ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
B5TQ41 | IFWLLTWVAEYFFKSKNNKQKHQFYECGFRALSELNIQINLNFSIVCVFLILYDVE | 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) + NA... |
A0A3B6I0I8 | MLRAAARLLIPRRLLSPAAATATPTVWNLRHFSLSTPQPRPAEAEIFTPAEAQRMVRLVGLEVLKRRLRNREDEVVTYQEFLDACVEAGAAPTHSRAEALAGAMDHSGTIVLFRGKVYLHPEKIVDLVRSAVPPVLEIENDTRREEFELLKKKKGEIDQQACKQVRRILWSGFWFVQATVGLCFRFTFWEFTWDVVAPITFFVAGAHLLSGYAYFLITSRKLSYRTYMERLFKIRRRELCTKHDFDMERYLEMERHMRCPLGGDYSQAATKAIFGEIERRMQDEVISHGEPLGALMESGLMPMEAEALVQKMDEMSLVLL... | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes a pore-forming and calcium-conducting subunit. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cel... |
A0A0Q3GYN7 | MASDSRVAMMWCVLVLVLQSAGGGDMPCRREEQPEGERRAQGRLPQAQLSAGGVHCSGRGRQGPLREPGPRRGPDPHGLPRLLRPRLRRVGPPNFPSLRGFEVIDEAKSILERACPGVVSCADTLAFAARDSAYFLSRSRINYAIPSGRFDGNVSLESEALEFLPPPSFNLSQLVASFEAKKLDADDLVVLSGAHTIGVSHCSSFTDRLPPNNTSDMNPRLATLLQGQCPANPNFTDDTVVQDVVTPKLMDSQYYRNVLKKDVLFRYDAALLESRRTARKVLQNAFVRGRWERGSLRRPWSRCPGSSSRPPPMARSGECA... | 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... |
A0A3Q9DD29 | VTFINRWLFSTNHKDIGTLYLIFGAWAGMIGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPALTQYQTPLFVWSVLITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVT | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A158PLD2 | MSTAKQRYDAVRPRERVEFGGYRFVIPSLNFQMPKFLCCNGIHEGIMSEHHDENSFDLNECVSEVEDTSMYIIFSMFSINQGTLEHLVFQGFVFRMLCDIMLLCLDMHGQFRGFLKDDSDEFEDDVAALGEPLGQEVYRTLKEKFGFNSFRHRQKTTITAILLGHDAFVLMPTGAGKSLCYQLPAVLSDGVTVVVSPLKSLIEDQRLKMRDLGIPCEALTSDLSLSDQTVIYNRLMCSPPDIKLLYITPEKISASGRLASVFGSLHRRNFLARFVIDEAHCVSQWGHDFRPDYTKLQSLRRDYAEPKVQIVALTATATPK... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 819
Sequence Mass (Da): 92455
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A0A2A6BKT1 | MEMENGDPSSGTIRFEIDNISMLTNVGRYSEAVEVEGVPWRLFAQKLVEPDNKVYVFVFLAYVKSDSNLWSFDVSAEFDLVCNTKKPTLKFQRTYNNEMFSRGFRMGYIKDGKLTVAVKFSLKNIMGIRRIARVDFSDKDEPHDDIALEIGGENYLSLHSPVFDAMFFGNFAEKKKKIVEIKDVDRQEFVELLKVIYPSQDKITDTNYKYFLSLADRFQIKLVIDKVEQHLISTTKLSIPEKLKLADDFRLVKLHDVCLDSFITVQDITKIKSTESYKSLSDKAKQLKNHSDNSKIVEFVFNSMVLLVQSVNAINMVAPI... | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 503
Sequence Mass (Da): 57385
Location Topology: Single-pass type II membrane protein
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A0A1C6FI01 | MKNRIDACFEKLKAENKKALVTFITAGDPDMDTTEKCVLEMYKNGSDIIEIGVPFSDPIAEGATIQKASLRSLSGGTNLDKIFDLVRKLRTQTDKPMLLMMYINTIFKFGTAKFFELCKETQIDGVIVPDMPFEEREELQGEAEKNGIYTIFLVAPTSHERVKMIAEKSKGFLYVVSSLGVTGMRSEITTDFNELLAPIRNNDHCPCCIGFGISNPEQAKKMSQYADGVIMGSAVVKIVEEHGKDAPEYVGKFIKSVREGMDN | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-s... |
A0A497G4E9 | MSLQKIRCFIAVDIDDPVIVDRIVSIQYRLSGTGVRMKLVEKNNLHITLRFLGEISRPLLEKVIDIIKTVSFNSFQIKLQNIGCFPTPSRPRVIWIGVTEGEEKLREIHNELESKLRKLGFPKEKERFVAHLTIARVKSFSQVSRLIQVLNELRDIEIGEFTVNCIRVKKSTLTPKGPIYSTLYEQKATK | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 190
Sequence Mass (Da): 21891
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Q9C0P5 | DFSSETIAGLQSLSQKHNFLIFEDRKFVDIGNTVQKQYHGGALQISQWAHIVNATMLPGPGIIDALAQVASAPDFPHAAHRGLLILAEMTSKGSLATGKYTELSVEMARKYRGFVLGFVATRSLADVDTAAK | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Length: 132
Sequence Mass (Da): 14245
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A0A3B6KKN3 | MEEKIGMTKLWALFLVVFVLLRNAQAAADGNKSRGGMRRLAGAPGVPVPMTLLTSAVAMGAVCLDGTPPAYHMDPGSGAGKNRWIIHLQGGSWCESVGSCLYRKASSLGSSNLMNKQIYFGGILSSSPLDNPDFYSWNQVVIRYCDGASFAGEGYDAGSGLFFRGQRIWNAAIQHLLAMGMSSADQVLLTGSSAGALAVVLHCDQFGAVFAGRGTTVKCLADAGFFLDAVNVAGWHTLRYYFGGVVATHGVAQNLPRSCTSHLDATSCFFPQNVIGGINTPIFVLNAAYDTWQIRESLAPDGADPGRAWRACKSSRLACN... | Function: Hydrolyzes acetyl esters in homogalacturonan regions of pectin. In type I primary cell wall, galacturonic acid residues of pectin can be acetylated at the O-2 and O-3 positions. Decreasing the degree of acetylation of pectin gels in vitro alters their physical properties.
EC: 3.1.1.-
Subcellular Location: Sec... |
I1H4Q3 | MASSLAARRLLSHAAAARRVLSCASPVPSSPSFRRLATDASPPTPLPPPPLQPTVDPPKSEGASSSDGAGAGGAYQAGHGAATGSRRPGGAGYEEEQEKVLRASLLHVPRMGWSESAMIQGARDVGVSPAIVGAFPRKEAALVEFFMDDCLQQLIDRVDAGEGEQLKNLILSERLSRLVQLRLEMQAPYISKWPQALSIQSQPANVSTSLKQRAVLVDEFWHAAGDGGSDIDWYVKRTVLGGIYSTSELYMLTDNSPEFRDTWTFVSRRIKDALDLGKSFKEVTYLAEAMGAGMGGSIQGVLNKVFQK | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration.
Subcellular Location: Mitochondrion
Sequence Length: 308
Sequence Mass (Da): 33056... |
I1IHZ5 | MSTAKGNPPSPDPAAVEEMARDATAWCAMHGLVVGDRAEQRSGTVPGVGLVHAPISLLPARLPESFWSQACELAPIFNELVDRVSLDGDFLQDSLSKTRQVDDFTSRLLEIHRKMMDINKEENIRLGLHRSDYMLDSETNSLLQIEMNTISVSFPGLCSLVTKLHRVLINQYGNLLCLDSKRIPENVASQQFAEALSRAWDEFNVDSAVVMMIVQPEERNMYDQYWIVKYLKESHGVTTIRKTLSEVEAESQVLPDGTLVVDGRTVAVVYFRAGYTPNDYPSEAEWSARLLMEQSSAVKCPSISYHLVGTKKIQQELAKP... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2.
EC: 6.3.2.3
Catalytic Activity: ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + glutathione + H(+) + phosphate
Sequence Length: 401
Sequence Mass (Da): 45366
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A0A7M7R8V0 | MNIQKLTNATMNFDQSAIDEKINSIRSRVYKLEKHVKTTWLIKAIGFLDLTTLGSDDTPAKIEALCDKAVHPFKLSNNSNLHTASVYVYPLRLMDAITALEKLDKDHKISRATVGGGFPSGQYLLETRLREVELDVELGADEIDIVINRPLVLMHQWQKLYEELKLFRTACGNKCLKVILGTGELGNLENVYKASMIAMMAGADFIKTSTGKEAINATLPVGIVMCRAIKDYYESTQKKVGLKPAGGIKAPQEALEWMMLVQMELGEEWLCKDFFRIGSSNLLDNIIEEIQSN | Pathway: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
EC: 4.1.2.4
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Length: 293
Sequence Mass (Da)... |
A0A2N6V324 | MVLAPIGWYRKYISPAIAPRCRYYPSCSTYAVEAIEVHGVFKGLALSAWRILRCNPYSRGGVDHVPEVGHWRYAYPKDVARFQVPSASAGQDAPQTRQGQLG | Function: Could be involved in insertion of integral membrane proteins into the membrane.
Subcellular Location: Cell membrane
Sequence Length: 102
Sequence Mass (Da): 11382
Location Topology: Peripheral membrane protein
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A0A3B6LQ29 | MPMIFPFPVAVAAALFAAAALAPRHASALTRHDFPEGFVFGAGTSAYQVEGAAAEDGRKPSIWDTFTHQGHSSDGSTADVSADQYHHYKEDVKLMHKMGLDAYRFSISWPRLIPAGRGQINPKGLEYYNNLIDELILHGIQPHVTIYHFDLPQVLQDEYGGLLSPRFIDDYTAYANVCFKSFGDRVKHWVTVNEPNIEPIGGYDNGSQPPRRCSYPFGADCAEGNSSTEPYMAAHHLLLAHASAVSLYREKYKAAQGGQIGITLLGWWHEPATDTPQDAAAAVRMNDFHIGWFMHPLVYGDYPPVMRSRVGRRLPALPAP... | Catalytic Activity: DIBOA beta-D-glucoside + H2O = D-glucose + DIBOA
EC: 3.2.1.182
Subcellular Location: Plastid
Sequence Length: 511
Sequence Mass (Da): 57334
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A0A7R9R3M1 | MALRIEGKVWRFPDNIDTDLIIPGKYLRTTDLSVFAAHAMEGIDPDFAKKVGKGDIIVSGRNFGCGSSREQAPLALKHAGVGCVVAESFARIFFRNAINVGLPIMEASVGCRTGDHAIVDIEAGTVACNGRVYHGTKLPDFLVEILADGGLVAHRRKESR | Pathway: Organic acid metabolism; 2-oxosuberate biosynthesis.
Function: Hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarbo... |
A0A2A6D1H9 | MCDDAVREVAFDPNYDPKRKGEGPGGDYAAYFSVRLRVFCDEQEISIDDEVDGADEKCKHYALFKGSQAVAVCRLSIEPPYAKIERVACLKEARGQGYARTLMLAVLRIVDAEYPNEIVAAHSQSAVLKFYERIGFIAVSREFLDEVDILHRSIVFPPRREKIRTLSLLSSPPSKHNEFAGDLYDGQVVTTIRRMLNEIENLSFIPLCSLVVSSISSLFIPSSLHEALCTVALRAQRANGYAENYTPFSPRLSTIEGVSDEEYLKAVAAKKMNTGEKITVEMLPLTALPGTGNGQDGLGCEGVTPFARGRSDNGTRCGRD... | Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
EC: 2.3.1.4
Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Leng... |
A0A1E3FK49 | MTARDGIAPPRATFGSHVLADLAGIDAVLLRDAARLESILTEAAQQAGARVIGAHFHHFGGDHGVTGVVLLAESHITIHTWPEHRFAAVDAFMCGAARAADAVDAIAAALGTQAQVRQQVARGGAPTSAGHSSP | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme... |
A0A3B6HXW6 | MSAAQIRAEINGLIASKFAEGTVDQYFLQLYVMWRYKNIRKGMVVEVMERFLQDADKILTEIAVLLSAPLSLWCRHSRLFGNQPQLDYDKVEGIADQLEGCSSSSVGAKRVNLSCVEYFHPEATTEEGNQIVVDFRKVDALVQQLKGCSSSVGANKLSVSCMHFRRFNHSKTKEGYLIALAPIMNEFCDVRNMFLTILQMEEQVDALGPKY | Function: Functions as two-component phosphorelay mediators between cytokinin sensor histidine kinases and response regulators (B-type ARRs). Plays an important role in propagating cytokinin signal transduction.
Subcellular Location: Cytoplasm
Sequence Length: 211
Domain: Histidine-containing phosphotransfer domain (HP... |
A0A3B6NRW2 | MVCSSHFLERIKELRSTASEISLELNDAVRALGDLHLKHRQLTEKHHEERYLNARSKAEQKRLKVELASAAAELEESNHKLAVLKAQGDTTHGTPILFPTLGNKSFPQDNVRDKQKELQDLGASHKEFTGLISQRLAEIRRLHEERIEILNKLATFQNILTDLKSISSSKAFQVLKDQLQKSQAELDHCRTLLEKLQVNKDKLIWQEREINVKVDLSGIPHRVSLNCESTLAVLDQNLRKVVDEKNMLALKLEESSREPGRNQTISEFKALVSSLPEEMGAMQTELSKYKDDASELHSLRAEVRSISDILARNEHAINES... | 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: Nucleus
Sequence Length: 6... |
A0A0Q3RDA1 | MASSPRRGHAVVVLLLLLACHAPSAAADDRDFDDDKPAKFPDCDNHFQKVKVKYWVGGEEQSALTGVTARFGRLLPDTTAAAQKLPAVVPTPKNGCAKSSASLAGSVALAERGVCTFFEKAKTIESSGAAAMIVVNDMNDLSKMACTPEDKISRIDIPVVMVSKAAGAKFTSAMEGGAKVAILLYSPTKGPFDGAIPFLWLMAVSITACAAVWTVVVVGEEPKKPPTTEVVDQEAAEPDVVELQTKTALVFVVTSSCVLLFLFFFSSIWSAWLMVVLFCIGGLQGLHFVTATLIMRVCSGCRDSKVKLPVVGNVTVVTLV... | Function: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane.
Subcellular Location: Endosome membrane
Sequence Length: 515
Sequence Mass (Da): 55388
Location Topology: Multi-pass membrane protein
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A0A077RFF4 | MAMVQSVARRGARSVATAQLGMHLFSVSCCSPAALGVGTARTAATLKKGEKEAASYWGVAPARLVKEDGTEWKWPCFRPWDAYEADVSIDLKKQWRTQGVCQKHHRPATLGDKVALWTVKAMRWPTDLFFQSLRRFEQSGGWIRPLLEEAENERMHLMTFMEVSQPRWYERALVVAVQGVFFHAYLATYLASPKVAHRMVGYLEEEAVHSYTEFLRDLEAGKIDDVPAPTRRTTGTSNHYASDIHCQGHALREVAAPIGYH | Cofactor: Binds 2 iron ions per subunit.
EC: 1.10.3.11
Catalytic Activity: 2 a ubiquinol + O2 = 2 a ubiquinone + 2 H2O
Sequence Length: 261
Sequence Mass (Da): 29436
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A0A341RP79 | MENGGEPSIKKSRLQKEPMAVKHERAETRESQGGEGALLAVEEAMQVPWVAAEVNPLFYLCFACQLPLRPPVHQCEGGHRVCGRCHGDRCTACDPPAAYSPFPFMDDALAAVRLPCCYRADGCGRKLMYHEAADHALQCAFAPCHCPGHGCSMWASPPALLDHITAAHSWPVTEVGYGSPFRIAVPAPWRGGGTHLLVERNDPRLFLVTLSDFGEATAVTVVCVREGTAAAAPRFRSTVWAEVASNTEEKLFRRQSTVPSSSSGGSLPGGGPPVCLLVPPDFGSESEDLFLGVRIDKL | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ub... |
A0A0R3C2Q1 | MLRIWKATINSRNGLAFAFRSEQAVREEIFALLLSVPLAWFIGATAMRAVELVCSVAFVLTVELLNTAIEKLADRLTLDHDKQIGRVKDMGSAAVGVALLMTGAFWIIAIIERLGFL | Function: Catalyzes the ATP-dependent phosphorylation of sn-l,2-diacylglycerol (DAG) to phosphatidic acid. Involved in the recycling of diacylglycerol produced as a by-product during membrane-derived oligosaccharide (MDO) biosynthesis.
Catalytic Activity: a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosp... |
A0A2A6C1F7 | MRLLVVVLCLESALGFKFLAYNPLFGSSHVNFMGKISDALVEAGHEVVMLATQTDDAIKLTATKARVVHVPQCSASVADKQLLDDIVTNLWLANDPFTMIIQFHHMMTSWIDQCNVVDLHTLQSARENRDMGEALEKLSSLIAATIRHPGLLDALRAEKFDAAFSETLDPCGFGLFELLGIENRAVTQTMAIVDGTHYFTQTPANPAYVPTLMVAPSGEQMPFLDRVRNTLSHLVMVIHNMNSMRRFEPVFRAADPNFDSLEKSMQSNSLVFMNSDPLLDFPAPRSSRVIDIGGISVSFGHSMLNETWSAILDLRPTTVL... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 533
Sequence Mass (Da): 59572
Location Topology: Single-pass membrane protein
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A0A936SK26 | MDTNAINSDRHNDQHETVIQATAVSRGVAAGRAVCLFGTKRQYFLTHIENSAIDHEIGRFRTAVTTASKQLNDLIKSPDIKAKSSGDIFDAHLMMLEHSTLAADVEAFIRSALVTAEWALRRVAENFSNKQAAVSDANLRDRIADFEDLCDRVLNALDGKAVTLPVITSDSVIVASIIRPSTLIELGRQKPSAIVTEHGGWTSHSFILARELKIPAVTGVKSALKLIRDGTSLSVDGFTGALTIDPSSETLEQIKSHTFVAEPIKFDAASTRSTTIDGREIILRANIDLVDPAPLLAQTAAKGVGLLRSEYLFQDVSVGY... | 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 transfer... |
A0A1C6GYZ5 | MSEENRTNAPEEELTQEDINSLKKIRMDKLEELKAKGKNPFEITKYDVTASCAEAKAQYEKLEAELKEQAGEDEEKLKELLEANRITVSVAGRVMSRRLMGKASFFDLRDKSDKVQVYLRMNEIGKEEFDDYKKGDIGDIVGIEGFVFRTKMGEISIHAQKFVLLSKSLLPLPEKWHGLKDQDTRYRQRYTDLICNPEVKDTFIKRSQIISSIRRYLDRQGFMEVETPMLVSNAGGAAARPFETHYNALDEDVKLRISLELYLKRLIVGGLERVYEIGRVFRNEGVDARHNPEFTLMELYQAYTDYYGMMDLTENMFRHV... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Catalytic Activity: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys)
EC: 6.1.1.6
Subcellular Location: Cytoplasm
Sequence Length: 523
Sequence Mass (Da): 60326
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A0A1W4XBR3 | MIHTFATIKANFKLFPQSIYIDNYVFKLHYRITTLLLLVATILVTSRQYIGEHIRCISDNGVPPHVINTFCFFTATYTVVKYLNSSLVDLEAIAHPGVGAFGPLGYNSPEPIIRHSYYQWVPFVLFIQAIMFHLPHLIWKHYEGGQMHFPQVRSLRINSVPRCHVHYGFKYNKRQDLHVPLVLVFILADRVHFGNGLAFSHVLSTCTQSSVQ | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 212
Sequence Mass (Da): 24386
Location Topology: Multi-pass membrane protein
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A0A3B6PFI6 | MGGGSNSGKPGASEALSLVFRITTVGLSLASAIMTAASTQSQCVHDDCNGEATATVSFGNYNSFKYSALADLLSAVLQGVAICLEVARKDKAAKVVEFIDKLLLALTSTSAALLLAVDDITSCGSPRGGGRRRSRRFCTQAGRFCGKIRASSALSLVAAVSVSVTVYTRHIPVSFTLTPRLRASPPAREIPMKGHPTAPPPSVRPKPPKPESPTGPKCGEEPGPCTDIGTPQPPVMPRPCGGCTTLTIPQGCEIAEQVVSPPCCGCPRRTIPQGCENPEPCGAACVYVHE | Function: Regulates membrane-cell wall junctions and localized cell wall deposition. Required for establishment of the Casparian strip membrane domain (CSD) and the subsequent formation of Casparian strips, a cell wall modification of the root endodermis that determines an apoplastic barrier between the intraorganismal... |
A0A842LQ96 | MLEELIKRSGAIKFGDFLLRSGKRSHYYIDKYMFETDPEALRGIAEEIAKRIDPRDFDRVAGVELGGVPLAVAVSLKTGLKSLFIRKRQKEYGTANRIEGDFRSGMRILLVEDVVTTGGALLDAINIIEEAGGIVKKIFVVVDRMEGGVERIREKYDVEVLTNVRSLGISEEIRKS | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
EC: 2.4.2.10
Catalytic Activity: diphosphate + orotidi... |
A0A2C9JT88 | MADHTNGSVQRRNNGDDRDFHDNGDTSESVVKDNNSTHSPGQSLSTQPVKRFVNQTLVPITLLLIMPNFVIVIWYTIVHCHGSYLKMVSVMFEKSVFSGLVHIWSLTRSPSPVIIWSLVLYCAYALAMMKLLPGKTVYGPMTPKGNIPEYKDNGFLFFVLTIGMFWALVLLLRPFGISPSIYYDKMDEICVTLNIFSLVFCAFLYLKGKLAPSSTDSGSSGNIIFDYYWGMELYPRIFGFDVKIFTNCRFGLMIWALMVCIHAVKSYELHGFVDSMFVSALLQIVYLAKFYWWEAGYLSTIDIMVDRAGFYICWGCLALV... | Pathway: Steroid biosynthesis; cholesterol biosynthesis.
Subcellular Location: Membrane
Sequence Length: 481
Sequence Mass (Da): 54974
Location Topology: Multi-pass membrane protein
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A0A967FKB7 | MWNSINRIGTXTGSARLRFSSHFYLVAMFFVIFDLEAVFIIAWAISFKEVGWFGYIGVLIFIFILLVVLIYEWRIGALDFGTSGKNIVKLYKKLNKKEFI | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 100
Sequence Mass (Da): 11635
Location Topology... |
A0A3B6SFV7 | MVEEKRERAEEASESPQKSPRLDPLAGPGCSDAPASPTESSDEWPSSGEVEAGISSDSTGDSMDDSGRCDHIRFDLDMVVHDLKVANQVLKEPRKCQHRNCKTTWEGASEDDQGMMKCIDCSYFFCSGWPVDRDDPQGHARWHAGEHQHWVAQWCDEPNLGYCFMCARPMRLSDWSEDDYAVAARNEKDQQMPGDSVAKDGWGSVSGIAKDERQRVPRIAMDDVASGYAIGDGHVIKGMPNHGQTCFMNATLQCLLALGKLRTKIRSPDAHLGSIGLHLQQLFKETRISNDARGMLDPCMILAAVRERYPNRFEAWKMED... | Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins.
EC: 3.4.19.12
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the ... |
A0A497GLW4 | MKYLRGIKVSDEIFEDCGVVGIKSYKGENVVPAIYWALLTLNHRGQQSYGIVTYDKKFNVVKGLGLIADLDIERMSGWCVKLRASLGVGHVRYATSGSIDKRKLFEDAQPIIVAHEGRKVCIAYNGNIANVVPLRREIEEMGIEINGTSDAYVLAYELLLGIEDEGDLIEGVKRVLEKVDGAFSVVGITSEGEMFAFRDPHGIKPLIFGISEDEETVGIASENVALAVNGILKNRSIAPGELIVAEEDVNSYQLHNGTEALCAFEYAYFARPDSKLSNGKYVYEVRRELGRRLARRYHEVAQRVDIIVPVPQTAEDAAYG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
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 1/2.
Function: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
EC: 2.4... |
A0A1C6CUF7 | MRRVVITGMGTVNPLGKNVEEFWANIKANKNGLSYVDQFDTENFPVKIVGAVKDFDCTEYIDKKEAKRMDRFTQFAVCSAKQALKMAGSDFKDVDPFKAGVIIGVGIGGLNMTEKEVTKFNEKPDKVSVFFIPMMIGNMAAGTVAMHTGFKGDNFCTTTACASGTHAIGEAFRKIKDGYLDVCLCGGSEACISHFALSGFNNMKALSKATELDKASTPFDLNRQGFVLGEGAGILCLEEYEHAKARGANIIAEIAGYGATGDAYHMTSPSPTGEAAAHAMKYAYEEAGLKPEQVNYINAHGTSTGLNDKYETTAIKLALG... | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Involved in the type II fatty acid elongation cycle. Catalyzes the elongation of a wide range of acyl-ACP by the addition of two carbons from malonyl-ACP to an acyl acceptor. Can efficiently catalyze the conversion of palmitoleoyl-ACP (cis-hexadec-9-enoyl-AC... |
A0A7M7GWC2 | MTEKKRVLMICLGNLCRSPIAEAVFYDQINKLGLSDSWEVDSAAIIGYHIGKNPDHRSMSIIREKGITDYSHKARQITRDDFFKFDWILAMDNSNIKYLNSMKPPNTTAKIELLGKYDPEGELTIRDPYYVYCFNMMFTLLDFIRYMNNVCEVQKHFWKNIKINNQIEALK | 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: 171
Sequence Mass (Da): 20089
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A0A2A6C3V7 | MQQLVWKPTIGLLWFALYHKRARIEVVEVTFLICISMFGISASVMVICSAFIIEALRSMKVSTAKKVQQRMLFRALLIQTLIPCIFSYFPLCIIWMFPLFTGIALGAFGNILTMTSTVFPSVDAIIIIIFIPAYRHSVKMWILNKIRPSDLVIVSTPCRIQMLGRAAGRIASSHRRAQILTQLRLLNLQEYQSKGILDRNGCSVQKFVTATSLKEAEEKLKDFSVYEYVVKAQILAGGRGKGRFIGGPKDLGGVHISYKPEEALSAAKEMIGRRLVTKQTPKEGVLVEKVMIAEGVTIKRETYLAVLMCRETNGPVVVAS... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Function: 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 ... |
A0A7M7MQ32 | MATTKDDSTDSVQFFEGVEKLLEIWFTSSSSINRKQGDLRQIPQWKWQSLLKIVRCEIISICRTEHVDAYVLSESSMFLSKRRLILKTCGTTTPLQCLEPLLELIKEYTGFEEVENVFYSRKNYKKPELQISPHQAFEEEVGLLDTFFPGGEAYCLGSVDSDCWYLYTLNKEKSVDEPSEPDQTLEILMTHLDPEIMALFTRDVCSSADEATQKSGIDKLIPNMIIDDFLFEPCGYSMNGVSKNGNYMTIHITPEPEFSYVSFESNIPEASYEEIIRRVLNTFKPKKFVVTVFANKESIAASCPRDLEQTDFLKCSGDWL... | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
EC: 4.1.1.50
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Seq... |
A0A3B6AZG2 | MSLAAESPSPSPSSSSGSDDFAALLDAELDLASAVDSASVGDPSTSPTSSDDEEDDDEDVVADVETVEQSSAKRRKVKVQYQDRETAIRPDEDSIGSSEDAQIKICPPHPGYFGGLCFRCGKRQDEEDVPGVAFGYVHKGLRLGTTEIDRLRGSDLKNLLRERKLILILDLDHTLINSTKLHDISAAENNLGIQTAASKDDPNGSLFTLEGMQMLTKLRPFVRKFLKEASNMFEMYIYTMGDKAYAIEIAKLLDPHNVYFNSKVISNSDCTQRHQKGLDMVLGAESVAVILDDTEYVWQKHKENLILMERYHYFASSCRQ... | Function: This promotes the activity of RNA polymerase II.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Nucleus
Sequence Length: 540
Sequence Mass (Da): 59806
|
A0A077RPY2 | MQGAGAEGGNRGSPSTMEKADESAKKARLELPNGHVKQEVGVQHAVGGDDGGAIVPAEAGHGSRVELAVKIDMSVLHCPLCTLPFKPPVLQCNKGGHLACGGCVALLPGGQCRACEDGGGFFSPCPALDAIVSSTKIVCPNAGCQTYVPYHEAADHRSACPHAPCHCTEPGCGFVGAPQALAGHLVDLHSVPVRTVQYGRVSQVPVSGRRQLLVAEEDGRSFLLTVGALGAAAAAVSVVCVRASASTQPRFSCKMWVNLVQPASGGRADMVLVDIQMRSSATPGAVVAVDEPTFLAVPRMYMVPVDGDAASMEVPLNIRV... | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ub... |
A9HS47 | MTLLKIARMGHPVLLRRADEVADPTAPDIARLIDDMIETMEDARGAGLAAPQVHVSLRLFVYRVPAERSAGGDDPPRETSVLINPVLSLVDDEMALRPEGCLSIPGLRGMVPRHVRIAYSGLDRAGQAVQGVASGFLANVLQHEYDHLDGILYPMRMTDLGQMGFDEEIGRYGVRT | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic ... |
A0A0Q3GY12 | MVPRSLNSTSLPDADTPPPPPPPPIDPNDDAEEQLSAEAPDLAARLEALELAASERAADLSSSSRAGVILEEPAEPSSSKPWWSPPRGWRVAFSTATISDTLERLDDSIVLRLRGRALHCFNNEAYDLQCYPIIHSNGQYLFKGSLFQYLFFEDEKLHAEIARYKFSSYETPFLPSLLMEPITRIPWSLQGLHPAAESININERVLIRYFYEFLPMLVNEGSDGQPVSSSQCDVKILQALSNRIHYGKSVAESKFLEEPEKYTSAIREQDNDNLMETLTNPDAEEEVITRVKNKAMVYRQEVDPELVGELYDKLVIPMTK... | Pathway: Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1.
EC: 5.4.99.5
Catalytic Activity: chorismate = prephenate
Sequence Length: 332
Sequence Mass (Da): 37587
|
A0A6I9SL11 | MDLKSTNGSLIVADPAPITKSRLGAYSGLMPYSQSGPSFSANITTVPRKKPGKLDDVRSNGWLDAMISSSPPRKKIHKDFNAFDIVSDEADVAYQSWMIRYPSALKSFQLIMDRAKNRKLVMFLDYDGTLSPIVDDPDRAFMSNEMRSAVRSVAKHFPTAIISGRSRDKVYDLVGITELYYAGSHGMDIMFPTRDTVSPNHLNCVKSTDLQGKEVNLFQPASEFLPMINEVYRTFVEITKDIKGAKVENHKFCVSLHYRNVDENSWPLIAQYVHDILKDYPRLRLTHGRKVLEVRPVIDWDKGRAVEFLLESLGFSNSSD... | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose. Trehalose accumulation in plant may improve abiotic stress tolerance.
EC: 3.1.3.12
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
S... |
A0A088E7W1 | MKVVPSIDISKGMAVKRVRGREGTGLVLGDPLKIAEELRNMGYTSVHLVDLDAAEGKGDNVEVIERVMKDFSEISVGGGIRDRSRLERFLSSGATKVVMSTLAFTKPDTFRRVVAGYENRVLVSVDYCERKVLIKGWNESAMSFEEAISHVNSLGVRGVIFTYVCNEGTRNGIDPEIGRYVNLVQGEKGYAGGIGSIQDLQELDKMGFHFAIVGMSLYAGVLRGVTSV | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho... |
A0A370LIG4 | MAKIWVEAYGCSASYADSEMISGLLVNGGHSLAENSDDSDLSVVVTCSVKDATANKMIHRIKSLKDKPLVIAGCLPKAEKSTVEKFSENASLLGPNSLGKTLEVINATLNGKKKIELLDSDLNKVGLPKVRLNPVIGIVEIASGCMSECTFCQTKLSKGDLSSYRLGDIVRQVKTEVDDGCKEIWLTSTDNGCYGLDIGSDLSELVNAVSDIPRDFRIRVGMMNPMYMPRIREGLLKAFENDKVYKFLHIPVQSGNNKVLNDMKRGHTAETFRDVVMRFREKFPKFTISTDIIVGFPSETDEDFNDTVNLLKETKPDVVN... | Cofactor: Binds 1 or 2 [4Fe-4S] cluster. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs... |
A0A657AVF4 | MNKARQYHSDLASLLLGIQHVPSALNTQIHGLVSDSRKVKQGDLFLALPGINSPASTYVQDAIERGAAAVLIDCNANEANDLTVHEDGRAIELFVPNLSNFVGEIAHRFFHKPSEELQVIGVTGTNGKTSVVNYIAQFFASLGVSSAVIGTLGYGLCARDEELTDTGHTTPSVVDVHKYLANLRDAGAELVAMEVSSHGLDQGRVDGVRFEGAVFTNLSRDHLDYHQTMAEYAKAKARLFASEGLRYAVINADDEYASVMFQALRPEVRKLRFSLNGSAEVLVKDFQLGMTTTAKIEVADKIIDLNSDLLGQFNLYNVMA... | PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in... |
A0A965C9S6 | MRPSDRQEVEPARLDNVWTALDQCAKTLGLAIIRGYEYTVRPVLGPSCRFLPNCSEYARQALQSHGSVKGAYLSLRRLCRCHPFHPGGIDEVPAPSSSHGTKPAEARVSKKNDREPAAS | Function: Could be involved in insertion of integral membrane proteins into the membrane.
Subcellular Location: Cell membrane
Sequence Length: 119
Sequence Mass (Da): 13101
Location Topology: Peripheral membrane protein
|
A0A2W6APG5 | MKSRLASGPRRPEVVIWGAGAIGGLVGAWLARAGVDVTLVDRDEEHVEAIRARGLLVDGIRGEFRVQVPVVLAAELREPVDLAFLCVKCLHTESALDELVPRLADGGRIVSLQNGLNEEVIARRIGRRRTLGCFINFGSDLLGPGHIRHGGEHPVYIGELDGARSESVEHVRALLANFCDTVITDNIWGYLWSKLCYASLLFGTAMVDAPVHDTVRQPEAGPVLLGLVREVIDVADAEGVRLERLADFWPDEFRDGDWRSAMKRTAAHYQGQLKTRTGVWRDLAVRHRRTEVDCQVGAAIRKGESLGIEMPLNRRLLELI... | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 341
Sequen... |
B1G158 | MTDKHRLIHITRDTHRVDIDLVYATPRNFTGKPIYREAHCLLLEPAEAALRKAVELAESIGMSLLIFDAYRPPQAQKVLWDFLPDPTYIAELGRGSNHSRGTAIDLTLIDGNGEPLDMGTGFDEMVKASEHFHHGLPQHVQRNRLLLLGIMHAAGFTHIASEWWHYELPGSRALPVIDNSESGPLKLM | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide.
EC: 3.4.13.22
Catalytic Activity: D-alanyl-D-alanine + H2O = 2 D-alanine
Sequence Length: 188
Sequence Mass (Da): 21132
|
A0A967FAR5 | TGRWTCPECGHMYHEEFNPPVEDLVCDNDGAELYQREDDKPETVKNRISVYREQTQPLIDYYEKQGVLTEIDGDQEISEVTDELLSILS | Catalytic Activity: AMP + ATP = 2 ADP
EC: 2.7.4.3
Subcellular Location: Cytoplasm
Sequence Length: 89
Sequence Mass (Da): 10338
|
A0A454XZJ7 | MTDFMPDVNSLFAGRTVFLTGGSGFVGKVVIEKFLHAIPDVKRLYVLVRPAKGKSAQERWEAIHTKSEIFNRTRADCPETIAKVFPVEGDITIDDLGLSEENLKRVLEETSVVIHCAATVRFNDTLKSAIELNIKGVNRMIKLCKRMPKLDCFLHCSTAYVNVDKEGDIEEKQFDVVCDPYKLMDAQSWMTEEMLEGISNSMSNKYFNTYCFTKHVSEELVRRECVDLPTLIFRPSIIGGIWKDGIPGWADAFQGITANALGFGTGTIPRMPIPDTTIPLDAIPVDIVSNMMIVCAAYRLHLTNLKDKSMPIFHCNSSHL... | 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: 558
Sequence Mass (Da): 63621
|
I1ICA9 | MDLSNGSPVITDPMAMGQPLMGVLPSNMMPFSVMPGSYSSPAGAGLNVSRRKIEEVLVNGLLEAMKSSSPRKKHNLVFGQENLPEEDPAYTAWTATTCPSALASFKQIVAGAQGKKIAVFLDYDGTLSPIVDDPDKAVMSPVMRAAVRNVAKHFPAAIVSGRSRKKVLEFVKLKELCYAGSHGMDIMTSSANYEHNTEKAKEANLFQPAREFLPMIDEVSKSLLEVTSGIEGASIENNKFCVSVHYRNVDEKDWELVARLVNEVLEAFPGLKVTNGRMMSRRFCRF | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose.
EC: 3.1.3.12
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Length: 286
Sequence Mass (Da): 31349
|
I1IE59 | MDGRESAAASGANFSPFYVRPWGMGAARAAAGNPDGLHGPPPVGYRQHLDAVSAGYSFQQPHFGGSHIGQEYHHDHVEGSPHVVQHTAGMDIVAVGVDAKGGDQGSVEGQDEQVKKKRGRPRKYKPDRAVTLGLSPSPSTPHSSSSGMGAMVTTPGAGFGSGTGSGGSGSGALTEKRGRGRPPGSGKMQQLASLGTWFLGSVGTGFTPHVIIISAGEDVAARIMSFSQQGPRAICIISATGAVSTATLYQDSDSGAVTYEGRFEILCLSGSYLVLDEGGTRKRSGGLCIALCGPDHRVIGGSVSGVLTAAGTVQVIVGSF... | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Subcellular Location: Nucleus
Sequence Length: 450
Domain: The PPC domain mediates interactions between AHL proteins.
Sequence Mass (Da): 46781
|
A0A3B6HYW4 | MARAVSLSALCLLLAAAAAGARVDPIYSGKLVLDWSKEPKFKLQNFSLNREDNLQLLSRSRDVTRRKLGERTGVIKMETVQQDDEALVKLENAGFERSKAVDSAVLGKYSLWRRENENEKADANVRLMRDQMIMARIYSVLAKSRDKLDLYRELLARIKESQRSLGEATADADLPKSASERAKAMGQVLSKARDQLYDCKEITHRLRSMLQSADEQVRSLKKQSTFLSQLAAKTIPNGIHCLSMRLTIDYYLLSPEKRKFPNSENLEDPDLYHYALFSDNVLAASVVVNSTIVNAKEPEKHVFHLVTDKLNFGAMNMWFL... | Pathway: Glycan metabolism; pectin biosynthesis.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 461
Sequence Mass (Da): 52531
Location Topology: Single-pass type II membrane protein
|
A0A497FAL9 | MGKVFVVPGSASENLARKITQEVGVEVLGVERKVFPDGETYLRICAEDLSGASVYVVQSLARKPNDYLLELLLLVEAAKGLGAKKVTAVIPYLAYARQDSRFKPGEPISIVAIARALEAVGVDEVVTVDMHLHRFHDVSEVFRVPATNLTSIPLLAKFVKEVWKLEKPVIIGPDEESEQWASIMGRELGTTYSVLEKERLSATEVQIKVRGEVSVKDRDVVIVDDIVSTGGTVAEAAKVLKQLGARRVFAAVVHLVLAPGAIERMKSAGVVDIVGTDTIESPYSHVSVAPVIAKYIKEREGL | Cofactor: Binds 2 Mg(2+) ions per subunit.
Pathway: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1.
Function: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-p... |
A0A454XR98 | MSSDDSPIEFIDITNDEGLRARVLTWGATLVSLWFKDKNGREHDCVLGYDTIDEYKSDRVQMGKTIGRVSNRIKNGEFEVNEEKIQVEKNEGNNHLHGGPKGCSQRNWSIHRRAHNSVTFLITQTHDLDGYPGDANMKCTYTVNDLNQLVVEHWAETTVPCPIAMTNHAYWNLDNDSTTCLDHHLFVRAHYYLPVDDDKCPNGDTKPVFGTSYNFNKMRRIGPSPPIDHDLILTDHEKTKIVLALENPTTGIRMTMRTTYPSIHIYSAEQFDGSIIGKGGRSYPESAGIAIEPQQYTSAVHFDWFPPVIVDPSTPYEQEI... | Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.3
Catalytic Activity: alpha-D-galactose = beta-D-galactose
Sequence Length: 333
Sequence Mass (Da): 37839
|
I1IV26 | MADSAMKKYLVQVEEGRAAAAAAEDGTAGAPSVGPAYRCAAGGGAASPPVVPGLDSCWDIFRLSVEKYPGNPMLGRREIMDGKAGKYIWVTYKEVYDSVLKVGASIRSCGVSKGGRCGIYGGNCPEWVVSMQACNAHGIYCVPLYDTLGAGAIEFILCHAEVEIAFVEEKKIGEVLKTLPNATKFLKTIVSFGKVSPDQKEKVEQNGLYIYSWTEFVLKGDGNEDKYELPPKEKDDICTIMYTSGTTGDPKGVLISNKSIITIVSAVDEFLSNSNEQIRENDVYISYLPLAHIFDRVIEEVFIHHGASIGFWRGDVKLLV... | Function: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation.
EC: 6.2.1.3
Catalytic Activity: (E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP + diphosphate
Sequence Length: 672
Sequence Mass (Da): 74254
|
A0A839V128 | MIDHLVETLRTPLAFVVVLGVLVFIHEMGHYLAARLVGVHVDVFSIGFGPVLRRWHDRVGTEWRLCALPLGGYVKPHGFEEPDESDVESRAGLRPGQTFHDKPVWARAVVILAGPAFNFAFAVLLFSALYMAAGKPVSSTRVESVTADSAAASAGILPGDRLRSIGGVRVDDFDDIMAQVAPAPGRHTQVVLERDGHTLSVPVTIGRAVSDGTPIGRLGIGGVVEPGPRLGPLAAVSAACGETWTVSVQTLRALWQMVTGYASPRALQGPLGIARLSGQVAKLGVASVLSFMALLSINLGLINLFPVPVLDGGRLVFYAI... | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 370
Sequence Mass (Da): 39153
Location Topology: Multi-pass membrane protein
|
A0A3B6U1S4 | MAAQNNKEVDALVEKITGLHAAIAKLPSLSPSPAVDALFTELVTACVPPVRVILMMSFGLLYSCFLASSYICIYDCFCLLVIQVAYFPNMVLELGLFSRTHNSC | Function: Synthesizes nicotianamine, a polyamine which serves as a sensor for the physiological iron status within the plant, and/or might be involved in the transport of iron.
EC: 2.5.1.43
Catalytic Activity: 3 S-adenosyl-L-methionine = 3 H(+) + nicotianamine + 3 S-methyl-5'-thioadenosine
Sequence Length: 104
Sequence... |
I1ITB2 | MGCGGRSSTTAMTWPRWRRRHGWQLPLHPLQLVAAAVFSVLVAAFYVVLGPYLGSTVAGNTLLALFSFSAAATAALYVRCTAVDPSDRTHAKKMKRQRSLARGGGGGKLPRLRYGYILWRYAVRLLKRVEARVMNRWVRRSYLEQWNTSVQLDPMLPFAFTSLDDIVSPHATEDQDISFCPVCDCEVKLRSKHCKTCERCVDGFDHHCRWLNNCIGRRNYAAFILLMFFVLLMLVIEGGTAIAIFVRCFVDSKGVKMEMEHRLHIRLPKGAHAALSMAFVIFTMYSTAALGQLFFFHVVLIRKGMRTYDYILAMREAAQA... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 519
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 58979
Location Topology: Multi-pass membrane protein
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A0A2G8B1E1 | MHIEARLFEFVAAFFIATAVLYGVLTQLFATGGVEWAGTTALALTGGMALIVATFFRFVARRLDTRPEDYEGAEISDGAGELGFFSPHSWWPVLVALSGSVAAVGIALWLPWLIVAGVAFVLSSAAGLVFEYYLGPEKH | Function: Part of cytochrome c oxidase, its function is unknown.
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: Cell membrane
Sequence Length: 139
Sequence Mass (Da): 14900
Location Topology: Multi-pass membrane protein
|
A0A965SC64 | MTGVDSPPQNPTVWSDPAPLTVSALNRLARERLESAIPLLWITGEVSNLTRAASGHCYFSLKDADCSVRCVMFRGRVAASGLQLVNGQQLDVRASATLYEARGEFQLQVDALRLAGLGSRFAALEALKQRLLAEGALDAARKRALPTMPRAVGIVTSPSGAAVRDLLTLLEQRMPSLRVVVYPTLVQGDSAPSTIAAAIELAGQRLEVDVLIVGRGGGSIEDLWAFNSEAVARAILACPLPVVSAVGHETDTVLSDLVADVRAPTPSAAATLVCPDHRQLLAHLTQQQQRLQRGMQMRLEDREQRLDHITARLLSPAQRV... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
C3XU25 | MDVVQDVAEVFATLPLFPVFNACHYTLMILTTRYDTGSLALSRSNPLANWVASMIACFGGYILADLLLGHSVLSFLAHPEDVVLASAIWYLLFYCPKDLFYKIISVLPLKLVITALKETARVRKLVAGIGAAAKVYPHSLLAQVIVGVAKACGNEFLLNFEQAVRGVWKPDINAILQPSFSIKACVVGAVMIILGRSDVLMGISQEMVVLAVSLWLISVAVSMKAFHADDPFKPVENLFSPFIFGSADSLPADAHHHHPPAPEPSPAPKPPSGRRRGKAAKAD | Function: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores.
Subcellular Location: Membrane
Sequence Length: 283
Sequence Mass (Da): 30586
Location Topolog... |
A0A0Q3HC50 | MADVVLLDLWVSPFGQRCRIALAEKGVAYEYSEHEQDLSQKSVLLLQSNPVQKMIPVLLHSGKSVSESLLIVQYIDEAWPETAPRSSPPRSLRPRSGPLLGRLHRQEGAYSFGALVIEVE | Function: Is involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
EC: 2.5.1.18
Subcellular Location: Cytoplasm
Sequence Length: 120
Sequence Mass (Da): 13381
|
A0A2A6B4F5 | MKWRDEYFEPYQWTADQQETQSECMRQSISGNDILCQAESGAGKAALLVIATLQQLDILDGQLSTLVLCFSRENVYKIREYYERFAKYMAIKTEISLGGMSCDKDREIFEKESPHIVIGTALRIRNIIQSGSLKMDKFKWTFFYLENYGFDVKGKANFAFLTDSH | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 165
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): 19117
|
A0A183LS69 | MNSKHSSPSVGLKRLYSLLKLLLNITASVTDSLDDYVVCGNQMLTDNLLRWVLGERGQLRHVYVKHHRVGETLPPSQYTILDDVIYTIKIETKDDNGNWVPFNADDVQLEFVRIDPFIRKKMEHKNGEYKLVMKLPDVYGVFKFVVDYYRVGYTHLLSVTQVPVRPFTHTQYERFLVAAYPYYGSAISMMIGLILFSFVFLYLKDDKEKGE | Pathway: Protein modification; protein glycosylation.
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus m... |
A0A536ZB31 | MSELQVGLLVVGAVVVTAVFLYNKWQERRYQREAEARFASHREDVLMRSGGGIGLGTPLTPGPEQFGPALVSFEAEHQGVGHPGRGLSEFLDFIVPIETPQEVSAAALIGATAAALERCSKSISWEGFDETAASWEPLDPDRSYSRLRSGMQLVDRRGAADAEELAAFGAAMQKAAASVGALATLPDPAPALAKARELDRFCGEIDIRVAVHIISDAAPLKGTQLAGLAKAAGFRLDEPDGKFRLPDEAGRIICALANFEPTPLSVDGLNALSTRGVTLELDVPRAPYGAFNRFRQSAQMLARELKARIVDDNREPVGPA... | Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 3... |
A0A662FXH8 | MKIAYLVKSSTAHTSPDFNIRSIASTSGRFDLILRSILSAFSMPNRFKGMIKFYALLEGPPSPPLVIEIDGNRVSSLPESEIDLCEILIDAMRGRKFPGIKLYKLDFRKLVTNLIREFKPIYLVEDGSPIQEFNFNRKVNYLFILGDQKGLCVEQERFLNNVNATRISLGPVSYLTSQCITLVNYFFFKKIT | Function: Specifically catalyzes the N1-methylation of pseudouridine at position 54 (Psi54) in tRNAs.
Catalytic Activity: pseudouridine(54) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylpseudouridine(54) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.257
Subcellular Location: Cytoplasm
Sequence Length: 192
Seque... |
A0A811KZE1 | MCSDGAGFTKDFPGLTRHLTTLDIQFKIPFRRTILSAFGVIPASSRFITKLLSNKTRNGTSLANGTSGAKTLASGTNGTHMPSSGVYGITNRAVSANSTINLTSGTNGTINLVSGTNGITNLASNANGTPNFISGANAPKIPKQTQNPQPTGKAICLVVGGAEEALESHGNVYKLRLNDRKGFCRIALKTGSYLVPVYAFGETSGYRQVRNPIGSKLRDWQTKIKKVWGFSPVLAYGKDLIPGLPSVTPFEGEIVVVFGSPIPVTQLDDPTDEQVDQLHSLYKTKLVALFEEHKGNYGIPKNVQLSFY | EC: 2.3.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 308
Sequence Mass (Da): 32981
Location Topology: Multi-pass membrane protein
|
A0A6A4WDS8 | METVSMSMPNYSYVFKFEEDFAEKERRQWMSENWYVCMYYIGAYMIFIVVGQHYMQSRPRFELRNTLALWNFFLAVFSIIGTMRTVPEMLFVLRHFGLHHSCCVAGPSFVQNNTVSAFWSYLFTMSKVPELGDTVFIVLRKQPLIFLHWYHHVTVLIFTWYR | 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: 162
Sequence Mass (Da): 19521
Location Topology: Multi-pass membrane protein
|
A0A7S3IW43 | VGDIIDVKSLNIVEDRTPAPGFLSEADLITMMEANGIGTDASIPTHISNIIERNYVTVKEGRKLVPTPLGQALVKSYCEIDPELVLPKVRSNIEKSCELISKGRAD | Function: Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by... |
A0A426YQG5 | GNGGEETWSHRLVRRRRDAHRPEEGPIRSVIDHLSGVITPQMLEFMRDLREVVKDPALYFVVTVGVVGGSDLVKITEQLGKPVMNDYDYVFSENGLLAHKNGELIGRQSLKSFLGDNSLKVRYSILHVIHEAF | Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.
Function: Catalyzes the interconversion of mannose-6-phosphate to mannose-1-phosphate, the precursor for the synthesis of GDP-mannose. GDP-mannose is an essential sugar nucleotide... |
A0A7T4T5L6 | MAWQAEALCAQTDPEAFFPEKGGSTRDAKRVCSECPVSTACLDYALAKDERFGIWGGMSERERRRLRRQSR | PTM: The Fe-S cluster can be nitrosylated by nitric oxide (NO).
Cofactor: Binds 1 [4Fe-4S] cluster per subunit. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
Function: Acts as a transcriptional regulator. Probably redox-responsive. The apo- but not holo-form probably binds DNA... |
A0A2A6CRF0 | MSIACVATHRRRTTFTEEYLRMADQSAGSGHIKSKSRNGFDVFINFTDPHRVMCGQPNSSIQYFMASRGDLNHGFPHNQTLTNFIQWQQYYICFSDGLIWTINAFTKAWNVVTVRNSDDFEWQPNSRHDFLHTEDDRMTLVKFLPNRANCERVILHEYTLFVHNDNHLNTEVHTPITSSRSGRHPSEISQSTTSSTNASHNSSFSQSHGSIDSTTPIFSTQSSPSASEPLLEPENDDISECSTGQSATALESSDKSDDKSNYLSCKICLIEYGNRARSAIVPCGHLACSNCIRQSMKENNRCPFCRKNIECTLRIYE | 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: Nucleus
Sequence Length: 3... |
A0A811JSG6 | MQAAARLIEKVKSRHDDDVIDRANYVYTATMFGMFATITMAKQYVGEPLQCWIPPEFKGWWEKYSESYCFVENTYYANIHEKLPDSKADRESRELQYYQWVGFMMIGQMIFFILPKAVWNSLNLKTGLNIQSLISTSKLTLKKGNNAVIKDNTKDDIQKASEYMKTLHRFNKDRISTQSRKPLNAKFWNGYITKLYLLFKVINLFNSIIQLYALNRFLGPKYTFWGYGLLMDLLQGKQWQESGHFPRVTYCDVDVRLPGDVVAQYTLQCVLAINMFNEKIYIFIWFWLFGLSILNFLNLCNWIFLVLSEKNAIKFVQTQL... | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 407
Sequence Mass (Da): 47559
Location Topology: Multi-pass membrane protein
|
A0A811L1S0 | MGAKLILTSVLIAITSLYVYNRITAEPEKVNWPKAGYFGPGKPKPDDEKVYPFKIQVPEAAIKDLSSRLKNVKISHDDLEDAVGMTYGFTKKLLHVFKDYWLNNYNWRAEEEKLNKLSHFKTEIEGINLHFIHQKSDKYKKVLPLLLSHGWPGSVHEFSKIIPILIDPKSHGIQSEYAFNVVVPSIPGYGWSSASAKTGMNAGAVARIFHKLMIRLGYNKYLVQGGDWGSVIVANMARLYPEHVTGCHLNMFSSFRPDSLLQSLLITVAPGYFLHEESLKDYNIFKTLKFMIINGGYFHIQATTPDTLGIGLNDSPIGLL... | Catalytic Activity: 1-(4-methoxyphenyl)-N-methyl-N-[(3-methyloxetan-3-yl)methyl]methanamine + H2O = 2-{[(4-methoxybenzyl)(methyl)amino]methyl}-2-methylpropane-1,3-diol
EC: 3.3.2.9
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 451
Sequence Mass (Da): 50982
|
W8CAS9 | MAENKTDSNVLTSAARNSSSSSDSSTDVPVGPYPEDKLNTLMNKCWTDAIIKSGVGFGIGFLCSVLFVRRFWPPLLGASFGLGVAYKECERNLLSLTECEPIFEVKGKRIL | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 11... |
A0A0Q3K901 | MVATFASMSKVPGTRDLWSYHSQRQFVGILITFSRGLRPQETTEQHQLIQIHSIDPSMARATRTSTMVLAAALATLLLLASAPALATAARTAPAADKASPDEKSSTAAAADVDCEGGAETAEECLARRTLAAHTDYIYTQEHHN | PTM: PSK-alpha is produced by endopeptidase digestion. PSK-beta is produced from PSK-alpha by exopeptidase digestion.
Function: Promotes plant cell differentiation, organogenesis and somatic embryogenesis as well as cell proliferation.
Subcellular Location: Secreted
Sequence Length: 144
Sequence Mass (Da): 15424
|
A0A497FX20 | MKKWEKISILLELALRGAILSPIEISTVEMAKILGLSQQSVSRKLIRLEEAGLIARRMRRRKSIILITDKGFKLIYEHYLKLRKIFDKTTQTIILRGVAVSGLGEGAYYVTIPYYYEQFKERLGFSPYPGTFNVKLTKDSTKMKQLLLYTPGIEIEGYYDGKRMYGGVKCFRVVINNEIKGALLLIERTHHEPDIVEIIAPVCIRSTLGLSDGDFVVIKVLLNDL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (CTP route): step 1/1.
Function: Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN).
EC: 2.7.1.161
Catalytic Activity: CTP + riboflavin = CDP + FMN + H(... |
A0A965CAD4 | MSTQNNRWNSALIILLGFSCLLYLYRIDKPSAPFWDENYYIATTERYKAGLAHLESHPPIGLMLIAAGDWLTGANSTLSTAPLARERHVSGDQIPKGYSFVGIRLFPSLFAILCIAAFFALLRRCSGSDSVALAASVLLLVENSFITHFRAAHLDSIQLFFVLCTIYQLVVVWKRNLAIGVKDFAIFGALCAAATLVKVNSVFLLALAPVMLLRDLSFVRSASRYGKFDRVFTNLGGLSGGAIAVCFAVFALHTILGSHTPDRNSPSGQVTWAHSSDTYKAYYTGQEGLSFFVVLHVIRDYGRFMNQDHRGVPKLDICKP... | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
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 Locatio... |
A0A811K8E1 | MGANCNIVCVHCGAEATDLYRNYGKNVIKLCECDNCGKFVDHYIEYDSVLIYIDLLLQYTAAYRHVFVNRVYLVKSLWRIVCLFSICEAYRKWAVRMESANKSVLDGFIDLEWKFYECIVESLSEIAAFGFSTLGFSLIFDLKTKLSLRSVFWISCCGYYGKAFVLLAVIWNLHHTWEYVFLIEAFLILSHYQIQNILFSDSPKLNALMVLLSWITSYLAGSYCHIVFDYTNQNYKSWFDYIRAL | Function: Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 245
Sequence Mass (Da): 28618
Location Topology: Multi-pass membrane protein
|
A0A0N4THY5 | MTISYTGNFCRLLIRWKGSLWRLVWRELFIFLILYYIIRLIYNQILPLLDKENPEKYRFEFERIAITFDQYTRMIPLTFLLGFYVSNVVIRWWRQFECIPWPEDILSLLCTLIPGKDIKSQQRRHTIARYVNLVAALVYREISSTIRRRFPSLSHLVQSGLLTETELQLINECSVSTITYANLT | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 184
Sequence Mass (Da): 22064
Location Topology: Multi-pass membrane protein
|
I1HU91 | MPLSAAATEAAIKPIPRALSITAAAAAAVTTSLLLISAVVSRARPDPPSPPPSTSASTTAALPPAPEPSPLLPDHPRPPPCPPNASHLTPCHEPPPSGERHCPPPPPPPHPPHSPDDPPPHPPHSPDDPPPHPPHPPPPPPHCRVPPPPGYHPPPPWPVRRERARYANVDLPLLTAAKTAPSGSLDPARARGEWLVFPKGVGTYVEKLERVVPLRGGTVRTALDVGCGVASFGDYLLSYGILTMSIAPRDIHDAQVQFALERGLPAMIGALGAHRLPYPSRSFDMVHCADCHVSWTAHDGRYMLEIDRLLRPGGYWVVSS... | EC: 2.1.1.-
Subcellular Location: Membrane
Sequence Length: 624
Sequence Mass (Da): 67956
Location Topology: Single-pass type II membrane protein
|
A0A662HXI0 | MDFQEVMHLKHLSKTIRPKGGKTVKIEAWVSENKLEKVMFSGDFFAYPAEALEELEQRLAGSPLNVEEIKSVFKQYKGKVSLVGASLNVLEEELLRLLGLSAE | Pathway: Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
EC: 6.3.1.20
Catalytic Activity: (R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate + H(+)
Sequence Length: 103
Sequence ... |
A0A811L3W2 | MGTESTKNVANWEKWLQLAQVYYFFTLFVVGSVFTPILLVVLLFTRFWWYSVFYATWTIVHKFYFFTLPKPWEWLRNHTFWDHYGRYYPMKLHKTAELPPEKNYLLIWHPHGILSFSAGATVMTNITRFTETYPGITRYAATLPLHFLYPLRSFCMAMRGFIPSNFSNIFKVVSHKQGGNAVILAVGGAEESLESHEGNYKLVLNSRKGFVRLALKSGCSLVPVYAFGETSTYHQVLNPVGSKLRRFQTQVKKILGVAPAFFYGTMGFWRLYGPFPLSAELNTVVGAPIEVEPVAEPTQEQIDQLHDTYKSKLIELFEAH... | EC: 2.3.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 335
Sequence Mass (Da): 38653
Location Topology: Multi-pass membrane protein
|
A0A2A6BD57 | DLDTSQLQSNRSTFLWSVDDPFSGARAYLFGTIHVPYTAVWDQISPRVKEAFDRADSVAFEVDLHDEIAMRKLVRCKNLRKRQNVHSYLPNSMYKRLNKVMNSFYDRIYNALAGKNAHSGEEVEAVRIQAQRIHEAITENWDRKRPEWLLLLLYQLCENLNERMGSAPILDLFLAETASASGKTMHSIESVEEVLFAINYTIAYLEKPEKLIAARRKERTLSDIVRDYRCGQVEHTMKSTRDLAIVIDPEMDRKEQLIEDQLKDDILVTRNERMARRIASLMQAKPHSKMFAAVGTGHFFGPRNILDHLNNIGYVVAPVA... | Cofactor: Divalent metal cations. Mn(2+) or Co(2+).
Function: Metalloprotease that acts as a negative regulator of the Wnt signaling pathway.
EC: 3.4.-.-
Subcellular Location: Cell membrane
Sequence Length: 384
Sequence Mass (Da): 44340
Location Topology: Single-pass type I membrane protein
|
A0A2A6BMX3 | MNFLGDPFKLIKPRFDDSGVDRLNYYYTPVVIIVMAVTITAKQYVGEPLQCWVPAQFSRAWEQYAENYCFVYNTYWVRPGEEIPSDVDERLAAQLIYYQWVPFIMIIEAGLFHFPAKIWAVLSKTSGLNLAGMIGAVVKAEEGNDESKLQSAALNVCHLLENSNKMRKLRTVGASRMGKYARLGELDGTYLSNVYLVAKLIYCINTVVQFTSLNKFLKQPDMFWGASVLNDLVHGHNWEDSGNFPRIAMCDFEVRTMGNVQRWKGPQHMTGLLTLIDSLAHFITMKMPSRRQRFVKRFITCPPEEKAVLEDFTKEYLNPD... | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 416
Sequence Mass (Da): 47909
Location Topology: Multi-pass membrane protein
|
A0A0N4TDH9 | MVYSKKQTFRIVNWLLFIVASISWICVFIASVNISKRYIENLVHGNTKLQNTQQHIAVALPFLYSHYCSHYSLHSRHNEYREQAAVYYKQRFIILLKGKAPNDYYVWSSYPLLNHAEETHIRIAVIEEYESDFNDDGKPDL | Function: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling.
Subcellular Location: ... |
A0A023TLZ2 | GIWAGMDGTSLSLLIRAELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMRLNNLSFDQMPLFIWSVGITAFLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A811JWF0 | MTTFNIYWPKISGGEDVEGQMMDSSSSGYRRMGGRSAPPRNIFFFGVLLILVVLFSVFFLYLSASSDLTALRDEVHYLNDQISKLKSDLLNVNSQLEGSNNKLTACNVEIKQKTSELESCTTQKSADRTKVEALTKQNSELQIEKKAIEDEMTSKMAAMKTVGVNQEAILTKQNETIDLLRRDLILKDELIQKLQKNEANPVLNTDNGQAKSLDATSSSLNGQAGTIGRLSSVNDVNRQASSVNVLNGQSSRAVGQVTTTKFNENINVVLRPVENLNGGVMSNGQAQNIINNANSLKPIQNAMENVAPKPQEVAKPVQAQ... | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosoli... |
A0A158PDT0 | MSALFLPDKSLTCRIESTAMLYIAKYFPSLRYTILREKKCRLLINDISAIMAHREELEVLKNYGFDAAFAEQIDFCGIGVIRYIGIKNLLWISTTPIMDAVSYNLGIPAPPSYVPTIEENDNNDIMTFWQRAFNIYMYIGAIFIHRWSTNMMTEIFRKVDPDFPNIREIASNASLCFVNIDEMFDLPRPIIQKNVYIGGLGVQKPKPLDQKFSILMEKGEKGVIIVSLGTIAPFHAFKQVTKVAFANVFKSMLDYHFILKIEKGRSKEQRSTKFRNLLENRHEETNRMQDV | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 291
Sequence Mass (Da): 33616
Location Topology: Single-pass membrane protein
|
A0A183LI06 | MWRYVALFSGARKYCSTQSNYMLNELCIVVDKCDHVLGFANKKVILFGKSLLHRAFSLFLFQEDTIQKRSANKLTFPSLWSNTCCSHPIMNFPDELIESDAIGVKKAAQRKLFHELGINNTFVPLNRIHFLGRVLYTAPNEPCTQAAFAEHEVDYILVSVLDPVASKLFSCSSFPFVLF | Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
EC: ... |
A0A1C7L1W0 | TLYFIFGIWSGMLGMSLSLLIRMELGNSNPFINNDQIFNTIITAHAFIMIFFMVMPIMMGGFGNWLVPLMLGAPDMAFPRMNNLSFWMLPPSLMLLIFSSFIEGGAGTGWTVYPPLSSNIAHSSSSVDLTIFSLHLAGISSILGSINFITTTINMKPKIMKFESLPLFIWSVLITAFLLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A4P8JBM3 | ILILPAFGVISHVVSHYSHKKSTFGPLGMIYAMLAIGFLGFIVWSHHMFTVGLDVDTRAYFSSATMIIAVPTGIKVFSWIATLHGSRPKFEPALLWALGFIGLFTMGGITGIILSNASLDVALHDTYYVVA | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A0N4TTY9 | MLFTCTVHQLRSLGIRCLANSAGDSHTHYPISTVTRKSIDEVLEPSQAPTKIKVSDEVQKQTVDLSGVPVDFLRSRRVRIYRPAREATQSGWARTRTWKIELDNLERWENSLIGWSSTGDPLSNISMAMDFASKEDAVRYCETNNLNYEVIEPNERYVLFCYVLKLSGLPPGDYKMTTLSPIQCKRTQILGLEHLLRKLICTFASAIFYTNKAFIVFNFHVHIYYGY | 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.
... |
A0A0Q3GP92 | MEAAAAATTTNKAPSMADPEDDFDLSRLLNHRPRINVERQRSFDDRSLGDLYLSAMDGRSGGYMDSYDTMYSPGGGLRSLSGTPASSTRHSFEPYPLVFEAWEALRRSLVCFRGQPLGTIAAVDHSAGEVLNYDQVFVRDFVPSALAFLMNGEPEIVKNFLLKTLLLQGWEKRIDRFKLGEGAMPASFKVLKDPKRGVDTLSADFGESAIGRVAPADSGFWWIILLRAYTKSTGDLTLAETPECQKGIRLIMNQCLAEGFDTFPTLLCADGCCMIDRRMGVYGYPIEIQALFFMALRCALLLLKPEGEGNKDTVERIVTR... | 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: 564
Sequence Mass (Da): 63368
|
A0A811KMH8 | MSVCTNRWGFNLDKRKTSTLILVAVLVHTCTASITEKDVIDKSKQSEETTLNSKDFENAPSKEEDLKRIGIKVPDDPTMGSKNEGDILMPKLKEKVFLDERTGLGRNAIRQSYRKWPNNEIPYTLSTQYGSYSRSVIAKAMNEYHTKTCVKFVPRDTKKHRDYVYIHPDDGCYSLVGRVGGRQPLSLDSGCIQTGTIVHELMHTVGFFHEQSRYDRDQFIEIVWPNVINGADDQFEKYGTNVIDQFNEPYDYSSIMHYGPYAFSANGKRTILARRNGANKMGQRVQFSEIDLRKINRLYQCDSQSMIKKPPRPQLPVQVS... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
EC: 3.4.24.-
Sequence Length: 773
Sequence Mass (Da): 86510
|
I1IH32 | MAILACLLTVVPTILGLAIRRLRILLRFPSPHAAAGFFHPYTNDGGGGERVLWCAVRAVQDLCPGLPCAVFTGDADASPDGLAARALDRFGVRLLRPPQVVHLNKRKWIEASTYPHFTMIGQSLGSVYLAWEALNKFAPQFYFDTSGYAFTYPLARLFGCEVICYTHYPTISSDMVERVKQRNSMYNNNSRISGSIWLSRCKILYYTIFSWLYGLVGSCAHLVMVNSSWTRSHIVNIWKIPECTKRVYPPCDTSALQMLPLERSTMPPILISVAQFRPEKAHGLQLEAFALALQRLDPDSIKPKLQFVGSCRNKEDLERL... | Pathway: Protein modification; protein glycosylation.
Function: Required for N-linked oligosaccharide assembly.
Catalytic Activity: alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP-alpha-D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-... |
C4PV68 | HPEVYILILPGFGMISHIISQESSKKESFGVLGMIYAMMAIGLLGFVVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGIKIFSWMATYHGALISFNPSSLWSLGFIFLFTMGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAILAGIVQWFPLFTGLTLNNKFLKTQFMVMFIGVNLTFFPQHFLGLSGMPRRYSDYPDAYTQWNAISSIGSLISLVSVFYFIFILWEAFAVKRMNLSASSMITFIEWFQFLPPASHSYLEVPAVTSNF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A967RIF3 | MMEAAALGKPTLFGPHAFNFRQTVDALLEDEGAVMVKDEQDLLQTMQKCLTDADFAQKIANNGRQVIKKNQGATQKTIEQITALLNDRYI | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
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