ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
B2A8Z1 | MDTPPPRNHYTTLSLPPSLFSSGLTPEEIKQTLKKSYRRALLAHHPDKSTTSSPSVTIDEITLAYTTLSTPSLRQAHDLSLSSSGSGPAALGRHKLQTGIETIDLDDLTHHEGEEEDEWYKPCRCGNPKGFLVHESDLEEAANGGLEEVVVGCQDCSLWLRVVFGVVVQDQDQEGETPEQKKGETPAAERR | 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 facto... |
A0A6P7FLF3 | MTDPTQPQTIKIQHYGTVPAKQPKEKRVFLQSLRKPKPATQTPNKLLDYGAHPRRGRRSSMNFPREIIRGVYQLTQTINGYTIDSSIFRLNTNATVILLITFSLAVTTRQYVGHAIDCLHARDIPEEVLNTYCWIHSTFTVVQEASRRHQQNDQLSLSGIETTGKRAIKQIKYYQWVEFFLFVQAILFYTPRWLWKSWEGGKIHALMMDLDVAVCTEIEKKQKKKLMIDYLWENLRYHNWWAYKYYFCEILALINVIGQMFLMNRFFDGAFLMFGFEVLSFINSDQEDRIDPMIQVFPRMTKCTFQKYGVSGEQEKHDAL... | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 436
Sequence Mass (Da): 51738
Location Topology: Multi-pass membrane protein
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A0A174NBY8 | MNAIAQLRKDCERIGCICLADEPMAAHTSFKIGGPADLLLKPRDAETAARVIARARELSVPLLFIGKGSDLLICDEGVRGAVLSFDEASARPSLRDETVIDCPAGASLTALCCFALEQGLTGLEFAYGIPGSVGGAVYMNAGAYGGEIRDVVGSVRFLDGQGKLRALEECALELSYRHSYFTDHPDCLITSASFHLRRGDRDAIRARMDDLMERRRTKQPLEYPSAGSTFKRPKGAYASALIDGCGLKGRRVGGAMVSEKHAGFVINYDNASCTDVLTLIGEIQTQVREQTGFSLECEVKYIG | 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: 303
Sequence Mass (Da): 32665
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A0A0F4PYT6 | MDITALLIEAAWLMATGMVVVFVFLLILIGALRLMSYIFADTEQAQANQQASATTTHHSKRPSKAHIAAIAAAVHQYKKQ | Function: Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation.
Catalytic Activity: H(+) + 2 Na(+)(in) + oxaloacetate = CO2 + 2 Na(+)(out) + pyruvate
EC: 7.2.4.2
Subcellular Location: Cell membrane
Sequence Length: 80
Sequence Mass (Da): 8738
Location Topology: Single-pass membrane protein
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A0A949F6T2 | MQKIAILGSTGSIGTNALDVVSRFPGKFKVSYLSANSNIKLLAQQIKRFKPKAVCVGSGNVNGARVYRGEQGLRRIVKDMPVDVLVVGIVGSSALLPILAALPNIKRLALANKEALVMAGDIIMKKAKRNKVGILPVDSEHSAIFQCMAKDNAQEIKNIYLTGSGGPLLRTPMKNFKNITPHQAINHPRWKMGKKISVDSATMMNKGLEVIEAHHLFGLGVDRIKVVIHPETVVHSMVEFVDGSTLAQMATCDMRTPIQYALTYPSRVASPVKGVKFSELGALNFSQPDFKRFPCLEIAYDAAKKGKTYPCVLNASNEMA... | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 1.1... |
A0A356VB70 | MTRVFGVLGHPIGHSLSPLMHNAAFAARRLDGIYAPFDVPPAVFAEVVRGLVACGISGFNVTVPHKETIVPLLDTLVRDARALGAVNAVVAHRGRLTGHNTDTIGLMGALAELGWRPRRCTAMILGAGGSAKAVAWVLTRAPGTHVIVANRRLDRAQRLAEWLRPLRPRCRIEVRPLEPVDVRGCDLLVNATPIGMAHDADIPLIRGLGSRVMVYDLVYNRTTALVRRARRQGCVAANGVSMLVYQGAASFEWWWHRRAPIAAMRRAVERALRYNS | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydr... |
A0A6N8I2Q3 | MTDQLNIADRIWKWGNRTYIMGILNVTPDSFSDGGNYFDMDSALKHAAQMEEEGADIIDVGGESTRPGVTVPVSAEEEIRRVIPVIKRLSKESALPISVDTYKAKTAALAVEAGAHMINDIWGLKKDPEMADVAASCKVPVCIMHNRTNTGYDNLMEDILSELGESIELAVKAGVKDENIILDPGIGFGKTWEQNLTVMRNLNLLKELGYPILLAASRKSFIGKTLGLEVNDRLEGTLAVTSVGILKGADIVRVHDVLQNVRVAAMTDSMVR | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
Function: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7... |
A0A6B1AM23 | MADERAGRTKAYDYALPAELIAARPAERRDDSRLLVLDRARGRFTDAAFPALLERLSAGDALVVNDSRVFPARLLGRKPTGARAEILLLRPESDALRPFAPFDEADTRLWRAMVRPGGKLKPGRTVDIADGFAVEILESAADGTRLVRLAGDGDPWSLIQRHGRVPLPPYIVRDDAGSEREGRDDAEDRERYQTVYSAPSGSVAAPTAGLHLTRKMLATIESRGVRLVSLTLHVGFGTFRPVTATRIDEHEVAPEAYRFSASAAEALNATRAGGGRVFAVGTTSCRVLETVVAGGGTSAGGGSSTGGPFAPGRGWTNLFI... | Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxy... |
B7QF57 | MEAVKHLPIGLLHDYYASDSTLPWNITVHFQNFPEGQLLHCGSRAVVEAHFMSTVKEADMLKHRSQVMSSMQKKDHNQLWSGLLNSKFDQFWAVNRKLMERTGGEGFKHIPFRLYLSDCTLLQRLITPVTASGEKATLETLLQQVAPHVLTGDGAAFSVVTHGIQVPLDSPLQWMSEHLSYPDNFLHLCVLPTT | Function: Involved in autophagic vesicle formation.
Subcellular Location: Preautophagosomal structure membrane
Sequence Length: 194
Sequence Mass (Da): 21893
Location Topology: Peripheral membrane protein
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A0A834VAT6 | MRNLKNYPKFIFLLLFLITIVSFLYQIIRKCTDFRSPNRVLNSNTVSKVTIYFITPTYNRPVQEAELTRLSSTLLLMPNVHWILVEDASNRTGLINDLLDRVYKRRIYQFNYTHLYAETPIRFKTRLRDPNWLKPRGVWQRNEALRWIRENVPNNKKGVVYFGDDDNTYDPRLSEELITTEKVSVFPVGLVGGLLVEKPLVQNNKVFGFNSIWKTKRKYPIDMAGFAINLKLIHKFKNVFFSPYVPRGYQETHLLSQVIQSIEDLEPKADQCSKVLVWHTRTENPKIKKINNKS | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: 3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP
EC: 2.4.1.135
Subcellular ... |
A0A834R2B6 | MMKLNLIILALKSRFFILLLAFFTDYLIEDHQPDAYQNEPLTEHFIRSLNKNNTENLTRLDRILIPLLKPLARWDAQYYLSIAIEGSYPTEQHLAFFPLYPFVIRSISSLLSRWIVPSYLSQITLISLIGYLLNLVCFVISLLSLYNLSVYLFQDYKFCDEVAKLFAYNPASIFFTALYTESLFLCLTLLGLEMLYNRNLPFLASILFGLSALTRSNGLVSLGYLIFYHCIQIYLEFDRSKISKVKFFAQNAMKIFTSISMMVAPYLMYQIYLYHLYCSVQNQIKVEWCHYRIPISYGYVQKKYWNLGFFSYYQWKQIPN... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 455
Sequence Mass (Da): 53611
Location Topology: Multi-pass me... |
B7P6Q6 | FPRALQEGKLRDSVSMGASDTPLEEKTLTVVYGPDLVNVSVINFCCNSRETAQLWTDELLRMAYNLLSLNAPASRFLEKAHTKLLLTTDREGRLPVKGVLRMFAQHRDDRRRVERALDAVGLAAGKNDTLAPDRLCFDVFLRFYRQLVGRQEVDAIFERLCGGAKKKAMTVDQLVDFLNKEQRDPRLNEILYPYANPARAKDIIAQYEPNKSYVAKGLFSVEGFLRYLMSADNPIVSPEKFDLSLDMDQPLNHYFINSSHNTYLTGHQLTGAHHHARLHRGDGGAPPRSGSRPLPRALKTSDFPVVLSFENHCSPKQQAK... | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+)
EC: 3.1.4.11
Subcellular Location: Secreted
Sequence Length: 754
Sequence Mass (Da): 84202
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A0A174PPJ3 | MDKIGQTISFPGLGIGDFTVNRVAFTLFGQPIYWYGIIIACAFLLAIGYILKRARTFGVDPDRALDVVIGGVIGGVVGARLYYVAFTWENYAANPLDIFNIREGGLAIYGGIIGGLIVVIIMCRLRRVKLLPFIDLAAGGVILGQAIGRWGNFFNVEAFGSNTTAPWGMAGPSIAAYLEAHKDILAAQGVAVDPLLPVHPTFFYESVWCLAGFVLIALYTKRRRFDGELTLIYAAWYGFGRALIEGLRTDSLMWGNIRVSQALAAALTIAAAAVLVYVRADMKRQSGEKARRLYVDTEEGQSVVNGTFYKKPGAPAETDD... | Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,... |
K7U5D4 | MVPQIPDPCDDDGQDHRCPPAAALPPPWPYPPLPPPASHGRSTFVTALIIATSVLVFLALCLSILVFVRRRRLRRRREALLEAALAPAAAATFPDEGEGDGGPGGEVVHHVWHIRTVGLDNAAIESIALTRYCAGGVLGASDCTVCLGEFQDGELLRLLPKCAHAFHVECIDTWLRAHVSCPLCRADVMDPGAAAADADAEQPPGTDAADASAERSASNTPTTELERLDQQANEHHQELRVQIDQPDHSSSLELERRRRQVRHHGARAQNFRRVASMDSRSPPPVSAEVDPEGEPAGREEQGTCGAVCCEVSPEPAELKR... | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Membrane
Sequence Length: ... |
A0A0U5JMH1 | MLETANWIQKYFNQSPDAIFLFKNDDLLVSNEPAQRLVTMLNLDVNYLLQIGKNAWSQLENDDCASCLIKKRLTGATVPITFHSNATHPFHFSMVYRPLDDKESVFALTLENREQQQRLSQIEEHRILNQYVNEAHEKERQKISQDLHDSVAQGIYAAIMGIQRLATVQKQRNTEQFQAMSAAIEKQLQMTLKEIKGLALDIRPSVLDNFGLIPAIKALAKRLQNSTGITIDVIALTSAEKLQKNIQNVLYRITQEAINNAIKHAHSTEISIIVTDHNSYLQLEILDNGIGFDIDQHSGFNGHSLGLMNMNERVKAYNGA... | PTM: Autophosphorylated.
Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved ... |
B2AKY3 | MRLQTSAGLLPLISLTTALTETPFLGFPSPWISPDPSDAEWQAAYEKAAAFVSQLTLTEKVNLTTGTGWEGDRCIGKTGSVPRLGFEGFCLMDGPLGVRYVDKASAFPAGMNAAATFSKRLIRARGEAMGEEFRGKGVDVQLGPVAGALGRTPQGGRNWEGFSPDPYLTGVAIAETIRGIQSRGVIACAKHYILNEQEHFRGSVDVRIGDKTMHELYLWPFADAVRAGVGSVMCSYNRVNGTYACENEWVQNYLLKSELGFRGFVMSDWGAQHSTLGSALSGLDMAMPGDMMGPPSASSPPYGSHWGGALTQAVLKGEVP... | Pathway: Glycan metabolism; cellulose degradation.
EC: 3.2.1.21
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Length: 872
Sequence Mass (Da): 93580
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K7USX8 | MRGQTETGRWRGGDGVAAWWVAVVALQLGHSLSRARAGLLESNPGLAYNFYQSSCPSAESIVRSVTWAQVAADPALPARLLRLHFHDCFVKGCDASILLDNAQSEKTAAPNLSVGGYEAIDAIKAQVEKACPGVVSCADIVALAARDAVSYQFGASLWQVETGRRDGGAPSLASDALGALPSPFAGFGGLLAGFASRGLNLTDLVALSGAHTIGVASCSSVTPRLYQGNATSVDPLLDSAYARALMSSCPNPSPASATVGLDGGSPARFDSGFYARVRQGQGTLASDAALAQNAAAAQLMADLSTPASFYAAFSMSMKKM... | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor... |
A0A1D6F699 | MKGRLLFKSPLPRSYLSHTSSVTSAAVATHRVYQVWRGKNRFLCGGRLIFGPDASSIVLTVALIMTPLALFVAFVSFRLAEVIGKPLGAAVPVTAVAVGVFDVVVLVLTSGRDPGIIPRNARPPEPDSFATTTTEMSSGSPATGASWSLPPTRDVYVNGVAVKVKYCHTCMLYRPPRCSHCSVCNNCVERFDHHCPWVGQCIGRRNYRFFFLFIASTTFLCLYVFGFCWVDLLLTSRRRGGVGIGRAVAESPVSGCLIAYTFVTAWFVGGLTAFHSYLVCTNQTTYENFRYRYERKANPFNRGAGSNVAEIFCSPVPPSR... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 455
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 49387
Location Topology: Multi-pass membrane protein
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A0A653GXU5 | MNAWIYISHVEKLVENKNKHLSDLNFFLEEEKKDDNNELTSNGEDSQSNDNIENESDVDIVDDSNDSDGSDDSNYSDDDDNLSNNENDKKSDVTKKMDKAKKQDNAQQSDEEKQSDEKKQSDEEKQLEKAKQLAKAKRLDKKKINEIRKTLSSNCRIIKVENEQIYIASWNSIKKNTPINSYIIDKLINKFLYTKFLPCQSTTLEYTLLYKNGSNSILNGDMYIEAPTGLGKTLCYVIPILDYYLSQNDNTFFCVILTPTEELVKQVTKVITMFDIKNLIISTIKPKTYNTNMCFDEINNENDFYKSHVNTNEQRFEQKN... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 657
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 76869
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A0A223MFD4 | MSRKLRRTKIVCTMGPATDRGNNLEKVIAAGANMVRMNFSHGVPEDHIERANKVREIAARLGKTVAILGDLQGPKIRVSTFKDGKIFLNIGDKFTLDADLPRGEGHQDAVGLDYKNLPNDVVPGDILLLDDGNVQLKVLSVEGVKVHTEVTVGGPLSNNKGINKLGGGLSAPALTEKDKEDIKLAAKIGVDYLAVSFPQSSADLDYARQLAREAGLEAKIVAKVERAETVATEEAMDDIILGSDVVMVARGDLGVEIGDAALVGVQKRLIRRARKLNRVVITATQMMESMIKKPMPTRAEVMDVANAVLDGTDAVMLSGE... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 479
Sequence Mass (Da): 51512
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B4FTH5 | MSMDRMARRSVSLLLALALLAAAASADSWLYEKFTTEGNVRADYNAQGQQVTSLILTQQSGGAFSSRQKYLYGEFSIQMRLIPGNSAGTVTSFYLSSGDGPGHDEIDMEFMGNASGQPVVLNTNVWANGDGKKEHQFYLWFDPAADFHTYTIIWNDKNVIFKVDDLFVRCFKRYPDLAYPGGKPMSVHATLWDGSYWATQQGKVKVDWSAAPFAVSYRGYSADACVPDGDGRPLSCPAGTDRWMSRQLDAAEWGTVAWARQNYMHYNYCDDGWRFPQGFPAECSRN | PTM: Contains at least one intrachain disulfide bond essential for its enzymatic activity.
Function: Catalyzes xyloglucan endohydrolysis (XEH) and/or endotransglycosylation (XET). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construc... |
A0A0U5JSW2 | MKIYTRNGDKGQTRIIGKQILYKSDPRVEAYGEVDELNSWVGYTKSLINSHTQVLADELEEIQQLLFDCGHDLATPVDDERHSFAFKQEQPTAWLEGKIDSYTQTVPAVKKFILPGGTQLASALHVARTITRRAERQIVQLMREEQINQDVLIFINRLSDYFFAAARYANYLEQQPDVLYRNSKDVFH | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
EC: 2.5.1.17
Catalytic Activity: 2 ATP + 2 cob(II)alamin + reduced [electron-transfer flavoprotein] = 2 adenosylcob(III)alamin + 3 H(+) + oxidized [electron-transfer flavoprotein] + 2 triphosphat... |
A0A9E8G491 | MDPIIKRLNKELLEMKNNPPLNCSAGPEDEDNLFKWTATIYGPEGSPYEGGIFILDIDFPLDYPFKPPKIIFKTKIFHCNINYQGFICLDILKDKWSPALTISKVLLSICSLLDDQNPNDPLEPEIANLYLDNQEEFIKKAKLYTHLYANL | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.23
Subcellular Location: Nucleus
Sequence Length: 151
Sequence Mass (Da): 17365
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A0A0D6XQY0 | MINLFEHYDKQTQTLYDTLRIAGYDNDTIVLEDDGFLPEHFITPYRFFAQYKVPKNATARYFNQVGIPRYWEIMGNNQSATVRDVNKQRATIHYHRPSKPRIVSHVEWLDEAERLLYVDHYTQHGVLFAQTFYDLAGKRIFRKYLDQQGAEVIYENFVAQSIILNWKGKAHHFNNKVQFIQFFLRALDKARNGFVINTLGLPFSVLYHLDEPGNDLIFWQEQCHGHVPGNMSLVLQGGLVRDYHVIVPDSQEYEILKQQVDDNMQQRLIPAGYLYDYASKNGYTSNVVTMTNSDQIHHVEAIVEACPTATFHIGAVTEMS... | Pathway: Protein modification; protein glycosylation.
Function: Required for polymorphic O-glycosylation of the serine-rich repeat protein in this bacteria. A stabilizing protein that is part of the accessory SecA2/SecY2 system specifically required to export serine-rich repeat cell wall proteins usually encoded upstre... |
A0A1D6EQP7 | MAGRARHPPFRLMFYLIGLLASLIPATSRAQPPETVTVGLIIDADSPVGRIASTTIPMALDDFYAALPNSSTRVQILQHDSGGDVVAAASAALQLMTTQGARAILGPQSSVESAFVADLATRAEVPVVSFSATSPSVSHSEARFFVRAALSDAAQAEAIAALATYFGWRRVVPIYQDDDYGAAFVPFLVDALTAVRAEVPYRCALPSGASRDAVAAAMYRLESEQTRAFVVHARPALAELVFAAAVEAGMMAEGYAWVITDGLTGLLGSIHPPQGVIGLAPHVPSTARLRDVRKRWAHKFMRQHRDADLAQAEMGCYALW... | Function: Glutamate-gated receptor that probably acts as non-selective cation channel.
Subcellular Location: Membrane
Sequence Length: 980
Sequence Mass (Da): 105452
Location Topology: Multi-pass membrane protein
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A0A1D6LFH4 | MAARRGGMASGAGAAAAHIASSMVLSLLLVGVGVSRAQLQVGFYSDYCPDAEDTVTAAVQDAAGNDPTILPALLRLQFHDCFVKGCDASVLIRSASNDAEVDNGKNQGLRGQNVVDAAKAQLEDQCPGVVSCADIIALAARDAVAMTGGPSFDVPTGRRDGLTSNIRDADVLPDAGDSISVLRSRFAASGLDDRDLVLLTAAHTVGTTACFFVKDRLYSYPLPSGGRGPDPSIPASFLAELEDRCPPGNFNTRLALDRGSESDFDDSILRNIRSGLAVIASDAALANSNATRALVDAYLGPWAGSFEQDFAAAMVKMGTI... | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor... |
A0A2K1J8C2 | MSRMGSRSVYRAVSCFARQIGKQKGTADDGFAVSRRTMMMPRWFVAPRNSANSMVSNGVESQQPTMVASGVYQTHSSVTRILPLQVGGTPNVVKIREEYPSQSASAELTKERGLEGESESWSRLSDQGRLATRVDAPENEPGSSPSSNSVTGERQAHSTHEARKNSVDTRETAKFAAIASTWWDPKGPYKPLHIMNPTRVSYVRSQICKHFGKDANTPRPLEGLKILDVGCGGGLVCEPLARMGGEVTGVDAVDKNIGVASVHAARDPATASIKYVCTTAEHLVQEQQKFDVVLALEVIEHVADPEDFCKSLAALAKKDG... | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Catalytic Activity: 3,4-dihydroxy-5-all-trans-polyprenylbenzoate + S-adenosyl-L-methionine = 3-methoxy,4-hydroxy-5-all-trans-polyprenylbenzoate + H(+) +... |
A0A2K1L437 | MSAMAARVQSSCKMLPCMSRLHSIYLSSRRVTFTACSASKVDPPNVSVLCEKARLTLTAEEVKDFEPQIGRIVDWFAQLQDIDLDNVPPAIRVGEIDPTKTLRPDMAQLFPDREAMLASAPDRDGPFLKVPKIMKENQE | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in chloroplasts and mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glut... |
A0A8S1AFC0 | MINWSDEMRAQDYGYFCKIACQDATEKPIWIVSDIRRKTDIQWFKETYENIIRTIRITADENTRKERGFIFKPGVDDVTSECDLDDYTEWNLVIDNGKGKQKLEEQLGSILTLLSNL | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 2/3.
EC: 2.7.4.2
Subcellular Location: Cytoplasm
Sequence Length: 117
Sequence Mass (Da): 13760
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A0A0N4U2H9 | MFAFLMFCRANLVERYRALFVLRNLADDRAVHWMAKCFDDTSALLKHEVAYCLGQTNNLTALPILKTVLQDENQEIIVRHEAAEALGAIGDESSVAILQKYAYDKQQELLETCQLALKRIEWRLEQKAIGKDFIDRSPYNSIDPAPAAEENDVELLGQLLLNPTKSLWERYRAMFALRNINTDKSIATLAKGLQCKDSALFRHEVAYALGQVASNVAFEQLRLGLENIDENPMVRHECAEALGSIGSPDCEALLTKFLCDKEHVVRESCVVALDIAEYRNSDDIGYIVDSTAESPS | 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... |
A0A183JFP7 | LTPEKTYKASTASGAITLEIGQQISIDLNIVDSKQISLTAHQVFIQLTHQKTQQAITYTCTETITDKKSEKKSYKLLLDPDSSAAEFDYLSGIYKVDLIVGDSSIKAPILWHMFDLDLRFVGEAGDETKRRIAQATDISRQESSSPAGSRRAFTPNAIIGSGPTTAKPEIDHMFRAPEKRAPPFLALTFTILCLIPLLGLIIAWSVIGFNISNFKFSISNIIFHAGLISICYLYFVYWCRLDMFTTLKYLSILGVPTFLAGHRVLRAQVIAKQQQTVSSTQSLNVKK | 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... |
A0A0R6LUQ0 | MSNVNIFSILSIILNFSLVLIILVRSPNEQSLQENLDPFKLFESSSRAEKSIDKLIQILTILYFVLALVYTIQRYF | Function: Involved in protein export. Participates in an early event of protein translocation across the chloroplast thylakoid membrane.
Subcellular Location: Membrane
Sequence Length: 76
Sequence Mass (Da): 8825
Location Topology: Multi-pass membrane protein
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A0A077HC08 | LMLGAPDMAFPRLNNMSFWLLPPSLSLLLLSSMVENGAGTGWTVYPPLSSNMGHMGSSVDLAIFSLHLAGISSILGAINFITTIINMRPMSMTYEQIPLFVWSVGITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP | 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... |
A0A6C2YNZ3 | MSNPPESAANQPEPAASVHSASPMVPNPAHSEGDAALQALQQTVAAVTPARLLVGRVGESYRTQTLLQLRADHAAATDAVHAPLALSESWLREYKFLVVQSRAEDRRRYLLRPDLGRQLSAESQSILRESGHLECDVQLIAGDGLSATAVQNQLPTLFPMVWNQLRDQGLRLGRPILVQHCRVGILNAIGEILRPKVAVLFIGERPGLATAESLSAYLAYSPQPGHTDANRNLISNIHDRGVPVADAAPRILALIRAMLAQRISGPAIKESLPGILPPYSESPE | Cofactor: Binds between the large and small subunits.
Pathway: Amine and polyamine degradation; ethanolamine degradation.
Function: Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. Allows this organism to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of exte... |
H9WPM9 | MSQAAQIPIKDNPQANEAASALIQADKLREVKAGHDGTWAAHPGLISLIAEVFDKNMKHPNQIDLKREDVKV | Pathway: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2.
EC: 2.3.3.9
Subcellular Location: Glyoxysome
Sequence Length: 72
Sequence Mass (Da): 7884
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A0A090L7A1 | MNIIIILLFFFINIFSYISSKGVLEVKLISFISKSISPIEINVCIKEYQTIVEDTGDCRFGTKSIILPKGYYIPEANSNISHVLIFPFDMTWPKSHSLIVKGKLLNNDEVKVNDSVVIIYKQSFLHSGNLFLDVGKAENTNASIHFFSSIKCDVNYYGTDCSKICYSNVFENEHVECDQNGKPICKEGWSGIKCDQPICKFGCGLNGKCVAPDTCDCLSGYTGKSCEECLPSVGCQNGYCKNKGNECICNEGWAGEFCEIDIEPCHKKNKCKNNGVCLNGKDGSVRCECKGRFYGKYCQHEKISCSSFPCQNGGTCVMTS... | Function: Putative Notch ligand involved in the mediation of Notch signaling.
Subcellular Location: Membrane
Sequence Length: 516
Sequence Mass (Da): 58254
Location Topology: Single-pass type I membrane protein
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A0A183I4Y7 | MTIHVSSSKDQSKNSELLVCLKQFRNEWFRYCCAAVFTIKFLLIPCYHSTDFEVHRNWMAITHALPICSWYYDDTSQWTLDYPPFFAFFEYFLSQVASKIIPSALILQKGAYFSTELLYFQRFSVIATDIFYILSCVFLTKSFFGRCKNDSSIEKNSLAAEIFLITNASLVMIDNIHFQYNGILTSILLISLGWIMRNSFLRGPNIKLNSAVIFTGPFIYSCGLDILKQIWRRLFPFERGLTHAYWAPNLWAFYNFADWYFYQVLKLTKRLPSNVQSPTYISGLVQEFKHSILPPVSPFGTLLMTLALLLPILSLIRTRH... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 451
Sequence Mass (Da): 52342
Location Topology: Multi-pass membrane protein
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A0A183I7S1 | MYGQYREAGSLLYRGFSIEKFMHQCYGNAKDIGGGKQMPIHYGSPEHHFVTISSPLATQLPQAVGGGKQMPIHYGSPEHHFVTISSPLATQLPQAVGSAYAFKRFRKVRDFAVY | Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
EC: 1.2... |
A0A183KJ81 | MAEEHLADPHSRIDEGDCLNGDREKAIEYDQLMQPLLVHPISESYPWLPKFYFVPTEELEKERRCRGSAIRKSSFRLVGESRFLWGQSIYIISQLLISGCLLPSDLDPIGRRPSHRFSGMSSTLGNELLFSGKSMNVTIQVVLISESVRLQQVLATYGIITQTPVQVEPIQIWSPDQLVRVGKFMGCSERLGLSGRPPRPYGQLGTSKFYRQVIVLSKIVFWQMIVIII | Pathway: Glycan biosynthesis; glycogen metabolism.
Function: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I.
Subcellular Location: Cell membrane
Sequence Length: 229
Sequence Mass (Da): 26023
Location Topology: Lipid-anchor
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A9U4D9 | MSMEKSPPPHNGNYPSYYAPPRKHEKSHWPIFTLVAVVANIIVFIVVMYENNCPAKIGPGRTCVLGSSFKRMSFQPWSENPLLGPSSATLVKMGGLRTVLVVDQKEGWRLMSCVWLHAGVFHLLVNMIAVLVLGLPLEKTFGFIRVGVLYLASGLGGSLLSSLFNQNGVSVGASGALFGLLGGTISDVIINWSLYSNYCGVLLNLIILAAINLAIGLLPLVDNFAHIGGFLTGLLLGCVLLMKTQHGYVPRRDLLDPNMERPVKNRFNAFQIILFIISALVLIAGFIGGFVALYNRVDAHKKCSWCHYLNCVPSSHWTCD... | EC: 3.4.21.-
Subcellular Location: Membrane
Sequence Length: 321
Sequence Mass (Da): 35072
Location Topology: Multi-pass membrane protein
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F0WCN9 | MMARWQHERLIGQHAGHFEILQTDILTFGDHFAPIMEPCVLIALEVLDNLPHDKVSVRNGEWFETIVTSNGENTQRSGDPSPNTITEAERKLQDPLILQTIEYFGCDLPLNKHQSLRTSVVHWLRELMGEELELTKAFIPTGSIQLLNTIKSSFPRHRLIAADFDSLPPPHLCRSSPIKPLYHPMSQTSLCSGTLHAANAPIVASKVQGETVDHDTYLIQKGDVDILFATDFERLKKAYCQVQGCPSDNVSIVKSSAFLKTFADTRKTRTISRYNPMVEDFSNTSFLLS | Function: Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine
EC: 2.1.1.320
Subce... |
A0A183HDD0 | MIDLEATFEKLENELQEVNQNEEMLKKNFSELTELKHILRKTQQFFDEVEHGRWPNTRREEHQHRFIPEEEQSLLSESRSTAAGTETIVPPNASVGSGLPEQIVLQETEGIGIELSGAVTGQMFANF | Function: Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase.
Subcellular Location: Membrane
Sequence Length: 127
Sequence Mass (Da): 14497
Location Topology: Multi-pass memb... |
A0A183L1J1 | MKFMLNGALTIGTMDGSNIEIFQEVGHSNAFVFGRTIEEVNYLRKTGQVNEAINLTFFSKDLLLVIRRIKL | Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
EC: 2.4.1.1
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + phosphate ... |
A0A183I5E0 | MLFLRMKSKANPKSYYAWFYRLWCFKQLTNPDIAAELAACEKFLNLDGRNFHCWDYRREIAEFGAHSAEEELKFSDRLIDANFSNYSSWHYRASLLPSLFPDPEKQMIVNQQTLYNEYQKLQNAFFTDPEDQSAWIYAEWLLLSDQKKKKCELVSMSSEMMNRKAFRAKNSYRFEIAGELAECQLRPSLSEPYEIIDMERGYVNFEEIYQIYHIRCKPVSEARRHIIEKVMDNCQELLKELEVEQKKEILKWPLLTYTFAILELEPIEMLSTILTNLEELATKVDPQRCQMYEEMAMNLRISQKLREKLGDVHRIDILFR... | Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to cysteines occuring in specific C-terminal amino acid sequences.
EC: 2.5.1.60
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Length: 3... |
A0A183KD84 | MYYNSKFILRHVDSNCQLIPPSSSNSDTNTIQLTDPSSSAITITNPTSRIESSPNEQGIDHVDKNRRIGEIVLGLDIAPGEEPLPEGWELARTASGRKFFINHNEHTTTWDDPRVIRPNNQITNGSLLTHEAQRHVMKDLGPLPPGWEERVHSNGRIFYINHNARTTQWEDPRLERLGGPAVPYSRNYKQKYDYFRSRLRAPRDPQAKFELRVTRAGIFEDSFRLIYGIKRPEVLMHRLWIEFIGEKGLDYGGVQREWFFLLSREMFNPYYGLFEYSAASLDQRLEQSSVYPRLRTNNAVTTTTTTTTTTTTTTTTTTTT... | 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: 325
Sequence Mass (Da): 37337
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A0A0N4ULB1 | MENCKYKCIVITNQSRYLSAGAIVFHNRNINFTTLPLNRHSNQLYVFLNAESPIYTLKMPDEMNDNYFNISMTYRKDSDIPISYGVMSRISNTTPPDKIWSWDQVIKVVNNKTKSVLQLVSHCSSNSARHLYTDTLKNFINVTVFGHCNQNPCDEECEEMALKEHRFYLAFENSVCRDYVTEKAFHSMNNLLIPIVLKGSLCKNILPEGSFIAIDHFNSPKELAQYLKYLESNKTAYMR | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 239
Sequence Mass (Da): 27695
Location Topology: Single-pass type II membrane protein
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A0A090LB86 | MGTKLSVSLENSMSPNTAPRTDRPPTFDPLYGFPKGRKPREMKVTMEEMDEWKLNNGQRDYCAHHLIDLLKCQRKYAPLAGHACDTERHTWDRCEYDDYIMRIKEFERERRLLKRRARKEGLE | 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.
... |
A0A481U5Y7 | LYFIFAAWSGMVGTSLSMMIPTELGNPGSLIGNDQIYNVIVTAHAFIMIFFMLMPIMIGGFGNSLVPLMLAAPHMRFPPMNNMSFWLLPGSIC | 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... |
A0A2R3VHR3 | FIFGSWSGMVGTSLSLXIRAELGTPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLMSSMVENGAGTGWTVYPPLSAGMAHSGASVDLAIFSLHLAGISSILGAVNFISTVINMRSMGMTFDRMPLFVWAVAITALLLLLSLPVLAGAITMLLTD | 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... |
A0A653H3Y2 | MVKKRESACDTSLIKKEEKKKRSSTDSGSKRHNDESFNLVYTYILLHYFFENSKMKIINEPFYLQDNVLTITEKLIGQLFWVYDDTTNELYGSRLIELESYNGISDKGSHAYNNKKTKRNMPMFEKGGISYVYLCYGVHYCMNIVTNVVNIPDAILIRAVEPIYNVPFFFLNKFLKYYKQKNNYINTNLLNQKKQQHQKVENVINNLLKKKKIKINYDMDKVNDVIDKVNDVICKEKNDKKNDEKKDENKYSKQIEELTDISKIINKKKLAKIGSGPGCVTKCLGITIQDNNKSFFFENKFMEVDSNENSSDNLLNINSN... | Function: Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.
EC: 3.2.2.21
Catalytic Activity: Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine.
Sequence Leng... |
A9SY86 | MAAAAGSAGVVCWSRAEKQHAPVRGGGTSVTSSTSGSGHASLKGSFDRLQGNRLLPQALTMPSLFRAKRNGRRTPGNAVTNFGKSEFHREISGSTRATTQVAEATTAGLRETIEDRAIIDGHSHSFEGIQSEEELMQVIEKEVESGRLPKRAGAGMVELYRNYRDAVVSSGVENAMDIVVKVMSTVLDRILLQFEEPFTFGSHHKRMVEPYDYYTFGQNYVRPLLDFRNSYLGNLKIFDQIEKNLKEGHNVIFLSNHQTEADPAVMALLLEHSHPYLAENLTYVAGDRVVLDPFCKPFSMGRNLLCVYSKKHIHDVPDLA... | Pathway: Lipid metabolism.
EC: 2.3.1.15
Subcellular Location: Plastid
Sequence Length: 494
Sequence Mass (Da): 54767
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A9S9A5 | MDAPENDLCRAGQSPPGHPLLKSWNPPTQHSFTKAQLRTLISICDAFSPSLSPPAECEEKQEIASFYTCSASDMGVPEDIAGLLHVLLKPQLLMAIRVFLWLLSTRIGTLILGGRASLTTQFPFFQSFAYLSTDKQEDILRGWSLSTLGAFRAVYKLFKMITMWAVYTKIENGGFNRNWKAIGYCGADPQVIRSRKCSSNDGVRSNPLQDMVIATQAAGDKLEKVLSRAGVKVLNDDIPLKKLASGNRNRNNSAAGGDLGISCDVVVVGSGCGGGVIASVLAKAGYQVVILEKGKYFRTEDLTTLEGPSQMAMFEKLGSL... | Function: Long-chain fatty alcohol oxidase involved in the omega-oxidation pathway of lipid degradation.
Catalytic Activity: a long-chain primary fatty alcohol + O2 = a long-chain fatty aldehyde + H2O2
EC: 1.1.3.20
Subcellular Location: Membrane
Sequence Length: 775
Sequence Mass (Da): 83906
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A0A061RWW5 | MESGSSSASDEQIMGAIKAQLDAAMFQEFFNGVRDKCFEKCVTKPGSSLSSSEQTCLQRCCDRYQEVTAITEQAILKMSGLK | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer me... |
A0A183KKU3 | MGFLSNDFYKNSFESYISKGGPLGELVQWTDLIGALYILGHNITITFEAVEAKLTPLCKFRILDTFGTEALYNRKKELWSGLHLNLQQFYTFFPHSPDNTFLGFVAEILPPKSKFSHQSSFKPVALVYGKEAYMWSNKTNYLRILSDYFELHGNVMDNVDKLPKFVHIHQMQYGQPYLELMSKAQVSLYAIAFMLNCPVKKVGFFFSVL | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-... |
A0A183JIQ4 | MNEHSLLLAYLGLPLTPSDLLILLTSPESNSFSVSPSNTTAPISSSSSSSTNSLNFIQPEKLLHISLLSESLWLARLITSWCLTGRQSLSRQIYQSLYNRYVNNDKTNNTLSIIHDLIPYPNTHLPNLIQLPKEYTNLLLLATDMDCHAEGHTHSDLSLCLVCGHLACLFCYGCRQFEQKTDSSIFGSGTSTTIISNNNNSSSSSNNNNNQEFAVYRMQAHSRRCHSGYSLLLRIHSCRVILLSDQARRITEMPAPYRDSFGETDPDLRRGNPLFLVESEYERINQLWISHQLASSTSSDLITPSNLQFGLY | Pathway: Protein modification; protein ubiquitination.
Function: Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
... |
A0A183KPY7 | MLADMNKDVTNCPVNNCVIHTDTTRWIQSDLILIPNRQFPSGKRPHQQAWVAFEYESALHTRFSDELNDKINFTASYRFDSTIRTPYGMYTPNEPKTDDINKTIHSTKLENIAKGKDRAVAWIVSNCYPRSPRNVYANELAKYITVDVYGRCGRMTCSGSQCFDLVRKHYKFYLSFENSLCQDYITEKFFFNALM | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 195
Sequence Mass (Da): 22717
Location Topology: Single-pass type II membrane protein
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H9X2B7 | TFYHLTFVLDKSWHVLGLGYNPNVDSTEIERAAVIHYNGNMKPWLDIAIPKYRHYWTKYVKYDHIFLQLCNISE | Pathway: Glycan metabolism; pectin biosynthesis.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 74
Sequence Mass (Da): 8888
Location Topology: Single-pass type II membrane protein
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A0A4Q9M3L5 | MNNNYKIIKENKNTRDIKKWALNLTIENMKQYNSTSLYKYTKNKSISNKKSEFIICYFLNKKVGFCMIRKENRLIFIYEIHVTFEHRSKGVGTLLLDFCKKYYLNQKKYENLVLFVLKNNYKAISFYEKNNFLIDKSYDDSILHYCYKFNLNNKF | Catalytic Activity: acetyl-CoA + N-terminal L-seryl-[histone H2A] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[histone H2A]
EC: 2.3.1.257
Subcellular Location: Cytoplasm
Sequence Length: 155
Sequence Mass (Da): 18896
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A0A183JUE9 | MGLGKTVQTVAFLASTLHDWTQEFAKFLPAFRLVPYWGTPTERKVLRRFWSSTRSSNAESFDESGDINPGQAGTKDSQLQLVIKLFRKMRNSLIKPHGPTLF | Function: ATPase component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.-
Subcellular Location: Nucleus
Sequence Length: 102
Domain: The DBINO region is involved in binding to DNA.
Sequence Mass (Da)... |
A0A2S9G067 | LDSEIPDKGRVLTAMSVFFFGHLTVPNHLAGPPDDERIPDEVLGRALVVKQLEMLPVEAVARGYLTGSGLIDYQQTGAVCGIAL | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(... |
A0A6B1ACG1 | MRLRERDRRFLRGKGRHRGRGRRWSGAGRRGPRSSGPRRPRDIDAVSVSAGHRAARRRARDEAAGARAPGAAGRGGHVSLWIGVMSGTSLDGIDVAVVETAGDDERPADWRVVAFETESYDRGARGRIAGAITEGSAASICALDFELGERIGAAVNRTLASASLRPADIEAIGSHGQTVWHEPPAGARGGSTLQLGQAAVIAERTSCTVVSDFRARDVAAGGEGAPLTAYTDWLLFRAPEARAIQNIGGIGNVTALPAESGGATPQAYDTGPGVVLIDGAVEFLTEGRSRFDLDGEMARRGVASEEALSDWLSDPFFRRS... | Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the... |
A0A158Q3U4 | MIWRDGIIPYEMDSVPKEIKLFEEVFEHYRRNTCIRFKKRKAENDFLYITKGTGCYSQVGKAGGKQELSLGRGCLFYEIITHELMHAIGFWHEHSRTDRDDYIRILWENILPGMEPQFDQISAAVQDLLGEKYDYRSIMHYDSTAFSKNGMNTVETIENGFTEIIGSALELSELDIKKINKLYKCENNNSNSNEGPATSSLESSSDPPGINFSNFNESANSNRFLFFPLLKFFSECFDHFSDCKQFQENCNRPAFFFVMKTYCQLTCGHC | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
EC: 3.4.24.-
Sequence Length: 270
Sequence Mass (Da): 31304
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H9V7G9 | KVRVLPNCNHGFHMECVDKWLASHTSCPMCRHSLNLGNRNGKPEGGSAPISQATESNNGIHVVIESTDSTQAIPPLAEVSERTLQEATGITNSSPLPPSTASENETSSHPMNNVG | 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: 115
Sequence Mass (Da): 12215
Location Topology: Single... |
A0A183L7L3 | MNHIVINFYSELITKLKCLCFDSNTYCFTFLTQVAETLVNPMGEDDEDIDINEIIDFNWRISWCVVDGVRTSAP | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 74
Sequence Mass (Da): 8569
Location Topology: Multi-pass membrane protein
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A0A8T2TT08 | MTSTRMTTTENSTLLHTFYHLMASQVASRVFSFSLNLLITRHLSQEDYGVFSIQFHLLITTVLFLSREGFRRACLRTDSRSKDSALREEKYFMAVTWLTVPTGFILSVVTCLVFLQQKGVNKSRESAHAVVILGLSCVIEILSEPPYILAQNMMLVQVRVKIEAFATFVRCLTTYFLVLNGLGKVGGVLFAYSQLLYAFCVLIGYWGYFLLFSKLKSDLEQKNISVLSHMSPKWGMWNHNKPLLYMCLMFTFQSFQKLILQEGEKFVLMIFDTAYNQGVYGFVDNLGSLVVRSVLQPFEESAFTIFAKYSSSNDVPRMRE... | Function: May be involved in N-linked oligosaccharide assembly.
Subcellular Location: Membrane
Sequence Length: 528
Sequence Mass (Da): 59647
Location Topology: Multi-pass membrane protein
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A0A183HB33 | MLNKIRDVNLPLHPGDWWTQNVVLALQLIFSDLIPDLIIIDHSASTIEYRNLTLIDTMHKLEMFNSCLPMLKWRFPKVKILFYCHFPQQLVIPTRFFLYRWYSRIVGLIEEKQFLRVMPEVNPSRLMVVYPPCNVDAIKTGDNPVSRKQCQYNNKRYTFLSMNRFWPEKKLDIIVKAAALLKRSRKMRPRIMLAGSVMPYIPESRIYYNLLKKMVQDLEVDDIVEFVPSPTDSEKFALYRECDTVLYTPQNEHFGIVPIEALEQRRPVIVCNSGGPAETVIEGITGSKVIFFSALYSYLKSQGLFFLFLVNRSLKDSRTL... | Pathway: Protein modification; protein glycosylation.
Function: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Catalytic Activity: alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP-al... |
A0A183JFC0 | MKTKRKHPSSSKYERGMAETQVCGSNLSNEAHREILTAMWDFEQCDPKRCSGRKLVRLGITKLLRLNESFGGIVLTPTATCVLSPDTDRQLMYSGGIAVVDCSWAQLEQTGFKKLKFHHGRLLPLLIASNPVKYGKPFQLSCVEALAASLYILGEHNQATELLNKFSWGHQFLTLNDQWLQSYAKCSTSKEILCFQERFLDEITRVDSSNTESYADIYAELDKQISAGSSSSEYCSSSEDFTEQATKTHSPTDDNSDQHDPPMIEGEKINKAIAKQIDTLASSFERTKLFKECGKNWDRFYKRNGVRFFKDRHWTTREFT... | Function: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine in 18S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi).
EC: 2.5.1.-
Catalytic Activity: an N(1)-methylpseudouridine in 16S/18S... |
A0A2K1J6Q5 | MGSGLLRGGFKLKGFGAEISAPGLRKNACVAQALQSPDAPESLSFFSAGCELSRVGCRFVIGTRLVRQGVSSVARSAWGGGFVGRTSLDDGGGGEVEEEEEEAEWTVQDSDALYRLHGWGAPYFAINVAGHLCVRPSGGTEGRDEVDMMAVIDSLTAQQLQLPVILRFPDILHHRMRELQGCFSSAIAKFGYQRHFEGVFPIKCNPECHLLDQFVEFGFGLEVGSKPELLIALSKLSSRDGALLICNGYKDSVYVENVVLATRLGIRAVIVLEQIEELEEVVACSQRLGIRPIIGVRAKLSTKHNGHWGETSGDKAKFGL... | Pathway: Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.
EC: 4.1.1.19
Catalytic Activity: H(+) + L-arginine = agmatine + CO2
Sequence Length: 415
Sequence Mass (Da): 44995
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A0A090LN80 | MIDKNKTLSPKIIIFSLSILCFIVSFNGEFAFDDHRAVVNNKVVVSPSNYGLNIKEILKNDFWGTPMESKFSHKSYRPLPTLIFRIGYLINGLDTKIYHFLNILIHGCNSILLYEVLKLWIPNIEEKIYFYTSIIFATHPIHCDAVASIVGITELLMTFFFLLGMRENLLYKNKITIKYILYVILSLFSKEQGIMLLPLSILQIFIYYKKITKKLCQLIFMTFFLIYMRLYINNFEEPKFSSLDNPISFTKSIFSKISTQLFIYLMNIKLLIWPWYLSIDYSMGTIPLIENPNDLRFLITFLIILCPIFLLNRISKIIIK... | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellul... |
A0A158Q5H8 | MMKTAVKSAVDGKEKTNGKVSKLRKKVLHTILQLMDVVDDSFLIEKLNLLDSNSWSDLIEERYILNLCGYPTCSNFVETQQRQLYHIDRVHRKIYERISEISMFCSNDCFKKAVSIKSQLPIDPLWIRGEETSNFYFIYLVVIYCKNFVLNGQMLMTTIEDKSDMIEYVEERIEKSLRNLHIGDIEASDDEDDANECDVSGNDCDDRFFSPHLPVCTSGISCNMEVLHARTPSVFESQVNNQERSMVDGGAEIEDHKSCEKEKLARIRSLYCNFKIKRPPIIIDAKPLDIHQIAQLSTELAEAEDGEKGQVYMKSNSIKF... | 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: 591
Sequence Mass (Da): 67553
|
Q8GS38 | MAARGASPGHVQELFVYEINERDRGSPVFLPFGGKKQPGTDAHVNSLGDLVPFSNKIYDGSLKTRLGITAGLCTLISHSDQKNGDRYEALYSFYFGDYGHISVQGPYITYEDSYLAITGGSGIFAGCYGQAKLHQIIFPFKLFYTFYLQGIKKLPEALCAPCVPPSPSVAPADEAKQCLPNHVAPNFTK | Catalytic Activity: (9Z,13S,15Z)-12,13-epoxyoctadeca-9,11,15-trienoate = (9S,13S,15Z)-12-oxophyto-10-15-dienoate
EC: 5.3.99.6
Subcellular Location: Plastid
Sequence Length: 189
Sequence Mass (Da): 20604
|
A0A1D1Z9P6 | MGSIFLLLLPFLLSLNGHSVNCERPRAVNIGAVLTFDSVIGAVAKVAIETAVDDINANPKILGGTRLNLVMENSNCNAFLGSIGALRLLEKDAVAIIGPQSSTVAHTISFVANGLQIPLVSFAATDPTLSSLQFPYFFRTTQSDFYQMAAMADVIDYYGWKEVITVFVDDDYGWNGVSTLGDALAKKLSKIVYKVALPVGASYSTISESLNRSKLIGPRVYVVHANPDSGLLIFSIAQHLQMMTDEYVWLATDSLSTSLDSTETPGNNLLNLQGVISFRQYIPDSGPRKAFVSRWNELRKKGRVSYRLNTYGFYAYDTVW... | Function: Glutamate-gated receptor that probably acts as non-selective cation channel.
Subcellular Location: Membrane
Sequence Length: 907
Sequence Mass (Da): 100426
Location Topology: Multi-pass membrane protein
|
A0A183HLY4 | MRRNCLEAFANRFFSLYPCIAEILVDVSKYEGESVVYAVGSRIIHISVQILSSESQCLKLDNEINLKDIMISSAYGVLKTGVEKSTITQAFAYFYDNTPPSTIDDDLFKWFIYSVGDANHPLRKASYWTLVSDLQNLLTHGTIARRILRNQKTMKNYIALIAPMQGMNLNYRIIAGNHLEYESTHSYQLAFHLEWEVSALNMFNTLAALTIERDCMNTYLLQWKTILEVS | Pathway: Protein modification; protein ubiquitination.
Function: Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
... |
A0A0H4QIA0 | QGRPTPVYHCERLSRAIGNCQIYLKREDLNHTGAHKLNHCMGEGLLAKFIGKKRLIAETGAGQHGVALATAAAFFGLECEIHMGEVDIAKQAPNVTRMKILGAKVVPVTHGLKTLKEAVDSAFDSYAKNYKDSIYCIGSALGPHPFPLMVRDFQAVVGYEAKDQFKEMTG | 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: 170
Sequence Mass (Da): 18557
|
A0A183HSU8 | MTLNKLSIDKVDVKDKRVLIRVDFNVPLKDGKITNNQRITAAVPTIKYALDHGAKAVILMSHLGRPDGMKKMEFTLEPVVAELKSVLGKDVTFVHDCVGPEAEKVTANPAPGSVILLENLRFYLEEEGKGVNEKGEKV | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
EC: 2.7.2.3
Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Length: 138
Sequence Mass (Da): 15195
|
A0A090MW17 | MKCILIILLYLNFTSTLKSNKASKVLKKSKNPMFTILSWNSRWWEDFGVCKKYNCLYTDNRKLLKNADAIMFNDFFYNCDTDMKNIVKRPKKSTLYVNVFSESFVRNKIRLGKLSLPYPKNYFNLTYTYLPNGDIYRSYGNDTFQIKNLTSHNIQILEEKLHKSFKNKKKDIIWLVSNCETPSGRMIAVNALKKYLNVVQYGSCNKKSIKLSDNEKKKLFEKHYFYIASENTDCKHYITEKFFERFFYDSIPIVSVRKLYDGYAPPNSFIAMDDFESPQKMGEFLNKLKNDKNEYLKYFEYRKLGWVQKQEKFDSRCYIC... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 362
Sequence Mass (Da): 43547
Location Topology: Single-pass type II membrane protein
|
A0A3N0AA93 | MRIVFMGTPRFAADILACLLEQLPEGCELSAVYTRPDAVRGRGKKLVPSPVKEVALGAGLPVFEPRTLRSDEAQAQLAELRPDAVLVAAYGMLLPQVVLDIPRFGCFNAHASLLPRWRGAAPVERALLAGDEQVGVCVMKMEAGLDTGDFAYCAAVDCESRSAEELLALMAPLAAEGFRALLRAVEAGDVPWQRQDEALVTYARKIEKGELDLSPALGPLDNVRRVRSASEAHPAKCSIDGVRAAIAQAAPVDEDGLPEEGLAPGAAVFFRKRLLLGARGGAFEVRRLKPEGKKEMDAAAFVAGRQNLRAAGATWETE | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
A0A090KUD5 | MIHGVDKFLKRIRESEITNGVDKMNYLYTVLWLLLISSIGISRNMVGEPMQCWIANQVTRWESYIENNCYLRGGYRYHNKSINNIEEIEKIPVNYYAWVQPFNIFQAICFALPFLAWNFISIQSDFNPKTIVKRATIIKKNMKFLEFVQGNTMVIAQETVENLFKGLKKKSFYLENKKNNFFSQFIHRSYLTNCYIFFKFSNILNIILQIYLLCSFYSIPNFYNAGINVMFGNSDNSGIKIGNSPYFPRIITCNVTLHDVAYSTPTIVNDCVIRVNLYNEAFFIITWIWYVTLFITTITDFQAWIVNSYVTKVRNSFIKS... | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 780
Sequence Mass (Da): 92511
Location Topology: Multi-pass membrane protein
|
A0A090L641 | MQSFNNLIVFIFLIFFSILFLFSFLSTNNSYYDSSVLSRLKKYDLLNQLDLLELEVAEEKAELEKLTMIVSKFEKELNSINYEKVQNSTVIPVVVLVCNRVEALKSLISKLLKIRPSIETFPIYVSQDCNSPDILEMIKNFYIKNITYIKHTSPLENNNVVIPQNMLRYKSYYYISRHYKLILQHIFDQLNYEAAILLEDDLDVSDDIFSYFNATYHKLLISDKSLYCISAWNDNGLPELIDLKDNVGLYRTDFFPGLGWLLTKNLWMELGNRWPDGFWDDWIRKPEQRKDRMCIRPEISRTSMTKFGAEGASKGYFFRN... | Cofactor: The cofactor is mostly bound to the substrate.
Pathway: Protein modification; protein glycosylation.
Function: Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.
EC: 2.4.1.101
Subcellular Location: Golgi apparatus membrane
Catalytic... |
A0A183KH17 | MSTVTLDTNIKLKNTGSLGLDSLWLEPVHLQYPKNIRFVINKSLETSGPLSHLLPLSSIPNLRQYISNINKVQYVKNEDLYGQLPTRDNFNSTRSSPKHVMIIQVHNRSIELSLLIESLRRTKGIETALIIFSHDFYSDELNNLIGSIRFTRTVQIFYPHSMQLFPNTFPGTDPRDCNSRIKPTEAMNIECLNARWPDTFQHYRESHFTQIKHHWLWKFIVVIRYDDNIWSYTEPN | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-Glc... |
C0LJJ3 | ENGTGTGWTVYPPLSSIIAHNGSSVDLTIFSLHLAGISSIMGAVNFITTVINMRSTGITFDRMPLFVWAVMLTAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQISYSPTLIWSLGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNPKWLKN | 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... |
A0A352CP77 | MAGFRTRAVSAVVLVAVLGSALYFGGYYLWALMLFASETGFFEFSRAMRDPSGRDDMKPDILELLGYCGIAVLYIVMLVWDSDVHIMYTLILLLIALMIVYVLQFPRYPTSKMMQIYFGVVYVGLMLSFVYLTRMEKQGLKLVWLIFISSWICDTAAYLTGMALGRHRLAPELSPKKSVEGAIGGVAGSALVGFLYGLLISPDAGALVYALISAIGAVISQFGDLTASAIKRNHDIKDYGKLIPGHGGIIDRFDSVIVTAPIIYILSRIFA | Pathway: Lipid metabolism.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 271
Sequence Mass (Da): 29754
Location Topology: Multi-pass membrane protein
|
A0A2K1IHE4 | MAVRRLLPSALRSRSFCSSSGGPAQLSGVQEIAKPASTHGEIGEVSGIPADQLKRKVVIYSPSRCTTQSGPATDKWKISFESVNKWENPLMGWTSTGDPYQSVGEASLNFDTKESAVDFAEKYGWQYTVREPHQAILKPKAYADNFKWKGPVPEYD | 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.
... |
A0A183HYF9 | MGSHEKNSSRSSRDKNELKRHRSPKREKIRRNRSRSPRDKRAKDRSRSPRKRDRSRSRDRSDRDGKKDKKKDKDLDLGEIVAMTDKNEAERKLEVEMQKRRERIEKWRLERKKGVVTTSEESTSKIEEQQQQEKKWTLDNEEEDEESTPQDIEKKELEDDDEIDPLDAFMSEVNKEVRASKYGLEQSNEGKVRIVVIKSDTNLEPKKGEIIEAEDEIEVYYRPFRKNFYVETAELAKITKKEIDEYREELDIRVRGRNCPKPVRSWAQCGVEWKILSTLKKLGYKKPTPIQSQAIPAIISGRDVIGIAKTGSGKTLAFLL... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 718
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 81937
|
A0A183L3X2 | MGIQFGLLARLTWWEYSWDIMEPVTYFVGYGTSMAMYAYYVITRQRYNELRDELAHLKSELRRLKDPLLYQLPLQQTEYMIPEQVENILNQTKNSPQK | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes a pore-forming and calcium-conducting subunit. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cel... |
A0A0N4UF08 | FQYGTRILFIVGLSQNEDINDQVKQEAIIHQDIHQINIIESYHSMTYKARSWITHLHSICPEKKISFVVKLDDDITIDLQSLIELLTDSSIRKNFVGCRLFMKGMITRNPFISREEFPFDNLGLYCQGLAYILSGDLISKMYYNIAKVQFLWVRIQL | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 157
Sequence Mass (Da): 18379
Location Topology: Single-pass type II membrane protein
|
A9TEG8 | MGPRRAPSRSCIAIALLCLSIFVGGGHAQSRPGRGLAASFNPWTKNVKYTNDGRGVQLVLDPLSASGAASKTSYLFGGFGAWIKLPPRNSAGTVTTFYMLSTGPKYCEFDFEFLGNETGQPFLLHTNIHVNGVGGREQQIYLGFDPSETFHYYNFQWNKDVLVLYVDNTPVRMFKNLEGIVPNFKYPNSQAMGIYMSIWDGSTWATQGGRIPINWSAAPFVATYQNFRLNGCAVHNVLDQNSLRLCQGSKYASPGAYAQTVGMARVRQMRWVRANRVVYNYCDDRKRYPIAPAECAHNTL | PTM: Contains at least one intrachain disulfide bond essential for its enzymatic activity.
Function: Catalyzes xyloglucan endohydrolysis (XEH) and/or endotransglycosylation (XET). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construc... |
A0A0N4U353 | MPYLQINNTNKMKYISCSVDGDKLLKCIADNNDIYFPFNKFLKRRFDLSGKYRKDDYFEWWTSYSKVRYPEFTHYDPKESFGHFASYNVETRDRVKCINGRYGLLLSIFLCSYILLYIFFYTLFIKGILRFALQHYSRNKTDDKRCVWLVNNKDSHALGKEPHESEWRFISRDLLVDINRAFLATNQRKMTILHSGDIRIMSITFRGRCVVREVRQSSSAHMEQFLTAADWFIKNQNERGGWHVPVDRWIAGKQLFLKAGWHSAMAQGHALSVLTRAYHVTKDMKYINAAAKALHLFKIVSVDGGVRNELFGHTWFEEYP... | Pathway: Glycan metabolism; heparin biosynthesis.
EC: 5.1.3.17
Catalytic Activity: [heparosan-N-sulfate](n) = [heparan-N-sulfate](n)
Sequence Length: 435
Sequence Mass (Da): 51094
|
A0A2K1J124 | MAVQSVGQLSHRIAMLAVAAQGVMNTKDLPTHVVLVDFANTMGDLAISLKELQKDLEIHFQAEPIQFQQHDIEAEMTVVEQLVMAHKAQSQLSSLLSCPFLLTKLQNFRGNLSRGLECILPDTCSELVKLQISRTQQQLKDGPPKLGLKEQAVIDLLGQITETSTPLKCKELVESVADYLDVVPGDSTFADLLENTKKDISKVDVCDSGTFSTYLENCIKVLEKGLNFQQEPAEGNNGALLNLLSPPSSHRTMREVVAPSSPLSSFICPITKQIMNDPVQIASGQTYERAAIEQWFKDGKTTCPLGKKLKNTKMMSNFAL... | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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: 1011
Sequence Mass (Da): 111996... |
A0A2K1IG48 | MEAVQVGSSPTAGFASDGFLARKSAHVAPKIGPCTAPCSAWRPQSSEPRGFAWRPVADNGIAKVVKFSRHVTTRVALMRGLGGMLKEGYVLRKHEILDEHTPVQSTGDVIEKLKNGFKNFKKNEYNQKPDLYAKLAEGQEPKVMMITCADSRVCPTMLHGLEAGEAFIVRNVANLVPPCEGSGEHHGTSAAIEFAVTVLQVERIVVMGHSNCGGIRALMTRDIYSGDFVGSWVRIGLPAKEKALSLMAGKSFDEQCGFCEQEAVNVSLVNLLTFPFIEERVKAGKLRIFGMHYDFVQGHLTSWEIEREDDFVHA | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 314
Sequence Mass (Da): 34463
|
A0A090N0T0 | MATQLALSSCVLFPLLLCWIGLLNEWIPLINQNLPQIIVKNLKYAPLYVIFIFTLYALTSLFIGVVTFSDCKEAKIELMNEVNQAKEELRKR | 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: 92
Sequence Mass (Da): 10575
Location Topology: Multi-pass membrane prot... |
A0A1B6DAA9 | MMNNSEVSAFAVYSKSKRKRRDNNKNKLEEKKATNVNDILKKEKLSGYKDLYKQSFDRKSNLNCLRGNNIITDKFGKNKKSNLLRKNSDKMNRQKNSNSSHKKTKNNLPSNSFGDFNTKIKFTTLVNKKNNQKLKLKNSRSSTTKAFFKSTITMDNITLAETGKKKLISNNCSKQDINDDPENFTSSESDDENDLNQSTSSSTNENGLLHDNSLNVATDLFSWMINPVPVDKFKRIYWESAPLLIRRKFCGGYYSSLLSTPEIDLILRNNNVLFGKHLDVTSYSNGQRETHNQIGRAQPHVVWDYYSNLCSIRLLNPQVF... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code.
EC: 1.14.11.27
Catalytic Activity: 2 2-o... |
A0A2K1KB31 | MPASESRAGHVKDVGTLTRLRMLGLILNFSVFYRATFKLLDVNGGFNEDCLSASVEDELGYKLSVKEEPEMSISRTFALKSAGGVKGYNFEVCPSRLKEYVPCIDNVAAIKELQSVSRGENWERHCPTLTERMCCLIAAPITYKVPIRWPKSRDEVWYSNVPHKQLVADKGGQYWIRLEKDRFIFPGCGTQFAHALKEINLHLIVGVYLMQMRPIIEYGRRTRVVLDIRCGVASFGASLFDRDVITLSIAPKDVHENQIQFALERGVPAMIAILATRRLPYPSQVFDLIHCSRCRINWTRDGNCLSSLCHEKHLHISALR... | EC: 2.1.1.-
Subcellular Location: Membrane
Sequence Length: 609
Sequence Mass (Da): 70131
Location Topology: Single-pass type II membrane protein
|
E6N3Z5 | MASAGQRPRLVIVGKKPVFRYVTASIVLFNRGSKEVELVARGKNIPLCVDTVELLRKSFHQDLRIKDISTWSEEFVVNGKTRRISYMKIVVERP | PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.
Function: Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DN... |
D4DSQ8 | MPTLLIVRPAAQAAADRQTCTAAGWQGSIFSPFAIEADADALARLPGQFQTASAVFWVSPSAVAVAAPHLEFSDRSPPQIAVGGSSARALQAYSRTPVCFPDDGNDSEAVLRLPLWQTLPQGVAVLIVRGHGGREFLAHQLTLRGFNVQTAEVYFRRPLEPDWTQFAAAPPDAAWITSAESVRLLFAAAPPPFTQKLQSLLYFTHHQRVAEALRAAGATRVELIPALDIDTLNRYAEQNR | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
A0A1D1YN45 | MGNNGSSSGGANGGRRRRNAGLNGSHGPVPAHPPSPHQQQQQLPLPPPPQPEITGNRYVFAAATPYPPQYPSPTNTPQYYQYPGYYPPPPAMPSPLPAPFDHHHRGGGSAAPPPPTPLPHAPHPTWVGGYMPPPPPPPPPPPPTLPFVEHQKAITIRNDVNLKKETLRVEPDDKNPGRFLIAFTFDATIAGSITVLFFAKEGFDCNLTSTKENLLKPVTVPFNEGLGQKFRQPSGTGIDFSMFEEAELLKEGEMEVYPLAVKAEASPSGEQGQACEDEKMGSLNSQITQAVFDKKENGEYHVRVVKQILWVNGTRYELQE... | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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: 404
Sequence Mass (Da): 44268
|
A0A183HI07 | MIRRLVSTRLEDIRDGFEEELQETKSKKQSFKNNERMTDSEEEDETFNEVPAKIPKGVYENKGAVLLAKMGYDGGGLGKSGQGRTEPIPFSTQRGREGLGQPTNQKIARDWNAVWDFTEEEKHVEESVLWLSASDNIREKFTKELQDQDNWIIIGDRKETIDDEGKYCDSKLMKKMLDAKSVFDQLNVRDLQEARTRANPYETIGSAFFQNRDRSFIDLSANIWLP | Function: S-adenosyl-L-methionine-dependent methyltransferase that mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of RNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA to produce m(7)GpppNmp (cap1).
Catalytic Activity: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucl... |
A0A090N039 | MLLNQLSGYYDITINTKYNLTLPTRYVIVQTIGSGAQGVVFSAFDLITLKYVVIKKLDKPFLNEFNAKRAFREVCLLSGIKHSMIIPMYSMFTPQQTPDSLKDIYFVMEKMDGTIDKCYDKLLDHTRISFLTYQILCALKHLHASGVIHRDLKPHNIGLNDDCTVKLLDFGLSRYIENQIYLTKNVVTLFYRAPEILLSLNYNEKIDVWSVGCIMAELITGKIFFKARDELSLWNNIIEKLGYPNDNFLNTLPSILKDYMKKNLKFKSIDFEKHFPESLFDNTSPDNQPIPTDLNSNNCRDVLKKMLTIDPNERISVDEA... | Function: Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating a number of transcription factors, and thus regulates transcriptional activity.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.24
Subcellular Location: Cytoplasm
... |
A0A7I4AFL9 | MATASVARNAYLTCYNSLQSLGWALVLLRLVNDIVETKSLRGGFSAAGNVVCFLQLAAFLEILHSALGLVPTGILFAFMQWLGRSHVLFAIVAKIPEVQEQPPIMITFLAWSAAEVIRYPHYTLGLLGLCPHWLTWLSASDVFIIGFHQGSEPLCKQLQVASL | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzy... |
A0A183HLA3 | MVAIFLKHFLDSYKNSGYHSLVVAHFHEWQSSVGLINAKLWNLDVALIYTTHATLLGRHLAAGGSDLYNNLDRFNLDEEAGKRKIYHQYCMERAACHMAHVFTTVSEITGVEAEHLIHQKPDILTPNGLNVIKFAALHEFQVYD | Pathway: Glycan biosynthesis; glycogen biosynthesis.
Function: Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.
EC: 2.4.1.11
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + H(+) + UDP
Sequence Length: 144
Sequence Mass (Da... |
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