ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A1B6LNW7 | FGNETEAAVFAKEQDLEEKEDLHKVALLMTNLPKQNTNRSRIVIITQGADPVILAKDGVTKEFPVTTLPLDKLVDTNGAGDAFVGGFLAQLIQGSSIDKCIDCGVWAATQIVQRSGCTFDGPANYSP | Cofactor: Binds 3 Mg(2+) ions per subunit.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.
Function: ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives.
EC: 2.7.1.20
Subcellular Location: Nucleus
Catalytic Activity... |
A0A0M9UCH2 | MLTGKRIVVTRSRKQASALSERLRALGAIPIEFPTIAIVPPADNYAALDAELQRLETYDWLVFTSVNAVEHVWQRLGVLGIPAEAVAARHIAAIGPATAATLEARGVPVNVVPEQYVAEALLEAIPNPAGLRFLLPRADIARAALREGLQAAGAEVVEVTAYRTIPATPAPDVLAELKRGVDVITFTSSSTARNFVAALGREDARTIAGTALVAAIGPITAQTAREEGLRVDVVAEEHTIEGLVQAILAAFTSS | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
A0A1G3IEC9 | MDRKILVTGSSAVAGSAFKTIRDDYAETGFIFSSANECDLTDIKQTITYVQDVHPAAIIHLAAVSGGIGLSMKRQASLMRDNTLMIFSVLEAARRSGVDKTIMTLSGGMYPAKAPLPLNEDNIHDGQAHESNYGYAFAKRLIEPAVRSYREEYGLSVIGLIPSGIFGENDNFNENDAPMLPGLIRRFYENRNAESKIIVWGDGAPLREYTYSSDIARIYMWALDNYDDPQVLNIGSTEEHSVKEIAFMIADIMGIDKGRIEFDKNKPSGIFRKNMDNSRFIGLSNFRYTPFREGLEKTISWYVETAENNPEKLRLYERSC... | Pathway: Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 2/2.
Function: Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction.
EC: 1.1.1.271
Catalytic Ac... |
A0A1B6KQP2 | MHKLERPKNTYPQVRASLLFAAATLIILLVSSTQNWLSYLFDEANAQQNGNDSSFNTSLTEVGERRSIQDFIEVSEILPNCGIKEQCPEDSFPVHIYTGQDKDDQPKLCIHGKYLIGNNINGGGRGLNAAIVDAVHFQVVAVHNFDLYSQNSTSLELWLAKQVMDNDIIIVFTFDEASKELSRKAKMSLYRLGSGKIQDLQFRSQWYMISQKGINGFTSLEKLTFAKNEHWGEAIDERLCVPRQIPAVTIAPDPPPRANPLRENFCDSVKKMKCKEFCGAIAQHEAIYPALLTNRSLIGNAVYSTPILVVGGTSLASLSL... | Cofactor: The cofactor is mostly bound to the substrate.
Pathway: Protein modification; protein glycosylation.
Function: Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.
EC: 2.4.1.101
Subcellular Location: Golgi apparatus membrane
Catalytic... |
A0A2H9NVM7 | MKKNVQNAHNTLEEKGVLVRIAGPVVVARGIVARMYDVVRVGNEKLMGEVIQIDQEKTIIQVYEDTSGLVPGEPVVNTKEPLSVELGPGLLRSIYDGIQRPLPVLKEKMGDFIKRGVYAPGLDHKKKWEFVPTVRKGDYVGPGGVIGTVQETETIVHKVMLPSAVSGKVASVRKGSFTVDESVATLEDGTEITLMQKCPVRVPRRVQQKLSPKVPLITGQRIFDAFFPLAKGGVAAIPGPFGAGKTVSQQQLAKWCDADIIVYIGCGERGNEMTEVLQEFPHLKDPRSGKPLMNRTVLIANTSNMPVAAREASIYTGVTI... | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal alpha chain is a catalytic subunit.
EC: 7.1.2.2
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Sequence Length: 363
Sequence Mass (Da): 39721
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A0A2K3MB17 | MEEDQNETEPPNSDPVLNQQTPEIGGSLAETSRESFHHVVNLNTGQDVMASLYEISAHYRRDVCVLCAAGAVSSVVLRSSLGTFTRREGHFEIMSLTPTDKPGSFFASFADTNTGRVFGGVVVGSLIASGPLHLNVSDFKQSKEILKKNSANSSASGNSGSEVHRMLLTGESSGSSSLKTSEPLPTETTDHDTLPAGGGVSDNVSINPANAQNMNSASQNQ | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Subcellular Location: Nucleus
Sequence Length: 221
Domain: The PPC domain mediates interactions between AHL proteins.
Sequence Mass (Da): 23299
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A0A2K3KYS2 | MSEAENSNGCFDCNICLDFAHEPVVTLCGHLYCWHCIYKWLHVQSDDSLGVDEHPQCPVCKDDISHTTMIPLXVQSDDSLGVDEHPQCPVCKDDISHTTMIPLYGRGGHAPPSAKSSRCDDSFIPPRPTASGAQALLAKVSQSEQQQQLPYRNPYRGQYLNSSLYQQEDDATSQMLNLGASMTSGSHHHPLVGMFGEMVFAGVFGNSPNSYQQAGTRGMPYAWL | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase.
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
Subcellul... |
Q5AN96 | MLAKFKLPNAEVWKTFPPFDTPVPPSPFENEFLNKIYYASMNVTTPLTIAIIYFTSVHFINSIIRNKQIAKYNSKTSSESKVDITKLDDKKLQKILPTVPNSIAKTSIFKLFVFLHNVFLCLYSIWTFLGMSHTIATTMNLFEGNFLQSLVNYQPKKLDIFLHSVCDPKIGIFSRLLTNEKGLHNLEVFGWWFYISKFYEVLDTAIILLKGRPSSLLQSYHHAGAMMCMWAGIRYQSPPIWIFVVFNSFIHSLMYFYFSLSCLKIRVPNFFKRILTTMQITQFIVGGSIAILHSFVWIVDTSHVISPDNLKWVSCISTPD... | 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: 353
Sequence Mass (Da): 40672
Location Topology: Multi-pass membrane protein
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A0A2S6FV53 | MELIESLKSLLNKKYTEDKPLITFMTNYVTVLDLVDCCVYAGGSPVLTDDIVESHNLIPHAGVNAVMFNFGTITRQYLDIMVNIGKSANKFNVPIMLDPAAISASPFRGEAIKRVLDEVHISILKGNLGEIKTILGYEAKAKGIDSFEDESDGEECCIKLAKERNMIVAMTGKEDIITDGKTLVKIKNGTPRLQKVVGTGSLAPAH | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1.
EC: 2.7.1.50
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Length: 206
Sequence Mass... |
A0A2H9NVX3 | MAYDVEQKNEYMYEVKKQGNMHVPLRIYASKKIMEQLKGDNAIQQGINVACMPGIIGQSIMCPDAHQGYGFPIGGVAAFDAATGIITPGGIGFDINCGVRLLASELDRKDVEPKIVALVDRLFANVPCGVGESSDFLRLSPEELDRVLELGTEWAVKQGIGNEEDRARCEQQGRIESADASKVTPRAKKRGRTQLGTLGAGNHFLEVQYVDEIYDEETARVFGITRKGQIMAMIHCGS | Cofactor: Binds 2 manganese ions per subunit.
EC: 6.5.1.8
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + GTP + H2O = a ribonucleotidyl-ribonucleotide-RNA + diphosphate + GMP + H(+)
Sequence Length: 238
Sequence Mass (Da): 26051
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A0A971HWJ6 | MSTFIQKKTDVEDAQASMTFRPGQFRRPPFQLQEKNIYLIGLRGSGKSTVGQALAQELGCAFVDTDQVVVESCKQSIEAMVVDQGWKFFREQEKKALAQVAILPGKVIATGGGMILDAENRALMGQTGVCFYLAADVTLLVDRVQKDTQVQRPA | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
EC: 2.7.1.71
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Length: 154
Sequence Mass (Da): 16915
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A0A1B6LP40 | MMMNGLTNFGELLKTHVIAGFGNPLLDMYTTIKGKTILDKYNLQPDGQKEVSNDEFCSLLSTLQSENYSTTQSPGGCAQNTLRLVQMLVNHSFFCVLFGGVGDDVEGELLESEVKKCGVDTRYARNSAYPTGRVVSLINGENRSLVAHLGAAEVYTTEDFVTDDNVKIMEEVSIVYIEGFFITHSFDVSLEVVKLCGNFSVPVVFNLSGAYLAEICPQQLTAMAAASDIIIGNDVEYRALANILGLEDSSVEDIALKVHCSLWGNNLKLKCRSSHLERFGKTVVMTRGKTSVLCVCSDRHLIKFEVPYLDTKLIKDSTGA... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.
Function: ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives.
EC: 2.7.1.20
Subcellular Location: Nucleus
Catalytic Activity... |
A0A074YS58 | MYSNLVQRCFEHCVDDFTSAKLSSKEEGCTMRCVDKFIKGSERLGQRFQEQNAAMAQSGSLMR | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer me... |
A0A1F8ML48 | MAVVFKEPAASERELYVVGMGELVVTDSPDAVLSCIGLGSCIAVCAYDSQEKIGGMAHIVLPHNTGLNGVNPAKFADTAVPLLINEMIKKGGIRSRLIVKIAGGAQMTLAPGLRDTFKTGERNIAQVLLVLQRERIKPAAADTGGNIGRTVRMYVKTGHVTVKTAYGTAKEL | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
EC: 3.5.1.44
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Length: 172
Sequence Mass (Da): 18175
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A0A3S3PCB5 | MMNSFKLLKVILFVKIFSVNATTKLPQVFLDVNAEEEVLGRIVIELRSDVVPKTAENFRALCTGEKGFGYKNSTFHRVIPNFMIQGGDITKHNGYGGMSIYGKSFPDENFILNHTLPGIVSMANSGRDTNNSQFFITTVKTCWLDGKHVVFGMVVKGMDVVKKIESYGSSRGKTSKKIIVTNSGQV | 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: 186
Sequence Mass (Da): 20607
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G0SG79 | MKLPIGHSVASQRPTQSSGKLADDPNDPISHACAYISLVPQALLVVYVTLLWATREAEVFLTFAGQLGCELVNYILKHLIKEERPLRKWVLSENLSEDRAVGSGYGMPSSHAQFVFYWAFSVTLFLMVRHNPSRLHRVEGIAAAASEDKDGECDNNEQRSTSSEPPSLRTIQQAYRAGGLAAASASIEAYSHGPWTLTQRVIVSVAAFTIAILVSWSRVYLSYHTPRQVVAGAVAGTGCAIAWFAVTYVLRETGMLAWALELPVARWLRIRDLVVEEDVCQPGWEVWESRRRVTMQKERERERNKKKGE | Pathway: Protein modification; protein glycosylation.
Function: Required for efficient N-glycosylation. Necessary for maintaining optimal levels of dolichol-linked oligosaccharides. Hydrolyzes dolichyl pyrophosphate at a very high rate and dolichyl monophosphate at a much lower rate. Does not act on phosphatidate.
Cata... |
A0A2K3KIZ5 | GCDASVLLNNTDTIVSEQQAFPNNNSLRGLDVVNKIKTRVEKACPDVVSCADILALAAEASTFFNIRNSNLTPDVPTN | Cofactor: Binds 2 calcium ions per subunit.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Length: 78
Sequence Mass (Da): 8335
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A0A068VKT8 | MSWIPDLHIGRFGKFSRGVPLSTLTEQVVRQVGEISNTLRMVTKEAITQIDPLIITQASLQSAVPVESSSTDVVAVISKSSEFPDDALFLEISRILMPGGSVLIFGKKSSWKIGSYFSLKKQTKSLPAVQIDDDTDLIDEDTLLSDEDLKKPQLPVGDCEVGKTRNACKNCTCGRAEAEEKVKLELTMDQLNNPQSACGNVLKGLHLKPGGLLNLTSCGLGDAFRCSTCPYKGLPPFKMGEKVTLSQNFLAADI | 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... |
A0A0N8GS93 | MVHVKIGEVAFAEAPDVVLASYGLGSCVAICLFMPKLKVGALMHALLPHPPSTLQDAHNPYKYVRLGIEALVNDFKARGISPRRLVAFIAGGANMLKSAPLDIPAMRVGERNVEMAHEVLSEMQIPIIAKDVGGQRGRSVVFDPSDGIVYVKTLEETRMHRLM | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
EC: 3.5.1.44
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Length: 163
Sequence Mass (Da): 17757
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A0A914K0B9 | MIISVIYRFALDKEHQSTFAKVAAYIDENMDYIPLTFLLGFFVSVIFGRWKDIFSHIGFIDRAAFFVTNYIHANDEEEFIVIKRNILRYLCLTQVMVLRDISVPVRKRFPNMQSVMDAGFLLPNELKSMEKVITEYPKYWMPINWAISLAIKCRKEGKILADVFLNTTCVEIASFQEHLRILLNYDWVPVPLAYPQVVFLAVRVYFILTLISRQYIIAEDDPHYSKVS | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 228
Sequence Mass (Da): 26738
Location Topology: Multi-pass membrane protein
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A0A914JIE3 | MKIEEDDRMKNIWKYYCYIGIIIWMFSTIFHSRDFWLTELLDYFGAFGIVCYTFYVSIIFTFPWLQRNQDGLKINYFIAGCLIAFYSTRVLLFLTGIDYGLNMFYCIILSIITGIIYITWILKEIIQGKKRESLKYLGIIIGIGLISACFEILDFPPILWIIDAHSIFHALTIPTPLLLAKFAYEESEYEQGRRKMVIGKYV | Function: Involved in the lipid remodeling steps of GPI-anchor maturation.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 202
Sequence Mass (Da): 23798
Location Topology: Multi-pass membrane protein
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A0A7S3VHU6 | MGVGNSKLEKALAESSDEERFYGLENFGNTCYVNSVFQALYFCKPFRERMLQYAEQRKGNTDDLPGCLAELFLQISSSKKKTGVISPRKFVAQLKRDNELFSGYMHQDAHEFLNYLLNQAAEVLEEEVKQQRQVQGGGAVMKMQQQPQEPIVTWVHDIFQGKLVNETRCLQCETVTSREEVFMDLSLEIDQNCSLTSCLRNFSAMEMLDREDKFYCDHCCCLQEAQKRMLIKEAPKCLILHLKRFKYIETQGRMRKLMYRVVFPLELKLSNVLPDSQGADALYTLFAVVVHVGAGPHHGHYVSLIKSHASWLFFDDENVE... | 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 ... |
A0A2A6FRJ9 | MSLAAITAEPVVPVPHARSVFLPTEPAGTVIPMPKHRKDWRDYAACTDKPAEMFFPGKGQPTKPARQVCASCDVREQCLQWALENDEQFGIWGGTSQQERRRLQRKSQQSRPQNDKRRTGRAPNPEITKRNEEICQARANKIGVEELSVKYSLSVNTIYRISGRVRRTKTEAQENQA | 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... |
A0A068U7C6 | MFLYALTFFFSNFGPNTTTFTVPAELFPARFRSTCHGISGAAGKLGAIVGVVAFQWASPDNYHQPGIRMTAPLVLLGLVSLVGCVTTYLFTRETMGRSLEENENEDQACGSGTGWGLVRHFSFTRCSLPKLCANNEVADG | Catalytic Activity: NH4(+)(in) = NH4(+)(out)
Subcellular Location: Membrane
Sequence Length: 140
Sequence Mass (Da): 15150
Location Topology: Multi-pass membrane protein
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A0A3N0ZV27 | MILSHKIFGVAGKPILHSKSPDIFKYISMKYNILDNSYIRIISDSARETVEIMKSLDICGLNITYPFKADILDYIDEISKEAELISSVNVIISEDKRLIGYNTDYLGVINSIKEKNIDVIGKRCLVIGCGGAGRAAVYGMIQSGMKVKIINRTNDIAKDFANRIKCEFAEWNCLVDEINNSDLIINTVPSGELNIDEYLTEGKYILQADYSKLSNKLQGDVISGIHWLVNQAIPSFEHFTGVNLREDNEVSESLRGFLEPSNPGVQKKGNIALIGFIGSGKTTIGKMLAKKINWDFFDTDEMIVNEENIPIKEIFRTRGE... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
S... |
A0A1I1PM31 | MDSFFVSVECREDNSLKGKPLLVGGMGDRAVVAACSYEARRYGIHSAMPMKIALKLCPHAVVRKGDMELYSNTSREITDIIAGRAPLYEKSSIDEFYLDLTGMDKFFGSMKWTIELRQHIMRKMKLPVSFGLASNKMISKVATNEAKPNGQMEINFGNEKSFLAPMPVEKLPMVGKETAGQLRRRGVETVKTLSEIPVALLEAWLGKNGISLWNKANGIDESPVVPYHEQKSISTENTFSTDTIDMQFIHAELVRMTEKIAFELRQQDKLTGCVTVKIRYSDFETVTKQMTIAYTGSDHVLLAKVKELFNKLYDRRLLIR... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
A0A7X8D7W1 | MQNNINAELYEKTNELPYLIDFARIPLQDILRNRHFEDPLHMLLKSLAYSSLIKTYLSPLSGVLPSFERKELFRALSSAIAPASYQYIAFQNILKKLFNMDVSAFIEDFDAAYDDICGKLRHSNLGTNGILNSLNIHSMHIITDISEDTRPFTLINSDELLHFPVAPTADLSKLCKINSSSFSNALKSISASVNRPITSFDELIKAIEERIAVFYSMNCKSVYIEPDYFPTSKINLENADGVFKSVANGTKVSRKISAGYKAAFIFSVARICAKHNILLSIKPPCGDEPILASIKRIVDRLVKTSSMPRLMIISNSFQQY... | Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
EC: 5.3.1.12
Catalytic Activity: D-glucuronate = D-fructuronate
Sequence Length: 426
Sequence Mass (Da): 47677
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A0A443RLL9 | MSENCVRHTRCPNVICDLCSYECTIDNLGVHFESLRHKDRYKRLHDHLYLLALPYPTDAHLEALTSAVYNFVSDALKTEDFEKRFHSVQRFDQIVKSLSNTCTVRVYGSTINGFGLKNSNVNVELIRNGEEIVETPGEFLKKLADFIQQVQTPNFYYSEVIKEFDIKIPRLHFIEVVPRTSRLQFELSITAEKSFKASNLLLKYSLFDERAHILGLALRKWAKIFRFDNQESGTWPPHTFPILVIHYLQQIQPPVLPCFHEMQTEKAPTSETTESSEDDASTDVNEDEFDLIKHKWVSRNTKSVGELWIGLFRYYIFDFL... | Catalytic Activity: RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide
EC: 2.7.7.52
Subcellular Location: Cytoplasm
Sequence Length: 961
Sequence Mass (Da): 111951
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A0A914JZU2 | XIMFFMALVNATSNVLFMPYMATFHPTYLTAYFVGMGLSSLVPSFFSLVQGTGNYECHKNETTGEVIPNYFAPNFDVRGFNLIMFVWMALTIISFALLHWGRDWISRKKKPTEEGDDANEPQTDEFSPLNTVSGNADTDDRGNFTRYCILLVCLAFICAQMNGVVPSVQSYSALSYSQLTYHLALALGNLAQAVACFVPLWIQPRSVWILVLLTVIASSFCGYIVYLAALSPTPFLLHSFWGSFFSVGASICAAAFHAYLRTVFTSXXXXFSPLNTVSGNTDTDDRGNFTRYCILLVCLAFICAQMNGVVPSVQSYSALS... | Function: Plasma membrane transporter mediating the uptake by cells of the water soluble vitamin B2/riboflavin that plays a key role in biochemical oxidation-reduction reactions of the carbohydrate, lipid, and amino acid metabolism.
Catalytic Activity: riboflavin(in) = riboflavin(out)
Subcellular Location: Cell membran... |
A0A4Y7LLQ2 | MGKPRDKKYKEKNKGRSKADDLKNKHTEWSENEFGGKLEKLNLSEAENGDTGSNSGDSSEDSGEASLEVNFPVAMWDVAQCDPKKCSGRKLERFSMVKILRLGARFNGILCSPLGEKCVSPADRDIILEHGAAVIDCSWAKINETPFHKMKSPNPRLLPYLVAANPVNYGKPCKLSCVEAFAAVFYITGFIDVAKLYLNKFKWGNTFLELNSELLEKYAACKDSAHVILTQQQHMDLFWPPEDFTSLCNLEICDLSSSNILMVPKDFGNLGNLTHLNLAFNKVPLIPKSFQLLENLEFLDLYMNEIEVIEANLALLPKLN... | Function: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine in 18S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi).
EC: 2.5.1.-
Catalytic Activity: an N(1)-methylpseudouridine in 16S/18S... |
A0A914KEF2 | MLFKVPSNLIAPFSKLNTDPLDDKFDRLSSAISVYILIFCCILAGTKLYVGEPIQCFSPANVPGTWHDFYTAYCFIQPKSKIPKNFTVGYDDVKNLDLEVSFYPWVPYVLILQAICFYLPKFYWNATSSKFSIDLKSILKESKQVCGTKDNDERSKRVTVLASYTLSYLRYVYGTRCGILVPKAVFFYITKKFLYFVNAFAQFYFITHFIGKGNYLWGVESLSNIISHEPWSFSLFFPRLVHCDIGYVQDAXXXXNHCQTSSAMNLGVFRCFFHVWFIVILVTFKMLXXXTYGSVVAETLLYEMWEMHQQLRPKATVFNY... | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 408
Sequence Mass (Da): 47111
Location Topology: Multi-pass membrane protein
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A0A2K3K7C0 | GEWWNANVEEVERNATDTGNPPLESIASTINGFPGDLFNCSQDKTYTLKVKRGKTYLLRVINAALNEQHFFKVANHTLTVVAMDAIYTEHYNTDVIVLAPGQTVDVLLRTNQAVDSYYMVFTPYRSSNVGTNNITTRGVIIYDGANSTTKTPIMPILPDEHDTPTAHKFYTNVTGMIK | Catalytic Activity: 4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O
EC: 1.10.3.2
Subcellular Location: Secreted
Sequence Length: 178
Sequence Mass (Da): 19848
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A0A3P6S1X5 | MTAAEDEYICINCCHPSSSLFLKYSDNGIRLTPCSNCGKAVDEYIEYDTVLIIIDLMLQYIEAYRHFLMNTNNRVTFLLFRTM | Function: Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 83
Sequence Mass (Da): 9671
Location Topology: Multi-pass membrane protein
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A0A2K3N8A4 | MRAGRNGPLISHLMFADDLLLFGQATDDNMTTVMDVTPKFCKQYARVGDVINKALLDYKEAVINGSFPDVQHSPYKISETDGNGFLNEVQKLGFDKAASAASEAVIRRWLQNQQSDNLVKLPIAPSFFI | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
EC: 2.1.2.11
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Length: 129
Sequence Mass (Da): 1... |
A0A443QAZ7 | MREKGALLALLAGCGLTLTLYTLYVELQHERNRNYKALCDINEHMSCTKAFTSRYGKGFGLFDTQSHFNIPNPVYG | EC: 1.17.4.4
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 76
Sequence Mass (Da): 8603
Location Topology: Multi-pass membrane protein
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A0A2S2PCH8 | MVLCPEENKPLTLYHLIRSKGLKRVICFVKSKIEVHRLTRLLCKLSEFDENNSPLRVNEISSDVSQKAHSGYIKQFSDGKIDILICTDSLARGIDIERISCVILYNVPKYPKNYIHRIGRTARAGHKGKAITFVTPEHKELFENVLSSAGKTSLKNMKVKISDLEQYEQMYIDALKAVKTESTQKPKTVRKRRLRKNKQPKK | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 202
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): 23239
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A0A2K3M9B8 | MDGKVQLQKQLFDYTASLFQEGFLDNQFNQLEQLQDESNPDFVVEVVTLFFDDAERILNELTTSLGQEXIDFKRLDAHVHQLK | 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: 83
Domain: Histidine-containing phosphotransfer domain (HPt... |
A0A2K3JPI6 | MADEVILLDFWPSPFGMRIRIALAEKGIKYEYKEEDLRNKSPLLLQMNPVHKKIPVLIHNGKPIAESLIAVQYIDEVWNDKSPLLPSDPYQRSQARFWADYVDKKTLFPLVDAFPF | 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: 116
Sequence Mass (Da): 13530
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A0A646RSU9 | NXXYGWLLRNLHANGASFFFICIYLHIGRGFYYGSYLYKETWNTGIILLLTLMATAFVGYVLPWGQMSFWG | Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membra... |
G0SGS9 | MAPKRSSARGRSVSPAPPAAAPSSTTTTSINTSSTTPAVTTAPQPAPQSTPAPAKSKHSSAPPSFQKIVSNVVDHYLRTTPQRTKLLDAFMAFLVAVGGLQFAYCILAGNYNQWTDGQFGRAFADYIVCSLILHFFCVNFIN | 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... |
A0A2K3P920 | MIMVPKNATAQNCGCNGLCCSQYGYCGSGDEYCGTGCKEGPCTGQSSPSPTNNVNVADIVTQDFFNGIINQADSSCAGKNFYTRASFLDALNSYDQFGRSGSEDDSKREIAAAFAHFTHETGHFCYIEEIDGASKDYCDETNTQYPCVANXDADFCYIEEIDGASKDYCDETNTQYPCVANKGYFGRGPIQISWNYNYGPAGQDNGFDGLNSPETVANDPTVSFKT | Function: Defense against chitin-containing fungal pathogens.
EC: 3.2.1.14
Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Sequence Length: 226
Sequence Mass (Da): 24473
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A0A2K3LH29 | MRVRWGGGDCDESELEWYGGGCDGSVLRGHGSVGSGAVGVWLMSSLCIYLAYSTSVVTILEGRLRAETCLPRVQIALKLKGIEYKFVEENLAIKSDELLKYNPVYKKVPVFVHNDKPISESLVILEYIDETWKQNPILPSDPYQRTLARFWSKFIDDK | 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: 158
Sequence Mass (Da): 17864
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A0A2S2PKF0 | MDLEELYHKYRIRLKQSLFTTFASIGLVVSTITLIMLILFYNAESAVRSPFLSVSVAWLTFAFTFCLTQAAPTALNSRPAVAALSAATVAASATAVLSSSSVAHAAYALVPIMVATHSMVPTHVTVASFATAAMVAVHIMSLLAETQWTPNAQHVKQMIAEIILLFSASSTGWYYKFMTHKANRIMFSGTRTCIESRIKLECEKEQQEQLLLSVIPAYIAAEVKRSIMLKMADACQDDVANKQTRFHEMYVQRHNNVSILYADIVNFTPLSEQLSASDLVKTLNELFGRFDQIAQDNQCMRIKILGDCYYCVSGLPVSRP... | Catalytic Activity: ATP = 3',5'-cyclic AMP + diphosphate
EC: 4.6.1.1
Subcellular Location: Membrane
Sequence Length: 738
Sequence Mass (Da): 82634
Location Topology: Multi-pass membrane protein
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A0A914FIZ3 | MSTIWEFVKRHRGKIIASGAFVGSVYAAKKVYDSEYVKEYIQSPSHQEHEVQLSSARRHFIFDAHQQSCDKNLVESIADIKAILKSRYPVEILVESLKDSDAISNEQKIQIWEDIKHKSISRIVSTSVALSIIIIATKIQKSILCSEMCKIVEETRQKQTSATHGIIVSTSVALSVIIIATKIQKSILCSEMCKIVEETRQKQTSATHGIINLGLNQIFTKIEAITEESLNNFSLTKKVTVSEVETLIHQILDKFEKEAGAKNYCDYIVPVTNVRTKFDGNDATQLENLLSRFVNLLQIQTCRQLMHKFVRIFIQKAITF... | Function: Involved in peroxisome biosynthesis and integrity. Assembles membrane vesicles before the matrix proteins are translocated. As a docking factor for PEX19, is necessary for the import of peroxisomal membrane proteins in the peroxisomes.
Subcellular Location: Peroxisome membrane
Sequence Length: 397
Sequence Ma... |
R6DVE2 | MKKQILIPTVALFIICLVATTLLALANNVTAPIIEKNSAESEAQSRMEVLADAKSFEDKTLNGISYAVGLDGSKQTVGMVFTTTSKSYGGDLLVMTGVDNEGKVTGIQILSISDTAGLGMKAQTDSFKDQFKGLVDGIKVAKNSADHDNNEILALTGATITSNAVTTAVNEALANYKTITENGGAN | 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: 186
Sequence Mass (Da): 19420
Location Topology: Single-pass membrane protein
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A0A4R3KMP2 | MGGNYIEVIFTLPQPGSIQQDLLIAGLGEAGYESFLETEEGFNAYIRQEAFSDGLLQAAIREVPGDSLGYEIKLVEARNWNQVWESNFTPVVIGDTCRIRASFHEPDPSVPLEIQIDPKMAFGTGHHETTWLMASWLLELSLPHKKVLDMGCGTGVLAILAAKTGASQVFAADIDPVCVESTVENATLNEVPVQPLLSDIDALPYSGFDLILANINRNVLLDHLPFYAEKLNDGATLLLSGFYQGADLEAIRDRAGECGLTFTETRSRNKWAAAQFRK | 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: 278
Sequence Mass (Da): 30490
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A0A220EKD7 | MFGTWAGMVGTSLSVLIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLSGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVAITALLLLLSLPVLAGAITMLLTD | 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... |
A0A1B6M0V9 | LVPCWRILGCLECCFIVLTVLCLFKLTACPYFTDCIAFQIHFLSSLSMEDYQNMLAAIEETAKCPVCLERVRSPTTLCNNGHAICRQCKQLQKVCPTCRAPFSRINPVFLNTLIELLPSQCRNSSRGCDKVLSMECLSDHELQCEYRLERCRVRGCSWHEEVTQLLDHVGAQHPESLLSPCTTTRVPDFIVSDEEYSASLVTLEDSLFWVYITNNFYKKQIPVFVQWVQRGVQVSRCSCDVRVVKDHFSFCYSQPVTTVEPVEVTLCSTLAKQFLVTPNSIFPNFVSSKYDVEIKFNLRIDCDNS | 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... |
A0A1D8PFE0 | MPLNTPYPVEKNTFNISDEDDDFPTRNLNESSPLTQSTKRYMKQDFANSVTSLPSLPPKPSHLQPQNRPQHQQQQQQQQYPYGNLSAKQSNKHKQMFENSVPETNKKDYLGNTTTVRELPPIPDNEKLHSKNPFSDSRYASRDYDDVDLPPSPPHSDPFRNDEISDDDSHSDLKHKMKRNEKNRIRSLRRKPRFHYTKLPYFTMVISLIQIIVFIVELAKMAHLTGSAFQTKPYFNPMLGPSTFLLINMGARYVPCMHQIKDITDDTSILFPCANSTSVDTYVCSLSELCGLTKLKLSSDGSAYLPDQWYRIFIPIFLHA... | EC: 3.4.21.-
Subcellular Location: Membrane
Sequence Length: 669
Sequence Mass (Da): 74839
Location Topology: Multi-pass membrane protein
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A0A2K3L398 | MSYDVVGAQIIQTGIPSSKANLIGTTEVAVASLAESLMLGVAIIANDPSHFGCLAILSLLSVVGAACMFCRWLSNPTDEQKSLFAYHPQF | Function: May be involved in iron transport and iron homeostasis.
Subcellular Location: Membrane
Sequence Length: 90
Sequence Mass (Da): 9502
Location Topology: Multi-pass membrane protein
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K8WYE3 | MPNHININMPIASTSTAQHEQTHCDTRALVGNIRAVRESNEDINKKAGLFPCPSTEVKSKEINQKEYLEDWNQWLKNSPDEEKYSRSIALSKLKKCIFHNECTLDLSRLSLTSLPKLPPCIKTLSCERNRLNELPDLPKGLKYLICHSNNISVLPELPERLESLFCNNNQIRTLPKLPKYLDRLICTKNHIITLPKLPDTLTELRCDNNNLNVIPQLPNTLEILDCADNRLSMLPKLPDKLYSVNCSDNNINELPKLPDNLKYFLCSRNNITSLPNLPHGLFFLHCSSNHINMLPNLPHGLINLQCSSNRINMLPYLPSS... | 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: Host cytoplasm
Sequence Length: 713
Sequence Mass (Da): 82087
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A0A1B1PNA9 | MTFLNLLRRVERTILVALFLLMVALFFGSVVMREFGGTMASRFAWIEEAVRLMNLFLVFLALGLALERGKHVGITNLRDKLPEGARRWLLRLIDTVGLLFSLYVAWLGVQMVEFVLKSGQTSPTLGIPMGLIYLAPVIGFLLLALRYGLSLFGVIDRFAAQAEVE | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 165
Sequence Mass (Da): 18492
Location Topology: Multi-pass membrane protein
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A0A5P9IYT1 | MFANFNVEKAQKLIEEKLGGWLETAISHIPNLVVAIVITIVFALLARVLGSIISKVLKRSLDSEQIAGLMTSIVKILILTLGVFIALDFLGLKGTVTSLLAGAGIVGLAIGFAFQDMTENLIAGVAMGIRKPFRPGDVIESGDVFGTVKSINLRNTLVENFYGQLIIIPNKILFRNILTNYNYLGTRRIEVPVGISYGDDIEAAEKAIVEHINNLDFVIRKEDTAVYADGFGDSAINLLVWFWIAYPNDDPGYMEIRNQAYITVKKALDSVDVTIPFPIRTLDFGIKGGEKLVQMLPSQSPEEGTHKQRGQDEKPGEDSE | 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 con... |
A0A074YQ32 | MRFSEHFICNSCFEKLTLSSGMLDLVIFLRASFLLAAIAALLTHIVPSLRTRFLAYGSRQNGQQPSKLSANPLDALATLQVPHGWFGSFYVVSTLCSFIWFSQILLDQSLWRNLAVLTTFNKSMTLDQVIVTWVLMLLQGVRRLYESLEFTRPSSARMWIGHWALGMWFYASMSVAVWIEGSPTLLKESFEFSHLTIEPPSLRTFVGCLIFILASGVQHDCHAYMASLKKYSVPEHPVFNHLVCPHYFAECLIYFAIAIVAAPVGAWLNWTVACALVFVGVNLGVTADGTREWYVQKFGPESVGGKWKMVPFVF | Pathway: Protein modification; protein glycosylation.
Function: Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-gly... |
A0A8S9W4C2 | MIELKDVYFSYPSGAVLEGIDLTVKKGEYVGIMGHNGSGKTTLARLITGLLLPGKGYVRVNKIFTTDSERLLDIRRSTGMVFQDPDAQAIGEIVEEDMVFGLENLGLPVPEIDTRIEKYLDLLGIRELRHRNIRTLSGGQKQLVNLAAVMVMEPECIILDEPVSMVDARCRKMILQHIARLNHEGTAIVHITHDPEELIWCHRLIVLSRCRVTNQGTPHEVFGQLLDEKKMDVPAPYAISRKLGLPPALTIKALLEELCRSRSGN | Function: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system.
Subcellular Location: Cell membrane
Sequence Length: 265
Sequence Mass (Da): 29614
Location Topology: Peripheral membrane protein
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G0SB96 | MAWTVFACIHIVIRQFRLKDDPNLVLGNNVFIYVVMSTISTIGPCFVMSFMYLDPWRMFTSFLQYLILLPSYICTLQIYAICNTHDVTWGTMSDNLNKTDLGIAKGDGSKVVLETPSKQLDIDSGYDEALRNLRDRVEVPKQLSPRNSCSKITTRASVPTWC | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Subcellular Location: Cell membrane
Sequence Length: 162
Sequence Mass (Da): 18425
Location Topology: Multi-pass membrane protein
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A0A068V3A4 | MGVVVIANPQPHFSCSTFSFSIRQAPHPKSSCLRIRPGFSSRRWLNCPRLIPSRLEHFHPKCSATETDVFNQLATEEEISEDLTASESNCSVQIVHLKSDVLETEALNLLAEGTFVDMLLTALPVLSEEEQNIIAATPAHPAGLYALYANCLAGNVVEQLWSFAWPASIALLHPSLLPVAMIGFFSKLAVIVGGPLVGKLMDHFPRIPAYNYLTIAQAAAQLLSIGMIIFAHTICPTSTSSILLRPWFVILVTAGAAERLSGLALGVAMERDWVVLLAGTNRPIALAQANAIISRIDLLCEIAGASVFGILLSKYPLVAC... | Function: May be involved in iron transport and iron homeostasis.
Catalytic Activity: NH4(+)(in) = NH4(+)(out)
Subcellular Location: Membrane
Sequence Length: 593
Sequence Mass (Da): 63639
Location Topology: Multi-pass membrane protein
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G0SB50 | MDIPRPRSSGFPAPRRVVTAPVPQSTPQSPSSPQVSSGLVDTLYVHPNVKIVSFTATGRSLSVGPRTASVHEVEPGSLPWTSQLERTIAVGSFKIYRAPGSVAFLSCGSALQPILPKSQAWCVDVESSKFVLQIRRPQYWRIEVPVKEEEEVRLALQLREVFDAILLFEKTPCPFQRPFTVELPELPKTPVKKRPWTPARRSSASLPLTPVTSVEIARLHHGTPRGSFCVSDLRSKKEAAKALSEHGRRLAVPEEEETSGGDKPTSSQPIVITQPEARITKPIETSNVPREPQRNQAWLSVPLPPSPPLSSPGSPLLSRL... | Function: Required for peroxisome inheritance.
Subcellular Location: Membrane
Sequence Length: 706
Sequence Mass (Da): 77092
Location Topology: Peripheral membrane protein
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A0A1B1UE01 | MALPAFAQKSASANEEAKATFVGGKGEQIGKGELVQMPGGVLIKAELRGLPPGEHAFHIHGIGKCETSDQFKSAGDHFAPLGHKHGYASEGGYHAGDMPNQFVGQDGTLRLNVINANVTLGSGKNSLLDQDGSSLVIHAKPDDYKSQPSGDAGDRIACAVIEK | Cofactor: Binds 1 copper ion per subunit.
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: 163
Sequence Mass (Da): 16961
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A0A1B6MV37 | MQTKLKTFDLIAYAGYKYVGIIIALLLSIVLNKTGYYMGLLYCGFSLAFFMMRSLKWQVLAEVTTTNADSYSNYATTGNKRRLYFLLCMACLQPILMWWLSAHLVPPPLPPIPPNLMQS | Function: Has a role in transport between endoplasmic reticulum and Golgi.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 119
Sequence Mass (Da): 13554
Location Topology: Multi-pass membrane protein
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A0A2K3MDK3 | AAHRGPSVNIMEKLTADNHFHIAVGMIIGPGIDSDLKDVQHTGVTLFMPENAAYGKLSNSRYYNLHTLQSAKIPSQMTLASEDKKAPSFLLNISSINGSVVVISTGVVEAVITRTVFDHYPVVIYAVSKVLLPKELFGTIPDDDAPPPRCV | Function: May be a cell surface adhesion protein.
Subcellular Location: Cell membrane
Sequence Length: 151
Sequence Mass (Da): 16314
Location Topology: Lipid-anchor
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A0A2K3P021 | MQKDAAMGMNSSNADAVNGNLSPEKPADRAMGLSELKNSIEEAKIVDADRLSELQDSRERNQILTKQFQELQNELNDDKYVRSSRIYSLANDQLQHWIAELDRYKSLAESLQAGRANVIKREKELKLKLESTDNARHILDSSDSGTDELELQLQKCIIERNDLELTLEEAKQDTGRKDIKVEFRVMASALSKEMGMMEAQLKRWKDVALEAVSLRDKAHSLRATLSGKMSRCGCVENLTLNEIWFETMFIIGGKSSLITLQVGITSDLKNLANKCAEQVLEIKSSKASIGKLQQENQELEFVLDMYGSEDYQKSLPEVRE... | 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: 4... |
A0A2S2NZB1 | MPLDCEARYKIAILVPYRNRLENLCWFLLNLHTFLTKQKLDYTIFIIEQFNNGKFNRGKLLNIGYTEALKLNNFDCFFLHDVDLIPMNNNNIYSCPNQPIHMATANEKYGGRMPYGNYFGGVVGINRTHFELINGFSNMFWGWGGEDDDFLYRIIYHKLNYTRLPPYLGRYHALAHEIQEPNPERYNLLQSSFYRFNTEGLNTLNYVVKSLEILPLFTYFLV | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
Sequence Length: 222
Sequence Mass (Da): 26257
Location Topology: Single-pass type II membrane protein
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A0A2S2NCJ1 | MLYLQWILGEPNSATFFGAVGNDRYSEILKREANRDGLDVKYQYHSDKPTGTCAVIITNGGKYRSLCANLSASKSYTDEHLELPENKKIIQNAKFYLVTGFFLVSNPSASEKIARIAYERNRPLLFNMSAPYIYESYLDSVMSIFPYINIIVGNAKEAKSFALANNWETTDTETIALKLSTFNYVRNYGHRLVILTQDENPVIVATGNHVKKFEVPKISEKDIVDTNGAGDAFVGAFIAKYVLGYPLKICILSGIEAGSYIIKQHGMTRGDAFIV | Cofactor: Binds 3 Mg(2+) ions per subunit.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.
Function: ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives.
EC: 2.7.1.20
Subcellular Location: Nucleus
Catalytic Activity... |
A0A7S3R1B1 | MHPAMLLLNACWVLVLATLANAARDLPTIPLGIPLPSQSPFNPEYHIASPQMEVLSADARIFLFRNFLSEAECDYIRERAEKRLTRSGVVDTKNGGSEINDIRTSMGMFFNRGEDPVIQAIDRRIANVSMTPVYHGEGLQVLRYEVGQKYEAHWDYFFDEKNAAKGANRYATMLTFLDTVEEGGETVFTKMPTPNGRDNKGFSECAKHHLAVKPHKGDAVLFHSMTFTGELEQRSMHGACPVIKGTKWSMAKWIHAKHYPMGDLYDLEAEAAKKPKPAEPSTEEF | Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 285
Sequence Mass (Da): 32022
Location Topology: Single-pass type II membrane protein
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A0A8T4K5U9 | MNVMEHLRKKNPLIHCITNYVTACDVANAVLAVGGSPIMADAPEESSEVTGMADALVINLGMLNSGKREAMFRSCKKAGELGLPIVLDPVGVGISAFRRETAAELLKAFPFAAIRGNLSEISYLCGLPAAEKGVDSGAGTGEGAAIFAARKAAKDYRTTVVVTGAEDIVSDGTRTAKIANGVPEMRQITGMGCMLSGILGACAAAEPDTFQAAVTAAAAMGIAGESSLEGIGKNGVGSLHVGILDALGRMDDETVRLRGKIKYDE | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1.
Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
EC: 2.7.1.50
Catalytic Activity: 5-(2-hydroxyethyl)-4-m... |
F2X0N6 | WICGGYIISDPTLKRFFVLHFIFPFIALCIVFIHIFFLHLQGSSNPLGYDTALKIPFYPSLLCLDIKGFNNVLVIFLAQSLFGILPLAHPGNAIVVDRYVTPLHIVPEWYFLPFYAMLKTIPNKTAGLLVMLA | Cofactor: Binds 2 heme groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a p... |
G0S870 | MSSEASPEAKPNPKPLKGILKKPSAPPNQSTPTKSTSSPSSSSTKPSSSTPAKKSATTPTRPSTRRPSQTLSRSSQPPSPQQSQSPTNEEENEEDLPLAEQQRRREAAARLRLLQQIKSQVLPPPVPIEVFEHLCTLPTTSNPASSPSAEDIQTFLNALQKFQPREYLDLIEERNCLGKCGYTLCPRPRRQLPGPYKITRSGVGKAEELNKWCSDACAARALYIKVQLDNPSYERRKGPGGKDELFIKLELRAEKGQENKTEMGRKTAYKDEQAEKDLADAMARLELDKATKAKKDAAQLALERGDAAGGLFAAEGRVEV... | Function: Putative RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase involved in RNA polymerase II transcription regulation.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Nucleus
Sequence Length: 374
Sequence Mass (Da): 41231
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A0A1B6K8P1 | PVRGYIDNMYGPVGFLVGAGHGIIHAFLGNLENVLDMVPVDYVVNCMIAAVWRNGTTRNPRFTKVYNFTTSPMKTVFWKTICKFAFNQRDLWPFSRSIWYTSYLYTEKELEYKIMAFLLHTIPGLCIDKAVELTGGQPILSKIFSKMNSLSKQGAYFATRSWEFKNDNLLRLWHDLSNEDKQLFHF | 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: 186
Sequence Mass (Da): 21597
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A0A1G2BVX6 | MATKMWAKDNEILMIKFVIGIDEAGRGPLAGPIVAAAVLNTHSLVDKKILSRAQDSKKLSAQAREDLFLPMIQNMLWAVRVFDNKFIDKYGIQKANILLVYELSRDLLKQVNGQAVVLADYVGGAERVLPQINFFKNGESQHQEIAAASIIAKVYRDKLMNSLDKSFPDYAFALHKGYGTKRHYENLKKFGPSPIHRQSFLKNYDFFKTS | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 210
Sequence Mass (Da): 23767
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A0A2S2PAM5 | MKETLISEVSIVFHGAATLNLDASLTEAINLNTTGTLRMLELCSNMKNLEAFVHFSTAFCHVDLDTLNEEVHKSAFDAHNIIRLPSWLDENSIKMVTPHLIKPHPNTYTFSKRLAEDVVGDFYPQLPVVIARPSIVTPALKEPLPGWVDNLNGPTGILAAGGKGVLRSILCNSEYTAEAVPVDFAINAVIVIAWKTAITKQKTTSVPVYNLTQHNLNPITWDAVMTKGREETMKNPFELMLWYPTGSLTANRFVHTYKVICYHWIPAYLIDGILFLLGQKRFMIRVQQKISDGLRVLQYFTLRNWDFTNDRLLALRESLS... | 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: 399
Sequence Mass (Da): 45413
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A0A2K3KB29 | MEVAASGGGGPQFDPRTVEAVFRDFKGRRAGLIKALTSDVDEFYQQCDPG | Function: Histone-binding component that specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes.
Subcellular Location: Nucleus
Sequence Length: 50
Domain: The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence Mass (Da): 5391
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A0A2M7Y809 | MTQDGFIARLTKANGGRGVLTDPRATERWRKGWRSGGGDAEAVVAPRGLLELWRVLQVCVEGGRIVIMQAANTGLTEGSTPSGEYDRPVVVINTLKLDKLHLLGDGRQIVSHAGGTLYALEKLLKPLGRQPHSVIGSSCIGASVVGGVCNNSGGALVRRGPAFTELALYAQITAEGRLELVNHLGLRLGDTPEAMLARLERGGFTEDEIDWSAGRASQDGYAEKVRDVEADSPARYNADPGGLHEASGCAGKLAVFAVRLDTFPQETDARVYYIGANDPAALTALRRGVLTDPRATERWRKGWRSGGGDAEAVVAPRSLL... | Function: Catalyzes the oxidation of D-lactate to pyruvate.
Catalytic Activity: (R)-lactate + a quinone = a quinol + pyruvate
EC: 1.1.5.12
Subcellular Location: Cell inner membrane
Sequence Length: 838
Sequence Mass (Da): 90717
Location Topology: Peripheral membrane protein
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A0A2A4FTP0 | MSRLGAVIAGGRSSRFGTDKAEALWQGRPLIDHAIDALRPFVDEIVVCGRAHGGLPVLADRPAPDMGPLGGINAALHHGRERGDGIVLTVGCDTPLLPAALFERLIAAGGPAYVAQLPLIGCWPTYLATGLDGFLASDAKHAIRAWAALAGAEAIDWPGLANINEPGDLAALPSTSFPRKRESMDGGPQEP | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytopl... |
A0A401LPR5 | MVQAIIKEIIMQKNLVIVESPAKAKTIEKFLGKDFKVLSSYGHIRDLKKKEFSIDVEKNFNPDYEIPADKKTLVNTLKAEAANATTVWLASDEDREGEAIAWHLYEVLKLKPENTKRIVFHEITKTAILKAIEQPRDIDLNLVNAQQARRILDRIVGFELSPVLWRKVKPALSAGRVQSVAVRLIVEREREIHAFKTEASYRVTAIFLVPDTDGKLVEMKAELARRIKTKEEAKAFLNVCQGATFTIDDISTRPIKKTPPAPFTTSTLQQEAARKLGYTVAQTMMIAQRLYESGLITYMRTDSVNLSEYATTSSKEAIIQ... | Function: Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is ... |
A0A955GAX8 | MDAVEEVKQRLSIEDVVAEYVELKRSGRNFKGLSPFTSERTPSFIVSPEKQIWHDFSSGRGGDMFSFIMEMEGVDFRGSLEILARRAGVDLSLYDKGDGGGMRKKKDAAQAALTMAVRYYQQSLLHSPSALSYVTDTRALRRQTIADFGIGYAPNTGTALVDALTKKGVSVHDMKLAGLANDRYGKVNDMFRGRIVIPLYDAQGNPLGFTARILHKEDSGPKYINTPQTILYDKSRHVFGLHAAKEAIRTSGFVVIVEGNMDVISTHQAGYKNVVATAGTAMTGFQIKALQRLTTDIRLCFDQDAAGVAAAERAIDVAQA... | 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: 585
Sequence Mass (Da): 65075
|
A0A930RIW2 | MQHQLTAFFRRNVENYTEKKYVLAVSGGVDSMVLLNAMVTLFGDDAKNRLVVAHVNYGLRAQAEDEEQLVHRFCKLHQIPIETKHWHEAEGVTASEKSLRDFRYDFFREVTKKHQADYLVLAHHQDDQLETVLMKWSRGSTLEGLSGMKEKRHVKSLSILRPFLSYEKKELYEEAEKYDVPYLEDESNESDDYTRNRYRHHVIPFLKEENPNAGSHFQKSAQMIADAVACLMPILEEKQEQFFQRRKKKVTFHREAFLKEPIEMQRLLLQQVLMQMDTTISVVQMEQILEKVGSDKAQLTLDLSNGWRFKKRYEECSFEK... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A2H0W4P2 | MPFEDISSVKQNIRLADMTNYRIGGPAKYFLETDNFDKLIKVLNEARAQKIPIFILAGGSNILIADEGFNGLVVKLKNHDIDVNGETVIAGAGAGIDNLVDAVADAGLTGLEFMAGIYGTVGGAVRGNAGAYGGSISQAVVKVKVFNGQKILEMSNDECKFDYRESIFKHNDYIILEAELKLAKGDAAQVKAKVADIRKTRNAKLPEIEPNAGCIFKNLELHEVVDPKKIKKGLDITDAEYDEATKFGKLPAGYLIEKLGLKGKTIGGAQLSPKHGNIIVNTGNATAKDVVMLLSFLKQQVRDKTGVQLQEEIQLVGF | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 318
Sequence Mass (Da): 34322
|
Q7M8U7 | MITINDTTLRDGEQAPTVAFTQEEKCEIAKLLYEAGADELEIGIPAMGEAEREDIRAILSLGLPLRLMSWNRATQSDLEASLACGMKAVDLSIPVSTKMVAAKFRGKYAKVLSNLEETLTIAKKEGLFVCVGMEDTSRANARFLKEVIALAMERGADRVRFCDTVGILTPLQTYRAIRSLRRHCTLPVEMHCHNDYGMAVANSIAGIEAGAQSVNTTVIGIGERAGNAGFEQVLLSLIGQFGQNRTLDSTILKALVQKVAKAAGVALAPTAPVVGSRLFWHESGIHADGNQKSEGLYEPFSPELVGASREYPIGKHSGSA... | Function: This protein is a Fe-Mo-cofactor biosynthetic component.
EC: 2.3.3.14
Catalytic Activity: 2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA + H(+)
Sequence Length: 376
Sequence Mass (Da): 40917
|
A0A955GBS4 | MNKPKVKDFDVFIGNNRNSRNLNHMSLGKKQSTEKKSAVDNSQDIDEDIISEVSSKLYKSDGSKFAIKKTLGDHMAEFRTRLMWSVIALVFGGVIGYYLQDQIIAFLVKPLGQELFYTSPTGGLDFLIKICLFFGFLLAIPVIIYNLIQFIAPAVPNHITYNVYKILLISIILAITGAAFAYYVCLPAALHFLNTFTNSTIQSLISAQEYFNFVMIYMAGFAALFQMPLIIYFINKVTPLKPAKLLKNQRVVILVSFVIAAILTPTPDPINQFLMAAPMIGLYQASVGVVWQSNKRQKKRPPTPEQLFMLAD | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes.
Subcellular Location: Cell membrane
Sequence Length: 312
Sequence Mass (Da): 35040
Location Topology: Multi-pass membrane protein... |
A0A1H8YA29 | MDRRGFLRNAVGGVGALSLLPASMVRALAAPAPPGGLGNVEHVVILMQENRSFDHYFGTLRGVRGFADLNAVQLPTGRSVFHQPGGSEGYVLPFPTSLQNLNGLDHSLGSGNQAWHLGRYDQWCAAKSPTTMAYYPPEELEFYHQLAGAFTSCDHYHCSVAGPTLPNRRYLMTGKVDNPAAYENIETLMRDVILGSDAGLRFALAFGDQAVADGVAALLRGVASPPVASVLGPLVKGAVGFDLSSPVYRRMTDDPNLPANLLEALQGFRWTSYPERLESRGVSWRVYQEWDNYGDNVLDYFAPFVRVMEKVLRNTGTGAA... | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycerol + H(+) + phosphocholine
EC: 3.1.4.3
Subcellular Location: Secreted
Sequence Length: 981
Sequence Mass (Da): 105371
|
A0A955FD28 | FIHPFDDPLVIAGQGTIGREILEQLPDVTHIFVPVGGGGLLAGISQYVKALRPETVIVGVEPVDSAAMTKSLAADRRVRLAHVGIFADGVAVKQVGEYAFQTAKQLVDDCITVTTDQICAAIKDTYEATRSIVEPAGALALAGLKTYDLPSDAQAIAICSGANVSFERLQQIAERTQIGSGKEALFAIEMPETPGSLHTFCEVAVHDRNISEFAYRLRGRGDAHVLVGLTVKDTKDRQLLMNRIRQHGFGCEDMSDDDLAKEHVRHMVGGTTGVHTTEALYLVDFPERPGALSEFLAHMADKWNISMFHYRSTASDIGSV... | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine: step 1/1.
Function: Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (amino... |
A0A6J0PB88 | MSMPGGRGRIRVLNVAEKPSVAKAVSEILSRRGGGFRSREGRSRYNRVFEFEYAIGPQLCHMLVTSVTGHLMELDFDDRFRKWHSCDPADLYDAPVRKNVPQDKLDIKRTLEEEARSCQWLVLWLDCDREGENIAFEVMEVCTSINHRLNVWRAHFSALIDREIHEAVQNLGRPNKLFADAVDARQEIDLRIGASFTRFQTMLLRDAFVLDFAGDDRNVVLSYGPCQFPTLGFIVERYWEIQSHEPEEFWTINCSHTSDEGTAAFSWMRGHLFDYTSAVIAYEMCVEEPTATVMTVRNQEKLKYPPYPLSTVELQKRASR... | 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... |
A0A9D6VG73 | MKILLVGGGSGGHITPLLAVASQLKKDKPNVQVAVITERLGVFNHLFDDADQIDSLYFINAGKFRRYHGEALHRKIFDIRTILLNIRDAFKLMVGTAESIWALMRIRPDVAFIKGGYVGVPVGLACRLFRTPYITHDSDAVPGLTNRIIGKGARYNAVGMPPDNYSYKKEKMVYVGVPVTDDFIDPEPSIRKSKRSELDLKKDDLLLLITGGSNGARRMDKIIHDCLEKILDKNPKLNIVHQVGKNNENIYEDYPLKLHSRIRVASFLQPLSSYVAAADIVIARAGATAIAEIGHMKKPLILVPNPYLTGAHQIKNAKVL... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-t... |
A0A8A1ME89 | MKDALTRNEIWSLLALLVTSLGVITNTFQGDGQPLITSLALSGIAFAATFSLIRWLGGVFVKAGLKGRDMAKLRRVELPEAMGAVCAVVYILLLIVFIPFPFYKDIVAATSGGGNRDVVLEVQHVETGRFLHRFPHSKLASYLSGLLSLQSILILGIGDDMLDIRWRHKVLIPALASIPMLIVYFVDFGVTVVVVPVPLQPYLGPFIDLGWLYYVYMAAVAIFCPNSVNMLAGINGIEVSQSLVIAVLLLINDALYLTPFTPYPHPAMDSHLFSIGQSL | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: a dolichyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UMP
EC: 2.7.8.15
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 279
Sequence Mass (Da): 30458
Location Topology: Mu... |
K6YU16 | MQYNFITSNQELADFCHQASQVEAIAVDTEFVRTRTLYPQLGLIQIYDGKQLVLVDPLAIDDFSSLTALLTNPNVVKVLHSCSEDLETFWHAFKVMPSPIFDSQFAASIVGMGPALGYAKLVEIMLEVTVDKGESRTDWLARPLRIEQCDYAAKDVLYLFQLYPELKARVIEQDKLSWVYSEIAHLSVKKQTLLPLDSVYLTIKNNWKLSSKAVMILKKLAAWRTSTARLCDMALNFVVREENLLSIAMLQPTSKNELRSIPGVNPHEVRIHGDALLSIVADCQNVSENAYPPKVKRLNDIENYKNTAASVKKLCLEIAE... | Function: Exonuclease involved in the 3' processing of various precursor tRNAs. Initiates hydrolysis at the 3'-terminus of an RNA molecule and releases 5'-mononucleotides.
Catalytic Activity: Exonucleolytic cleavage that removes extra residues from the 3'-terminus of tRNA to produce 5'-mononucleotides.
EC: 3.1.13.5
Sub... |
A0A9D3S1Z0 | MDSGYINASENPIDNATMLLYNSYMALWEDFDSSVNDMRYFLIGLYTTVSVLGLLGNVLILTALARKWREKSIINLLVGNLAFSDILVVLFCSPFTLTSVLLDHWVFGEVMCHVVPFLQCVSVVVSTLVLMSIAMVRYHMISRPLSAHMSVHSGYVLLAAIWTLGLSICSPLPVFHRTVDVSRAFRLGPPRRSKWLCVESWPSGAYRVAFTLGLLLVQYILPVVCLTASHATVCRRVWA | Function: Receptor for neuropeptide Y and peptide YY. The activity of this receptor is mediated by G proteins that inhibit adenylate cyclase activity. Seems to be associated with food intake. Could be involved in feeding disorders.
Subcellular Location: Cell membrane
Sequence Length: 239
Sequence Mass (Da): 26720
Locat... |
A0A3T0RRF1 | MMPTVIRISKKNLPALLPKRTKTVHKQNGGKCLIIAGSPGLWGASILCAKAAYRVGAGYVYLPEKTKDLILHPDFVSMKISVKTNFEPFAAIAIGPGSIATSDLRKVYESLLKKFKGPVIVDAGALKLIKKIPEYWIMTPHEAELARLLNSTADKIRADRFQAVQLAQKTFGGIVILKGPHTLIANSKNIFEITTGNKALAKAGTGDVLCGMIAGFLSQGLSPTKACVLGCGLHGYIADEWVKKNDYLSLMASEVIDLIPQAIFKLRKSQLKKYPLSANLTHS | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
A0A3D5HNT4 | MVGAETSPQDAFARAATAFADDDEHAQRLYDYASKLWFMFSTPVLSNGGTTRGLPISCFLNYVDDSREGITGHYTENAFLSSVGGGIGGCWNGVRSVGSKTSNGSESTGVIPFLKVVDAEMLAFSQGVTRRGSYAAYLDMSHPEIEEFLDVRKPTGGDINRKSTNLHHAVVVPDRFMQLIEGATKQEGFDDSWSLIDPHTNQVVKTVSAKTLWVKLIQNRVETGEPYIMFEDTVQNALPSFQKELGLKVHHSNL | Pathway: Genetic information processing; DNA replication.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
EC: 1.17.4.1
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [... |
A0A932NXK8 | MTRNQRNQRKLSTKTSPKVLPFIEHIHELRRRLFIVAASVVGFSVVGYFINEQLIQILLKPAGNQQFIYTSPGGAINFIFQICIYFGVAASIPIIVSQLLGFIEPVLRNSSKKFLVLNGLFSIILAASGMTFGYFVGLPAAMHFLTSQFTVSRIEALLTIQEYMSFVTIYLVGSALLFQIPLIMTTINRIKPLKPSGLFKIERFVIVGAFVLAAIITPTPDVFNQLLVAGPIIAIYHLGILLIWLQNRQTSSTRIMKLLENDAKVQAERLAHIATLGSPKIVRSQSELSRAKTVLSEGEVAVATSREEKLFVFDSEVSPQ... | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes.
Subcellular Location: Cell membrane
Sequence Length: 383
Sequence Mass (Da): 42482
Location Topology: Multi-pass membrane protein... |
A0A024HEU4 | MVTNVTNFSRSGLYDWMAQRVSAVVLAAYVLFLLGYLVTHPNISYEEWHGLFSHSLMKIFSLLTLVALSVHAWVGMWTITTDYLTPMALGKAATVVRFLVQAACGMAMFAFFVWGVQILWGN | Cofactor: The heme is bound between the two transmembrane subunits.
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Cell inner membrane
Sequence Length: 122
Sequence Mass (Da): 13684
Location Topology: Multi-pass me... |
A0A5C5VV96 | MCSPQLILASASPRRRELLEAAGYAFQVVSPREGAEPEGACSACGPAQLVVDLAVAKLRDVLDQLRLKGAQADPRPTTLVLAADTVAECGGQVLGKPRNEDHAVAMMRMLSGTEHRVYTGVALATLTSRGQPYAEAVITTLRMNDLSEAWIANYAESGAWEGKAGGFGYQDGLGFVHVVAGSESNVVGLPMERVAELLADRGVHPSLKSTL | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Seque... |
A0A6I9SEN3 | MGQSSSSGRRRDDYYHYSPSSSSQIPPPISSGSSHPPPPPNYAYSAPSRPSYSNPYPMPAPPPPPPNTNSSSYYQTPSAWLRNSVPWASRTPYHPTYYGPNPGAGWRFPPPQSSAAAITHPQPPPPPPPPPPPPIEHQKAKTVKNDINLHKDSIRLVVDELNPDQQLVSFTFDAVVDGSVTIYYFAKEGANCRFSPIYPDIYTPRKVAFQKGLGQKFIQPSGFGIDLGFFDLDDLARPVGGDVFPLVVCAEACPPLPSTDEQVGPSTAAANAQITQAVIEKTNSGAFQVRVIKQILWADNERYELQEIYGIASSVKTEIG... | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 386
Sequence Mass (Da): 42214
|
A0A955E059 | MMNIVQLLASAEPAESQGIAALGLSPWAILAQGVTFLIFFLLVKKFALGKIVDTIETRRKTIEESLNKAEELNKQNEEAEKRVNSLLSEARKESEEIIKKSREEASAVITDAEKIAGEKAEKIIADGKLQIEAEVLKAREALKKETLGLVARATEAVLGEAVDSKKSESIIRKALEETK | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 179
Sequence Mass (Da): 19630
Location Topology: Single-pass membrane protein
|
M1FF19 | MTLDKLTGGLPLARLISIVAIAMSVYHLVTAYFGTPIAEVHLPVHLGFALVIIFWVYRSAGTGAWRYLHALRDLTLTAMAVGGCSYLAFNADEVQQRMLYFDPLTTEQLVYGCVLILAVLEAARRVIGWPLVFLGAGALGYALFGNLLPSPFWHRGYSLQAVIETTYLTQDGLWTSPLRVTASYVFLFVLFGAFLVASGAGVFFTDLARSLTGKFTGGAAKTAVVSSALMGSLSGSSAGNVVVTGSFTIPAMRKAGFPGRFSAGVEAVASSGGQFMPPVMGSAAFIMAEFIGIPYIEIAQAAIIPAILYFISVLAMVHFE... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 634
Sequence Mass (Da): 66608
Location Topology: Multi-pass membrane protein
|
A0A2N1W8K2 | MEITVHEFPDMKKLSGQSALYIAGIIKGSIENKGRCIIALSGGKSPKQVYEKLAEAEVNAGINWRRVFVFWGDERYTGHTSDDSNYYMTYRSFLSKVNIPQENIFRVPVEVSPASYAAILYERMMEKFFMSMGAVNGKKRTPVFDLMLLGVGTDGHTASLFPGHEAVNEKKRWVVSLKTADNIQERVTMTLPVINSACNVVFIVSGEGKGKIIRSVLEERGTDKKEYPAAKITPETGTVWFVDKRAVK | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
EC: 3.1.1.31
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequen... |
A0A7K2YNP4 | MPERAPIFPPAGSAPLPAGPGGPAGSPPGGDGPGGSGGPGDSGDPGDSGEGPGGSDTEAADTDGASATPPPKRKGSFWKELPLLLVIAIVLALLIKTFLVQAFSIPSESMENTIKVGDRVLVNKFTPWFGAEPERGQVVVFHDPGNWLSEAPKQSDNAIVRGLQKGMSWVGLMPSASEKDLIKRVIGVGGDRVQCCDAQGRLMVNGKPLDESSYLKKGVAPSTMQFDVTIPKGRIWLMGDNRDNSSDSRYHQGEPGGGTVDKDQVIGRAFTVVWPLSRIHGLGVPGTFDQPGLGMGAVGSAPLAAGFAGALPIVLWRRRR... | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 340
Sequence Mass (Da): 35273
Location Topology: Single-pass type II membrane protein
|
A0A832QCP1 | MMKKIAILTSGGDAPGMNAAIRSIVRIGLHYGMEVYGVIDGYRGLIERNLVKLTHRIVSEKLNSGGTFLGTSRYDEFMDIEVKKKAVENLKEEGIDVLVVIGGEGTIKGAQTLSTLSLNCIAIPATIDNDVAVTDYAIGFDTALNTVVETIDKLRDTSSSHQRCSIIETMGRNYGELALQAGIACGAEVVITPERNYSLDEVSKMINEGLEKGKKHAIVIVAENILDVKEFAKELGEHIHLPATVTVLGHVQRGGTPTAFDRVLATRMGSHAIQLILENKYNKIVAIKGNKIVDVDLEKIKKSETKIPDDLFRITTETE | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosph... |
A0A178MXW6 | MNLEARLLYRDAMVLIIDKPAGIAVHAGPRDGSANLMQWLDQLRFGLPRAPELAHRLDRDTSGCLVLGRHRKALARLGELFASNSVDKVYWAVVVGRPQADEGLIEAPLKKLERRHGWRMIVDPKGQPSATRWRVLGYDQRLTWIEARPLTGRTHQIRVHLASIGLPLAGDAVYGRGTGDLEAPRLHLHARSISLPFTPKKPPITATAPVPDHMAELLRRCGWADTEAAGN | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 231
Sequence Mass (Da): 25618
|
S9NX72 | MSPLRNNGDKAARQDAIRRIVRTHQVGTQEELGQLLSREGFDVTQATLSRDLAQLGAMRVSLPEGGTVYGLEAAPPRGGESRLMELGEMILSVEDNEMLVVVRTRPGSAPLVASAIDHARLLECLGTLAGDDTIFVAPARGRSTRTLNRKLKAFFGKEDTP | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Function: Regulates arginine biosynthesis genes.
Subcellular Location: Cytoplasm
Sequence Length: 161
Sequence Mass (Da): 17424
|
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