ids
stringlengths 6
10
| seqs
stringlengths 16
1.02k
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stringlengths 117
4.4k
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A0A1G8RVH3 | MRRVLTVLSPLLLVGVCLTPQDSSDGHVRFISRHSNKALEVQGATESNPCNLQLLYQGRSPNSGGDYGLLPYRPGLLTLQR | Catalytic Activity: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.
EC: 3.2.1.55
Subcellular Location: Secreted
Sequence Length: 81
Sequence Mass (Da): 8876
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A0A834H327 | MGLPDPHPFNFVDLNKHSDLQIDSRTLLLGAVFMLLLLISILSLVYFLYTCIRRSQSSASTLSPSPPPSTGLDKATINCLPIVQYGSSLSADSTCRVGECSICLAVFQVGDKVKVLPLCYHGFHSECVDEWFRSRPSCPLCRACVVRVDSLAQSV | 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: 155
Sequence Mass (Da): 16968
Location Topology: Single-pass membrane protein
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A0A3L6R4D9 | MRGECRAVEHVGVEQEFAQPMRMTVKEPGVDLHGGASKPEWSTRSSRHGARSGHQGDLQGRDGTLSASNGDPTVVPPTLPRGPQTWVHQPNRRAATLPRSVGASQTHEGHEAGSGLDDDDTGARVRASGSLPSFLLPPSVSSSVRLHSLLPLRLPAPNSRLDPSDLSSLGGARRRRMEGPPVALFDSLKAAKPFFLLAGPNVIESEEHVLKMAKHIKGITTKLGIPLVFKSSFDKANRTSSKSFRGPGLEEGLKCEAVGRVADIIQIPAFLCRQTDLLVAAAKTGKIINIKKGQFCAPSVMVNSAEKIRLAGNPNVMVYDLIVDPRNLEWLREANCPVVADITHALQQPAGRKLDGGGVASGGFRELIPCISRTSVAVGVDGIFMEVHDDPLKAPCDGPTQWV | Catalytic Activity: D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate
EC: 2.5.1.55
Subcellular Location: Cytoplasm
Sequence Length: 403
Sequence Mass (Da): 43089
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A0A1V6XWD2 | MLNFTASDMSRFAPRSDVRRGVEPRLLSIINLQLPRDYNSPLNHTVKTPRTPKMTASYPRPDFQRTSLNWNTLDGPWTFTFDDKDEGLSSQWHKTSLEGKPSHQIIVPYAFQTPASGVNLIEAHEVMWYERHITDIRTPDEKQKGNRLLLRFGAVDYECSVWVNGVLVGGHRGGHVPFDIDVSDALADGATEARLTLRVRDSPYDMTQPRGKQFWGPVPESIFYTPSGGIWLSVWLESVPAMRLLCGSGGTVLRSDDIEGGQLHAKVHVAGRQVGNTAKAEVEVSLGGMSVAKADGELLRDKTFVALDLGIKVTDAAVTDLKAKNQELFGVDGVWSRGVALWAPEHPTLYDITLRLFDAAGRLVDEVQTTTGMRSLSWQNGDGTFRLNGKPYFQMLFLDQGYWPGTGMTPPSSEALKTDIELAQKLGFNGCRKHQKVEDPRFYYWADRMGFLVWGEMANAYEFGTEYIERFTSEWTEAVKRDINHPSLITWTPLNESWGVSALKDNIEQRNHVRTLYYLTKTLDPSRPINDNCGWEHVKTDLTTFHDYSDSAELGAACTGMPAILEPKGGHEIFTKPIYSGYSGSSIVDKGARHTPGAPVICSEFGGVNIAPPKNSAAAGERDWGYTTASDPADFLVRFEKLVMAVVKPGHICGLVWTQLCDIEQEVNGLYTYDRQEKVPTEKVKAIMDAARDHYYHHVASHHSKGFRKLLDQYKHVVQR | Pathway: Glycan metabolism; N-glycan degradation.
EC: 3.2.1.25
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.
Sequence Length: 720
Sequence Mass (Da): 80616
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U1GNW8 | MPPPTKQVTRDSLLPSMRLAPDASPQIYRLTPTTVAKTGDLVSLSEAAVMRLVRSKTSIPVPQVLDAYIRTEDGSGHGCIIMEYVEGETLDKAWEACTPTQKDGIVKQLKSRLATDGPRTYAGLARSLRERRQNTWIDMVCRFIDALPHNHQIVLTHNDLAPRNILVREGRVVALLDWELAGFYPEHWEYVKTLFWPEWNSSWIKDGIVDRILDPYTLELACLLHARDIIW | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Chromosome
Sequence Length: 231
Sequence Mass (Da): 26314
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A0A1G0HYM7 | MKNLALAGLETAINTYLQLDPDTVARLPQLANKVIALCITDWHIQLFILPQKNTITLLSDYESEPDTKMQADLCSFINIAKHKGSTDSLFKNNLRIEGDAHTGEQLRDILSNMDIDWEEHLSKLTGDVVAHHVFQSFNSLANFAKRAKSRLCENITEYVQEEKRWSPGKKETDDFFYEIRDTRDAVERLEARLQCLEVGEQA | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Required for ubiquinone (coenzyme Q) biosynthesis. Binds hydrophobic ubiquinone biosynthetic intermediates via its SCP2 domain and is essential for the stability of the Ubi complex. May constitute a docking platform where Ubi enzymes assemble and access their SCP2-bound polyprenyl substrates.
Subcellular Location: Cytoplasm
Sequence Length: 202
Sequence Mass (Da): 23111
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U1I398 | MGPFDGMVGKGLKPLTAQKQKVHSQTIKTGPTTTSKHRSQPAQSTSKPSPPLSNGQGKTLNGNAPKPQKQASPAHSRSNEPKARIKEEKRSSSLKRSSPTVSTPRFDSDNSDEDAEVKSSKRRKVGEDACVDLSRRIRNIHSFSVLQDSGALPMIHAADVANLGTDEKPNPNYATFFTALTGDEDEAPVIELRYPSVSHKERYQMVQGKAGDDFKPLDEIIHVISTVAENYLLPSQAEPITNESSGLLRDLKRARLRGHKGEAGAQSKYVAGVEKYNALLDSLSKDGSIQKNLDELHSLKLPLVETILQQIYARTVSPHIHTLRAYENGTDNVYGELLPRFCSTIFKHTRLNSSHVFVDLGSGVGNVVLQAALQIGCESWGCEMMPNACELAALQHEEFIARCRLWGLAPGEVHLERGDFLQNEAIGKALKNADVVLINNQAFTPALNDKLIMHFLDLKEGCQIVSLKSFVPHGHKMQARNMGSPINVLDVRELEYFSNSVSWTDAPGRWYVQTKDSRKVEAFQRKMNGA | Function: Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone.
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: 530
Sequence Mass (Da): 58477
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A0A1G0HHW0 | MFVQVLKFNSIAKQGLSIIEQAGIHIAEHSTQQDGIILRSQQLHDYVFPDSVKVVVRAGAGVNNIPVAELTKKGIVVLNTPGANANAVKELVLTSMLMASRNIFPACQFVSSLDETGEGLEKTVEQAKKQFVGRELPGKILGVVGLGKIGLNVANCAISLGMRVLGYDPHISVENSWKLSANVERAHTMAELFYQADFLTLHVPLIEQTRHFISNKEIADMRRGMALFNFSRADVVDNQAILEAIQNKHLSCYACDFPDAKFKNIPNILMFPHLGASTIEAELNCAVMAANQLKAFLTTGEIINSVNFPETRLSPIKAHRVTVINDNIPSMVSHITNEFANANINIDELVNKSRQDVAYTVIDISTKPSADLLKKIEQINGVLRVRSLAHE | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.
Function: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
EC: 1.1.1.399
Catalytic Activity: (2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH
Sequence Length: 391
Sequence Mass (Da): 42931
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A0A1L6HAB7 | MQKNKELDRYKAVSSEEWVKCPECSAIFSVLEITDKKSCPYCDHYFRMTVGERINQLIDYKTFKLIEIDMETENIINFPGYSQKIKKLKNEYKQEGVTIGVGKINNKEIALGVMNSRFIMGTLNRVVGEKIIKLIDVAIKKSLPLLLVTVSGGARMQEGIFSLLQMARIQNKLNEYSKIKKPYLALLTDPTMGGVTASYATVADVILGEKGATVGFAGKRVIQNVTAEKLPEDFQSSEMMLSHGFIDQVVTRENTKDIISKILMLLEGKK | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
EC: 2.1.3.15
Subcellular Location: Cytoplasm
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Length: 270
Sequence Mass (Da): 30359
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A0A3L6T2P6 | MLVLGCSRLLIEAVVCGETAIWGPSPLSQALKRRRPAPALRPPHLRGAFLLSCCTSSARAGRCCPPPPRGLASECQAAAGRPELGLGLDRARRTLVPAEASADGVLAMGDAQTDGEGPRCVGCGGRVKTLFVQYSPGNIRLMKCDNCKAVADPYIECEFMIILIDLILHKTRAYRHILFNKLSMGSSVDKVIGDALLGNIIFMIMLFLGVRFILKLSFDITRYREVLFAVIISSYFKLFLFTMMVWEFPSSVIFIVEMFVLSSNVVALRGLNNMRPTKTRICTNYYSTQDLLIIARLQLVSDILRIGNQRSHIMDQVQLHIQELFGVQPGSFSVHLHRPEDFLIVFNAPADMLRVLNATYPPNTPFRLFFKPWRREAQAVVAEMNYLVRVALDGIPAHLWLLSTAQAALGPACDIVSMAPATVSKEDVSRFIVEARCIHPDLVPRERLVSLPDAPPSTRLLGYHVRLEILEVQDLRTSQAGQLAGAGPPSGGSGAGDGGVGGGAAGSAAAVGAHLNASWPGVTPGGAVHPSGASDGHYQVAGDTPGGWCSGAASGGPLVRTRHPEVALVTFDPMLVEVEVAVAFGGGPDRATSLDMLPAHLPPPGSLLGRPPWSGPVLQRIQFPVAHDSLGEWLTVTRKVRVASPLSETDDTAVAASAVVATAGSATGGAAPSTPLVLPPRVTISPAPTGTPDSRVPLGASPTLCPPAGTTPTAGEKEDLAGLARSLGDDATQDGSLVASVPSGQALEGAQPPITVDEGQQHSVPPSVSAIDVSHVNLLQLRSPGLDPVDEFVSSIQSTTQESVLHVPPIRRRSKLADRPAMPWRSKRLAAKSRGQPACPYTRASNVLMKKWGVTGEDHPPDATPGRCRTMTRSMDNLCRKIILRL | Function: Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 886
Sequence Mass (Da): 94402
Location Topology: Multi-pass membrane protein
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A0A7S3ITK3 | MSRQEDRMTFKERFQNSDLNAFYAVFDGHAGCEAAHFSKEVLGRRLEQHVNLKSEWGLNDSLRKVCKSIDDEFLQIANASRLKAGTTLLVAMLFSGKFTLANLGDSSAHLLKTTGQISKLTADHTPDREDEYNRIVGNNGFISKKDNISRVDGSIAVSRAIGDRQYKQYLISDPETYSYSIQ | Function: Enzyme with a broad specificity.
Subcellular Location: Membrane
Sequence Length: 182
Sequence Mass (Da): 20474
Location Topology: Peripheral membrane protein
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A0A7S0W267 | GSAAFNLFVITGLCMMALPSGETKQIDKYSVFMLTSAHSVIAYVWVVIIVSVNTKDVVDLWEALVTFAFMPWMVCWVYAADKEWFRTDNRVFIDDEEGKAALTQESGPPKHSSSANAESAEGSTPVPEGPNAPAAAPTADNPSGIDGRLSSASQNLANKSQELGGFIPVQQRNLDENGRPIKSLAPKANLSVAQRKREAMRTLVAPQTAVHHQFETMSMQRSALDGIPEDNLTRVHFQTPKVSVLENVGQACIGVIRTGPSEFPFKVNFHTKEGSAKPGVDYAEVSGVLAFPAGETYQEIQVGIVDDSTQWNAEKDFTVVLDLDGQENAAGHEVKLGQIHVCTVGIIDVDNPGEFCFTESAYVCLSTDSKVAMSIERRSGVTGEATVTVKPVAASAEAGQHFVDEEILVKFHQDQAAALVQMNLLHEGWKDSDPSTAKTLRFFVELVKPTPAEGAKVIPPGRAEVIVRWNEDAGGADEVEEPSWGAQFRLALAIENPEEASRTDLCVHYATIFWKLVAAIIPPPELKILGRDTNGWATFTTAIIMIGFVTTIINDLASIFGCIVGLEDSITAITLVALGTSLPDTIASMMSARADTNADNSIGNITGSNSVNVFLGIGLPWSIAALYWEVTPPTEAWKERYADWLRTDIGMQYAEKGGFVVIGGDLAFYTLIFVILACSTIGLLIFRRFVMGYELGGSKITSTAHGYICVSFWFIYVIVSIIKVYAPEGTFIDVGR | Catalytic Activity: Ca(2+)(in) + 3 Na(+)(out) = Ca(2+)(out) + 3 Na(+)(in)
Subcellular Location: Cell membrane
Sequence Length: 736
Sequence Mass (Da): 79739
Location Topology: Multi-pass membrane protein
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A0A091IP88 | MPVTVGPYGQSQPSCFDRVKMGFMMGFAVGMAAGALFGTFSCLRIGMRGRELMGGVGKTMMQSGGTFGTFMAIGMGIRC | Function: Has antibacterial activity against a variety of bacteria including S.aureus, P.aeruginosa and M.tuberculosis. Acts by inducing bacterial membrane breakage.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 79
Sequence Mass (Da): 8275
Location Topology: Single-pass membrane protein
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B0DVP6 | MAAAGLTILAQCSHIWHLEGQRPVTGLTHNLPKFKIDVVSLSGSLASTQLPSNLALGNYLTRHEIIALHLAKSLGGAEFYPACSQLTVGASGTGVPDPLGGHLPGACSDNDPGIFDSQVFDACAPYIHLPRSSCRCICERWHFHSWKRNHNRIFKGNGNPDRWCHWDIDDV | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
EC: 3.2.1.4
Subcellular Location: Secreted
Sequence Length: 171
Domain: Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.
Sequence Mass (Da): 18663
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U1HVN5 | MPLILDSPSESSFETPPDPLEERRRLHHDADVVIVGAGILGSALAVALADQGRSVILLERSLKEPDRIVGELLQPGGVEALEKLGLRHCLEEIDAIPVKGYEVIYYGEEVAIPYPGNAHGSKASPEKTSKPEGRSFHHGRFVSRLRSAALIHPNITTFETEVTSIIKSTHTSEVLGVESLTNKTKPEFFFGSLTVIADGYASKFRKSYLPHTPKTRSKFWGLELIDADLPLPEHGHVILGDGAPVLLYQIGTHETRALVDIPDNTPTASVKVGGVKAHLRNVVLPSLPQQVQPSFAAALDKGALRSMPNSFLPSATNKTPGLILLGDAMNMRHALTGGGMTVALNDVVLLRSLLSPHHVPDLADSKAVLHQMRSFHWQRKNLTAVINILAQALYSLFAANDPYLKYLQMGCFRYFQLGGQCIDGPVGLLAGIIRQPSPDARGLEVDQAAPGSPKMRLPQDKLAVIKRYIHAAQGAIVAIAWLLCIIIFTRQGHSDGRVGWYFGLCWLSIPILVYLVMVPMWPRARRFSNVYAFATLDALSVVFWLSAWAAMASYVSQGIGKGDNEEATGCDNFKFGSPGRCKISQGVIVLGVVLMLCFAATAFISFKAVMHYKRTGEMPNPTMGNENFAKQTQDAFSSNIRNDDPFDDNHADLDARQGGTSGYGPARRSEDDEYTLLQNDHDEINQAQPTQPAGPLGYGPNSGAIMHDYDTSYAGSYGQNIPDGGYGNAPYSR | EC: 1.14.14.17
Subcellular Location: Microsome membrane
Sequence Length: 733
Sequence Mass (Da): 79801
Location Topology: Multi-pass membrane protein
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A0A136KL23 | MTDSTTSQNANLNEQTPTATEAENPAVTENTMVVLETTEGTIKLELFNSTMPITAGNFLKLVEDEFYNGVIFHRVIPNFMVQGGDPTGTGMGGPGYKIKDEFTTNNKNERGTISMANAGPNTGGSQFFINVVNNNFLDSKHPVFGKVVEGMEIVDKIVAVETDGADRPIEEVRIEKAYKVTTPE | 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: 184
Sequence Mass (Da): 20010
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A0A023I0E2 | FIGSSMSMLIRLELGTCNSVMFNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNYLVPLMMGSPDXAFPRMNN | 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: 72
Sequence Mass (Da): 8123
Location Topology: Multi-pass membrane protein
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O15972 | MKVLLVLAFVGLAFVAAEDKRLTCTAFSDSLIEKMNDQINLELHASYLYHGYARYFDRDDVALSGFADFFKHASSEEKDHADKLMEYMNTRGCRFLLKDITYKDVCDKINEKKPAELSSACICEFTAAATGGDPSSCSANRPEWFNGKQAMENALTIEHHVNDELLKLHRSTNDPHFEKFLEDNYLDEQVNAIKELSDYITILKRTGDGLGEYLFDKDLDSKY | Function: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.
EC: 1.16.3.1
Catalytic Activity: 4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O
Sequence Length: 223
Sequence Mass (Da): 25425
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A0A3L6SPR8 | MRRRSTRRYLLCIGRDAAHGHVEVIRDGVAGRHGSPILAATLRVQTEESPSSPGLTHHGGPAAPQRARDAELVRDAEAAREDVAPRAGTAAPLVARAAAVEQKASLLRLAVEAGLEEMQLRVVPPGRAGGGAGAGLGCAGARGSVLPRRKVPAAAPALEEDIEGFSIRNREATEGSQSMSGVGRRRQGRKRRDSRFDAPVARMALPTPVVTGIAAGGAALLLAAVLVAAWFVRRRRRARRDRSSDTGSSEAPPTLAEWGRFGRTSSAPEFHGARQFLLEELAHATKNFAEANLVGAGSFGLVYKGLLLDGTVVAIKRRAGAPRQDFADEVRRLSEIWHRNVVTLIGYCQEGGLQMLVFEYLPNGSVSGHLYDTGKEPMTRLEFKQRLSIAIGAAKGLNHLHTLAPPLIHRDFKTSNVLVDENFIAKVSDAGIDRLLRGFEGAAPPNVSVYQDTEVHSLAQLSESSDVYSFGVFLLELITGREAAGLIPPELKEPLAYWMEAHFSSNELIDPRLGGSFTSEGMTELVGLAFQCLSPSARRRHRMRLVAAELDRILEKEMTLTTVMGDGTAIVTLGSQLFTS | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cell membrane
Sequence Length: 580
Sequence Mass (Da): 62446
Location Topology: Single-pass membrane protein
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A0A0D6WNR6 | MSAIAATVTSTGEAVQFWILGTVAVIGALATILMKKAVHSALSLAGTMIILAVFYLANGAYFLGVVQVIVYTGAIMMLFLFVVMLVGVTAADSLKETIKGQRWLAALCGLGFGILLIGGIGNAGISHFNGLGKVNSAGHVEGLAQLIFTKYVFAFELTGALLITATVGAMVLTHRERTERAATQRELAERRVREGVQLP | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 199
Sequence Mass (Da): 20954
Location Topology: Multi-pass membrane protein
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U1GT46 | MTVVAPPPNPSLVAIILVIQARSGPRFVYHYPPSPLSRAGLDSFEEGPSSYENSSVPDDDITSTSNEELLADEYGRGRTKLKRADFTDEEDENSSSPGTDDKQHGGWRVPWENLLGLDASALERLLMPSDRSWHKRKFEVGFNDLVFVGWPIFIREDGTWRKKRRKERVNTVKAEDNRVDSSLEVVHKGEYATEDELNHERHVDLENSPATNPASSQADESREMTIFNVVFVLNPPILEYSLRVNEMYDHVVKKLGKALKWEQARANYVWQQSDLILKAKTQARHKRSSITALYATLLRISSLASAIATIYDNISRSMIAAITLTPTVPISLQIPPVTSTSVLPSSTDPPSARTQPGVWLTTATAGSSDEIADTDHPQSAMSLAKHFTLLLLDKESKILADISQSGGPLAAALAHYIRVSSPTKSFAKISALHSISLPDIQLLAQHLVDWRRARAIPPLHQRDTYIVSPNADLKKLSTAVKSYESAFPTLPSLPKMLQALSGIPRPYSSLIPSKDHKQAYFRILAWLLRGGWVTQLRSFAFVRIDSSIKIAVKEQTKTDRNGKGPSDRDNPLEASHDTITSLHLAKRPSMVSRVSSDIRSSTSSHSNPKMNSIILQPARASPTESKWLDYIADHLHELLSADLHEDEVLELQQCWPTFTRYFNGMEPLEKIPVREGLKRKAAWDLLNRLGLFESLSNEAARQRDTQQRILVGFRHW | Function: Mediates inactivation of the TORC1 complex in response to amino acid starvation. Required for meiotic nuclear division.
Subcellular Location: Vacuole membrane
Sequence Length: 716
Sequence Mass (Da): 80211
Location Topology: Peripheral membrane protein
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A0A834LQT6 | MGMGKMTDFTVVLIVTTTLVLIFSPSAYSQSDNLGDILGAPASSYSSFYSLLESSTGTSRILQDQANTQQGLTLFVPNNNAFATDPVPWGTLSPAQIQSLILFHAVPQYYGISALNTLSQLSPVVTMAGGQYTLNFTVVSQALYLNSGWTIAKVVDVVKLNTSTLQIYQIDAVLKPEAIFGEYDEDRVATTPYLESLDRHKGFRGTRSVAFVASNKEIISSGRICFLF | Function: May be a cell surface adhesion protein.
Subcellular Location: Cell membrane
Sequence Length: 228
Sequence Mass (Da): 24761
Location Topology: Lipid-anchor
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A0A1H1MIT6 | MPPSPQVVVVGSIMQDLTFACAEFPRAGETIMARLAGGQGGKGSNQAIACGRTGMKTVFIGAMGRDGFAGQVTAFYRREKIGCHLVLKAGQSTGTAVILLNREGQNQIVIEPGANAALAPADVPRSLLAKARVVVTQLESNLATTAHVLRVARQAGVTTILNPAPMRTDFGPALLRHVDILIPNESEFVALVRALPGIRRRGFDERALQAMPREALHGLCRQLGVPTLIVTLGRRGCFISERSGHHFIPAHRGMRVVDTTGAGDAFCGGFAAGLVRHKGEVVAAARLGTAVAALSITKPGAAFAMPTRSELQRFLRKTGAA | Cofactor: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 2/2.
Function: Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
EC: 2.7.1.15
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+)
Sequence Length: 321
Sequence Mass (Da): 33794
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A0A522W9X2 | MAGRLEFPGAGVEPDIYVLALPLAHGADALALLAFLGGLSAATGMVIVETIALATMFSNYVVMPVLLHTVIAASPATGNLAGIVLTVRRLAILGCIFLGYLYARLIGEGFTLVGIGLMSFAAVAQFAPAMLGGLFWRAGNKAGALTGLSLGFMVWFYTLFLPSLARSGVLPASFVEAGPFGLALLKPYALFGLSGLAPVAHAMVWSILANFGTYVLVSLITRQGAMERIQASLFVDAFGAIPGGAAQFWRGNATVSDLQALAGRFVGTERADRAFSHFAATRGLKPGEDEATPELVGFTERLLAGAIGTATARVVVASVAKGEIVSLNEVMAILDENSQVIAYSHKLEAKSRELEVASAELRDAYQKLTELHRLKDEFIATVTHELRTPLTSIRSFSEILFDNPGIDIDQRQEFLGVVIKESERLTRLINQVLDLAKLEGGTAAWDLSEIDVIPAVRDAAESMGQLFKDKGVALVLDMPAGPIMLTTDRDRFSQVVINLLSNAVKFCEPRSGRVEVGVTADGEGVTVEVADNGPGVPDWAHQKIFEKFQQVGDTLTAKPEGTGLGLTISHNIVTRLGGRIWVESEPDQGAVFSFFLPSHIIAPQEAATEEKA | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 612
Sequence Mass (Da): 65151
Location Topology: Multi-pass membrane protein
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Q8USS4 | MRVMGTQRNCQQWWIWGILGFWMLMIYNVGGNLWVTVYYGVPVWKEAKTTLFCASDAKAYEKEVHNVWATHACVPTDPSPQEIVLENVTETFNMWKNDMVDQMHEDIISLWDQSLKPCVKLTPLCVTLNCSAANNTVAEMKGEIKNCSFHISTEMRDKRQKEFALFNILDIVPLNNENNNTKNFSDYRLISCNTSTITQACPKVSWDPIPIHYCAPAGYAILKCNNKTFNGTGPCNNVSTVQCTHGIKPVVSTQLLLNGSLAEKEIVIRSENISDNAKTIIVHLNESVEIECRRPNNNTGKSVRIGPGQTFFATGGIIGEIRRAHCDINGTKWTETLQKISEKLRGYFKKTIIFAPSSGGDPEITTHSFNCRGEFFYCNTSQLFNSTYRANSTNSTSNSNITLPCRIKQIINMWQGVGRAMYAPPIAGNIICKSNITGVLLTYDGGEGVKENETFRPAGGNMKDNWRSELYKYKVVEIKPLGIAPTKAKRRVVEREKRAALGAVFLGFLGAAGSTMGAASITLTVQARQLLSGIVQQQSNLLRAIEAQQHMLQLTVWGIKQLQARVLAIERYLRDQQLLGIWGCSGKIICTTAVPWNSSWSNKNEEDIWGNMT | Subcellular Location: Cell membrane
Sequence Length: 613
Domain: The 17 amino acids long immunosuppressive region is present in many retroviral envelope proteins. Synthetic peptides derived from this relatively conserved sequence inhibit immune function in vitro and in vivo.
Sequence Mass (Da): 68555
Location Topology: Peripheral membrane protein
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A0A1G0KBC7 | MSDEDRRPPGGGPLARGAHPRSPFGVLTLALNVIGTVLIIIIAVAVNSDIIGRNLFNQPIAGVTEFVGLSIVAVVFLQMANTLREGRHISNDLIMAWVGGSHPRVALFFYGVFHLIGVFLMCFIVWYVVPIFRENYVGNFYKGTAGVVQIPVWPFMLVVLVGGTAAAIQYLLLAWGEFRRFLGKKTQ | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 187
Sequence Mass (Da): 20514
Location Topology: Multi-pass membrane protein
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A0A4Y7JW28 | MLVHVSTAYVCGEESGVISEKPFLMGKTLNQTSEILDIEAELKHMRNRLEELKGLQVSKSEETEAMENFGLERSRAFGWPNTYVFTKAMGEMLIGKYGGNLPIVIIRPIIITGTYKEPFPGWIEGARYKS | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 130
Sequence Mass (Da): 14645
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A0A0S1SXA0 | MELLLKLGINWQLLIAQIVNFAIVMGVLGFFLYRPILNLLDARAERIRKAMEDAKRVENQMQELHKLREEEMKRLDKESGEYFDRMRKEAQALHEEMMATAKKEAETTLQNALKRIDEERRVMMEDVMKTVNTVIVRMTEKLLEREFTPADQKRIQENLVAELPQSMR | 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: 168
Sequence Mass (Da): 19921
Location Topology: Single-pass membrane protein
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A0A554MR30 | MGRDFLLSIMEEFVSKLGLDWRLFTAQLVNFLLLLFILKITVYKPVLNMLADRSRKIEQGIKDAEASTKRLSEINQLEQSRLAEATAKAEELMRNMEKNAVAKEVALVAKAEAKAADLVRNAEARMLASQKESEALLLGQAKELIRSVVFKIAKKDPEAFDARLVEEAFSELKKK | 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: 175
Sequence Mass (Da): 19739
Location Topology: Single-pass membrane protein
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A0A1G0KCP0 | MTDLRVVLLLAGVLILALIWMLEMRRERNAQRHRTVLRQRSTPSYHDENEPVSRDESPEPRAETLDLPPMSPTGTGRRADAESAAPAPADFIAIHVQGAARSTFALSAVFNAAESAGLVFGDRQIFHMPGVNSSAAPLFSMANMLEPGTFSRDATAQPTRGLTLFMCLPTETDVNMVFDLMLHTADLLATSLGGVVNGMDRQPLSQDRIAALRQKIAGRRT | Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 221
Sequence Mass (Da): 24095
Location Topology: Single-pass type I membrane protein
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J9C3L5 | VYTIEHAMAALYAAGVDNCLIELTGPEMPILDGSAKLISEKIEEVGIVEQNEDALVYVVRQRSTIKDESTTASIKVVPDSDFSIDVMIEFNSAVLANQFATLESLEDFNKDIASCRTFVFVREIEELVKHNLIKGGDLNNAIVIYDSPIAQEELDRIADMMNVPRKKVTEFGFINDNGLVFKNEPARHKLLDVIGDMALIGRRIQGRIIATCP | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 2/6.
EC: 3.5.1.108
Catalytic Activity: a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate
Sequence Length: 213
Sequence Mass (Da): 23644
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A0A072Q4F7 | MSTNATPTSHQTAFAVGNPYTYYDILQLARGGAEGSNFPKDGIKAAYRRALLLHHPDKTSHTSVEPSSSSQTQPPTPKYSIDEIVSAYEVLSDSKKRAEYDKALKRNEKDMQGQHRTHIGIEMYDLEDLVYDEDKDIWSKGCRCGDEHGYILTVLDLENESQHGEVYVGCRGCSLFIKVLFAMDEG | Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Function: Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2.
Subcellular Location: Cytoplasm
Sequence Length: 186
Sequence Mass (Da): 20840
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A0A8A5RKX5 | TLFILFGVLTCMVGTSLSMLIRTELGSPGSLIGNDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLFLLIMSSVVESGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTVINMRPKGMTLDRMPLFVWAVVITAILLLLSLPVLAGAISMLLTDRNLNTSFFDPAGGGDPI | 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: 213
Sequence Mass (Da): 22767
Location Topology: Multi-pass membrane protein
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A0A136JLZ8 | MKVLAIDPGYDRVGLAILEKITTGEILHHSECLETDRSTDFNDRILDIGNRIENLINLHQPDTLAIETLFFNKNIKTAIGVAEARGMIIYLAKKYNCTVFEFGPQEIKIATTGYGKSDKKAVIDMVKRLVKNVPTNAMDDEYDAIAVGITCIAHKGIGR | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
EC: 3.1.21.10
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Subcellular Location: Cytoplasm
Sequence Length: 159
Sequence Mass (Da): 17652
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A0A2W6ZCC5 | MPLAPAAPPLRPLQVWVLLAAAAVSSSVSLVLELMLATQASYLLGDHTLATGIVVGTFLAAMGLGAWLSQFLACGPNPFARLLRLFLLVELLLSPLCLLAPLGLFALFGAGGPVWLGLVVLTVLVGVLGGMEVPLLTRLLETQQHLRTALARVLALDYLGALVGALLFPLVLLPWLGLLPTAGLLALVPLLSCLVICRVFPLGRRWRWLVAGALPLVALVAWAVLPLGDRIEDSLYDDPVVGRLQSRHQRIVLTRRRDDLRLFLDGNLQFSSLDEYRYHEALVHPVMAFHPQPRRVLLLGAGDGLALREVLRWPGVQRVDLVELDPAMLQLARRHPFLRRLNQGSLDDPRVHLHSGDAFERVRHLPGAYDVVIADFPDPATAALARLYSVSFYGRLLELLAPHGRLVTQASTPFFTPKVLASIQATFEQLPLTTRAYSVDVPSFGPWGFVIAYRAGQTLMAAPLPFTARWADDAQIARLFPLPRDLRLPPGERVQPNRLLRPVLAEYQRQSRWSGP | Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Subcellular Location: Cell membrane
Sequence Length: 516
Sequence Mass (Da): 56740
Location Topology: Multi-pass membrane protein
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A0A286QUY7 | RAELGNPGSLVGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVDTGAGTGWTVYPPLAANIAHGGSAVDFAIFSLHLAGVSSILGAVNFITTVINMRSPGMTFDRVPLFVWSVIITAVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL | 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: 197
Sequence Mass (Da): 21055
Location Topology: Multi-pass membrane protein
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A0A4Y7IRZ2 | MVYQDTDPDLAMAEIDAIRGLLQNSSLSLVSVFLAAITPLVSMGFPNGLPGCINAEVIFDSMANLIEQELQKFSNPEKVMMLFSAHGVPVSYVEDTGDPYRISDGGLHHIDHATAES | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
EC: 4.98.1.1
Subcellular Location: Plastid
Sequence Length: 117
Sequence Mass (Da): 12638
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R5ZX57 | MSFSFKQFHIDDAHCAMKVGTDGVLLGAWANVCEADRILDVGCGCGLIALMAAQRNRAARVVGVELDAAAAADALANVQHSPFVSNVEIVCADVLQYAADCGLAFDSILSNPPYHEESLLPPASQRAKARHTQGGGLTFAALLRVVEHLLNPATPKATFSAILPMSAVAGFVAMAAVHGLQLTRRTDVVTRKGRPCKRVLLEFCRTPQSLVHTTLSLVGDDGTRAEAYADLCKDFYL | Function: Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
Catalytic Activity: adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine
EC: 2.1.1.223
Subcellular Location: Cytoplasm
Sequence Length: 237
Sequence Mass (Da): 25250
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B0D106 | MPTINKILVGSRVVGVGREDARLALGMATVVPEFLDWFQAHQGTIDTSSVDVINFLPSEGGRGAVAVKDIPEGHVLFTIPRDLTLSTRTSSLPLRFGMGAWKNAKLHEGWAGLILCMMWEAAQGSSSKWSGYFDILPTSFDTPMFWTEEELAELRGTSVVEKIGRADAEKDYKEKLIPAINSRPELFLPRDIHTRYSVEMYHVMGSRILSRSFNVEKWAPDEEEVGDGAGDVSMGSGMDVDLPDGAPAPPTHSSHGTDDLEHEGGEEEEQEDSSDIAMVPMADILNARYGSENAKLFYEENYLKMISTRPIKGGEQIWNTYGDLPNAELLRRYGHVDVIQLPNGGQGNPGDVAEIRADLIVSVAAEQHSLSTDDTHERIDWWLEEGGDDVFDLYFDLEIPPSIISVIRLLLLPDEEWEKIKEKAKPPKPKMDAVALTVLHEVLQRRLKEYPTSIQDDEQLLMTAPSLNLRHAIIVRLGEKKILDGILTKTAAALAMESNTKKRKTTHEDRPAAASTLKKSKRQA | Function: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that monomethylates 60S ribosomal protein L42.
EC: 2.1.1.-
Subcellular Location: Nucleus
Sequence Length: 524
Sequence Mass (Da): 58220
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A0A133V2G6 | MNFNFKRWIVVGFLAALMIFSFVHLSSAGSDYKVLTTSDSGFFYGIARSTDKLDGLPDTYELSHPPQGKSVGGSTQGQPLMLVMFYRGLHTLNPTVSLMDASQYFSPFLFMLALIGIFLAGRELGGNFAGGASAFFMSVLVGSIYWTKIGAFDREISLVFFGAWMFYLLAKLFNSTKQEIWKYSILSGLVYGLFLITWPGALFIAPILILPLVLILLERAVSGLGISVWGVFLLWFGNRVSVGSGLFLAIGVAAFLIGLFKIATNWDALSKIENRIFASIRSHLHLIGGIAVMFLVTTLLAITIGGYKHDFWIGFAQRIGGFLGLGGGGGGLASPRVATEMQVPGNYLNSLNVQLFRNVLLLRITMIFSGFAILKALWTRKKRELLLITWLIIPAAMATTQARFFRVFWPMWPVLAAYGIWTVIWIGRRLMKTPTLITSKWLDRFKQPIVIALVAIVFMTPFIYNARANATNTRPIPHGGTRPSVYHSLVDSYRWLRNNSPENAVVAVEWSYGHLLTGTARRRSVTDGATTSGIWENRELPPPDYVKLDVNGDGKITEVDDTDGDGKWEVAGGRRPDMQNLYNADENEFAQTIQTYRDNYGLKIDYVVFNLYRISSALWSSSTNEKNLDNYKNLDGNTLLLQFDNENVWYNTQSQLAYYQEENTTRYPLILTYELSTGGMGYSLPQISPEMKVLQIFYRGGELYALRWADLAYIPMVARVSWSYQVPAYLDVVYESLHGYAAVGKINHYPSLKTPGNGASINDNTPTLEWTSSIGGEKYELLVDDNSDVSSPEILENTSSTSYTTSLPLADGNYYWSVRAFNEDNESFGWSDVWSFKIDTVAPNTPVLSSPSDNSTLSDNTPTFQWNEVSGVKDYELLLDNNPGFTSPEVQTVITENTYTPKESLDDDNYWWKIQARDAAGNKSPWSDAWSFTLQT | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
EC: 2.4.99.21
Subcellular Location: Membrane
Sequence Length: 936
Sequence Mass (Da): 104762
Location Topology: Multi-pass membrane protein
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A0A136KJ57 | MTSNSFEKEIKPLELKKDYPLAKHTTWKVGGPAEYFVEVKTKQDLIKSIIAARKADIAVTIIGWGSNILVSDKGIKGLVIKNSYSEINILEECSYSPDKTNYARLKQVDSSQYYSFTDIDYIEETSVARKVNISSGTPLPLTINTLIRQGITGLQWFSGIPGTIGGAVYNNIHGGSHFIAEFVSRVEVLDENNNLTWIDKEQLDFAYDYSIFQTNTNYIVSVEFCFPIGDKDKALAASTEWARKKSLQPSNSAGCTYQNITETEQEKLGLESNSWGYIIDKILGLKGKQIGQAKISDKHAAFIETYPGATSEDVIKVMELIASTSKEKLGIIPHPEIFFLGFNDDELKHIK | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 351
Sequence Mass (Da): 39161
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A0A0C3KN39 | MQTRRYRSTRVASLRWGPSSLPLKGSWPAKFSIPSFVSAIHFDAVVVKLYFAESLTNSANGAQIWWKRGDLNRSGSHQINYELAMCLKTYRVIADLGAGAENATRQVLNIFHMKMLVVEVVSVEIDSKTLKEAVSDAMGDWDANLATTHFLIGSIINSHSFIYVVSRMGSTGSSVQGFVNSEFPDIIARICKHAFIPLAVGFGVATQVHFDAVVEAGAHGVVVGSGIVYLIKEAPAGQVPQVVENFCRGLKGSSPSNSSTAGVQSSQYHYPVVAAISRPTGMRLLLPRFGQYVPEALFDCLIELEEAHNATQNDPMF | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Length: 317
Sequence Mass (Da): 34510
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A0A0Q3X7Y3 | MQMPTNLWSRFGRDVGNVVEALYGDLPPPIMLIGHSMGGAIAVHTAVANLVPSLLGLCMIDVVEGVDRLDKDLTIGQMQACPGPAVKGVGDDTKAG | Function: Demethylates proteins that have been reversibly carboxymethylated. Demethylates PPP2CB (in vitro) and PPP2CA. Binding to PPP2CA displaces the manganese ion and inactivates the enzyme.
EC: 3.1.1.89
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine methyl ester + H2O = [phosphatase 2A protein]-C-terminal L-leucine + H(+) + methanol
Sequence Length: 96
Sequence Mass (Da): 9985
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A0A2G2KG86 | MFKIKYLFLIFFVAQLSCQDKQTLQKKAVKDTNAPEKKTITHKEFKPIISQKTVVPFLTQYASKHKENNVLIKTRLGDIHIQLFNETPLHRANFLLLIKEGYFNTSCFHRVVKDFIIQAGQSDKNSTRELRKKIGTYKIPPEFTKHKHHKGALSSARRWNENPKKLSDAYEFFIVQKKMGLHHLDHEHTVFGKVIKGLDVVDKIAQEAIDKGEWPIKDINLIVSIY | 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: 226
Sequence Mass (Da): 26325
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D6NVC2 | 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 | Subcellular Location: Cell membrane
Sequence Length: 854
Domain: The 17 amino acids long immunosuppressive region is present in many retroviral envelope proteins. Synthetic peptides derived from this relatively conserved sequence inhibit immune function in vitro and in vivo.
Sequence Mass (Da): 96541
Location Topology: Peripheral membrane protein
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A0A842HH31 | MHDFFFYLFSALTVLAALLVVINPDAVNSAVFMIVSFVGTAALFLLLDAFFLAILQVLVYAGAVMVLFLFIIMLLDVERSSRLRPDTISVVASVVATLLLIFGMAYLFLTGPDATATALAAAPDVPGAANPMGYATASRAFGYGLFTKYMLPFQVSGILLLVAMIGVIVLSKRLGGPGSGAPSASEIRKAEVRES | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 195
Sequence Mass (Da): 20621
Location Topology: Multi-pass membrane protein
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A0A4Y7JN64 | MYLSMLHHVRFYLPEMYPKLRRILFLDDDIVVQRDLTGLWDIDMDGKVNDAVEPCFGSFHHYVQYMNFSHPSIKESFSPEACARAYGMNFFDLDAWRKEKCTEHSTTAGRLW | Pathway: Glycan metabolism; pectin biosynthesis.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 112
Sequence Mass (Da): 13301
Location Topology: Single-pass type II membrane protein
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A0A0C3JWP2 | MSTDNQPLAAKQNLTWPKYLEIRRQKRRWETAVTIPFTLLGLAGGAAYFGSIETDATKVIMGIDPLFFYGGCTIACMGLGYLIGPVVGSACWRLTHRRTMGLIEEKDREFHKRIVKNRVDPTAQSATNPVPDYYGEKIGSLHQYRQWLRDQAKFRRKAQFDEQ | Function: Component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner.
Subcellular Location: Membrane
Sequence Length: 163
Sequence Mass (Da): 18657
Location Topology: Multi-pass membrane protein
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A0A3L6PU88 | MRRQGGPHPGEAHRARRVAAGRHLPRRRRRAAARRKAKKELMMMNSSSDGDASKTAERKAMKELGLQRARHFGWSNTYVFTKAMGEMLLGQLRCDMPVVVMRPSIITSVRADPLPGWMQGTRTIDTLIIGYAKQNLSCFLGDLSVVVDVVPGDMVVNAMMAAMVEHSEEKGAAAVPVYHATSSLRNPATYSVLYEAGRRHFYENPRVGKNGEIVPTREMCFFTTIARFHLYMLLTFKLPLEILHLVNLLLCGLFSRLYNDLNLN | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 264
Sequence Mass (Da): 29717
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A0A084GWH2 | MKPIFITGFMGTGKTTVGKVLAEKLGCPVLDTDQMIEHAAGKQIKDIFKEDGEEVFRSLETQMIERAPSENAVITTGGGLPVRKVNREKMKESGIVIFLQTDLDVIFERVQQDENRPLASKASKEELSSLYESRVNAYEDCTIKIKTEGKTIEQLADELIERIKELETRHTS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Length: 172
Sequence Mass (Da): 19318
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A0A7Z2NNG4 | MAPQPQRRSCCRDTIMKVAIYGCGQLARMMAEAAHSLGVSVCFLAEPNEDTRCVEHLGTVIRIDPSNPKASLLGVSDIDAITVEREQIDLSVLQRLNEEVPIYPPIEALAKTQHRLKEKSLLTDLNLPTSPWVSSCVEPSIIAKSLRFPVVIKHPTQGYDGKSQWHAKTLDETVHITSKLTDTAVLIEERINFEFEVSIIAARDQFGDIVCYPVVENQHQNSILISSIAPAPLISAEQQHTLERYASTLLQELNYVGVLTVECFVTQNGILINEIAPRVHNSGHWTLQSGLCSQFEQHIRAVAGMSLVHQSFPQVYGLVNILGPVEQDQIPTNKQFEPVWYGKENRPKRKLGHIALWAATETELLREQDALLAQLYPKEAVRTASLCSDKALPGAHVIDKGLTQTLGR | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
Function: Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
EC: 6.3.4.18
Catalytic Activity: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP + hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + ADP + 2 H(+) + phosphate
Sequence Length: 408
Sequence Mass (Da): 45340
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A0A841EHN5 | MKRIIFFLFCISFISCKKDLRLFDQDPKTFLIQYGTENPETKVKVHTVGGDFVIKLHTETPLHRANFIRNVKAGYYVSRMFYRNIYRMGIQGGGEYMDQLDFLVPPEYRPEFTHKRGAVAMARYDEGNPDRASSPTEFYIITNEAEARQLNGLYVVFGEVIEGMEVVDAIQAGKEYNERPAIPVFFRIDVVEE | 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: 193
Sequence Mass (Da): 22371
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A0A7S3IT34 | NMLNRLFQRSIAQTSRLTFMQCRSFASFQKAVLKPLPYAINGLEPIISQNLMEFHYGKHHQTYVTNLNNLLEQASVALEGGDHQKYVDLSQAIKFNGGGHLNHEFFWESLIPVANGGGVLPKEGSDLYAGIVDAFGSFDAMVAHFSANTAAVQGSGWGWLAYNKTSDEIEFHTTANQDRLSDKGAHLTPLLTIDIWEHAYYLDYQNVRPNFMTEIWKVVNWEKVSERYLAARN | Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
EC: 1.15.1.1
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Length: 233
Sequence Mass (Da): 26346
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A0A1B7X964 | MQACDTLLFAEIIVTQDETRSIIHNGGIAITDGTIVCIDAADTVRSQYTSENVMELGSSLLMPGLINSHTHAAMTLLRGAADDLPLMDWLNNHIFPVEQNLKAEQVELGALLACAEMTRYGTTSFTDMYLIEDATYKAVDQSGLRVLGGEALFMFPSPAYPDFDTGIALVRELESKWRNNPRIRQAVMPHAVYTTTPEILTICREVAEELDLPIHIHLAETQTETQACIESFGKRPVEYAHSLGLLSERTTVAHAVDLTDDEITLLAETGTNVAHNPESNMKLASGMAPIEKMLAKGVNITLGTDGAASNNALNMFTEMASCAFLHKVQHLDPTVASAQTVLDMATCNGSRSMRQPDIGSLAVGQQADIIAIDLTQPNLLPMHNPVSQLVYATTGAEVHMSMVAGDILYQNGKYLRIDYPALIEAAKDVAKWVQKKIQKRS | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
EC: 3.5.4.28
Catalytic Activity: H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine
Sequence Length: 441
Sequence Mass (Da): 48083
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A0A0H2NAY1 | MKILEISDLEVQELVSREEARQQSTLSMLASENIQTKNSLLAQSSLFANKTLEGYPGKRFHAGGQLADQLELLCIDRAKALFGCQYANVQAHSGSQANHIVYNALLAPGDAVLALSLDAGGHLSHGAKVNQTSALYRFQHYGVDDGDLIDYAQIQELADRHQPKIILCGGSSYTREIDFSAIADIANSVGAYLFVDMAHFAGQVAAGRYSNPLEYADIATTTLYKSLAGPRGAIILAQSSDIGARIDRSLFPGYQGTPSINNIAAKAICLHEASTQEFKSYIDLSISLAKQLCFTLKNRGLELVTDGTDTSMVLVDLRQQMISGKQASDLLERCGIIVNHNVAPNDTRSVMEGSAVRLSTNVMARRRIKDDNAQIIFDIIADVFISLIQEKPFDFKAASETVAHICQRHPVASVLSIEHMEPELSVVA | Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
EC: 2.1.2.1
Subcellular Location: Cytoplasm
Sequence Length: 428
Sequence Mass (Da): 46528
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A0A1D9J498 | MQPLVILSIVALVVVAIIAIVVWSIVFIECKKLR | Function: Enhances virion budding by targeting host CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its host receptor CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to promote the degradation of host IKBKB, leading to NF-kappa-B down-regulation and subsequent apoptosis. Ion channel activity has also been suggested, however, formation of cation-selective channel has been reconstituted ex-vivo in lipid bilayers. It is thus unsure that this activity plays a role in vivo.
Subcellular Location: Host membrane
Sequence Length: 34
Sequence Mass (Da): 3778
Location Topology: Single-pass type I membrane protein
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A0A7S0VB52 | DGGKGVSIGRRQPDAIDLPTVHETDLAGDEEELTVQVGGEGAADEEADAANNILYVETGTGRAFKRKKKDKDGEKAAPSDRVSDADRNLKSFLDLMATLVASSFIFCQGMLGGISLLLFYLQVNQDDRSFMRVYSPIAADGQKAFVFLSTVSMVGAFDKWSKDQMAAWHLRGGYLQGIDAVIIVCYTICFVFTLLCVPLEDVMHASHLRVREWYRWELSADFQDRYATWGVFHAIRCVFGILGWVMSAWETRNYLHNAPNKPLHDVYEKLFGKKVEKEA | Function: Component of the transition zone in primary cilia. Required for ciliogenesis.
Subcellular Location: Cell projection
Sequence Length: 279
Sequence Mass (Da): 31247
Location Topology: Multi-pass membrane protein
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A0A3L6QQ97 | MASAEGPVDNNIDSTQPAESSANLSHGKKVYTNYSVTGIPGDGRCLFRSVAHGACIRSGKPIPNEDLQRKLADELRTMVADEFIKRRAETEWFVEGDFDTYVSQIRKPHVWGGEPELFMASHVLQMPITVYMHDKEAGGLIAIAEYGQEYGTEAPIQVLYHGYGHYEALQIPGKGGPRRRDTGSKLRSTLLCFCGEEQMARIRHMPGAAKGTEICTRFPTKTFQLLSPVRCPCWRFRVINIIARSDAEDYLTVDVLLESKAAYSFLPLKPWLYRVLVKYCWQHRLMGRVFLSSCVHPHFSSTYDTHTLSVLVFAESYFEVEPIKLTCRTLDGYHETGGSVKREETQLRRSAVASSGRSGKTGELQSLNPRPENLTRNRNPSQFADPEITLAIHTQRAESFL | Function: Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
EC: 3.4.19.12
Subcellular Location: Cytoplasm
Sequence Length: 401
Sequence Mass (Da): 45139
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A0A0C3NGN3 | MHKQGMKAWVVPLAIATSAWVKWSIGLGDYSGHATPPMFGDYEAQRHWMELAIHLAPQQWYTYDLQYWGLDYPPLTAYISWLCGKVGSLIDPSWFAFEESRGIETYNSKLFMRSTVVALDILVYVPALYAFTRIWHKSRSLRTQHASLLILLFQPALLLVDFGHFQYNSVMLGLTLLALNSFAVGLDLLGAVCFVLSLGFKQMALYYAPVIGSYLLGKCVFLGPVQGTRLFIRLAVVTLSSFILLFAPFLPPIAPLSTFFAAISRIFPFARGLFEDKVANFWCFTNVTLVKWKQLFLGKESRLIRLSAALTVAGFLPAVFGLLWGSFKTRLRTHPQVVSRE | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 341
Sequence Mass (Da): 38483
Location Topology: Multi-pass membrane protein
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A0A517P622 | MNVTVMGLGVHGGGAGAVRSFCRRGARVTLTDRRTEQELAEPLAALGCEPAVFKLGGHDPADFLNADLVVASPAVPYRHEFLEAARSVGVPVTTELAVAAAALPANVATAAVTGSNGKSTTCALLHAMLTARHARLGRGAAWLAGNGGGSLLDRMDDVRPGDAVVWEVSSFQLEYLAEVQFRADAAVVTNFAPNHLDWHGTLAAYRSAKQALLEHLRPADTAVLNAADLDVRTWPTAARRVLFETRICPLPGVHNAQNAAAAEAAALALDCTAADAEAGLKTAVLPPHRLHCVAERGRVRFVDDSAATTPESVIAALEALPAPLFLIAGGADKGADLSAAAAAIAARTAGAYFLGTTGPRWRELTLAANPRHPAIHCGDLPAAFAAALTAAEPTGGTVLLSPGCSSLDQFASFEARGAAFAALAGSYSASSSRE | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
EC: 6.3.2.9
Subcellular Location: Cytoplasm
Sequence Length: 434
Sequence Mass (Da): 44622
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A0A1G0KDD4 | MKIVADSAIPFLQHFFSPLGDIAAVDGRDIGPAQVRDADALLVRTVTRVNEALLTGSRVRFVGSPTSGTDHLDIAWLDRAGIGWAAAPGCNARSVAEYVLSALLVLTESAGRELDCMRAGIIGCGHVGSEVARMLRGVGVECVLHDPPLQATTGGAEYQPLSAVLNADIVSLHVPLTRSGPFATAGLVDAAFLDALKPEAILVNTARGEVVDETALLGALRTRPGLRAIIDVWTNEPGVNTELLQEADIATPHIAGYSTDGRLRATAVIADALRHISGAQQNETALPDLPHPGVPAVHIAPGMDRMTAVQLAVLSSYDARSDAIVLRRLAPGDAAALSSGFSEARNTYPLRREFSAHSVLLPPDTLPDTRAALAALGFQVREDGR | Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5.
Function: Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Catalytic Activity: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + H(+) + NADH
EC: 1.1.1.290
Subcellular Location: Cytoplasm
Sequence Length: 385
Sequence Mass (Da): 40445
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A0A653SUE1 | MERSRAPVDRWREALALAVLALFSLGLALVGRVSLVGATDHALVWPLSGFVVLWLLHRGPRAGVVDALAVAVASAVALAWTGVSATESAIGGVLVLVQPLVTVALLRRFAPGLARPRGQRVSLGSLAVLGRLALSLVGGVLATVATLLLVSVVGDTGLSWSVGLLWVLRDLAGAFVAISVGLVIAQYRTGGAARGPAGRLHRGSRVEMVGVLGLSSAIFAATFVYEGLPLSFPLLIATGWLALRFDMLVTTAHTAVFGGAITAATLLGHGPFAAVGTPVEAASFVQGFVLLMGASGLVVSAERAQVHALNAELVRAAAANRDQADLLQEMIDAMAEGVMVVDDTGEVLASNPALDRLLATGEGRHTERLQGLMGHRLDGTRMAEDERPSRRALAGERVVREQVLYRADGLPDRVLAATALPLPDHTEAERRRAMILIEDVTADHDRRADLVTFAQMVAHDLRNPLSSILGWTGLVGKRFEETQEISATELGGYLRRTGEAARRMDDLIEHLLDRATRDVEPQDAEVDLDDVLRQVVRERGIGDLVEVAGMPVLRADPGMLHQLVDNLLANAVKFARPGVVHSICCTSRMADGGVVVSIADNGRGVPAGQHEQIFAEGHRAHASLVDGTGLGLAVCRRIVGRHGGTIRAVDDLDGPGAVFEIVVPMERVVSLPQRVPQRVLPAAWRIEERVGPGAAPQR | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 698
Sequence Mass (Da): 73896
Location Topology: Multi-pass membrane protein
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A0A678PCT7 | MLNRIKKQGLDITPRILIITRLLPDAVGTTCGQHLEKVYGTEHCHILRVPFRTEKGIVRKWISRFEVWPYLETYTEDVANELAKELEASQILLLETTVMETLLPLC | Function: Sucrose-cleaving enzyme that provides UDP-glucose and fructose for various metabolic pathways.
EC: 2.4.1.13
Catalytic Activity: an NDP-alpha-D-glucose + D-fructose = a ribonucleoside 5'-diphosphate + H(+) + sucrose
Sequence Length: 106
Sequence Mass (Da): 12262
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U1GV44 | MRFHGAISALLLVASHYTCACPTQIDEREAAAHLSPILKGRDVTINTYDYVPTNGPLTWHKTPGNGLCKSGTRQSPILLGNEIHQTGVGAVQFSAPNAAGKLEHKGTGIEVKEVKGTLKYAARTYELDNFHFHTPSEHRIHKEHYPVEMHMVHRDTNGNNTLVLGFVIQLSTKQYSSLPHVALAKVGQISPGQHVMTTTLQFDEIAYYTSHQRFYSYGGSLTTPPCTQDIQWLVGTEPLHMDVGTYNALKHAVKYNSRIIQNSPGSTNVIQLAC | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 274
Sequence Mass (Da): 30257
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Q4RY65 | MERVQHMTKSAIRRASQIEVNPQAKRNLQELFVNFTLILICLLLIYIIVLLSS | Function: Reversibly inhibits the activity of ATP2A2 in cardiac sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Modulates the contractility of the heart muscle in response to physiological stimuli via its effects on ATP2A2. Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in the heart muscle. The degree of ATP2A2 inhibition depends on the oligomeric state of PLN.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 53
Sequence Mass (Da): 6169
Location Topology: Single-pass membrane protein
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A0A0X8HCA3 | MAPGRPERDARHERRPIPLLAWXATRFDPTRIGKQGAGRDHSDSGSSYEGIALPPPLQGAIAKRRAEFIAGRLCARRALWLLDGRNATPGMNEDRSPCWPVDCVGAITHNDGWAAALVAPRQAYLGLGLDAERLLDAAQALRLARRVLTPEEVARLERLPESEAGLMVTATFSLKESLFKALYPVVGQMFHFQAAELVSWHGVGAARLRLLNNLGSGWTAGREVVGEACLHEGRLLSLVSLPARVHDSFGT | Pathway: Siderophore biosynthesis; enterobactin biosynthesis.
Function: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo-domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-forms which make them competent for the activation of 2,3-dihydroxybenzoate (DHB) and L-serine, respectively.
Catalytic Activity: apo-[aryl-carrier protein] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[aryl-carrier protein]
Sequence Length: 251
Sequence Mass (Da): 27318
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L2GWA9 | MSSELKREKIEIDYYADKSILSSFIHFFTDNNNEPKYLNMVSRKKISLDLNDIAIHDHMLMQRLKNNFATYLRMLYEIIDGVNTPSDVAMIHRLERMKEKYPGVDATKIFPPSLMRDYLFRIVPHTQYTLGIRMLRSDKIGHFITTRGIVTKVSHTRPSIKVAVYVCDSCGSETYQQINNQEFSLLAVCQSEKCKTMKIRGTLSLITRVSKFEPFVSICLQEMQGDTPEGCIPRVVNIEMKEADVRPGDCIYVCGVLMARQVFGLMNEIYLEGFGIAECKTKGTDELMLDEVVDDQIGDENQIPDEIKWDGDINEADRANFTVQNLVASFAPHIYGMHDVKKILLLMLIGSPSIQKSDGMRIRGDLNVMLMGDPGIAKSELLKYCMGLSKRGVYTAGRGSSGVGLTASVLRDPFTKEFVLEAGALVLSDKGICCLDEMDKMDENDRLSLHEVLEQQSISINKAGINVRLNARCCVLGAANFKRGFYDEKKSLEHNTGLPVSLISRFDVIVILRDDRDENKDRELADYVARQHLKESDTNDHSAALSQTDLKNFVQKAKTLNPRIPSHLNDRIVNAYTDARDKYERLTPRFLLSLIRLCMAHARLRLSDEVNEGDVEESARLLEVSKLHKTKEKKKEVSSKYQIYNQIMKMKADRTRPLRLEDLVRNINYDEQTILNVIKEFEENGIWVVEDGELQIFD | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 698
Sequence Mass (Da): 79592
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A0A2W0HDT1 | MKFPVRLPRGLTKRFIFLGLWIFLLPMTLIFMLAVFLSQQTLENQSDDQTFEAARALSVQTRQVFDHQIDMLETFVFDYRNDENLERLDERAAQHTFREPVFSSLALYDAGGSEAVPDEAETDENENTMIEDPAVRQVFEETVWRRSTFVKSITEPGGHARIFISVPVQEADHQPITGALIGEINPSYFYHLIQTSTIGERGWNLLVTSDGTVYTDTQENRYRNDSVKDEAIFSYLSRGRMGAYRGDFLDSDSVAGYAPVERLPFYAVTIQPESQAGAPIATLQQVLSSGWTVLFLAGLVLLGVSARWIVTPVRKLTDQAMSYAEGESWHLQVMKEEDEIRTLTKAMQFMADDLQEKERFLQRILASFPYGVITTDSDGIITSVNREGAELLNSRPKVLTGRPVETVPSKGLSRHVRALCSRKRPFSKESEEFPYVNHTGQKLVIKVSTTPLQNEKRERIGVLTTFWNHTDYRKLEQHIQRSEHLAAIGQMTAGLAHEVKNPLGTIQMAGDLIEAEMDGLKKKHRLNSPAVSMIEEASGDIQEEARRLNELVTRFLKLSKPHKDEETSLNVGETVEEVARLISHQMKRADITCNVYHKAEQLTVKGDRNQIIQAFLNLSLNALEAMKETESGVLSITVSREKDQAKIVFHDSGDGIPASKLNRIFNPFFSTKQEGTGLGLSITHDLINEHKGSIEVESEFGKGSEFTVRLPLEPDRTERKEAN | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 723
Sequence Mass (Da): 81611
Location Topology: Multi-pass membrane protein
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A0A0K8MB21 | MPELPEVEIVCREMRQALLTQTIQKVEVRERRLRFLIPPAFEKNLEHLTISSLQRRAKYILVGFQGTSDTLVIHLGMSGRISLLSSAESTLCHKHEHVIFTFTSGKEMRFFDPRRFGSMVLMTTPTSLFHKIGPEPLSEDFSVITLKDSLLNKKSSIKSALLNQHIIAGLGNIYVSEALHKAQIHPERLAKDLNLYECDALVSAIKKILQRAIAAGGSTLRDHQRTNGEAGSFQKQFAVYNQEGKNCPNCQESVIERILQANRSTYFCKKCQH | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
EC: 3.2.2.23
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Length: 273
Sequence Mass (Da): 30892
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S4T2Y5 | AEMLANIDLKYFNESTRKKIEKIRPLLIDGTASLSPGMMMGMFNMLSTVLGVSILNLGQKRYTKTTYWWDGLQSSDDFALIVNAPNHEGIQAGVDRFYRTCKLVGINMSKKKSYVNRTGTFEFTSFFYRYGFVANFSMELPSFGVSGINESADMSIGVTVIKNNMINNDLGPATAQMALQLFIKDYRYTYRCHRGDTQIQTRRSFELKKLWEQTRSKAGLLVSDGGPNLYNIRNLHIPEVCLKWELMDEDYQGRLCNPLNPFVSHKEIESVNNAVVM | Function: RNA-dependent RNA polymerase which is responsible for replication and transcription of virus RNA segments. The transcription of viral mRNAs occurs by a unique mechanism called cap-snatching. 5' methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides by PA. In turn, these short capped RNAs are used as primers by PB1 for transcription of viral mRNAs. During virus replication, PB1 initiates RNA synthesis and copy vRNA into complementary RNA (cRNA) which in turn serves as a template for the production of more vRNAs.
EC: 2.7.7.48
Subcellular Location: Cytoplasm
Sequence Length: 277
Sequence Mass (Da): 31573
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A0A2X2YMN2 | MHPAITDKPSSKKPMEGNIMRIGIPKERLTNETRVAATPKTVEQLLKLGFTVAVESGAGQLASFDDKAFTEAGAEIVEGNAVWQSEIILKVNAPEDDEIPLLNAGTTLVSFLWPAQNPELLQKLAERNVTVMAMDSVPRISRAQSLDALSSMANIAGYRAIVEAAHEFGRFFTGQITAAGKVPPAKVMVIGAGVAGLAAIGAANSLGAIVRAFDTRPEVKEQVQSMGAEFLELDFKEEAGSGDGYAKVMSEAFIKAEMELFAAQAKEVDIIVTTALIPGKPAPTLITREMVDSMKSGSVIVDLAAQNGGNCEYTVAGQVNHDRQWREGYRLHRSAGSSADAILPALRH | Function: The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane.
EC: 7.1.1.1
Catalytic Activity: H(+)(in) + NAD(+) + NADPH = H(+)(out) + NADH + NADP(+)
Sequence Length: 348
Sequence Mass (Da): 37100
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A0A0C1SAH3 | MRLCDKDIIHQLKSGRISISPYPKVERISGVTVDFHLGNEVRIFRKKKIFPYIDLSQLSKKISNNSLEDMISRRVLLKDCENILLNPSEIILAITYEHLSLPSNVVGWIDGKSSFARLGLMIHVSSNRIDPGWSGKIVLEIVNLGKFPLLLKPNMVICEISFEEISQSSLRPYNSKKESKYHNQFHPSISFISG | Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.
Function: Catalyzes the deamination of dCTP to dUTP.
EC: 3.5.4.13
Catalytic Activity: dCTP + H(+) + H2O = dUTP + NH4(+)
Sequence Length: 194
Sequence Mass (Da): 22095
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F9ZBX5 | MLNIAVILAGGSGQRAGGGIPKQFKKINDKTILEYSLEKFNSAPSIDEITVVIHPEWRQECEHILSDCRISKVKHLLDGGKERYHSVLAALKFYAGRPCNLLIHDAVRPLVTRRIIEEVITELQTYKAVNVAIPATDTIIEVDPTHTYVSRIPDRNILYQVQTPQGFHNQTLQEAYALALKDPDFKTTDDCSVVKKYLPQEEIKIVKGETYNMKFTYKEDIIILEQLLKNEGKCYV | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 2.7.7.60
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Length: 236
Sequence Mass (Da): 26828
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A0A177DX04 | MTSDIEDNPYNVCFIGAGFVGATTAAVLALKNPSTQFTVVDNDRGRIAAWNSMELPVQEPGLLEIVQSVSHWHAACVGSKIVSPESNNCVDGQPTHDKFNPQRNQSNVRNQEVCVSMHSKPNLRFSTDIREAIRTADMLFITVNTPSKMSPMEHEWDLSYFDAVLELVIDASMGSTIIVEKSTVPCGNALRISQMVQSKAEPNKSFTILSNPEFLSAGSAVADLLDPYSVVIGSPSSTPRSDPNTLSLVRLYDSWIPDERIRLMSTSSSELVKIANNAFEAQRISSINSLTVLCERLGANIKDISHSLGMNPNIGPRFLQAGVGFGGSCLRKDTLGLSGIATDISMPEVADYWRQVVVINDFQVQRFTKRVCQYASESPSRDVAILGFAFKKDTNDPRNSIAKDVILALLSQGANVALHDPLVSADAIRSLLPPAHEVQICRTPYEACQGAETIAILNDSKEYTDLDWNRISANMEGKKRVVVDGRDVIDAGRLAGLGLIVEKLGKPSHMDGIM | Pathway: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.
EC: 1.1.1.22
Catalytic Activity: H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate
Sequence Length: 514
Sequence Mass (Da): 56025
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A0A1W9VP60 | MIKMVVFLGNPGNQYQKTRHNIGWIFEKLIRNGLTPSTKFKAQYYKSTKDVVYLLPQTLMNNSGESVIKAMQFFKIKIDEILVIHDDLETVFGSFKLKNGGGLAGHNGLRSIATLTGSKDFHRLALGISRPKYGSVSSYVLGRFTQEEEAELELFLTGVVTYFNSYISGDDKNVGKKIAILQQIKE | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
EC: 3.1.1.29
Subcellular Location: Cytoplasm
Sequence Length: 186
Sequence Mass (Da): 20903
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A0A1G1LVA8 | MDLIGQVKSFITKGALIKRRDHVLLGVSGGPDSTALLSILENLRNDLGFRLTVCHVNHGLRTTALRDEIFVKKICRDLGIKCLFVKLKPLKGSSEETARDKRLAAFFKIAHQQKANTIALAHTQDDLAETVLMRIIRGSGLRGLPSILPKRMMQGFSLIRPLLSVKRRNVLAYLNEKRIPYKIDPTNRQTKFLRNRIRLELLPLLERKYNSNIKESLANLSLIAALDYEYLNSQTHKIFHSLKARTKDKIIIPLKRINKLPRSLQRMIFYQAIEALKGDTRAITHAHILEIEGLIENKTAQARGHLPQGILFQKEKGRLSVTLEK | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
EC: 6.3.4.19
Subcellular Location: Cytoplasm
Sequence Length: 325
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Sequence Mass (Da): 37026
|
A0A4R3N1H3 | MSPADGTIAGMESPLPAFDPGSDADAGITAAAALLAQGRLVGLPTETVYGLAADARNPEAVRAIFTLKQRPADHPLIVHIGSVEELHAWAAAVPPAALALARAFWPGPLTLVLPARPDVPRVVTGGLDTVALRMPAHPIALALLRRFGRGVAAPSANRHLHVSPTTAEHVRAEFGDALPLVLDGGPCTVGIESTIVDVSTDPPRILRPGRISAAEIAACLQRDVDLRPAAGTRSPGLMKRHYSPRAAVVCAPPAAVQTQVEACLARGLRTAQLSALPPAVAHPALLWLDAGNSVETRMQRLYALLREADARGAEVIVAELPEGDGTAEALRDRLLRAAGQGSVPSS | Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine.
Catalytic Activity: ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-threonylcarbamoyladenylate
EC: 2.7.7.87
Subcellular Location: Cytoplasm
Sequence Length: 346
Sequence Mass (Da): 35929
|
H3CH89 | SQVRVITDHRVPVPASSVAAHCREEDVLVAVKQDFLGNGQLIHPTDLTLGGCVARPASDRILGFQTELHGCNSTSWMTEDALVYSFLLVYLPTPIGNTVILKTNPAEVLIECLYQRRHYVSSNALRPTWMTFAAMMQAEKQQHFSLRLTTEDWQSPRQSNVFFLSDVIRIEAAVLRGFHVPLRIYVDSCAATVGPNPDSQPRYPFIANHGCLNDSKQTGAKSVFLQRSQEDKLQFQLKAFRFHQNQPGNNSIYITCHLKAMTLSAPVDSQHKACSFLTEASRWVASDGDNVVCRCCETSCDERKRKRRLAADVVSQWEGRASLEVILLEEDAPEL | PTM: Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.
Function: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP3 is essential for sperm binding and zona matrix formation.
Subcellular Location: Zona pellucida
Sequence Length: 335
Domain: The ZP domain is involved in the polymerization of the ZP proteins to form the zona pellucida.
Sequence Mass (Da): 37578
Location Topology: Single-pass type I membrane protein
|
A0A2S7TPU8 | MIPQSFIDDLLYRLDIADVVGRYVQLKAAGANLQGLCPFHNEKSPSFTVSPSKQFYHCFGCGAHGNAVGFVMEHLGLTFPEAVENLAGNLGIDVPYEKGMDVPAEVRSEREELVELLTRAANYYKAQLKKSPVAIDYLKNRGLTGQVAARYGMGYAPDAYQNLEAVVENYASNTQLDLAGLTKISDSNRRYDAFRGRIMFPIRNAKGQVIGFGGRVLGDEKPKYLNSPETPVFSKGHEVYGLFEARQAIHKMGYALVTEGYMDVVALAQWGFENAVATLGTAVTPDHVLKLFKQTDRLVFAFDGDGAGQKAAWRALQACLPHVSENKRADFIFLPAEHDPDSFIRTEGPDASRPWWRKPRPCQNFWRATWSATTPCSKLRAVRLPFHS | 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: 388
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): 43144
|
A0A932QZU6 | MQRHEAIIPIQVVKDQFKRAAVILRQGGVVAFPTETVYGLGARGFDGEAVARIFSIKGRPFDNPLIVHIAEQEQLRLLTSEVTATADELIKTFWPGPLTLVLKRLDAVPAIVSAGLSTIAVRMPSHPMALALIRELNEPIAAPSANRSGRPSPTSARTVREELGTSVDFILDGGPCAVGLESTVLDLTASPPRILRPGAIAVEALRDVLGAVTSYIKNSISVGSPGLKYGHYAPALKLVLVEPDEWQTVMEEALQLGKRLGTICRYKKGEAENFLPLRPCNYNRVMTDLADYAKNLFAAFYEAEAAGVEVLFVEKVAQEGLGVAIMDRLERAAALR | Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine.
Catalytic Activity: ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-threonylcarbamoyladenylate
EC: 2.7.7.87
Subcellular Location: Cytoplasm
Sequence Length: 336
Sequence Mass (Da): 36362
|
A0A061H0S6 | MASKFYTPAYNFHPHQPAFKHRWGAKLLGATMWFWIFYRAKQDGPVLLGLRHPWDGHHGHHDEAHGDSHH | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 70
Sequence Mass (Da): 8237
Location Topology: Peripheral membrane protein
|
A0A1G1LTE2 | MRNIKLIIEYDGTSFHGWQIQNKKPTVQGELKKALKKILREDVTLISAGRTDSGVHALGQVTHFKTRSLLGLYQIKQALNAHLPPDISITEAEEADKNFHAQYHAKTKTYRYTILNRRGRSAYMRHFCLHHPYPLNTKKMKEAAKFLIGRRNFRAFQSNNPSNLNSKDTIRTIKRISISKKSDFVYIDIEADGFLYKMVRNIVGVLLEVGNNRLAARSIKDILKSKNRTQAKKSVAAQGLCLLKVKY | 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: 247
Sequence Mass (Da): 28298
|
A0A931F8E3 | MDGLNKFKDKKIHFIGIGGISMSAIANFLLDYDINVTGSDLSYNNKIKELESRGVMINIEHDEENVKSADIIVISSAIPDENPELTYARDNNIKVFKRAEMLAEIAKDKRLIAVSGSHGKTTTTGMLTSIFLQSDRDPSIMIGGDIDLIAGNYKSGEGEFFITEADESDGSLLYFDPDISIVTNIEPEHLDYYGGEEDLYDTMYEFIKKTGESGIILCLEDEGVNTNLIKSRLNKDGALEFTGYGLTNGDYRADIIKNNNFFTSYNLFYQGEFIDKIEMQLTGEHNVLNSLAAIAAARKAGLDWNDIIDGLFNFKGVKRRFEFKGEVNSIKFIDDYAHHPSELETVIKSAKNLKSNKIRFVFQPHRYTRTRDLWNDFKEVLSDRDVFYYIVDIYSANQPKIDNISSKKLVAEIKSNEPDVKIEYIGSIDEATNKLKKIIEEDNLFLTVGAGDVYKIGDRILKSLRSEQNA | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
EC: 6.3.2.8
Subcellular Location: Cytoplasm
Sequence Length: 470
Sequence Mass (Da): 53062
|
G2SQT6 | MANMEFTWQNHSGKKATVKRILANHGVSHRMIAKLKRGQGNVKLNGEKTVLSALVGQNDKVTLVLPPENDDERILVSHERIKVVYEDENWLLLDKPAGISSVPGPSNDHDTMMNRVKGYLIDQKSENLVPHAVTRLDRFTSGLMLCAKHGFAQGLISKQVQEHSMEKRYLAVCSGFVKKDHGIIDLPLKKEDNGFRRIVSCDGQNAVTEYWVRERFGNEATLVECVLHTGRTHQIRAHFAHFAHPLISDELYGGKRNDACKRQALHACCLAFDDPFSCKRLRFELPLENDMEHLLGELRCINCD | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 304
Sequence Mass (Da): 34431
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A0A1H4CR10 | MSEFDLIREYFFWQPKPDNVCVSVGDDAAVLRVPAAKQLVVSVDTSNAGVHFPLETAPHAIGYKALAVNLSDLAAMGAEPAWFTLALSMPAADEGWVREFTRGMRELAEQHGIFLIGGDTTRGALSITIQVMGFVEPSKALLRSGAQHGDLICVSGTLGDAAAGLAVLQQRLTLPTEAAAFCIQRLNYPSPRLAFANSLLGRANACMDISDGLLADLGHLLRASGVGARLQHTLIPFSAALQHIALAQRLDFALRGGDDYELLFTMPKQNLCEVQQAAGRQQVQVTVIGEVDANQDGLVIDYTFADNRQGYEHFS | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
EC: 2.7.4.16
Catalytic Activity: ATP + thiamine phosphate = ADP + thiamine diphosphate
Sequence Length: 315
Sequence Mass (Da): 33895
|
A0A832A4Q3 | MQGLDGKKALVLGVANKMSLAWAIARAFRAHGADVALGCVESSRRRVEKLAREAGCGPVLVCDVRREDDIGALFRKLAEVFEGRLDILVHSIAYADLEYLGGEFIGTPRRVWTEALEISAYSFLACVREGRPLLRASQGASVITLSYAGSREVVPGYNIMGVAKAALESAVRYLAYDLGPENIRINALSPGPVRTVSALAVQNFETALKVMESHAPMLRNVTAEEVAAAALFLASPLSRAMTGCVLPVDAGAHILCRPSIARCELKR | Pathway: Lipid metabolism.
EC: 1.3.1.9
Catalytic Activity: a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH
Sequence Length: 267
Sequence Mass (Da): 28665
|
L0EUW5 | MVINKTPHNSLDENPTNSEKDLNDMRTPLEQQEKIDTNMPSLELSAEHKLKEFNAQNNKDFNKDSSPVPETPLPLNSLSNSNLEMIMDIPINMQIILGSCRMQISSLMNLSEGAIITLDKRIDEPVDIAVNDRKIAKGEITILENNDAHFGIKLIEILNSN | Function: FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation.
Subcellular Location: Cell membrane
Sequence Length: 161
Sequence Mass (Da): 18080
Location Topology: Peripheral membrane protein
|
F9Z593 | MIRIIKIGGKLIENDAVLNGLCDELSACYRDSVLVHGGGSMAGQLSARLGIRTRMIDGRRITDRETLEVAVMAYAGWANKKLVAALQVRNVNACGLSGCDQKVILAHKREVKEIDWGFVGDIDRVDTGVLAGLLHRQVMPVISPITYDGAGQLLNTNADSVAGAVAVALSRIDDTELIFCFDKPGVLLDVNDADSVIPVLDKEKYAGYLEQGAIHAGMIPKLDNAFKTIKAGVKSVRLTDPCHLDGGTVLR | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.
Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
EC: 2.7.2.8
Subcellular Location: Cytoplasm
Sequence Length: 251
Sequence Mass (Da): 26922
|
A0A1G1LLT5 | MKNSNTENIDLGLNRSPSGIADEDVMVALLNMGGPKTNADVRAFQSRLFNDTRLIRFPLSKILQPLFAWALVTFRGKASEERYQLIGGGSPLFSSTQAQTEALRRELKKRGRGFSLTFSFNYSEPLPEQTIAETKQANKKYLLPLSMYPHYSSATTGSNLYYLKKAAEGIYPQLQFLPTPLYYLHPDYIQGFVDRVHEQLKPGESLDDFYLIFSAHGLPVYFIMEGDPYPNQIAQSVALVLNQLKRKDKWIVAYQSAVGPMKWMTPSTEGVLRALAKQGMTKVLVVPIAFVNDHIETLCEINMEYKEFALKEGIKDFRMSRALETHPGFIKALADVIEALLPKSEKFQVSGVKSPVNT | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
EC: 4.98.1.1
Subcellular Location: Cytoplasm
Sequence Length: 358
Sequence Mass (Da): 40331
|
A0A6S7B2M4 | MSRLNFLLLLIVTLCALSVVNATNRQRELFIALGRGQMQERQLQQELARLQYQQSALSKTTRVEGVATSDLEMQPVTAGRTQYLTVAGASVTAPDDGASGPASTGSNTGASNTGASNTANASEIAGITSGTASAGASSPAGSSAGSSAGSTAQSAAATSSRATRASGASAAAAGASQ | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.
Subcellular Location: Cell inner membrane
Sequence Length: 177
Sequence Mass (Da): 17427
Location Topology: Single-pass type II membrane protein
|
A0A1G1I1B6 | MRIGVFGGTFNPIHVCHLRVAARAKELVGLDRVVFVPAAHPPHKADEKLVAARHRLEMTRRAIAGRPGFEVDDLELRRPGPSYSVDTLDEFRRRHPAAELYVLVGVETFLELSTWREPHRLFAASRVVVIARAGRSFEALAGVPWIGDTPRAVLAGFDATTGEAALDLGPTVRVVLVKIAPCDVSSTQVREDLAAGRAVKNLLPAPVYFYILEHRLYGARDAGA | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Length: 224
Sequence Mass (Da): 24557
|
A0A268SJD3 | MLRTIVVPNKYKPKLNLRETAEAIHFSKKRFQERLEQNLNLIQVPSPVLLQEGTGINDNLNGVERIVSFDALDMEEGQIEVVQSLAKWKRIALKTYGFQVGEGLYTNMNAIRRDEWMDNLHSIYVDQWDWEKVIAEDQRNLETLKEEVSKIYRSIQATEQELYTQYSCLEPILPDQIFFITTQELENRYPDLTPKERENEITRQYGAVFIMQVGGLLNSGIVHDGRSPDYDDWTLNGDILLWFPVLEQALEVSSMGIRVDAAALEKQLNLSQANERAALDFHQSVLNGVLPFTIGGGIGQSRLCMFLLRKAHVGEVQTSVWNDRTWRECEEGNIPLL | Pathway: Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (ammonia route): step 1/1.
Catalytic Activity: ATP + L-aspartate + NH4(+) = AMP + diphosphate + H(+) + L-asparagine
EC: 6.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 337
Sequence Mass (Da): 38773
|
A0A2N2L1U9 | MNRLLKNDLELCESSLVGIDEAGRGALAGPVVVAAVILSYTYPLDQLNDSKKICAKTRENLYELIMEDLVAFSIIEIDKAYIDEYNILEATMEGMRQAAKATARRNSLILIDGNSVPKDMVARAVVRGDSLHGCIAAASILAKVHRDRLMTAASEQYPDYGFERNKGYGTAEHLRAIEKFGPCPIHRMSFAPLSELSIWSRIKSS | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subcellular Location: Cytoplasm
Sequence Length: 205
Sequence Mass (Da): 22650
|
A0A6V7XT26 | MQENSTSDSVNTTLRLETDFNAESGDDETQVFIKSGNYKKEERTPLLPERSPTSREMSSPDEVGIRSERVNTLDSHHSDEEISRMCNEQYGTTIGTDFADNLAEAIRAINHEIYPERIAQGSSGSYFVKNLKREKIAVFKPKNEEPYGSLNPKWIKWLHKLFFPCCFGRSCLVPNQGYLSEAGASLVDQKLGLNVVPKTAVVSLAAPTFNYSRVDRAMTRTKERIRDRYPDIGRHFRRIGLPPKRGSFQLFVNGYQDASYWLRQWELFPEMAPPTSVMSEFQLEFEKMVILDYLIRNTDRGNDNWLIKYEPVTVEGKIGDITSGLLGKTRDGTAPGTAMRLNEEINSQDDAKLIDLHEDNEEIDGADETLNDSAGWESVLMPNAKIAAIDNGLAFPFKHPDQWRAYPYQWVGLSIAQRPFSDEIVSKVLPLVDNTDFVRELGNDLRKIFEADKGFDKKTFAKQLSVIRGQMFNLREALRARKSPAQLVQMTPQYMIEIKRKKLRKFRKLVKNIKSSNSQITTTTELTPSTTNLNQSTSGKSLAEQPRIQDNVAGTSSSVPINEAAIASEAMTTTEDEYENPKSWHNTFKQKVQTRSPFFVMW | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+)
EC: 2.7.1.67
Subcellular Location: Membrane
Sequence Length: 602
Sequence Mass (Da): 68448
Location Topology: Peripheral membrane protein
|
F2I7G0 | MIKVLIIYFQFFTRIPIPIAVDHPLERYRQGIYLLPLFGALLFSLLAFIYALLAYVLPIHVVWLLVLIFETVITGGFHMDALADTCDGIFSARKKEDMLRIMKDSRLGAFGGIALIFYYLLYYVLGSEVLNGLSGLGSQMGVIISLGLISRAMLALGHWQLVYSGYNPNGMGKMMVGTPKWGILLGQVLTLLILFFILGFKGLLAYGMTTVVVLLYRRYIYQLLGGMSGDTVGCMGPLSEVTFLLGLLALGGI | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)
EC: 2.7.8.26
Subcellular Location: Cell membrane
Sequence Length: 253
Sequence Mass (Da): 27925
Location Topology: Multi-pass membrane protein
|
Q06SA6 | MIFYWGFIYFFFVLGVGGIFLGLALTLGRRARTVGWETLSAYECGFQPMCNVRIPFSLQFYLVAIIFLLFDIELVLILPYLSDSESYGTVFIFLFFLVLLLGLIHESNEGSFEWR | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Mitochondrion membrane
Sequence Length: 115
Sequence Mass (Da): 13321
Location Topology: Multi-pass membrane protein
|
Q4T4B8 | QDLEEFVNGSEDHGFIVFTLGSMVDNMPEEKAKQFFDAFAQIPQRVLWRYNGAVPENVPKNVKLMKWLPQNDLLAHPKAKVFVTHGGAHGIYESICNGVPMLMFPLFGDQSDNVQRMVHRGVAETLSIYDVTSQKLVAALKKMVQDKRW | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 149
Sequence Mass (Da): 16919
Location Topology: Single-pass membrane protein
|
A0A0P6WSK9 | MTRIGLFGGTFDPPHLGHMILAAEAFHSLSLDRIFWILTPQSPLKDERTISSVQQRRELVLAALQNVPEFELSQVDILREPPYYAVDTVKILKREYPGTDFVYLMGGDSLRDLPAWHDPNQFVQELSGLGVYRRPGSQPDLEILEKLCPGIKTKTTIFQAPQIEISAADIRQRIREGRPFRFFLPPEVYQLICAQNLYR | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Length: 199
Sequence Mass (Da): 22823
|
A0A8H2QRY1 | MIDYIKGSIYQITNDAVVIDKGGIGIKILMPSTSLKKLSEGQETTIYTDLVVREDDISLYGFIDLHERQMYQLLITVSGIGPKVAMNILGGMNSSLLQKSILLEDLSILTQAPGVGKKTAQRIVVELKDKLSKMDSFVPSDVEVQQIHSLDNPALEALIQLGYQEKEANKMLQGIDKDQPIELILRQALKNR | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Subcellular Location: Cytoplasm
Sequence Length: 192
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Sequence Mass (Da): 21312
|
A0A7I7WS75 | MSPVNPAQLTAEALDGQVIAGAKVVSRIVPGAYFTSISATVQLVEDEQPELLIMLGEFGGRSMITVERLAQNVSDCARYGVADTAGKVLGGEPTAPEGPVAYWATTPNRAMVLAMRRAGVPADLSDAAGTFVCNHLMYGMLHHIATNALTTRAGWIHLPFLPEVAALDQNLGAPSMSVETMTTGLAAAIEAALTESADTTEPFPSRLQI | Function: Removes 5-oxoproline from various penultimate amino acid residues except L-proline.
Catalytic Activity: Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro.
EC: 3.4.19.3
Subcellular Location: Cytoplasm
Sequence Length: 209
Sequence Mass (Da): 21906
|
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