UniProt ID stringlengths 6 10 | Protein Sequence stringlengths 5 15.6k | Functional Description stringlengths 6 12.4k |
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B4GUT1 | MDDLKIILEFSAGAELLFGNIKRRQLFLDGHKKWTIANLLKWMHANILTERPELFLQGDTVRPGILVLINDTDWELLGELDYELQANDNVLFISTLHGG | Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by MOCS3. The sulfur is then transferred to tRNA to form 2-thiolation of mc... |
B7MCT5 | MIGLVGKKVGMTRIFTEDGVSIPVTVIEVEANRVTQVKDLANDGYRAIQVTTGAKKANRVTKPEAGHFAKAGVEAGRGLWEFRLAEGEEFTVGQSISVELFADVKKVDVTGTSKGKGFAGTVKRWNFRTQDATHGNSLSHRVPGSIGQNQTPGKVFKGKKMAGQMGNERVTVQSLDVVRVDAERNLLLVKGAVPGATGSDLIVKPAVKA | One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. Part of the 50S ribosomal subunit. Forms a cluster with proteins L14 and L19. Methylated by PrmB. Belongs to the universal ribosomal protein uL3 family. |
F1QNE2 | MENRDDEVEHQHSTMGSEGGTAGDGTPPPKRKGKFSTLGKIFKPWKWRKKKSSEKFKETSEVLERKMSMRRPRQELIEQGVLKELPDNESGEAHGHKAPYVKNGHTLPVGVGGSLALEQVHSPSESEFRINPVWLPQPEDRRARAPSDGDHRGALGPRASNQDDGRRGGWSVGTEDWKNNLAWHGEDIRRGGRAHAEMDKRPGLMKAPSEDGRRTRPEPDWKPTLPRHSSVEEGRGRRESDSSQYLPNSEMMRDTLREPLPPKQSIMPPKWLMTSTPEPGSDSLPRTPVHNPAAPSFCSSNSSSSSSAGKPLRNVSSAGA... | Regulator of protein phosphatase 1 (PP1) required for neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. Acts as an activator of PP1. During neural tube closure, localizes to the ventral neural tube and activates PP1, leading to down-regulate cell proliferation wi... |
Q8C5U1 | MHRQSSKSGVALPPVGQGPDACQMLSRAQLGQDPPQRTVLGVLTENEQYRRTCGQEITAIRCFSGSENVFPAAGKKVLSDHGVNEPAKRGFDIYMDDPEQGDRDTCSGKEGIIFEDVYEVDTSMLKSDLHFLLDFNTVSPMLVDPTTHAQSEEATDFGSDVINVTEYAEEIHRYLREAEVRHRPKAHYMRKQPDITEGMRAILVDWLVEVGEEYKLRTETLYLAVNFLDRFLSCMSVLRGKLQLVGTAAILLASKYEEIYPPDVDEFVYITDDTYTKRQLLRMEHLLLKVLAFDLTVPTTNQFLLQYLRRQGVCIRTENL... | May be involved in the control of the cell cycle at the G1/S (start) and G2/M (mitosis) transitions. May primarily function in the control of the germline meiotic cell cycle and additionally in the control of mitotic cell cycle in some somatic cells. Interacts with INCA1 and KLHDC9 (By similarity). Interacts with the C... |
Q45U15 | MEYEDLELITIWPSPTKNKLCQFIKQNLSKEHVVTQLFFIDATSSFPLSQFQKLVPPTLPENVRIYENIRINTCLDLEELSAITVKLLQILSMNKINAQRGTEDAVTEPLKIILYINGLEVMFRNSQFKSSPQRSHELLRDTLLKLRVMGNDENENASIRTLLEFPKEQLLDYYLKKNNNTRTSSVRSKRRRIKNGDSLAEYIWKYYADSLFE | Involved in chromosome segregation during meiosis. Promotes efficient recombinational repair and functions in the protection of the genome from spontaneous and induced DNA damage like mutations and gross chromosomal rearrangements (GCRs). Component of the SHU complex composed of at least CSM2, PSY3, SHU1 and SHU2. Pres... |
B3GZ71 | MSIEERVKKIIVDQLGVKAEDVKPEASFIEDLGADSLDTVELVMALEEEFDIEIPDEEAEKITTVQSAIDYVTKANA | Carrier of the growing fatty acid chain in fatty acid biosynthesis. Lipid metabolism; fatty acid biosynthesis. 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the pr... |
P43912 | MWIGVISLFPEMFKAITEFGVTGRAVKHNLLKVECWNPRDFTFDKHKTVDDRPYGGGPGMLMMVQPLRDAIHTAKAAAGEGAKVIYLSPQGRKLDQGGVTELAQNQKLILVCGRYEGIDERLIQTEIDEEWSIGDYVLTGGELPAMTLIDAVARFIPGVLGKQASAEEDSFADGLLDCPHYTRPEVLEGLTVPPVLMSGHHEEIRKWRLKQSLQRTWLRRPELLEGLALTDEQRKLLKEAQAEHNS | Specifically methylates guanosine-37 in various tRNAs. guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine Homodimer. Belongs to the RNA methyltransferase TrmD family. |
Q5PNG1 | MKLPIYLDYSATTPVDPRVAEKMMQFLTLDGTFGNPASRSHRFGWQAEEAVDIARNQIAELVGADPREIVFTSGATESDNLAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQRNGIIDLNELEAAMRDDTILVSIMHVNNEIGVVQDIATIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRIRIEAQMHGGGHERGMRSGTLPVHQIVGMGEAYRIAKEEMETEMARLRGLRNRLWNGIKDIEEVYLNGDLEQGAPNILNVSFNYVEGESLIMALKDL... | Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur and selenium atoms from cysteine and selenocysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis on... |
A5EWR9 | MKSLQKGFTLIELMIVVAIIGILAAFAIPAYNDYIARTQVSEGVSLADGLKIRIADNLQDGKCTSEGDPASGEVGNTDMGKYALATIEGTPDANLAGLTPKDPNGCKVKIEYGKGTAGDNISPLIKGQMLVLNQLVNGSYDKDSSSTVKPKFLPKALKEATP | Major component of the type IV fimbriae that plays an essential role in twitching motility, natural transformation, and protease secretion. By PilR (PilR/S system) and RNA polymerase sigma-54 factor/RpoN. Deletion mutants do not colonize the ovine hoof. Mutants show also altered secretion of extracellular proteases and... |
A4D120 | MMLHSALGLCLLLVTVSSNLAIAIKKEKRPPQTLSRGWGDDITWVQTYEEGLFYAQKSKKPLMVIHHLEDCQYSQALKKVFAQNEEIQEMAQNKFIMLNLMHETTDKNLSPDGQYVPRIMFVDPSLTVRADIAGRYSNRLYTYEPRDLPLLIENMKKALRLIQSEL | Required for calcium-mediated regulation of ciliary beat frequency and mucociliary clearance in the airway. Might be involved in the regulation of intracellular calcium in tracheal epithelial cells. Interacts with LYPD3 and DAG1 (alphaDAG1). Found in the cytoplasm, which could include the endoplasmic reticulum. Express... |
Q9B813 | MATWANLGLQNSSSPLMEQLNFFHDHTVLILIMITVMITYVMGMLFFNKFTNRYLLHGQTIEIIWTILPAIILMFIAFPSLRLLYLLDEINSPLITLKAIGHQWYWSYEYSNFMNLEFDSYMIPTNELDLNGFRLLDVDNRIILPLNNQIRILVTATDVLHSWTVPSLGVKIDATPGRLNQTNFLINQSGLFFGQCSEICGANHSFMPIVIESIPMNYFIKWVSSQLN | Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CII... |
Q5JDG9 | MKLDVIGIGNLNYDIIFTLERFPEFHEKINARGAHFGLGGAAANTISWLAHFGLKTGYIGAVGNDDVGEMHIKYFQGIGVDTGGIDVVEEPSGVAVAMVAGDDKRIVKYPGANLRRRFKPEYASRAKFLHLSSNPPELIEEAVNFASQRGIKVSLDIGEAPLPRELESKVDYLMMNEDEYRRKYGSLDPSLCRAKNLVVTLNGGGALVREGDNVFEVRGLSAKVVDSTGAGDSFDAGVIYGVLNGWSLLDSAKLGMLLAYLTVQKVGARSAIVPLEEVKRIAREVGLDLPFNRT | Involved in nucleoside degradation. Phosphorylates ribose 1-phosphate (R1P) to ribose 1,5-bisphosphate. Can also act on deoxyribose 1-phosphate (dR1P), but is most active with R1P. ADP is the most preferred phosphate donor, followed by GDP and UDP. ADP + alpha-D-ribose 1-phosphate = alpha-D-ribose 1,5-bisphosphate + AM... |
D6W017 | MQKIFRPFQLTRGFTSSVKNFRQWRLIETRKIAKQPNYQVGDAKPLHMPKERKKFPDYKYGESNIFKQSNKGLYGGSFVQFGNNISESKAKTRKKWLPNVVKKGLWSETLNRKISIKMTAKVLKTISKEGGIDNYLTKEKSARIKELGPTGWKLRYRVLKRKDEIENPPHKDAPIIEMAGGKKAKIYYDEIVNGSPRKISVGRRRLMSFLYPLEKLEYRSVGKDLNYKKFVELFADVPVKDILARLEDHKFDLSTITV | Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial in... |
B7IYM7 | MRIAVIGAMEEEVRILRDKLEQAETETVAGCEFTKGLLAGHEVILLKSGIGKVNAAMSTTILLEKYKPEKVINTGSAGGFHHSLNVGDVVISTEVRHHDVDVTAFNYEYGQVPGMPPGFKADEALVALAEKCMQTEENIQVVKGMIATGDSFMSDPNRVAAIRDKFENLYAVEMEAAAVAQVCHQYEVPFVIIRALSDIAGKESNVSFDQFLDQAALHSTNFIVKVLEELK | Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethio... |
B3EP45 | MGHVEKVARRHKIKTRSKARGQGTVEKPRLCVFRSLSQIYVQLVDDVNGAILLSVSSMSKENKGLKGTKCDISRTIGKQIGEKAVQKGITKVVFDRNGFRYHGRVQALADGAREAGLVF | This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S and 23S rRNAs. Belongs to the universal ribosomal pro... |
Q8X984 | MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFSMASALASFDILTAVHKHYSVEEWQAFINNSSADVLKHVMVSTGTSDADFEKTKQILDLNPALNFVCIDVANGYSEHFVQFVAKAREAWPTKTICAGNVVTGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGMIISDGGCTTPGDVAKAFGGGADFVMLGGMLAGHEESGGRIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVG... | Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. IMP + NADP(+) + NH4(+) = GMP + 2 H(+) + NADPH Homotetramer. Belongs to the... |
F7VWB6 | MATIILGSQWGDEGKGKLTDILCPKAQICARAAGGHNAGHSIVANGVEYDFHLLPSGLVNPNCMNLIGSSVVFHVPSFFSELSKLEEKGLTDVHNRILVSDRCHVDFDLHAAVDGLEEVELGDRKIGTTGRGIGPSYSTKMARSGVRIHEIFNEEIFERKLRQLANGYKKRFGDLLKYDVEEEIARFKEYRVKLAPYTVDAVQYMKQAQDRGYKILIEGANALMLDIDYGTYPYVTSSNTGLGGIITGLSINPTKIDNIIGVVKAYTTRVGGGPFKTEDLEEAGTKLQDIGREWGVSTGRKRRCGWLDLVVLKYSTAINN... | Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity). GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate Binds 1 Mg(2+) ion per subunit. Purine m... |
A6H1A3 | MNTIVGTYECKVDSKGRLMMPNPLKKQLNVSLQEGFVLKRSVFQQCLELYPMKEWDLMMQKINKLNRFVKKNNDFIRRFTAGVRIIEIDATGRLLIPKDLAVFASVTKDIVLSSAVNIIEIWDKDLYEKAIDDSVGDFADLAEEVMGNVNDDEYGIS | Forms oligomers. Belongs to the MraZ family. |
Q7P112 | MTQMTPQEIVHELDQHIIGQHKAKRAVAIALRNRWRRQQVAEPLRSEITPKNILMIGPTGVGKTEIARRLAKLSGAPFIKVEATKFTEVGYVGRDVDTIIRDLVDVAIKDTREAAIKRNRTRAEDAAEERILDVLLPQPRKQPSGFFAEEPAVEEKHEDGATRQKFRKMLREGKFDDKEIELEIAAPAAQMNVMAPPGMEDFASQLQGMFQGLGAGKKQTAKMKVADAFKQLIDEEAAKLVNEEELKAEALKNVEQNGIVFIDEIDKVTSRGEGHSGADVSRAGVQRDLLPLVEGTTVSTKYGMVKTDHILFIASGAFQL... | ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before... |
Q9TEH4 | MTPMRKTNPLMKLINHSFIDLPTPSNISAWWNFGSLLGACLILQITTGLFLAMHYSPDASTAFSSIAHITRDVNYGWIIRYLHANGASMFFICLFLHIGRGLYYGSFLYSETWNIGIILLLATMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVQWIWGGYSVDSPTLTRFFTFHFILPFIIAALATLHLLFLHETGSNNPLGITSHSDKITFHPYYTIKDALGLLLFLLSLMTLTLFSPDLLGDPDNYTLANPLNTPPHIKPEWYFLFAYTILRSVPNKLGGVLALLLSILILAMIPILHMSKQQSMMFRPL... | 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 membrane that is... |
Q04832 | MSETEDVKRPRTESSTSCRNCGKEGHYARECPEADSKGDERSTTCFRCGEEGHMSRECPNEARSGAAGAMTCFRCGEAGHMSRDCPNSAKPGAAKGFECYKCGQEGHLSRDCPSSQGGSRGGYGQKRGRSGAQGGYSGDRTCYKCGDAGHISRDCPNGQGGYSGAGDRTCYKCGDAGHISRDCPNGQGGYSGAGDRKCYKCGESGHMSRECPSAGSTGSGDRACYKCGKPGHISRECPEAGGSYGGSRGGGDRTCYKCGEAGHISRDCPSS | Binds to single-stranded DNA located in the 5' hexanucleotide repeat region of the L.major leishmanolysin (GP63) gene. |
Q1LIF3 | MKASISTKLDQLAERLDEVNALLAREDATANMDQYRKLSREHAELSPVAEQYGQYRQAQDDLATAQALLDDPEMKEFAADEIDAARERLQSLENSLQTLLLPKDPNDDRNLLLEIRAGTGGEESALFAADLLRMYTRYAERRRWQVEIMSESPSDLGGYKEVIVRIAGDAAFSRLKFESGGHRVQRVPATESQGRIHTSACTVAVMPEADEVGEVEINPSDLRVDTFRASGAGGQHVNKTDSAVRLTHLPTGIVVECQDDRSQHRNKEKAMKVLAARIKDMQLRAAQAKEANTRRNLIGSGDRSDRIRTYNFPQGRVTDH... | Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA. Methylated by PrmC. Methylation increases the termination efficiency of RF1. Belongs to the prokaryotic/mitochondrial release factor family. |
Q9UDG7 | MGEPQGSMRILVTGGSGLVGKAIQKVVADGAGLPGEDWVFVSSKDADLTDTAQTRALFEKVQPTHVIHLAAMVGGLFRNIKYNLDFWRKNVHMNDNVLHSAFEVGARKVVSCLSTCIFPDKTTYPIDETMIHNGPPHNSNFGYSYAKRMIDVQNRAYFQQYGCTFTAVIPTNVFGPHDNFNIEDGHVLPGLIHKVHLAKSSGSALTVWGTGNPRRQFIYSLDLAQLFIWVLREYNEVEPIILSVGEEDEVSIKEAAEAVVEAMDFHGEVTFDTTKSDGQFKKTASNSKLRTYLPDFRFTPFKQAVKETCAWFTDNYEQAR... | 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. GDP-beta-L-fucose + NADP(+) = GDP-4-dehydro-alpha-D-rhamnose + H(+) + NADPH Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via de novo pathway; GDP-L-fucose from ... |
Q252V9 | MGQKGCPIGFRTGVTKKWRSLWYGNKQEFGKFLIEDVKIREHLRKKPSCQGAAGFVVRRMSGKIEVTIQTARPGLVIGKKGAEVDLLKEELRKLTGKEVWVEIAEIKRPELNAKLVADNIARQIERRVSFRRAMKKAMQSVMEAGAIGVKIQVSGRLAGAEIARSEWYKNGRVPLHTLRADIDYATASAETTYGIIGVKVWINLGEKTSTANASAGSAVSTAQ | Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation. Part of the 30S ribosomal subunit. Forms a tight complex with proteins S10 and S14. Belongs to the universal ribosomal protein uS3 family. |
Q2FSR2 | MIFDTEEFKKRGKEDFESAWHAGPSVLTPPTTDLMYPRLTYLRAQAHPVFETIHRLREAYLAIGFQEAENPIIVDEQEVYRQFGPEAMAVLDRVFYLGGLPRPNVGIGKEQIQKINSILGRDLSEDEEESLRKTLHAYKKSEIDGDELAYELSGVLHTDDARIVEILDRVFPEFRALKPESSRQTLRSHMTSGWFQTLGAIWEKVPHPIRLFSIDRCFRREQAEDSHRLMSYHSASCVVAGEYVTIEDGKAVARALLSAFGYTDFEFRPDDKRSKYYMPDTQTEVYAAHPDHGWVEVATFGIYSPVALAEYGVGIPVMNL... | Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys). ATP + O-phospho-L-serine + tRNA(Cys) = AMP + diphosphate + O-phospho-L-seryl-tRNA(Cys) Homotetramer. Interacts with SepCysS. Belongs to the class-II aminoacyl-tRNA synthetase family. O-phosphoseryl-tRNA(Cys) synthetase subfamily. |
P19991 | AAAPF | Main peptide from the subesophageal ganglia. |
A8H7X2 | MIKDAVNTETVEVNPVDQVRSTIYQLLSSLFAKEIDHKILHDLTSEQAQQFWAQLGSEAEFKADVDVLVAELAKLNTDKALLELAADYCGLFLVGTKYSASPYASLYLDDKPAKKGDEPLLFGEQHQQMTQFLKQSQLQVQSEFPEPADHLAVILAYVAHLCTHSDEAEQHSFIKANLANWLGNFVAKVTEVDTGNFYQALARLTYSWVKSDAEWLESELN | Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor. Belongs to the TorD/DmsD family. TorD subfamily. |
A2RGK2 | METWQEVTVHVHRDAQEAVSYVLIETGSQGVAIADSADYIGQKDRFGELYPDVEQSDMIAITAYYPSSTNLADVIATINEQLAELASFGLQVGQVTVDSQELAEEDWADNWKKYYEPARITHDLTIVPSWTDYDASAGEKVIKLDPGMAFGTGTHPTTKMSLFALEQILRGGETVIDVGTGSGVLSIASSLLGAKTIYAYDLDDVAVRVAQENIDLNQGTDNIHVAAGDLLKGVSQEADVIVANILADILVLLTDDAYRLVKDQGYLILSGIISEKLDMVLEAAFSAGFFLETHMIQGEWNALVFKKTDDISGVIGG | Methylates ribosomal protein L11. 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 Belongs to the methyltransferase superfamily. PrmA family. |
A5FMG6 | MNTLQAIVLAVIEGITEFLPVSSTGHMIIASSFFGIAHEDFTKLFTIVIQLGAILSVVVLYFKRFFQTLDFYFKLLVAFIPAVVLGLLLSDFIDGLLENPVTVAVSLLIGGLILLKVDEWFNNPNAAETSQKITYLQALKIGLFQCIAMIPGVSRSGASIVGGMSQKLSRTTAAEFSFFLAVPTMLGATVKKCYDYYKAGFELSHDQVNILIIGNVVAFIVALLAIKTFISFLTKNGFKVFGYYRIIAGIILLLIHFFIHPLTII | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin (By similarity). di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate Bacitracin is thought to be involved in the inhibition of peptidoglycan synthesis by sequest... |
Q8RF65 | MKVLFATGEAFPFVKTGGLGDVSYSLPKTLKQKENVDIRVILPKYSKISNELLKDARHLGHKEIWVAHHNEYVGIEEVELEGVIYYFVDNERYFKRPNVYGEFDDCERFLFFCKAVVETMDITKFKPDIIHCNDWQSALIPIYLKERGIYDVKTIFTIHNLRFQGFFFNNVIEDLLEIDRAKYFQEDGLKYYDMISFLKGGVVYSDYITTVSDSYAEEIKTQELGEGIHGLFQKYDYKLSGIVNGIDKISYPLSKKPHKILKADLQKKLGLDVEEDTPLIVIITRLDRQKGLDYIVEKFDEMMSLGIQFILLGTGEKRYE... | Synthesizes alpha-1,4-glucan chains using ADP-glucose. [(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+) Glycan biosynthesis; glycogen biosynthesis. Belongs to the glycosyltransferase 1 family. Bacterial/plant glycogen synthase subfamily. |
B7M928 | MSPCENDTPINWKRNLIVAWLGCFLTGAAFSLVMPFLPLYVEQLGVTGHSALNMWSGIVFSITFLFSAIASPFWGGLADRKGRKLMLLRSALGMGIVMVLMGLAQNIWQFLILRALLGLLGGFVPNANALIATQVPRNKSGWALGTLSTGGVSGALLGPMAGGLLADSYGLRPVFFITASVLILCFFVTLFCIREKFQPVSKKEMLHMREVVTSLKNPKLVLSLFVTTLIIQVATGSIAPILTLYVRELAGNVSNVAFISGMIASVPGVAALLSAPRLGKLGDRIGPEKILITALIFSVLLLIPMSYVQTPLQLGILRFL... | Confers resistance to fosfomycin and deoxycholate. Belongs to the major facilitator superfamily. DHA1 family. MdtG (TC 2.A.1.2.20) subfamily. |
Q9U4I8 | MGNMRRLLIFAVLVILTVISNSKSSYKYDGSLFSSKELDYDETDTKAMGSVFSRYMSDSDAQLILDLDFFRHFFNYAEAYRDGAEEGNLELMKYAVEMVEKLKSFDISMACVGDMMHLAWTGVEYATHVEEHKNCSDCKCTPLFQQKKSERHWIFNVFDAMGKVPAGIMSGNNLWVGSWSTCRKIDVVKNAQGQKWKGQYCLATIDAYERDNPLVYFGNMMSGPPDKHCYDKTVKNVTDDGFCFALFPVLKFGVCMPNTCTNHDVKQMLSFAIRATEGAVGTKSVCNVDVECRAESYSDAMSENGLAMFALYLLIATVVL... | Plays a role in the uptake of a range of molecules including lipids and xenobiotic compounds from the intestine to surrounding tissues. Mediates transport of lipids from intestine to the reproductive tract. Required for efficient yolk transport into oocytes. Vital for embryonic development. In L1 larvae through to adul... |
P06209 | MGAQVSSQKVGAHENSNRAYGGSTINYTTINYYKDSASNAASKQDYSQDPSKFTEPLKDVLIKTAPALNSPNVEACGYSDRVLQLTLGNSTITTQEAANSVVAYGRWPEFIRDDEANPVDQPTEPDVATSRFYTLDTVMWGKESRGWWWKLPDALRDMGLFGQNMYYHYLGRSGYTVHVQCNASKFHQGSLGVFAIPEFCLAGDSDTQRYTSYANANPGEKGGKFYAQFNKDTAVTSPKREFCPVDYLLGCGVLIGNAFVFPHQIINLRTNNSATLVLPYVNALSIDSMVKHNNWGIAILPLSPLDFAQDSSVEIPITVT... | Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms the vertices of the capsid (By si... |
A1SBD7 | MAKSLSITPVSGLSRLPWRAYLEMTKPKVVTLMLLTVLVGMCLALPGAVPLQPLIAGMLGIAMMAGAAAAMNHLIDRRIDGLMARTYNRPLPKGKVPVSHAATFAALLALLGFACLYWLVNPLTAWLTLASLLGYAVVYTAYLKRATPQNIVIGGLAGAMPPLLGWTAVTNDFHGHGLLLVIIIFAWTPPHFWALAIHRKADYAKVDIPMLPVTHGVAFTKTCIFLYTILLALACLLPVLVGMSGALYLLGSTLLSIGFIYKAWQLKYHETPGMAMDVFRFSIYHLMLLFILLLVDHYI | Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1... |
D6VVZ8 | MFQQLSASIRHNAHIIFLCISWYFISSLASQVTKQVLTVCPLPLFLGEFQFIYTAVLAWFTCYIAYSFPGFYRIFPNGTFPEYYIDDRETSRAARKESKLSSLIIPPSKPILQTVLPLGLFQFVGKYFGHTATSLVPVSTVASIKTLSPMFILLLQKILKISTLKITLTLIFSLCTLVLGVWIIVQEDNRSPASSNELREFSKYGVICAMISMFIFVLQNIYGKTVFTYRSQTDESQSNSGFSRQESPLPLYEKLDEKLVAKKKPKSYDKLTLMIYISLVGFCLSFGWFITLEFPVLFRYFFQINSSSTVIKAFPVSLFL... | Belongs to the TPT transporter family. |
Q66KH2 | METLHRLRQFDAYPKTLEDFRVKTCGGAVVTVISGLIMLILFFSELQYYLTKEVYPELFVDKSRGDKLKINIDVIFPHMPCAYLSIDAMDVAGEQQLDVEHNLFKQRLDLDKKPVTSEADRHELGKSEEQVVFDPKTLDPNRCESCYGAETDDFSCCNSCDDVREAYRRKGWAFKTPDSIEQCKREGFSQKMQEQKNEGCQVYGFLEVNKVAGNFHFAPGKSFQQSHVHVHAVEIHDLQSFGLDNINMTHEIKHLSFGKDYPGLVNPLDGTSIVAMQSSMMFQYFVKIVPTVYVKVDGEVLRTNQFSVTRHEKMTNGLIG... | Possible role in transport between endoplasmic reticulum and Golgi. Belongs to the ERGIC family. |
Q9JID2 | MTLESMIACCLSDEVKESKRINAEIEKQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGAGYSEEDKRGFTKLVYQNIFTAMQAVVRAMDTLKIRYKYEQNKANALLIREVDVEKVTTFEHQYVNAIKTLWSDPGVQECYDRRREFQLSDSAKYYLTDVDRIATVGYLPTQQDVLRVRVPTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQHSSVILFLNKKDLLEDKILHSHLVDYFPEFDGPQRDAQAAREFILKMFVDLNPDS... | Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Acts as an activator of phospholipase C (By similarity). Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs) (By similarity). Together with GNAQ, required for heart... |
Q28PF8 | MSDTVRVELGARAYDVEIGAGLIASAGARIAPLLSRPKVWIVTEETVAALHMDALRAGLDAANIASEALVLPPGEATKSWPHLQRIADWLLSERVERADIVIAFGGGVIGDLAGFAAAIHRRGIRFVQIPTSLLAQVDSSVGGKTGINAPQGKNLIGAFHQPSLVLADIDVLGTLMPRDFLAGYGEVAKYGMLGDAPFFEWLEANGPAMAKGDPALRQEAVRRSVQMKADIVARDETEQGDRALLNLGHTFCHALEAATGYSDRLLHGEGVAIGCALAFELSARLGLCSQEDPSRVRAHLAAMGTRRDLSDIPGDLPDAD... | Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+). Metabolic intermediate biosynthesis; chorismate biosynthesis;... |
A6QHI7 | MLKLNLQFFASKKGVSSTKNGRDSESKRLGAKRADGQFVTGGSILYRQRGTKIYPGENVGRGGDDTLFAKIDGVVKFERKGRDKKQVSVYAVAE | Belongs to the bacterial ribosomal protein bL27 family. |
Q128M1 | MTNRTPRISAIRSAALAALLAGLGMGAAQATEFRSADTHNADDYPTVAAVKYMGELLEKKSGGKHKIKVFNKQALGSEKETIDQVKIGALDFTRVNVGPMNAICPLTQVPTMPFLFSSIAHMRKSLDGPVGDEILKSCESAGFIGLAFYDSGARSIYAKKPIRTVADAKGLKIRVQQSDLWVALVSAMGANATPMPYGEVYTGLKTGLIDAAENNIPSFDTAKHVEAVKVYSKTEHSMAPEILVMSKIIYDKLPKAEQDMIRAAAKESVAFERQKWDEQEAKSLANVKAAGAEIVEVDKKSFQAVMGPVYDKFMTTPDMK... | Solute-binding protein that binds D-galacturonate and D-glucuronate (in vitro) (PubMed:25540822). Probably part of a tripartite ATP-independent periplasmic (TRAP) transport system that mediates solute transport into the cytoplasm. The complex is comprised of an extracytoplasmic solute-binding protein and a heteromeric ... |
Q6NSI1 | MRRSSGFGGQKGQGPSCSFTGCWCCRGDDVAESDDSPFAQCGYNIQEKHLGKLHRAASRGEVSKVECILSSGSADLDERDKKKRTALHLACANGHPEVVALLVDRGCQLDVFDNKNRTALLKAVQCQEEECATILLEHGADPDLPDVYGNTTLHYAIYNEDIPMTKKLLLHHANIESANKDELTPFLLAVHEQKQQMEDFLRKQKENLTAVKLESIHQVMSEYKENETPRNPQNSNPEGTSNKMACLGEGAAGAKVDEIPGNPVKRLFNKPSIDDSRPMSANEDFDFDTEEKATEPANGKRQNGMGIIESAPQEHTNNEN... | Could be the product of a pseudogene. |
P83621 | GFGSLFKFLAKKVAKTVAKQAAKQGAKYIANKQTE | Has antimicrobial activity against E.coli, E.faecalis, P.aeruginosa, and S.aureus. Expressed by the venom gland. Belongs to the cationic peptide 04 (cupiennin) family. 01 subfamily. |
Q8SRH0 | MSRDKSERDNLQDTTTINLRRRRRVKEGKAASKPPQVYPLMKCKLRYLKLKKLAHLLSLEDNILSLCEPDKSSEGSNSQKHVVEQLRGSPLSVGTLEEFVDDHHGIITTGVGLEYYVNIMSFVDKDLLEPGCTVLLNYKDNSVVGVLEGEMDPMVNVMKLEKAPSETYADIGGLEEQIQEIKESVELPLTNPELYQEMGIKPPKGVILYGLPGTGKTLLAKAVANQTSATFLRVVGTELIQEYLGEGPKLVRELFRVADMHAPSIIFIDEIDAIGGKRYNTSSGGRREVQRTMLELLNQLDGFDTRNDIKVIMATNKIEA... | Acts as a regulatory subunit of the 26S proteasome which degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability ... |
Q75BL8 | MSDSITNPENSEIQTNYDKIVHKFDELKLKEVLLRGIYGYGFVDPSAIQQRAILPIIEGHDVLAQAQSGTGKTGTFSIAALQRIDESIKAPQALILAPTRELALQIQKVVMALALHMDVKVHACIGGTDPREDAEALRAGAQIVVGTPGRVFDMIERRNFKTDHIKMFILDEADEMLSSGFKEQIYKIFTMLPPTTQVVLLSATMPKEVLDVTDKFMNKPVRILVKKDALTLEGIQQYYINVESEEYKYDCLSDLYDSISVTQAVIFCNTRRKVEELTKRLTDDSFTVSAIYSDLPQAQRDTIMKEFRTGSSRILISTDL... | ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal ... |
Q2SZW2 | MTTVNLAAYRFVSLDSIEQWRPLITARCNALGLRGTILLAPEGINLFIAGSRGATDAFVDYLRHDPLFEGKFADLPFKESLSDSQPFRRMLVRLKREIITMKKPAIKPELGRAPSVDARMLKAWLDRGHDDAGRPVVMLDTRNAFEVDVGTFDNALDYRIDKFSQFPGVIEANRADLEGKTVVSFCTGGIRCEKAAIHMKDVGIENVYQLEGGILKYFEEVGGAHYHGDCFVFDYRTALNPQLAPTADVTCFACRAVVPADAQQSPLYVPGKSCPACHPGDQGRRADHRADPAHAA | Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. AH2 + O2 + uridine(34) in tRNA = 5-hydroxyuridine(34) in tRNA + A + H2O Belongs to the TrhO family. |
A1VDR1 | MNISGLIIGLGNPGREYDRTRHNFGFMFIDALLEEAQRNPFARCEQLSGGKKKYDLWRCDIVEGQAPWLLAKPQTFMNLSGEAVLAIASFYRVKPAAMVVAHDELDLPLGRMRFKMGGGNAGHNGLKSITQCLGTPDFHRLRLGIGKPPAGGETTGWVLGRFSQSDTAMVDAVLEAAIQGIRTFATEGDVAATQYINAFRP | The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+) Monomer. Belongs to the PTH family. |
P17599 | MNYLRRRLSDSNFMANLPNGYMTDLQRPQPPPPPPAAPSPGATTGPATATAERASSAAPVASPAAPSPGSSGGGGFFSSLSNAVKQTTAAAAATFSEQVGGGSGGAGRGGAAARVLLVIDEPHTDWAKYFKGKKIHGEIDIKVEQAEFSDLNLVAHANGGFSVDMEVLRNGVKVVRSLKPDFVLIRQHAFSMARNGDYRSLVIGLQYAGIPSINSLHSVYNFCDKPWVFAQMVRLHKKLGTEEFPLINQTFYPNHKEMLSSTTYPVVVKMGHAHSGMGKVKVDNQHDFQDIASVVALTKTYATTEPFIDAKYDVRIQKIG... | Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release. The complex formed with NOS1 and CAPON proteins is necessary for specific nitric-oxid functions at a presynaptic level (By similarity). Homodimer. Interacts with CA... |
B7N4V3 | MTTNTVSRKVAWLRVVTLAVAAFIFNTTEFVPVGLLSDIAQSFHMQTAQVGIMLTIYAWVVALMSLPFMLMTSQVERRKLLICLFVVFIASHVLSFLSWSFTVLVISRIGVAFAHAIFWSITASLAIRMAPAGKRAQALSLIATGTALAMVLGLPLGRIVGQYFGWRMTFFAIGIGAFITLLCLIKLLPLLPSEHSGSLKSLPLLFRRPALMSIYLLTVVVVTAHYTAYSYIEPFVQNIAGFSANFATALLLLLGGAGIIGSVIFGKLGNQYASALVSTAIALLLVCLALLLPAANSEIHLGVLSIFWGIAMMIIGLGMQ... | Involved in the efflux of sugars. The physiological role may be the reduction of the intracellular concentration of toxic sugars or sugar metabolites. Belongs to the major facilitator superfamily. SotB (TC 2.A.1.2) family. |
B3BM80 | MVNATLSVVQKNSAFVGSATGELAARAIGMLYPGVKQSDLSEEQKQTISTLATVSAGLAGGLTGSSTASAAVGAQSGKNAVENNYLSTNQSLTFDKELSDCRKSGGNCQDIIDKWEKISDEQSAEIDQKLKDNPLEAQVIDKEVAKGGYDMTQRPGWLGNIGVEVMTSDEAKAYVQKWNGRDLTKIDVNSPEWTKFAVFASDPENQAMLVSGGLLVKDITKAAISFMSRNTATATVNASEVGMQWGQGNMKQGMPWEDYVGKSLPADARLPKNFKIFDYYDGATKTATSVKSIDTQTMAKLANPNQVYSSIKGNIDAAAK... | Toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (PubMed:21829394, PubMed:25174572). The C-termi... |
Q9UX31 | MKIVLAYSGGLDTTVSIRWLKETFKAEIITVTVDVGQKDDFKKIEERAYIAGASKHYTIDAVRQFANNYIAYAIKLNGLYEGVYPLSTALARPLIAEKVVEVAKKEGAEAVAHGSTSKGNDQVRFDLAVKALYPDVKIIAPARIWNMTREDEIKYAKEKGIPIKVESDKYSIDENLWGRSIEGDIISDPSLEVPEDAFEWTKQIYNKKEIVSIEFSNGVPTAVNGEKMELNKLVDFLNLKFGSHGFGRVEHIENRVVGFKSREVYEVPAALGLIYAHIDLEKTIYTPMELRFKRHIDQLWSDLVYQGLWFEPLRETLHKV... | ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+) Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. Homotetramer. Belongs to the argininosuccinate synthase family. Type 1 subfamily. |
P26412 | MALRDERVTLAHGGGGKAMRDLIEEVFTSVFQPPGMEDQARLTEAALAEPGARLAFTTDSYVVTPVEFPGGDIGKIAVCGTVNDLAVGGARPLWLSAAFILEEGTEVALLRRIVATMAREAEAAGVRIVTGDTKVVGRGACDGVFVTTSGVGVIPPGREMAAGRVRPGDVAIVNGVLGDHGATILAARGDLALTSDIESDCAALGHLMADVIAAAPGIRAARDLTRGGLASALNEIAQTAGCGLVIEETALPLRPEVVGLCEILGLDPLYLANEGRLVVFVPEAEAAAALAAMRARPEGAGACVVGRAVAEHAGQVRMRT... | Involved in the maturation of [NiFe] hydrogenases. Along with HypF, it catalyzes the synthesis of the CN ligands of the active site iron of [NiFe]-hydrogenases. HypE catalyzes the ATP-dependent dehydration of the carboxamido group attached to its C-terminal cysteine to a cyano group. ATP + C-terminal S-carboxamide-L-cy... |
P0C9M3 | MPTPLSLQTLAKKLLATQYISKDYYFILKYCGLWWHGAPIMLSTNEDNQLMIKSASFKEGLSLDLALMKVVQENNHDLIKLFTEWGADINSSLVTVNMECTRNLCRELGAKEALNERDILQIFYKTRDIKTSSHVILCHELLSNNPLFQNIERMRSIIYRSLEKLSINFILDDISFSEMLTRHWYGLAILYNLTEAIQYFYEKYKHFKNWRLICGLSFNNLSDLYEIYNLEKVDMDIDEMMYLACSMYGGNYSTIYYCFVLGADINQAMLTSVINHHIDNLFFCIDLGADAFEESMELAKQKNHNILVHILSFKNYSPDF... | Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Belongs to the asfivirus MGF 360 family. |
Q6NMK7 | MEPERLKFGGPRELCGAADLISQFKLVQHHEFFCKKSLPVSLSDSHYLHNVVGDTEIRKGEGMQLDQLIESISQSRETNIRIQPFDIDELQESFQLNDMTPVELPPAEKGAPTIPSKSKSESKDRDRKHKKHKDRDKDKDREHKKHKHKHKDRSKDKDKDKDRDRKKDKNGHHDSGDHSKKHHDKKRKHDGDEDLNDVQRHKKNKHKSSKLDEVGAIRVAG | Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a com... |
C0ME18 | MVFSKISQVAHYTPKQVISNDDLSQIMDTSHEWISSRTGIEKRHISTVEMTSDLAIRVAEQLLAGSGYDATALDFIIVATISPDASMPSTAAKVQAAIGATNAFAFDMTAACSGFVFALAMADKLIASGAYQRGLVIGAETLSKIIDWQDRSTAVLFGDGAGGVLLEASEQQHFLAEALHTDGARGQSLTSGQSSLRSPFSQGQEVNSFLQMDGRAIFDFAIRDVSRSITAIIEQSGLAKEELDYLLLHQANRRILDKMAKKIGMPREKFLENMMHYGNTSAASIPILLSESVQNGQLKLDGSQHILLSGFGGGLTWGSL... | Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-A... |
B4E5W7 | MLDREGFRPNVGIILLNARNEVFWGKRLREHSWQFPQGGIKYGETPMQAMYRELHEETGLHPEHVKIIGRTRDWLRYEVPDKFIKREVRGHYRGQKQIWFLLRMVGRDCDICLRATDHPEFDAWRWNEYWVPLDAVIEFKRDVYQLALTELSRFLRRPAQRAEKPRGPRVSRYPRVIGAQAQTLTIVDASVVCSEIEVEASTLDEMPPRVIVGK | Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage. Belongs to the Nudix hydrolase family. RppH subfamily. |
B2I8J2 | MARYIGPSCKLARREGADLSLKSPSRALDSKCKLEQRPGQHGAVRKSKLSDYASQLREKQKVKRIYGVLERQFRNYYKNASTKKGNTGENLLQLLETRLDNVIYRMGFAVTRPAARQLVSHRSVLVNGKMVNLPSYHVKPGDVVALSQRAQKYLCVQESLTIKDQHGSAFSWIEVDSEKFSGVFKALPDRADLPSDINEALIVELYSK | One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit. With S5 and S12 plays an important role in translational accuracy. Part of the 30S ribosomal subunit. Contacts protein S5. The interaction surface between S4 and S5 is involved in control ... |
Q5PLH8 | MATELTWHDVLADEKQQPYFINTLHTVAGERQSGITVYPPQKDVFNAFRFTELGDVKVVILGQDPYHGPGQAHGLAFSVRPGIAPPPSLVNMYKELEASIPGFVRPAHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVVFLLWGSHAQKKGAIIDPQRHHILKAPHPSPLSAHRGFFGCNHFALTNQWLEQHGEKTIDWTPVLPAESE | Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil. Belongs to the uracil-DNA glycosylase (UDG) superfamily.... |
Q8BHA2 | MWELRSASFWRAIFAEFFATLFYVFFGLGASLRWAPGPLHVLQVALAFGLALATLVQTVGHISGAHVNPAVTFAFLVGSQMSLLRAFCYIAAQLLGAVAGAAVLYSVTPPAVRGNLALNTLHAGVSVGQATTVEIFLTLQFVLCIFATYDERRNGRMGSVALAVGFSLTLGHLFGMYYTGAGMNPARSFAPAILTRNFSNHWVYWVGPIIGGGLGSLLYDFLLFPRLKSVSERLSILKGARPSDSNGQPEGTGEPVELKTQAL | Water channel. Channel activity is down-regulated by CALM when cytoplasmic Ca(2+) levels are increased. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core. Plays a role in cell-to-cell adhesion and f... |
A1AVI4 | MVNYAINQFKNGLKLILDGNPCSIVNNEIVKPGKGQTFNRVKFKDLITGKTLIKTFKSGETLEGADVMELDLQYLYNDGNTWNFMDLDSFEQYTIDNATMNDAKGYLVEQDMCTVTLWNDNPISVIPPNHVILEVLNTDPGLKGDTAGTGGKPATMNTGVVVQVPLFVDIGDKVKVDTRTNEYVGRA | Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation. Protein biosynthesis; polypeptid... |
Q59ME1 | MITHMVTPDSTSSAPNSPYGEDTIKLNSSVISSSSPVRSTSYLQNLQLQQQFSQLQFLQLQQQQQQQDQQLALQQQQQQQQSQSQQAQPYANPYFQTPIDQLFQFDNNPNSSFNPTRPPNIHTNQPYVSPYLHSAPLTNHSDLQPQPPPASLSDSELGLGLVKQQQDSLPPQQQAQSQPTPLLNQQHPFYNEYINDMPSTQHPYLIFNNTNAAHSTTSLPNLDAANPSSILPQSALNQSEYYKVTNGSMSNDPQPSTFLYNLHNHSADLVMNNDLEFSNASFDSIGGVSVSAAATGAGAGAGDYSHTNITSNFAQTNLHS... | Component of the RPD3C(L) histone deacetylase complex (HDAC) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progressi... |
A4XB58 | MELLHSGKVRDVYADGDDLILVASDRVSVYDVVLPTPIPEKGKLLTALSLWWFDQLAELVPNHVLSATDVPVELAGRAIRCRRLEMVPVECVARGYLVGGGFAEYQRTGVVSGIELPRGMVEAAALPEPIFTPSTKAPVGEHDQPMTFGEVVDKVGAETAERLRQITLDVYRRGAELAADRGILIADTKIELGWAADGTLTVGDELLTSDSSRFWPAESYQPGRAQFSYDKQYVRDWATRSGWDRRSPAPEVPDEVVDATRARYVDVYERLTGERWG | 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-... |
Q3V3E4 | MQMKMMFFCLSDWQSNQQMHGKMAPLKSHVPCTEKPGKVQEPPDDGSLHWSEGSKGEDIKKYSREGTLRSKYNQQYHKLFKDIPLEEVVLKVCSCALQRDLLLHGRLYISPNWLCFHASLFGKDIKVVIPVVSVQLIKKHKMARLLPNGLAITTNTSQKYVFVSLLSRDSVYDMLRRVCTHLQPSSKKSLSIRKFPEEAECESPEVLIPEMKWRKACSAPASLSLPDSISCISQIPTDSTDSCFPSRKPPGSEAVCEKDALEEEPSTDQELRLWDSRLLKVIFVMICFLVLSSSYLAFRISRLEQQLCSLSWGSPLPRDR | Participates in the organization ofendoplasmic reticulum-plasma membrane contact sites (EPCS) with pleiotropic functions including STIM1 recruitment and calcium homeostasis. Constitutive tether that co-localize with ESYT2/3 tethers at endoplasmic reticulum-plasma membrane contact sites in a phosphatidylinositol lipid-d... |
Q2G2X2 | MKRVITYGTYDLLHYGHIELLRRAREMGDYLIVALSTDEFNQIKHKKSYYDYEQRKMMLESIRYVDLVIPEKGWGQKEDDVEKFDVDVFVMGHDWEGEFDFLKDKCEVIYLKRTEGISTTKIKQELYGKDAK | Catalyzes the transfer of the cytidylyl group of CTP to sn-glycerol 3-phosphate so the activated glycerol 3-phosphate can be used for teichoic acid synthesis, via incorporation into both the linkage unit by TarB and TarF. CTP + H(+) + sn-glycerol 3-phosphate = CDP-glycerol + diphosphate kcat is 2.6 sec(-1). Cell wall b... |
B8GQ85 | MADISFSLHAEQTLESLLERMSEFDALADLDMDIIDGVLTLEFDDGGKLILNRQEAASQIWLASPEGPAHFGYDADRDAWLNDRTGESLTDTLNRVLSAGCGETIRL | Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. Belongs to the frataxin family. |
Q5XI55 | MASATLGSSSSSASPAVAELCQNTPETFLEASKLLLTYADNILRNPSDEKYRSIRIGNTAFSTRLLPVRGAVECLFEMGFEEGETHLIFPKKASVEQLQKIRDLIAVERRSRLDGSSQKVEFSQHPAAVRLPAEQPEDPTGLMQHSGNQPGQPLSLPSAPLVVGDSTIFKVLQSNIQHVQLYENPVLQEKALACIPVNELKRKSQEKLFRARKLDKGTKVSDEDFLLLELLHWFKEEFFHWVNNVVCSRCGRETRSRDEALPPNDDELKWGAKNVEDHYCDACQLSNRFPRYNNPEKLLETRCGRCGEWANCFTLCCRAL... | Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing co... |
I1BYN6 | MVRFTSFTSPFSAILLLSFGINKVATASTNTCVVAKSDSDDAITILEAFEKCKTGGTVVFPKDSTYNLNSIVTTSGLKNVNINLAGTINLPVREESYRNGDYYIQIKGTNIKMYGGGTINGNGQAWWDALDRTAPSVLRIAANDSSFGNFNIINSPRAHLNVTNSTNLLLHDFIIHTVSNNSNPAKNTDALDLYHSSGVIFRDSDLTIGDDCLAVKENVTKVTVSNITCRGGHGYSIGSLGMGGRRDFVTQVNVYNSTCIDCQNGVRVKTWAGGKGFVEDINFTDIYLEKAENPIIITTHYCDKNEMGYCNNNYETSLDI... | Specific in hydrolyzing the terminal glycosidic bond of polygalacturonic acid and oligogalacturonates. [(1->4)-alpha-D-galacturonosyl](n) + H2O = [(1->4)-alpha-D-galacturonosyl](n-1) + alpha-D-galacturonate Optimum pH is 4.0. Optimum temperature is 30 degrees Celsius. N-glycosylated. Belongs to the glycosyl hydrolase 2... |
P16202 | MNNATFNYTNVNPISHIRGSVIITICVSFTVILTVFGYIAKIFNNKNNCTNNVIGLRKHIKCSGCEPFCNKRDDISSPRTGVDIPSFILPGLNLSKSTPN | Putative viral proton channel. May play a role in virus entry (By similarity). Dimer. Belongs to the influenza viruses type B glycoprotein NB family. |
Q50740 | MPGSAGWRKVFGGTGGATGALPRHGRGSIVYARSTTIEAQPLSVDIGIAHVRDVVMPALQEIDGCVGVSLLVDRQSGRCIATSAWETLEAMRASVERVAPIRDRAALMFAGSARVEEWDIALLHRDHPSHEGACVRATWLKVVPDQLGRSLEFYRTSVLPELESLDGFCSASLMVDHPACRRAVSCSTFDSMDAMARNRDRASELRSRRVRELGAEVLDVAEFELAIAHLRVPELV | To M.tuberculosis Rv2557. |
P01310 | FVNQHLCGSHLVEALYLVCGERGFFYTPKAXXEAEDPQVGEVELGGGPGLGGLQPLALAGPQQXXGIVEQCCTGICSLYQLENYCN | Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver. Heterodimer of a B chain and an A chain linked by two disulfide bonds. Belongs to the insulin family. X'... |
Q645Y3 | MQAALMAFFMLLFSLLSLLGIAANGFIVLVLGREWLRYGRLLPLDMILISLGASRXCLQLVGTVHNFYYSARKVEYSGGLGRQFFHLHWHFLNSATFWFCSWLSVLFCVKIANITHPTFLWLKWRFPGWVPWLLLGSVLISFIITLLFFWVNYPVYQELLIRKFSGNMTYKWNTRIETYYFPSLKLVIWSIPFSVFLVSIMLLINSLRRHTQRMQHNGHSLQDPSTQAHTRALKSLISFLFLYALSFLSLIIDATKFISMQNDFYWPWQIAVYLCISVHPFILIFSNLKLRSMFWQVLLLARGFWVA | Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity). Most tas... |
A9R2X3 | MAQANLSEILFKPKFKHPETSTLVRRTHCNHVVNIHSALDGDTANHWYRMINRLMWTWRGIDPLEIEEVLSRIACSKAEHSNNELLDTVVGYRNGNWIYEWANQGMMWQQKAMEETDPGSAGQFWLNAANLYSIASYPHLKGDELSEQAEVLSNRAYEEAAKYLPYTLKELTFPISDGGSLSGFLHMPTVGSAPFPTVLMCGGLDTLQSDYHRLFRDYLEPKGIAMLTIDLPSVGASSRWKLTQDTSYLHQQVLQALADVPWVDHQRVSVFGFRFGANVAVRLGYLEPQRVRAVACLGPIVHHLLCNSDSLRKVPDMYMD... | Catalyzes the hydrolysis of esters. a carboxylic ester + H2O = a carboxylate + an alcohol + H(+) Belongs to the FrsA family. |
Q8R5X8 | MEGIIVINKPKGITSFDVIRKLKKFLKTKKIGHTGTLDPLAIGVMLVCVGKATKLASDLEAKDKVYIADFDIGYATDTYDIEGKKIAENIIEVSKENLEQSLKKFIGNIKQVPPMYSAIKIDGNKLYHLARKGIEVERPERDITIEYINLLDFKDNKAKIETKVSKGCYIRSLIYDIGQDLGTYATMTALQRKQVGEYSLENSYSLEQIEEMTLNNNFKFLKTIEEIFSYDKYNLQTEKEFILYKNGNTVKIKENLENKKYRIYFQDEFIGLANIENNNLLKGYKYY | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. uridine(55) in tRNA = pseudouridine(55) in tRNA Belongs to the pseudouridine synthase TruB family. Type 1 subfamily. |
A5GVQ6 | MTTPRQSSLEPLSIANWRWQPFLDHACGALQPLELEPYPVAPEFLLQTSQTGSKSKPVQVTTATWACKTNKLRQVRAACVEAGAAASVLNFVVNPSTSYDLPFFGADLVTLPAGHLLALDLQPALKTDAEHTKAVWERLMPIFERWQQRLPGGGPIPEEAKPYFSPGFLWTRIPLGSEGDALIEEAVKPAFRDYLELYLQLVHEAEEVSPERSAELLAGQKRYTSYRAEKDPARGMLTRFHGAEWTEAYIHGVLFDLDKKWM | Catalyzes the two-electron reduction of the C2 and C3(1) diene system of 15,16-dihydrobiliverdin. (3Z)-phycoerythrobilin + oxidized 2[4Fe-4S]-[ferredoxin] = 15,16-dihydrobiliverdin + 2 H(+) + reduced 2[4Fe-4S]-[ferredoxin] Belongs to the HY2 family. |
P30828 | PVAGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEEMMKRAIFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGERDI | RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site (By similarity)... |
Q1J924 | MARILDNNVMGNEEFSDRTLRPQYLHEYIGQDKVKEQFAIFIEAAKRRDESLDHVLLFGPPGLGKTTMAFVIANELGVNLKQTSGPAVEKAGDLVAILNELEPGDILFIDEIHRMPMSVEEVLYSAMEDFYIDIMIGAGDTSRSIHLDLPPFTLIGATTRAGMLSNPLRARFGITGHMEYYQEKDLTEIVERTATIFEIKIDHEAARKLACRSRGTPRIANRLLKRVRDYAQIIGDGIITAQITDRALTMLDVDREGLDYIDQKILRTMIEMYQGGPVGLGTLSVNIAEERNTVEEMYEPYLIQKGFLMRTRTGRVATQK... | The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. ATP ... |
Q98M18 | MTAPRKPAAFRIEPEAAPTQETPKARQAELSRKPRGLKTDVALVIPAEVDVFDEPDIVAAEPPPAAAPRKRSLFGSIFFGAIGVLVSLAVGLWTDQLIRDLFARAEWLGWLAAGMAAIAVLALVVILIREFLAIARLAEVEKLQKRALDAIARDDPKAARSVVDELSAFVAAKPETAAGRRALAELRGEIIDGGNLVRLAEAEILGPLDARAKVMILEAAKRVSLVTAVSPRALVDVAYVVFEAGRLIRRLSELYGGRPGTLGFFRLARSVLAHLAVTGSIAVGDSFVQQIVGHGLAARLSAKLGEGVVNGMMTARIGIA... | Belongs to the UPF0283 family. |
Q5R7Y1 | MASKCPKCDKTVCFAEKVSSLGKDWHKFCLKCERCSKTLTPGGHAEHDGKPFCHKPCYATLFGPKGVNIGGAGSYIYEKPLAEGPQVTGPIEVPAARAEERKASGPPKGPSRASSVTTFTGEPNTCPRCSKKVYFAEKVTSLGKDWHRPCLHCERCGKTLTPGGHAEHDGQPYCHKPCYGILFGPKGVNTGAVGSYIYDRDPEGKVQP | Interacts with TGFB1I1. |
B0R7F7 | MFKAIVSADTLQETLDSVSVLVDECKIHLDDDTLSIRAVDPASVGMVDLDLAATAFESYEADGGLIGVNLSRLEDIAGMADAGQLIQLELDEETRKLHIQIDGLEYTLALIDPDSIRQEPDIPDLDLPAHVAIEGRDIDRAVTAADMVSDHIALGVDTGDDLFYVNAEGDTDDVHLELAPDQLIDLDAGDAHSLFSLDYLKDMNKAIPTTAEVELELGDEFPIKLHFDIADAQGHVTYMLAPRIQSN | Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication. Homotrimer. The subunits circularize to form a toroid; DNA passes through its center. Replication factor C (RFC) is required... |
P20158 | KICRRRSAGFKGPCMSNKNCAQVCQQEGWGGGNCDGPFRRCKCIRQC | Inhibits protein translation in cell-free systems. Belongs to the DEFL family. Was initially thought (PubMed:2226781 and PubMed:8380707) to be a thionin. |
C1AG91 | MTARPLSELVERGWAAALEPVADQVAHMGQFLRAEIAAGRRYLPAGSNVLRAFTFPFDNVRVLIVGQDPYPTPGHAVGLSFSVAPDVRPWPRSLANIFDEYTADLGYPLPSNGDLTPWAQRGVLLLNRVLTVRPSNPASHRGKGWEAVTECAIRALAARAAPLVAILWGRDASTLKPMLAAGNCVAIESPHPSPLSASRGFFGSRPFSRANELLVGMGAEPIDWRLP | Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil. Belongs to the uracil-DNA glycosylase (UDG) superfamily.... |
A8LYC4 | MGERTWPQLLAALLRGDELSTADTAWAMGEIMSGSAGSAQIAGFAIALRAKGETPAEVSGLVEAMLQHAVRVELPEDLRATAVDVVGTGGDLAHTVNISTMASLVVAGAGVRVVKHGNRAASSSCGTADVLEFLGLPLDLGPEGVAACVAEAGIGFCFAARFHPGMRHAGPVRRELGVPTAFNFLGPLTNPARPRAGAVGCFDARMAPVMAAVFAARGDSTLVLRGEDGLDEFTTAAPTRVWAAQNGTVREALLDAADLGVPRATLADLRGGDVACNADAVRRLLAGETGPIRDAVLVNAAAALATQAPLDGDLTEALRT... | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose 1-diphosphate + anthranilate Binds 2 magnesium ions per monomer. Amino-acid... |
B7M1A9 | MATVSMRDMLKAGVHFGHQTRYWNPKMKPFIFGARNKVHIINLEKTVPMFNEALAELNKIASRKGKILFVGTKRAASEAVKDAALSCDQFFVNHRWLGGMLTNWKTVRQSIKRLKDLETQSQDGTFEKLTKKEALMRTRELEKLENSLGGIKDMGGLPDALFVIDADHEHIAIKEANNLGIPVFAIVDTNSDPDGVDFVIPGNDDAIRAVTLYLGAVAATVREGRSQDLASQAEESFVEAE | Belongs to the universal ribosomal protein uS2 family. |
Q6FNG9 | MQLQDLVVTVSLLAAFNGGVEAWSPTNSYVPANVTCPNDINLLRNATGLSQSEIDWLKKRDVNTREALESFLKRVTSNFTSNSSASNLIDQLFSTNSSNIPKIGIAASGGGYRAMLSGAGMVSAMDNRTDGANEHGLGGLLQAATYLAGLSGGNWLTTTLSWNNWTSVQDIVDSQDNDSAIWDISHSIVSPGGINIFKTGSRWDHISDAVEDKQKAGFNVSLADVWGRALSYQFFPTLYRGGVAYLWSDLRESDVFKNAEMPMPISVADGRYPGTAVIDLNSTVFEYSPFELGSWDPSLSAFTDVQYLGTKVSDGKPAEE... | Catalyzes the release of fatty acids from lysophospholipids. Phospholipase B may well contribute to pathogenicity by abetting the fungus in damaging and traversing host cell membranes, processes which likely increase the rapidity of disseminated infection (By similarity). a 1-acyl-sn-glycero-3-phosphocholine + H2O = a ... |
A3PFA2 | MRSSWIKPRLGKDNVTQMNFARNGYITEEMDFVAKKENLPPSLIMEEVARGRLIIPANINHLNLEPMSIGVASRCKVNANIGASPNASDINEEVEKLKLAVKYGADTVMDLSTGGVNLDEVRQAIIQESPVPIGTVPVYQALESVHGSIDRLTEDDFLHIIEKHCQQGVDYQTIHAGLLIEHLPKVKGRITGIVSRGGGILAQWMLHHFKQNPLYTRFDDICEIFKKYDCTFSLGDSLRPGCLHDASDDAQLAELKTLGELTRRAWEHNVQVMVEGPGHVPMDQIEFNVRKQMEECSEAPFYVLGPLVTDISPGYDHISS... | Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deo... |
W3WT07 | MFQSILFLAFYGRPVFGSAAARDYACVNTAESRDCWKDGFNIETDYYGKEEAPEGKLVEYELTLSQQIISPDGYEMLGMVVNGQYPGPTIEADWGDTLRITVKNNFTENYNGTAVHWHGIRQKETNWLDGVPGVTQCPITPGDSQVYEFRVTQYGTSWYHSHYSLQYSNGAYGPIVIHGPSSANWDVDLGPWLLSDWYHDDAFALDHVGITTNRAAIPKSSLINGKGYYECDPTNDAKCTGTRDYYEVVLKQGTKYKFGIINTSTILTYTFWIDGHNFTIIAIDFVPIEPLTVDTLNVGIGQRYEIIIETNPDFDDDSSF... | Oxidoreductase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes (PubMed:24302702). The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA (PubMed:24302... |
Q06903 | MSGKARLHYPVTRQSEQLDHYFGQAVADPYRWLEDDRSPETEAWVKAQNRVTQDYLAQIPFRDAIKGKLATSWNYAKEGAPFREGRYHYFFKNDGLQNQNVLCGQLAGKPAEVFLDPNLLSPDGTTALDQLSFSRDGKTLAYSLSLAGSDWREIHLMDVESKQPLETPLRDVKFSGISWLGNEGFFYSSYDKPDGSELSARTDQHKLYFHRLGTAQEEDRLVFGAIPAQRHRYVGATVTEDDRYLLISAADSTSGNRLYVKDLTREGAPLLTVQGDLAADVSLVDNKGSRLYLLTNRDAPNRRLVTVEADNPGPEQWRDL... | Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. Has an absolute requirement for an X-Pro bond in the trans configuration immediately preceding the Pro-Y scissible bond. Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides. Belongs to the... |
Q1H1I4 | MLISQPPAIFLMGPTASGKTGLAVELVQAMPLEIISVDSALVYQDMDIGTAKPGQEVLQRAPHHLIDVIDPMQVYSAAQFREDALRLMADITARGKAPLLVGGTMLYFRTLEQGLGGLPEADAQVRAELDREAAKIGWPGMHAKLAAIDPETAARLQPADSQRIQRALEVYRLTGKSMTALHRQQAAEILPYRLLKIALQPSDRSVLHARIAERFVAMMKGGLLEEVQGLLKKYPGLHPDMTSMRCVGYRQTLEYLAGNIDDEAWKAQGIAATRQLAKRQLTWLRGMDDTLVLDCLEQDVYGQAQRAISGFLSAV | Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA Monomer. Belongs to... |
A4XLW0 | MTKKEIAKFIDHTFLKSNATHADIKKLCDEALKYSFASVCVNPYYVKVCKEYLKDSPVKVATVVGFPLGATSMKTKIFEAKEAFEDGADEIDMVINIGALLEGNVDYVYEEIKNIVDIARGYKNKIVKVIIETSELSDQQKIEACKIVMDAGADFVKTSTGFSKSGAKYEDILLMRKVVGDKIKIKASGGIRTYEDALEMIEAGASRIGTSSGVAIVSED | Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate. 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehy... |
Q8L9H6 | MTHVLVRRQGQGKKRRWDVNMTMCFFLFFFVFYVSFQIVLSSSASVGYSRLHLVASPPPPPPRKALRYSTAPFRGPLSRDDIYGDDKRVVHTGPNPLHN | Extracellular signal peptide that regulates cell fate. Represses root apical meristem maintenance. Regulates the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem; this signaling pathway requires CRN and CLV2 (PubMed:28607033). Mo... |
Q63601 | MAGSTTIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMDQNLKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDKLKCTKEEHLCTQRMLDQTLLDLNEM | Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing c... |
Q4FN38 | MKKDIHPDYHTIKVEMTDGTQFETRSTWGKEGEVLKLEIDPKSHAAWTGGKQKLMDKGRVSKFNKKFQNFRSEKKD | Binds the 23S rRNA. Part of the 50S ribosomal subunit. Belongs to the bacterial ribosomal protein bL31 family. Type A subfamily. |
C3LEQ2 | MKIYVDADACPVKDVIIFEATKAEIPVILVTSFSHYSNAEQPKGVETIYVDSGADAADYRIMQLAQKEDLIVTQDYGLASLALAKGCIVLHHKGYKYTNENIEQLLQTRYLSAMVRKSGKRTKGPKPFTAEDKEKFRALFKSMIAL | Belongs to the UPF0178 family. |
Q7NE01 | METRYNPHAIEPRRQKQWEEAPHLAMDGRPKFYALSMFPYPSGALHMGHVRNYSITDVISRYKRMRGFNVLHPIGWDAFGLPAENAAIDRGIHPAQWTEQNIAQMREQLKRLGFAYAWEREVATCSPAYYRWTQKLFLEFWKAGLAYRKAGVVNWDPVDQTVLANEQVDAEGRSWRSGALVEKRPLEQWYLKITDYAEELLQALGTLGDWPERVRVMQENWIGKSVGAELCFPINGEPEGIRVFTTRPDTVYGVTYLVLAPEHPLVERITAPERREAVRAFVAQVQSESEIERVSEDRPKQGVSTGAVALNPFTGQAVPV... | ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu) Belongs to the class-I aminoacyl-tRNA synthetase family. |
B2IEP2 | MSRRCELTGKAVLTGNLVSHSNRKTRTRFLPNLCNVTLISDTLQRRIHFRVAAATLRSVEHRGGLDAFLVKAADAQLSPGALSVKREIVKKQAAAAAQ | Belongs to the bacterial ribosomal protein bL28 family. |
B3H341 | MSRVCQVTGKRPAVGNNRSHALNATRRRFLPNLHTHRFWVESENRFVTLRLTAKGMRIIDKKGIDAVLAEIRARGEKI | Belongs to the bacterial ribosomal protein bL28 family. |
Q3SWK6 | MARVKRGVTAHAKHKKVYKVTKGFSGRRKNTIRAAKAAADKAGQYAFRDRKRKKRTFRALWIQRLNAAVRPFGMTYSRFIDGLSKSGITVDRKVLSDLAINEPAAFQAIAEKAKAALAA | Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit. Belongs to the bacterial ribosomal protein bL20 family. |
P59497 | MCYSKINNSLRKRFRTFYPVVIDIETAGFNPETDAILEIAIITLKMNEFGLLEKEHLLHFHIQPFKGSRIDKKAIEFHGIDPFSPLRRAISEYEALYSIFNLIHKGIKSNNCTKSIIVAHNAIFDYNFLTAAITRTKIKNNPFHSFVIFDTATLSGLAVGQTVLARACKAIGLTFDNNQAHSALYDTQQTANLFCKIVNRWKTLGGWPPNDTRTIKL | Trims short 3' overhangs of a variety of RNA species, leaving a one or two nucleotide 3' overhang. Responsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis. Binds two Mg(2+) per subunit. The active form of ... |
Q8L720 | MALNFSHRPFSSHLSEEPMMIANGNWCSSFDNGRKNTGGDASSVDILDVLPSDPFGMDINNTFTAITGWLEDLEDDYNNQYGRRRRDDIWIGDGNRQQLFAGLSFFWNNAMQFQSSGYSYGSESLFGGAFDGSLFSTCKFPESSGENNGFGGALDGDGSCHGAFISASSVDEVLSHENARNGEVVGSSDRCNNGEEDAYVHPAIGFCLYHLRGKDLLSVSMVCKSLHTTVCDDTLLWKHIHICRPLNEKITEEALLHLTERAQGTMQCLRIVDCCRITDDCLKRVVARNRQVVKIGVPGCTRITIDGILSVLRDLKSAGK... | Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Protein modification; protein ubiquitination. Part of a SCF (ASK-cullin-F-box) protein ligase complex (By similarity). Interacts with CUL1, SKP1A/ASK1 and SPK... |
C8ZCN3 | MSQYKTGLLLIHPAVTTTPELVENTKAQAASKKVKFVDQFLINKLNDGSITLENAKYETVHYLTPEAQTDIKFPKKLISVLADSLKPNGSLIGLSDIYKVDALINGFEIINEPDYCWIKMDSSKLNQTVSIPLKKKKTNNTKLQSGSKLPTFKKASSSTSNLPSFKKADHSRQPIVKETDSFKPPSFKMATEPKVYRVVDDLIEDSDDDDFSSDSSKAQYFDQVDTSDDSIEEEELIDEDGSGKSMITMITCGKSKTKKKKACKDCTCGMKEQEGKEINDIRSQQDKVVKFTEDELTEIDFTIDGKKVGGCGSCSLGDAF... | 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 scaffold complex CF... |
G5E9W4 | MCMVIFAPLFAIFAFATCGGYSGGLRLSVDCVNKTESNLSIDIAFAYPFRLHQVTFEVPTCEGKERQKLALIGDSSSSAEFFVTVAVFAFLYSLAATVVYIFFQNKYRENNRGPLIDFIVTVVFSFLWLVGSSAWAKGLSDVKVATDPKEVLLLMSACKQPSNKCMAIHSPVMSSLNTSVVFGFLNFILWAGNIWFVFKETGWHSSGQRYLSDPMEKHSSSYNQGGYNQDSYGSSSGYSQQASLGPTSDEFGQQPTGPTSFTNQI | Intrinsic membrane protein of small synaptic vesicles. Probable vesicular channel protein (By similarity). Belongs to the synaptophysin/synaptobrevin family. |
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