ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A8T2HYJ9 | MVNYEHMGGMREADPAAVAKLRNKLVDSSTTLSQKYRILFSLRNLAGSDAHEAMLLGLKDPSALFRHEVAYCLGQRQDPAAIQTLTTILQDTAEHPMVRHEAGEALGAIGKESCLAPLREHVDDQCLEVAQTCQLALQRIEYHLAEAEKHNTRNTSTEMQHPETESGPSPYLSVDPTPPAPDSIPSTDLRSCLLNDEERIFDRYRALFALRNRGGTEEVQALSASFKSNSALLKHEVAYVLGQIQDANTVSQLKIVLEDSKENPMVRHEAAEALGSIAAPECLDLLKQYTLDIDPIVADSCIVALDMLEHEQSGEFEYAK... | Cofactor: Binds 2 Fe(2+) ions per subunit.
Pathway: Protein modification; eIF5A hypusination.
Function: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.
EC: 1.14.99.29
Catalytic Activity: [eIF5... |
F3BGD8 | MTKLGLRDSVLTLTLIPTVIIGLLLGGYFTINRYIELDEILYQQGTTISEPLAIALEQPMLEKNKQLLNRLISYTHNKHSPTIKSIAIFDKNNALLMTSNYHRSFEKLISQKTLINLKTTHVQKSDELVTFFTPIINHTSHDSKWDPSAFQSSLGTVIIQLNKDQAVIGQQRALLISGIVIILSLVFAAILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLNDNMIGEFELLREGLNTIAHTMVMQKDEMQKNIDQATSDYRETLEQYETSNIELSFAKKEAQDANRVKSDFLAKMSHELRTPLNGVIGFTRQLYKTPL... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 924
Sequence Mass (Da): 103366
Location Topology: Multi-pass membrane protein
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A0A8B8YBS5 | MVSCVRRSSLRRSRRRGGLARLPETPESASLVARSAMETLRKALIAGAVLGAGAGVGTALFVLVAPGEQQKQTMLKEMPEQDPQRRDEAARTKELLLASLQEAAATQENVAWRKNWMSGGGGKSA | Function: Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex), mediating cytochrome b recruitment and probably stabilization within the complex. Thereby, plays an important role in ATP production by mitochondria. Cardiolipin-... |
A0A075B060 | MPHIETNVFPDQINFSTVQQTLPPNYIIRPLRSNDFDKGFSQLLSQLTDIGDLSAQNFQDRFHEMLAMPGTYYIIVIENTTTQKLVASGSLILEKKFIHGNGLAGHIEDIVVDEKERGNSLGKKLIEQLRLTAIQLNCYKVILDCHEKTVGFYEKCGFKVKGVQMAYYKE | 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 Leng... |
A0A6A3NRF2 | MRLGYLLVVVVATLLAVSCDVTSAESSTPSTRLLRTAGEQTPERRLVNKLPASFVRDLLKDKTKLEGTLTSWQESGLGVKRLAKSLGLSSNWVKMLRNAKNHGKVDEVALLKLYRARVGPKAK | Function: Effector that suppresses plant defense responses during the early stages of pathogen infection.
Subcellular Location: Secreted
Sequence Length: 123
Domain: The RxLR-dEER motif is required for the delivery of the effector to the host cell cytoplasm.
Sequence Mass (Da): 13503
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A0A6V2P2J7 | VETTLDTSLPWLDGGPRAAHPPRDMGFLLDATPLEWDESLEVIRYVREHGIAQFIHLYNRIKDIEGDRLLWGDEVEYAIFKLDAERGTVKLSLRGAEILAGLQEGERSVPVGQQCNWVPEWGSWMVEGTPGMPYSGYATDLLLVEKNMRTRRARLLAALAEDEICPTLPCFPLMGVGTFTDPPARPTPGLSDSLFVPDEIINPAPRFAALVKNIKRRRGSKVDIRVPRYRDEKTPDAARPVGCPPPATLEEALEMDEVYMDAMAFGMGCCCLQVTFQARDLSESRHLYDQLAVLGPIMLALTAATPIARGVLLDTDVRWD... | Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 433
Sequence Mass (Da): 47303
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A0A7J4L660 | MKTELIGKKIKIIESNNKNSIGKAGIVVDETKNMLSVEIDGKEIKVIKDQCVFEIEGKKISGKDIAKKPEERIKK | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
EC: 3.1.26.5
Subcellular Location: Cytoplasm
Sequence Length: 75
Sequence Mass (Da): 8398
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A0A7J4P504 | MEIRVIENSKDKGKLSFLLKDSSAVFANTLRRLITDEVPVMAIEEVEFRDNSSILYDEMVAHRLGLIPLKTDLKSYKLVEKPEDRESLKCIVKLVLKAKGPCTVYSGDLKSKDPEIVPVDKGFPIVKLLKGQSLELEATALLGRGKEHTKFNPGHVYYRYKPVIEIGSVRNPEEVVDKTHGTVFAIKGGKLEVVKDNLFSVDLAGAAEEISQGAIKEGHDSDIIFTIESWGQLSCKEMVLRALDEFDAMLDELSEKVKSAQ | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
EC: 2.7.7.6
Subcellular Location: Cytoplasm
Sequence Length: 261
Sequence Mass (Da):... |
A0A7J4LCZ8 | MLKGVLSRISYFYEHRYKQLLILPVFLLLFSLFILGNNYAKTGEFIQTGVSLKGGTTISIAQSFDIKEFESFLTEKYPGSDLSVRSLSRAGTDVGMIVEASDVSSGDLLKSIEEKTGPLDKSLYTIDTTGPSLGKSFFKQAMIALLLAFLAISFVVYIYFRSFLPSFYAVFSVVADLLFAMTVFVLFGLKLTTGSIAAFLMLIGYSIDTDILLTTRVLKRKEGTVSERMASTIMTGLTMTLTAVVAVTIGYFFTESELLKQITFILAWGLPADIIYTWLFNAALLRMYVEKKEKQNEH | Function: Involved in protein export.
Subcellular Location: Cell membrane
Sequence Length: 298
Sequence Mass (Da): 33216
Location Topology: Multi-pass membrane protein
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A0A3D2NKW8 | MASNRATQDSDDLEALFDSIVSAHTQEEAGEGTHCLSQSAANDQSDANKEKSGKVINQLGQMTRTLHDTLRELGLNKAIEAAASSIPDAHDRLHYVATLTQQAAERVLNATEAAQPLVENMETEANRLAAQWKKLFDKQLDVADFKALALQTHAFLEVIPRQTKATNAYLLEIMMAQDFQDLTGQVIKKIIEVTQQMEQQLLSLLLENALPTDKKIEYSGLLNGPVIKPVGRADVVTSQDQVDDLLESLGF | Function: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P).
EC: 3.1.3.-
Subcellular Location: Cytoplasm
Sequence Length: 251
Sequence Mass (Da): 27596
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A0A075AQL0 | MKIQEFIDLICDQEAKESLGTIRTGVPPRSVAIANLNMSLKDIGIKDRDTITIENGNTFKRKTISNEMMVIRKMADDNSCLFSSIGYLLENKRACQADALRQKVVEFILSHPDDYNSVILGKNVSEYCQWISKPTSWGGAIEISIFSKLYKIQIASIDVKSLRVDLFGEEDSFPDRCYIVYDGIHYDCIVSTYSNNETAQDITIFSSKDDFALASAISVVEEISKKNMFTDLANFTIRCETCHSGFIGTDDAQRHAQETGHTNFAEFKN | 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 u... |
A0A2E7FUX0 | MSMPSQPSSRWVFGYGSLIWRPGFVFERAERALLRGVHRRLCIYSHLHRGTAERPGLVFGLERGGACVGMAFKIAESDWDEVRDYLRAREQVTMVYVETHRPAKLANGEIVETLTFVADPHHPQYAGRLSLEEQFALVDGAVGEAGSNIEYVINTARHLKEMGIADRQVQALAAMIASKHAPAENQSAAG | Function: Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides.
EC: 4.3.2.7
Catalytic Activity: glutathione = 5-oxo-L-proline + L-cysteinylglycine
Sequence Length: 190
Sequence Mass (Da): 21061
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T1UP47 | IGKAGNPDTMENVNPNMIIGASTEVHAGENLIATPGGIDTHIHFLSPQQIEHALYSGITTMIGGGTGPFDGTNATTVTPGAWNIERMLQATDNIPMNLGFFGKGNCSHLAPLKEQVEAGVLGLKVHED | PTM: Carbamylation allows a single lysine to coordinate two nickel ions.
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
EC: 3.5.1.5
Subcellular Location: Cytoplasm
Sequence Length: 128
Sequence Mass (Da): 13403
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A0A8B8WMG5 | MKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMIALAKGQRAEDGYVIDYELTDQEAWDLRVAGMKRRGTNVPKWMSIMTEQSVCHLQKVFERYKSYSPYDMLESIKKEVRGGLENAFLNRVQCIQNKPLYFADRLYDSMKGRGTRDKVLIRIMTSHSEVDMLKIRSEFKKKYGESLYYYIQQDTKGDYQKALLYLCGRDD | Function: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechani... |
Q8M0U6 | GLVGSALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLASNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSLPVLAGAITMVLTDRNLNTA | 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-cytoc... |
A0A8U1EKI9 | MATTVNSGNAPVSDTQSSTSADPRYEGSTFQYSMLLEHLIGEKRPIKDLNPTVMGGLPNPMKTDDQKMIERGMESCAFKAVLACVGGFVLGGAFGVFTAGIDTNVGFDPKDPMRTPTAREVLKDMGQRGMSYAKNFAVIGAMFSCTECIIESGATIFSKLELRNAYHLVRICEGDELKTAFNTASGYYEYCFPGFGK | Function: Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. In the TIM22 complex, it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane ... |
F0VNK4 | METKSEASGRDLRDPVLLSLLPRFSSVSSAGHSAESSLVPEPSRGSLQRSLRGARLHSVDPLDRGVCTPGIRSTANARGDVPPFSTVTSAFYRASFSFFRPPVLSLFPASSGVAFCSSELPNVSPKAVPSTSPRANPSSCPVSRPTVTSAGQGCPFGHGKSERAASDLVPAGPSDVSTDSSSSGTANAVSCPASVFGSVCPVEHGSSGASLSGNSAELPQECPMKRLPVRKSFFSSLFSSSPAPSSCPYGLGEGGENAQGVQVEVPAGLSDAREKSTIPSVSGENWNYPSEKQFYRVTRAKGHQVDPGDMPAIVAIHNAV... | Function: Lyase that catalyzes the covalent linking of the heme group to the cytochrome C apoprotein to produce the mature functional cytochrome.
Catalytic Activity: holo-[cytochrome c] = apo-[cytochrome c] + heme b
EC: 4.4.1.17
Subcellular Location: Membrane
Sequence Length: 437
Sequence Mass (Da): 47155
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A0A959F1Z7 | MDILTLKALHVIGFVAWFTGLYYLGRLFVYHAEAGQKPANERDILQKQYQHMMKRVYKILCNPAMMLTWTFGIAMLALNPSYFKMGWLHIKLTLLVLLLVYHVYSKSMIRKMESGKSTMSDLRLRLYNEVPTWFLAGIVFTVVLGKAELLNYAYLGGGLIVFAALLYFGIRASQGKKAA | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Function: Catalyzes the oxidation of protoporphyrinogen IX to protoporphyrin IX.
EC: 1.3.99.-
Subcellular Lo... |
Q1W563 | LGQAGSLIGDDQIYNVVVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAADMAFPRMNNMSFWFLVPALIMLLSSSLVESGAGTGWTVYPPLSSNIAHAGSSVDFAIFSLHLAGVSSILGAVNFISTLGNLRTFGMMLDRMPLFNWAVLITAILLLLSLPVLAGAIT | 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-cytoc... |
F0VDV8 | MRLPRYAREASESASTLASPSGSTLAGESEGVALEDSKLTHSASCKGTNRDGVFCSETCDKDAGNAAFAPGTLRPNCPVHGQLFSESEVALCDAEPRSGGRCLVIFNTCVYDLSNFSHPGGSRLLKGHAGRDITEPFQEVGHSVHAFKLLDALCVGVVKERLDRHKQTVGERCLCGSGQAETATLSQLRYRGLAPGGDSSEAARQLGEHAGSTSPTATPSAHELIDFTKPLLPQVWRLSKTDYERLIEVPCMIEGSMTLMPYAWMEPLSQTRWWVIPLLWLPVVFWCIRENLKTLSPTCCFVSVSVGLALWTLLEYVMHR... | Pathway: Lipid metabolism.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 452
Sequence Mass (Da): 50231
Location Topology: Multi-pass membrane protein
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F0V9V3 | MVGTNAPSAQASCVQHVGGARTSVPRRRVTSGGGASNSAAQRPRGMPASSQGILRFYTDDTPGLKIGPQTVLIMTLCFMACVVLLHIAGKVHQTYGGEN | Function: Necessary for protein translocation in the endoplasmic reticulum.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 99
Sequence Mass (Da): 10269
Location Topology: Single-pass membrane protein
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A0A7J4V4Z2 | MAQKLKALRPSLREKKRYMVFQVISGRPVTAQEASDAIMGACRQFLGELGMSRAGIIMLHDKWQQASQRGVMRISHKEVQNVRTALMLVRSIGSREAVITTKGMSGILRKAVQRFLLAPEGQPPAVPG | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
EC: 3.1.26.5
Subcellular Location: Cytoplasm
Sequence Length: 128
Sequence Mass (Da): 14156
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A0A0D1ZR10 | MNVHSYCQWQTLGLVCTTKSTTLPNFPNSLGTNGSQFFVTTVKTPHLDGKHVVFGEVINGKNIVRKIENLPTQSDKPVHDVVVSDCGQLEGSAYSAATEKALDSTGDPYEDFPDDQGEGLKGEEYYKIGLDLKEYGNKAFKAGDVEVGIEKYQKALRYLNEYPATNDNDPKELQGNLDSLRFTLHSNSALLANKTKRYAEAQKWAGFAIDGMPKDAKDADKAKVYFRRGQARVALKDLEAGLQDFEQAAKLAPTDAGIKHELAKTKKTLQDSLRREKESYKKFFS | 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: 285
Sequence Mass (Da): 31684
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A0A8T2HUT0 | MIGDVQLILQRGSAVLAAEATGLAFLRVVLPSTTGHLPFAARGIASSSARVAATESEKRAEKKAAETAEREMVAADEEFSAITDKIPQRPITVVEGTSYTVVIIAALGFAAAVIYAALNELIFSPKEYQCYTHTLNRIKDDPRITVRLGSPISAYGTESRNRAARQRIPHRVYNDSEGREHVQLQFHMRGPSGRATVNADMYKDGSEWRYHFLYLNVESPIQQQVVLVRPGQVDEY | Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Location: Membrane
Sequence Length: 236
Sequence Mass (Da): 26091
Location Topology: Single-pass membrane protein
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A0A7Z8Z8M8 | MKKTVIALLALVASSACSAATPWQKITQPIGGSAQSIGAFANGCIVGAQALPLNSVNYQVMRTDQRRYFGHPDLVRFIQRLSNQVYSRGMGTMLIGDMGMPAGGRFNGGHASHQSGLDVDIFLQLPQTRWSPAQLLKPQALDLVSGDGKRVVPARWSPQISQLIKLAAEDSEVTRIFVNPAIKQQLCLDAGSDRDWLHKVRPWFQHRAHMHVRLRCPAGSLECEEQAPPPAGDGCGAELQSWFEPPKPGSTPPVKKTPPPLPPSCQALLDEHVL | Cofactor: Binds 2 Zn(2+) ions per subunit. Zn(2+) ion 1 is bound in the active site. Zn(2+) ion 2 is bound at the dimer interface by residues from both subunits.
Function: Murein endopeptidase that cleaves the D-alanyl-meso-2,6-diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the r... |
A0A485KR35 | MESSLENDTSVQETASDAAACKLSAVRLGYWEDPFASMFAKPNRKMPIINRGYYARARSIELLIHRFFATPVATPSGGGNQPHTRQVIVLGAGQDSMFFRLKTQHPDLLATTMYVELDFPAVTRSKVRLCRRHKVLADALGPVETNETELKAQGYALLACDLRDLKTVQSKLATARINPQLPTLILSECVLCYMNAEDSLPLLSWIGASFADAAVVVYEQIRPHDAFGQTMVENIHMRGCDLKSIFSCVATILCFPPRHCRYPEADDQRRRFLDVGFAHVDCWDMNKVYYEYLDVTERKQKERLELFDEVEEFHMLQGHY... | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
EC: 2.1.1.233
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl es... |
B0X8W2 | MLPKFFQRIARCESVYDVIYVKYLLYKFFGFTIFTVDGRPQDGKVKLTAWDVFSLVRVLAMEAVVFYVSYTTLQSRESTGSSILDNGTRYTFVGGSLYISLVTLLNYRRYRGVWKIFAKMDRFDGRAKQINAPVDQRTQQIRILQSIAGLIISFVLMTISGIAMVFWSEETSIYRWSIPVSVIFFNIPFLLMQHQVLIVTYLVYYRVQHLNATFEVHFIPQKEPTLVILAELPAPRSIHDKPTILHNLVIQWDEIRRIVQRISNEFYAQLIFVVLVSIMIVTFSLFALYRAFLTGDRVQMVRALMYMECDVFYLVMLVLF... | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 403
Sequence Mass (Da): 46792
Location Topology: Multi-pass membrane protein
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Q8MKK7 | MRIRSNPMPSRMVDILCFLIIAVFLPVVFMFEIVVVLPAFHEPGGFFHTFTFLMAMFLVFNIKGNMIACMMIDTSVNVKKVEPPSDQLNWRECGECQKLAPPRSWHCKACKVCILKRDHHCIYTGCCIGLRNHRFFMGFIFYLFVGSVYALVYNSIYMWVIHGHIYSNWVTVLKLACPMLHLLWLMESSSWPTMCPLF | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 198
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 23048
Location Topology: Multi-pass membrane protein
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Q3KNZ4 | MILVSTTSGIAACQVLIFREIHASLVPGPSERAGRRRRGHRTGSPSEGAHVSAAMAKTVRMTLVIVIVYVLCWAPFFLVQLWAAWDPEAPLERPPFVLLMLLASLNSCTNPWIYASFSSSVSSELRSLLCCAQRHTTHSLGPQDESCATASSSLMKDTPS | Function: Involved in renal water reabsorption. Receptor for arginine vasopressin. The activity of this receptor is mediated by G proteins which activate adenylate cyclase.
Subcellular Location: Cell membrane
Sequence Length: 160
Sequence Mass (Da): 17371
Location Topology: Multi-pass membrane protein
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A0A1I8N9E8 | MFNKNNTGAGGAGASGPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGEVWERAQRLHDKMQTNLSMARDRLHFLELRDEQLRMEALHLREEQQNKKQDNTRNRSNLKHRKTTTPSTTSKAASATKNVQVVQPMQMEYNSSNNNSSGGAAGASCSIPMVRINNTTKLRSIAAHNIRNNYNSNNASSNAGSPSATASGRKLTVSSKRPGNLAVVNKSQTLPRNLGSKNAIAGVSQRQPIKTAATPPAVRRQFSSGRNTPPQRSRTPISGIGGGSSGGGQSNSGASTPVVS... | Function: ATP-dependent microtubule severing protein. Microtubule severing may promote reorganization of cellular microtubule arrays and the release of microtubules from the microtubule organizing center following nucleation.
Catalytic Activity: n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tub... |
A0A1D7W417 | MKPSFVQIAIVILIIVIIFGAPKLPALARSLGQSMKIFKSEVKDLRDDDEPKKTEPGELNREATENDTSTTAEAARKPEQPAKEKQDPQSHEK | 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: 93
Sequenc... |
A0A134BSZ8 | MTTIKIALLGFGTVAQGTFNLLQDNAELIKNRTGVNVEISKIYVRNPEKYSHITLPETAKYVTDIDEVLKDDSIQMVVELMGGTSFAKDCVEGALKAKKNVVTANKDLLAEAGPYLLDLASKNGVDLRFEASVLGGIPIIRTLYESLAGNRITEIIGIMNGTTNFILTKMSEEGLSYQDVLKEAQDLGYAEADPTADVEGLDAARKLAILASISFNRRIFFEDVTVEGITCIDTEDIKFGKEFGYNIKLLGIAKETAQGLSLNVYPAFIPTTHPLASVRGSYNAIYVKGNGIDDVMLYGRGAGSLPTGSSVVSDIMEVAK... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
EC: 1.1.1.3
Catalytic Activity: L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH
Sequence Length: 429
Sequence Mass (Da): 46780
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A0A2I4HGT4 | MDRCYRLFPCLSDPARRSSLGLKLAMVMVHLVYAGILFLFDEDLIEKMKRVPWYIALYLLLFFATLVQYFITSCSSPGYVIDVMRTINVKDSVFQTPSMASKQPASSKNRSLVITVDGSQLGRNLLGSDTTSWSKLVMDLYPPGTSARTWTCSYCNVEQPPRAKHCHDCDKCVLQFDHHCAWLGTCIGQDNHCRFWWYICGEMALCIWTGILYISYLKSNISRAWWKDAIMILLLIALSIALIFLLLLLLFHSYLILTNQTTYELVRRRRIPYLRSIPERVYPFSKGICKNLYGFCCARSSIYSMDPLPTPQEIEEKLRP... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 332
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 38304
Location Topology: Multi-pass membrane protein
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A0A817CVQ3 | MNNNQIRPSLSPQDSATMLAQIQQKNPQMYARLQAMRSDLTETAYEQLLAAVAVSAANSNGQGHGHSHTHSSSCAHSNSQMHFSQPVPDVPPKPNAAEMNIVQAVQYNEIERVKQLIESGQADVNTPDSEACHLLHWASINNHVELVRYLIAKGATVDIIGGDLKSTPLHWALYSIVTYIYIYIHAGRQGAAETFFLLVDNGAAIDSRDINGVQPIHIAAQYGQIKILAYLLGSGVDVECHDGRDFTPLIYSCLGPPQNYVPLPNSSHVCCTQFLLTFGADVNYQEPTRRFTPLHFSINNLNSISFQVLLKNPQINVHLK... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 543
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 62004
Location Topology: Multi-pass membrane protein
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Q9VRU1 | MVNVTEDVFANGAVNPFTKSKDTIKRFTLTNGAGMSVQLITRGATITSIKTPDASGQIDDVTLGFDDLAGYQSERNPYFGATIGRVCNRIANGSFYLDGKLVQVSKNRDNKFQLHGGFVGFDKAHWEVVEVRVDGVTLSHTNPDGHEGYPGKVTATASFTLSEDNCLHVQMSALADKTTPVNLTNHSYFNLAGHKSGANGLYEHTIEINAYGITETDQSSIPTGRITPVEGTGFDLRVSSNLGERLKALQPARGYDDNFCVTFSPPQPLAKVARATHPPSGRWLEVVSNQPGVQFYTSNFMPDVERGESPIPGKDGAAYA... | Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.3
Catalytic Activity: alpha-D-galactose = beta-D-galactose
Sequence Length: 364
Sequence Mass (Da): 39627
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D6RHN2 | MATKCTKCGPGYSTPLEAMKGPREEIVYLPCIYRNTGTEAPDYLATVDVDPKSPQYSQVIHRLPMPYLKDELHHSGWNTCSSCFGDSTKSRNKLILPGLISSRIYVVDVGSEPRAPKLHKACH | Pathway: Organosulfur degradation.
Function: Catalyzes the oxidation of methanethiol, an organosulfur compound known to be produced in substantial amounts by gut bacteria. Selenium-binding protein which may be involved in the sensing of reactive xenobiotics in the cytoplasm. May be involved in intra-Golgi protein trans... |
B0WY73 | MKMRTTIKVFKFHASDWIFYLGLGFIVTLCVTFVVFLVHIRHRQKLPSYGMGRTAPDPQHTYTHEFQKKLTHNSTGGHATPDINIRVNNYEYSNGSTMEAPKIPGQNVPLLLPRSISSEHHYDEPQFASSYSTPIDSKNHEKVTTTLANGGANPAPVTTTNLYHQQKHYQQLQQQIHLYQQQQQPHPSPVASLKGPQHHLQQQQQQQQQALLQSQLSSLQKASSQQYMSTDSLVTNSNTNTSNSTYAVATTDSLETSSSTGTMHKSNSMRQVVTSDGGWLELDHLQTSLSIPEGALPESLKINVFLAVMYDSKDTILVEN... | Function: Receptor for netrin required for axon guidance. Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding.
Subcellular Location: Cell membrane
Sequence Length: 551
Sequence Mass (Da): 62130
Location Topology: Single-pass type I membrane protein
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A0A1E3A7I4 | MTTEQVMEVMKEAMLVAFEMAGPLLILSIIVGLIVAVFQAATQIHEQTLTFVPKLIVIAVVLLATGSWMLNTFDGFVQRLFEIMASL | Function: Role in flagellar biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 87
Sequence Mass (Da): 9585
Location Topology: Multi-pass membrane protein
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A0A2I4DM93 | MGSPSTGETTRIAARASMIDSLKGCALLGSQIDKAELRRRLLMPQYLRLAVRDSIRSKDPTAGMTWMHDRGGDEENLEPPEAPMIVFINPRSGGRHGPVLKERLQQLIAEEQVFDLADVKPFEFVQYGLKCLEMLADLGDSCAKETREKMRVMVAGGDGTVGWVLGSLGELKKQGREPFPPVGIIPLGTGNDLSRSFGWGGSLPFAWKSAVKRSLHKAITGPICRLDSWHILLSMPVGEVADPPYSLKLTEECALDEGLEVEGELPDKVTCYEGVFYNYFSIGMDAQVAYGFHHLRNEKPYLAQGPITNKLIYSGYSCTQ... | Function: Phosphorylates the second messenger diacylglycerol (DAG) to generate phosphatidic acid (PA), another important signaling molecule. PA is required for plant development and responses to abiotic stress and pathogen attack.
EC: 2.7.1.107
Catalytic Activity: a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycer... |
A0A448NWG2 | MCDDGRVSETTNTDLDSCSPPPADGWVALTPAGRAVARAVGHDPAGTLLASDVDGTLSPIVADPTRAAVSERARRALAGLDGRVGTLAVITGRPVARAREMVDVDRRGGLDHLVMLGLYGVERYDVGTGQLQVPEPPAVMGQARHRLQEAVDRAVAADPAMAGTMVEDKGSAVVLHTRRAVEHDRALALLGPVARDLAGELGLAVEEGRDVVELKAWQTTKGDALRRLIAERMPSVLLMCGDDLGDLPAMAVVEEWIGEGRPGARVVSWSAEQPRVARSADVLCDGPEGVAAFLDEISGRITESSTM | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose.
EC: 3.1.3.12
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Length: 307
Sequence Mass (Da): 32300
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A0A815F1D0 | MLISVILIPVFLIRARNVINIRLAAQVLNPILNLFGIKYRIENAKVLDKEESCVIVANHQSSIDFIGMMRLWPEHIRYCTILAKKELIWALPFGFAAWLTGLEFVDRKNRERSSETMRQVTKKVQDKSLRLWVFPEGTRNMADTFLPFKFGAFRLAIEAQVPIVPIVFSSYKPIYNVDKTSKNYYWRQGCVTIKCLEPINTKGMTIEKDLQQLTEMTRQRMIEAHQTIQTTTSQNKKNN | 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: 239
Domain: The HXXXXD motif is essential for acyltran... |
B0W2L5 | MIHWKVALLCTLVVASSARQIVQKSEEGHEREHYHRSSNLHVKPVKQAFTEAELESKYWNDAAQESLGAKLKKEEVSKVAKNIIFFIGDGMSPQTVAATRMYLGNENEQLSFEKFPYLGQAKTYCVNRQVADSACTGTAYLSGVKINYGMLNVAASVPRYDCDYEKTNETEIFGIMKWAQDAGKATGIVTNTRITHASPAASYAQSATRGWEYDVEVRAAGCDQEKTMDIAQQLVRNEVSKNFKVAMGGGRRYFLPRDVNDGEGARGYREDGKNLVEEWLETHKEMGESEFVWNREQLLAVDPKKTEYLLGLFEASHMKF... | Cofactor: Binds 1 Mg(2+) ion.
EC: 3.1.3.1
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Length: 564
Sequence Mass (Da): 62970
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A0A450XBE8 | MNTKSPMISDHRHYARHFSVVILSILLAACSLLPKSPLIQVTDPFATWQARSRKLTNIEEWSAAGRIAIRAEDDAWNVNMRWQQKIDDYRIRFNAPLALGAAEITGDPYGVRLRTTNRRTFFATDPESLLWDTLGWHIPVSGLRYWILGMTDEDAPVDGLEIDAAGRLEQLHQSGWKIRYLGYRRFKDMDLPIRLELKNDRLDVRIRISRWVLAPAPESIRSTSKGSSEASPQSNEPQPGKSGTKKVR | Function: Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
Subcellular Location: Cell outer membrane
Sequence Length: 248
Sequence Mass (Da): 28307
Location Topology: Lipid-anchor
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B0W3C7 | MGITGLIPFLEKASRKCHLRDLRGQCVAIDSYCWLHKGAFACAEKLVRGEATDVHIQYCLKFVNLLLANEIKPILVFDGRHLPAKAGTEAKRRESRDSSKKRAAELLRMGKVEEAKSFLRRCVDITHSMALELIKECRKRNVDCVVAPYEADAQLAFLNKKGIAQVVITEDSDLMLFGCSKVLFKLDLTGSGLLIEREKLAVAMGCKEEKFTFDKFRYMCILSGVIIWTRFRGLGCQGEEVCTDNGGHGYSKGAGQDSGLQVSEEYKDSFLKADATFRHMVVYDPTERKQTRLNDPEEVGTDPELCCNAGTFLEDKIALQ... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: 5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Function... |
A0A2S2PZQ5 | MANVTHVDLNNFISKTMHTFSNLINQELKFDEVADSWVFMRTPWPMFIILAAYLLFVLKLGPNMMKNREPYNIKHIMMIYNLAQTAYNIYIISAVFLIPGTYTYLLNIVCIPDETESNRFYKRQFYIQSWHFVISKVFDLLDTVFFVLRKKQSHVSFLHVYHHVNMVVTTWIFLRFIKGQQGALCGIMNATIHAIMYSYYFLAALGPQVQKYLWWKKYVTCLQIVQFIVGIIYGVYLFIYDCDFPRLFSIYMIFDVLLFLYLFVAFYNRTYNQKQKSQ | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 278
Sequence Mass (Da): 33220
Location Topology: Multi-pass membrane protein
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A0A1I8N2C0 | MLATALIWIAALLAVIGPLPLTVDGRRHNLKILGLFPHPGISHFHFFHPILRGLAERGHDVTVVSHFPDKSPPVGYTDIPLTGKETLANSVDLKVFENRRFYNHFLEFFLLYEWGKEACNHTLRSEALYKVMRQKVRYDVILLEQFNSDCMMGVAHMLQAPVIGLSSCAMMPWHYERMGMPIIPSYIPALFLGQSEDMSLGGRIANWISFHALNLMYKVFSIPAADALVQYKFGHDVPSVGELVKETTLMFVNQHFSLSGAKPLPPSVIELGGVHIQKAKPLDVDLQKFLDNADNGVVFISWGSMIKAETLPVAKRDAIV... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 524
Sequence Mass (Da): 59100
Location Topology: Single-pass membrane protein
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A0A078KA89 | MGNIFLFGVITFRLVVLVTYIYLKNNYNIILANINTYFLFYSISFLLYLISSLCNPGYITACPTRYIARDISDEFKKNIYNKKNTEKTQPFYNFSTSDEDKSTISNISSSAPSLTLSKNDIYDELTSLTILHNLPNDIVLTEKCIKKKEKYKKLNNLASYTHKNYDKEQISISPVKNKYNKKNINTKLNNIYLEFFLKQKKNISLYATNIKKKKNNKIKKLYKYKPVFINNVNKINNTKINIFNKITQKKTNVIKTETNKYYDSTLYKINSSNIIFSKNIKYEKNNSLTNPFYIYRDNIYQHNIKLNYCIHCDIVQILRT... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 543
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 64677
Location Topology: Multi-pass membrane protein
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A0A183E3E6 | MRRRRKSVCLFQRILAAGAGAVSLAGAGLLYALESAVKVEAYEHFPHPAPLPWTHKRLFGTIDMASFACHSMKWIAYRHLIGNIMSEEEAKAEAAAVVMPDFDEAGNAIERPGEINDHLLSPYPNAAAAKAANGGTFPPDLSMLLLTREGAEDYVFALLTSYHDPPAGLKLDAGKYYNPYFPDGVIGMPQQLFDGGMEFKDGTPATASQQAKDICTFMRWTAEPFYERKKRLFLKTLLFLPLVTFILVYGKRHIWTFIKGRRSVWKTVKGRERPGT | Cofactor: Binds 1 heme c group covalently per subunit.
Subcellular Location: Membrane
Sequence Length: 276
Sequence Mass (Da): 30786
Location Topology: Single-pass membrane protein
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A0A937Q1L7 | MKFWRKTRPSFWDKREIAPGASTHQFNYRRIWKLAVLLTGGVALVPLIFITVVNYEAMQDAIASEFLLRTTRIVSNTRRAISFFLSERKSALDFIVHDNSFESLNNKERLAGILENLKRSFGGGFVDIGVVDSSGFQNNYVGPYKLEGKNYSGQEWFKQVVDSGMHISDVFLGYRKVPHLVIAVKGINQNGSFYVLRSALSIAPFEGLLSNLELGGMGDAFMINHQGILQTPSRYHGNVLQKLFLLVPKNSPKTEVLEEKNRFGQDLLIGYRYIDDTPFILMIVKKKEELMRPWYRTRLRLIAFLLISVTVILTVILGTA... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 577
Sequence Mass (Da): 64785
Location Topology: Multi-pass membrane protein
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F9D2X1 | MPAGQSRLTKEERMCSKKLIEVLFKGGQSRSMSAFPLRVVYMLLAEGGTADDGILSEMLVSVPKRCFKRAVKRNHVKRQVREAYRRHKTLVGQPAAIAFVWLDNKLHASEEVERKVVNLLRRVGERIQQEAKV | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
Q9XZ68 | MDFTTFVKPSNGGGDSGGGGDADGGGQKLQFWKHVEYIENHGKQEDDYEYCMTEFLRMSGIYWGTTALDIMGQLERLERKSIIEFVKRCQCPNTGGFAPCEGHDPHLLYTLSAIQILCTYDALEEIDREAVVRFVVGLQQPDGSFFGDKWGEVDTRFSFCAVASLTLLGRMEQTIDVEKAVKFVLSCCNQTDGGFGSKPGAESHAGLIYCCVGFFSLTHRLHLLDVDKLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLTIMGRLHWISSEKLQQFILSCQDTETGGFSDRTGNMPDIFHTLFGIGGLSLLGHSGL... | 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-ger... |
A0A347VRP1 | MLEIEVLKILKDSKNLLAFSHGCDSSALFFILLNLNIDFDIAIVNYNVRKQSKDEVRNTRSLARKYNKKCYVLESNILDFISFNENKNSKDSIESNAKNTQDSIESIDNFASNFELKARQIRYNFFFNLLDSKNYKNLITAHQLDDKIEWFFMRFLSGSGINSLLGFESVESRFYGGKEFKIIRPLINVSKSEILEYNKINNIEYFIDKSNENTKFFRNYVRAKITKNIESRFYKNIKKSFEYLQKEKEILYPKVMICVDFNLFYCKNSNFKSALHRIYIIDKLSKRLGYVLSSKQKNEIDELFFNLDFGREPYKECVMG... | 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)... |
A0A1D7W1G7 | MVEYQVMLNSSAVAQQIARGLASSGVTEVVIAPGSRSAPLIYALAPLAEAGVIRTHVRIDERDAGFLALGLARGLRAKQSRAGGVRTRAGTAGGRDGAVALVTTSGSAVANLHPAVLEASYGHLPLIAITADRPARLRGTGANQTIDDQSQVLSDVRVRIDVPAGSADAGQLFAEAVAHSLGLVTDPGSGRDLVTGAASDTESESGTGEVGPVQFNVQFDVPLVPTVTELAEWKAAVQSLAAKSANEASKSAFAGSDAVSYSDSAKDISVRILPGTVIVAGDAGGHAATALKSLAEEHAIPVLAEPSSPLTSELRDSSVV... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting s... |
A0A6G1FU29 | AEAKNKRNREIAVHHARLIQAQKDAEARILESIEELIEFPLSKDADPANPAASDLQRIQTLLAAFQPSDFDDLLEERRCADLCAYVLCPRQPRRQLGDSEFDLVWGVADMKILPHRNTKLWCSPECAKRAIYIKVQLIEEPVAFRKSGATPPISILKETSGDDPVVPDIRKPTADRNPDLSRALAQLALERGDKISSTRATDLMQSDIVEKPVSGAPAAPTQLAATGYGSIEGYIP | Function: Putative RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase involved in RNA polymerase II transcription regulation.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Nucleus
Sequence Length: 236
Sequence Mass (Da): 26033
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A0A351VM96 | MLKKGLVGKIAAVFGMVAVAAGIAFASSHGGAGVTPDEALQKLMDGNKRYVGNQMTGAKLSDSAARASLAKSQKPYAIVLTCSDSRVPPEIIFDNSLGEIFVIRVAGNIPDPVVLGSIEYAVEHLGSPLVMVLGHERCGAVTATVGAKGKSTGSANIDAIVKTIAPNIKSAVKNCEACKGDAKCADINKDAFIECVTDANARTVAANLTKKSKIIKHMAAEKKIKIVVAKYDLDDGLVTVFK | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 242
Sequence Mass (Da): 25155
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A0A6G1FY73 | MFNQNDRTFGGGQGHHRYGMQHTHLQNLGGVHQHQNFPHGSHARGQNSAHRYTSSGTPLSLAHQYDRHAHEEPSGSHIEELDESGNEQWKEHIKAYREYMQSGTPHYHAKTFARRPPPDIVKVNAADEDNEDPDDRSRAAIAKPKERSAWAGLDLSGQGLRLLSSALFRFEFLEELHLDHNKLVRIPPEIGRLKNLIHLDISNNLLVELPGEIGLLSNLQELLLFDNSLEHLPVEIGYLFRLRILGIRGNPIDHDVGPEIKEAGTENLIKYYRNRITPPPHPDRDWIGFFETSDQSQETFTALSYNILCQRAGTSAHHGC... | Function: Acts as catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover (By similarity). Ccr4 has 3'-5' RNase activity with a strong preference for polyadenylated substrates and also lo... |
B0W2Q2 | MNWCSEYFDRKASNPIESLVRQSTKVPCPYKKAGCTWLFGSSDMRSHLEECKFRPYRCIASKLNVLTCPWEGMQFQIEDHLMEDHAKLGEPFTYFQESEIPFSEQSSKGGIKLVDAFSKKFLFYFLSSAKARVAYFMIVYFGRREEARQYYYEFEIRSKSDSELRKIKFVQNCVSDCEDLSRCIVEEDCVAVSFKTIRHFLHEGTIPFRFIVKKKDDEPGKEGRERKLSDGSVTKPNKPRPTPFNFSEKGKLKPNLRRSTSSGSFSGGGGQSGPGKSGGAKKASEEAPSRKTSAPAQVGTSGVQRSPEFSSINRMGVSGQ... | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ub... |
Q9VPX8 | MIEVLCLLLGRILLLLVGGYELMWRLRERLNALAVRSYDLWRSKAAREAHERRVLADCRSQLTKTPQHLVLVISPVDAGVDAVLLSRIFDFALDVGIKHVSLYDRRTKGRGYVDMADLCRSTNADTGSCLKWPPVASPSKLENQPKNGQKTNGYVNGSHSPQLQLHQISASDGHALIADVCRELYEDSKTELVQSLLKQKREALTEQISDMLSKRLGFEAPEPELGIVFARQTCTYGLLPWHARFTEFHTHPSGRHFDVETFASILCKYSRCEQRWGT | Pathway: Protein modification; protein glycosylation.
EC: 2.5.1.87
Catalytic Activity: (2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = di-trans,poly-cis-polyprenyl diphosphate + n diphosphate
Sequence Length: 278
Sequence Mass (Da): 31475
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Q76NQ0 | MYVSKFEASMATNFVIYLALGALLCLATANGEIVNTNVERTLDLTSQLVKTTTKISAEDSAGKPIVEYVFFTSEPSLAYIDVKDASDKSVPFKRNEPVKGEQSFTFTFPRAAAKQTFIVETVASKGIRPHPEEIRQNDKQFVKYTGNLHLYSKYRTNSQKTNVKLSSSNILSHTQVKPFSVSSNKITLGPYENVEAFSQEPLVIHYENSAPFVTVNTLERTLEISHWGNIAVQESIQMTHTGAKLKGSFSRYDFQKEGRSGLAALKSYKTYLPASASGVYYRDTNGNISTSNMNAVRDFIELELRPRFPLFGGWKTQYTL... | Pathway: Protein modification; protein glycosylation.
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus m... |
A0A2I4EFW2 | MASGGGNTVEWQVRPPNPKNPIVFFDITIGNIPAGRIKMELFADIAPKTAENFRQFCTGEYRKAGLPVGYKGCQFHRVIKDFMIQAGDFLKGDGSGCISIYGHKFDDENFVAKHTGPGLLSMANSGPNSNGSQFFITCAKCDWLDNKHVVFGRVLGDGLLVVRKIENVATGPNNRPKLACIIAECGEM | 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: 188
Sequence Mass (Da): 20471
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A0A089QJB6 | MEWKIGDIVIPNQVVVAPMAGVTNVAFRMICKEFGAGLVVCEMISDKGIHFRNKKTLDMLFVDPTEHPVSVQIFGGSKETLVEAAQFVAENTATDIIDINMGCPVPKVTKTDAGARWLLDPDKIYEMVHAVTSSIDKPVTVKMRTGWDEDHILAVENALAAEEGGAKALAMHGRTRKQLYTGHADWGILKEVADHLTKIPFMGNGDVRTPEEAKKMLDEVGADAVMIGRAALGNPWIVKQTTHYLETGEILEEPTPAEKIKVAKEHLHRLVKAKGEVIGPKEFRSQAAYYLKGIPRSARTKAALNSADTEAEMIDIFDNF... | Function: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
EC: 1.3.1.-
Catalytic Activity: a 5,6-dihydrouridine in tRNA + NAD(+) = a uridine in tRNA + H(+) + NADH
Sequence Length: 330
Sequence Mass (Da): ... |
B0X677 | MAAAFQRRVHISVDDNITEDNADTDNDSISLTNDETEEEDDDDPPPSVQEVTLVTSSSLDRQDTVDSLVIEEASGREEPVAPPEDEVGLDALSANLADDHEETIRPAVVRAAAEAVLPTGWSMQLAPNGRVFFIDHNEKKTSWVDPRTGRASPMPNASSSAAISDSRRPEDGLAPLPEGWEERVHTDGRIFFIDHNTRTTQWEDPRLSMPNVAGQAVPYSRDYKRKYEYLKGQLRKPANVPNKIEIKVRRASILEDSYRIINSITKVDLLKTKLWIEFEGEAGLDYGGLAREWFYLLSKEMFNPYYGLFEYSAMDNYTLQ... | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.26
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.
Sequence Length: 568
Sequence Mass (Da): 65306
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A0A0K1R1V8 | MGMSNVNRMTWRLWSLQSSASLLSLVILSVLAIAAAFDGLGYPCYYAILVDYTTLNVSNYGSWEPAITPVLFLERLEMAFYVYATVVLLMAFGIYLLIGVILVGRLDVIDIKKFTRLVASNHLVFVLGFMFWAFGVFINLLAFKTIVLAAAFHTIYYGLLILFVIYSTTRGVSPNMYHTSNAMVKQPHKQLYNLVVYGKGVVINCLHICFALSTLMQCLLIELVIGNNFRLKIADVISIGIGLFCTLVVIFMLVSEIVLVRYVSGTIGIPLGAILASILIGIPTLRYETKFSYIINGETKRLNQLVSGLLGAVAVLAVIL... | Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network.
Subcellular Location: Virion membrane
Sequence Length: 412
Sequence Mass (Da): 46141
Location Topology: Mult... |
Q9VG87 | MATDVQSFYKDKTVFLTGGSGFLGKVTIAKLLCTTEVKRIYVLLRAKRGQEMRERCAAWDKDPVFGNLMKTNPEALKRVVPCGGDCQEPDLGLSNSDRQVLIDEVQIVIHTAATVRFVEPLHIALAVNTRATRLMIQLAKEMSHLESFVHVSTAYSNCVVEHVSERFYPEHLTCPAEKILELLESISPELLDKMAPALMGKYPNTYTYTKALTEQVIQKEAKDLPLSIFRPGVIIASYKEPMPGWIDNLYGPIAVLYGAAFGILHITLLNLKAQAGIVPVDYCVNMVLTCAWNTARDTSIKLSPEPPIYNFTPNNDNLIT... | 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: 502
Sequence Mass (Da): 57235
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B0WII5 | MDSMIRYISPVNPAVFPHLASVLLLIGIFFTAWFFVFEVSRPKLGGKEGVIFKELLISLFASIFLGFGILFLLLSVGIFV | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
A0A1C0W104 | MYVVIEGIDTSGKSTQIQELKLALQEAIFTFEPGATPLGKKLRKILLEDSIELDSRAEMLLFLADRAQHTHEILKANPDKLIISDRSLISGMAYAKDFDFETLKAFNLFATQGILPQKVIFLELQKEDLQQRLQSKNEDKIEQRGLEYLLELQQRTKAIIKKLQLPYISINANLPKTTITQQIINFIKE | 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: 189
Sequence Mass (Da): 21659
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A0A1L9D043 | MFRITKEFHFSASHQLKSLPSDHQCNRLHGHNYIVEVELSGEELNEHGFVRDYHELAPLKRYIDDHFDHRHLNDVLGHDRVTAECLAKHFYDWCKDRLPETSAIRVSETAKTWAEYRP | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
Function: Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
EC: 4.-.-.-
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H... |
A0A0T5YYC5 | MAKDAAKEDLELGDEKPGKKKLIIIIAVAAVLLLGGGAAAYFLLMGDEAPTEEEVAQEQEQAKEEGPAAEVEKGPPQYHALDPVFVVNLPGKPSLIQVGVTVRVRSDQMVEFLKHNDPMIRHHFLDLLGAKDGKVLKNREAKEALQQEMLDKLNGIVKELDGPGEVEALYFTNFVMQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell inner membrane
Sequence Length: 177
Sequence Mass (Da): 19383
Location Topology: Single-pass membrane protein
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A0A485KM72 | MQRIAARSARPWLYMVTPSISSSDKLVSMVEKALVGGVNIVQLRNKLFAADSAELKAMAVALRTLTRSYNVPFIINDHVSLALEVGADGAHIGQEDTTIADATALIDAENATAFLLGVTVRDAAQAALACKAGAAYLGVGPVYSSSTKQNANNGQTIGLDGLRAVVQTAQEYDVPVVAIGGIDIGRVGPCMATEAAGVAVVAALSGSADVEAAARALSAAVHQTRREC | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
EC: 2.5.1.3
Catalytic Activity: 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidin... |
A0A2I4DH32 | MSRTTVELDFFGMEKESSSSSSSSSKSQFQKFLDRQRSFRGMPSAISMINPEVLKSVIASTANQGSEACNAIPSKNLVSVPSSPVLPVYTPPIVRPSSENLPDTAPLTIFYNGTVSVFDVPQEKAENILKLAVEGTLNPKVAVPSSDQQQLLDSLGGGIADLGIPRRKSLQRFLEKRKERLTCVSSPYACYT | Function: Repressor of jasmonate responses.
Subcellular Location: Nucleus
Sequence Length: 192
Domain: The jas domain is required for interaction with COI1.
Sequence Mass (Da): 20848
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A0A2S2QV25 | MDIISIIKKKCQKEELTKDEMTFFIKCIVNGSIDQCQIGAMLMTLYLNDMTNIEVSNMTMAMANSGKILDFKSSSFVVDKHSTGGVGDKVSIPLVPALRATEEDFVIPMVSGRGLGFTGGTLDKLESIPGFSAFSFDYKQLFNIGNEFGCFIVGSDDLSPADSILYRARDVTATVDNSGLIIASIISKKAAAGIKYLVLDIKIGSASFFHSVDEAKTFGKQFVLVAKLMGIECRALMTRMSAPIGNYVGNSLEILESVNCLKGEGPRDLQNLVELIGGHLLHMTHKVNTVEEGRKRIAESLNNGTALEKFKQMLIKQNID... | Pathway: Pyrimidine metabolism; dTMP biosynthesis via salvage pathway; dTMP from thymine: step 1/2.
Function: Catalyzes the reversible phosphorolysis of thymidine. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis.
EC: 2.4.2.4
Catalytic A... |
A0A2I4HSS0 | MSRATVVLDFFGMEKESPHSSSSSSSSKSQFQKFLDRQRSFRGMQSAISKINPEVLKSVIASGSANQGSETGTPIPTKNSVSVPSSPALPVYAPHTLRPRTPESLPDTAPLTIFYNGTVSVFDVPRDKAENILKLAVEGRSDPKVAVPSSDQKQLLETLDGDLPIARRKSLQRFLEKRKERLTCASPYACYT | Function: Repressor of jasmonate responses.
Subcellular Location: Nucleus
Sequence Length: 192
Domain: The jas domain is required for interaction with COI1.
Sequence Mass (Da): 21003
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Q8INR5 | MSTVLAQKLWCTLWSAGSLGRFAQHMSNAAHQVSCIGSEEQRVYEEPHVIFQNWLMAAQKEAPQVRPRLACMATVDKSGEPVTRLTSIEEVNSHGITFFTTLGSRQAGEISANPHVSLHFNWAPLMRSVRIAGSAHQLTEEQVRDQFRRFPRHVQMSITHGPRYAAAEWQSRSGFFARIGQRLNTWLGKQPEEIPMPHNWGGYILTPSLYEFGMLSGEKAGRTRVRFRRCLEMPRGTRVGHVQAERQDWVYDSCDEN | 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: 257
Sequence Mass (D... |
A0A2S2QWJ2 | MTIENELIRLSVDDFPPRNKPLIAKYLRSFAFPVLSKLSPFNISKTGSYLEGNKNSILQKYGADAEKDITSVLTKLNTLRKEILSNAPFRELISDNVDVQIWNKLLEDYSDEDGKRPTWMFTNWLYCECYIHRRLFEAFETSIYLKTYDPFYEQKMKGLVSCEDAMKILGQFLINYFNKSEVEIKNLREDLPKIIKCALWGNRCDLSQTGGDAIAQTESPLKLVDSLQDLMLVDESSKAVDFLCNSLSITNDDKILDIILDNAGYELFTDLCLADYLVTYKFVNIVRFHGKAIPWFVSDVTNQDFITTIDYIANKSTCEG... | Function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate. Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function... |
A0A6J0T6A6 | MADDQPLTRVTCTAPVNIAVVKYWGKRDEDLILPINSSLSVTLHQDQLKTTTTAAVSRDFTEDRLWLNGKESDIEHPRLQSCLREIRRLTRKRCSESNGEGNSDRPPLSLTYKVHIASENNFPTAAGLASSAAGYACLVYTLAKLYGVEGELSEVARQGSGSACRSMFGGFVQWLMGEEADGKDSVAQQVAPETHWPELRILILVVSAEKKPVGSTAGMQTSVKTSLLLKHRAKALVPERMAEMIRHIQQRNFEAFGKLTMQESNQFHATCLDTFPPLFYLNDTSKQVIALVHRFNAHYGKTKVAYTFDAGPNAVLFMLE... | Pathway: Steroid biosynthesis; cholesterol biosynthesis.
Function: Catalyzes the ATP dependent decarboxylation of (R)-5-diphosphomevalonate to form isopentenyl diphosphate (IPP). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoids and s... |
F0TEE5 | MEKSFVFKFMGLNFDLTGIIGSTLMALTVFFICFWLARKVELKPNKRQNVLEYLLEFTNGIVKDNVSDVDAQNHLSLYAFVLFLFIWFMNQLGMFLEVKVDDWVFVKSPTADPVATMSFAMMTLLLSFTFGVQRFGVGGYLKNYTQPVGFMLPINLIEEFTNFLTLSLRLYGNIYAGEVLLTLIGNDLAHAGGPFTLILAAPLAMIWQGFSVFIGSIQAYVFVTLSMVYIGKKVTTE | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 237
Sequence Mass (Da): 26729
Location Topology: Multi-pass membrane protein
|
A0A1I8NHF1 | MCSMRLSGISWHSRRKTSCCTFSLGMLDNFCGTNGGSITEQPIQNVCHWDPTAILSEPYLAAGQGHGCLVLNRNIKSPSHVVKALWQNASVRCCVDGGTNKWLNFIRNELQNDCSIKLPDLITGDFDSISQETEEYFSSRGVKRIHTPDQNNTDFTKAVDVLKPIIREKKLRDIIVLHDTSGRFDQIMSNINTLFTRNDDFCNIYLLGSCSLTWLLRPGKHSIVIPPHLVEEQRWCSLLPIGHEATNVTTKGLKWNLKNSPSYFGGLVSTSNTYASTHIEIETNSTLVWSMGVFYFGDD | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine: step 1/1.
EC: 2.7.6.2
Catalytic Activity: ATP + thiamine = AMP + H(+) + thiamine diphosphate
Sequence Length: 299
Sequence Mass (Da): 33581
|
B0X4L8 | MTRRSHQNTPSSSINIRLIPFQLAGLCPFSPTSPALTIALLVWTFANLTLVVILLVKVTGSASLLFMDPDGGKGHQLNPILLIKSSFTIAAHVLVLVETLIQHVTFRRVEERLESTDKSLSMVGSKSGPSQRKLLFYLVICATSEVGNFWLAQPLYRTAWYTTVASQAVIRLKHLQHMQYVEGLSIRFRVLKKQLQQFVTTTNAAKDEEKARYSGGKFASHAKQQHSIDGNLPDCLRKVFIIKSTYLALWDAGQLLAGAFTLAQLANLLQNFVQCTCDLYTIYSHLYRNDHHFGDIFDTVLGLIPTLVALLLVLGSCEAC... | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 339
Sequence Mass (Da): 37903
Location Topology: Multi-pass membrane protein
|
A0A945LSD8 | MSTDSYTLPCVPLRDVVLFPHVSTPIFVAKGRALITVESLPPSATKLLLVAQRDARDEDPEPEGLYEVGTEAEILQVMRLSDGTIKLLLEGVSRCHVNEFYFEGDSLWADVRPIDDSEVESIDLLARCRGLMALFEDYLRVNQRIPHEVYAAIEGLGSVSAITDAVAANLPINNAERQHLLETFDPADRIKALTTLIDKEIELLKVERKVRSRARRQMNRNQKEFYLTEQLKAIQRELGNSDGVAGDGEELRQIAQKVRLPKEVSEKVEKEITRLEMMTPLSPEASVVRTYVEWLLEIPWANKTRDRNNLKEASNILENE... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
A0A2S2QMV1 | MPVKDMAYFMYNLFRLKKYLKYIFIIILFLIYYFGVFTHFFELDYFTDFEYPLGTNISKCIINMRSGNSDQLPCIKINPFEYDLLLANNNKCDKNIHLLILVKSSLNNFERRSVIRKTWGFESRFSDVFTKTVFVLGKSYDIDLEKRITDEHKQYGDIVQYDFIDQYFNNTIKTLNAIKWASTHCNNSRFYFFSDDDMYVSIKNLLRYLRNPFEYPHYLNQEIKGKQSQHNLPSDIELFTGYVFNSYPLRHQISKWYVSLNEYPYHMWPPYVTAGAYVLSHAVLIKFHYGSYYTKLFRFDDIYLGLLAKKLNISPLHCKY... | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 361
Sequence Mass (Da): 43426
Location Topology: Single-pass type II membrane protein
|
A0A351KHB1 | MEEINVHTSKNYKIFFSNVRDKLQNLIDEYGIKDIYLITDKNIYNLYANEFSYFKGIKGLYIINPGEENKNKDTVFDIYNDMLSKDCNRKTSIVSLGGGVVGDIAGFVASTFMRGLKFINIPTTLMAQCDSSVGGKNGFDFNGYKNIIGTFYQPEFVFVDTNFIHTISCQDYKNGLAEIIKYGFIYDDTFFDYIDANKEQIKKRNEDVINTMVYRSLKIKSDIVCMDEHDNGIRQILNFGHTIGHGIESASNFSIKHGEAVAAGMLIESYLSLKCSLLSTHEFKRLLDIINYFEMPTYFDDMNEKSIMKSMLKDKKRNDS... | Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP)... |
I2CSU1 | MSNYAAAFTGEIFQCDTTESFSTDVVYGLVVSVTSTPSSSVTVGGLLLNPKVGTSAGTLISGTYSLASLYLGRYSSSCFMEPTGGLIVSSGTESSVECDMAWMLETPAPSIVSRQSVCEPLATGIVSIDAMIPIGRGQRELIIGDRQTGKTSICLDTIVNLKYEKVLSVYVPVGQKAASVLDAYQQLVKRDVYQALAIVMASASTSAVMQYLSVYAGTALAEFFMYNLSLPVFIAYDDLAKQASAYREISLLLRRPPGREAFPGDIFYVHSRLLERSAKLNYACGSGSITAFPIVETLAQDVSAFIPTNLISITDGQLFL... | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
EC: 7.1.2.2
Subcellular Location: Plastid
Sequence Length: 464
Sequence Mass (Da): 49702
Location Topology: Periph... |
A0A1I8MLG9 | MLEFLNKSSLVIIFNCQSFYTGCRRMYRVEDNRLFTFSRICDEIAEERSYLNKAQILEKFFKKGCNNKEFKGDLLLWVRMLIPSDSQRVYNLQNKQMLKLFSRLFNTDTREMQLDLEQEGDVSETLRKFFENSNKLKPQKDSSLYLQDVEEFLVKLEQRSKEDEQTVLLKELCKQATSQDLKTIIRIIKQDLRMNAKASHVLAAFGPMAYSSYQATRDLAAVVKQFAFNKKQNNNILTAAAAPKAKKGKASAVSVQVMTPISPMLANACNSVEEAFRKSPSGLFSEIKYDGERVQIHKQGNEFKFFSRNLKPVMEHKVKR... | Catalytic Activity: ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
EC: 6.5.1.1
Subcellular Location: Nucleus
Sequence Length: 882
Sequence Mass (Da): 100614
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A0A6P9E321 | MRSAQLDEANREAEFSEAISRLTRVPSRLKVAVDEDFLLFFQMQVPGKLFPAELGTRSQILVSVHFPSHLQTCSPTERDPEMKPLCFQPSGAQQQPRPFADRPFLEPAIHKADYGQHKLLSFASQLGPQKNKQLAFADTIWEEGMSDEPPQVTVERIRQRQSRLESGLLHPCPSCPAFFGEGRIYSSRNVLQVLHFLGRQLFQLLWGPRRVQISAWGVNLVSDGSLEEFGTLEIRTMMEQLSDLSWQLCALEEQSGSWHQKELFLYAMLVSAWLFNMWMWLRR | Function: Plays a role in mitochondrial and peroxisomal fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface.
Subcellular Location: Membrane
Sequence Length: 283
Sequence Mass (Da): 32578
Location Topology: Single-pass type IV membrane ... |
A0A2S2QXH7 | MNGYKFFLFGCLFTSLTWSLSLFMYWKLNTKPDSYSQVKLYRRENTFEYVKKQKSKYFKSHVDNSDLEDLGIIKTDEDLVIRDKGYIDHGFNALVSQRLGNYRKSLPDTRHKLCSVIQYDQNLPTASIVICFYNEHPQALFRTIQSVIRRTPKELLHEVILINDYSDKPNLHEIVEQYLKDEKLLKVVNLKKTNKREGLIRARLFGANLATGQVLIFLDSHVEVNIDWIQPLLTRIHNNRTQIIAPIIDIIQPDTFEYKSSPLVRGGFNWGLNFKWDSLPKGTLTTDKDFVKPIKTPTIAGGLFAVNRDYFNEIGQYDSG... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 588
Sequence Mass (Da): 68256
Location Topology: Single-pass type II membrane protein
|
I1XMN7 | MVNIEIDGIPLKVDSAKMIIQAADEAGIDIPRFCYHKNLSIVANCRMCLVEVDKARKALPACATPVAEGMKVFTQSEMALAAQRGVMEFLLINHPLDCPICDQGGECELQDLSLGYGSGISRFSEKKRVVKDKDIGPLVQTDMTRCIHCTRCVRFGQEIAGIKELGATGRGEHMEIGTYVEHSLASELSGNIIDLCPVGALTSKPFRYKARAWEMTSHPSIAIHDALGTNVEIHTRQNEVMRVVPRDNESINQSWISDRDRFSYLGLKHPDRLLHPMIKQNGEWQTTDWQTALEFAVEGLKHVKIKNGADQIAGLISPMA... | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
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 ... |
A0A485KVL4 | MKHPSPPPPPESKGSSGAEDDDGDSPKTRPPRITGLDAPHSRDQFISCSGHVVSGLAFYAAMGCMLLPQTFAPSPTHTEDYELWKWIVLMAHVVLNALLVCAWVSCETCNPGDEGSSWLGVSLQGPRWEKSRYCAVCRKTVPGMDHHCTWLNTCIGRKNYAQFFTIAVCGVVIFSIQAFVAVYCTSVWRDWAAPRQVDFAVGSAAQACFILCALVSVPCLVMYTTLLAFHVYLFCLGYGTYDYFLKRRDALRAERRKKRNAQMELARQIEAIEALGKDASAAVVV | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 285
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 31480
Location Topology: Multi-pass membrane protein
|
A0A7J4JL85 | MARPVFPPAFSKRLLTLEGIYFGSGLESPLKSALSQAIDGKLSPTALGEGLRQILSGQATDAQTACLLTCLRLQGLEAPQLVAAVLALQEFMHAIHPNGDQPLLDIVGTGGDQAGTFNVSTASMFAAAGAGCRVAKHGNRGFTSKTGAADVLEKLGVNIGLSPAASARLLEETGACFLFAPTFHPALAYVAGVRRELGFRTLFNLLGPLANPANASTRLVGANSPENARVLAKALQRLGLAHCLVVHGSQGTASRAPGLDELSTLGKNLCIEVKGKASKEFFLRPAEFGFKPAALADLQVHSVDESAAAVLSVLRGEAGA... | Cofactor: Binds 2 magnesium ions per monomer.
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
... |
A0A485KZX7 | MHRLECVVQQYAWGKKGTNSVVANLKAASDKTFRVENDQPYAELWMGTHPNGPSSLADTSQLLSEWIKENPSALGTSIGDIPYLFKVLSVNKALSIQAHPDKDAAKRLHRDFPHIYKDENHKPEMTIAVTRFEALCQFRPMDQIIDSIQHVDELRLLVDPAVAQALVDARDLPTLRAFFRAMIYCDPEKAKTAINTLRARLESQRESLTPLEALVLRLNEQYPSDIGVFCPYILNYVVLEPGDAVFLGANEPHAYLSGECIECMACSDNVVRAGLTPKFIDKATLCEMLTYNVGSPPVCRGNALDAYLTQYESPVPEFQV... | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2.
EC: 5.3.1.8
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Length: 418
Sequence Mass (Da): 46183
|
A0A485L9H6 | MGDGGGYKLTVADLIKLIETPRESIEEALKQAGGTEGIAAGLRSSLTFGLDTSKTDDMMSREKAFGRNYVEPPKPASILELMWEAFHDTTIIILTLSGLVSLILGLTLEGGSTEWIEGCSIMFAVLLVVMVTAINDYQKEKQFAALNAVKEDEKIKVIRDGAPCEVSKFHLLVGDVVRVDLGDILPADGLIFDESEIKIDESTLTGESDLMKKSRHELPVMFSGTRVMEGVAKMLVVCVGVNSQSGIISALVQGKGSEEEKKKKKPPKESAVGPVNEVEVAKKEQEEEYEEATESPLQGKLNILTVLISKFGMTTSIIVF... | Function: Catalyzes the hydrolysis of ATP coupled with the transport of calcium.
Catalytic Activity: ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate
EC: 7.2.2.10
Subcellular Location: Membrane
Sequence Length: 1003
Sequence Mass (Da): 109465
Location Topology: Multi-pass membrane protein
|
A0A6J2MUB5 | MGKLMVLTLLGAGLALIGERVWMLRQKLNAFREVEPVDPHNCHLIEGIENGSEDIDILPSGLAFISSGLKYPGMPCFAPDEPGQIFMMDLNEQNPRVQALTISDGFDKASFNPHGISTFIDKDHTVYLYVVNHPHMESTVEIFKFEEQQHSLVHLKTIEHELLKSVNDIVVLGPEQFYATRDHYFTNFLSLLEMIMDLHWTYVLFYSPKEVKIVAKGFNFANGITISPDKKYVYVADVMDKNIHVMQIHGNWDLTQLKVIQLDTLVDNLAVDPDTGDIWAGCHPNAMKLFLYNHDDPPGSEVLRIQNVLSEKPSISTEYA... | Cofactor: Binds 2 calcium ions per subunit.
EC: 3.1.1.2
Catalytic Activity: a phenyl acetate + H2O = a phenol + acetate + H(+)
Sequence Length: 353
Sequence Mass (Da): 39889
|
A0A377HQE5 | MLENIRIVLVGTTHSGNIGSAARAMKVMGLKHMVLVAPECKVDGQAIALAAGASDIANNARIVDTVEEAVADCALVIGTSARNRSLEWPMLDPRECGIKAIEEAPQHPVAFVFGRERTGLTNEELQACNFHVAIPANPAYSSLNLAMAVQTLCYEARMAWIDSQAYKGEVKEQSYPLAEDLERFYVHLEQVLDKTGFINKSHPGMVMTKLRRLFNRARPESQELNILRGVLSSVEKQMKEAQK | Function: Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(32) in tRNA = 2'-O-methyluridine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.200
Subcellular Location: Cytoplasm
Sequence Length... |
Q9VQK9 | MFLMTAGTSNFLSAAWRSEAEESKSKENGSLCCCEYVAEDSRERSHILGCCCNCVDFDLVCTRLVTCRAIDRRNIDGMLIAFQDRLRLPWRGGAKRISPAAVAPAFIVPLMLGLATLNSKTAIVLMLTLVGFTIWGMELAKRTATRTNFFLSWLVFSVFYMIIIFEFQVPLLELAPEENYALMFFSCAALYCLYSAKALSPLNLVSAQYGTTPKDELPGIAEASSGEEQAEAQTTLQMESVLSLDDDEVGDMDTAERSGLMHGQPNICEICRKVTPRRAYHCPVCGTCVKRRDHHSYWLNCCIGERNYVWYIVGLALSEI... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 420
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 47014
Location Topology: Multi-pass membrane protein
|
A0A2I4E350 | MYSNFKEQAIEYVKQAVQEDNAGNYAKAFPLYMNALEYFKTHLKYEKNPKIKEAITQKFTEYLRRAEEIRAVLDDGGPGSASNGGDAAVASRPKTKPKNGEGGGDGEDAEQSKLRAGLNSAIVREKPNIKWSDVAGLESAKQALQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEAESTFFSVSSSDLVSKWMGESEKLVSNLFQMARESAPSIIFIDEIDSLSGQRGEGNESEASRRIKTEILVQMQGVGHNDEKVLVLAATNTPYALDQAIRRRFDKRIYIPLPDLKARQHIFKVHLGDTPHNLT... | EC: 3.6.4.6
Subcellular Location: Endosome membrane
Sequence Length: 435
Sequence Mass (Da): 48372
Location Topology: Peripheral membrane protein
|
A0A6J2LU38 | MDIKIGNKPAGCIQMLLHSDVVPMTTGLLSMANSGPNTNGFQFFLTCDKTDWLDGKHVVFGEITKGLDVLWKIEAQGSKDGKPKEKVIISNCGEYV | 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: 96
Sequence Mass (Da): 10472
|
Q9VB73 | MTRITWRGHSTQELLSILRLRWSYMKHCWHSLTFNAHMNSSYASDVCLTPIFWFVDNYTHCLGPFFVVGVAALTTSVVSIAYWIGLPFWWAKSQLVTYFLLIVGNWLLLNVVFHYVMAVITPAGHPPEGVSLVEAVSMCGKCIAPKPPRTHHCSICNRCILKMDHHCPWLNNCVGYGNHRYFFLYMTYTTLGCLFLILFGLEIGHKYLWLDHGENWTEIEPLEGQPVKFNLSGHIIPVTHPNEYDEFVLPPAVHNLPTPIVDTDAASPGRRRALWFMAFTNVAVVLALGSLSIWHAKLITRGETSVEAHINEAERKRHLQ... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 381
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 43802
Location Topology: Multi-pass membrane protein
|
A0A183EVY9 | MLQIVVLTSIDPAVSNLRRDVRPAHYDASKHEHVIENNYCNICLIYVSVILFDSTCKHCRTCNKCVPGFDHHCKWLNNCIGAPNYRWEIIS | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 91
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 10517
Location Topology: Multi-pass membrane protein
|
A0A163KK98 | MTRAQQTISIAMLLTSLYLAVFMELISFPEKFQKEVVPVIPFWALISFGAYLLFKLGWGVFTFNDVPQAHAELMTQIKEARADLRAQGVDVGADD | Pathway: Protein modification; protein glycosylation.
Function: Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit to the ER.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 95
Sequence Mass (Da): 10667
Location Topology: Multi-pass membrane prot... |
A0A4U8T4E0 | MSFIVAFMESKNGIFMQKSYKNNNVIKSRTLSKDSKSYKIYKDSNISNNFGKKVSKLDSNISNNLCEKVSNLDSKDSNISNNSLDSKNYDISNKNYKKIAIFGGSFSPIHNGHIEMVKLALKKLDIDKLIILPTFQNPLKDSSIFSPQTRLEWVKEVFLDSNIMDTKDSKENIESRFYKNNEITNLDSKKLENIESNSKDSNLTPVFLESIAKKILISDYEIAQNRAVASIESILHFKNLYNAKKIYFLIGGDNLFQLPKWKDFEKLKKVTEFVVFTRKDSINLNSPCGEKIDLQHIESKRQDSKKNIESNQKDSKKYYD... | 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... |
A0A1I8MV56 | MPPTKEINYKSIWSIEPAASSSSRPPNPNTQCSQRNTKEAYLEAVRIILLLLDNIINHPNENKYRTIRIENKTIKEKLLTLEGCVELLTSIGFQRSDDQYTLPNDSSLELIRSYRDALSKRREFWMNRKEDDALQAIPTNLSNINPATSLSAPIQASKPYRQRISFPRFLRTSNQFLASLEQYSDAVMQYEDEQLLAAGRQLIPIDELTQRASENYLRIQEESSKAVEEGKPAPKEPGIRDLILVELVAWFKNDFFEWVNCLPCKVCGSEESKLSRTVQEGDVRVEVGICCGQETKFHRYNDIAELLVSRKGRCGEFANC... | Function: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those ... |
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