ids
stringlengths 6
10
| seqs
stringlengths 16
1.02k
| texts
stringlengths 117
4.4k
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A0A6C2YKD5 | MTLHEQIPLGATRHGDGTVTFLVWAPLATQVRLHLHPDRWEPMTALADGYFHTILTDLPADSRYTYELDGRDWPDPVSRSQPDGVHAPSAIIEPHFDWTDAAWTGRHLADCIVYEMHIGTFTPEGTFDAAIGRLDRLVDLGVNALEIMPVSQFPGSRNWGYDGVYHFAVQHSYGGAAALKRFVDACHARGLAVFLDVVYNHFGPEGNYLSQFAPYFTTKYDTPWGQAVDYEGPHAHGVRRFVLENARQWQVEFHLDGLRLDATDAIFDASDKYILQELVEQCRQREATTGRPFSLIAEMSSNRPKVVRPIEQGGYGLHAQWNFDFHHCLQAILTGDRHGYYVDFDHAAQLARCYRDAYYFTGQLSQYRGHFGEMPVGARGDQFIVYSQSHDEVGNRAKGDRLAAQVEFEALRFAAAAVLLSPFVPMLFMGEEYAEPSPFYYFVSHGDADLIEAVRAGRRREFAEFAADEDFPDPQSELIFERSRLQWLKAGHGRNLIMWAFYRELIALRKRNAVLRTPDRDRCEVIGGEPGRAIRLRRWQGDADQPHEELLIGLNASRDPVQLEWPAGTWTQILDADERLWRGRGPLQPATVTGGTTTTMHPWGVVVYARQLPETT | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Catalytic Activity: hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-[(1->4)-alpha-D-glucanosyl]n trehalose to yield trehalose and (1->4)-alpha-D-glucan.
EC: 3.2.1.141
Subcellular Location: Cytoplasm
Sequence Length: 616
Sequence Mass (Da): 69880
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A0A655AJT1 | MRGKHADCAKVGITSIRRDLPADISTATLNETIDELNANPDCTGYIVQLPLPKHLDENAALERVDPAKDADGLHPTNLGRLVLGTPAPLPCTPRGIVHLLRRYDISIAGAHVVVIGRGVTVGRPLGLLLTRRSENATVTLCHTGTRDLPALTRQADIVVAAVGVAHLLTADMVRPGAAVIDVGVSRTDDGLVGDVHPDVWELAGHVSPNPGGVGPLTRAFLLTNVVELAERR | Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Length: 232
Sequence Mass (Da): 24500
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B7Q3E3 | MPTIGSFFAGRNVLVTGSTGFLGKVLLEKLLRSCPDVGSIYLIVRTKRGLRAEDRIADILKMQLFQRLRQERPEAFQKIVVLEGDLTLPDLGLKPKDRQLLVATVNVVVHSAATVKFDEPIKNAVRMNLGGTRRIVELCNEMEDLKVLVHVSTCYCNCDRGEIKEEIYAPVHDPDHIIKIIDWLDTETLEACQTKLLGSMPNTYTFTKGLAETLVQRESKGYPVAIVRPSIVVCSWKEPFPGWVDNFNGPTGLIIAVATGLLKSVYTDPDMETDFVPVDVVVNCILAAAWNVATTRPSDVQVYQCASSGRSPRLRWRDMKAIQESLMGELRFTSAIRYPDVQLRRNLTAHRAAMFFQHYVPACLGDALLACLGKKQW | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 377
Sequence Mass (Da): 42193
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B7P3G5 | MWSLRRRRAIRQLTISVVVVAFLSGGVYLCAHGGIEFRGTKDFTSTPSRALQSLPPKVFPKQRIYAHPFDYIINSPHLCLGNDTRPHRVDYLFVVFSAAENSGHRVAIRETWGQDLREYPATRVMFFLGATNDSRLRSTLRSESSVHSDIIQGSFIDAYSNVTLKSIMMLQWASTFCRCARFVVKVDDDTYLNAANFFATIAPRPPDAIYGRLFEGSIPIRDPADKYHVSLEDYPASSYPNYVAGSSYVLGGHIVETLYRATGQVKPFPIEDVYITGSCAESAGIRRVGLSGFHSQRVGSPCGLKNAVTSHYTPPRKMYTLKDQLRRLEFVCYRVLFDFAYYCYCRTLLPT | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 351
Sequence Mass (Da): 39658
Location Topology: Single-pass type II membrane protein
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A0A0Q9WFA8 | MASFLARAGGTLIESVKPKTVTKILNYTPIGLQQLRNLNVQEHVSYTLLNESSIPTPRFAVAKNGKEAHDIAQKLKTDNLVLKAQVLAGGRGKGTFKNGLKGGVRVVFSPESAEEYATKMIDQLLVTKQTGAAGRICKKVMVAERKFPRREFYFSVMMERAFNGPVLIASKEGGVDIEEVAKENPEAIIYEPIDIGKGLTKEQACKIVDKVGLGGSSADEHIQMLLNLYKLFVKKDALLVEINPYAEDAMTGCFFALDAKLRFDDNAEFRQKELFSMRDWTQEDPKEVEAAKYNLNYIALDGTIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGATAEAVKAAFKIITSDKKVMCLLVNIFGGIMRCDVIAEGIIAAAKDLNLNLPIVVRLQGTKVKEARELIRSSGLKILARDDLDKAADLAVHLAQIVSLAREMNMDVNFEIPDAQKDKCKKDQKKEEKKDQCKDKKK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Function: ATP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
EC: 6.2.1.5
Subcellular Location: Mitochondrion
Catalytic Activity: ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Sequence Length: 473
Sequence Mass (Da): 51986
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A0A379YM82 | MENLEGLLKQAPDLIVTYGLKVLFAIIIFFVGKYFAGVAQKLVRKLLNSRKVDPTVVSFVANLAWAIVFVFAVIATLGQIGVQTASLVAVIGAAGLAVGLALQGSLSNFASGVLMVLFRPCRVGDYIEAAGIAGTVDEITIFSTKLRTPDNKVIVAPNSSIMNGTITNYSAMDTRRIDLVIGVSYSADIALTKKILTEILDNNQYVLKDPSYTVGLAELANSSINFVVRPWVKTADYWTARFQLLEQIKNALDAADIGIPFPQMDIHVKELPLSK | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions.
Subcellular Location: Cell inner membrane
Sequence Length: 275
Sequence Mass (Da): 29753
Location Topology: Multi-pass membrane protein
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B0NAA1 | MNDTISIKKTGKQILVFLFFLFLIFLFLLKGKDVSQILKIAACASFPAIAAGIAMAGAFNLSEGLNLGILLKAMGHKVSFAQGMKYAYTGFFFSSITPSSTGGQPMQLYAMKKDGIDLSHGSLALLMELASFQAMAFLFELFAVAMIPVLGISLPVTIKILIIAGFIMNAAFVAFLLVVIFSERMGQRILGLLKKILPRLPFVKEETKSQWIGKMEDGLQEFHACALLMKEHKRAIAKMCVISAGQIICWFGVPYMVYLALGYQGSSFLHLFVLQILIYMSSSLLPLPGAMGISEYAFLQLFGSIYSGSSMTAAVLLSRGISFYFLLALSGIMLLLIYGAARQRKCKTIFS | Function: Catalyzes the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-lysyl-tRNA(Lys) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-glycerol + tRNA(Lys)
EC: 2.3.2.3
Subcellular Location: Cell membrane
Sequence Length: 351
Sequence Mass (Da): 38420
Location Topology: Multi-pass membrane protein
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Q4LEC9 | MSFSTTMRYSEGKLVLEKPPYLSPPKKITVLLNHITPLPTGGYTDRRYLMMKGEAVTEGNTIIFKPYKQYGWDEKTKPFFQYCEERVPQAKSYVRRLSEAVGRQVKPRLPTLQLLFRATRFPFLTATAAPVLIGVGTAAYLGYFDPLLFILTLIGASLIHLALNMANDYYDTKLGADPANITPTPFSGGSRILHYGLMTPKQLLTLIVLFYGVGIAIGLYLAFLRGLIPILAVMTTGVLISIFYTAPPLKLAYRGLGEVAVGIGFGPIIVLGSHYVQTQFFSPEALLASIPIGILIMLILYVNEIPDAPYDKAAGKHTLVTRLSKENVLKGYKLSLAATYAVIVAAVVLRLAPPTTLIALATIPKAISTVRNVAQTYGNPYLMIPALASNINVATFTGLLHAAGFFLWALISFLINL | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 1/2.
Function: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK).
Catalytic Activity: 1,4-dihydroxy-2-naphthoate + an all-trans-polyprenyl diphosphate + H(+) = a 2-demethylmenaquinol + CO2 + diphosphate
EC: 2.5.1.74
Subcellular Location: Cell membrane
Sequence Length: 417
Sequence Mass (Da): 45594
Location Topology: Multi-pass membrane protein
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E6N7D1 | MAEKQIAPTVLVGKKPAMSYVLACLTGFQSGSKEIVVKARGRAISRAVDVVQIVKNRFLQGVNIKDIRIGTEQITDEQNRTLNVSTIEIVLSSS | 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): 10229
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A0A963Y8P7 | MKTTTLTRTFWSYTLPAMAALMVSGLYAVVDGIFIGHALGAPGLSALNLAWPLAGLIWAVAMLVGMGGGAETGRARGAGDSRALGETLAVTLLLMVLVGIATGAVILGFGGPFLALQGADAELAAMGLGYLSVQGWAAPAIMAGMAFPLLLRNLGAPGLATVAMLAGAFVNVAFDWLFVIELGHGLAGAARATVIAEIVVILICTAAMARLGAFAALSPGAGALVRAGRILAIGFSSMIMALYISFVVVLHNMLFLKHGGTLTLAAYTVAGYVMSFFYYFAEGVAGGMQPLASYYHGARDRMRMAQVLKLALMLGVGGGVALTALVVAFPGPVAQVFAGSDTALIAEAAHGLRLHLSAMMLDGFIVLAATYFQAVGQARNATIITVGNIAVQLPFLYLLPQLMGVDGVWLAMPLSNVALSGAVVWMLWRAHRGTFARAAVLARRALEQSAPAYDG | Function: Multidrug efflux pump.
Subcellular Location: Cell membrane
Sequence Length: 455
Sequence Mass (Da): 46918
Location Topology: Multi-pass membrane protein
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A0A834R820 | MRKNSSRSAKFTQKLLCYIISNHNESVLLWDQSLGSKNGNFVIWDYHVILVYFDRHNGIALVFDFDSILPFPCDFEKYQCSVFKAQDKLFEKYCSLFRVVDAYEYLYTFASDRTRMKNEKHEFIKPPPNYPCIRTDTEINNLNSFISMDSKSFSIGEVCTFDEFRRRFSLSQ | Function: Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position.
EC: 3.5.1.122
Catalytic Activity: H2O + N-terminal L-glutaminyl-[protein] = N-terminal L-glutamyl-[protein] + NH4(+)
Sequence Length: 172
Sequence Mass (Da): 20409
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A0A8T2R0A1 | MRRHGWQLPYHPLQIVAIAVFFALVFAFYVFFAPFVGSRLLEIAVTVLYSPMVIVVFALYVWCVAVDPADDGLLHSKRCNSTACSRRTASSVDGKDLGISGHSRVDGCSNLEADQDEHLNLCWSQKFCTCIHGLFCASKARTPPNEADMLYCSLCKVEISMDSKHCRVCDKCMDGFDHHCRWLNNCVGRKNYKDFVALMVSRIAMLILQWCVGLWVLVHCFLSFKHFQGVITSKLGSSFSYVAYISVVAVCTILAMAATYPLTQLFFFHNLFIRKGFSTYDYIVAMREQEQKVTGGVVQSSQPQFQPLWELLKVLVSQRELYKEELGVLHHGSLWIMRNCNKVFFHRKDLYLSRMLLWDLQR | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 362
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 41483
Location Topology: Multi-pass membrane protein
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B7QKU6 | MYDQFMSMRDPRTVGWGLTRNLKFILPISLGYLYIVKVWGPRWMAQRKPYKLKSVITAYNLFQVIVNGFFFVQYARHSYVGGGYNVLCQGVSYSRDSNSMVILNLSWWYIFVRIADFMDTFFFVATKKFSHITFLHANKVE | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 141
Sequence Mass (Da): 16672
Location Topology: Multi-pass membrane protein
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A0A1D8UR70 | MSRRSAPPHPVLSAFYGEAEARPEFVRSIFDRTARHYDRINNVFSFGSGRWYRGQMLKQAGLKSGDQVLDVATGTGLVAREAARIAGMRNVIGLDMSAGMLAECRRHLPIGLVQADAQYLPLADGSIDFISMGYALRHVADLRATFTSFRRVLKPGGRLLILEISRAENRFAQAALRFYLGRIVPVFSGVAASTDSRTLMRYYWDTIAACVSPEEIMENMREAGLKNVRCETMFGIFRAYMANVP | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
EC: 2.1.1.163
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 245
Sequence Mass (Da): 27324
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M5E9J0 | MMKKIPGFSHVQSFTTKGQGKSSENKSQTEGLRNDIIIRAARGEKTERAPVWVMRQAGRYLPEFRKLREQHEFFECCRNPEIASEITIQPIRRYEGLIDAAVIFSDILVVPQAMGMEVQMVPGKGPSFLKPLETPKDMARLKKVNVEKDLGYVTDAIRLTKIKLAGAVPVIGFCGSPWTLMAYMIEGGGSKTWEKAKKWLFDYPNESKELLSRIASVCAEFLVAQVCAGAQLLQVFDSWAGELTPYDFRNFSLPYLTAIAVDVHDRLSAISMSTPPMILYAKGAINHSMTQICRSGYDVIGIDHTVEPAWARKCVAEAQTSARKFAKTCGDKDTAHPVALQGNLDPALLYAKPEVIFDRVNRMLDSQYGGFGGGGALICNLGHGITPNVDPEHLRAFLMAVRRISKEIIARQDE | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
EC: 4.1.1.37
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Length: 414
Sequence Mass (Da): 45958
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A0A804PE79 | MAASALLTGSPWLRMRLLPDAPARPFRHLHLRRSFSVRASGADGSPAPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGRFVLRVEDTDLERSTRKSEEAVLADLAWLGLDWDEGPDVGGDFGPYRQSERNSLYKQYAEKLLDSGAVYRCFCSSEELEQMKEVAKQRQLPPVYMGKWASASDAEVQQELEKGTPYTYRFRVPKEGSLKISDLIRGEVSWNLDTLGDFVIMRSNGQPVYNFCVTVDDATMQISHVIRAEEHLPNTLRQALIYKALGFAMPSFAHVSLILAPDRSKLSKRHGATSVGQYKNMGYLPQAMVNYLALLGWGDGTENEFFTIDDLGTVTLNFGAISFAVQKFTINRVNKSGAVFDATKLKWMNGQHLRSFPHDELIKAFEDRWTDTGILQESESGFAKEAAELLKDGIDLITDADAALTNLLSYPLHTTLSSEEAKPVVQDKISEVAWSLISAYDSGELGQALAEGRDGWQKWVKGFGKSIKRKGKGLFMPLRVLLTGKLHGPDMGGSIALIHKAGVCCAVTPQSNFVTLDERFRMLKDVDWESLAKEQETPAVPAAAS | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
EC: 6.1.1.17
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Sequence Length: 576
Sequence Mass (Da): 63749
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B7PRY0 | MALKESVSIYSRLITKIKSFGATSNPVPPYEFMCQVGDPVLRVRAEPVDPQKITSPEIRKVIHTMRQVMRGTYSVGISAPQIGCPLQITMMEFSNSNIRMAKKEDMTARLYQAFPLKVFINPTMEVVNNQQLVFPEGCESIRGYSAEVPRYYEVKISGLNEHGEHHEWQARGWPARIIQHEIDHLEGCLYIDRMNSRSFQFNYWQYIKRLPKSRKLF | Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins.
EC: 3.5.1.88
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Length: 217
Sequence Mass (Da): 25202
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A0A132AKJ8 | MDNFLQAHKIIDEIHDSLIKRLESCRDSQQAQAIEKSIDERLKQLEIYIDKSEIALNKSSGPQRSTLKFKTDQLKYDHKQLLNSFRTLHQRRLHREREQKEREELLTRRFTTNAEARSSERDTHIDLGFREYFDQEREKLGGFDRSIDELFHTGSAVLSNLRQQRSMLANTKRNLLETLNSLGLNNSVMRLIEKRNLGDKFILFGGMISLTIVFLFIWIYLG | Function: Involved in transport of proteins from the cis/medial-Golgi to the trans-Golgi network.
Subcellular Location: Membrane
Sequence Length: 222
Sequence Mass (Da): 26200
Location Topology: Single-pass type IV membrane protein
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A0A834R5E0 | MMNLSDSFELETNDLFDDDDFINKALNENATNLNLSENKQEENFSIHSNTKVDVSNLIASSTKVNRDLPKCKLDFNIPETPTYCCEIRDRKRKIFSRRCLSIDLNSVQSSESNQNSFQDFRYSKEMKISKENLPTNIFKSPSVLSSIENRFSSPKNSKMNISLELTPEFNTSNKIREPANRPKDESSPRYPFKLNNNSNTKEIRSSLILGGGIPLQKCFSENHASIMRAVQISSSDPSLIGDFSRAYALPLMQNSKHRDLRSITCHVMADLLQQRYEDLIQSFTIIDCRYPYEYEGGHIQNAINLYTQDHIYNTFVKNQSKEAEIQTINSKRNILIFHCEFSSERGPSLYRFLRNRDRVKNSRVYPNLYYPEIYLLDGGYKEFFQHYSHLCEPCSYKPMHSKDHEEDLRRFRSACKSFDSKFSTMKKITRL | Function: Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle.
EC: 3.1.3.48
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Length: 431
Sequence Mass (Da): 50240
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B2AZX6 | MSLFSLKKAALAALSFCSLAATVQGSPLPSPSEVEVTIRQSGGYKNIVYFTNWGIYGRNYQPAQLPASQITHVLYSFANLRPDGEVYLSDTYADLDKHYPGDSWSEPGRNVYGCVKQLFLLKKSNRHMKVLLSVGGWTYSTNFASAASTPASRARFADSAVRLLADLGFDGLDIDWEYPASSGEAANYVLLLQAVRSALNSYSATHASNYHFLLTIASPAGPTHYNTMQLRSMANYLDFFNLMAYDYAGSWDFRAGHQANLYHTNDTATPYSTERAVSDYISAGIPASKIVLGMPIYGRAFTNTNGLGQAYSGVGGGSWENGVWDYKDLPKPGAQVVYDAAASATYSYDPAKRELISFDTAEMIQRKVAYLKQRGLGGSMFWEASADRTDGQSLIGTSFRELGGIDSSPNQLRFPDSQYENLRAGFV | Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
EC: 3.2.1.14
Subcellular Location: Secreted
Sequence Length: 427
Sequence Mass (Da): 46747
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B2AEK5 | MSGILRSKYRTALPLFLSIFQGLAEAVSPVSIKGTKLYDESGAQFFLKGTVYVAGDNRNDPLLNTTQCQIDAEHLKNVGANAVYIYSIDVSKLGQHRGCMEEFDKQGIYVWLQLGQLPMVLSRSDNTPRWDLGFYNTWTSIIDSFSEHDNLLAFGIGQETINGTSVTTLVAPSVKAAARDLKLFRDKRGYRPIPISYTAGDFEQYRLLTAQYLTCGPAESSVDLYGINIFNNCSDDKLDRLRSEFSNHHTPVVFAEDGCFPETREFSEVQTFFGESEFSRIFSGMNIYQWGRNEFGFALVVYGDEADRNLGQPGTFLPAYTSLQQVWSETVPQSTSRDAYTFSSTQLPCPTANPQVGWLVDRAAALPVISGLDINTVTARTRRTRPTTSTSATAVPTESGDNSRDNSRDEEVLASSGMSAGAIAGMAIGIVAAVVGGAGAAFWFLRRRKSRQGEPDDHNGPYEKAAADSDRLSTAKTELPDQERAANELEGRFHYHQLPVKTDWKYPLEAGSKPVSELPDGAGRPGNHFELEGSPVHGPGYNPGAELPAPAPVPK | Function: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall.
EC: 2.4.1.-
Subcellular Location: Cell membrane
Sequence Length: 555
Sequence Mass (Da): 60820
Location Topology: Lipid-anchor
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A0A351HI85 | MNIGKTLIHWYEQYQRELPWRTTKNPYLIWVSEIIMQQTRIQQGLPYYLKFVTDFPTIEALASAPQDKVLLNWQGLGYYSRARNMHETAQIIVKNHNGIFPSSYHELLKLKGIGPYTAAAIASFCFNERIPAIDGNVNRVISRIYDIELPINKGPGQKMVRDFSIQTLGKNDPCTFNQAMMDFGALICTPTNPLCKNCPISLECKSLKNNTITLRPVKEKQAPPKARYFTYLVVNHKGSTLLMQRQHNDIWKGLYEFPMWEFDSPMVAEEFLQLPKIMKLLKGCRISSISENRLPIHKLSHQNIYSQFIQLTTEPLPKISNTLEVKADELKNYALPKLIINFLHHQKKEFSRI | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Adenine glycosylase active on G-A mispairs.
EC: 3.2.2.31
Catalytic Activity: Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.
Sequence Length: 353
Sequence Mass (Da): 40887
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A8DIU0 | MDSGMQQCQFYCGPRALTLFVLLHICLSLPNESLAGYNEKRLLHKLLDHYNVLERPVANESDPLQLSFGLTLMQIIDVDEKNQLLVTNIWLKLEWNDMNLRWNASEFGGVKDLRIPPHRLWKPDVLMYNSADEGFDGTYPTNVVVRNNGSCLYVPPGIFKSTCKIDITWFPFDDQRCEMKFGSWTYDGLQLDLQLQDDAGGDISSFITNGEWDLLGVPGKRNEIYYNCCPEPYIDITFVIIIRRRTLYYFFNLIVPCVLIASMAVLGFTLPPDSGEKLSLGVTILLSLTVFLNMVAETMPATSDAVPLLGTYFNCIMFMVASSVVSTILILNYHHRNADTHEMSEWIKVVFLIWLPWLLRMHRPHGSCEYGQQPSRPASVATDRKPLHFQDVELKERSSKSLLANVLDIDDDFRHNHRGGGTPTPLPTATFFRTVYRQNEDNGNGGRLHESLVSNHSCLSADYELALILKEIRFITDQLRKEDEAADITRDWKFAAMVVDRLCLIIFTLFTIIATLAVLFSAPHIIVS | Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular Location: Cell membrane
Sequence Length: 528
Sequence Mass (Da): 60101
Location Topology: Multi-pass membrane protein
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A0A834R3C6 | MEQRNKSYPKDGKFFDRLRFFIIIGFIVWITMFMIDYYFFSKTNEIDANNQYISFLENLSAIDSVGEIRIETQQLSHYVRISPKNAQNYNIILYWTKYFNEDIMNQMEQSFGRNVDHSLFRPIQCYRKYPKCLITSDRDYVREARALIFHWRDFNASDLPKRFRSDQQWILYNLESPFHTPKLPDDHFNGFNLTATYRFDSDVPIPYGKIINRTKPLRNDLKKTINILGKIKPIVWFVSNCVTESRREIYVKNLSKYLPVDIYGKCGDLNCSVRYKDECYRKAAKKYLFYLSFENSICIDYVTEKLFNVLNYDIVPVVFGGANYTKILPPGSYIDASRMDPQSLAIELIKIANNRNLYLKFFEWRKFHFVEFPSLFCEVCEKIQLDRIESSKRIISKWKSYKEINHWYFDNSCNKTSESM | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 420
Sequence Mass (Da): 50265
Location Topology: Single-pass type II membrane protein
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Q3MQ08 | MADDKDVLRDVWFGRIPTCFTLNPDEVTEREAEPYYLLLPRVSYLPLVTDKVKKHFLKVMRTEDVEEMWFEHEGTPLKWHYPIGVLFDFHASNTVLPWSITVHFKNFPDVDLLHCPTNSMVEAHFMSSIKEADALKHKSQVVNDMQKKDHKQLWMGLQNDKFDQFWAMNRKLMEYPTEEGGFRYIPFRIYQTTNDRPFIQRLFRPVSTEGNPHTLFDLLKEMCPDALTKDGEEKRFQVVIHGIEPLLETPLQWLSEHLSHPDNFLHICIIPAPTD | Function: Involved in autophagic vesicle formation. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. Involved in mitochondrial quality control after oxidative damage, and in subsequent cellular longevity. Plays a critical role in multiple aspects of lymphocyte development and is essential for both B and T lymphocyte survival and proliferation. Required for optimal processing and presentation of antigens for MHC II. Involved in the maintenance of axon morphology and membrane structures, as well as in normal adipocyte differentiation. Promotes primary ciliogenesis through removal of OFD1 from centriolar satellites and degradation of IFT20 via the autophagic pathway.
Subcellular Location: Preautophagosomal structure membrane
Sequence Length: 275
Sequence Mass (Da): 32454
Location Topology: Peripheral membrane protein
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H2MJU7 | MKKLSESLLHLLSCFHLLAAVTSQVNPDVCRYPLGMSGGQIRDEDISASSQWSESTAARHGRLDCEEGDGAWCPETTVEPDNLKEFIQIDLNLLHFITLVGTQGRHAGGMGNEFAQMYMIKYSRDGSRWISWRNRQGKQVIEGNRNTYDTVLRDLDPPIIARFVRFMPVTDHSMNVCMRVELYGCKWLDGLVSYNAPAGEQMKLPAFPVFFNDSVYDGAITHMMTEGLGQLSDGVMGLDDFTQSHVYQAWPGYDYVGWNNESFPSGFVEIMFEFDRPRNFTTMKVHCNNMFSQHIKIFRQVVCYFRSDSDWESTVLSFSPVVDENDPSARFITVELTNRMANAIKCQFYFKDAWMLFSEITFQSDRAMYNTTLVPPTIGPPTNTPPEDDPTHKIDDSNTRILIGCLVAIIFILLAIIIIILWRQVWQKLMEKASRRMLDDELTASLSIQTEVFGHNHSQSRVTNEQESNAAYERIFPLGPDYQEPSRLINKLPEFAQSSEEPASTSTASSKSTTTTALVQDGAPHYAEADIVNLQGVTGSNTYAIPAVTLDLLSGKDVAVEEFPRKLLTFKEKLGEGQFGEVHLCEAEGMQEFLHEEYLFDIPEDQPVLVAVKMLRSDANGNARNDFLKEIKIMSRLKDPNIIRLLAVCIYSNPLCMITEYMENGDLNQFLSRHEPEGQLALLSNTATVSFSNLCYMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWEILNFCKEQPYSQLTDEQVIENTGEFFRDQKRQIYLPQPVLCSDSLYKIMLTCWRRNAKERPSFQEIHRRLSDLES | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
EC: 2.7.10.1
Subcellular Location: Membrane
Sequence Length: 861
Sequence Mass (Da): 98039
Location Topology: Single-pass type I membrane protein
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A0A075JDR3 | MTWPLIALGGAVGAVLRFVLDGEMKARGPRTWPHSTFAVNLLGSFVLGVLTAHPRPGWLSALVVTGVCGGFTTFSTASVETLTLLRARRAATALGYAVGSVVACVAVILLAHRIA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 115
Sequence Mass (Da): 11928
Location Topology: Multi-pass membrane protein
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B7Q9K0 | LPPRDICVSAPTGSGKTLAYVIPIVESLKPRIMRAIRAVVVLPVKELAAQVQAVFQQYLRGTSLRSQLVTGTKPFSEEQLSLVHKNARGYSSLVDIIVATPGRLLDHIRKTPGFSLHLLKFFVLDEADRVIEDVRTTLIPEVEQAVEPAQKLLYSATLTQDPEKLQSLMLFQPKLFTAAGKRDPAVERAAFAGKYTTPQGLSEFYRVVQNAKKPLALWDLVANRGYTGTLCFTGTKDDAHRLCLVIKEMGGVRVEEFSSDLSATERARVLRRFASGGLDLLVCSNVLARGLDVANVRNVVCYDPPKYVKTYVHRVGRTARAGVPGTAVTFLRQGQLEAFQTMLSSAGKSPVEALEEGEAGLEVFHEKYRVALKAVEAAVGREKKEVQIGKKFK | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 393
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): 43248
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A0A955MIL1 | MPANDETGEKTEEATPRQRERAREEGRVASSREVGTLFVLTAATVTIYFSSTYMIGRLESLFIRIFDAMGSAELSMGGAIRILQEMLFQTILAILPVMLGLIVASLMGWILQIGIIFVSKPLQPQLSRINPIEGAKRIFSTQILAETAKSIFKFTVVGSVSYYLLKPAIPFAAATMSRDSKIILATIFELGFDLALYLLLFLLAVAVFDYSFQKWRHSKDLRMSRYEVKQELKEQEGDPQIKARVRSIRQQQLRQQMIAEVPKAEVVITNPTHYAVAIRYDMDNRPSPHVLAKGRGVIAQRIKEIATENNIPLYEDKWLARQLYAACDVGDSVPVDLWQAVARVLAYVRTLNDQRKAVTA | Function: Required for formation of the rod structure in the basal body of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin.
Subcellular Location: Cell membrane
Sequence Length: 360
Sequence Mass (Da): 40560
Location Topology: Multi-pass membrane protein
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B0NHG4 | MITLTGKSVFGGVAIGRIAFYKRNEITIKRTHVDDIEGEVKRFETAKEKAVAQLQELYNKAMEDVGESNAMIFEIHQMMLEDLDYVESIVNIITTQKVNAEYAIGTTADNFAAMFQAMDDAYMQGRAADVKDVSERLLQVLSDNSTDAMKMDEPSIIAADDLVPSETVQLDKEKALSFITMYGSANSHTAILARTMNIPAVISLGEDLKKEYDGKLAIVDGLEGKVYIEPDAKTMEAMQEKQRKDQEQKELLEQLKGKENITKSGQKVNLYANIGNLADVGAVLKNDAGGIGLFRSEFLYLESETYPTEEQQFSVYKTVAENMAGRKVIIRTLDIGADKQVDYFGLCKEENPAMGYRAIRICLTKPEIFKTQLRALYRASAFGQIAIMFPMIISVNEVRRIKDIIEEVKKELTEEGIAFRENVELGIMIETPAAVMVSRELAKEVDFFSVGTNDLTQYTLAIDRQNQKLDAFYDSHHPAVLEMIRMAAANAHAEGKWIGICGELAADLSLTETFLEMKIDELSVAPGMVLPLRKRIREAW | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
EC: 2.7.3.9
Subcellular Location: Cytoplasm
Sequence Length: 540
Sequence Mass (Da): 60407
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A0A1U7YPS5 | MASADQEKQAQAMENLEGFPPLSPLSQIMHSLTIIVVAGFDVPFDKSQTVELLKAMHTTSDPRLFSVIVTDRKGVHRWKKVTQVAYEDHIFVASFPEGLSMEDYDKHFKDYLTKVSVTPFSDNLPPWEVHAIMYPTSNGAGSLVFKFSHALGDGYSSLGSIMTLCRREDDPSLPITFPSSTSKAGRKNSWSRSASVLISWFINTVRDSAVSTLQGTFLRDDKTPIRSGTPPVGLQPMEISPVSFSLDCIKRIRSKLGATVNDVVIGILSYAIQLYIQRMDFISSGARVTALIPLNMRMLNGYQDIGDMLKANLWGNRFGLLSISLPSFSDEEKVDPLHFITSSRDNIRKKKNSAAVHFSSGLLTMLNNVLGPKALAGFIKSSFRNTSTTISTVVGPTHKISLENHPVKRCYFTVVGAPQDVVFTIASYMEELCIVATAEKSFIDSNVLISCVKKAFEDIYQAACGINKVELK | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Subcellular Location: Cell membrane
Sequence Length: 472
Sequence Mass (Da): 52099
Location Topology: Single-pass membrane protein
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A0A424Z125 | MISIKKILLSLASLPIILSAAEYQLSTHILDISKGGNAKNVKVELYKLENNNQWTKIDEKYTGENGRITDFLPYTNTQNTVSGVYKLKFYTKDYFDKENTKSFYPYIEVGFEASKDQKHYHVPLTLSPFGYSTYRGS | Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
EC: 3.5.2.17
Catalytic Activity: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+)
Sequence Length: 137
Sequence Mass (Da): 15738
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A0A1D6QKX3 | MAVRKGKLCCGLLLAGVTWKLSQASLLNFRPPCCRCWDEGPDEAELLPASTQPSRPRARLPPPRDGQKITVLSIDGGGIRGLIPAVILASLEEKLKEVEKEADPEGDWEDARIADYFDLIAGTSTGGLIATMLATPRPGDENRRPLFAAKDIRNFYYKHGASIFSPVSKTDSLFSWLNDQYRAFVRGGPKYDATPLEGKINRLTGTLTLADTVTKILVPAFDVRRLNTVTFSSYDAPEMLKPHKKHYLSDVCLGTTAAPTYFRPHHFWSHYTDGDRRHPFHLIDGGVGANNPTMLAISRIAREILCGKNPDFEPLEEDQAVDYSKFIVISIGTGSTKERGRYNADDCARWTDIKWVRKDGHRPIIDMFAHASDFWVDTHVSTLLDGQRCKNYLRIQALKEDGLVGPMLLLDNVCKHNMDNLIKVGENLLQKKVTKVDMITMRYEKQDTEMTNEEELKNFAKMLYDERKLRLGKDKQKRPRVDQNEQALPDGAMTTDTKAQATADEMAEK | Function: Lipolytic acyl hydrolase (LAH).
EC: 3.1.1.-
Sequence Length: 509
Domain: The nitrogen atoms of the two glycine residues in the GGXR motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Sequence Mass (Da): 57271
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A0A357APX8 | MERFCIITNRSKDEELAVTNEVAEYLKSKGKFVFVAQEECQCEKGCYTDVEKLPENIECIIVIGGDGTLLEASQDLQKMNIPIVGINKGTVGFLADIEAEDYASALDDIIEGNFRIQNHMRLDATVFRKTPDKKGNGARGSALNDVTITRYGFSRIMSTAVYVNDVYMTTYKGDGVIVSTPTGSTGYNLSAGGPVCDPALYSIIITPICPHSLTARSVILPADAKVTIKVDVSKKTQENEAVVSIDGEMISELSAGGYVEIKKSDIDTKIIKFKRTSFMQIISEKLGK | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Location: Cytoplasm
Sequence Length: 288
Sequence Mass (Da): 31450
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A0A834R8E7 | MTLESEDHRGESVLSKSNSNSSTSISSLKKQPNQISLLTSTENYRNNLQNHFGQKNGKISLNNNAKPNDATMNLNNHNHNSYRNNNNNNDNHKSNNDDEKDYDQMNEKKPEIIVHLDFNNDSENIDYDKKRGRITIFGYRPSQIKWTNVIWLLFTHTLAVFAYVYVSLYPVKLFTIPWIVFLGVAGGFGVSIGAHRLWAHRSFKARWPLRAGLVLAETLSMNGGCYSYARDHRCHHKFVDTNGDPKNAKRGFFFAHIGWWMLKKHPDVFRMGKKLNHKDLDDEPLITWQKKLYVPLFILISIVMPTLVPYYVWNEDLIISFFMSAVLRTVVVVHHLFTVNSIAHIWGLRPYNRDIGPTESKLTMYLSLGEGSHNYHHTFPMDYANCEKKWWEVFNPSTLFVDICALLGLAYDLRKPSEKVIQGVVRRIGDQKFYETKLIVHRSLRHRIMHGINDWLIGTIVAGWALYPPILFKLVTGRPLIVF | Subcellular Location: Membrane
Sequence Length: 483
Domain: The histidine box domains are involved in binding the catalytic metal ions.
Sequence Mass (Da): 55959
Location Topology: Multi-pass membrane protein
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A0A0D6XNL2 | MKKEKRLDLILTAIQENNFNKKQQIVDYMMRHFGVYYSLTTISRDLQELDVYKIPVENNKYIYKKMNKNKQLDARKHLEAYRDEILKITIIKNYVLIKTSPGFAQSIGYYIDQLQIKEIIGTIGGNDALMVLTASSEMAQYVYYQLFHTAVETQN | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Function: Regulates arginine biosynthesis genes.
Subcellular Location: Cytoplasm
Sequence Length: 155
Sequence Mass (Da): 18230
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A0A0U5HE52 | MTLLFDRFDSPIGVLTIAGDERGLSHVLFPENRHPARGRDDWHYAPDALPEAREQLLQFLHGERSSFDLVLAPRGTPFQLRVWQALALIPFGQTWSYLQLAQHLGQPSATRAVGAANGRNPLPIILPCHRVIGSNGALTGFGGGLETKAALLRLEQRQAPLFA | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
Catalytic Activity: a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a thymidine in DNA + S-methyl-L-cysteinyl-[protein]
EC: 2.1.1.63
Subcellular Location: Cytoplasm
Sequence Length: 163
Sequence Mass (Da): 17922
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A0A0D0G2T7 | MYAEQSIINENGYTLVEMLLSLAIFSLIIVYLTNMVPLLRYHTYSSEIADQMQWEMFMNQAKREIRQSDEIFLTASYNRILFWKDGTNTLYERYGNRIRRRVDGMGHQLILFRIRRFDYEQIPHGIKFIVTHENGKIYEEEIYLPREIPITNNK | Function: Required for transformation and DNA binding.
Subcellular Location: Cell membrane
Sequence Length: 154
Sequence Mass (Da): 18566
Location Topology: Single-pass membrane protein
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A0A7I4CD25 | MEPLRCATGSSSSSLSSVVSASKASFCGGNVGGRNLVALRSVGTNACFPRRSLSVVRAVDGNSTTTTRTPSAAEEVPTSTPASSKEVEVEVPIEKRYPAFPAVLDINQIMDILPHRFPFLLVDRVIEYNPGQSAVAIKNVTINDNFFPGHFPQRPIMPGVLMVEAMAQVGGIVMLQPDVGGSKETFFFAGVDKVRFRKPVIAGDTLLMKMKLTKLNKRFGVAKMEGQAFVGGELVCEGEFMMALALGDSNLSDNNWSFCVGDAANITLPLTWPGLWRSTS | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
EC: 4.2.1.59
Subcellular Location: Cytoplasm
Sequence Length: 280
Sequence Mass (Da): 30065
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A0A948U5X8 | MKTLKALKSRREGIEKINKIARAMEVIAATRLRRYETDVAGFRPFVQAQRLVMGSLALRLKKLNNLWAEPPAQDKMGIVILISSERGFCGGFNNQLFRLIESLKDEQSLSFIALGKKGAAYLKRQHFNLIEELVLPGDAQMQDFVRRITEKIISSYQEEQQSIYLIFNKFRQHLLGRGFRKQLLPLEIQEEKGMVLDYIFEPDTEALLEELLPVYVGSEIKAAILESKAAEEMARMVAMTQARRNAEDLIKRLTLQYHKARQTGITRELVEIANAIR | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Subcellular Location: Cell membrane
Sequence Length: 277
Sequence Mass (Da): 31823
Location Topology: Peripheral membrane protein
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A0A1D6GZA1 | MVQCTQPPPQLKLPESKITEPTDDENQDLPPKPEKRTRMHHIERHRSCVVTLSDIELNGLQPRHLHQPIEISPGGSQCSLHEETPTDTNASHRHAIADAAWEALKRSMVYFRGQPIGTVAAIDKSQGAALNYDQVFMRDFIPSALAFLMKGEHLIVKNFLVETARLQSREKMVDLFKLGQGVMPASFKVHHRNPTQKTESLLADFGETAIGRVAPVDSGLWWIILLRAYTKWTGDNSLAESTNCQRAMHLILRLCLSEGCDTSPALLCADGCSMIDRRMGIYGYPIEIQALFFMAMRCALSLLKQESDADFVNHITKRIQALSYHLHSYYWLDFQRLNDIYRYKTEEYSQTALNKFNVMPESIPDWIFDFMPSRGGYFIGNVSPARMDFRWFCLGNFIAILSSLATGEQAEAILDLVEERWQELIGEMPLKICYPAMENQEWQIVTGCDPKNTRWSYHNGGSWPVLLWLLVAVSVKLGRPHLARRAVELMEQRLAKDDFPEYYDGKAGRYVGKQARKFQTWSVAGYLVAKMLLDDPSHLRIVALEGDSHSRAPFLKRSNSCP | Function: Invertase that cleaves sucrose into glucose and fructose.
EC: 3.2.1.26
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
Sequence Length: 562
Sequence Mass (Da): 64008
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A0A354CYI6 | MSDKLIITGLAVPCRIGVTEAEREKPQTVWIDLELAIDAEQAATHDDVRQAVDYSAVVETVSRYATARPFNLLETLAEDIASGVLALSSTTHLVLRVTKRALPSIDSASVEIARSREASG | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
Sequence Length: 120
Sequence Mass (Da): 12934
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A0A7C9DYK4 | KILAMAVYKVKLIGPNGEENEIDAPDDSYILDSAENAGLELPYSCRAGACSTCAGLLVSGEVDQSDGSFLDDNQIKKGYVLTCVAYPKSDCVIYTHKEGELY | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Subcellular Location: Plastid
Sequence Length: 102
Sequence Mass (Da): 10972
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A0A090KUH4 | MKKQYKIDGMFFGSFAILVLTDRLWWFIQTFVLSNFGQFRLMSIYMGIESLMLMIFTGYGGAWLDKHSRFYGIKVLLCIVTILSIISCIAINFAFKLNYLNEEKINKISNSCYFSLLISVISTSIGSFFYNLIRLVLTKDWIVILSKEFKKNEFDDESIRSKKFKNDKKLTYYNTISALIYQISFIIEPIITGFVMNYLNYQMASIVFCIFNISMWIIISLFLNFIYKNVNRLKRIKKRRHEEEKLKTICNSNISTCINDNKLDVKNELKIIKFLKHPVSFVAVALSLTYMNILQLSGVSITYASINNVSEQSLNLFRCIGSIFALIGTILYPLFKKFFGLKKTGFIGFFMQQIFLLPSVISIFLPGSIFEYNIFFKELTNINYSIYIYLIGITFSRLGLFIGDCAVNQQMQHMIEEEIRSEIFGIHTSLSYTLTLLSAGLIFLFPDPKYFGFFIILSMIELIVGIIFYIIHMYSYYK | Function: May be involved in iron transport and iron homeostasis.
Subcellular Location: Membrane
Sequence Length: 478
Sequence Mass (Da): 55687
Location Topology: Multi-pass membrane protein
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M1X9I3 | MNALTIYLILVPVVGFVLLLVSILLGKHVPYAEKVTSYECGFSPIHGQNRSPFTIQFYLVGILFLIFDIELFMTMPYALTVYETGYYGFWIIMVFFGILTLGFVFEFSSKALYFSQVIIEEEDDQE | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Mitochondrion membrane
Sequence Length: 126
Sequence Mass (Da): 14496
Location Topology: Multi-pass membrane protein
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G5EBS5 | MGDYDYLIKFLALGDSGVGKTSFLHRYTDNTFTGQFISTVGIDFKEKKVVYKSSRGGFGGRGQRVLLQLWDTAGQERFRSLTTAFFRDAMGFILIFDITNEQSFLNIRDWLSQLKVHAYCEQPDIIICGNKADLENRRQVSTARAKQLADQLGLPYFETSACTSTNVEKSVDCLLDLVMQRIQQSVETSSLPLSECRGVSLDGDPSAASSYCANC | Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
EC: 3.6.5.2
Subcellular Location: Endosome
Sequence Length: 215
Sequence Mass (Da): 23979
Location Topology: Lipid-anchor
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A0A0D6XRV5 | MSYRQWLTEAKNRATEAGLEAAAVEWLLLDLLDWTRVTLLCDGDLAMLDMDAQRLDQGLSRFLAGEPVQYITGKATFYGRDYDVDARVLIPRPETEEVVAQFLQVCPQSGVVADIGTGSGIIALTVKQERPTLDVWATDISSEALAVARHNAKRLDVAVNWLQGDVLAPFIERDIRLDGLISNPPYIGTEELDQMGKDVVAHEPHLALFVEQAGYAIYERLLQDLPKVMNNGAPVVFEIGYQQGETLAQMAKHMYPHLSPQVLTDINGHPRIFYMTWKAIPSEK | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Length: 284
Sequence Mass (Da): 31705
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C5CBR9 | MSTLRRLVVTADPALLLTDVPPIGVPDDAERLSDDGLLGWRFTADEWAAAPEPGSGWDVLTLPAAVAAAPVPLVVTDVDSTLIRQEVIELLAAHAGREAEVAEVTERAMRGELDFAASLHARVEALAGLPVGVVADVVRAIRPTDGALALIEAVTAAGGRVCAVSGGFTQVLAPLAEAWGVHAYCANELEVRDGHLTGRVLGDVVDRAAKAAMLRAWAEDAGLTPEQAVGVGDGANDIDLLEAAGCGVALCAKPILREHADVVVDVPSFTPLRWLLGL | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
EC: 3.1.3.3
Catalytic Activity: H2O + O-phospho-D-serine = D-serine + phosphate
Sequence Length: 278
Sequence Mass (Da): 28826
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A0A6C2YMM7 | MNVLVIGKGGREHAIVWKLRQSPRAGKIFVAPGNAGTALEATNVPIQPNDVAKLIQFAKKESIGLTIIGPEDPLAAGIVDAFQAEGLRVFGPSKAAAQLEASKVFSKTLMRNADVPTSEFRLFDHPDPAKSYIESREYPVVVKADGLAAGKGVFVCSDKPAAVRAVERIMIHEEFGAKVGRQIVIEKRLEGEELSSFALISGRTILPLPCAQDHKAVFDNDEGPNTGGMGAYCPAPIGTPELLAEVDESILVPVVHAMKRGRTPFKGVLFTGLMLTNQGPKVLEFNCRFGDPETQPLLMRLKTDLLELLEAVVDERLDEFPAESLQWDPRPAVCVVLASGGYPGKYETDKIISGLDEVAQMPDVKVFHAGTKLIGNRVMTDGGRVLAVTALGDDLLAAKTRAYEAVAKIHFNGMHYRKDIADKALRVKPTPKAPSELNPALAARIARQSASDAKRKTE | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
EC: 6.3.4.13
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Length: 458
Sequence Mass (Da): 49425
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A0A3D2TY18 | MNNQKVPMIILSECVVFPGSSVYLNLYDSRSENAVSQAIGPGGKLVGVTRMPAETADDDHSKLYSVGTLLEVKQMNTPRKGHPQAVVRGVCRVMIEEVHRESDCYYCEYSEFQEIESEEDSQTILAMGSILNALQRKYAEFREDVPATVWDAIADEKDRGAYVDQLSGLLESDYTQKQKLLEEPSIDEREKRLAVYMTQEINLFIEQEKIQKKIRENIDKKQMEMYLREQIDAIHEELGDDDVGSQAAKYLHKLEKLKAPKRVKKAIREEIMRYQRFAKNPSESEMIRDYLDNLFAFPWKKKSEESLDIAYAAQVLDEDHYGLTKVKERILECLAVKAMKKDAVSPILCLVGPPGTGKTSIARSVARALGRSYVRICLGGVNDEAEIRGHRRTYVASMPGRIVKAFCQAKTNNPLVLLDEIDKIGKDYKGDPSAALLEVLDPEQNKHFSDHYMEIPINLSHAMFWCTANSLESIPLPLRDRMEIIQLSGYTDNEKFHIAKEFLWKKQKNANGLTNSQITITDKAIRMIIARYTREAGVRDLERKLILLCQKAAKSIATGEKDKVRISERNLKEYLGKEVHTIRMANKRAQVGIVRGLAWTAVGGETLEVEVGIMPGNGKLLLTGKLGDVMKESAQIALTYVRSQTAKLVKDSYYAEHDIHIHVPEGAVPKDGPSAGVTMATALYSAVTGWKVRADIAMTGEISLRGSVLAIGGLKEKMLAAKAAGIAQVFIPKDNESDLAEFSEDILEGITVTTVSSIKEIWKQSIETASGEA | Catalytic Activity: Hydrolysis of proteins in presence of ATP.
EC: 3.4.21.53
Subcellular Location: Cytoplasm
Sequence Length: 773
Sequence Mass (Da): 86483
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A0A3Q2I0J0 | MARLLRTLWGLPFREAPGRALRGRAGCGGLGARAGHGDAGSPTKPELSLAKSEWQKKLTPEQFYVTREKGTEPPFSGIYLNNEESGMYHCVCCDSPLFSSEKKYSSGTGWPSFSEAHGTSGSDESKTGILRRVDHSSGSVRTEVVCKQCEAHLGHVFPDGPGPTGQRFCINSVALKFKPSSN | Cofactor: Binds 1 zinc ion per subunit.
Function: Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residues.
EC: 1.8.4.12
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-dithiol + L-methionine (R)-S-oxide
Sequence Length: 182
Sequence Mass (Da): 19634
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A0A496S5K8 | MIGIVGYGNMGRALLGGLLSNYRRERVLVYDKDRSKISKLKKDSLLRKAKSLEEVADKSSTIIIAVKPQNIREVLEGIREFYCNQLIISIAAGITTSFIEKAIGKKPKVVRVMPNLSAEVKRSVTGISKGRYASLVDLKKAERIFKSIGSCLILKEKYINPLTAISGSGPGYIFYFLYCLEDSAVSLGFSKREARFLVFNTFKGAGELISEKDDFLELVKKVASPRGTTEEALLYFKKKNFKRIVKEAIEKANKRAEELSKPCTTA | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
EC: 1.5.1.2
Subcellular Location: Cytoplasm
Sequence Length: 266
Sequence Mass (Da): 29678
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A0A1U8AUJ5 | MSALFNFHSFLSVVLLVICTCTYVKMQFPAILEQKTGFRGFFWKAARIGERLSPWVAVGCFAMGVSIIFS | Function: Involved in the early part of the secretory pathway.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 70
Sequence Mass (Da): 7870
Location Topology: Single-pass type I membrane protein
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A0A6C2YUB7 | MRLIHRIGPKIATEPGMRPTRGEPGMSGDAGGDVSWGLSLWPLGRYSDRTGDWDSLRGAIMSLDVDRICVVVGRTRHKMVAIELQEAVKRGAKFIELRLDFLARAVDYKRLMAHKACPLVATVRRTADGGRWPGTEEQRQMVIRQAIVSGYFEWVDLETDVADTIRRFGKVKRIVSYHNFQEVPEDLGEIYEKMCNQDADVVKIAVMAQSPIDNLRILKLLERAPKPTVAHCMGDLGFPSRILALKYGAPFIYAAFNKDRGIAPGLPSMEDLRAIYPIDRINRETKVYAVLGDPIAQSYSPQLHNALFQKLNMDAVYVPMRVPRAQLQATLNAMESLPIHGYSVTIPHKETVATLAQEVSPMVAQTAAANTLVRRDNGFFADNTDAPAAVESIRSVAPKQADGTAYEFQGKAVVLLGSGGVARAIAHALKREGVNLTIAARNHAAALKLAEEVGAKAIDWQVRHNGSYDILVNCTPIGMFPNMNDSPTHPSYFRENTIVFDTVYNPENTLFLKTARERGCIVVSGLEMFVRQAGLQFQAFTGQEPPLEELRQLLRRAISPVTHHAATQAEGEGEGEGESEPTEGDE | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
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).
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 586
Sequence Mass (Da): 64679
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A0A834R2K3 | MNDEAVAHYSAIIDNLSTGVKWLNQTFGKCGLTKTGWQIDPFGHSREQASLFSQMGFDSLFLGRIDFQDKNLREKTRTMEMIWKASPSIGDQCDMFTGVLPNVYWPPKGFCYDVNCFDETLNQQNIMRKAREFVQIVKQQAQTYATNHTIITMGMDFYYQSAEKWYSNLDYLIDAVNSLTHQEGVHVLYSTPGCYAKALNKLGRSWPIKLDDFFPYADAPEAYWTGYFTSRPSLKYAIKKGSNLLHVADQLNVLTMKGIEHTKTYWDLRNVMGILQHHDAVTGTCKQYVNDDYQRMLSEAREKAEIAVKDCYRSMIRAKSAPGQSVLGFCNHLNISQCAFTEHIDDQMSTVMSVYNPIPHSMRHFVRIPVTNDQYKVMDHYETIIPSQIIPIHPKIVSLKERNSYATHELVFMSTLDSLGISSYLIAKHNDFSSSVVSEKIHSNGQDVFLHNGKMGILIDGISGLIKELQLPTGDNIPFVQAFWYYKGTSRYMGDKPSGAYVFHPSHKTPYIVSNKASTKIYRGPMVDEVHQVFTSWCTQVIRLYRNYNYIEFDWVIGPIPVGKFPDENGLEIITRYETNFHNKQTFFTDSNGRETIRRIRHHRPTWELQTNEEVSSNYYPVTSWIFIRDLSKDLQMTILPDRSEGGSSMTDGTIEMMLHRRLLFDDGYGMDEALNEPGINNEGLVVRGKHRLILDKIQESVRFMRKLSKTTSWIPIYLFQNVPEVYGPSFVINLNYAGLREKLPVNIHLLSLEQWDEHHVLIRLEHFYEINEDIKYSRETQIRLRNLFNPFTIEDVREMNLLGTEELDQSESLKMRWIPELNPYENYTQVLASTFIKSSQTIRRDDGTFTIFMKPMQIRTFLVRIRPRLYRKRSIFLSSSSSFEQQKKL | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.2.1.-
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.
Sequence Length: 890
Sequence Mass (Da): 103354
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B7PZU6 | NVRVRFAPSPTGEMHLGSLRTALYNYLFAKKHGGQFILRIEDTDQTRVVPGAAQRIVDTLEWAGLAPDEGPSLGGNFGPYVQVTTDLVWSAELEFQLEDTGHAYRCFCTDMRLDLLRKDAMRNRQIPRYDNRCRSLTPDSTKLSGKPHVIRFKLSEGDLTFEDGVHGPVTLNTAEREGDPVILKSDGFPTYHLACVVDDHLMHVSHVLRGVEWQVSTPKHIMLHEALGWEPPRFFHLPLLLNKDGTKLSKRQGDVHVGKLKDAGFSPETLLNFLVLAGGGFGKQEKDTFYDLDDMVSQFNPDELKGSSCRLDPERLVQLNRLHLRRCLDDPGKTLSLAGELRRLLDQHQEPVPSDFLSDDDLVRVLRETAGRLTSLNDLLDPSMDFVWRSPSLVEEDQQFVENRDALQDLCSRLESVSADKFNRETLGVLLHNAASDSGIKYSQLMQSLRKLLSGLQKGPGVAEMMTLLGKKQTLLRLRKQIDQRGSEKSCSRG | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
EC: 6.1.1.17
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Sequence Length: 494
Sequence Mass (Da): 55577
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A0A131ZYV3 | MSDKRGVLFVCLGNICRSPIAEAVFQKLLDQRGLNDRWFCDSAATADYHTGEMPDHRAIKVLQENGIETKHRARRIKKDDFQRFEFIFGMDTNNIDSMKRFAPKGTESKIQLLGDYHPDGAQIIEDPYYLGGIDGFYANYDQCKKCCEAFLDKMSK | Function: Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
EC: 3.1.3.2
Subcellular Location: Cytoplasm
Sequence Length: 156
Sequence Mass (Da): 17915
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A0A0F6P104 | DAIKLMNKEYFFPIKSSFYLYITSPSIMFILIMMIWMIYPFYTNLLMFDYSLLYFLCLMSMGVYTLILAGWSSNSSFSMIGSIRSIAQSISYEVV | Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Membrane
Sequence Length: 95
Sequence Mass (Da): 11118
Location Topology: Multi-pass membrane protein
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B7Q1Z5 | MPRIEPLEPLKESSTIYDALAIKEEKEQPPPKPAKKPAKKKPKETEKQQAPRSLAYTLSQLEGDEIAQLMAEVELRFPSTPLLWLKDLAAFLNKRLEHTPESPNLAEHPTGFPLSGVSAGVRAQLRAAMSNKALHGLFWEHCLSNLLTDFAKGTSWVFQLVELRSKNQQKQPQCLLVLWAACQAGLSDLSKGLAVWMDLLLPVAGVRPYAALVVDYLSNLLERHPSKVAGLGDQGVRQLFTILDLAFGGSLPVSPKQQETLLALYYKFKELSYAGRREKVLHKYFPSYLRRLGGNKRHSSLDAELLSSLVECLSQDEQTYRVWRSTHYQLQLVPSRLLIQHLEHQWQLMPRRSQALLRETLASFALPNPSAKPSAEADETCRQSQILLKKMSGRGFPWFLVLVTLAAAVGALVVWDVQGSFQRSRTRQLLKDAGLLSHLEPAIAKGAVYWQDGLSWVGTHTPRLYKQACEQFGPTLDAVWVQALASAAWAWDRAAPARDWLCKQGHPLLQWGDEWVPFCAATVLRAAHEAWATVGVGVSWLLTNLVTGAQLTSAWLTQNVLTGAWSPEKLQGHASDLAATFQGYAVEAYRWLHDQVAQSPVAK | Function: Critical mediator, in cooperation with CASP4, of endoplasmic reticulum-stress induced apoptosis. Required or the activation of CASP4 following endoplasmic reticulum stress.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 603
Sequence Mass (Da): 67266
Location Topology: Multi-pass membrane protein
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E6N9D1 | MITVLRLGHRAQRDKRLSTHVALVARAFGADNLFYTGDYDQTLEDSVNKVVEKWGGAFKIEYTSSWKTLVKTWSGKIVHLTMYGLPLKTVIEEIRAIMRQFDLLVIVGGEKVEGEVFQVADYNVAVTSQPHSEAAALAVFLDWVFQGSEMDRVYPDAAISVIPSTKGKVVVKRRDLLETDFGVDGLTR | Function: Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
Catalytic Activity: cytidine(56) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(56) in tRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.206
Subcellular Location: Cytoplasm
Sequence Length: 188
Sequence Mass (Da): 21036
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A0A062XLA0 | MGQPVKPVKVAPSLLAADFTRLGEEVQEVERAGADLLHFDVMDGVFVPNLSFGPVVCQAVRRVSALPLDVHLMVTKPEVLIEPFAKAGAHRLSVHVEAVTHLHRVLAQIREAGMVPGVALNPLTPLASLDEVWPFVGFILLMTVNPGFGGQSLIPETVGKLGRLARIREQVAPHVELVVDGGVTVDNAPALRQAGADVLVAGTAVFAEADRQRAISLLKGGS | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Carbohydrate degradation.
Function: Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
EC: 5.1.3.1
Catalytic Activity: D-ribulose 5-phosphate = D-xylulose 5-phosphate
Sequence Length: 222
Sequence Mass (Da): 23511
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A0A834VEJ4 | MDSAKSISARSNSNPLTNGRSSLSLSSSSPTSSSLSYPMEISEESEYFETKQKDWSIKASPKALATINPIRRIVETMNLQPNKEKSFIPLSIGNNLASDPTLCENFRPCNEIIESLLETIKSSKFHGYQPASGKEESRHAVAEYCQAYGMNVNFKDIILTSGCSHALDMAMSVLAVPGCNMLVPRPGFPLYKTLSAQLEIEIRYYDLMPEQNWQIDLEDLESKIDLNTSAIIYNNPSNPCGSVFPDHHIRKFLEIAERYCLPIIADEIYENIVFSGHKFHAIASLTEEVPILHCSGTTKKFLIPGWRLGWIAINDQKDRFGQEIRTALNSLSQRIIGPNALIQGALINILTKTPERFFNETIECLQRNAHLAYNHLKMIKGLTPIRPAGAFYLMVRIEMEFFPMFHNDLHLVETLVAEESVFCLPGACFEYPGYVRLVLSLETETLQEALNRIENFCRKYFTHVDETVYDLHPHHNDHHKHTHHHHHSHHSSDHHQRRHNHSSNHHRNVHTHDRHHKHHGQRQHHNE | Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 2/6.
Function: Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate.
EC: 2.6.1.5
Catalytic Activity: 2-oxoglutarate + L-tyrosine = 3-(4-hydroxyphenyl)pyruvate + L-glutamate
Sequence Length: 527
Sequence Mass (Da): 60329
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A0A1B6C0I7 | MESQNNKQRPKSLSDASTDSSQSHIPSKKSSIGQQVTILQELSKTDPNHSYYKESLNYVEKLKISDSAPNIKFNSYRNNYTRKKQPHKYLNCKKVAVSRSGTKTSTSHDSTRATVITAVLKDLQEDVIMSRFSQPPVKSDEEPIQDFKITGRDNVYVQNRSGFVVTPRERALTQNTTMRSTHQDWMEDLTDTTRETPLDVAIQVQSMFTPISGICFGLLGGIAVFQLILAFSLSMGMDGSEGLVFLESYSKIARIAPIAFYILLAFCIVSVFDRFDLAHLDMNHCIELLAYRQSWAIAIIYILVLLSTLMCAYYDDLLILYPHDKSFTLNKYQLSQSLYEWQLWNTCRTILAVVGWVVFSLTMPDDLLLHHLQNIKQYERPDKPVFIVQSSNAS | Function: Component of the transition zone in primary cilia. Required for ciliogenesis.
Subcellular Location: Cell projection
Sequence Length: 394
Sequence Mass (Da): 44888
Location Topology: Multi-pass membrane protein
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A0A2E8ZQV0 | MKMSIRSTLLMLLFLVLVLAILINSVLGHMLVRQEVNEVFDAELAVTTKLIKGLLEDDDLMEDLPRIVEALNQSLDHKQPAQRELELYENTRLIQIWRNDGRELLFRSPGAPDHALAPMKAGFYHHKSDKREWMVYVIDLHTKNASGENGPAKDAWLMVGEYPHARQDIIYALGGIFGVSGIVALILCTLIALAVIEYGLGPIRQLGSRLRRRSVDNLQPIQLHRTPKELQPVVDGLNEMFSRLAGGLERERRFVDDAAHELRTPLAVLKLQSQRLQTLPPEQLNEALKELETGTERTSRLLEQLLILARMDNNQQINSSRIDLAEPVRRTLAAMQWQADVHRVELTLDAADNLPAVNMDPSLLEMAVRNLVDNAIRYGGDGHEVETRLCQEGTALYLSVRDHGPGVPADDLQRLTERFFRAGNRYESIGSGDTAEQYQDSGAGLGLSIVSRIMETCGGELLLENAQGGGLRVTLVMPLPQDLQWP | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 486
Sequence Mass (Da): 54405
Location Topology: Multi-pass membrane protein
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B7QN70 | METIHVVSGALRDLLSMRDPRTKDWETLKNPSYVILLIGSYLYMAKIWGPEFMKNRKPYDLRTVIRAYNVFQVTANAYCLYRITYHTFWMVGYSPICQGVSYGTDDNSMALLDVFFFYFLVRIADFLDTVFFVLHKKFSSHVTVLHVTHHTLVVINGWVFLQFGSDGQPVFGLCLNQFVHIIMYSYYFMASLGPSVRQYLWWKKYLTAVQITQFVIMISHGMIPLFVDCGYPPVLLCIAVPQVAFVLVLFINFYIKAYVKRSPGGRAKECSKEPNCRQLTMNGVRNSLLVEKKQI | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 295
Sequence Mass (Da): 34197
Location Topology: Multi-pass membrane protein
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A0A174Q7E8 | MNEHYPFKLTPLPYPCDALEPYIDKLTVEVHHDRHQAGYVKKLNEALADCPDYHCWSLEQLICGCAQLPPNIRRDVYRNACGVWTHELYFDCMTPNQTAPHPCGRLAQAIDKCFCSFDRFRDVFTQTAAARFGSGWAWLACAPDGGLRVFSTPNQDTPLTRGLRPILCVDVWEHAYYLKYMNLRADYLDAWWHIVDWQFAEENYIFETGGKKC | Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
EC: 1.15.1.1
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Length: 213
Sequence Mass (Da): 24705
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A0A3Q7NJZ0 | FLQRHHFHSFSCSEAFVLVAVAYDRCVAICRPLRYPVLMTSRTSAALAACAWLPALLLPIPAVVQTSHLAFDNTAPISHCFCDHLAGVQASCSDTTPQTFMGLCIAMVVSFLPLLLVLLSYAHILAAVLRISSREGRSKAFSTCGSHLLVVGTYYSSIATAYVAYRADLPLDFHIMGNVVYAVLTPVLNPLIYMPRSKDVKAAITKIVAYYKTVLFLDFENSISS | Function: Putative odorant or sperm cell receptor.
Subcellular Location: Cell membrane
Sequence Length: 225
Sequence Mass (Da): 24612
Location Topology: Multi-pass membrane protein
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A0A0U0QRD8 | MTGKLDSFAPEAKVIHADIDPAEIGKNRHADVPIVGDVKAVITELIAMLRHHHIPGTIEMADWWAYLNGVRKTYPLSYGPQSDGSLSPEYVIEKLGEIAGPDAVFVAGVGQHQMWAAQFIRYEKPRSWLNSGGLGTMGFAIPAAMGAKIALPGTEVWAIDGDGCFQMTNQELATCAVEGIPVKVALINNGNLGMVRQWQSLFYAERYSQTDLATHSHRIPDFVKLAEALGCVGLRCEREEDVVDVINQARAINDCPVVIDFIVGADAQVWPMVAAGTSNDEIQAARGIRPLFDDITEGHA | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Length: 300
Sequence Mass (Da): 32561
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A0A6N8I4G8 | MIKSLFAIILTAILTENYILDKFLGICPFLGVSKNRSSATGMSIAVTVVMVIATAVTWPIYYGILVPKDLAYLETIVFILVIAVLVQLIEIILRKYIPSLYNALGVYLPLITTNCAVLGVTMLVLDKHTADPSAYGYLQALVNAFGAGIGFLVALVMFSGVRERMELNDVPKFMKGLPITLVAASLVSLSFLGFSGLVNGMLG | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell membrane
Sequence Length: 203
Sequence Mass (Da): 21855
Location Topology: Multi-pass membrane protein
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A0A2K1LAN4 | MAGWDEGNVFYSDQQLEDNDVNVADAATRHTAQRKFKEFIRSFGDVKGPFPYRESLLQNPNVLQVALEDLHNFDDELSERLRTMPADYLPLFEQAAAEVLVGLKSKVAGEDGELEEPNTGDVQVLLTSKEKAASIRGLAANSISRLVKITGIIIAASRTKAKATSVTLICKNCKNVKSVACRPGLGGAVMPRSCDHVTQPGEEPCPLDPFVVVPDKSKYVDQQTLKLQENPEDVPTGELPRNLLLAVDRNMVQKTVPGTRVTVVGIYSIFQAGGSGPEQKGAIAIRQPYLRVVGLEQAIDAHKAGGSMNNTDEDMDFKEFARRPDAYQKVCGLIAPSIFGHDDVKKAVACLLFGGARKRLPDGVRLRGDINVLLLGDPSTAKSQFLKFVEKTAPIAVYTSGKGSSAAGLTASVIRDSSTREFYLEGGAMVLADGGVVCIDEFDKMRPEDRVAIHEAMEQQTISIAKAGITTVLNSRTSVLAAANPPSGRYDDLKTAQENIDLQTTILSRFDLIFIVKDARDYARDMQIARHIVNVHATADSIVRGTEVQDKENWLRRYIEYSKSQCSPRLSDSAAQLLQSNYVKIRQQMRQQNDENGGSPIPITVRQLEAIIRISESLARMQLSAVATEEHVTEALRLFHVSTLDAARSGITANLVVTPEMRAEIQQVELQVKRRMGIGSFLSERRLIDEIMRTGLGESTIRRALIVMAQRDEIEYRRERRVIVRKA | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 727
Sequence Mass (Da): 80158
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A0A2K1K4B3 | MAKWWVVWGGGTLGICVRFLLVVMGSLSLLDRRVEVVSPVTSLSRLAEGYWLKEYGKSPYAGSAYHGSPLLLSLIGPVIGDRQDTSIGYLLCSCSLFVVADLMSALLLRSTGKLLEHGHSKHLQLLGLTNLLREKTDRKDKLGIGDISFLVYLFNPFTIAVCVGGSTSSIENMLIILSLYGAAAGKVPLAGFGWAMATHLSMYPVFLIIPIYYLLTNGLDSPPNKLFELAKSVEPAAKEDSCHGKDANDSYLQSSKSSSKGLQTTPMLSSRRKWVVISKLVFWSAISWVCILRLCKVALLGRSSLITMWLETHKYMLTVDDLTPNLGLFWYFFTEVFDFFRNFFLMVFHANIAFMVPPLTIRLRHRPIFLAFILTAICSMIKSYPTVGDAALYIGLMALCVHELSELKYFYLLLNGYILISVLGPVMYNLWIFRGTGNANFYFATNLVYATLQTVLIVESVSTVIGYDKHLLKEIKLHSSNKSSQLHPKSMEVSA | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Component of the GPI transamidase complex. May be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 495
Sequence Mass (Da): 55161
Location Topology: Multi-pass membrane protein
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B7PGF2 | MATALVRLLPRITVIALCLLFGYGLLYRPLSFGSLAGRPRPDMSWLLAQQDIRQLISNGSLLLSPKDPCPSFLAVVICSAVNNFVARRAIRDTWGQDARSPLVRAFFLLGRTDNETLQEDVVRESRLFGDVIQADFMDTYNNLTVKSVVLLKWTGQQCPQTRYILKTDDDMYVNVPNLVSYLNKKGGRKMLLGCLISGATPIRDWTSKWYVPPFVYPHHTYPDYLSGTGYVMSGDVLGQLFRTALETPFFYMEDIFVTGMVAQKVGIKPVNYDAFKFYKRKNNPCVFRKLITAHIMTPSELRSMWSRVRDRRIKCS | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 316
Sequence Mass (Da): 36049
Location Topology: Single-pass type II membrane protein
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A0A3Q2GYA2 | MKGRRRRRREYCKFALLLVLYTLVLLLVPSVLDGGRDGDKDAGHCRGLQRSLGVWSLEAAAAGEREQGAEARAAAEGGAGQSPRSPGNLSGAVGEAVSREKQHIYVHATWRTGSSFLGELFNQHPDVFYLYEPMWHLWQALYPGDAESLQGALRDMLRSLFRCDFSVLRLYAPPGDPAARASDAANLTTAALFRWRTNKVICSPPLCPGAPRARAEVGLVEDAACERSCPPVALRALEAECRKYPVVVIKDVRLLDLGVLVPLLRDPGLNLKVVQLFRDPRAVHNSRLKSRQGLLRESIQVLRTRQRGDRFHRVLLAHGVGARPGGPSRALPAAPRADFFLTGALEVICEAWLRDLLFARGAPAWLRRRYLRLRYEDLVRQPRTQLRRLLRFAGLRALAALDAFALNMTRGAAYGADRPFHLSARDAREAVHAWRERLSREQVRQVEAACAPAMRLLSYPRSGEEGDAEPPVDEETPLEMEADGAT | EC: 2.8.2.-
Subcellular Location: Membrane
Sequence Length: 486
Sequence Mass (Da): 54019
Location Topology: Single-pass type II membrane protein
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A0A8G0VAN4 | DYATKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYNIEPVAGEENQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALHLEDLRIPPAYAKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 164
Sequence Mass (Da): 18023
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A0A2K1K3J8 | MGQWWLLGVYLSLCPLLLTVLLCGDRPIFKGTFVERTHDFLTGGACDCCVRLVGVCFGQRGKNACAAAETYCCDKPNPALQLFYLSILGGCYFTLTWTSLQYIPGLYISFYHRYTGPVAACFGLCLFLLTSFTDSGTIDKSTVQSHLGVYPFDGVLYEEKTCSTCKIIRPARSKHCSICNKCVARFDHHCAWMNNCIGEGNLRYFLSFLGWHVLLCWYGAWVLVMILAGHVEERNVIRAIRWYIGRPATFHDIYPHVFQWLLAYYSTQVMLVIFLLVISLLLMGFFGYHLSLVAYNTTTNETYKWDRLKRYAEVEATKQASEAKDIPSAEQRQQSQGKCGWLRCMSCWGSAPKLEERNIYDRGIWKNVFEVLNPQGFKRSVRRVVKKKQ | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 389
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 44557
Location Topology: Multi-pass membrane protein
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A0A8T2RYZ8 | MTNAIDISATAVGILGNIAAVLLFLSPMPTFYEIWRKKSSGDFSGVPYVASLANCLVWVLYGSPLLTHGLLPVITINGFGVVLQSFYLLIFVPFSKGKKRIQMLAYVLTVLACFGLIIVVTIFVLPEGRKAFFVGTLAAVLNTAMYAAPLSIMRHVIVTKSVAAMPFLLSLCTFFNSCFWAVYGFLKKDTFIIIPNILGVILAAAQLVLYAYYHNYEKKHPTKDVSNGNLPNVKRLETVQQV | Function: Mediates both low-affinity uptake and efflux of sugar across the membrane.
Subcellular Location: Membrane
Sequence Length: 242
Sequence Mass (Da): 26609
Location Topology: Multi-pass membrane protein
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A0A653H2M7 | MFKTFIVNKFVTNKSVRVGWNNYKTYSKINNKPLFASSFSHLSFFKCNNDNNNKLKKIYIILFNKYSRTNNNISNNINEQKFIKVYKKYLLLRKKNIKIKNIKIKNIKLINSNKRIINIFDKKKKIAKNNLSNFEQNLHTSVKKWSNIELIKIIKRNGLLCIAPFIYGNSNINTVIDIVNCNSSGGSSGGSGGSGGSGGSSSGSSSSSSSSGNGSSSSSSGNGSNQYIGEDILTINKNINMNSIKSLSEVIKTKLVQEKANYPTKFNFKQEYINILSYVNILDYIKKSVGFKKIGIQLSTPKKINVTKKISLPNERKFSNYISLIKYNIHQYLELSKFKLTLWVTISSTFGYFMLGGTSNYIEFFSLLVGVFFCSCSANSFNQIIERNIDKLMLRTKNRPLACGNKLSVRHAKTFAFISAIVGCLLLYNFNNILTASLGLLNIFLYVSVYTPLKLKTYYNTHIGAVVGSIPTLMGCTAVEETLFSVEPWMLFVTQILWQFPHFYSLAHLYKEDYSKGNYKMFPLLDKQNGLYTAKLCRKYVIALSLLPFIFFHLDYTSYMYILTSILPNIFIYYTLQQIFKKPCKKNMRIFFKHSLWHIMLLLALTTYHTQIPKYENYKSKKETENIGETENIGEIKEIGEIKETEEMEETEEMEENVGKKVDNTHSNHAITKFKKIFLKYCIVFC | Function: Converts protoheme IX and farnesyl diphosphate to heme O.
Subcellular Location: Membrane
Sequence Length: 686
Sequence Mass (Da): 78633
Location Topology: Multi-pass membrane protein
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E6N946 | MVERNRIGLGTWIDKLAWEIIEREKQLGRSLENIRTEAGIAASGFIHIGSLSDSVRAYAVSLAIKNLGYGSEMIQFADDMDGLRSVPAEIPKEYEKHLLKPVSLIPDPFNCHESYAEHMETMLLDTLAKTGVESKFYRGFHVYGSGLLKNQISKILENAKTIGEKILELTGQQKFVETLPYFPLCASCGRIYTTHAESFDHKTGRVHYVCKGVSIKKRWFEGCGYEGEADISKADGKLSWKVEWAARWAALDVRFEAYGKDLAASVMVNDWVSENILGYKPPKHVQYELFLDESRRKISKSKGVSVFTPHEWFKYGSPQSLVLLFLKRIKGTRVVSPQLIPALMDELDALGEQHRRNTGDPRRTGLYVYAYMLKPPEKPPTKISYSLLVFLASIAPEDRETDFVVSRLKRYGYKVDEEVLRKVEYAVNYQKVFGRPEVKPVVVDDNMRRAVDEVAEAVRNASNPDTLQSTIFEIARRYMINPPQLFQTLYRILIGQDSGPKLAPFIIEDYGVERAYEALKRVSQGLYTAKTEYGHQKSEERI | Catalytic Activity: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys)
EC: 6.1.1.6
Subcellular Location: Cytoplasm
Sequence Length: 542
Sequence Mass (Da): 61735
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H2MT62 | MAHFETYQEYHRIEDFEEDSPAGEEDLLVHVPESLKDSWHHIKNLDNFFTRIYHFHQKNGFACMMLSEFFELIQFLFVVTFTTFLVNCVEYDILFANRAVNHTGPGHSPLDRNKVTLPDAILPSQQCTQRIQDDSWIIFLLIMAAIFWVYRLVKVFCNLLSYWEIRQFYIKALKIRMDELCNFTWQEVQGRIISLQKEQQMCIHKKELTELDIYHRILRFKNYMVAMINKSVLPVHLQLPLLGNVVFLTQGLKYNFELILFWGPGSLFQNKWNLHPKYKRSGNRLELAQQLSRVILLMGLANLLLCPFILVWQVLYAFFSYTEVIRREPGSLGARRWSLYGRLYLRHFNELNHELHGRLGRGYKPTSKYMNSFTSPLLTVIAKNVAFFSGSVLAVLIALTVYDEDVLTVQHILTAITVLGVVITITRSFIPDEHLVWCPEQLLQCVLAHIHYMPDHWRGNAHTSETRDEVAQLFQYKAVFILEELLSPIVTPFILIFLLRNKSLEIIDFFRNFTVEVVGVGDICSFAQMDIRRHGNPAWMSEGQTEASMYQQAENGKTELSLMHFTIKNPRWQPPQESSVFISHLKEKVQHDAQGGPSTQLLLSEAPLCTSLQSNESGTGPDNLLASVLAHPILTASGLQARDHRFIRPSTAASAAASVLASLSTSQLPQGSRGRPHGLLPSSLHPEATMYHSDRTAVDSLSNSDSHIRSNALHSEFASAEMSLHAIYMHELHQQSSYPQRTSGHWQNPVPMRDLHTNTSFHAHGGHVSNLSTSSPAPLGGWAEVEEENLEDQEINLGSTPTHGTGSSC | Function: Phospholipid scramblase involved in autophagy. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion.
Subcellular Location: Membrane
Sequence Length: 809
Sequence Mass (Da): 92260
Location Topology: Multi-pass membrane protein
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A0A248LCU4 | MRNRVLQFALVFLVAGGIIWTLYQLDYLYFVLTISAVVVPLAVIMIIFIENRTAESTIAWFLVLIFLPILGVIIWMMFGRNPRRRRRNRRSHDERMLLKQATRPVRSLAVSELPANHLKLANTIRNFGGGGVDVHTASKILTNGTETFPAILEAIRSAKHHVHIQYYIYRNDETGKAIREALIERLEAGVEVRFMYDGLGSYMLGEGFLRPLRDAGAKIAAYDPISSPLFIFTANFRNHRKIVVIDGKVGFTGGLNVGDEYDGKNKKFGFWRDTHLRLEGRAVKELQATFLDDWIYAHLEGTDTWETFGGEDGLARYFPKHDAETDGAVQVVTSGPTSKDPAIRNALIAAIISAQRSIWIATPYLIPDNETMTLLRLAARAGLDVRILTPGRGDSFTSYYGTRSYFGPLLKDGVKIYTYNRHFIHAKIVLIDGKIGVVGTANMDIRSFVLNYEIMAFLYDTESASKLERDFIDDFEVSIQLSSNDYVKRSLRFRLFESFSRLISPLL | Function: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Catalytic Activity: 2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a cardiolipin + glycerol
EC: 2.7.8.-
Subcellular Location: Cell membrane
Sequence Length: 507
Sequence Mass (Da): 57425
Location Topology: Multi-pass membrane protein
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B7PM93 | MQVLRPSFVGNKKVISFNEPRCTPKVDSMPRSLSAADIDTALKQADKDPSLIGNFSKKCALPLVEGAAHDLKMITPSTLADLIQGKYQSVVDNYTVIDCRYPFEYLGGHVQGAVNVFEPQDLLGAFLDETCLSSSHTRHVLVFHCEFSSERAPKLARLLRHEDRQLHMDVYPELRHPEVYLLQGGYKAFYELFEDLCEPCGYVPMRHKDYEAHLCVYRGQAKSTAKRRKARHVRTALCTPSSQHKETLQ | Function: Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle.
EC: 3.1.3.48
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Length: 249
Sequence Mass (Da): 28239
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B7QEW2 | MLGLESVLTDPWFPEKDHRSEGWFLTGNLWPLASLVALYVYGVKVVGPRMMKHRKPFEIQRMVLLYNLFMVLNCAFFLEEFVRLAYVHNGYNLLLQEVDKSETPATMRLVSLSWWYYLFRIFEFTETVFFVLKKKNNQVSGLHVTHHCIIAWNMWICVTYGGQAQTLFVTCMNTFVHLLMYSYYFLSALGPRVQPFLWWKRYLTQIQLAQFIVLMLHNSLPLFFEGQFVREFSVILVFEGLVFFVWFMIFYFDTYRKKKSVMLFECHKLD | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 270
Sequence Mass (Da): 32352
Location Topology: Multi-pass membrane protein
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K7U1D4 | MPSPSSYHPHHRARLRSRAAPLLIVVVLAVVAVTELLRSRTGLPAPARRAGSATATASPSSLASTNQSVAQRKILLDPAFTPRLPRQSQLSLSLSARNALPPRNRDRFPTLPVGHLKVVLYVHNRPRYLRLVVDSLSRVEGIGEALLIVSHDGYFPEMDRIVQGIGFCQVKQVFAPYSPHLFPDAFPGASPGDCQSKDRAKEKGCQGDPDQYGNHRAPRIVSLKHHWWWMMNTVWDGMEETRDFDGHILFIEEDHYIFPNAYRNAQLLVDLKPKKCPQCYAINLAPSDVKSRGEGWESLVAEKMGNIGYAFNRTVWRKIHAKAKQFCAFDEYNWDITMWATVYPSFGAPVYSLRGSRRSAAHFGKCGLHQGQGSSNVCVDNGSGAVELEDADKVPNIKADWPVRVIQRQEGYQAGFKGWGGWGDRRDRELCLSFAYMYHVKDPSSS | 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: 446
Sequence Mass (Da): 49965
Location Topology: Single-pass type II membrane protein
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A0A0N4UDQ8 | MKRHRGIIKQVTRRYLFTKMSSSELRSSFLEYFISLNHTYVQPSSIVSHDDPSLPFTNAGMNQFRPIFLGAVEANSELGRLKRAVNSQGCIRVGGKHNDWEHVGRDLTHHTFFEMLGNWSFGDYFKEEACYFAWNFLTKILSVPPEKLYITYFAGNDKYALPPDYECRDIWKKIGVNPGRILPFGLKHNFWEIAECGPCGPSSEIHIDVQGSNDASASVNINGSSVVELWNLVFLQFNKEPSGLLKPLPRQHIDCGLGFERMTAVMQNVITSYDTDIFIPLLEEVSKYSNVGLYEGRVGEHDLNNKDSAYRIIADHLRTSCILISDGVRASVKGQGNVLRRLLRRAARASYLFLKADQGHLSNIVPFFIYHLKNSYPDMLKNDEVIEKVVKEEEEQFWKLRKEGEKRFHSVISQLPENSLILPGSIAWNLHNEGVNIEMASLLAEEKGLIVDMVGFEKEKALAQALSKSSFERRRTVVSDCSNQLTNQEIPVTNDLFKYNYSRSNSGEYSFAEIGGKILAIFDMNRRICNSLSVSKEGYIVVDVTNFFAEQGGQLSDTGILFDKNRQPVFSVKDVQRHKNYVFLIGTTLHSDLTVNMEIYQRINEGRRLSLMRNHTATHLLRYAIQKVCGTGVQQCGSLISAENLRFDCSLNRDLTPDEIAEIDLLINDIISSSQTIADRNVSIENIEFSQNDFPQKFDWNDLGANRTVRIIQIGDISIGSKFEIKEYCCGTHVLSTSDIQAFTIYAGETVGRGKRRLYAWTGTLAESALYIGTTMRSKISLLSSNMKVEDAKNFMKDYIGIKHKLPLWMKREMKESVRQIKKDIKKREKKLI | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
EC: 6.1.1.7
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Sequence Length: 833
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Sequence Mass (Da): 94860
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B7QHW5 | MNVCFPSFCICLVTAGRVVFELFANVCPITCENFRSLCTGECGIGKTTGKPLHYKGVKFHRVIKSFMIQGGDFSVGNGSGGESIYGGTFKDECFDMKHDRPYLLSMANRGKDTNGSQFFITTQQTPHLDGVHVVFGQVIKGEEVVREVENQPTDDNSCPLQPVVIANCGELVLKRKQK | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 178
Sequence Mass (Da): 19591
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A0A090LF27 | MLTLNVNIIIRDENGICENSSKTFQISPEEEINSLVKQISTEEGKNVKLLFAGKLLNKHKRLIDYHLASSTKITAIVTNDVEDFEIISKESCNIEKSSQSLVKLFFAYCKKCDIVRMVSDPSNWNDLKKRFELYCFTCNDQKEANFYFKCQYCTNEAVGLKDYILNTKDKLCVICENNTNEVISLSCNDVICNFCFWAYIEDISERFGFVYRKEYGFTIACPIQGCNGCIEDVHMFYMLGNDVYKKYQKIATERFIAMQENTVFCPYPDCGDAFTAEEKEFIIQEGEEYGVPATIKCPSCNRTFCMSCSEIIGCVCFDNKYQDKKSRDVIEKICKKCPHCGAKTEKNEGCNALKCLICSTKWCWICETFFTEECRENHWFI | Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.
EC: 2.3.2.31
Subcellular Location: Cytoplasm
Sequence Length: 381
Sequence Mass (Da): 44037
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A0A357AT51 | MQWRKITIETTTQAEEIVESVLCDFGITGTEIEDNLPFTKEELEKMYVDVPEVGEDDGTAKVSCYIDMETDADKLIDELSKKLAEYAGAVDLGSLRFTKSVTEDKDWMNSWKENFKPIRVADDIVIKPTWEAGLELKNTDTIIEIDPGSAFGTGTHETTKLCVTAIKKYLKKDDAVIDVGTGSGILSILAMKLGAKCAVGTDIDANAVSTAKTNTVLNKITKNVVYLEGDVIGDEKIRKEVGYQMYDIVVANILADVVIPLTDVLKDMIKPGGTFITSGIIKERAGEVESALAKNNLKVVDKLELGDWVCFVAKA | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 315
Sequence Mass (Da): 34471
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A0A4P6LWD2 | MKESHRDKIVVIGAGNVGEAIAYTLMVRVQANDIVLVDLNEDRAEGAALDIAHGTSFFKQVWVRKGGYEECADAKIIIITAGIARKPGQTRLDLAKTNVSIVKSITQNIMKYAENPLILVVSNPADVTTAAVYKESGLPSGRVIGSGTSLDTARFRHILSEKLHVNVEDINAYILGEHGDSQVPIFSSANIGGFPLYDYAQQVGITLDEEEIARRTKDGGAEVIKLKGATFYGIAMAVSNIVETIMKDDDAILPVAHVLDESFDKWSGVAVSLPCRIGWEGIEQTLRIPMNEKEKTDMDKSVGILREFTEQVIG | Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Function: Catalyzes the conversion of lactate to pyruvate.
Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
EC: 1.1.1.27
Subcellular Location: Cytoplasm
Sequence Length: 314
Sequence Mass (Da): 34172
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A0A8T0CR98 | MYLLSVELMTMVKSFAAKTRNWLERRPSRKNALLILVLVGTCMVIGDGILTPAISVLSAAGGIKVNHPDVSGKVVVVVAVVVLVGLFSMQHYGTDRVSWLFAPIVLLWFLLIGGIGIYNIWKYDTGVLRAFSPVYVYRYLKRGGKDSWTSLGGVMLCITGTEALFADLGHFPVLAVQIAFTVVVFPSLLLAYSGQAAYLMKNKDHVFDAFYRSIPDSIYWPVFIIATLAAIIASQATISATSSIIKQALALGCFPRVKVIHTSKNFLGQIYIPDINWILMILCIAVTAGFENQSQIGNAYGTAVVIVMLATTALMVLIMILVWHCHWLLVLLFTGLSLIVECTYFSAVLFKIDQGGWVPLVIAAAFLLIMYVWHYGTVKRYEFEMHSRVSMAWILGLGPSLGLVRVPGIGLVYTELASGVPRIFSHFITNLPAMHSVVVFVCVKYLPVYMVPEEERFLVKRIGPKNFHMFRCVARYGYKDLHKKDDDFERKLFDSIFLFVRLESMMEGCSDSDEYSIYGQQTEKSRDALLSKYAKTAISDVDLTISSMDSIVPGKSPSSRPNSLTMSSGQEGNRTETDELEFLNRCRDAGVVHILGNTVVRASRESRFYKKITVDYLYAFLRKICRENSAIFNVPHESLLNVGQIFYV | Function: Potassium transporter.
Subcellular Location: Cell membrane
Sequence Length: 648
Sequence Mass (Da): 72411
Location Topology: Multi-pass membrane protein
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A0A352CPB1 | MIRGILAILFVLIFLTVSLILIPIAYLIGLFDRHARDVYAQSLVAWGFRVIGVIVGAKVTEKGREKLPRGEAALYVANHRSIFDIVLLDARMPAPTAIVAKKEIKKYLVLSWWMILKNCKFLDRDDIKQNLKIILECIDDAKKGQTILIYPEGTRSKAESELDMGPFKEGSMKIALKSGVKVVPVAIHGTRELFEKHLPFIRPGKVTITYGDPIDPGTLDKEQQKHLGEICRERILEMLKEENK | EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 244
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da): 27589
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A0A352WFR6 | MARFSSDKIEEVRERTDILDVIGQYVHLERRGNTYFGLCPFHSEKTPSFSVTPSKGMYYCFGCHKGGNVFTFLEEKENMTFPEAVEELANRAGIDLPKVEMSQEERKRQDRRSRLMDIHKDAATYFYKTMRSDEGERARRYFLDRGLSPETMQKFGLGYSGAKSDSLYQYLKSKGYSDDLMKASGLVTYKEDRGPHDRFWNRAMFPIMDPRRHVIAFGGRVMGTPGEHTPKYLNSPETEIFNKRKTLYGMHIARGTRRKEFILCEGYMDVISMHQAGFDNTVASLGTALTAENVEVLKNYRKPVLLSYDSDHAGIDATLKAIRLFKGAGIPCRVINMKPYKDPDEFMKALGAEEYEKRIASAENSFLFEIRMMMREYDLTDPQQKTAFQVAMADRVIQNFPIEMERNNYIDVLCRNYQMPLDSFKRLVADEARNGVRPELPAKEGGPSPLPTQRRAERLKSADEGMQESERLLLSWMAEYPMILEQVKPFLGPYDFTEGVHLDLAEAIYRGDTSQESYSPAALISSYELEEDQAEVARIFHTGENILEKPEDWTKALQETVFRLKQRAITEEQKRMDPRDPDRLKRTIEGRKLLDQLRRTDFRGPQ | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 606
Domain: Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
Sequence Mass (Da): 70056
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A0A2K1J7A3 | MTLRLECAVQHYDWGRIGAASEVGRLHALAVGSPAEDTPYAELWMGTHKSGPSWVVSDNSPVLLKEWLDTHSEALGDKVAERWQGELPFLFKVLSVAKALSIQAHPDKKLAQALHESQPHIYKDPNHKPEMALALTPFEALCGFVTSEELKEAVETVPELRSVLKEDTCKALIMLGTCKVERNEAKQALKQAYTTLMTLPNDVVASTVTELVNRLAKEKQVRELTAKEDLVIELEKQYPADIGVLSVFFLNYLQLVPGEAVCLDANEPHAYLSGEIVECMAASDNVVRAGFTPKYRDTQTLCSMLTYKQGLPEVLTGTHVNDYTTRYTPPFDEFEVDHIVVPLGSSSELTTMGPSIFLVFEGIGVIGNNDAEDITGLKKGVIFFVPADQKIVIAAPLDADHSYDDLKRKPLQLYRAGVNSSRMWPTA | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2.
EC: 5.3.1.8
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Length: 427
Sequence Mass (Da): 47181
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B0NJI3 | MDNQNNKNKNNKNNKQGLSFIILVTLITTILVLALYQFQGMTGDKEVSYDEFLKMVEKGKVEKVVIQNDKIVITQKKAKGDNRPAKQYYTGVVKDDTLSDKLYEAGVKYEQEIPDTTSAVVAQIIFTFLPIALLVGMIVWMTRRMSKGGGMMGVGKSNAKMYVEKQTGVTFKDVAGQDEAKESLQEVVDFLHNPGKYTSVGAKLPKGALLVGPPGTGKTLLAKAVAGEAKVPFFSLSGSAFVEMYVGVGASRVRDLFKQAQQMAPCIIFIDEIDAIGKSRDNQLGSNDEREQTLNQLLAEMDGFESNKGLVLLAATNRPEILDPALLRPGRFDRRIIVEKPDLKGRVDVLKVHSKDVRMDETVDLEAIALATSGAVGSDLANMINEAAINAVKNGRKAVSQADLFEAVEVVLVGKEKKDRIMSQEERRIVSYHEVGHALVSALQKDAEPVQKITIVPRTMGALGYVMQTPEEEKFLNTKKELQAMLVGMLAGRAAEEIVFDTVTTGAANDIEKATNVARAMITQYGMSEKFGLIGLESIQNRYLDGRPVSNCGQETASEIDQEVMKMLKDAYEEAKRLLSQHRGSLDKIAAFLIEKETITGKEFMNIFHEVEGIDPESAKKSEERIAMNPVDESSPALAADGEAQEEE | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
EC: 3.4.24.-
Subcellular Location: Cell membrane
Sequence Length: 648
Sequence Mass (Da): 71155
Location Topology: Multi-pass membrane protein
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B7P5N2 | MLMSRVSEQGPISSCRSSCRLPLRVAFAGKLKSEPQAILELMAANGALLTSPQDIEKECGEYYALLYAERPVESALWDGLFDPLPRLHEGLAEGLDGPVTRKENWEAMSTLFKGKAPGPDASLFHTRASAQQNLLALRDMSYWVGNRKIPMLVLSVDQERHSTVSHKFLFHVLSRVGLGGSFLSGVKRLYAAATSMVKVNGGVTQAFPIAAAFRREARRPLINKFRSLGASEWFLDLATRVLDIPERWIQRRVSVDDRAHRLPEGSLVRRFSLKRPLDVGPAWTHWGFGGDAAKLDVDFRVVCAQGFTGANCSDECPAPDAIGARFRCLANGSKECLEGWTEPECDVPACADGCHPEHGFCERPGECLCKMGWEGARCERCTPMPGCLHGTCNASFECNCLPGWDGFFCNRQLKFCEDHSPCSEGSTCVNKAEEDGFYQCLCPEKLAGRNCTVPVRRN | Function: Putative Notch ligand involved in the mediation of Notch signaling.
Subcellular Location: Membrane
Sequence Length: 458
Sequence Mass (Da): 50558
Location Topology: Single-pass type I membrane protein
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A0A6P6G8V6 | MQLAGEKKEGNSWHRFGRLRVCFRGAEMVVSGSPNGSQPTSQPAKKYGITKPISVAGPTEADLQRNIELEKFLIDSGLYESKEEAARREEVLGRIDQVVKGWVKLLTRQRGYTDQMVEDANAVIITFGSYRLGVHGPGADIDTLCVGPSYVNREEDFFIVLHNILSEMEEVTELQPVPDAHVPVMKFKFQGISIDLLYASISLLVVPEDLDIANGSVLYDVDEQTVRSLNGCRVADQILKLVPNVEHFRTTLRCLKFWAKRRGVYSNVTGFLGGVNWALLVARVCQLYPSAIPSMLVSRFFRVYTQWRWPNPVMLCSIEENELGFPVWDPRRNPRDRFHHMPIITPAYPCMNSSYNVSISTLRVMMEQFNHANRITEDIELNKAQWSCLFEPYRFFEAYKNYLQVDIIAADAVDLLTWKGWVESRLRQLTLKIERDTNGMLQCHPYPHEYADTSKPCPNFAFFLGLQRKEGVRGQEGQQFDIRGTVDEFRQEINMYMFWKPGMDIYVSHVRRKQLPAFVFPDGHKRSRMLRHVSLDAEKSCEEASGFQSGSAEKNAKRKADSETMDLKSTRPEKQAFISPQPPESASPESCASRSGITSHTSFNDRVIVESLTMVDRDSSSEMRSSGHLDSEKCTLANDVEMVNTMHESINLEEQASISEHSLPGVGNKNSREQIRLDLMGRICCSLTQ | Cofactor: Binds 2 magnesium ions. Also active with manganese.
Function: Polymerase that creates the 3'-poly(A) tail of mRNA's.
EC: 2.7.7.19
Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Subcellular Location: Nucleus
Sequence Length: 689
Sequence Mass (Da): 78354
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A0A6P6FKZ4 | MQTFNCCSNYDVVSSLYATIISARLINSISKEIYLVLLLSLSTHQKICLQYCRLREESEALCWRTRIYPPRKACQTRHQQQDLHLVGLDITDNKIQTMPWAATLEKVVQLQSLQQLCVVKDLSAHDVVMQLMQKENYLIGMLNKGVLAFPISKWVPGAGPTVKSGSKGKCRRLILTKTLEWTLNWCILQSMFDSGVGRFEKSTHSRWRCSGAISCLVG | Function: Phospholipid scramblase involved in autophagy. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion.
Subcellular Location: Membrane
Sequence Length: 218
Sequence Mass (Da): 24755
Location Topology: Multi-pass membrane protein
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A0A6P3YU04 | MAMIIMKFLLLSLFLNLQVILSENMPTTASQEAGYGYGGEIGGFLRIDLYKFACPEAEAIIFSWVNKAVMEDSRMAASLLRLHFHDCFVNGCDASVLLDDTESFVGEKTAAPNLNSLRGFEIIDAIKAELESVCPQTVSCADILAIAARDSVLLSGGPGWDVQMGRKDSFTASKAAANNNIPGPNSTVPILIAKFQNLGLDLRNMVALSGAHTMGKARCSTFSARLQDTSIHSPLDFIESLQQLCSGSDSGTTLAHLDLVTPATFDNQYYVNLISGEGLLPSDQALITGDDRTRELVQTYANDLFTFFEDFKNSMLKMGNIGVATGIDGEIRTNCRTIN | 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. These functions might be dependent on each isozyme/isoform in each plant tissue.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Subcellular Location: Secreted
Sequence Length: 339
Sequence Mass (Da): 36693
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A0A2E4ZCT0 | MLLLMTHRAALLILVLCATLFSAVPSYVAAQDSAPTEAPQEVTNATDDIAVKERLKSVTDEFKELGATALRLMPLLLIALIIVVLFWFAGGWLSRRSSWLQRLGLSELGALLGKRVIRLVVTLIGLIIALELLNATALFSAVLGVAGVFGIALGFAFRNIIENYLAGILLSARNPFRIGDLIQVGEFTGNVVRLTSRDTVLMTLDGNHLRIPNSVIITSSMTNFSLNPLRRFDFYVDITPDADLSEARQIARDVLRRMTGVLAEPAPQCLIQELGASTIVLRVLGWVDQGETDLLKARSEAIRLVKQAFDTAAIEMPEPTYRLRMGASLPETQTSRVPETRDEKAEQTDVSVDRSIDKQVSDDLAKSDEQNLLKK | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions.
Subcellular Location: Cell inner membrane
Sequence Length: 375
Sequence Mass (Da): 41196
Location Topology: Multi-pass membrane protein
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B7Q054 | MAFAGLKKQINKANQYVSEKIGGAEGTKFTEEYMEMERKIDLTNELVEELIVKTKEYLQPNPASRAKLMVSTKLRGTGKTHAYPQPEGVLGETMVKYGGDLGEESPFGQSLIEAGESLKQLADIKYALEDNVKQNFLEPLTQLQTKDLKDVLHHRKKLQGRRLDYDCKKRTQIRGAHATEDDIKLAEDKFEESFNLASMGMFNLLENDVEQISQLAALAEAFCEYHQQCAEVLQSLTERLLEQLTEAASRERQPYEPKKLCELNLPAAGASASPLPSPVRSPARGGPNGRGPCCRALYDFDPENEGELGFREGDLVTLVRRVDDNWFEGSHDGRTGLFPVNYVEVVVPLP | Function: Required presynaptically at the neuromuscular junction. Implicated in synaptic vesicle endocytosis.
Subcellular Location: Membrane
Sequence Length: 350
Sequence Mass (Da): 39165
Location Topology: Peripheral membrane protein
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A0A6P3ZDL9 | MRMEKFCVSDKEAKRNIYNKIGDDLEISAKVHSNSISSSTESLPACNSTMRMLHHDNHYRPPSSSSSLRGLGGGDLGPTCNRAPAGPDDIYDVVVVSNAGSHAAAVASAAVSGDAVVRPLQPFDISTTSPSTSSPTTAFKFSGGMAATLGFPFTNAQWKELERQAMIYKYMVASVPVPPDLLLPINTRNLSAPAASQYSLGSDFSLRLSNNNTDPEPGRCKRTDGKKWRCSRDVAPDQKYCERHMHRGRPRSRKHVEVHVNNNNKRTRHDHHHHHALPTTSSATMAVTNPTVNNNINGSHTQFIGPTSALPYHQSPVFLDKSTIKASTFDSSLSSEKVSTRNLDWMMKAEPAAMTASDPQWHQLMQTKMELSSKTTSYCDTSNSSVFNQHSEEVPFLNLNSYSNFNTGQDQHESDQCSLFLNPEVVSLENQTPAVHAVPVAPRSFIDAWSNSTIADKSCVSSSAKLSPSSLTLSMGGCNSINEEMSRTHQIGSGYNVNHSKTHVTSWLTPASWVAPQPGGPLAEVLRPSSLTGSTTSAVSNPSSPVNNGKGGDSSCSPVATTVSSPSGVLQKTLASLSDSSGSSSPTVVGCSSSNAKVEIALL | Function: Transcription activator.
Subcellular Location: Nucleus
Sequence Length: 603
Domain: The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively.
Sequence Mass (Da): 64649
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