWFALPVVENVGPEMKRFALWVPPVIGALTVACLYALLQRRLGVVAALVAAGLLAILPAHVEVTRVGALSQRCAGGLVAVLVLAAALRLVESELRAWGAALVTGLLLGFGVLLSVGGVLVAAVVQVGLLILLATRPVAGADGAAQRLVALQCVALLVVLPAAVLRATPEAAPFTVPYPSRTHLALFAVPAAIALAWVAARRSPMGASLSLRVVAMLVLAALGMAAGGILAPLVLDGGVTPWRAFFGPASLAAGRVEPPFTAGSLLGDLTLFGWAVPFALPLLAWRARCGSASTLLALGAGAVFLGVAFVVPGGHSLGSVAVALVVGYAVAAAVVLASPRLSGARGGVLVVGTSVLLAAPALVRSEFVGTRPATTVYGIDVPESRVRAVANWLREFTPPTKGWFDSGSEPPYGILAPWELGDFLTFASLRATAVDSLSKPMRVARSRKFFLASPGIGANLASLWNVRYAVMPVGIHAVLTPASPVSLGRSLLEFDGSETQDPQLGEPPAARQFRLVYELGDPSDPGGLRVYERVAAARIAGVTMPGRLVSASLKLRTNTGREFTWRTSAQSNREHGYYEIFVPYSTQGGSFRRFVEPVSDWVLECDGERRRVKVEEWKVLDGKVVRGPHFCFQ | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
Sequence Length: 717
Sequence Mass (Da): 75507
Location Topology: Multi-pass membrane protein
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A0A536EH65 | MPSFVADAGLLDVNGTLIAEVIAFILLVLILAKWVYPPIIRIATERESKIAAGVRAAEEAEKRLQEVQQQVQQVLGEARNQAREIVARAHTDATVEAEEVAARGRAQAEALLERARAEIAAERDRAIQDLRAVESDLVVDATARLLGEVLDRRAHERLIEEALVKIGDARSAASPSN | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 177
Sequence Mass (Da): 19287
Location Topology: Single-pass membrane protein
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A0A534Y6E6 | MTAPGRFIVFEGLDGAGTTTQSQLLADALRGKGRTVHLAHQPSGGCVGLLIRQILAGRTATQKADGKLDVVDERVMALLFAADRLDHLTSQIEPRLARGEDVILDRYVLSSLAYQGATVSHEFIQAANRYARKPDLTLFLYVPAPVALERVRKRGAKLERYETPGQMQQIEREYSRLVGTLASVVPIDGTRPIAEVAALCLAAVHEQLGIAAAG | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 214
Sequence Mass (Da): 23125
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C4TNR5 | MTVTYSNRVADARLGTFSRLLLRWRGSIYKLLYREFLIFISCYFIISVTYRFLLNEQQRIYFEKLALYCDNYAELIPVSFVLGFYVTLVVSRWWGQYESVPWPDRLMCLVSSNVHGTDERGRMLRRTLMRYANLTGLLILRSVSTAVYMRFPTLQHVVNAGFMTPTERSKFDGLVSSHNKFWVPCVWFANLAVTARSEGRIRDNVVLQLILKELNSLRTQCGRLYGYDWISVPLVYTQVVTVAVYSFFLACLIGRQFLDPQKGYPGHDMDLYVPVFTLLQFFFYAGWLKVAEQLINPFGQDDDDFETNWLIDRNLQVSLLAVDEMHQDVPPLEKDIYWNDSDPQPPYTASTVETRRPSYQGSAFDISLQKEDLEFQPLEQINENEEANHSTPLLGPLGRLLGVNSPGPQRSTSRLSLLMRRRNRGPAGVPHFNQRDPGNIKCGEALRDLNVFMSTPYYERPGFYSAPQTPLNGGPTVCPPRFSTHGNTTVFTTHWARKKVPMGEVAMESSSLSPGSKNCFVWPPGSMEEDVEGVISNGESVTTLQSEHSGNLQSTVQVPSKLPRALRLSSLIQGNSAQASPDALQTPGHRAPHSIFSFSPVTSPVLQRASLARPGQSDGESEMSNKEQHKAQCPSSKDSGISLAEGDFTDLMEVIMEDGEISEQSEEKSG | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 670
Sequence Mass (Da): 75598
Location Topology: Multi-pass membrane protein
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A0A6S7HT46 | MAEKAFKQEMPPRGGYASINIARNLKTRGPSGFMTFVLGTGIMLGGFLVVKYGNNKRRCKQNLKLFLKSVDFTVSVPQIIIVLCCRTLKMERQEAKVSLIPLIQAEQDRNMIRQMKENMETEEAIMKHVKGWKVGESVYHNERWVTPHSTELEKL | Function: Complex I functions in the transfer of electrons from NADH to the respiratory chain. Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 155
Sequence Mass (Da): 17786
Location Topology: Single-pass membrane protein
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A0A8E3MFQ7 | MLTVLNALNDNYIWLYSDNRKDLLVVDPTVAAPVLTFLQQHSEYQLTAILLTHNHYDHIDGVAELRLHYPQVPVYGPQEIENVQQGLLTQIIEVGRLNIGHYNIEILSTGGHTAGHLSYLINSHLFCGDTLFSAGCGRVFTQDYAQMFNSLQTLKKLPTTTIICPAHEYTLSNLAFARTVDLEDEGFQTAVKQHQQWAIQKRQAGEATLPVTLAGELQINPFLRAKNLAEFIQLRQAKDQFK | Cofactor: Binds 2 Zn(2+) ions per subunit.
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
EC: 3.1.2.6
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Length: 242
Sequence Mass (Da): 27299
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A0A536LT81 | MRMTVSNLRLPRPRSAHLLAGIFLLILIALVATGCIGGTDTPQNTLAPEGEVARHQRNLFMLAMWPALVVMILVEGAIIVTLLRFRRRKNDAVPKQTHGNTPLEIGWTIVPTLIIIGFVGVPMLPVLFDLGRDPKADAYPIEVTGQRFQWSFKYPNIKDARTGEPLESPPVTPGRAAELHIPAGKEIALTLTSIDVNHSFGVPRLAGTQDAIAGEHHRFWMKADHPGSFSGQCRELCGVDHWGMLITVIAQSQEDFDAWAKEAAAGVKQTPEGRVPSAVAATGSGD | Cofactor: Binds a copper A center.
Function: Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
EC: 7.1.1.9
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Subcellular Location: Cell membrane
Sequence Length: 286
Sequence Mass (Da): 31054
Location Topology: Multi-pass membrane protein
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A0A1M2U4P7 | MNTEATHDQNEALTTGARLRNAREQLGLSQQAVAERLCLKVSTVRDIEEDKAPADLASTFLRGYIRSYARLVHIPEEELLPGLEKQAPLRAAKVAPMQSFSLGKRRKKRDGWLMTFTWLVLFVVIGLSGAWWWQDHKAQQEEITTMADQSSAELSSNSEQGQSVPLNTSTTTDPATTSTPPASVDTTATNTQTPAVTAPAPAVDPQQNAVVSPSQANVDTAATPASTAATTPDGAAPLPTDQAGVTTPVADPNALVMNFTADCWLEVTDATGKKLFSGMQRKDGNLNLTGQAPYKLKIGAPAAVQIQYQGKPVDLSRFIRTNQVARLTLNAEQSPAQ | Function: Cytoskeletal protein that is involved in cell-shape control through regulation of the length of the long axis.
Subcellular Location: Cell inner membrane
Sequence Length: 337
Domain: The helix-turn-helix (HTH) motif in the cytoplasmic domain of the N-terminus is involved in the formation of spirals to maintain the rigid rod shape. As this protein is anchored in the cytoplasmic membrane, the HTH motif may contribute to protein-protein interactions to form the RodZ helix, which is localized beneath the cytoplasmic membrane. The C-terminal domain may be critical for determination of the rod shape by probably interacting with enzymes required for synthesis of the peptidoglycan layer, including PBPs in the periplasm.
Sequence Mass (Da): 36163
Location Topology: Single-pass type II membrane protein
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A0A0A9WN79 | MKTYFFVLNGMLSTPNTWSWQFALVLIILLSLMAPLSSNNRVRYYACYICYVFNVSLMAIILIPFFMFRPKNIGNLWIAGKICKHITKFIGITWTLRNGHILEEQKGAVITANHQSILDVMGMFNIWETMGKCTAIAKKELLYIPPFGQAAWLAGLVFIDRSNPTAALQTIQMSSHIIHDLKAKLWLYPEGTRNKNGEKLLPFKRGAFKSAIDSRAPIIPVVFSPYYFIDGRNKTFNRGEIIISVLDEVSTEGLQPEDTNELMKKVHDLMSAEYDKLKQEIEIKYRLKK | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 289
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da): 33137
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A0A034WP08 | MMNAVTRAYLRAGSQTVSNVLKPATVASAQVQRNAHTDLQVPDFSPYRRESVNTPNRKDDSAESRKAFSYMLIGAGAVGSAYAAKGLVTAFVSSMSATADVLAMAKIEIKLSDIPEGKSVTFKWRGKPLFIRHRTADEISTERSVAVSTLRDPQGDDQRVIKPEWLVVIGVCTHLGCVPIANAGDFGGYYCPCHGSHYDASGRIRKGPAPLNLEVPAHEFPDDGTLVVG | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Catalytic Activity: a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out)
EC: 7.1.1.8
Subcellular Location: Membrane
Sequence Length: 229
Sequence Mass (Da): 24648
Location Topology: Single-pass membrane protein
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A0A0A9XXL6 | MISTSVMNGGDVASCDYSSSYELIRGIADFLLSRTDLRPKIGIICGSGLGSVATILDVKKEFSYSEIPHFPRSTVPGHAGKLLFGYMGNVAVMCMQGRVHFYEGYDLVKCVMPVRVMKLCGVTHIIMSNAAGGVNEKYNVGDIMIVKDHVNFLGLGGLNPLRGPNDDRWGPRFVALNKAYDQWMRKKAKEIASQYEQPSRTTFHEGVYAVVGGPNFETVAELRMLRKMGIDAVGMSTATEAIAAHHCGMTVFAFSLITNKCVLEYDVEEMPNHEEVIESGLKQESLVKDWVSSLVQAVGNQWLMHTEKGCNGLAL | Pathway: Purine metabolism; purine nucleoside salvage.
Function: The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
EC: 2.4.2.1
Catalytic Activity: 2'-deoxyguanosine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + guanine
Sequence Length: 315
Sequence Mass (Da): 34596
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Q7Q8K4 | MKLFNFYNKSVYIQYRNQLCSTTTVVVCALTLAAFAVPYYLLSSIRQGELWDQQRTVYEQPKMSFQYSYLFLAEMEDSEEGRATSASVVTCSSFPSYNTLTEQLHPCSDVQVIPTDTNHDHTLDHLSVSVSFNPPDRASRLSFYTFYFFLEATVSSQCRFVIPAFVSLEKVPPPAARTFLSGTIVHSGLMATRQTVALQCPFFMRHQQSHFSDRYYPNENTTLDGFQPRVIRAQIEAANPAYYEYRPQHIDWTMDGSGTVRVQVDVAIGGNESTSVALLYKTSLWWKLCQFWGSYFPLLIVSLWLAEKSKQYLFERFFLRAVEVVPWKNKYN | Function: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling.
Subcellular Location: Cell projection
Sequence Length: 332
Sequence Mass (Da): 38290
Location Topology: Multi-pass membrane protein
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A0A6B1C4A1 | MNDAGMDRARSTDGTMPLMGHLVELRSRLIKCILAVVAGAVACWVLYPQILDLMVQPYCDIVPEQAVAEEAARQNLFGGCELLVLDPLEPFSVRLTVAGYGGLTLAIPIILWQVWRFVQPGLYPRERRHAAAFTVVGALLFALGAGLAYWSIPRALKFLATIGGEDLVTGFSPAKYLSFVIKMMAAFGIGFEFPILLVFLQFAGIIHYRQLIRWRRFAIVGIVALVAVITPSGDPFTLMVLSVPMYLFYEAAIVVGWLRDRRNRRETTGEADTNALEASPAVSPSED | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides.
Subcellular Location: Cell membrane
Sequence Length: 287
Sequence Mass (Da): 31606
Location Topology: Multi-pass membrane protein
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A0A8T7F6S8 | MRPSVIYCDVPVCCCSCTNAKKRLMKYPILLLIRFYQKYISAGLPSGCRYDPTCSHYTYQAIERFGLIRGGWMGLQRIARCHGLSPGGYDPVPEKKRPHQHPKHSQKLPKKLQEEQH | Function: Could be involved in insertion of integral membrane proteins into the membrane.
Subcellular Location: Cell membrane
Sequence Length: 117
Sequence Mass (Da): 13505
Location Topology: Peripheral membrane protein
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A0A162TP34 | MKILRHYISREILLTLSATLIVLLAILLVQRLALMLNEVMNGGISANVIFSMIGIQILRFVAELVPLSFLLASIVAFGRLYKDSEMTAMFALGMPLTNLYRVLFQLAVPFSIILLLLNFWVIPYFSQKHFAIQQQAREEAQLTVVKAGTFRELSRGKNIVYVREISENQQEIKDVFIKTLEGEGAYTITLAKTGHQIVDRETGVRFLVLENGKRYSFLKNGGIDVLDYQEITLRLDSSTQPVFPKLATYSTREIVDNLNRTDFNSEFNRRFASAISVLILAIMIPALAHSNPRQGRFGKLLSAIFIYVVYFNLLNVAQNWVRKGVTPSWLGMWWVHGVMLIVALVIAYRYSKRLA | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 355
Sequence Mass (Da): 40387
Location Topology: Multi-pass membrane protein
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A0A388NV74 | MTSFYPALRPLLFQLDAETAHAITLQALRAVQHSPALLRILTRMFAFEDARLRTEVCGLRFRNPIGIAAGYDKNAACVPGLSALGAGHVEVGTLTPLAQRGNARPRVFRLAQDAALINRLGFPNAGIVAALPRLAALRARGHAAPLGINIGKGRDTPLELALEDYSTLLQQVHPFADYIAINISSPNTPGLRTLQSSAALAPLLGALQQLRRQHCPRLPLFVKIAPDLSPAQLDELLDAALANDIAGVIATNTTTARPNLRSPAAGAEGGLSGVPLQPASTAAIRHIRKYSGNQLAIIGAGGIDCAAAALEKLSAGANLLQVYTGLVYQGPGLLQAINRGLVQMLAQRGARSLAELAAG | Cofactor: Binds 1 FMN per subunit.
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
EC: 1.3.5.2
Subcellular Location: Cell membrane
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Sequence Length: 359
Sequence Mass (Da): 37617
Location Topology: Peripheral membrane protein
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A0A5B0Q3H6 | MDRPVSTIIRRTTTTTLTTRIQTRPTNKTKGQFNWASRSYSTNGRTTPIRVAICGGGPAGFYAAKALLSQQSLIPTRPISIDLFEALPTPYGLSRYGVAPDHPEVKNCEHKFDQVGRHPQFRYFGNTIVLGDQQEGPSWGQASVRLSTLRAQYDLVLLAYGAGEERSLGGLEGEDSLANILSARTIVGWYNGYPSTPITNPTITHKKFGVDLSKIDTVTIIGMGNVSLDIARILLSEVDVLRRTDISDEALSELARSRVRHVEIVGRRGPLQTAFTTRELRELVRLPDLAMRIDSPPLVDAAARIAEPGALARMPNGRLTKRLLEVMLAAAKQPPSSSSAATRTCSLRFLQSPIAFHGAPPPPSSSSSSDDDNESTSVPQKVGSVQWAHNRLEYPTDSRTLPPLDYSAIKARPIMPLVTHSSPTDLVLKSLGSVPLLFPPLSPDPSHSRARNVAGRVVGADNQIIPGLYVTGWLSTGSKGVIGDTMSGSTTVSQTMISDILSSSSASIPTRSGMESVAGEDFQPTLEGKEFGVDWQRWRLIDEFERERGRATDRPRVKCSGLQQMLAVAGVL | Catalytic Activity: H(+) + NADP(+) + 2 reduced [adrenodoxin] = NADPH + 2 oxidized [adrenodoxin]
EC: 1.18.1.6
Subcellular Location: Mitochondrion
Sequence Length: 572
Sequence Mass (Da): 62101
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Q7PS69 | MAQEKKENQSVLVKGYLTLYNTAQFAGWTYIFVQFIQHFAVHGQSLDTLWSRVGQATFFFQMLAILEVVHAMVGIVPSNVAMTFLQVFGRCMIVAGAIEGTPTGQKSPGLPLALFCWSLTEIIRYSYYVAHLLLPAVPSLLVWLRYTIFIPMYPCGFLGELLCSYWAQSYIRDTGKWSVELPNRFNFSFSFYYFIWIMAVCYMPLFPQMYLHMFAQRRKVFGRGTQTRQKLTKAN | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Catalytic Activity: a very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain (2E)-enoyl-CoA + H2O
EC: 4.2.1.134
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 235
Sequence Mass (Da): 27155
Location Topology: Multi-pass membrane protein
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A0A7D9ID92 | GLTCRVTSGNSFALCINSLLKIYGELDSRVRPLCHCFRLWAKICEVDRQTTGTLPPYSFFLMVIHYLQQIESPVLPVLHEKFGDELNKYLEEEDYGLLALIRKGWKTGNKTSLGELWLGLLRFYSDYENNEIYVVSIRQKRRLKRSEKSSWGKKKFAIEDPFSTKRNVARTVLKNNVYRYIIEHLRVALVYFSCHPNSSGTRLNENKGNDPDEHKGQKNVQESHVSKRENRPHSSTEEDVEVASSDSDEDEQGNEDDDEAGDEDGDEDGDRSETEDLIDGIFAIDSINDSVLSDNDGADTTATDQSVLEDSDCATSTTTIRSGLIIAHSILPGDSATSSEQLDVEWRNAEYRFDDSVLRKGDAPETKCTYCGEEGHIVENCTAEQVTRTTKPLPPMPDWFKDILSKVCYCCKDDFGMTNDEIRRRQFYLKTLETYIKDYLPDARLHLFGSSCNGFGFTGSDIDLCMTLDGKAKNDIDCIEHIKKLANVLRKYSQCTDIVAITGAKVPIVKFFLRHAKVEADISMYNEVALMNTKLLATYVHIDQRVQILGCTLKIFVKLCDIGDASKGSLSSYAYILMLLHYLQQRRPPVLPVLQELYDTPEQPQSVVEGHNCWFYDDLKNLGTKWKARNTESCGELWLGFLRYYTEEFDYRRNVVCVRYLKPLTKFEKLWNGRQICIEDPFVLTHNLGAALTLNMVRFIRSTFERARERFGTARPDIPANGQDRQRFFFDTYFLTNGFMPPTDRNCNVCGKIGHWAKECPYNKSRRKKGEQNKAEKGQQNKAEKDQQSKTDKGRQSKDEKIPPDKIPPEKIPPEKIPQNIGEQGKQNSVEKGSQNQDKNIPINWAARIQANSTEKAQERQQEEMTKSNLEGNNDVI | Catalytic Activity: RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide
EC: 2.7.7.52
Subcellular Location: Cytoplasm
Sequence Length: 877
Sequence Mass (Da): 100247
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Q9HNW3 | MTIDWGSVTHITKVDPADPLPDDASVLGHTDLVIVGGSDGVTESNTLATIERIATEAPDIPVWQEPYSGSHVSKDTIEAVDNVAVPAVYNGDSANFVDKHVDFFTQAARKPAQLTGANLPLVGDIVESKGRDAVTDLTDAVLAEGYVVQNLDSKAAAESGVDTLYTPEQVAGAALATESFFDFPVFYVEYSGTYGGPADVEAAAQYLEDTTLLYGGGIQNGTQTRAILDAGADAVVVGDIFHEDPDRFIDTIP | Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Function: Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate + sn-glycerol 1-phosphate = diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate
EC: 2.5.1.41
Subcellular Location: Cytoplasm
Sequence Length: 253
Sequence Mass (Da): 26636
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A0A932Q2J6 | MRLLATLEYDGTDFRGFQFQKRGRTVQGEIETALTHVTRDKTRVVGAGRTDSGVHAIGQAAHFDTTWQRSLAELQRALNAVLPNDIAVVDLKQVAENFSARYAATSRLYRYTILNQAQRAPLVDRFALIVPEPLDENAMDRAARLLIGEKDFGAFGTAPEGTNTVRVVTRAHVQRAGARVWFEIEANAFLYRMVRRIVGSLLKVGKGRQSVADFQAVLEKKRRAEIAARPNGLCLMRVQYNFSPSRENENILS | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
EC: 5.4.99.12
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Length: 253
Sequence Mass (Da): 28346
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A0A7C8AEG8 | MEPVKKRRSRRKKSRREGEVRRGTYIWPNLFTTANLFSGFFGIVNSINGNFELAAMAVFASCVFDFMDGKVARLTGGTSRFGVEYDSLADLVAFGVGPGLLMYLMALKPYGRLGWLAAFVFMACGALRLARFNVQVETTNKKYFVGLPIPVGASIIAASVLFMNHWNIAVQGSLIRLVLLGMTFVLGVFMISTMPFNSFKEVEFIKARPSFVVFGVIVLVSVVAVTPAFMLFLLLTIYAVSGPVRWVAWKIQGKKGFQEGLTTRQTAAPAPESISGEQQSLEQPGKPGENIEI | Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + CMP + H(+)
EC: 2.7.8.8
Subcellular Location: Membrane
Sequence Length: 293
Sequence Mass (Da): 32232
Location Topology: Multi-pass membrane protein
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A0A6S7IVV7 | MSSKHLQTGDPKPAFDKTKKFRIYSMKFCPFAQRARLVATAKGLKDYDIVNIKLRDDLPEWYTAINPARAVPAIEFPDGRAINESLIVADLLDELYPENQLQPKDPIEKAKQKLFVEKQGET | Function: Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA).
EC: 1.20.4.2
Catalytic Activity: 2 glutathione + H(+) + methylarsonate = glutathione disulfide + H2O + methylarsonous acid
Sequence Length: 122
Sequence Mass (Da): 13935
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A0A6S7GV76 | MAGKQSKEISFISKAYLLSYNIVQTLGWSYIFVISCQHFMSQNAITSKGLFAKVEVILKLFQTAAILEIIHCAIGIVPSSAFTTAMQVFSRLCTVWLFTVPDKEVQNNTSILLYLTAWTITEIIRYSFYACGLLNYLPYFLPWCRYTFFIILYPIGVTGEILTVIAAIPFVKKTGIYSLSLPNPMNISFSFLYFLYFALVIYLPAFLMLYTYMFRQRKKVLGKATQTSAKLD | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Catalytic Activity: a very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain (2E)-enoyl-CoA + H2O
EC: 4.2.1.134
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 232
Sequence Mass (Da): 26520
Location Topology: Multi-pass membrane protein
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A0A034WNG6 | MKVLTANEIREAFLGFFKEKDHLYVHSSSTIPLDDPTLLFANAGMNQFKPIFLGTADPNSEMAKWVRTTNTQKCIRAGGKHNDLDDVGKDVYHHTFFEMLGNWSFGDYFKKEICTWAWEFLTERMKLPKDRLYVTYFGGDKASGLEPDLECKQIWLDLGLCPEHILPGSMKDNFWEMGETGPCGPCSELHFDRIGGRSVPELVNVDDPDVLEIWNLVFIQYNRESDGSLKPLPKKHIDCGMGFERLVSVIQNKRSNYDTDLFVPLFKAIQEGTGAPEYAGRVGAEDVEGIDMAYRVLADHARTITIALADGGTPDNTGRGYVLRRILRRAVRYATEKLSAKPGFFGSLVHTVVDLLGDAFPEVRKNPQQIIDIINEEEAQFLKTLSRGRDLFNRTVAKLSNQNVIPGDLAWKLYDTYGFPVDLTQLMAEEKNLEINMEEYEQAKQAAYIMSQGKSTTKADEIDLDVHAISELQSKSIQITNDSFKYKYEAESENLDSPYKFTSCTAKILALRFGNQFVHKIEAGSKAGIILDQTNFYAESGGQIYDKGLFVKLNNVDDKFIVDAVYNRGGYILHIGVADGEFTVGDEIDLKIDTERRWLTMKNHSATHALNHSLLQVLGKETDQKGSLVVPDKLRFDFSSKSAMTIEQVAKAELLTRDIVYKNVPIYAKETKLANAKKIRGLRSVFDEVYPDPVRVISFGVNVEELENNLDSDAGEKTSVEFCGGTHLQRSGHMMEFVITSEEAIAKGIRRIVALTGPEAVKALEKYDQLHKQIQTLKTTIEDDKDGKSSKNYVRQIVELTEEVSQAIIPYVKKDEMRNLLKQLKKTLDDKERTLKAAVSVTVIEKTKEICQENPKATLLVKQFEAYNNTKALDGALKQVRALCPDAAALFLSVDPDSKKIFCLASVPKSAVNKGLKANEWVQQLSEVIGGKGGGKPESAQASGTNYENVDEVIRVATEFAKLKVGA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
EC: 6.1.1.7
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Sequence Length: 967
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Sequence Mass (Da): 108264
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Q7Q289 | MGKTSKDKRDIYYRLAKEEGWRARSAFKLIHIDEVFQIFDGVTRAVDLCAAPGSWSQVLSKRLYESRDPAERDEVKIIAVDLQTMGPLPGIIQLQGDITKLSTAEAIIEHFGDQQKAQLVICDGAPDVTGLHDIDEYIQSQLLLAALNITTHVLTPGGTFVAKIFRGKDTSLLYSQLRIFFERVTIAKPPSSRNSSIEAFVVCQDYRPPEGYVPQLINPMLDDVQVIACETSAPVNRSIVPFLVCGDLREFDSDMSYSLNIDPEKDYEYRDVVQKPLAPAYSEVLERMKTTSLKHGSIKVEADKKKD | Function: Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs.
Catalytic Activity: cytidine(32)/guanosine(34) in tRNA + 2 S-adenosyl-L-methionine = 2'-O-methylcytidine(32)/2'-O-methylguanosine(34) in tRNA + 2 H(+) + 2 S-adenosyl-L-homocysteine
EC: 2.1.1.205
Subcellular Location: Cytoplasm
Sequence Length: 307
Sequence Mass (Da): 34429
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A0A7D9IJK7 | GKPRPKPDISIQTSVAYGKDVTLKCSAIGTVKLTWYKSKRNGTRNDWQLMNAGEADHTFHRRTGLRETKRFLVIKKFNVSDNGVYICDLYRYYVNWRAHKEKYVGIKGFQKPNFTAFPKPLITVQPVSRFSIHLDYRVEGIPSPSITWYKINGDKIKVLSNCDKSKCINNDPNDHYLDITRTVFGKYYLSYPSDNATLKCVASNSLGSATKTFRLNMLAKPKIAKKNKENLSFVHVYKEGQELVCMVEEANPNQISFTWVAQLTGCTNADCKPNNSNWQVVTGTESGLEIITTNSKSTLILEKSEQHFFYRCTARNTVGEDNHIWKVVPVTESQPLKAVQSLVEVNEAENAELSCAVAKFISNQVYWSFNNVALQLGPRMKVDNSSSNGTVYNTLHITNVNVTDAGKYQCFGEFDGISEAAEIQLKVRELNAPSVSLKNLTRKQSSSFLVRCNVSGHPKPRITWKKDGEMLKVRGSVQGTDDCKSRKKAYGGFYILTLPPLTDYIKKLDPHTPLTEQTNKLPYDAEWEFPRNRLKFSRELGCGAFGKVFLADAMGIVAFDPRGSTKRRPSRRRFGGSIRRNHYVNNNKMTKVAVKTLKEDSGETEYKDLLSELKILIHVGEHKNIVNLLGACTKGRESELWVIIEFCSNGNLLQFLRNRRDIYETEWKGVSKDPNFQLTMTDLVIAAYQVARGMEFLASRLCIHRDLATRNILVTENYVIKIADFGLARDVGEESQYVKTSN | EC: 2.7.10.1
Subcellular Location: Cell membrane
Sequence Length: 742
Sequence Mass (Da): 84113
Location Topology: Single-pass type I membrane protein
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A0A165XSR5 | MEKIKVCIVDDNRELVALLDEYLSSQEDMEVIGVAYNGQECLNILNEKSPDVLVLDIIMPHLDGLAVLQKLKELNKAKKPNVIMLTAFGQEDVTKKAVDLGAAYFILKPFDMEQLAGNIRQVSGKPSPLMKNISLHKSGSAVSENKNDNLDASITSIIHEIGVPAHIKGYLYLREAISMVYNDIELLGSITKVLYPDIAKKFNTTASRVERAIRHAIEVAWSRGNIESISSLFGYTVSMSKAKPTNSEFIAMVADKLRLEHKAS | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with Spo0H (a sigma factor) to control the expression of some genes that are critical to the sporulation process. Repressor of abrB, activator of the spoIIa operon. Binds the DNA sequence 5'-TGNCGAA-3' (0A box).
Subcellular Location: Cytoplasm
Sequence Length: 264
Sequence Mass (Da): 29231
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A0A538PFH9 | MADLDDTRARRALIVELVRTRHIATQGDLRDLLRARGHDVTQATLSRDLAKLGARRVALPGGGTAYEVDGFTARTGEPAQLAAMAPLVLGIREGAAIVVIHTRPGAAQAVAALLDQVRLDSIIGSIAGDDTIFVVPERRVTPLALTRTLRRLLRLESA | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Function: Regulates arginine biosynthesis genes.
Subcellular Location: Cytoplasm
Sequence Length: 158
Sequence Mass (Da): 16915
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A0A523JSV9 | MSMQPAEKRAGSSGHQLRLPKPDGMKVTTRWVIIGCRGQLGTALVRQLEADPESEILAAVDLPELDVADPEAVVRLFDGLGGDADVVVNAAAFTHVDRCEREPESARRANADAPGLLARACDRVGCGLVHVSTDYVFSGEIDPEQARPQAYREDDPTGPNSEYGRSKLAGEERVREISGEFLIVRTSWVFGRGRNFVAAILGQAESRHRGEAKGALRVVDDQCGRPTYAVDLAGGIRSLCGLEAVGTYHLAGGGEASWWELARATLDSAGYTDVVVDRIRTSDLDLDAPRPAYSVLDCSKAAEQGVRLRDWRAALDAYLGSEDSPVQLQALS | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 332
Sequence Mass (Da): 35758
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A0A9E0L3X3 | MSGAAVVLAGGEGRRMGGGKPLRAWDGRPLLAQALGLARSYAPHVAVAVRDAGQVGQGAGIPLLFDPPDIGGPLAGLASALDFGRRRGAPWVQTLACDMPYLPADLSDQLAQALESGVGAVLPVSDGRVHPVCGLWRVGTRDRLEAYVASGRSSLRGFAEYVGLREVAWEVAGPDPFVNLNTLEDLAAYQPPAGPDRAPTEQSGAGSR | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytoplasm
Sequence Length: 208
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Sequence Mass (Da): 21515
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A0A535MUQ9 | MATTLQLAAGRVPPHDLDAEISVIGSVLLDPLSIAKVLQFLHPEDFYRENNGQIYRAALDLFAAGEPIDNVTLASQLQSMGLLERVGGRAQLASMQSAVPTAANIEYYGRIVKEKAYKRRLISAGGNIAGYGYDDSIEAEDAINQAQSLVFGVADDRDQRELARLYDLLGPAMERISLQMESGQGVVGIPSGFHDLDRMTGGFKDSDLIVVAGRPAMGKTSWILNVGLHAALEAHKSIAIFSLEMSKEQLTERLLTEQAQIDAQRMHRGLLSEAEFDRVSNALGPLGEAAIYIDDTPVMDELTLQLKARQAKMRHNIDMILLDYLQLMHGRARGDDNRVQEVSAISRALKGLARELRIPVVAISQLSRAPEQRPDKRPILSDLRESGCLAGDTCIYLVDEGREVRIGDLVGRTGYRVYAKDKQNSSLQARAVSNSFSTGEKPIFRLSTRDEGNIRATANHRFLTHSGWQRLDQLRPGDEIARSTFWDRVEKVEADGVDEVFDLTVDDLHNFLANDLIVHNSIEQDADLVMFLFRPEYYKSDEKPGVAEVHVAKHRNGPTGTIELKFRRDHTRFYNLETRRPEPGTE | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 586
Sequence Mass (Da): 65271
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A0A7K2AYC3 | MAVIGTTELIIILVIVLVIFGGAKLPKLARSLGQAQREFRKNAGDEVEESASSGSADTKNSDA | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 63
Sequence Mass (Da): 6588
Location Topology: Single-pass membrane protein
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A0A6G2K2Z9 | MPPVGGPPAERPPGGRPPAGRPPGGRRCGRTRRRRRLTVGILAEDVARVREATDIVGLISNTVALRKAGRRWQGLCPFHAEKTPSFSVNAEEGLYYCFGCRASGDAITFVRQTEGLDFTPTVELLAARADITLRYDNKGEAAQSGRRKKLIEAVAAAVEWYHERLLEHADAGAARRYLRSRGLTGDEVRAFRLGWAPAGWDALSRALRSKAPAEVLIEAGLARQNEWGRLTDHFRSRVLFPVFDVRGDPVGFGGRILPDADGPAGPKYKNTAESALYAKSRLLYGLNWAKDAIVSARDGAGEVVVCEGYTDVIGLHAAGLRHAVATCGTALTENHVQTLSRFTKRIVLAFDADAAGSAAADRIYQWEGKHELDVFVAELPDGADPDDLARRDPDLLRQTLAEPTVFFEYRIDRALEGVSEATASGRVRFAEQALEALDEHPDEVVRNQYLDYVAGRCSLDPDLLRPTVERHRTSRRARRGQTAGPGGEGATAAAGAEAGDPSIAEQILLLRAKDPQALPDWVSAELFESEAHQWIFVALLGAASLRALVDRAGDEVDAAVAHLAVREPPANPRAVIGRFVHDAATRRIAELRRAARQSGDADLGLRLRDTQLARDELRTGNWAPEVAERLAAMLAEDRSGSEELRR | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 646
Domain: Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
Sequence Mass (Da): 70391
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A0A7D9DZB1 | MAGHGIWFLPCCLTSLWIYIISFIFIIYVLSSTFRFYLKFLCLLVYYFIMILVTFAILMWTPGSKNNLHKMSKILKCTEWLWGIQYTVKGLENYKKDSNYVIVSNHQSSFDMHVLANFMPPKTTVLSKKEVLYIPMFGILFWLAGVLFIDRENRGKAINMMKKVADKIKQEKFNVWIFPEGTRHTGSKLLPFKKGAFHLAQQTQMPVLPVVVSNYENVVNLGKRWFTTGSIDITILPEVSTEGLESSDVEQLTEKVYSIMCNEYEKCIPSQQ | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 272
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da): 31537
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A0A0K4GXF0 | MKIYEKATRFFIGSLEAIMVICISIMFLLVLINVLMRFIFNSGIDIAEELPRFLFVWMIFIGAVVAIKDQSHIRVDLFINKMPVLGQQICQLVSQVLMLVCSITLIYGTWIESDILSTTYSPVLDVNMLLIFGISWLTGVCIFISVLINIISVFTKISLLQAKTLSSTSSREDK | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 174
Sequence Mass (Da): 19666
Location Topology: Multi-pass membrane protein
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Q3MQ22 | MAGSIPRKLWEGKIPAAFSLASYEVSSSKQPSPVYMMLPRSSYLSLFTSKMVEHFSHYMEEEKRGEVWFEFNGNPLRWHYPCGLLFDLHCDTTSDLPWPITVHFQNFPQGELIRCNSEKEIQAHYMSVIKEADQLKHKGQVINGMRETQHDQLWHGVKMDNFDEFWSINKQFMSGFETTDYFRFIPLRVYFQNRIIQKLFKPSNNENLTLNEALTICLPSFFANDKTLPLKVKVLTQGIEPPLTCSLQWLSENFSYADNFLHICVHQS | Function: Involved in autophagic vesicle formation. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. Involved in mitochondrial quality control after oxidative damage, and in subsequent cellular longevity. Plays a critical role in multiple aspects of lymphocyte development and is essential for both B and T lymphocyte survival and proliferation. Required for optimal processing and presentation of antigens for MHC II. Involved in the maintenance of axon morphology and membrane structures, as well as in normal adipocyte differentiation. Promotes primary ciliogenesis through removal of OFD1 from centriolar satellites and degradation of IFT20 via the autophagic pathway.
Subcellular Location: Preautophagosomal structure membrane
Sequence Length: 268
Sequence Mass (Da): 31361
Location Topology: Peripheral membrane protein
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A0A6B1E0L6 | MVKVHGRVTASPLQYGGGGGDYFWAAAEAAPDKTFIAYQGRELTFAQVNHLTAKTSAWLQSHCQSQPGDKVGILMPNCLPYVWTVLALMRLRVIIVPLNTRLTADELQWQLEKAQCKLVICAPETLAKAKSCTTKFLLFPPESQLHPPAAIDRFARPALAEDFAIIHTSGTSGRPKATVLSYGNIYHSALASAQRLGALPDDRWLCVLPLCHVGGLSIILRSLIYGTAVELLPAFDVDAVNRLLSEQPISLVSLVPTMLQRLLAAKQRGWNPRLRLILLGGEAARLSLIERCLAEQIPVAASYGLSEASSQVATALSQQLREKSGTVGKPLPGTQARIVDEQGRTLAANTAGEVLVKGATVMRGYYDDVAATNRALRAGWLRTGDIGYLDADGDLFIMQRRSDLIISGGENIYPAEVEAALRQHPALDDALVFGLPDEQWGQRVAALVQLKPGEIVAVNELIDFAGQRLARYKIPREYAFAKLPRSAAGKVNRSAARKTFHAAIARR | Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 5/7.
Function: Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA (OSB-CoA).
EC: 6.2.1.26
Catalytic Activity: 2-succinylbenzoate + ATP + CoA = 2-succinylbenzoyl-CoA + AMP + diphosphate
Sequence Length: 507
Sequence Mass (Da): 55094
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A0A6L7JL29 | MRWQQLKLHEHQSRQLLSDSGIPVPAARLAADPAAAARAAAELGGPVVIKAQVLSGGRGKAGGVKLASDPDGAAAAAAEILGLEIGGNLVENVMVAEAVDIAAEYYLAALPDRESGQLMVMASAAGGIEIETVAAQDPEAIRTVDCGVDSGLAPHQARRLAFQLDIPLPLLGDFIRIATATVDCLVSNDASLVEINPLVQSGDRLLAIDAKITIDDSALFRQPQLREMRNPEEETATEAEARNSGISYVKLDGTIGCMVNGAGLAMALLDVIVSEGGEPANFLDVGGGADAGQVAKAMNLILADPEVEVVLVNIFGGITRCDDVAHGIVQALDGLSRRVPLEIRLVGTNQAEGLKILREAGLNAHRDMLSAVRAAVALAG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
EC: 6.2.1.5
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Length: 380
Sequence Mass (Da): 39339
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A0A6S7HYC5 | MEWIAVTFSKASFFNGVIAITAGVVANTLSEWINFGPVSPFLLAIPFLIMSGMLILTNWDENYGGKSIRLAGPCIASLRLIVTNSKILLIGAVTSLFESVMFVFVFLWTPVLDPAQPPLGIVFSCFMACVMIGGLIFDAAISWKISPIRIIEVAIFLGLASNLASCFASANHPRKTFLAFLLMEFACGLYFPAMNWLRQRILPEAHHAGIINWFRVPLNITASIVLLVLHDTHSGEGITAIFALCSVLMMIAEVCTIKLAMSLNVGDFVSDGQDIENDNGGENLV | Function: Mediates high-affinity intracellular uptake of the rare oligo-element molybdenum.
Subcellular Location: Cell membrane
Sequence Length: 285
Sequence Mass (Da): 31008
Location Topology: Multi-pass membrane protein
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A0A6S7GLH0 | MRVRFMKRLWFYPKVMAFTIYTLTFNAFQSNSPVADCAFEPVIWLVDHFAGLLGRALVILVSLAISGVVVVFYIYVMPIVLEYDNILFIVCHLICGHWLLLNVAFHYYKAVSSSPGYTPSGKQALILKDIQVCTKCIQPKPPRTHHCSVCNKCILKMDHHCPWINNCVGHFNHRYFFLFCVYMCLGTIYVSFTLFPTFLDRIDFFAKNILKDYFNVGNAQPTLGHKKYFLRPKDLIVDEDKESVPSIVVFEFMLCSCVAVAVGALAGWHVMLISRGETSVEVYINRNTRKKLKKQGKKFLNPYNYGFIGNWKMVLGLGRGRGLWSIVMPSSHPPNGDGITWPQPLQSSGESIGTDKLAAFMA | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 362
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 41154
Location Topology: Multi-pass membrane protein
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A0A0A9Z6C9 | MSQHEVCGMIVAAMFAGQHTSTITTTWTMLHLMDKRNTKHLAKLHEEIDEFPAKLNYDNVMDEMPFAECCARESIRRDPPLMMLMRQVLKPIQLGKYTVPVGDIIACSPLLSHQDDEAFPNPREWDPDRNMKIIDGAFCGFGGGVHKCIGEKFGLLQVKTILATVFREYDFELLGPLPEPNYHTMVVGPTASQCRVRYIKKKKSSTSPIIGEEMM | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 215
Sequence Mass (Da): 24346
Location Topology: Peripheral membrane protein
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A0A6N6KSS5 | MSSRRRRAAERRRQKNEGSPPPVQGEPDFVLVGILQKPHGLRGEMLMRVMTDFPERLKPETKMYLGDEHEVVTIRSVREHNKGLLVAFEEFKGRNELDHIRNVPLFARASELPQLEEGEYYYHQLIGMQVVSDEGLEVGVLAEILETGANDVMVVRSEKYGEVLLPFMDEVFLGVDVEKKIVQVHLMEGLIDETA | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Subcellular Location: Cytoplasm
Sequence Length: 195
Domain: The PRC barrel domain binds ribosomal protein uS19.
Sequence Mass (Da): 22298
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A0A512TQP0 | MMKKIIIMFTILIAVVLIGIGTLFYYFQRLNTVNKENSYLIINSESSLEDISKQLQGKSIIKSKDTFLLYTKLNRFSNNIKGGNFIVKPNTSYKELSLKLQSSQSDFTVVTIPEGFSFYQIAERLEKNTSIKKEDFLGVRVSNLTTNSLVLNKTNIYYGLEGFLYPDTYYVPNGATEKEIANLMFDRFNSVFSDKYVDRAKELGLDINDVITIASLIEKEAANDSERSKIAGVIYNRIEKGIPLQIDASVIYAITKGESKMKKVLYDNLKVQDPYNTYVNKGLPPGPIASPGKPSIEAALYPEEHDYLYYVVNGSGGHVFSKTYEEHLNNVKKYIK | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 336
Sequence Mass (Da): 38067
Location Topology: Single-pass membrane protein
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A0A166C4P1 | MHQVVCATTNPAKIQAILQAFHEIFGEGSCHIASVAVESGVPEQPFGSEETRAGARNRVANARRLHPEADFWVAIEAGIDGDSTFSWVVIENTSQRGEARSATLPLPAVILQKVREGEALGPVMSRYTGIDEIGRKEGAIGVFTAGKLTRASVYHQAVILALSPFHNAVYQ | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
EC: 3.6.1.73
Catalytic Activity: H2O + ITP = H(+) + IDP + phosphate
Sequence Length: 171
Sequence Mass (Da): 18394
|
A0A2U2XDQ2 | MKQEKTKFCVVDAGNTRVKVIDFENGEVLSQVFISIEEKEKIKSIISSKKEVTSILSSVLNEEMRNWIADLLQPNVVLSNQTPLPIRIDTYRTPQTLGADRIANAVAANHYSKTTNSLVIDIGTCIKFDFVQEGKFIGGSISPGYGMRLKAMHEFTGGLPLLELEEQSQLIGDSTKNAMMSGVLNGIQAEIEGFINQYNQQYQPLTIFLTGGDLKRFDKELKNSIFADDYLTVKGLYLILKHNV | Cofactor: A monovalent cation. Ammonium or potassium.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
EC: 2.7.1.33
Subcellular Location: Cytoplasm
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Length: 244
Sequence Mass (Da): 27242
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A0A4Q2M013 | MSLNEYLKSVSRRWLMIVLLAALGAAGGYAMAAATPDVYRSTSSVLLTSENGGSAAELVQGTAYIENLVSSYVLLADSELVLDQVIDDLDLDMSTARLAGQITAGSPLNTTVIDLSVVDGTAEGAQRIARSVTTHLSLAVSEVSPTSPDGTPTVRLTTIQSASLPSFPIAPNTRLMVALGAAVGLVLGLVYAIIRGLVSQPITDPREIAHLTDDPVVGEVVLAKRDSTLPARVLIDPQGLEAESLRTLAANLTFLTVDGGLRSFVVTSASPGEAKSSIAASLALTLAESSQRVLLIDADLRRPTIATLTQLDDAVGLTGVLIGQYDLDVAVQRWAHDRLDVLTSGAVPPNPTQLLSSDSMQHLIEQASAEYDVIIIDSPPLLAVTDAAWIGRITDGALVVARYNKTTARALTHLFEKLESAGVRMLGVVISCVPRRTRARYGYVAEYAPKSKEAPRKGAAPRETPAPTSPPAHSKSAAKSPTAESVETAS | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 490
Sequence Mass (Da): 51429
Location Topology: Multi-pass membrane protein
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A0A0N5D713 | MVKSQEKRASNCFVIKRDGRHEDVSFDKISRRIKKLCYGLSPERVDHIEISQKVIAGLYKGVTTVELDNLAAEIAADLITKHPDYGFLASRITVSNMHKKIEKSFSKVAATLYFTKHPKSNRHMPLISKELFEIVQNNSNVLDSAIVHDRDYCYTYFGLKTLERSYLLKINGAVAERPQHMLMRTYQLMSERWFTHATPTLFNSGTCKPQMSSCFLLTMFDDSIEGIFETLKKCALISKNAGGIGLNIHCIRATGSAIAGTNGVSNGLVPMLRVFNSAARYVDQGGNKRPGAFAIYLEPWHSDIFEFLGLRKNVGDELERCRDLFLGLWVPDLFMERVRDDKTWSLMCPAESPGLHEVWGEEFERLYMKYEEEGRYREQIPARKLWEAIVCSQIETGVPYMVYKDTCNRKSNQKNLGTIKCSNLCTEIVEYSSPKEIAVCNLASIALSRFVTEERTFDFEALRQYCIDFYYMIVKKLFQITKVVTKNLNKIIDRNHYPVPETEFSNKRHRPIGIGVQGLADAFILMRYPFISEKARDLNKRIFETIYYAALEASCELAELYGPYETYHGSPVSKGILQFDMWDVTPSDQWDWKTLREKIAKNGIRNSLLIAPMPTASTAQILGNNESIEPYTTNVYTRNVLSGNFQIFNQHLVKDLINLNLWDEGMRMEIIKNKGSIQDITRIPEEVRNLYKTVWEMSQKGLKTGMYYLRTRPAVDAVQFTVDKTRLKKYFEKDLSTTSETTSDPTAATNPELCSKMESAVCVEFTIEGRTKEARKRRVYFVCLRYLRRMFRALVVAFGRQMSRPLARKIIAYAIKHPYLRNRILIPVGRSLHAISFRLRIKSIGLAIPSQTPTVSEQQAVEMASETLVETLIYLTTVSLIYAIYRSNPEKAKASDVERYVKENEERIHKFEEKMKEQDEIVMKIVKIIRESKLDDKNLLADKQKSQLLSFISDKMKTLIPGQD | Pathway: Genetic information processing; DNA replication.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
EC: 1.17.4.1
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Length: 964
Sequence Mass (Da): 110936
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A0A7L4QF22 | MSIEEQVLGRISPDKEYRSFIERIVDDLLKKLRSEAVKMGLEVEIMLVGSVAKDTYVLSPDIDIFILFPQKLPRDKLEKYGLELGKSIIDGQEKYAEHPYVHGEIQGLGIDLVPCYKLEDIAEMKSAVDRTPFHLEFVKKNLKPEQRDEVRLLKQFMKGLGVYGAEAKVEGFSGYLTELLIIKYGDFRTVLNNATQWTNGTTLWLEKKGRTKFKGHMVFYDPVDLKRNVASALSVDSYAIFIQACNDYLKEERIEFFFPRERNPIIMSEMEDMIALRGTSIVIASFNRPDIIDDNLYPQIRKTQEGLLSLLRERDFTIIDADFHVGDRISFVFELQDDVLPRCHRHVGPPVWMDHSERFLDKWEKSGLSPPFIDNGRWIVLAEREFTNALDLLAREAGKAALGSDFKQMKGYHVIGGNEVFGPGMEPVLSSLMDKRMNWEI | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded.
EC: 2.7.7.72
Catalytic Activity: a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate
Sequence Length: 441
Sequence Mass (Da): 50711
|
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