ids
stringlengths 6
10
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stringlengths 16
1.02k
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stringlengths 117
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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 factor 2.
Subcellular Location: Cytoplasm
Sequence Length: 191
Sequence Mass (Da): 20975
|
A0A6P7FLF3 | MTDPTQPQTIKIQHYGTVPAKQPKEKRVFLQSLRKPKPATQTPNKLLDYGAHPRRGRRSSMNFPREIIRGVYQLTQTINGYTIDSSIFRLNTNATVILLITFSLAVTTRQYVGHAIDCLHARDIPEEVLNTYCWIHSTFTVVQEASRRHQQNDQLSLSGIETTGKRAIKQIKYYQWVEFFLFVQAILFYTPRWLWKSWEGGKIHALMMDLDVAVCTEIEKKQKKKLMIDYLWENLRYHNWWAYKYYFCEILALINVIGQMFLMNRFFDGAFLMFGFEVLSFINSDQEDRIDPMIQVFPRMTKCTFQKYGVSGEQEKHDALCILPLNVVNEKIYIFLWFWFIILTILTFLTVIYRIIIIFSPRMRVYLLRMRYRLVRGDVIDTIVRRSKMGDWFLFYMLGENVDSLIFRDVLQELAHKLNRHDFHHGPGFKGEIQEA | 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
|
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 | MQKIAILGSTGSIGTNALDVVSRFPGKFKVSYLSANSNIKLLAQQIKRFKPKAVCVGSGNVNGARVYRGEQGLRRIVKDMPVDVLVVGIVGSSALLPILAALPNIKRLALANKEALVMAGDIIMKKAKRNKVGILPVDSEHSAIFQCMAKDNAQEIKNIYLTGSGGPLLRTPMKNFKNITPHQAINHPRWKMGKKISVDSATMMNKGLEVIEAHHLFGLGVDRIKVVIHPETVVHSMVEFVDGSTLAQMATCDMRTPIQYALTYPSRVASPVKGVKFSELGALNFSQPDFKRFPCLEIAYDAAKKGKTYPCVLNASNEMAVTEFLKGHIRFTDIARVIEKVQGLHKAVKNATLNEILEIDKWARCKTEEILGAYNN | 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: 1.1.1.267
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Length: 376
Sequence Mass (Da): 41220
|
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-dehydroshikimate (DHSA) to yield shikimate (SA).
EC: 1.1.1.25
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Length: 276
Sequence Mass (Da): 30202
|
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 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives.
EC: 2.5.1.15
Catalytic Activity: (7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate = 7,8-dihydropteroate + diphosphate
Sequence Length: 272
Sequence Mass (Da): 29667
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A0A6B1AM23 | MADERAGRTKAYDYALPAELIAARPAERRDDSRLLVLDRARGRFTDAAFPALLERLSAGDALVVNDSRVFPARLLGRKPTGARAEILLLRPESDALRPFAPFDEADTRLWRAMVRPGGKLKPGRTVDIADGFAVEILESAADGTRLVRLAGDGDPWSLIQRHGRVPLPPYIVRDDAGSEREGRDDAEDRERYQTVYSAPSGSVAAPTAGLHLTRKMLATIESRGVRLVSLTLHVGFGTFRPVTATRIDEHEVAPEAYRFSASAAEALNATRAGGGRVFAVGTTSCRVLETVVAGGGTSAGGGSSTGGPFAPGRGWTNLFIRPPYTFRGVDALVTNFHLPRSSLLMLVAAFAGRELTLEAYAHAIRERYRFYSYGDAMLIA | 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 + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
EC: 2.4.99.17
Subcellular Location: Cytoplasm
Sequence Length: 380
Sequence Mass (Da): 41095
|
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 Location: Golgi apparatus membrane
Sequence Length: 294
Sequence Mass (Da): 34656
Location Topology: Single-pass type II membrane protein
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A0A834R2B6 | MMKLNLIILALKSRFFILLLAFFTDYLIEDHQPDAYQNEPLTEHFIRSLNKNNTENLTRLDRILIPLLKPLARWDAQYYLSIAIEGSYPTEQHLAFFPLYPFVIRSISSLLSRWIVPSYLSQITLISLIGYLLNLVCFVISLLSLYNLSVYLFQDYKFCDEVAKLFAYNPASIFFTALYTESLFLCLTLLGLEMLYNRNLPFLASILFGLSALTRSNGLVSLGYLIFYHCIQIYLEFDRSKISKVKFFAQNAMKIFTSISMMVAPYLMYQIYLYHLYCSVQNQIKVEWCHYRIPISYGYVQKKYWNLGFFSYYQWKQIPNFFLAAPTLMVVIYPALKFLKKNFRLIKILIANKSRRSQAILLGRFLRPILKKNFFENSFLLPFVLHSLFLSMICLTTMHVQVSTRFLFSSNPWPLWAMVHLRRSTNKMLNKSITLWPIIYLIVGTSMFANFFPFT | 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 membrane protein
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B7P6Q6 | FPRALQEGKLRDSVSMGASDTPLEEKTLTVVYGPDLVNVSVINFCCNSRETAQLWTDELLRMAYNLLSLNAPASRFLEKAHTKLLLTTDREGRLPVKGVLRMFAQHRDDRRRVERALDAVGLAAGKNDTLAPDRLCFDVFLRFYRQLVGRQEVDAIFERLCGGAKKKAMTVDQLVDFLNKEQRDPRLNEILYPYANPARAKDIIAQYEPNKSYVAKGLFSVEGFLRYLMSADNPIVSPEKFDLSLDMDQPLNHYFINSSHNTYLTGHQLTGAHHHARLHRGDGGAPPRSGSRPLPRALKTSDFPVVLSFENHCSPKQQAKMANYCRKLFGDMLVTEPMLSHPLRPGQPLPSPQQLLRKIIIKNKKKHHARPHKPLASPSVAAAAAAAAAVAPGGGGEDDASPGEGPDDLNGDAKGSEADDWDTDSGTEEEEAPERSAEDQNEGTAAKESEAVAEMSALVNYIQPVRFHSFEHAEKRDRSYEISSFVETQATNLLKEHPVEFVNYNKRQLSRIYPSGTRVSSSNYMPQVFWNAGCQLIALNFQTLDLGMQLNLGIFEFNGRSGYLLKPDFMRRADRKFDPFTESTVDGIIAGTVSIRIISGQFLTDKHVGTYVEVDMYGLPADTVRRRFRTRTVPANGINPVYDEEPFIFKKVVLPDLAVLRISVCDDSGKLLGHRILPVVGLRPGYRHISLRNESGQPLLLQTLFVHVTVKDYVPDGLSELADALANPIKYQSRIEKHATQLRALTDDLDEVPF | 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 | MDKIGQTISFPGLGIGDFTVNRVAFTLFGQPIYWYGIIIACAFLLAIGYILKRARTFGVDPDRALDVVIGGVIGGVVGARLYYVAFTWENYAANPLDIFNIREGGLAIYGGIIGGLIVVIIMCRLRRVKLLPFIDLAAGGVILGQAIGRWGNFFNVEAFGSNTTAPWGMAGPSIAAYLEAHKDILAAQGVAVDPLLPVHPTFFYESVWCLAGFVLIALYTKRRRFDGELTLIYAAWYGFGRALIEGLRTDSLMWGNIRVSQALAAALTIAAAAVLVYVRADMKRQSGEKARRLYVDTEEGQSVVNGTFYKKPGAPAETDDAAGKELSADSIKEKTDAEQTTEGEDAEDESKAD | 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: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+) + S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[prolipoprotein] + sn-glycerol 1-phosphate
EC: 2.5.1.145
Subcellular Location: Cell membrane
Sequence Length: 353
Sequence Mass (Da): 38214
Location Topology: Multi-pass membrane protein
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K7U5D4 | MVPQIPDPCDDDGQDHRCPPAAALPPPWPYPPLPPPASHGRSTFVTALIIATSVLVFLALCLSILVFVRRRRLRRRREALLEAALAPAAAATFPDEGEGDGGPGGEVVHHVWHIRTVGLDNAAIESIALTRYCAGGVLGASDCTVCLGEFQDGELLRLLPKCAHAFHVECIDTWLRAHVSCPLCRADVMDPGAAAADADAEQPPGTDAADASAERSASNTPTTELERLDQQANEHHQELRVQIDQPDHSSSLELERRRRQVRHHGARAQNFRRVASMDSRSPPPVSAEVDPEGEPAGREEQGTCGAVCCEVSPEPAELKRSWSASSRWTLL | 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: 331
Sequence Mass (Da): 35780
Location Topology: Single-pass membrane protein
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A0A0U5JMH1 | MLETANWIQKYFNQSPDAIFLFKNDDLLVSNEPAQRLVTMLNLDVNYLLQIGKNAWSQLENDDCASCLIKKRLTGATVPITFHSNATHPFHFSMVYRPLDDKESVFALTLENREQQQRLSQIEEHRILNQYVNEAHEKERQKISQDLHDSVAQGIYAAIMGIQRLATVQKQRNTEQFQAMSAAIEKQLQMTLKEIKGLALDIRPSVLDNFGLIPAIKALAKRLQNSTGITIDVIALTSAEKLQKNIQNVLYRITQEAINNAIKHAHSTEISIIVTDHNSYLQLEILDNGIGFDIDQHSGFNGHSLGLMNMNERVKAYNGAFTITSKINKGTTVKVKFPYNNALNKDMVRTNV | 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 histidine residue, and transfers its phosphate group probably to a conserved aspartate residue of NreC. NreB/NreC activates the expression of the nitrate (narGHJI) and nitrite (nir) reductase operons, as well as the putative nitrate transporter gene narT.
EC: 2.7.13.3
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Subcellular Location: Cytoplasm
Sequence Length: 352
Sequence Mass (Da): 39879
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B2AKY3 | MRLQTSAGLLPLISLTTALTETPFLGFPSPWISPDPSDAEWQAAYEKAAAFVSQLTLTEKVNLTTGTGWEGDRCIGKTGSVPRLGFEGFCLMDGPLGVRYVDKASAFPAGMNAAATFSKRLIRARGEAMGEEFRGKGVDVQLGPVAGALGRTPQGGRNWEGFSPDPYLTGVAIAETIRGIQSRGVIACAKHYILNEQEHFRGSVDVRIGDKTMHELYLWPFADAVRAGVGSVMCSYNRVNGTYACENEWVQNYLLKSELGFRGFVMSDWGAQHSTLGSALSGLDMAMPGDMMGPPSASSPPYGSHWGGALTQAVLKGEVPQWRLDDMVTRIMTSFFRVHVGSYTSRPEPNFSAWTRNTTGPQYKYSNRPWTTVNSHVDVQANHSALIRELAAKSTVILKNTGILPLSKSSLTSLAVIGNDAHDNPNGPNSCPERACINGTVAMGYGSGTTDFPYLISPATALLGLSQEHNITFFNTTSNWDLTTAQSTASNASVAIVFATATSGENFVSIDGNAGDRNNLTLWDNGDALIRAVAAVNPNTIVVLHTSGPVVIDHADKHPNISAILWAGFPGQESGNGLADVLFGDVHPQGRSPFTWGKDLESYGVELLTVAPDPRSPRQEFPEGVFIDYRWFLSEGKGERGRVTYGFGHGLGYTEFEYGDLVVERVGGRGGYEVNKGKTIPAPVMGEVVDIGDVEGWTEPDGFEGWRIPRYVYPWVNATVYNSENGTARSPGIGDFPPEARDGGVQEELPAGGKEGGNEGLYEVLFEVKVDVKNAGTREGVEVVQLVSCLVCFFCCDPVRLMMNSTSHPTTLSPPLSSSAALTTSSSPPTPPKPSPSPSPVVTLASGTPKPRTGRFSPSISRPSLSGRARWI | 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 | MRGQTETGRWRGGDGVAAWWVAVVALQLGHSLSRARAGLLESNPGLAYNFYQSSCPSAESIVRSVTWAQVAADPALPARLLRLHFHDCFVKGCDASILLDNAQSEKTAAPNLSVGGYEAIDAIKAQVEKACPGVVSCADIVALAARDAVSYQFGASLWQVETGRRDGGAPSLASDALGALPSPFAGFGGLLAGFASRGLNLTDLVALSGAHTIGVASCSSVTPRLYQGNATSVDPLLDSAYARALMSSCPNPSPASATVGLDGGSPARFDSGFYARVRQGQGTLASDAALAQNAAAAQLMADLSTPASFYAAFSMSMKKMGRVDVLTGTNGQIRKQCRQINTS | 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 + H2O2 = 2 a phenolic radical donor + 2 H2O
Subcellular Location: Secreted
Sequence Length: 343
Sequence Mass (Da): 35451
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A0A1D6F699 | MKGRLLFKSPLPRSYLSHTSSVTSAAVATHRVYQVWRGKNRFLCGGRLIFGPDASSIVLTVALIMTPLALFVAFVSFRLAEVIGKPLGAAVPVTAVAVGVFDVVVLVLTSGRDPGIIPRNARPPEPDSFATTTTEMSSGSPATGASWSLPPTRDVYVNGVAVKVKYCHTCMLYRPPRCSHCSVCNNCVERFDHHCPWVGQCIGRRNYRFFFLFIASTTFLCLYVFGFCWVDLLLTSRRRGGVGIGRAVAESPVSGCLIAYTFVTAWFVGGLTAFHSYLVCTNQTTYENFRYRYERKANPFNRGAGSNVAEIFCSPVPPSRNDFRARVSPADPDAAALYYLGPLASESRISFYTRASGLSFDMAKASFDRNYSAASVASSSDFGDIYGAGGGLDRVSSHQQPRHSIFGVGGGGHAREGKKQAEDEADAVTAELGATMHMHYGRGAGRTRGREFGMV | 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 | MNAWIYISHVEKLVENKNKHLSDLNFFLEEEKKDDNNELTSNGEDSQSNDNIENESDVDIVDDSNDSDGSDDSNYSDDDDNLSNNENDKKSDVTKKMDKAKKQDNAQQSDEEKQSDEKKQSDEEKQLEKAKQLAKAKRLDKKKINEIRKTLSSNCRIIKVENEQIYIASWNSIKKNTPINSYIIDKLINKFLYTKFLPCQSTTLEYTLLYKNGSNSILNGDMYIEAPTGLGKTLCYVIPILDYYLSQNDNTFFCVILTPTEELVKQVTKVITMFDIKNLIISTIKPKTYNTNMCFDEINNENDFYKSHVNTNEQRFEQKNILITTTTKFEMLFYSNQNIFKKLKYLIIDEVDSILNMDFVNINIVVNALTKLVQQTENNIKYSSTSNNSYSNATDSNLLYKPKHFLQKILLSATICKVSNKLLSLNLYRPIFFYYILNYARNYEFYLHVLKKSDKLCNLIHLIQKTSPNGDKNILIFCNTEETVHFLFRFLTVYFSHVEKNCYKIKQYSHNLMQKLKKHTLNSFIFGENNILIATDKLSRGVDTKNVNCVINYEIPTYYNTLTYRVGRMTRANNVNGKVYHFIKPTEFSLIKRSAAQRNISEIKKLVYENLSIRKIRSSLSHINELVNIALEQEQKNIMHWNKFYSYNDLMLMNKIK | 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 | MSRKLRRTKIVCTMGPATDRGNNLEKVIAAGANMVRMNFSHGVPEDHIERANKVREIAARLGKTVAILGDLQGPKIRVSTFKDGKIFLNIGDKFTLDADLPRGEGHQDAVGLDYKNLPNDVVPGDILLLDDGNVQLKVLSVEGVKVHTEVTVGGPLSNNKGINKLGGGLSAPALTEKDKEDIKLAAKIGVDYLAVSFPQSSADLDYARQLAREAGLEAKIVAKVERAETVATEEAMDDIILGSDVVMVARGDLGVEIGDAALVGVQKRLIRRARKLNRVVITATQMMESMIKKPMPTRAEVMDVANAVLDGTDAVMLSGETANGDYPVETVKSMAEVCLGAETMPSINISRHRMEGTFATIDEAVAMSAMYTANHLEGVSALIALTHSGETAKLMSRISSGLPIYALSRNQQALNRTALYRGVTPVFYDEESRTFEGAKKAIALLKEKGYLMSGDLVLLTQGDELKEGGTNTSRLLKVE | 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 construction of growing tissues.
EC: 2.4.1.207
Subcellular Location: Secreted
Sequence Length: 286
Sequence Mass (Da): 31976
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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 triphosphate
Sequence Length: 188
Sequence Mass (Da): 21711
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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 | MINLFEHYDKQTQTLYDTLRIAGYDNDTIVLEDDGFLPEHFITPYRFFAQYKVPKNATARYFNQVGIPRYWEIMGNNQSATVRDVNKQRATIHYHRPSKPRIVSHVEWLDEAERLLYVDHYTQHGVLFAQTFYDLAGKRIFRKYLDQQGAEVIYENFVAQSIILNWKGKAHHFNNKVQFIQFFLRALDKARNGFVINTLGLPFSVLYHLDEPGNDLIFWQEQCHGHVPGNMSLVLQGGLVRDYHVIVPDSQEYEILKQQVDDNMQQRLIPAGYLYDYASKNGYTSNVVTMTNSDQIHHVEAIVEACPTATFHIGAVTEMSDKLMALERYPNVKLFPAIEIATVNKLYQLCDIYLDINEGGEIINALQKAFDHDMLILGYRDIAHNLSVTATENLFDKGDNAEDLIQALKDVQRKKRYFKVRQNYQKAHVHEVGVKDFKQVIDKVLK | 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 upstream in the same operon. The GtfA-GtfB complex adds GlcNAc from UDP-GlcNAc to the substrate protein, attaching the first sugar residue. Stabilizes the glycosylation activity of GtfA. Has no N-acetylglucosaminyl transferase activity on its own.
Subcellular Location: Cell membrane
Sequence Length: 446
Sequence Mass (Da): 51788
Location Topology: Peripheral membrane protein
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A0A1D6EQP7 | MAGRARHPPFRLMFYLIGLLASLIPATSRAQPPETVTVGLIIDADSPVGRIASTTIPMALDDFYAALPNSSTRVQILQHDSGGDVVAAASAALQLMTTQGARAILGPQSSVESAFVADLATRAEVPVVSFSATSPSVSHSEARFFVRAALSDAAQAEAIAALATYFGWRRVVPIYQDDDYGAAFVPFLVDALTAVRAEVPYRCALPSGASRDAVAAAMYRLESEQTRAFVVHARPALAELVFAAAVEAGMMAEGYAWVITDGLTGLLGSIHPPQGVIGLAPHVPSTARLRDVRKRWAHKFMRQHRDADLAQAEMGCYALWAYDAAWAVASAAERLVSPGDQPSLQGLVGGRSGPTDFSGLGKSMSGAKFLAAITSTTFEGLGGRFELINGELAVPAFRIVNIMDDARERGIGFWTRKGGLHRQLGRRGIASNSGLLPVIWPADSTVVPIGWVQPTSGRKLQVAVLGRVDPGYWPIMHLDVDPATNRTVAGGFVIEVFEAAVRLLPYALPFEYVLVGSMRYDTLVERVGKGEFDAAVADITITANRSQHVDFTLPYMSSGISMVVPMRDQRSKRAAWVFLKPLRYDLWLISFAFFVFTGFVVWAIEHRSNEEFRGPPSYQIGTLLYFGFSTLVFAHRENLKSNLSRFVVVVWVFVVLILQSSYTASLTSMLTVPQLEPAIGDFASLWPGTDKVGIMNNSFMREAMTKTGFPQYRLRPYQATQSFHEALLNGTIGAIVDETLYLRLFLNSYCDNFTQIAQSNKTGGFGFAFPKGSPYVGDLSRAILNLTESDELSSIERKWFGDADGCAAQGSPFTSASLSFDSFWGLFLITGATSLFCCALHLLLFVVANRRRICAARVPWRIRLRVVLKLLDDKDLSSHTFRTIKDGGGSVAGRSAGAHDAGASPAVARIAAGSPLSVSNHTYDMSEWSFGAQSPAPAAAGEIELAGAGEAGEVASAPPTLAAARGSSDQSGTVVHQASN | 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 | MAARRGGMASGAGAAAAHIASSMVLSLLLVGVGVSRAQLQVGFYSDYCPDAEDTVTAAVQDAAGNDPTILPALLRLQFHDCFVKGCDASVLIRSASNDAEVDNGKNQGLRGQNVVDAAKAQLEDQCPGVVSCADIIALAARDAVAMTGGPSFDVPTGRRDGLTSNIRDADVLPDAGDSISVLRSRFAASGLDDRDLVLLTAAHTVGTTACFFVKDRLYSYPLPSGGRGPDPSIPASFLAELEDRCPPGNFNTRLALDRGSESDFDDSILRNIRSGLAVIASDAALANSNATRALVDAYLGPWAGSFEQDFAAAMVKMGTIGAITGDDAGEVRDVCSAFNSN | 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 + H2O2 = 2 a phenolic radical donor + 2 H2O
Subcellular Location: Secreted
Sequence Length: 341
Sequence Mass (Da): 35278
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A0A2K1J8C2 | MSRMGSRSVYRAVSCFARQIGKQKGTADDGFAVSRRTMMMPRWFVAPRNSANSMVSNGVESQQPTMVASGVYQTHSSVTRILPLQVGGTPNVVKIREEYPSQSASAELTKERGLEGESESWSRLSDQGRLATRVDAPENEPGSSPSSNSVTGERQAHSTHEARKNSVDTRETAKFAAIASTWWDPKGPYKPLHIMNPTRVSYVRSQICKHFGKDANTPRPLEGLKILDVGCGGGLVCEPLARMGGEVTGVDAVDKNIGVASVHAARDPATASIKYVCTTAEHLVQEQQKFDVVLALEVIEHVADPEDFCKSLAALAKKDGLVFISTLNRSIPSFGLAIIGAEYILGWLPKGTHEWSKFVTPEELSTIMNRASITVKDTSGMVYNPLTERWSISASNTSVNYIACGVSRNV | 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(+) + S-adenosyl-L-homocysteine
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 410
Sequence Mass (Da): 44534
Location Topology: Peripheral membrane protein
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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-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
EC: 6.3.5.-
Subcellular Location: Mitochondrion
Sequence Length: 139
Sequence Mass (Da): 15535
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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: [eIF5A protein]-deoxyhypusine + AH2 + O2 = [eIF5A protein]-hypusine + A + H2O
Sequence Length: 296
Sequence Mass (Da): 33260
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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 motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 287
Sequence Mass (Da): 31900
Location Topology: Multi-pass membrane protein
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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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 157
Sequence Mass (Da): 17062
Location Topology: Multi-pass membrane protein
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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 external vitamin B12.
EC: 4.3.1.7
Subcellular Location: Bacterial microcompartment
Catalytic Activity: ethanolamine = acetaldehyde + NH4(+)
Sequence Length: 284
Sequence Mass (Da): 30623
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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 | MNIIIILLFFFINIFSYISSKGVLEVKLISFISKSISPIEINVCIKEYQTIVEDTGDCRFGTKSIILPKGYYIPEANSNISHVLIFPFDMTWPKSHSLIVKGKLLNNDEVKVNDSVVIIYKQSFLHSGNLFLDVGKAENTNASIHFFSSIKCDVNYYGTDCSKICYSNVFENEHVECDQNGKPICKEGWSGIKCDQPICKFGCGLNGKCVAPDTCDCLSGYTGKSCEECLPSVGCQNGYCKNKGNECICNEGWAGEFCEIDIEPCHKKNKCKNNGVCLNGKDGSVRCECKGRFYGKYCQHEKISCSSFPCQNGGTCVMTSDGSEFKPVCDCLPSFFGKYCQSTKDTNDYVEDIIVETNEIIDKKGVINEIELEEVKIKKNITSYIQWNFINIIVVLSLLIVIAFLIATRKKKITRNPTFSIVGKYHTEELNPSRLEKASKYPLSSNYINYTMENVYSYEPFSSILEKSRNFENVISEPQIENGIKHFKCEKNNEYDDLYSEVYSTISDRMGSKTQL | 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 | MTIHVSSSKDQSKNSELLVCLKQFRNEWFRYCCAAVFTIKFLLIPCYHSTDFEVHRNWMAITHALPICSWYYDDTSQWTLDYPPFFAFFEYFLSQVASKIIPSALILQKGAYFSTELLYFQRFSVIATDIFYILSCVFLTKSFFGRCKNDSSIEKNSLAAEIFLITNASLVMIDNIHFQYNGILTSILLISLGWIMRNSFLRGPNIKLNSAVIFTGPFIYSCGLDILKQIWRRLFPFERGLTHAYWAPNLWAFYNFADWYFYQVLKLTKRLPSNVQSPTYISGLVQEFKHSILPPVSPFGTLLMTLALLLPILSLIRTRHVKNFPLLLTLSAFAFFLAGFHVHEKAIILITVPYTVLASSDHRFLPSFIMLSVVANVSLFPLFFTPFENMLKISITLCYMFLSISIMLFLCPERSLHFLKKLYLYGLLIVQVYCLVLHQVGDFLFICRTIR | 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: 1.2.4.4
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+) = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + CO2
Sequence Length: 114
Sequence Mass (Da): 12676
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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 | MSMEKSPPPHNGNYPSYYAPPRKHEKSHWPIFTLVAVVANIIVFIVVMYENNCPAKIGPGRTCVLGSSFKRMSFQPWSENPLLGPSSATLVKMGGLRTVLVVDQKEGWRLMSCVWLHAGVFHLLVNMIAVLVLGLPLEKTFGFIRVGVLYLASGLGGSLLSSLFNQNGVSVGASGALFGLLGGTISDVIINWSLYSNYCGVLLNLIILAAINLAIGLLPLVDNFAHIGGFLTGLLLGCVLLMKTQHGYVPRRDLLDPNMERPVKNRFNAFQIILFIISALVLIAGFIGGFVALYNRVDAHKKCSWCHYLNCVPSSHWTCDS | 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
Subcellular Location: Mitochondrion
Sequence Length: 289
Sequence Mass (Da): 32516
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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 membrane protein
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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 = [(1->4)-alpha-D-glucosyl](n-1) + alpha-D-glucose 1-phosphate
Sequence Length: 71
Sequence Mass (Da): 8064
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A0A183I5E0 | MLFLRMKSKANPKSYYAWFYRLWCFKQLTNPDIAAELAACEKFLNLDGRNFHCWDYRREIAEFGAHSAEEELKFSDRLIDANFSNYSSWHYRASLLPSLFPDPEKQMIVNQQTLYNEYQKLQNAFFTDPEDQSAWIYAEWLLLSDQKKKKCELVSMSSEMMNRKAFRAKNSYRFEIAGELAECQLRPSLSEPYEIIDMERGYVNFEEIYQIYHIRCKPVSEARRHIIEKVMDNCQELLKELEVEQKKEILKWPLLTYTFAILELEPIEMLSTILTNLEELATKVDPQRCQMYEEMAMNLRISQKLREKLGDVHRIDILFRQVSGHVVGELKLDNLGLK | 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: 338
Sequence Mass (Da): 40170
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A0A183KD84 | MYYNSKFILRHVDSNCQLIPPSSSNSDTNTIQLTDPSSSAITITNPTSRIESSPNEQGIDHVDKNRRIGEIVLGLDIAPGEEPLPEGWELARTASGRKFFINHNEHTTTWDDPRVIRPNNQITNGSLLTHEAQRHVMKDLGPLPPGWEERVHSNGRIFYINHNARTTQWEDPRLERLGGPAVPYSRNYKQKYDYFRSRLRAPRDPQAKFELRVTRAGIFEDSFRLIYGIKRPEVLMHRLWIEFIGEKGLDYGGVQREWFFLLSREMFNPYYGLFEYSAASLDQRLEQSSVYPRLRTNNAVTTTTTTTTTTTTTTTTTTTTTTTTT | 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.
Subcellular Location: Membrane
Sequence Length: 123
Sequence Mass (Da): 14703
Location Topology: Peripheral membrane protein
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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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 93
Sequence Mass (Da): 10217
Location Topology: Multi-pass membrane protein
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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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 193
Sequence Mass (Da): 20603
Location Topology: Multi-pass membrane protein
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A0A653H3Y2 | MVKKRESACDTSLIKKEEKKKRSSTDSGSKRHNDESFNLVYTYILLHYFFENSKMKIINEPFYLQDNVLTITEKLIGQLFWVYDDTTNELYGSRLIELESYNGISDKGSHAYNNKKTKRNMPMFEKGGISYVYLCYGVHYCMNIVTNVVNIPDAILIRAVEPIYNVPFFFLNKFLKYYKQKNNYINTNLLNQKKQQHQKVENVINNLLKKKKIKINYDMDKVNDVIDKVNDVICKEKNDKKNDEKKDENKYSKQIEELTDISKIINKKKLAKIGSGPGCVTKCLGITIQDNNKSFFFENKFMEVDSNENSSDNLLNINSNKITNLEKCKYNNDKKYTHNKVHILNSEYYFSCNNITNLKKNRFFITTCPTVNDILNFYENLIIKKSKHLSFITTIYNKYKTHLLEYFDFMLWGDNQINIKKSPRIGLANAGEAALYEYRFMIMDHPSVSVLPK | 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 Length: 453
Sequence Mass (Da): 53204
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A9SY86 | MAAAAGSAGVVCWSRAEKQHAPVRGGGTSVTSSTSGSGHASLKGSFDRLQGNRLLPQALTMPSLFRAKRNGRRTPGNAVTNFGKSEFHREISGSTRATTQVAEATTAGLRETIEDRAIIDGHSHSFEGIQSEEELMQVIEKEVESGRLPKRAGAGMVELYRNYRDAVVSSGVENAMDIVVKVMSTVLDRILLQFEEPFTFGSHHKRMVEPYDYYTFGQNYVRPLLDFRNSYLGNLKIFDQIEKNLKEGHNVIFLSNHQTEADPAVMALLLEHSHPYLAENLTYVAGDRVVLDPFCKPFSMGRNLLCVYSKKHIHDVPDLAEMKIKANAKTLRQMTILLRQGGQLLWVAPSGGRDRPDPETNEWVPAHFDSSAVENMKRLSDIVRVPAHLHALSLLCFEIMPPPVQVQKELGERRAVGFSGVGLAVSEQLDYDSIAKLVDDSKNAKDAFSDAAWSEVNDMYNVLKEAIYGDQGCAVSTDSLRLEQPWFDGSRRTD | Pathway: Lipid metabolism.
EC: 2.3.1.15
Subcellular Location: Plastid
Sequence Length: 494
Sequence Mass (Da): 54767
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A9S9A5 | MDAPENDLCRAGQSPPGHPLLKSWNPPTQHSFTKAQLRTLISICDAFSPSLSPPAECEEKQEIASFYTCSASDMGVPEDIAGLLHVLLKPQLLMAIRVFLWLLSTRIGTLILGGRASLTTQFPFFQSFAYLSTDKQEDILRGWSLSTLGAFRAVYKLFKMITMWAVYTKIENGGFNRNWKAIGYCGADPQVIRSRKCSSNDGVRSNPLQDMVIATQAAGDKLEKVLSRAGVKVLNDDIPLKKLASGNRNRNNSAAGGDLGISCDVVVVGSGCGGGVIASVLAKAGYQVVILEKGKYFRTEDLTTLEGPSQMAMFEKLGSLATDDGGVNLVAGATVGGGTAINWSACFETPSHVLQEWKQISGLELFTSTRYKLAMKKIWHRLNVQPNIARENLQNSVLRAGCEKLSAEVGTLARNAPVDHDCGWCTYGCPSGQKGSTTSTWLKDAAESKNAVLLSECEAQRILFSKNHSGRKHYKARGVMAVVGSSKKRIFIEAQSVVVASGSLMTPPLLLNSGLRNPNIGKGLHLHPVVFMWGYFPEESGFPGTCYEGAIMTSYSPIYKKNGSFPVALLEVPSTHPGSFASFQPWTSAADFKERMRRFSRTVTLCAVTRDTSNGQVSVEADGKPKIDYTLNAVDEETILEGIEKGLRVLIAAGATEIGTHQQDGERFCVKGANSRDIEAYIKRVRSRGVKKNKIIIGSGHHMGSCKMGSDPRRSAVDGEGETWEVEGLYVSDGSVLPSAIGVNPMVTIQSVAYCIAHSVLQSLDSQYKSSTAKL | 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 membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 82
Domain: The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space.
Sequence Mass (Da): 8981
Location Topology: Peripheral membrane protein
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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-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP
EC: 2.4.1.155
Subcellular Location: Golgi apparatus membrane
Sequence Length: 209
Sequence Mass (Da): 24084
Location Topology: Single-pass type II membrane protein
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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.
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: 312
Sequence Mass (Da): 34980
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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): 11586
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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-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Length: 84
Sequence Mass (Da): 8990
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A0A6B1ACG1 | MRLRERDRRFLRGKGRHRGRGRRWSGAGRRGPRSSGPRRPRDIDAVSVSAGHRAARRRARDEAAGARAPGAAGRGGHVSLWIGVMSGTSLDGIDVAVVETAGDDERPADWRVVAFETESYDRGARGRIAGAITEGSAASICALDFELGERIGAAVNRTLASASLRPADIEAIGSHGQTVWHEPPAGARGGSTLQLGQAAVIAERTSCTVVSDFRARDVAAGGEGAPLTAYTDWLLFRAPEARAIQNIGGIGNVTALPAESGGATPQAYDTGPGVVLIDGAVEFLTEGRSRFDLDGEMARRGVASEEALSDWLSDPFFRRSPPRSTGRERFSRDRLLEWLRRHAALSPEDTIATLTELTARTVADAYRWIEEPPAACYLCGGGARNPVLAARLEQLLSPVPVRDLSALGLGADAREAVAFALLARQHELGYPANAPWATGARGPRLLGVRTAA | 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 medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
EC: 2.7.1.170
Catalytic Activity: 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate
Sequence Length: 452
Sequence Mass (Da): 48067
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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-pass membrane protein
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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 | MTSTRMTTTENSTLLHTFYHLMASQVASRVFSFSLNLLITRHLSQEDYGVFSIQFHLLITTVLFLSREGFRRACLRTDSRSKDSALREEKYFMAVTWLTVPTGFILSVVTCLVFLQQKGVNKSRESAHAVVILGLSCVIEILSEPPYILAQNMMLVQVRVKIEAFATFVRCLTTYFLVLNGLGKVGGVLFAYSQLLYAFCVLIGYWGYFLLFSKLKSDLEQKNISVLSHMSPKWGMWNHNKPLLYMCLMFTFQSFQKLILQEGEKFVLMIFDTAYNQGVYGFVDNLGSLVVRSVLQPFEESAFTIFAKYSSSNDVPRMREVLAAALKLVSIIGLVFATFGPSYSYVLLRILYGTKWSDGEASTALAFYCVYVMTMALNGTTEAFLHAVVTKGQLARSNVWLMAFSLVYVSMSIMLIHKGGAVGLIAANCINMLLRSIYSMNFILKYFRGSFNVWQGLPNARVLAVLVASLLVTHTSEKMILDIHRFPWTVALHIGLGAGCFTLFVYSLYKYEKPFFLELAAFHRAKAD | 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 | MLNKIRDVNLPLHPGDWWTQNVVLALQLIFSDLIPDLIIIDHSASTIEYRNLTLIDTMHKLEMFNSCLPMLKWRFPKVKILFYCHFPQQLVIPTRFFLYRWYSRIVGLIEEKQFLRVMPEVNPSRLMVVYPPCNVDAIKTGDNPVSRKQCQYNNKRYTFLSMNRFWPEKKLDIIVKAAALLKRSRKMRPRIMLAGSVMPYIPESRIYYNLLKKMVQDLEVDDIVEFVPSPTDSEKFALYRECDTVLYTPQNEHFGIVPIEALEQRRPVIVCNSGGPAETVIEGITGSKVIFFSALYSYLKSQGLFFLFLVNRSLKDSRTLII | 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-alpha-D-mannose = alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP + H(+)
EC: 2.4.1.132
Subcellular Location: Membrane
Sequence Length: 322
Sequence Mass (Da): 37652
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A0A183JFC0 | MKTKRKHPSSSKYERGMAETQVCGSNLSNEAHREILTAMWDFEQCDPKRCSGRKLVRLGITKLLRLNESFGGIVLTPTATCVLSPDTDRQLMYSGGIAVVDCSWAQLEQTGFKKLKFHHGRLLPLLIASNPVKYGKPFQLSCVEALAASLYILGEHNQATELLNKFSWGHQFLTLNDQWLQSYAKCSTSKEILCFQERFLDEITRVDSSNTESYADIYAELDKQISAGSSSSEYCSSSEDFTEQATKTHSPTDDNSDQHDPPMIEGEKINKAIAKQIDTLASSFERTKLFKECGKNWDRFYKRNGVRFFKDRHWTTREFTELSSLHNRIPRSLLEVGCGVGNFLVPLIESMLSISKAGINISEESCRVSKTNG | 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 rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyl-N(3)[(3S)-3-amino-3-carboxypropyl]pseudouridine in 16S/18S rRNA + S-methyl-5'-thioadenosine
Sequence Length: 373
Sequence Mass (Da): 42085
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A0A2K1J6Q5 | MGSGLLRGGFKLKGFGAEISAPGLRKNACVAQALQSPDAPESLSFFSAGCELSRVGCRFVIGTRLVRQGVSSVARSAWGGGFVGRTSLDDGGGGEVEEEEEEAEWTVQDSDALYRLHGWGAPYFAINVAGHLCVRPSGGTEGRDEVDMMAVIDSLTAQQLQLPVILRFPDILHHRMRELQGCFSSAIAKFGYQRHFEGVFPIKCNPECHLLDQFVEFGFGLEVGSKPELLIALSKLSSRDGALLICNGYKDSVYVENVVLATRLGIRAVIVLEQIEELEEVVACSQRLGIRPIIGVRAKLSTKHNGHWGETSGDKAKFGLTVTQIVSVVYRLRQEGMLDCLKLLHFHIGSQISSILVIKEAMREASHTYCELARMGAPMGYIDVGGGLGIDYDGSKGHSSASVNYNMQVGAELRK | 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 | MIDKNKTLSPKIIIFSLSILCFIVSFNGEFAFDDHRAVVNNKVVVSPSNYGLNIKEILKNDFWGTPMESKFSHKSYRPLPTLIFRIGYLINGLDTKIYHFLNILIHGCNSILLYEVLKLWIPNIEEKIYFYTSIIFATHPIHCDAVASIVGITELLMTFFFLLGMRENLLYKNKITIKYILYVILSLFSKEQGIMLLPLSILQIFIYYKKITKKLCQLIFMTFFLIYMRLYINNFEEPKFSSLDNPISFTKSIFSKISTQLFIYLMNIKLLIWPWYLSIDYSMGTIPLIENPNDLRFLITFLIILCPIFLLNRISKIIIKKEERYILFNSISLYILTFLPSSNIFFTVGFVIAERTLYLPSIGFCLLFTYYINKYENNIKKYINTKIFLKILILILLIKSVQRSYQWLNEEDLYKSSLQTCPRNAKLYYNLGKIYTKKNKTNEAIKKYEMAIKLWPGYCHAMNNLANLYETIGKYVIAEKLLKKCTIIDSTFPVPWMNLGILQMKMGKYNESEYNLLKSTYLRPNSPDGFFNLGNLYLNMKLYQEAKKAYINATNIDKKHLQSWVNLLILEEEHFNCHNIDNISKIILQQNNNKGILHHQMAKCFFKINNYIKAKYHFEKAVELERYNDMYRKNLKIFYKYINMEKIHL | 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
Subcellular Location: Endoplasmic reticulum
Sequence Length: 649
Sequence Mass (Da): 76830
Location Topology: Multi-pass membrane protein
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A0A158Q5H8 | MMKTAVKSAVDGKEKTNGKVSKLRKKVLHTILQLMDVVDDSFLIEKLNLLDSNSWSDLIEERYILNLCGYPTCSNFVETQQRQLYHIDRVHRKIYERISEISMFCSNDCFKKAVSIKSQLPIDPLWIRGEETSNFYFIYLVVIYCKNFVLNGQMLMTTIEDKSDMIEYVEERIEKSLRNLHIGDIEASDDEDDANECDVSGNDCDDRFFSPHLPVCTSGISCNMEVLHARTPSVFESQVNNQERSMVDGGAEIEDHKSCEKEKLARIRSLYCNFKIKRPPIIIDAKPLDIHQIAQLSTELAEAEDGEKGQVYMKSNSIKFAGIAREWCGPRTLEFLRIGGEIEPVKRNDELSDVEKALMRFYGGDQLNLIEEELEVFLPSVDKYNHTIKRQEVLLALLKSSFRLLENAIGCEGISQLTRPLISTLNLTAKNVSVEKNEAKFAVAFLFRLSAECNGGLLCQYFPDSKNFCPQFITFLQSFNCDVSFFLEIVNEILHKVNDDFGGLWWLGANIVRNLCKEIWFNLIDGSRGPRSCIFDPCICGNCISIYIYMGLHCGTVRYLSEEGYNHVRFYPLEGSVKCILQMSGQRLMVS | 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
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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
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A0A1D1Z9P6 | MGSIFLLLLPFLLSLNGHSVNCERPRAVNIGAVLTFDSVIGAVAKVAIETAVDDINANPKILGGTRLNLVMENSNCNAFLGSIGALRLLEKDAVAIIGPQSSTVAHTISFVANGLQIPLVSFAATDPTLSSLQFPYFFRTTQSDFYQMAAMADVIDYYGWKEVITVFVDDDYGWNGVSTLGDALAKKLSKIVYKVALPVGASYSTISESLNRSKLIGPRVYVVHANPDSGLLIFSIAQHLQMMTDEYVWLATDSLSTSLDSTETPGNNLLNLQGVISFRQYIPDSGPRKAFVSRWNELRKKGRVSYRLNTYGFYAYDTVWAVAHAINKLLNDSDNITFSPNNNLQDVKGKLQLGKLKTFDNGQLLLQKLLLSNFTGISGPIQFDIDRNLIRGVYEVINIGHSVIHSIGYWSTHSGLSVSVPSVLNTNVPRNFSENQSLHGSIWPGGRSLKPRGYVLASRERPLKIGVPYRASYVEFVTETGETHEVKGYSIDVFKAALALVPYDIPYQFVPFGDGHSNPSYDQLVYNVANNVFDAAVGDIAIVTNRTRLVDFTQPYIATGLVIIAPIGNKKSSTWVFLRPFTGRMWCVTGAFFVMIGFVIWVLEHRVNKDFRGPPKRQCVTMLLFSFSTLFNSQQEDTVSTLGRMVMMVWLFLLMVITSSYTASLTSFLTVQQLSSPIKGIDSLIATNQPIGYQIGSFARSYLIDSLNIRQSRLVSLGSPEAYEAALQLGPKNGGVAAIVDELPYVELFLAKTSGFGIVGKMFTKSGWGFAFPRDYPLAVDLSTAILRLSENGQLQRIHDKWLCKESCIKHGDSDSGPNQLHITSFWGLFLVCGLVTITALIIFLLKTIQQFVRFKRKHRDPSSTNQYSSERGSGVINNFFKFIDEKEEAIKNMFRQHESSSDPQVS | 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
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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.
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: 230
Sequence Mass (Da): 26387
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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
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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
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A0A090MW17 | MKCILIILLYLNFTSTLKSNKASKVLKKSKNPMFTILSWNSRWWEDFGVCKKYNCLYTDNRKLLKNADAIMFNDFFYNCDTDMKNIVKRPKKSTLYVNVFSESFVRNKIRLGKLSLPYPKNYFNLTYTYLPNGDIYRSYGNDTFQIKNLTSHNIQILEEKLHKSFKNKKKDIIWLVSNCETPSGRMIAVNALKKYLNVVQYGSCNKKSIKLSDNEKKKLFEKHYFYIASENTDCKHYITEKFFERFFYDSIPIVSVRKLYDGYAPPNSFIAMDDFESPQKMGEFLNKLKNDKNEYLKYFEYRKLGWVQKQEKFDSRCYICKELIKFYKSKKQRIYPDIKRWQKESNECLPNNYIPRKWKLTR | 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
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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 Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Length: 318
Sequence Mass (Da): 34037
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A0A090KUD5 | MIHGVDKFLKRIRESEITNGVDKMNYLYTVLWLLLISSIGISRNMVGEPMQCWIANQVTRWESYIENNCYLRGGYRYHNKSINNIEEIEKIPVNYYAWVQPFNIFQAICFALPFLAWNFISIQSDFNPKTIVKRATIIKKNMKFLEFVQGNTMVIAQETVENLFKGLKKKSFYLENKKNNFFSQFIHRSYLTNCYIFFKFSNILNIILQIYLLCSFYSIPNFYNAGINVMFGNSDNSGIKIGNSPYFPRIITCNVTLHDVAYSTPTIVNDCVIRVNLYNEAFFIITWIWYVTLFITTITDFQAWIVNSYVTKVRNSFIKSHLMCRNVTLNDKEINKFIDSTFFTDGVTILRWIAAKSGSNFTSDIIHVAFQKYISDKKSDITLLDDNDPKHHKDELKLISGAMNGRKVQNRKYHSMVDNFLTIGNITFFIILATVIGSFTSSFKGVYCHTPLEILRGGWERYTSAQCFLNGKYGNPIEKKKFSMYYYIWTTYLIILPIVFFTIPRFYWSYVSKDYENGIKNLLMSSKNSANEFQKTIKEYFKKREAFEERKKIVQMNIEDIDNEKYLAFSRFRSNLEKNSIAQKYLYYKLMLFIASLILFWYVKHVFQIKSNYEAINYISKKLNDTKYDDPQLFPTKVWCEVIVNDIKYSRKQLSRFYCSMPYNYIYQIIFCILFIYTPFIIIISGCSFLSWLYALYNKPYRTNYFKNLLILINNEYIKDNYFYSFISHFSKTDYVFFELISEKISYAETALAIENVFHNYKKQYKITNNEINKENQSLI | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 780
Sequence Mass (Da): 92511
Location Topology: Multi-pass membrane protein
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A0A090L641 | MQSFNNLIVFIFLIFFSILFLFSFLSTNNSYYDSSVLSRLKKYDLLNQLDLLELEVAEEKAELEKLTMIVSKFEKELNSINYEKVQNSTVIPVVVLVCNRVEALKSLISKLLKIRPSIETFPIYVSQDCNSPDILEMIKNFYIKNITYIKHTSPLENNNVVIPQNMLRYKSYYYISRHYKLILQHIFDQLNYEAAILLEDDLDVSDDIFSYFNATYHKLLISDKSLYCISAWNDNGLPELIDLKDNVGLYRTDFFPGLGWLLTKNLWMELGNRWPDGFWDDWIRKPEQRKDRMCIRPEISRTSMTKFGAEGASKGYFFRNFLSRIKLNDISVDFSNLDLSYLTEKNYEKYYMNIVYNKSKLISFNNLKTYLNQSNIIKKKNIFRVEYSTFNEYEEIAKFLEMMRDFKEGVERTAYKGIVTVFKNETRIFVAPKQNEWKGYDRKWEFIP | 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 Activity: N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2) + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP
Sequence Length: 448
Sequence Mass (Da): 53274
Location Topology: Single-pass type II membrane protein
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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-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
EC: 2.4.1.143
Subcellular Location: Golgi apparatus membrane
Sequence Length: 236
Sequence Mass (Da): 27660
Location Topology: Single-pass type II membrane protein
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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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 294
Sequence Mass (Da): 32203
Location Topology: Multi-pass membrane protein
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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
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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.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 156
Sequence Mass (Da): 17214
Location Topology: Peripheral membrane protein
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A0A183HYF9 | MGSHEKNSSRSSRDKNELKRHRSPKREKIRRNRSRSPRDKRAKDRSRSPRKRDRSRSRDRSDRDGKKDKKKDKDLDLGEIVAMTDKNEAERKLEVEMQKRRERIEKWRLERKKGVVTTSEESTSKIEEQQQQEKKWTLDNEEEDEESTPQDIEKKELEDDDEIDPLDAFMSEVNKEVRASKYGLEQSNEGKVRIVVIKSDTNLEPKKGEIIEAEDEIEVYYRPFRKNFYVETAELAKITKKEIDEYREELDIRVRGRNCPKPVRSWAQCGVEWKILSTLKKLGYKKPTPIQSQAIPAIISGRDVIGIAKTGSGKTLAFLLPMFRHILDQPELEEMDGPIAIIMSPTRELAMQTWKEANKFAKQLDIRVACVYGGVGISDQIGDLKRGAEVVVCTVGRLTDMLAANKGKVTNLRRVTYLVLDEADRMFDMGFEPQVMKIVNNIRPDRQTVLFSATFPRQMEALARKILDKPIEIMVGGKSVVCDDVNQSVVILEEHQKMLKLLELLGVYWENGNVLVFVDKQEKADDLVAQLMRSGYNCAPLHGGIDQFDRDSTILDYKAGKIKLLVATSVAARGLDIKKLILVVNYDCPNHYEDYVHRARAMAAKIAEAKQLGVTAPVEKDAASLTAEAVMRGSDAVPIALSVQEYADVGISVKGSYYPGNKEPKDGERKLFLFLEARSELALRRAREEILRIMKDTVRQMAQTGARNASTTGRYKVF | 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
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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 cell death pathways.
Subcellular Location: Membrane
Sequence Length: 98
Domain: Forms a well-packed pentamer with an overall cylindrical shape. The inner core of the pentamer is formed with the second transmembrane region and the second coiled-coil region: while the transmembrane regions pack into a five-helix bundle having a largely polar pore across the membrane, the coiled-coil outside the membrane forms a pentamer with a hydrophobic core. The inner core is wrapped by the first transmembrane region through contacts between the first and the second transmembrane regions. The second transmembrane is followed by the inner juxtamembrane region (IJMH) that orients at a wide angle relative to the second transmembrane. The two core domains are held together on the periphery by the outer juxtamembrane helix (OJMH).
Sequence Mass (Da): 11829
Location Topology: Multi-pass membrane protein
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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
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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 construction of growing tissues.
EC: 2.4.1.207
Subcellular Location: Secreted
Sequence Length: 300
Sequence Mass (Da): 33398
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A0A0N4U353 | MPYLQINNTNKMKYISCSVDGDKLLKCIADNNDIYFPFNKFLKRRFDLSGKYRKDDYFEWWTSYSKVRYPEFTHYDPKESFGHFASYNVETRDRVKCINGRYGLLLSIFLCSYILLYIFFYTLFIKGILRFALQHYSRNKTDDKRCVWLVNNKDSHALGKEPHESEWRFISRDLLVDINRAFLATNQRKMTILHSGDIRIMSITFRGRCVVREVRQSSSAHMEQFLTAADWFIKNQNERGGWHVPVDRWIAGKQLFLKAGWHSAMAQGHALSVLTRAYHVTKDMKYINAAAKALHLFKIVSVDGGVRNELFGHTWFEEYPTVPGTFVLNGFLYALIGLYDFSKLSNMYSNDTNELLNEGLKSLRALLPLYDTGSGSIYDLRHISLQSAPNLARWDYHSVHIYLLKWLYNIYNEDYLNKFAVRWTNYAMGNRAPHN | 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
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A0A2K1J124 | MAVQSVGQLSHRIAMLAVAAQGVMNTKDLPTHVVLVDFANTMGDLAISLKELQKDLEIHFQAEPIQFQQHDIEAEMTVVEQLVMAHKAQSQLSSLLSCPFLLTKLQNFRGNLSRGLECILPDTCSELVKLQISRTQQQLKDGPPKLGLKEQAVIDLLGQITETSTPLKCKELVESVADYLDVVPGDSTFADLLENTKKDISKVDVCDSGTFSTYLENCIKVLEKGLNFQQEPAEGNNGALLNLLSPPSSHRTMREVVAPSSPLSSFICPITKQIMNDPVQIASGQTYERAAIEQWFKDGKTTCPLGKKLKNTKMMSNFALKQSIAEWRERNYNIRLDNAEFRLRSFQPMEQMRGARDIKLLCEEDGINKYGIASRKMIPLLIQLIETTDSPTNLRELCFDALTALALDHQENQETLVFEGLIDLLVRSLRNYNEAEPAINLLKVLSGNPKAAEMISRTPNAVLLLVTFLGHKNENLVISTKGILVNLPTTDENVVIMAEANLMKPLVVRLVEGERESKILMARTLARLEHMPDSSRSLASSRDAIKTLINMANSEDEEEVDAAILALKNLSTAPTAGVVIADCIGLEVLIRLLSSKKISVVTKVGASHIIANVLVAIGNQWVRSEDMVADLDNFVETFFLLISSVSTPLAAQSHLLQGLLGLVEGKHTGQVVKDIMIRRNALSGLLSHFRKKELEARRDSLKLFASLSRKHGAEAWSAVRIHSGTLQLLVGVLKTEDISEPEKLAAARIISHFPAEDHSLTRTLQTLNIVPVFVNFLSSPNQSMQEASLVALVRFTFPEFPDLQKQLAEMGVIPVLVTLLDSRRPRVKISAAHALANFSKSTPRLVKPIASKKWWQCFTPPQESCKLHAGVCTIETTYCLIVAEAIHPLLSIVREDDGKITEVALEALYTLLDNEHWERGCHTINEANGISIILQNMPKCTARAQEISINMCEKFFRIPAYQASFGPPSQMHIITIAQQASPSTRDVAGRILRQLDLLQTQSHYWISSTSK | 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
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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
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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 protein
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A0A1B6DAA9 | MMNNSEVSAFAVYSKSKRKRRDNNKNKLEEKKATNVNDILKKEKLSGYKDLYKQSFDRKSNLNCLRGNNIITDKFGKNKKSNLLRKNSDKMNRQKNSNSSHKKTKNNLPSNSFGDFNTKIKFTTLVNKKNNQKLKLKNSRSSTTKAFFKSTITMDNITLAETGKKKLISNNCSKQDINDDPENFTSSESDDENDLNQSTSSSTNENGLLHDNSLNVATDLFSWMINPVPVDKFKRIYWESAPLLIRRKFCGGYYSSLLSTPEIDLILRNNNVLFGKHLDVTSYSNGQRETHNQIGRAQPHVVWDYYSNLCSIRLLNPQVFVKKIQTLTSTLQEFFGCFVGSNVYLTPPGSQGFAPHYDDIEAFVLQIEGKKHWKIYKPRSNSYILPRYSSPNFSQEEIGEPMLDVVLQAGDMLYFPRGYIHQASTVEGEHSLHITLSAYQHTAWVDLLEKLLPMALKRATMNSKHFRKGLPLGYLNSFGYGINPSSKPVLRKEMIEKAKRMVSSLASYLDDLDAAVDQMGVQFIHDALPPVLTPDESKCSVFGDGLHMMANGILTEPKMLSATVKVKFLRSNICRLVEEEGEIRLYYNVENPLEYHAEEPQYLLLSEDTVPLIKFLIEKYPNFVTVNEIPYPTDNDVKYQAVCDLWDRGILITDRPLEEMDEEI | 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-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2 succinate
Subcellular Location: Nucleus
Sequence Length: 664
Sequence Mass (Da): 75926
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A0A2K1KB31 | MPASESRAGHVKDVGTLTRLRMLGLILNFSVFYRATFKLLDVNGGFNEDCLSASVEDELGYKLSVKEEPEMSISRTFALKSAGGVKGYNFEVCPSRLKEYVPCIDNVAAIKELQSVSRGENWERHCPTLTERMCCLIAAPITYKVPIRWPKSRDEVWYSNVPHKQLVADKGGQYWIRLEKDRFIFPGCGTQFAHALKEINLHLIVGVYLMQMRPIIEYGRRTRVVLDIRCGVASFGASLFDRDVITLSIAPKDVHENQIQFALERGVPAMIAILATRRLPYPSQVFDLIHCSRCRINWTRDGNCLSSLCHEKHLHISALRNHLQLHQPVRTMLDDVVNLARSRRRSPKLVEMLYSDGILLIGVNRLLQAGAYFIWSAPPVYKNEEKQKNIWKGIESLTSRLCWKQVGKEGQVAVWRKPLNDSCYIDRPIDTGKPSATKRMIQTIIHSISMNARLARHQVLKGDRRYWYVIMKGYLRSLGLRKEEFRNVMDMRALYGGCEPFDTYPRAYDLLTTRLNNYFGEITQQVLDSNKSVTNVIDASRCNIAHIVLEMDRILRPGGWVLVRESNAIVRRVQRLAKSVRWRTQILDTENWKYCKDKLLSCQKLLWHN | EC: 2.1.1.-
Subcellular Location: Membrane
Sequence Length: 609
Sequence Mass (Da): 70131
Location Topology: Single-pass type II membrane protein
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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 DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.
Subcellular Location: Cytoplasm
Sequence Length: 94
Sequence Mass (Da): 10773
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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 + uroporphyrinogen III
Sequence Length: 240
Sequence Mass (Da): 25995
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A0A1D1YN45 | MGNNGSSSGGANGGRRRRNAGLNGSHGPVPAHPPSPHQQQQQLPLPPPPQPEITGNRYVFAAATPYPPQYPSPTNTPQYYQYPGYYPPPPAMPSPLPAPFDHHHRGGGSAAPPPPTPLPHAPHPTWVGGYMPPPPPPPPPPPPTLPFVEHQKAITIRNDVNLKKETLRVEPDDKNPGRFLIAFTFDATIAGSITVLFFAKEGFDCNLTSTKENLLKPVTVPFNEGLGQKFRQPSGTGIDFSMFEEAELLKEGEMEVYPLAVKAEASPSGEQGQACEDEKMGSLNSQITQAVFDKKENGEYHVRVVKQILWVNGTRYELQEIYGIGNSVDGEFDGNDPGKECVICLSEPRDTTVLPCRHMCMCSECAKVLGFQTNRCPICRQPIERLLEIKVNKSDEQQQEETPC | 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
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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)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.57
Subcellular Location: Nucleus
Sequence Length: 226
Sequence Mass (Da): 26078
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A0A090N039 | MLLNQLSGYYDITINTKYNLTLPTRYVIVQTIGSGAQGVVFSAFDLITLKYVVIKKLDKPFLNEFNAKRAFREVCLLSGIKHSMIIPMYSMFTPQQTPDSLKDIYFVMEKMDGTIDKCYDKLLDHTRISFLTYQILCALKHLHASGVIHRDLKPHNIGLNDDCTVKLLDFGLSRYIENQIYLTKNVVTLFYRAPEILLSLNYNEKIDVWSVGCIMAELITGKIFFKARDELSLWNNIIEKLGYPNDNFLNTLPSILKDYMKKNLKFKSIDFEKHFPESLFDNTSPDNQPIPTDLNSNNCRDVLKKMLTIDPNERISVDEALNHPYLRIWIEERELSSGQPEVYNPNIENTIFSIKKWKQLIFYKIKNYENTNNIFLKLHN | Function: Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating a number of transcription factors, and thus regulates transcriptional activity.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.24
Subcellular Location: Cytoplasm
Sequence Length: 380
Sequence Mass (Da): 44312
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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 enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Catalytic Activity: a very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain (2E)-enoyl-CoA + H2O
EC: 4.2.1.134
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 163
Sequence Mass (Da): 17885
Location Topology: Multi-pass membrane protein
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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): 16378
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