UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 5
15.6k
| Functional Description
stringlengths 6
12.4k
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Q1H3M3
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MSNLLVELFVEELPPKALQNIGISFADQIYHSLVTQDLIEPPSELDAANPSPWKWFASPRRIAVWIRNVTQKAPDKQLAQKLMPASVGLDADGNATPALLKKLAALGADESAVSQLKREHDGKAEVLLLDRTVRGATLAEGLQKALDEAIAKLPIPKVMTYQLEDGWSNVNFVRPAHGLVALHGNEVVPIRALGLTAGNRTQGHRFEATQSPIVLRNADSYAEQLQQDGAVIPGFKERRDEIARQLEAAAGKLKLRPIEDEALLEEVTALVERPNVLVGQFEQAFLAVPQECLILTMKANQKYFPLLDAQGRLTNKFLIVSNISPADPSAVVGGNERVVRPRLADAKFFFEQDRKKTLESRIPGLSKVVYHNKLGSQGERIARVSEIANLVGTALGDQTLAAQASQAAQLAKADLVTDMVGEFPELQGIMGRYYAQHEGLSDDIAYAIEDHYRPRFSGDALPRNKVGMIVALADKLETLAGLFSIGEKPTGEKDPFALRRHAIGILRILTEGGLSLPLNTLLEQTLSVFQHEFDHDTALQAVEEFIFDRLSGSLRDQGYSVQEVDAVLAMKPQLLGDITKRLEAVRAFASLPEAASLAAANKRVGNILKKSDSAIEAAINPALLQEDAEKTLAQALAQVQPQAQQAFAAGDYTGSLKALAALKAPVDAFFDHVMVNAEDPALKTNRLALLATLHQAMNQVADLSRLAA
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ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly) Tetramer of two alpha and two beta subunits. Belongs to the class-II aminoacyl-tRNA synthetase family.
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Q4QNM4
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MSIILGIDPGSRVTGYGVIRQTGRHLEYLGSGAIRTQVEDLPTRLKRIYAGVTEIITQFQPNMFAIEQVFMAKNADSALKLGQARGTAIVAAVNNDLPVFEYAARLVKQTVVGIGSADKVQVQEMVTRILKLSDKPQADAADALAIAITHAHSIQHSLHIANSVKMTETQEKMTALLKTRYSRGRFRLKI
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Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction). Binds 1 Mg(2+) ion per subunit. Belongs to the RuvC family.
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P0C8J3
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LFDPPDSXPXY
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Regulatory subunit of the blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) in a calcium-dependent manner by cleaving the Arg-Ile bond at position 234. Weakly hydrolyzes insulin B chain, fibrinogen and some components of the extracellular matrix in vitro, but does not activate prothrombin or plasminogen. Heterotrimer; disulfide-linked. The heterotrimer consists of 1 heavy chain (a metalloproteinase) and 2 light chains: LC1 and LC2. Expressed by the venom gland. N-glycosylated. Calcium is required for ligand binding. Belongs to the snaclec family.
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O22150
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MRKIIGFRIGRRVSRWIFRKTRIQRSGYNRIHSTQQACMLMRPLAKLKSWGQRLKQSFRRRSTRRSAYIPVDHKKADPVPRGHLAIYVGQKDGDCHRVLVPIVYFNHPLFGELLREAEKEYGFCHEGGITIPCLYSDFERVKTRIASGSSSRVFPWGRHCRN
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Acts a positive regulator of leaf senescence and may mediate auxin-induced leaf senescence (PubMed:23250625). Plays a role in the regulation of seed germination by gibberellins and abscisic acid (ABA). Plays a role in the regulation of light-dependent hypocotyl elongation (PubMed:23503980). Expressed in embryo, endosperm, growing hypocotyls and shoot apical meristems. By senescence (PubMed:14617064, PubMed:23250625). Induced by auxin (PubMed:23250625, PubMed:23503980). Down-regulated by gibberellin (PubMed:23503980). Increased leaf size and delayed senescence. Belongs to the ARG7 family.
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P85672
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GSTGLIPFGRT
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Mediates visceral muscle contractile activity (myotropic activity). Belongs to the periviscerokinin family.
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C1DLR3
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MARFFRRRKFCRFTAEGVKEIDFKDLNTLKAYISETGKIVPSRITGTKARYQRQLATAIKRARYLALLPYTDSHGR
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Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit. Part of the 30S ribosomal subunit. Forms a tight heterodimer with protein S6. Belongs to the bacterial ribosomal protein bS18 family.
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Q3B5U3
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MKPLIALVGRPNVGKSTLFNRILREKAAIVDPTPGVTRDRHIAEGHWQGREFRLMDTGGYAPEDGVISTAMLEQTMMAIQDADIIIFLADVRSGVSYDDLELAKILKRDFSDKPIFLAVNKAESPQLAIEAASFVSTGFTEPWAISARDGSGVADLLDEILLTFPESDGPPEEDGAIRLAVIGRPNVGKSSFVNALLGSNRQIVSSIPGTTRDAIDTRFTRKQQEFMLIDTAGLRKRTKISAGIEYYSSLRSERAIERCEVAIVMLDATPGIEKQDLKIINIAAERKRGVLLLVNKWDLVEKDSKTSKQYEESLRSHMGNLSYIPVIFTSALTKKNLYRAIDTAKEISQNRSRKISTSALNRFLEEALAANHPSTRTGKELKIKYMTQIEAPWPVFAFFCNNPELVQTNFRKFLENKLREKFSLEGVTISLRFMQK
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GTPase that plays an essential role in the late steps of ribosome biogenesis. Associates with the 50S ribosomal subunit. Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngA (Der) GTPase family.
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P04874
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MMSHQQVQMDLILMQGIWTSVLKMQNHSTLLQLGSSSSMPQRPRLLSRVSQRGRLTLNLESGRWRLSIIIFLETGTTQLVTTILPSTDYLGI
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Inhibits host transcriptional machinery, by producing modifications to the phosphorylation state of the C-terminal domain (CTD) of RNA polymerase II. Inhibits phosphorylation at serine 2 in the heptapeptide repeat (YSPTSPS) of the CTD of RNA polymerase II, suggesting that the elongation step of transcription and/or 3'-end processing is prevented. Inhibition of host transcription machinery leads to shut off of host cell protein synthesis and inhibition of the host innate immune response. NSs also seems to be involved in the nuclear relocalization of host PABP1 (By similarity). Produced by alternative initiation in the N gene, but encoded on another frame. Belongs to the orthobunyavirus NS-S protein family.
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C8VBV0
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MTTDSYPKKYDIVIVGAGPVGILLSLCMSRWGYKVKHIDNRPVPTATGRADGIQPRSTEILRNLGLKRKIMAYDPAKVYDVSFWDPRPDGSGIMRTGNWPSCPRFIDTRYPFTTLVHQGKIETVFLDEIKKAGTTVERPWTIIGFKNDGLDATYPVQVQLKCLDTNVVETVRAKYLFSGEGARSFVREQLGIQIRHKDPISYVWGVMDGVVRTDFPDIQTKCTIHSDAGSIMVIPREDDMVRLYVQIASSSDPDFNPRKTATAEEVQNVAKKILKPYYIEWDRVEWYSVYPIGQGISEKYTLDERVFMGGDACHTHSPKAGQGMNTAFHDALNMAWKLHAVESGLAQRSILSTYETERKNIAETLLDFDNKYAALFSKRRPNAGEVGEAATAETGRSAEEDPFVKTFKDSCEFTSGYGVAYLPNIFNWDPSHPAKSPLFDVPGINLVTGKAFTPSTVTRLADSNFVHLEQEIPANGAFRIFIFAGRQSRSKKAIADFAANLEKERSFLSAYRRSDIGEISFFERHNPHSKLFTLCLIYAEKKNDIDMDSIPQILRDYRYHIYSDDIPDVRVPNATYAAHEKLGFDPEKGGVVVTRPDSHIACTVQLAEGSGTVDALNAYFGSFSTKPLGQEQASRL
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FAD-dependent monooxygenase; part of the benzoic acid degradation pathway also known as the protocatechuic acid pathway (PubMed:25479309). Benzoic acid debradation begins with the conversion of benzoic acid into 4-hydroxybenzoic acid through hydroxylation by the benzoate-4-monooxygenase bphA, and its partner NADPH-cytochrome P450 reductase cprA which act as a mediator in electron donation from NADPH (By similarity). 4-Hydroxybenzoic acid is then converted into 3,4-dihydroxybenzoic acid (also called protocatechuic acid) by the p-hydroxybenzoate-m-hydroxylase phhA (Probable). Protocatechuic acid is converted into 3-carboxy-cis,cis-muconic acid by the intradiol ring-cleavage dioxygenase prcA, which is further metabolized through the 3-oxoadipate pathway to finally enter the tricarboxylic acid cycle (TCA) (Probable). 4-hydroxybenzoate + H(+) + NADH + O2 = 3,4-dihydroxybenzoate + H2O + NAD(+) 4-hydroxybenzoate + H(+) + NADPH + O2 = 3,4-dihydroxybenzoate + H2O + NADP(+) Binds 1 FAD per subunit. Expression is largely up-regulated in the presence of benzoate. Belongs to the PheA/TfdB FAD monooxygenase family.
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Q5DRD7
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MENGGAGTLQIRQVLLFFVLLGMSQAGSETGNFLVMEELQSGSFVGNLAKTLGLEVSELSSRGARVVSNDNKECLQLDTNTGDLLLSEMLDREELCGSNEPCVLYFQVLMKNPTQFLQIELQVRDINDHSPVFLEKEMLLEIPENSPVAAVFLLESAKDLDVGINAVKSYTINPNSHFHVKIRVNPDNRKYPELVLDKALDYEELPELSFILTALDGGSPPRSGTALVRVVVVDINDNSPEFEQAFYEVKILENSILGSLVVTVSAWDLDSGTNSELSYTFSHASEDIRKTFEINQKSGDITLTAPLDFEAIESYSIIIQATDGGGLFGKSTVRIQVMDVNDNAPEITVSSITSPIPENTPETVVMVFRIRDRDSGDNGKMVCSIPEDIPFVLKSSVNNYYTLETERPLDRESRAEYNITITVTDLGTPRLKTEHNITLLISDVNDNAPAFTQTSYTLFLCENNSPALHIGSISATDRDSGTNAQVTYSLLRSQDPHLPLASLVSINADNGHLFALRSLDYEALQAFEFRVGASDHGSPALSSEALVRVLVLDANDNSPFVLYPLQNGSAPCTELVPRAAEPGYLVTKVVAVDGDSGQNAWLSYQLLKATEPGLFGVWAHNGEVRTARLLSERDAAKHRLVVLVKDNGEPPRSATATLHVLLVDGFSQPYLPLPEAAPAQAQADSLTVYLVVALASVSSLFLFSVLLFVAVRLCRRSRAAPVGRCSVPEGPFPGHLVDVSGTGTLSQSYQYEMCVTGGSRSNEFKFLKPIIPNFLPQSTGSEVEENPPYQNNLGF
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Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
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P41956
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MINIPTAILCRLGARSSISRSFGTSIVTKSEAKTPIQKFGWEYLLKQRSKNRPIAPHLTVYQPQLTWMLSGFHRISGCVMAGTLLVGGIGFAVLPFDFTAFVDFIRSWNLPCAVTAVFKYIIAFPIIFHTLNGIRFLGFDLAKGVNNVGQIYKSGYLVSGLSAILALAIVFNSCQNKSNKTA
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Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) (By similarity). Mediates resistance to enteropathogenic E.coli infection (PubMed:16091039). The heme is bound between the two transmembrane subunits. Carbohydrate metabolism; tricarboxylic acid cycle. Component of complex II composed of four subunits: a flavoprotein (FP), iron-sulfur protein (IP), and a cytochrome b560 composed of two integral membrane proteins. Is expressed at a constant level throughout development. Belongs to the cytochrome b560 family.
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P86443
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YSQVARPRF
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Accelerates ovarian maturation in females. Widely expressed in the nervous system. Expressed in corpora cardiaca, hypocerebral ganglion, frontal ganglion, protocerebrum, antennal lobe, tritocerebrum, thoracic ganglia, esophageal nerves, recurrent nerve and frontal connectives. Not detected in corpora allata, circumesophageal connectives, subesophageal ganglion, abdominal ganglion and abdominal perisympathetic organs. Belongs to the NPY family.
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Q9YGU0
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MMDFDERVSVGSNMYLPSCTYYVPGADFSTLPSFLSQSPSTRPVTYSYASNLPQVQHVREVTFRDYAIDPSTKWPHRGPLAHCYPSEDSVHKECLPAVTTVGEMFPKNNASAYYHSTSNTTSASNFYGNVGRNGVLPQAFDQFFDTAYGGSDSVVDNDYAARDKMHSSKQSTPAPAPEQQPEGKERPETSSPESSSGNNEEKTSGANSGPRFRKKRCPYTKFQIRELEREFFFSVYINKEKRLQLSRMLNLTDRQVKMWFQNRRMKEKKLNRDRLQYYSTNPLL
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Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Belongs to the Abd-B homeobox family.
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B3N7D5
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MGSDDQSAGDRIQKGFQINYMILRDADSGKIIWQENKDFSAPDQEHEARVPVKILEMRAVSREINFSTIESMENFRLDQKVLFKGRIMEEWFFEMGFVGANTTNTWQSTIEAAPESQMMPAKVLNGNVTIQTSFYDNETLITKSVVRLYYI
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Interacts with Pde6. Belongs to the PDE6D/unc-119 family.
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A1K607
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MIELGVNIDHVATLRQARRTWEPDPTWAAVEAHLGGADGITVHLREDRRHIQDDDVRRLRELTQIKLNLEMAATDEMVGIARSIKPEMAMLVPEGRHEVTTEGGLDIVSQEARLKDVIARLADAGIVTSVFIDAEIAQIDAAARIGARVCEIHTGPYAHAFHAQGRDAESPAVLAEIDKIRRAGEAICSHGMRFNAGHALNYYNVQPIARLPGIRELHIGHAIVSRAVFSGIREAVAEMKRLMREAAAG
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Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate. 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = H(+) + 2 H2O + phosphate + pyridoxine 5'-phosphate Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5. Homooctamer; tetramer of dimers. Belongs to the PNP synthase family.
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Q6MAK8
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MLYPLSILTSEKNVFNEDVYSVNVPGADGYFEVLAHHATVIALLQPGKLTIINKDHQKLYFGITTGFIEVSHNSATIIADAIESVQEIDVERAKQSYERAKMRLESPDKHVDKERAKRSLNRAKNRIKLFLEIHPQVSFIPLKALLI
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Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family.
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Q2KDY8
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MAKRVTGPEIEKLIQLLAKVPGLGPRSARRAALHLIKKKDQLLGPLSNAMGEAYDKVKICSRCGNVDTVDPCTVCTDTQRDQSVIIVVEDVSDLWALERAGAMNAAYHVLGGTLSPLDGIGPDDLNIRGLIDRVGEGGIRELIIAVNATVEGQTTAHYITDQLQGLDVKITRLAHGVPVGGELDYLDEGTLAAALRARTVI
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May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO. Belongs to the RecR family.
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Q6M0Z5
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MVGTPLFSNAKKILLLGSGELGKEVIIEAQRFGVECIAVDSYENAPAMQVAHKYHIIDMKDAGALRAVIEKEKPDLIVPEIEAINTDTLKEMESEGYHVVPTANATKLTMDREGIRRLAFEKLGLRTAKYEFAENLEELKEAVTRIGIPCIIKPIMSSSGKGQSTIKSESDIKTAWNYAKSAARGIGTKVIVEEFIKFDYEITLLTARTAEGTRFCEPIGHIQVDGDYHESWQPHPMCAPTKAKAQEMAKKITDELGGYGIFGVELFVLDDEVIFSEVSPRPHDTGMVTMVTQKMSEFEIHARAILGLPVNVDIVSPGASHVIKSEILKWAPEYEIHEASKVKDTKIRLFGKPIAKVGRRMGVALAVSDDVIKAREHAEKVAHLVKIK
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Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate. ATP + formate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide = ADP + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (formate route): step 1/1. Homodimer. Belongs to the PurK/PurT family.
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Q7AKU2
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MKKQERQRYIKRLLSSNEIERQEDFVKLLRAEDIDVTQATISRDIKDMQLVKVPSATGGYHYSMPVQKQMDTEKKLKRTLKDAYVSYATQDKFVLIKVLPGNGPALATLIEAMHYDEIFGTLGDDAHVLIICKSLAMTLELQQKIQRLLSDH
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Regulates arginine biosynthesis genes. Amino-acid biosynthesis; L-arginine biosynthesis [regulation]. Belongs to the ArgR family.
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P58450
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GLPICGETCVGGTCNTPGCSCSWPVCTRN
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Probably participates in a plant defense mechanism. The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. This is a cyclic peptide. Belongs to the cyclotide family. Moebius subfamily. This peptide is cyclic. The start position was chosen by similarity to OAK1 (kalata-B1) for which the DNA sequence is known.
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B5FHV3
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MNRLPSSASALACSAHALNLIEKRTLNHEEMKALNREVIDYFKEHVNPGFLEYRKSVTAGGDYGAVEWQAGSLNTLVDTQGQEFIDCLGGFGIFNVGHRNPVVVSAVQNQLAKQPLHSQELLDPLRAMLAKTLAALTPGKLKYSFFCNSGTESVEAALKLAKAYQSPRGKFTFIATSGAFHGKSLGALSATAKSTFRRPFMPLLPGFRHVPFGNIDAMSMAFSEGKKTGDEIAAVILEPIQGEGGVILPPQGYLTEVRKLCDEFGALMILDEVQTGMGRTGKMFACEHENVQPDILCLAKALGGGVMPIGATIATEEVFSVLFDNPFLHTTTFGGNPLACAAALATINVLLEQNLPAQAEQKGDTLLDGFRQLAREYPNLVHDARGKGMLIAIEFVDNETGYRFASEMFRQRVLVAGTLNNAKTIRIEPPLTLTIELCEQVLKSARNALAAMQVSVEEV
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Catalyzes the aminotransferase reaction from putrescine to 2-oxoglutarate, leading to glutamate and 4-aminobutanal, which spontaneously cyclizes to form 1-pyrroline. This is the first step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate (gamma-aminobutyrate or GABA) via 4-aminobutanal. Also functions as a cadaverine transaminase in a a L-lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. 2-oxoglutarate + an alkane-alpha,omega-diamine = an omega-aminoaldehyde + L-glutamate 2-oxoglutarate + putrescine = 1-pyrroline + H2O + L-glutamate 2-oxoglutarate + cadaverine = 5-aminopentanal + L-glutamate Amine and polyamine degradation; putrescine degradation; 4-aminobutanal from putrescine (transaminase route): step 1/1. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. Putrescine aminotransferase subfamily.
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P15069
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MMPRIKPLLVLCAALLTVTPAASADVNSDMNQFFNKLGFASNTTQPGVWQGQAAGYAYGGSLYARTQVKNVQLISMTLPDINAGCGGIDAYLGSFSFINGEQLQRFVKQIMSNAAGYFFDLALQTTVPEIKTAKDFLQKMASDINSMNLSSCQAAQGIIGGLFPRTQVSQQKVCQDIAGESNIFADWAASRQGCTVGGKSDSVRDKASDKDKERVTKNINIMWNALSKNRMFDGNKELKEFVMTLTGSLVFGPNGEITPLSARTTDRSIIRAMMEGGTAKISHCNDSDKCLKVVADTPVTISRDNALKSQITKLLASIQNKAVSDTPLDDKEKGFISSTTIPVFKYLVDPQMLGVSNSMIYQLTDYIGYDILLQYIQELIQQARAMVATGNYDEAVIGHINDNMNDATRQIAAFQSQVQVQQDALLVVDRQMSYMRQQLSARMLSRYQNNYHFGGSTL
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Involved in pilus assembly.
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C0HLN4
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AGCKYLFGSCKEDSDCCKHLGCRRKAPQYCGWDGTF
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Gating-modifier toxin that targets voltage-gated sodium channels. Inhibits the inactivation of Nav1.7/SCN9A. Expressed by the venom gland. The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. Exists in two forms, due to cis-trans isomerization at 33-Asp-Gly-34. The cis isomer also acts by shifting activation of the Nav1.7/SCN9A channel to more depolarized voltages.
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Q7KLW8
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MVSLLQEIDTEHEDMVHHAALDFYGLLLATCSSDGSVRIFHSRKNNKALAELKGHQGPVWQVAWAHPKFGNILASCSYDRKVIVWKSTTPRDWTKLYEYSNHDSSVNSVDFAPSEYGLVLACASSDGSVSVLTCNTEYGVWDAKKIPNAHTIGVNAISWCPAQAPDPAFDQRVTSRSAAVKRLVSGGCDNLVKIWREDNDRWVEEHRLEAHSDWVRDVAWAPSIGLPRSQIATASQDRHVIVWSSNADLSEWTSTVLHTFDDAVWSISWSTTGNILAVTGGDNNVTLWKENTEGQWIRINYESGTAIQSKQPSHLPHSHSQQQQALQQHQQQAPSHPGPSSDSEHSSNLSNSQLSN
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Functions as a component of the nuclear pore complex (NPC) and the COPII coat (By similarity). At the endoplasmic reticulum, SEC13 is involved in the biogenesis of COPII-coated vesicles (By similarity). Recruited to transcriptionally active chromatin at the time of transcription initiation by RNA polymerase II (PubMed:20144761). Required for proper expression of ecdysone-responsive genes such as Eip74EF and Eip75B during larval development (PubMed:20144761). Required for reactivation of transcription after heat shock (PubMed:20144761). Required for nuclear import of phosphorylated Mad via importin msk (PubMed:20547758). Has no role in classical nuclear localization signal (cNLS)-dependent nuclear import via importin-beta (PubMed:20547758). A component of the GATOR subcomplex GATOR2 which functions as an activator of the amino acid-sensing branch of the TORC1 signaling pathway (PubMed:27166823). The two GATOR subcomplexes, GATOR1 and GATOR2, regulate the TORC1 pathway in order to mediate metabolic homeostasis, female gametogenesis and the response to amino acid limitation and complete starvation (PubMed:27166823). GATOR2 activates the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex, controlling the switch to cell proliferation and growth under nutrient replete conditions and during female oocyte development (PubMed:27166823). Probable component of the nuclear pore complex (NPC) (By similarity). Component of the GATOR complex consisting of mio, Nup44A/Seh1, Im11, Nplr3, Nplr2, Wdr24, Wdr59 and Sec13 (PubMed:27166823). Within the GATOR complex, probable component of the GATOR2 subcomplex which is likely composed of mio, Nup44A/Seh1, Wdr24, Wdr59 and Sec13 (PubMed:27166823). Interacts with msk (PubMed:20547758). Interacts (preferentially when phosphorylated) with Mad (PubMed:20547758). Localizes to chromatin, specifically to areas undergoing transcriptional activation. Chromatin localization is independent of the nuclear pore complex (PubMed:20144761). Salivary glands. Expressed during larval development. RNAi-mediated knockdown in the larva results in reduced transcription of developmental genes Eip74EF and Eip75B in the salivary glands, compromised transcriptional recovery after heat shock and defective recruitment of Nup98. Belongs to the WD repeat SEC13 family. Extended N-terminus.
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Q65593
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MKRRELEKKLRKVRVTPQQDKYYTIGNLQWAIRMINLMGIKCVCDEECSAAEVALIITQFSALDLENSPIRGKEEVAIKNTLKVFWSLLAGYKPESTETALGYWEAFTYREREARADKEGEIKSIYPSLTQNTQNKKQTSNQTNTQSLPAITTQDGTPRFDPDLMKQLKIWSDATERNGVDLHAVNILGVITANLVQEEIKLLLNSTPKWRLDVQLIESKVREKENAHRTWKQHHPEAPKTDEIIGKGLSSAEQATLISVECRETFRQWVLQAAMEVAQAKHATPGPINIHQGPKEPYTDFINRLVAALEGMAAPETTKEYLLQHLSIDHANEDCQSILRPLGPNTPMEKKLEACRVVGSQKSKMQFLVAAMKEMGIQSPIPAVLPHTPEAYASQTSGPEDGRRCYGCGKTGHLKRNCKQQKCYHCGKPGHQARNCRSKNREVLLCPLWAEEPTTEQFSPEQHEFCDPICTPSYIRLDKQPFIKVFIGGRWVKGLVDTGADEVVLKNIHWDRIKGYPGTPIKQIGVNGVNVAKRKTHVEWRFKDKTGIIDVLFSDTPVNLFGRSLLRSIVTCFTLLVHTEKIEPLPVKVRGPGPKVPQWPLTKEKYQALKEIVKDLLAEGKISEAAWDNPYNTPVFVIKKKGTGRWRMLMDFRELNKITVKGQEFSTGLPYPPGIKECEHLTAIDIKDAYFTIPLHEDFRPFTAFSVVPVNREGPIERFQWNVLPQGWVCSPAIYQTTTQKIIENIKKSHPDVMLYQYMDDLLIGSNRDDHKQIVQEIRDKLGSYGFKTPDEKVQEERVKWIGFELTPKKWRFQPRQLKIKNPLTVNELQQLVGNCVWVQPEVKIPLYPLTDLLRDKTNLQEKIQLTPEAIKCVEEFNLKLKDPEWKDRIREGAELVIKIQMVPRGIVFDLLQDGNPIWGGVKGLNYDHSNKIKKILRTMNELNRTVVIMTGREASFLLPGSSEDWEAALQKEESLTQIFPVKFYRHSCRWTSICGPVRENLTTYYTDGGKKGKTAAAVYWCEGRTKSKVFPGTNQQAELKAICMALLDGPPKMNIITDSRYAYEGMREEPETWAREGIWLEIAKILPFKQYVGVGWVPAHKGIGGNTEADEGVKKALEQMAPCSPPEAILLKPGEKQNLETGIYMQGLRPQSFLPRADLPVAITGTMVDSELQLQLLNIGTEHIRIQKDEVFMTCFLENIPSATEDHERWHTSPDILVRQFHLPKRIAKEIVARCQECKRTTTSPVRGTNPRGRFLWQMDNTHWNKTIIWVAVETNSGLVEAQVIPEETALQVALCILQLIQRYTVLHLHSDNGPCFTAHRIENLCKYLGITKTTGIPYNPQSQGVVERAHRDLKDRLAAYQGDCETVEAALSLALVSLNKKRGGIGGHTPYEIYLESEHTKYQDQLEQQFSKQKIEKWCYVRNRRKEWKGPYKVLWDGDGAAVIEEEGKTALYPHRHMRFIPPPDSDIQDGSS
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Matrix protein p16 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane. Capsid protein p26 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. Interaction between incoming particle-associated Gag proteins and host dynein allows intracellular microtubule-dependent virus transport toward the perinuclear region, prior to nucleus translocation and integration into host genome. The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for a polypurine tract (PPT) situated at the 5'-end of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPT that has not been removed by RNase H as primer. PPT and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity). Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA (By similarity). a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus. 3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid. Interacts with host light chain cytoplasmic dynein DYNLL1; this interaction is critical for intracellular microtubule-dependent viral genome transport. This strategy of translation probably allows the virus to modulate the quantity of each viral protein. Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation (By similarity). The reverse transcriptase is an error-prone enzyme that lacks a proof-reading function. High mutations rate is a direct consequence of this characteristic. RT also displays frequent template switching leading to high recombination rate. Recombination mostly occurs between homologous regions of the two copackaged RNA genomes. If these two RNA molecules derive from different viral strains, reverse transcription will give rise to highly recombinated proviral DNAs (By similarity). The sequence shown is that of isolate R29-127. Produced by -1 ribosomal frameshifting at the gag-pol genes boundary.
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B6EKA9
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MAKKKSKDKAGSNTIAMNKQARHEYFIEDEIEAGVELQGWEVKSLRSGKVNIAESYVYVRDGEIFISGMNITPLQAASTHVVANPTRVRKLLMSRKEIDNLIGRVNREGMTLVATTMYWVRSWAKIKVGVAKGKKLHDKRTDSKEKDWNRDKARIMKSSLR
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Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation. The tmRNA-SmpB complex associates with stalled 70S ribosomes. Belongs to the SmpB family.
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Q544H5
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MEGCRETEVTNGSNGGLEFNPMKEYMILSSGQQIAVAVLCTLMGLLSALENMAVLYIILSSRRLRRKPSYLFISSLAGADFLASVIFACNFVIFHVFHGVDSNAIFLLKIGSVTMTFTASVGSLLLTAVDRYLCLCYPPTYKALVTRGRALVALCVMWVLSALISYLPLMGWTCCPSPCSELFPLIPNDYLLGWLLFIAILFSGIIYTYGYVLWKAHRHVATLAEHQDRQVPGIARMRLDVRLAKTLGLVLAVLLICWFPALALMGHSLVTTLSDQVKEAFAFCSMLCLVNSMVNPIIYALRSGEIRSAAQHCLIGWKKYLQGLGPEGKEEGPRSSVTETEADVKTT
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Heterotrimeric G protein-coupled receptor for endocannabinoid 2-arachidonoylglycerol mediating inhibition of adenylate cyclase. May function in inflammatory response, nociceptive transmission and bone homeostasis. Localizes to apical dendrite of pyramidal neurons. Expressed by cells of hematopoietic origin. Expressed in skin in suprabasal layers and hair follicles, in brain by neurons and glial cells and by osteoblasts, osteocytes, osteoclasts (at protein level). Mutant mice are responsive to the psychotropic effects of cannabinoid but not to the cannabinoid-induced immunomodulation. They also show accelerated age-related trabecular bone loss and cortical expansion. Belongs to the G-protein coupled receptor 1 family.
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Q7PCJ5
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MELDAILDNLSDEEQIELLELLEEEENYRNTHLLYEFAPYSKQREFIDAGHDYPERCFMAGNQLGKSFTGAAEVAFHLTGRYPGTKGYPADGKYGGEWKGKRFYEPVVFWIGGETNETVTKTTQRILCGRIEENDEPGYGSIPKEDIISWKKSPFFPNLVDHLLVKHHTADGVEDGISICYFKPYSQGRARWQGDTIHGVWFDEEPPYSIYGEGLTRTNKYGQFSILTFTPLMGMSDVVTKFLKNPSKSQKVVNMTIYDAEHYTDEQKEQIIASYPEHEREARARGIPTMGSGRIFQIPEETIKCQPFECPDHFYVIDAQDFGWNHPQAHIQLWWDKDADVFYLARVWKKSENTAVQAWGAVKSWANKIPVAWPHDGHQHEKGGGEQLKTQYADAGFSMLPDHATFPDGGNSVESGISELRDLMLEGRFKVFNTCEPFFEEFRLYHRDENGKIVKTNDDVLDATRYGYMMRRFARMMRDIRKPKEKKIPAPIRPVRRGR
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The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome to initiate and to end a packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities (Probable). Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine (PubMed:22771211). Once the capsid is packaged with the DNA (headful packaging), the terminase cleaves the viral genome concatemer and is substituted by the tail (Probable). Nuclease activity probably requires 2 Mg(2+) ions per subunit. Interacts with the terminase small subunit; the active complex is composed of a monomer of the terminase large subunit and a nonamer ring of terminase small subunits (PubMed:17945256, PubMed:26301600) (Probable). Interacts with the portal protein; this interaction allows the packaging of viral DNA (PubMed:28134243). The ATPase region is in the N-terminus, whereas the nuclease region is in the C-terminus. Belongs to the Lederbergvirus large terminase family. His-326 has proposed to bind the second magnesium, but this is not in accordance with the sites identified in phage G20c and Thermus thermophilus RuvC, and with the mutagenesis results in phage T4.
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A8WTM7
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MKLLKKSSSLKKGVTKRAKLQKKPPSKDEASSSDEELAKLDGEGSLDGNESEEDDGTVQVEKGGMKKHKLDLEALKKSDPEFFKFLQQEDADLLNMEEDEDDDEEGEDNEDEEDEEEEEESDEDDDEEDDDKTKIKKIRKPKVKSDSSGRLIVDSNVYSYLQQVLVLDDETTTPINPSDVRMAIDVFVACVARVGADIEAPKYVINEQSIFEAVVRMCFQAMPDVLKRLLKARPDGEKVLFSKTMIKKYQTYVRTYLHAMIVFLNEVQTTEVIIATLKAITRLVDLYAHFSRMSKLLIKAIVKIWSRKTLECRLPAFVCMNLLVKNYPQHFVPLYKTAYVAFVANSKVVTNETWPLLQFMHRTFAEITMINPEQAYKYAFVYIRQTAVHLRNAMIAKGRKDLIFSIYNWQMMQCMYMWVRVIAKAHSVNGAEQIGELVYPLIQVIVGIFKLCNAPTFLPLRLHCCQMLIQLQASCTNYIPIMQLSCDCLEELARELKSKPKPAKGAVKLPDIECTLKCSTQYSDLPQWRKTISEHVFRTMMQSAHLLASQAAFPDVALPINHRIATILDTMKNADQAHLFRGFQTKLKEHSRFVLDVLARKHVDLNDEMQVRAVRFDLNNPDSPIKSFYRQWEKVWKMKEKSALENSKKDDKKKKKEEEAAKKRKATETLEDDDDEDAKPTIPKAKRKRIKIGAAAKRADATVPDQFADMSLANWSDED
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Required for normal somatic gonad development and for regulation of germline development and proliferation. Belongs to the NOC2 family.
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C1CN37
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MEKQTVAVLGPGSWGTALSQVLNDNGHEVRIWGNLPEQINEINTYHTNKHYFKDVVLDENIIAYTDLAETLKDVDAILFVVPTKVTRLVAQQVAQTLDHKAIIMHASKGLEPDSHKRLSTILEEEIPEQLRSDIVVVSGPSHAEETIVRDLTLITAASKDLQTAQYVQELFSNHYFRLYTNTDVIGVETAGALKNIIAVGAGALHGLGFGDNAKAAIIARGLAEITRLGVALGASPLTYSGLSGVGDLIVTGTSIHSRNWRAGDALGRGESLADIEANMGMVIEGISTTRAAYELAQELGVYMPITQAIYQVIYHGTNIKDAIYDIMNNEFKAENEWS
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NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH NADP(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADPH Membrane lipid metabolism; glycerophospholipid metabolism. Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
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Q7JLL9
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MDDNTATLTAIHQQQQSHNRFSNPLVCVGQLDHHSLLPEHSISSSLAPLTHNPYAFNYSIPLPPTDITTKLPKLELLSLDVKQEQDDNHLDTSSPTDSTGNGSTNGGKIQKPRRQRTHFTSHQLTELENWFSRNRYPDMACREEIAVWISLTEPRVRVWFKNRRAKWRKRERNYVIDNGQGTTKVTAQSLDPLGSLQNTFPQTLLQSSSSQLDDSAVTSSSFYGYGGAWQQNPYYSRNNQTTFNWQIKPQDQFQFQTIPMSPTTATSRFSTAANLAPLPTAQAAFSTSATSSNDKLKLMDGLSNSLSSSLGQPYQPCQYSGPL
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Transcriptional regulator within D-type neurons that controls terminal differentiation (PubMed:7997265). Required for the development and function of the 19 inhibitory GABAergic (gamma-aminobutyric-acid-secreting) D-type motor neurons, which control locomotion (PubMed:7997265). Plays a role in regulating synapse formation in dorsal D (DD) and ventral D (VD) GABAergic motor neurons, possibly in part by regulating the expression of the neural regulator oig-1 (PubMed:26083757). Also required for expression of flp-13 in DD motor neurons (PubMed:15882588). Plays a role in respecification of DD motor neurons through regulation of genes involved in the modulation of cellular cAMP including pde-4 which hydrolyzes cAMP and acy-1 which catalyzes cAMP formation (PubMed:29033363). Expressed in D-type GABAergic motor neurons at high levels in young larvae, in which the motor circuitry is formed, and at low levels in older animals (PubMed:7997265). Also present in six non-GABAergic motor neurons and is absent from the seven non-D-type GABAergic neurons (PubMed:7997265). Expressed in DD GABAergic motor neurons and VD GABAergic motor neurons (PubMed:15882588, PubMed:26083757, PubMed:29033363). Aberrant synaptic connectivity of dorsal and ventral D-type motor neurons onto ventral and dorsal muscle. Belongs to the paired homeobox family. Bicoid subfamily.
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Q6ERS0
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MEGKGVLEGRYEMGRVLGHGNFGRVHAARDVRTGRAVAMKVVSKDKVERAGMAEQIKREIAVMKMVSHPSVVELHEVMATRTKVYLALELVRGGELFDRIARHGRVGEGVARRYFRQLVSAVDFCHGRGVYHRDLKPENLLLDEAGNLKVADFGLSALACHARPDGLLHTACGTPAYVAPEVLAGNGYDGAKADLWSCGVILYVLLAGALPFQDDNLVCMYRKMRRGDFCCPPWVTTDARKLIKSLLDPNPGTRITVAGLLETPWFRKTAPVPRPIIADPAAAPVDTRGNAGDDKDEPPEVLNAFHLISLSEGFDLSPLFEHDPAASPGRATARAGGTRFATREAASGVVARLEALAMGGARVAPSLLMVDVKKDGGDAMEYRPFFSEELRPALKDIVWSPAAT
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CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity). ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] The activation loop within the kinase domain is the target of phosphorylation/activation by upstream protein kinases. The PPI motif mediates the interaction with the ABI (abscisic acid-insensitive) phosphatases (By similarity). Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.
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Q3Z6N1
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MSKFVFVTGGVVSSVGKGITVASLGNILKSRGLSVSVQKLDPYLNVDPGTMSPYQHGEVFVTQDGAETDLDLGSYERFIDIELTADSTVTSGQVYSEVINKERRGDYLGGTIQVVPHVTQEIKARIQRLADRSKADVVIVEVGGTVGDIEGQPFLEAIRQMRNDMGRDNVIYIHVTLLPYIQSTQELKTKPTQHSVNELRRIGIQPDIIVCRADYPISEGIRDKLSLFCDVERKAVIFMPTVSTIYEVPLKLESEGVGDLLVSRLHLNASPSDLSIWRGLVEKIKEPTPAVRIALVGKYVELKDAYYSVRESLCHAAIHNGRDIQIDWVYAEDIEKNGPEEYLKHVQGIIIPGGFGIRGIEGMITAVKYARENGIPYLGLCLGMQVMVIEFARHVLQSDKAHSTEFEPDSPYPVIDLLPEQRGVDSKGGTMRLGNYPCVIQPGTMAGQAYGNKLINERHRHRFEFNNDYRDTLSKAGMVFSGLSPDGKLVEICEVSGHPFMVGSQFHPEFLSRPNRPHPLFREFINAAKKVIRDGEQPSLPLSP
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Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate H2O + L-glutamine = L-glutamate + NH4(+) ATP + NH4(+) + UTP = ADP + CTP + 2 H(+) + phosphate Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition. Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2. Homotetramer. CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor. Belongs to the CTP synthase family.
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Q0T1Y8
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MRLTSKGRYAVTAMLDVALNSEAGPVPLADISERQGISLSYLEQLFSRLRKNGLVSSVRGPGGGYLLGKDASSIAVGEVISAVDESVDATRCQGKGGCQGGDKCLTHALWRDLSDRLTGFLNNITLGELVNNQEVLDVSGRQHTHDAPRTRTQDAIDVKLRA
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Regulates the transcription of several operons and genes involved in the biogenesis of Fe-S clusters and Fe-S-containing proteins. Binds 1 [2Fe-2S] cluster.
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Q89941
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MKRKERRINKDYGYNRKCVCHYEASQKRFCYSQYSCASVLYERVRDIAKIIDRLDSGLDAWCLRDAIISVLRATHCVPRVDRMLGRWYLKTSVFYDFCPDDLILSCPNVIMPNVLNFVKKYRDFIRSVLYKVSVSWKNQYMPGVLAASRFLEEISNSLNGVEESIPCIYLRMCATLTEIVLRIGYLREIYQENPYVMFEELAFSLFTQKWVLPFSCMTNLGLVEKANSTVFDVAIYNTCLYSLVDFTIVNGEHLFPALLNGSNISMNLTRYQQEAKNIFEILLSQIRVVERDTDKTVQLTVYVEVWHVSALMWLDLYEALPQTSRVTFCLIIPGIFMDRYELKRAQWSLFHKNIAFELGKCDEITFSTKYLEFERTTDHAKITMSSFIEKICLCLKGGRMGLIFRKNVYQYSMIPHVPLYCGGDFLDVLPVRDGINTCMRMLLNVVHFLGDEVSDELTEEIDFVRLQCKFFMFNELRRVVRKMVLVANAVIDYAVENKDFLCEGIEDGRSLGICVTGLHSVFMTVGLSYAHPDARRLYRMICEHIYYTCVRTSVDCCMKGAEPCNLFDRSKYALGMLYFDHFDNVECTLPEELWTTLRKDVLMHGVRNIHFTAGTAMQKEFDIINSSESFWPMEDNKILRRSNIKVVIGKDGLNDVTSVYSSELKSLYIPVYNNLLLNRFNKHQQYLKTVGYRVLNVDTNLFTDKELDDLAVFKDGFSYHLNDLIEMYKSGLPFLDQGQANVFYFNDTVSLRLLLPLLYKAGFKVAMYKVLCNSEMYKHLDLSNPLPLIGKCSDGVVMHVKNIL
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Does not possess a ribonucleotide reductase activity. Betaherpesviruses probably use another strategy to expand the dNTP pool in a quiescent host cell. Belongs to the ribonucleoside diphosphate reductase large chain family. Lacks the conserved sequence Asn-x-Cys-x-Glu essential for ribonucleotide reductase activity. Extended N-terminus.
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Q43460
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MRVVLITLFLFIGAAVAEDAGIDAITPEEGKANNIIEAYESPRFQKFVTHCSSHVTQTCSGNDPLNNQEASRMNSPFGLSFCLFDSMEKCLADHKASLKDPQDNNNLASMSSLPGSIQNQPLLIETVKFRTVLKTCSHVSAQYCFTNPNVATSALADCLMPSLNQCVYPGSILLPWPPPPPPPPPPPPPPPPPLI
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Belongs to the nodulin 20 family.
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C4K0J6
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MKKLTKTHSHRQQKLASIINEALIEILRRGKMLDSRLFDCPLTITKVIVTTDLKIANCYFLPFNTKLTIDEIMDALNNSKNAIRNFITNKINMKFSPDIRFHYDHGFDNAIKVAHLLKDL
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One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA. Monomer. Binds 30S ribosomal subunits, but not 50S ribosomal subunits or 70S ribosomes. Belongs to the RbfA family.
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P86195
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IIFVVGGPGSGKGTQCEKYGYTHLSTGDLLRVDSSNGFLIDGYPRQGEEFERKRLETYYK
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Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Also displays broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. AMP + ATP = 2 ADP a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-triphosphate + ADP Monomer. Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Belongs to the adenylate kinase family. AK1 subfamily.
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O13263
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MSNSGKKLTQKLKKNLPVTGPQAPTLYELMQWYCLNTNTHGCRRIVVSKGRLRRWIWIVLTLIAVALIFWQCALLLMTYYSVSASITVTFQKLVYPAVTICNLNPYSYSKIKDRLATLEKTTNQTLKKIYGFTEPLIRSKRDLDVNDENSTEDIFLKQIPLFRLESIKGNQLVVSDLKTKKRTQISGKVIQRDAGSVQDSDNMVGFKLCDANNSSDCTIFTFGSGVNAIQEWYRLHYNNILAKISMEDKIAMGYKADELIVTCLFDGLSCDARNFTLFHHPLYGNCYTFNSAERGNLLVSSMGGAEYGLKVVLYIDEDEYNPYLSTAAGAKILVHDQDEYPFIEDLGTELETGTETSIGMQLTESTKLSDPYSDCTIDGSDISVENLYNKKYTLQICLNSCFQREMVRSCGCAHYDQPLPNGAKYCNYEEYPNWIYCYVKLYKQFVQEELGCQSTCRESCSFKEWTLTRSLAKWPSLNSEEWMLRVLSWELGEKLNKNLTKNDLGNLNIFYQDLNSRSISESPTYNIVTLLSNFGGQLGLWMSCSMVCGLEIVEVFFIDSFWVILRQKWHKLCNWWKNRKENEIEEIPDITVPAMAGHNNPLCVDHPICLGEDDPPTFHSALQLPQAQDCRVPRTPPPKYNTLRIQSAFHLETIDSDEDVERF
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Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus. Heterotrimer containing an alpha/SCNN1A, a beta/SCNN1B and a gamma/SCNN1G subunit. An additional delta/SCNN1D subunit exists only in some organisms and can replace the alpha/SCNN1A subunit to form an alternative channel with specific properties. Apical membrane of epithelial cells. Belongs to the amiloride-sensitive sodium channel (TC 1.A.6) family. SCNN1G subfamily.
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Q9K1F5
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MADKKSPLIAVSVGEASGDLLGAHLIRAIRKRCPQARFTGIGGELMKAEGFESLYDQERLAVRGFVEVVRRLPEILRIRRGLVRDLLSLKPDVFVGIDAPDFNLGVAEKLKRSGIPTVHYVSPSVWAWRRERVGKIVHQVNRVLCLFPMEPQLYLDAGGRAEFVGHPMAQLMPLEDDRETARQTLGVDAGIPVFALLPGSRVSEIDYMAPVFFQTALLLLERYPAARFLLPAATEATKRRLAEVLQRPEFAGLPLTVIDRQSETVCRAADAVLVTSGTATLEVALCKRPMVISYKISPLTYAYVKRKIKVPHVGLPNILLGKEAVPELLQSEAKPEKLAAALADWYEHPDKVAALQQDFRALHLLLKKDTADLAARAVLEEAGC
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Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a lipid A disaccharide + H(+) + UDP Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. Belongs to the LpxB family.
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Q5PR53
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MISRQGKEFLVRIAGYWKPLFRGRFLIVTNTVSCGGMLAAGDLIQQTREIRRTPGRTRDWSRTGCMFAVGCSMGPFMHYWYQWLDKYFIGNGINNVCKKVLVDQLVASPTLGAWYFLGMGMMEGHTFIEAQQEFRDKFWEFYKADWCVWPAAQMINFYFLPPKFRVLYVNIVTLGWDTYLSYLKHRDTVEVTKEADGTA
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Required for the assembly and stability of the mitochondrial ribosome (By similarity). Is a positive regulator of mitochondrial protein synthesis (By similarity). Interacts with the large mitochondrial ribosomal subunit. Belongs to the peroxisomal membrane protein PXMP2/4 family.
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A4IK96
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MKVSLFVTCLIDLFYTNVGKATVELLERLGCEIDFPEAQTCCGQPAYNSGYIKDAKEAMKQMMRAFADADYVVTPSGSCAAMLKEYPHIFRGDPEWEEEAKRLAAKTYELTQFLVNVLRVEDVGASLPGRATYHTSCHMTRLLGEKEVPLRLLEHVKGLELVPLPNAHQCCGFGGTFSVKMGPISEQMVDEKIEHIEEVKADYLIGADCGCLMNIGGRIGRVGKPIRVMHIAEVLNHRN
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Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source. Belongs to the LutA/YkgE family.
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Q8WJR5
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MEEFQGYLELDKYQQHDFLYPLIFREYIYALAYDHGLNRSILLDNVGYENKYSLLIIKRLISRMYKQNNFIISANDSNQNKFLGYNKNLYSQMISEGFAVIVEIPFSLRLVSSLEATEIVKSYNLRSIHSIFPFLEDKFSHLNYVSDVLIPYPIHLEILVQTLRYWVKDPSSLHLLRLFLHEYYNLNSLITPNKFIFSKSNPRLFLLLYNSHVCEYESILLFIRNQSSHLRLTSSGIFFERIHFYEKRKYPGEEVFSNDFPSAILWFFKDPFMHYVRYQGKSILASKDSALLMNKWKYYLVNLWQCHSYVWSQPGRICINQLSKHSIYFLGYFSSMRPNLSVVRSQMLENSFIMDNAMKKFDTLVPIIPLIRSLAKVKFCNTLGHPISKSAWADSSDFDIIDRFVRICRNLSHYYSGSSRKKSLYRIKYILRLSCVKTLARKHKSTVRTFLKRLGSKLLEEFFTEEQQILSLIFPRASYTLKKFYRGRIWYLDIFCINDLANHE
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Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. Belongs to the intron maturase 2 family. MatK subfamily.
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P0C9Y6
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MADFNSPIQYLKEDSRDRTSIGSLEYDENSDTIIPSFAAGLEDFEPIPSPTTTSTSLYSQLTHNMEKIAEEEDINFLHDTREFTSLVPEETDNKPEDDEESGAKPKKKKHLFPKLSSHKSK
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Structural protein required for transport of intracellular particles from the assembly sites to the plasma membrane (By similarity). Binds to both ssDNA and dsDNA (By similarity). Suppressed the activation of the cGAS/STING pathway by interfering with the recruitment of IRF3 to TBK1, which in turn suppresses IRF3 phosphorylation, decreasing interferon production (By similarity). Interacts with the major capsid protein (By similarity). Interacts with host IRF3; this interaction interfers with the recruitment of IRF3 to TBK1 (By similarity). Localizes at the surface of the intracellular virion. Expressed in the late phase of the viral replicative cycle. Acetylated. Belongs to the asfivirus structural protein p14.5 family.
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Q9P2M6
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MERAMEQLNRLTRSLRRARTVELPEDNETAVYTLMPMVMADQHRSVSELLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSDVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAKYLPDKNGVTPLDLCVQGGYGETCEVLIQYHPRLFQTIIQMTQNEDLRENMLRQVLEHLSQQSESQYLKILTSLAEVATTNGHKLLSLSSNYDAQMKSLLRIVRMFCHVFRIGPSSPSNGIDMGYNGNKTPRSQVFKPLELLWHSLDEWLVLIATELMKNKRDSTEITSILLKQKGQDQDAASIPPFEPPGPGSYENLSTGTRESKPDALAGRQEASADCQDVISMTANRLSAVIQAFYMCCSCQMPPGMTSPRFIEFVCKHDEVLKCFVNRNPKIIFDHFHFLLECPELMSRFMHIIKAQPFKDRCEWFYEHLHSGQPDSDMVHRPVNENDILLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGMGQGVVREWFDILSNEIVNPDYALFTQSADGTTFQPNSNSYVNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVETDVFGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVSDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMGGSGLQNFTIAAVPYTPNLLPTSSTCINMLKLPEYPSKEILKDRLLVALHCGSYGYTMA
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E3 ubiquitin-protein ligase involved in Golgi membrane fusion and regulation of small GTPases. Acts as a regulator of Golgi membrane dynamics during the cell cycle: recruited to Golgi membrane by Rab proteins and regulates postmitotic Golgi membrane fusion. Acts by mediating ubiquitination during mitotic Golgi disassembly, ubiquitination serving as a signal for Golgi reassembly later, after cell division. Specifically interacts with GTP-bound RAC1, mediating ubiquitination and subsequent degradation of active RAC1, thereby playing a role in host defense against pathogens. May also act as a transcription regulator via its interaction with RARB. 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. Protein modification; protein ubiquitination. Interacts with RARB (By similarity). Interacts with RAB1 (RAB1A, RAB1B or RAB1C), RAB4 (RAB4A or RAB4B) and RAB11 (RAB11A or RAB11B); in a GTP-dependent manner. Interacts with RAC1; in a GTP-dependent manner. Interacts with the 26S proteasomal complex through the 20S core proteasomal subunit. A significant portion localizes to the endoplasmic reticulum. Targeted to Golgi membrane via its interaction with Rab proteins. Expressed in multiple tissues including heart, brain and kidney. Expressed in fetal and pediatric kidney cells. Down-regulated in sporadic Wilms tumor. Defects in HACE1 are a cause of Wilms tumor (WT). WT is a pediatric malignancy of kidney and one of the most common solid cancers in childhood. HACE1 is epigenetically down-regulated in sporadic Wilms tumor. Moreover, a t(5;6)(q21;q21) translocation that truncates HACE1 has been found in a child with bilateral, young-onset Wilms tumor (PubMed:19948536). The disease is caused by variants affecting the gene represented in this entry. Extended N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus.
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A8MH36
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MRVILSGGGTGGHIYPAISIANKIKEQHPKAEILFIGTENGMESEIVPKAGYPIKYVTVSYLKRKISLHNVKSAAMLLKGIAEARKIIKEFKPDIVIGTGGFVCGPVLYMASKLGIRTMIHEQNVFPGLTNRILDRYVDRIALSFKDAEKYFKHKNKLVVTGNPIRSDFMEVTEVEASARYKTDSDLPLVLVVGGSGGALKINRAVVEILNQYQPNKYRLLLVTGKRLYKSTLESINAESLQSKHKVFAYVNDMPHALKACDLIVCSAGAITIAEVTAVGKASILIPKAHTAENHQEYNANAMGNKGAAVVIREDELSGEILNKKIQDIIGNIQVVKKMEAASYKEGIRDAADRIYSEMQALLERK
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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). di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP Cell wall biogenesis; peptidoglycan biosynthesis. Belongs to the glycosyltransferase 28 family. MurG subfamily.
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B0Z4N9
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MKNTFSWIKKEITRSISLSLMIYIITRTSISNAYPIFAQQGYENPREATGRIVCANCHLANKPVDIEVPQAVLPDTVFEAVVRIPYDRQVKQVLANGKKGGLNVGAVLILPEGFELAPPARISPEMKERIGNPSFQSYRPTKKNILVIGPVPGQKYSEITFPILSPDPATNKDVHFLKYPIYVGGNRGRGQIYPDGSKSNNTVYNATAAGIVSKIIRKEKGGYEITITDASDGRQVVDIIPSGPELLVSEGESIKLDQPLTSNPNVGGFGQGDAEVVLQDPLRVQGLLFFLASVILAQIFLVLKKKQFEKVQLSEMNF
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Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. Binds 1 heme group covalently. The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are PetG, PetL, PetM and PetN. The complex functions as a dimer (By similarity). Belongs to the cytochrome f family.
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Q9KSX4
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MQTQRLRIAIQKKGRLSQECQELLKKCGVKFNIMGERLVVHSLNMPIDLLLVRDDDIPGLIMDGVVDLGFVGENVLEETRLDRLALNQRNEFTTLRRMDFGGCRLSIAIEKDAEYRGPQDLNGKRIATTYPQLLKAYMDRQGVDFSTCMLTGSVEVAPRAGLADAIADLVSTGATLEANGLKEVEVIFESKATLIQRPGAFAADKAALIDKLLTRMHGVQQAKESKYIMLHAPVEKLAQIKTLLPGAEDPTVLPLSADKSKVAVHMVSSENLFWETMEQLKALGASSILVLPIEKMME
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Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (By similarity). 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP Feedback inhibited by histidine. Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. Belongs to the ATP phosphoribosyltransferase family. Long subfamily.
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Q63E46
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MKIEAVIFDWAGTTVDYGCFAPLEVFMEIFHKRGVGITAEEARKPMGLLKIDHVRALTEMPRIANEWNRIFGKLPTETDIQEMYEEFEEILFAILPRYASPIHGVKEVIASLRERGIKIGSTTGYTREMMDIVAKEAALQGYKPDFLVTPDDVPAGRPYPWMCYKNAMELGVYPMNHMIKIGDTVSDMKEGRNAGMWTVGVILGSSELGLSEEEVENMDPAELREKIEVVRNRFVENGAHFTIETMQELESVMERIEKQELIIS
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Involved in phosphonate degradation. H2O + phosphonoacetaldehyde = acetaldehyde + H(+) + phosphate Binds 1 Mg(2+) ion per subunit. Homodimer. Belongs to the HAD-like hydrolase superfamily. PhnX family.
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Q6EM84
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MSRRGTAEEKTAKSDPIYRNRLVNMLVNRIMKHGKKSLAYQIIYRAVKKIQQKTETNPLSVLRQAIRGVTPDIAVKARRVGGSTHQVPIEIGSTQGKALAIRWLLGASRKRPGRNMAFKLSSELVDAAKGSGDAIRKKEETHRMAEANRAFAHFR
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One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Part of the 30S ribosomal subunit. Belongs to the universal ribosomal protein uS7 family.
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A6RF09
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MAPNRGSSSKSSSKPSNKSSSSSKSKSKPLASSSRVSKPKPKSSIRRPLPKEVKAKPRTAPENLKKRKKRIYTEKELDLPQLNMITPVGVTKPKGMKKGKVFVDDQESMMTILAIVNAEKEGQIESKMMKARQMEEIREARRKEAEARQMAKKEKLEKVKDSLRKKRRPDSGEGKGDGKNSSSGEAKEFSSSKTSRSKPNRKRVSFT
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Required for efficient assembly and nuclear export of the 60S ribosomal subunit. Component of the 66S pre-ribosomal particle. Belongs to the LOC1 family.
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Q5VRI5
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MEEGVVGGGGAAVLVALLVTVVLAVMRSAGSRSSKRGRLPPSPMALPIIGHLHLIRPPPHRAFDRILARHGPLVYLRLGPSTHCVVIGSADVARDFLKFEASIPERPPTAVTRQLAYGKAGFAFAPYGAYWRFVKRLCMSELLGPRTVELLRPVRAAELADVLRAAQSAAERGEGVDMSHELVRMANNSIMRMVASALPGEMAEAARDCAKQVAELVGAFNAEDFVAVCRGWDLQGIGRRTNEVHARFDALLETIIEAKEEARRRSLRLGRRESSSKDLLDMLMDAAEDDTAEVKLTRDNIKAFVLDIFTAGSDTTATTVEWMLAELVNHPECMAKLRGELDAVVGRSRLVGEQDVARLPYLQAVLKETLRLRPPAVFAQRVTVEPVQVRGYTIPTDTQVFFNIFSIGRDATYWDQPLHFRPDRFLPDGAGATVDPKGQHPQLMPFGSGRRACPGMGLAMQAVPAFLAALVQCFDWAPPPSQPLPLDMEEAAGLVSARKHPLLLLPTPRIQPLPSFYS
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Functions as flavanone 2-hydroxylase that catalyzes the direct conversion of flavanones to 2-hydroxyflavanones (PubMed:20647377). In vitro, can convert naringenin and eriodictyol to the corresponding 2-hydroxyflavanones (PubMed:20647377). Generates 2-hydroxyflavanone substrates for C-glycosylflavone biosynthesis by the glycosyltransferase CGT (PubMed:20647377). a flavanone + O2 + reduced [NADPH--hemoprotein reductase] = a 2-hydroxyflavanone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (2S)-naringenin + O2 + reduced [NADPH--hemoprotein reductase] = (2S)-2-hydroxynaringenin + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (S)-eriodictyol + O2 + reduced [NADPH--hemoprotein reductase] = (2S)-2-hydroxyeriodictyol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] Secondary metabolite biosynthesis; flavonoid biosynthesis. Belongs to the cytochrome P450 family.
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Q9FVU5
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MERNLLSILMRRRLAERNRDAIELAAVQKMEVIGSTEGYTFDDGSDHDDVTKIFVGGGRQGIHYIEFEYVKNGQLESGVHLGVRYRGFTETFEINHLNNEHLESVEGYYDYGSGYIQGLQFKTNFRVSELIGYDEGTKFSLSVKGKRIIGFHGYMKERKIISLGGYFSWIHPRKMEAKGSKGGNQWDDGTNNDGVTKIHVRGGVEGIQYIKFDYVRKSGQHINGSIHGLSGSGFTQTFEIDHLNNEHLVCVEGYYDDESGVIQALQFKTNIKTSELLGYKKGKKFSLVDKRKKIVGFHGYADKNLNSLGAYFTTVSPTKSECYGSSKGIYWDDGVFDFIRTVYVSSNVMNVRYIKFHYYNRAVVVRQHGWNSIVEEDGEKEFELDYPNELITSVEGTMKSFSRSEIRISSLTFKTSKGRTSPTIGIASGTKFLLASKGCAVVGFYGRHDDRDLVAIGAYFSPLPPPTAEKLQAQGGNQGDSWDDGVFEGVRKLYVGQGKNCVAFLKVVYDSNTQVVIGEDHGNKTLFEVKEYELEYPSEYITAVDGCYNKVNGTEVEVITMLRIQTNKRTSIPVGCESNSSFVLKKEGYKIVGFHGKASNMINQLGVHVVPLTE
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Belongs to the jacalin lectin family.
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Q6L732
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MALAAPPGELTLALTPDDKTLDPASLDRALAILAEHGILVLTGMLRTRLTDQLRTAMLDDLPEVLRQQDVPTNFVPGHVQQDPPVRESLLFPDVLLNPVVYQITHAVLGADARNAVYSGNMNLPGSHEQPVHLDEPHLWPGISHPPYCLCVDVPLIDFTLENGSTEYWPGSHVLNPDECYDERGCVLPAELERRRAVAPPVRFPIPVGSVVIRDGRLWHRGVPNLSAAPRPLLAMTHYTEWFDMPPIQLPDTVKSWVDGSDRHTHAHFVAGDVDHLTGDHPFAVR
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Mediates the conversion of kanamycin B into 2'-dehydrokanamycin A during the transformation of kanamycin B to kanamycin A. 2-oxoglutarate + kanamycin B + O2 = 2'-dehydrokanamycin A + CO2 + NH4(+) + succinate Antibiotic biosynthesis; kanamycin biosynthesis. Belongs to the PhyH family.
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A8F4T0
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MTKLEDLRPTPGSVKPRKRVGRGIGSGHGKTSGRGHKGQKSRGSGKVHMWLEGGQTPLHRRLPKVGFKSFTHKNYAIVNIRLLEEKFSANDEITPELLLEKGFIKKIKDGVKILGSGELTKPLIVKAHAFSNSAKKAIEMVGGKVEVI
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Binds to the 23S rRNA. Part of the 50S ribosomal subunit. Belongs to the universal ribosomal protein uL15 family.
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O12987
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LIRRPLLSWLAPSRIFDQIFGEHLQESELLPASPSFSPFLMRSPILRMPSWL
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May contribute to the transparency and refractive index of the lens. Homodimer. Aggregates with homologous proteins, including alpha-A-crystallin and the small heat shock protein HSPB1, to form large heteromeric complexes (By similarity). Belongs to the small heat shock protein (HSP20) family.
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Q3AUA7
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MSTTVRPDEVSSILRKQLANFESEADVYDVGTVLQVGDGIARVYGLTKVAAGELLEFPNNVMGMALNLEEDNVGAVLFGESTMVKEGDTVKRSGILASIPVGEAMLGRVINPLGEPIDGKGPIDAKLRLPLERRAPGVIYRKSVHEPLQTGLKAIDAMIPVGRGQRELIIGDRQTGKTAVALDTIINQKGKGVFCIYVAIGLKGSTIAQVVSTLEKYDALSYTTVIAATASDPAPLQFIAPFAGATLGEYFRDTGRHALVIYDDLSKQAVSYRQVSLLLRRPPGREAYPGDVFYLHSRLLERAAKITDDVEVAKKMNDLPDALKPLVKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESNLFNSGQRPAINVGISVSRVGGAAQIKAMKKIAGTLRLDLAQFRELEAFSKFGSDLDKTTKAQLDRGARLVEILKQGQYVPMPVEKQVAIIFVGTQGLLDSVDLKFIRKCEEEFLAMLEMKHADILSGIAEKGTLEADVASKLKDIATKFIATFKEKNKA
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Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a(1), b(1), b'(1) and c(9-12) (By similarity). Belongs to the ATPase alpha/beta chains family.
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Q8X845
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MGSQELQRKLGFWAVLAIAVGTTVGSGIFVSVGEVAKAAGTPWLTVLAFVIGGLIVIPQMCVYAELSTAYPENGADYVYLKNAGSRPLAFLSGWASFWANDAPSLSIMALAIVSNLGFLTPIDPLLGKFIAAGLIIAFMLLHLRSVEGGAAFQTLITIAKIIPFTIVIGLGIFWFKAENFAAPATTAIGATGSFMALLAGISATSWSYTGMASICYMTGEIKNPGKTMPRALIGSCLLVLVLYTLLALVISGLMPFDKLANSETPISDALTWIPALGSTAGIFVAITAMIVILGSLSSCVMYQPRLEYAMAKDNLFFKCFGHVHPKYNTPDVSIILQGALGIFFIFVSDLTSLLGYFTLVMCFKNTLTFGSIIWCRKRDDYKPLWRTPAFGLMTPLAIASSLILVASTFVWAPIPGLICAVIVIATGLPAYAFWAKRSRQLNALS
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Is likely involved in the transport of fructoselysine and psicoselysine to the cytoplasm, where they are degraded. N(6)-(D-fructosyl)-L-lysine(in) = N(6)-(D-fructosyl)-L-lysine(out) N(6)-(D-psicosyl)-L-lysine(in) = N(6)-(D-psicosyl)-L-lysine(out) Carbohydrate metabolism; fructoselysine degradation. Belongs to the amino acid-polyamine-organocation (APC) superfamily.
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Q0SYG9
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MKPYQRQFIKFALSKQVLKFGEFTLKSGRKSPYFFNAGLFNTGRDLALLGRFYAEALVDSGIEFDLLFGPAYKGIPIATTTAVALAEHHDLDLPYCFNRKEAKDHGEGGNLVGSALQGRVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQERGRGEISAIQEVERDYNCKVISIITLKDLIAYLEEKPEMAEHLAAVKAYREEFGV
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Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. Homodimer. Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily.
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B2UEE3
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MSDTLRRLGEVLESRKLANGGDPEKSYIARLFNKGDDAILKKIGEEATETVMAAKDARAAGMTDEARSKVVYEVADLWFHTMVLLSHFDLTPDDVVGELARREGLSGLEEKALRKLQARDAAGD
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1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+) Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. Belongs to the PRA-PH family.
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P35094
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AEVLTSEQAEELHKHVIDGTRVFLVIAAIAHFLAFTLTPWLH
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Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers. The core complex is formed by different alpha and beta chains, binding bacteriochlorophyll molecules, and arranged most probably in tetrameric structures disposed around the reaction center. The non-pigmented gamma chains may constitute additional components. Belongs to the antenna complex beta subunit family.
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Q50972
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MNTKLTKIISGLFVATAAFQTASAGNITDIKVSSLPNKQKIVKVSFDKEIVNPTGFVTSSPARIALDFEQTGISMDQQVLEYADPLLSKISAAQNSSRARLVLNLNKPGQYNTEVRGNKVWIFINESDDTVSAPARPAVKAAPAAPAKQQAAAPFTESVVSVSAPFSPAKQQAAASAKQQAATPAKQTNIDFRKDGKNAGIIELAALGFAGQPDISQQHDHIIVTLKNHTLPTALQRSLDVADFKTPVQKVTLKRLNNDTQLIITTTGNWELVNKSAAPGYFTFQVLPKKQNLESGGVNNAPKTFTGRKISLDFQDVEIRTILQILAKESGMNIVASDSVSGKMTLSLKDVPWDQALDLVMQARNLDMRQQGNIVNMAPRRAACQRQSLLTSGKRHCRSGRAVFPKLPIEIQKCGRIPQHPALDNADTTGNRNTLVSGRGSVLIDPATNTLIVTDTRSVIEKFRKLIDELDVPAQQVMIEARIVEAADGFSRDLGVKFGATGRKKLKNETSAFGWGVNSGFGGGDKWEAKPKSTCRLPCRKQHFAGARDFSGALNLELSASESLSKTKTLANPRVLTQNRKEAKIESGYEIPFTVTTRSGGGNSTNTELKKAVLGLTVTANITPDGQIIMTVKINKDSPRQCASGNNTILCISTKSLNTQAMVENGGTLIVGGIYEENNGNTLTKVPLLATSPLSATSLKHSGKNRPPRTADFQLPPREL
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Required for type IV pilus biogenesis and competence. Could function as a pore for exit of the pilus but also as a channel for entry of heme and antimicrobial agents and uptake of transforming DNA. Homododecamer. Tetramer of trimer (By similarity). Associated with the membrane through its C-terminus. Belongs to the bacterial secretin family. PilQ subfamily.
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Q8U1Q1
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MLGEVSKILAKSSMAIAFTGAGISAESGIPTFRGKDGLWRKYRAEELATPEAFKRDPKLVWEFYKWRIKKILEAKPNPAHIALAELEKMGIIKAVITQNVDDLHREAGSKNVIELHGNIFRVKCTSCSYREYLKESDRIGWLLSQELPRCPKCGSLLRPDVVWFGEALPEKELTTAFSLAKKADVVLVVGTSGVVYPAAYIPYIVKESGGIVVEINIEPSAITPIADFFLRGKAGEVLPKLVEEIRRISK
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NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Deacetylates the N-terminal lysine residue of Alba, the major archaeal chromatin protein and that, in turn, increases Alba's DNA binding affinity, thereby repressing transcription. H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide H2O + N(6)-succinyl-L-lysyl-[protein] + NAD(+) = 2''-O-succinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide Binds 1 zinc ion per subunit. 2 residues (Tyr-64 and Arg-67) present in a large hydrophobic pocket are probably involved in substrate specificity. They are important for desuccinylation activity, but dispensable for deacetylation activity. Belongs to the sirtuin family. Class III subfamily. Extended N-terminus.
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A6QLR3
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MAASISGYTFSAVCFHSANSNADHEGFLLGEVRQEETFSISDSQISSTEFLQVIEIHNHQPCSKLFSFYDYASKVNEESLDRILKDRRKKVIGWYRFRRNTQQQMSYREQVIHKQLTRILGVPDLVFLLFSFISTANNSTHALEYVLFRPNRRYNQRISLAIPNLGNTSQQEYKVSSVPNTSQSYAKVIKEHGADFFDKDGVMKDIRAIYQVYNALQEKVQAVCADVEKSERVVESCQAEVNKLRRQITQRKNEKEQERRLQQAMVSRQMPSESVDPTFSPRMPYPGFTAEGRSTLGDTEASDPPPPYSDLHPNNQESTLSHSRMESSVFMPRPQAVGSSSYASTSAGLKYPGSGADAPPSHRAAGDSAEESDDSDYENLIDPTEPPNSEYSRSRDSRPMTHPDGGSQI
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Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates. May act as a central scaffold protein that assembles the various components of the BRISC complex and retains them in the cytoplasm (By similarity). Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys-63'-linked ubiquitination of target proteins (By similarity). Required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activities by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination. Required for normal induction of p53/TP53 in response to DNA damage. Independent of the BRISC complex, promotes interaction between USP7 and p53/TP53, and thereby promotes deubiquitination of p53/TP53, preventing its degradation and resulting in increased p53/TP53-mediated transcription regulation and p53/TP53-dependent apoptosis in response to DNA damage (By similarity). Component of the BRISC complex, at least composed of ABRAXAS2, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Interacts with BRCC3/BRCC36; the interaction is direct. Interacts with BABAM1. Does not interact with BRCA1. Interacts with SHMT1 and SHMT2; the interaction is direct. Identified in a complex with SHMT2 and the other subunits of the BRISC complex. The BRISC complex binds monoubiquitin and both 'Lys-48'- and 'Lys-63'-linked polyubiquitin. Identified in complexes with IFNAR1, IFNAR2 and SHMT2. Interacts with THAP5. Interacts with ATF4. Identified in a complex with p53/TP53 and USP7; interacts directly with both proteins. Interacts with NUMA1. Interacts with microtubule minus ends. Binds polyubiquitin. A minor proportion is detected in the nucleus. Translocates into the nucleus in response to DNA damage. Directly binds to microtubules and is detected at the minus end of K-fibers. Co-localizes with NUMA1 at mitotic spindle poles. Belongs to the FAM175 family. Abro1 subfamily. Although strongly related to the ABRAXAS1 protein, lacks the C-terminal pSXXF that constitutes a specific recognition motif for the BRCT domain of BRCA1.
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A9VN80
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MKDYLVKALAFNGEVRAYSVRTTNTVSEAQKRHDTWRTASAALGRSLTAGTMMGAMLKGEQKLTIKVEGNGPIGPILVDAHANGDVRGYVTNPHVDFEGTEQGKLRVYQAVGTEGFVTVIKDIGMREPFIGQSPIVSGELGEDFTYYFAVSEQTPSSVGVGVLVNGDDSVLAAGGFILQIMPGAQEETISFIEERLQQIPPVSQLIEQGLSPEELLYEVLGEDKVKVLETMDVQFNCTCSRERIESVLISLGKAELEQIRAEEEETEVHCHFCNERHKFAKEDITSLIEKL
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Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteines. Under reducing conditions zinc is bound to the reactive cysteines and the protein is inactive. Belongs to the HSP33 family.
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Q4QMJ8
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MSEISVTQTLNTLGLRCPEPVMLVRKNIRHLNDGEILLIIADDPATTRDIPSFCQFMDHTLLQSEVEKPPFKYWVKRGK
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Sulfur carrier protein which probably makes part of a sulfur-relay system. Belongs to the sulfur carrier protein TusA family.
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A2CAU0
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MAQPSIGQKIVVDVPSTTANLGPGFDCLGAALDLNNRFAMRRIEGDSGRFELIIEGNEGSHLRGGPNNLIYRAAQRVWKAAGLEPVGLEAKVRLAVPPARGLGSSASAIVAGLVGANALVGEPLSKEKLLELAIDIEGHPDNVVPSLLGGLCLTAKAASQRWRVVRCVWINSVKVVVAIPSIRLSTSEARRAMPKDIPISDAVENLGALTLLLQGLRTGNGDLITDGMHDRLHEPYRWPLIKGGLDVRDAALNAGAWGCAISGAGPSVLALCPEDKGQAVSQAMVKAWEAEGVASRAPLLSIQTGGSHWQPQIEDE
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Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5. Belongs to the GHMP kinase family. Homoserine kinase subfamily.
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Q3UUR2
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MGDVTRGEWVVWGLEAGPGETASLHHPGLEDMLLFFPETLAILSDTGEPQGELTIEVQRGKYKDDIGILTHCLLVHASSRGFLDKSLCGSSLLGYLNNNLELMEQHSQEFIKFPVLPMERKMSVLKQDGQFVVTRSVKEGEETKTGVSVFPYKTFKGFVSSAANVVLLRVMAWQQSVPSGARFLALDSEGKLCHCTYKSLGFQTIQVGNQQAKMFIVEQTIHSEEGIPFSCQYYLLPDGHLAKRVQVGSPGCCIITKMPLIREEDVIESPPTFDKKPLVWGEDLELYSKFLDRKEQLRLSHASYLRHHPEAQALVSDFLLFLLLRRPEDVVTFAAEHFRPFAALRSPIPALRSSHQPSPFRTLENEEEEEAKEEEEKEEEEEEEEEIAGEIEGEEEEEEIEEGDDYLYMDEDEDIEDYTYYENYYYNYDEEVDSYDDVNNYDDDDIANVDDNDDIDNYDDDNDDDDDDDDNDDEDDVDDNDDDDVDKVRAKVDNLSVDNDDNDVVNSDNVDVDNDNNNQG
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Plays a role in primary ciliogenesis by modulating actin polymerization. Interacts with TTC17. Colocalized with TTC17 at F-actin rich zones and at dynamic plasma membrane protrusions. Belongs to the CATIP family.
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B6JL99
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MKTKAGFVALIGKPNAGKSTLLNTLLNAHLALVSHKANATRKLMKCIVPFKDKEGYESQIIFLDTPGLHHQEKLLNQCMLSQALKAMGDAELCVFLASVHDDLKGYEEFLSLCQKPHILALSKIDTATHKQVLQKLQEYQQYDSQFLALVPLSAKKSQNLNALLECISKHLNPSAWLFEKDLMSDEKMRDIYKEIIRESLFDFLSDEIPYESDVMIDKFIEEERIDKVYARIIVEKESQKKIVIGKNGVNIKRIGTSARLKMQEVGEKKVFLNLQVIAQKSWSKEEKSLQKLGYTHQRNRD
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An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism. Monomer. Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Era GTPase family.
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B5F3R6
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MDTSRLTLDHFLSRFQLLRPQITHETLNQRQAAVLIPVVRRPQPGLLLTQRAIHLRKHAGQVAFPGGAVDSTDASLIAAALREAQEEVAIPPQAVEVIGVLPPVDSVTGFQVTPVVGIIPPNLPWRASEDEVSAVFEMPLAQALQLGRYHPLDVYRRGNSHRVWLSWYEHYFVWGMTANILRELALQIGVKP
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Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. Belongs to the Nudix hydrolase family. PCD1 subfamily.
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V6REA7
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MSQSGATVSQDCITAFNDLKLNKKYKFIVYKLSDDYKEIVIDKASESRDWEDFRETLVNATAKSRTGAVGKGPRYAVYDFEYNLASGDGIRNKITFIAWSPDDAGIQPKMIYASSKEALKRSLTGIATELQANDTDDIEYDSILKTVSKGLAA
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Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton (By similarity). Throughout the cytoplasm (but not on the cytoplasmic cables) and major component of the cortical actin cytoskeleton. Belongs to the actin-binding proteins ADF family.
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Q3IYD8
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MMTHLRPALASLLALSLLTGVAYPLALTGIAAVIAPDRAAGSLILREGQVVGSALIGQGFDGPGYLHPRPSASDWNAAGTFASNLGPTSAALLAEVQERQAAYEARNGASAPVDAVTASGSGLDPHVSPANARAQAARIARARGLDEAAVRRLIEAHVEPPLLGLWGQARVDVLAVNLALDAAGA
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Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex. The system is composed of three essential subunits: KdpA, KdpB and KdpC. Belongs to the KdpC family.
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A1UKX6
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MSTTTAGILFALSLALALAAVHVPLGDYMYRVYASEKHWRAERVAYRIIGADPAAEQGWGSYARSVLAFSAVSILFLFGLQLLQGRLPLHLNDPATEMTPALAWNTAVSFVTNTNWQAYSGESTQGHLVQMAGLSVQNFVSAAVGMAVAMAFVRGLARRDTGELGNFWVDLIRGSLRILLPLSIIGAIILVSGGVIQNFALHDTVVSTLSGAQQTIPGGPVASQEAIKELGTNGGGFFNANSAHPFENPTTWTNWVEIFLLSCIAFSLPRTFGRMVGSRKQGAAILAVMAVIATLSLSLMMLFQSQTHGTVPTAVGSATEGVEQRFGVADSAVFADLTTLTSTGAVDSFHDSYTSLGGLMTLFNMQLGEVAPGGVGSGLYSMLVLAVITVFVAGLMVGRTPEYLGKKITPREIKLAATYFLVTPLIVLIGTAVAMALPGQRDGMLNTGPHGLSEVLYAFTSAGNNNGSAFAGLSVNTEWYNTALGLAMVFGRFLPIILVLALAGSFARQGRTPESVGTLPTHRPQFVGMVTGVTLILVALTFLPVLALGPLAEGLH
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Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the extracellular potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel. The system is composed of three essential subunits: KdpA, KdpB and KdpC. Belongs to the KdpA family.
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Q5FTZ9
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MASQQGLQERRRQRLRFQLRRKSGGRPRLSVFRSSKHIHAQIIDDAQGRTLASASTLEKTLRDAGKTGADVSAATVIGKLIAERGVAAGVKTVVFDRGSYLYHGRVKALAEAAREGGLSF
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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 protein uL18 family.
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P85712
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EQFDDYGHMRF
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Myotropic peptide. Belongs to the gastrin/cholecystokinin family.
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A6R4H9
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MDNTAITSQSSSTPLVCSVTPIIVGSPPSPANVIELSSPSTPPTPLTLLASLSETPSRKTTNPDTNGENTICHGVRQVRRVPRNNPVTGPSKEHKQRTRSPKTTTRREIKIVEGDRLIVGHDKREKKGETTKRMKKRDGVADKKLYARVSKVKSSENLDLDAKIPSSKVCNNTLPLVGDDMDNGSSELKLEQAIKRRHDWTPTREVTTPVVDVAELHSSPCGKAVTRMHGVGTLLSDYGFSGVVETSLGTKSESFRNAPTTKRPMELQKFSTVPAIPTPTESSTTEDVQGSSSKQQRVKAKKPQKGKLTTITSHATAKYCVADQTVDLDYIQNVAPKSPRRKNISNRPSGTKHSNSGRGKSSTLKNDNGRPVFRVVPPLEAFKSFEGQELLFGTSSQLERGYPEYPCDETQDTQNSPSNSAAVSELAVPYRISSEGKDLGSSLFGLSGSKNLWSASARDLTGAVFEGDEIDFQGASMGLSVLATKSRCHPGNRGPPRRNLVDVDNVPDKKLDIDTTEGENGNHSSVADNIVDRENLNPKISANTSETNLECAPQNKPAFSRFTTSELAKKVAAYGFKPIKSRDNMISLLEKCWETQSKTLILESKPNQGTDDARKNGFRKENHSDVRVRPDSATLANRRSPKKQQAKALSKFQEPNNFLPIENSTTTASMLPIISSHTILINDDQLSDSVGETVSFLPSLDHNGNGTTIQENMLEIKSPATPNARRSRQGSSSASFSIEPPSLASQITKAIKSQPRTRAFNGLKQPTWYEKILMYDPIQLEDLAAWLNTDGFGRIGEDREVGPGVVREWCESKGVCCVWKKQVSGRSHYLPMVS
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Regulatory subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Forms a heterodimer with SLX1. Phosphorylated in response to DNA damage. Belongs to the SLX4 family.
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Q6LXR0
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MALRPARCYRTIERRSYTRKEYVRAVPQPKVVHYVMGNPSAEFPVQVQLVSKSDILIRHNALESSRIAGNKYILSECGRTGYLFNIRVYPHEILRENKMAAGAGADRISDGMRLSFGKAVGTAAKVKKGQEIITIGVNPEKFYAAKEALRRCSMKLPTACKIVVTKGKELIKD
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Belongs to the universal ribosomal protein uL16 family.
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B4TJX2
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METYAVFGNPIAHSKSPFIHQQFAQQLDIVHPYGRVLAPINNFINTLDAFFAAGGKGANITVPFKEEAFARSDELTERASLAGAVNTLKRLEDGRLLGDNTDGIGLLSDLKRLNFIRPGLRILLIGAGGASRGVLLPLLSLDCAVTITNRTASRAEALAKIFAHTGSVHATDMDKLDGCEFDLIINATSSGIRGEIPAIPASLIHPSLCCYDMFYQKGNTPFLSWCVQQGAKRYADGLGMLVGQAAHAVLLWHGVLPQVEPVIELLQQELLA
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Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. Homodimer. Belongs to the shikimate dehydrogenase family.
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B1YLA2
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MPKMVHRSKTRPVRVGDLVIGGNNEVIIQSMTTTKTHDVEATVAEILRLEEAGCQIVRVACPEERDALALAEIKSRINIPLVVDIHFNYKLALMAIEAGVDKIRINPGNIGRREKVEAVVTAAKAKNIPIRIGVNAGSLEKHILEKYGYPTARGMVESALHHIKILEDLDFHDIIVSLKASDVQLALEAYQLASESFDYPLHVGITESGPLRTGSLKSAAGLGAILSRGIGNTVRVSLSADPVEEVKVAKEVLKSFGLAANAATLISCPTCGRIEIDLMAIAAEIEDYIDKIQVNIKVAVLGCAVNGPGEAREADIGIAGARNEGLLFRHGEIIRKVPEATMVEELKKEIDAIVLEKEAEKEAAKASQA
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Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + H2O + oxidized [flavodoxin] = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + reduced [flavodoxin] Binds 1 [4Fe-4S] cluster. Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 5/6. Belongs to the IspG family.
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A9BCR1
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MIGKHCILELCECNSVKLDDEAFIRTTIQMASKVAGAQLLNLITHKFVPQGVTGLALLAESHISIHTWPESGYAAVDVFTCGDQTMPDKACQLLVEELQSKRHSLKTLRRDTPVMISNALIN
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Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine. H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine Binds 1 pyruvoyl group covalently per subunit. Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers. Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain. Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.
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Q0I4B4
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MATIKDVAKMAGVSTTTVSHVINKTRFVAKETEQQVLQAIKNLNYSPSAVARSLKVNTTKSIGMIVTTCETPYFAEIIHSVEELCYRQGYSLFLCNTQNNPEKIKNHLDMLAKKRVDGLLVMCAEYTQNSLNLLATFEDLPMVVMDWGPFNENTDLIQDNSFSGGYIATKYLIDNGHKDIAIISGELKKTTAVMRYQGFEKAMQEANLAINPDWIMEGFFEPEDGYECMNKILVQDKLPTAVFCCNDVMALGAISAIGEKGLKVPDDISVIGYDNIHASRFFSPPLTTIHQSKSRLGVQAINLLFKRISEKGKEHEIIEIYPELVIRKSVKTL
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Is the main repressor of the genes involved in the de novo synthesis of purine nucleotides, regulating purB, purC, purEK, purF, purHD, purL, purMN and guaBA expression. PurR is allosterically activated to bind its cognate DNA by binding the purine corepressors, hypoxanthine or guanine, thereby effecting transcription repression. Purine metabolism; purine nucleotide biosynthesis [regulation]. Homodimer. Consists of two structural and functional domains: an N-terminal DNA-binding domain, approximately the first 60 residues, and a larger C-terminal domain, approximately 280 residues, which imparts the function of corepressor binding and oligomerization.
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A7KPU8
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MPDERTTGREGVGAAVLAAGFGERLRECGRPKPLARVAGLTLLERTVRTLRAGGLEGEIVVVVGHRGEEVAGHCKARGLPVRVVENPDYPRGNGTSVLAAMRFLPERFVVAMVDHIHTPESVRRLLRCEGDFVAAVDTRPVYADPGEATRVRLEGGRVVEFGKNLPRYDGLDAGLFLCSRPALERLREASGGERLSWNDLKRAWLASGGEVVACDLAGAPWTDVDTPQDLRLSEEMVLGWAASGNDGPVSRHINRRISRRITRRLLDTPLSPDQVSLLSFALAALGAGLLAAGRLRLGGALVQLASIVDGCDGELARARLESSPRGAVFDATLDRWADALIISGLALGAGTRLAAAAGYPALAGALLVSYTRARWEAALGRMPSRFTGLGATRDVRLAVLALGGLLGAPGAALLATGALGNAEALRRLLALKRGRS
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Involved in biosynthesis of di-myo-inositol phosphate (DIP), a widespread organic solute in microorganisms adapted to hot environments. Catalyzes the condensation of CTP and L-myo-inositol-1-phosphate into CDP-L-myo-inositol, as well as the biosynthesis of di-myo-inositol-1,3'-phosphate-1'-phosphate (DIPP) from CDP-L-myo-inositol and L-myo-inositol-1-phosphate. 1D-myo-inositol 3-phosphate + CTP + H(+) = CDP-1L-myo-inositol + diphosphate 1D-myo-inositol 3-phosphate + CDP-1L-myo-inositol = bis(1L-myo-inositol) 3,1'-phosphate 1-phosphate + CMP + H(+) In the N-terminal section; belongs to the MobA family. In the C-terminal section; belongs to the CDP-alcohol phosphatidyltransferase class-I family.
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Q04U64
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MKASKYILPTEKENPSDAVVASHRLMIRAGLARKSSAGLYFYLPLGLKILQKIKQIIREEMNKTGALEFDLPILTPSDFWEQSGRWTAMGKEMFRIKDRHDLSYALGPTHEESFSFLLKPLLKSYKDLPLNVYQIQTKFRDEIRPRFGVIRSREFIMKDAYSFHIDDVSLDETYQSMRAAYRKIFDRCGLKTIPVQADSGSMGGSASEEFMVVSPIGEETLLLCNSCGYSSNSEKTPLVLKKENVSSASVEKKEISTPGKKTIVEVSAFLEIPESTTIKAVTLKSEKKKILVYLRGDLELNLHKLHSLLRIVDSEPMTDAEIRELGLVPGFIAPVAPNDKVKVLYDRSLQKDFPYVVASNKEDFHTQGFVLEKEVSGLPEFADVALAREGDLCPNCNAPLKAEKGIEVGHIFKLGEKYTKAFGIQVLDQNGKARTLTMGCYGIGVNRTMATVIEQRNDEKGIFWPISIAPFEVTLVSITKGEEQYSKAEEFYNVLKNENLEVFWDDRDVGPGFKLKDSELIGFPIRVTIGKKFFENGEISIYNRKADKEESFVFAGFENLIARVESLRQELFAELE
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Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS. ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro) Homodimer. Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain. Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily.
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Q8EZP1
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MQTALYISVLIISSCGLVYELLAGTIASYLLGETVTQFSLIIGTYLFSMGVGSWLSKYLEKDLIPKFLEIELAIGLVGGFSSAILYLSFGQIRYFQIPLFLLVILIGILVGLEIPVLLRILKKELQFKELVSRVLSLDYVGALLASILFPIFFAPKLGLMRTGFIFGILNVGVALWGTWVLPLRQSKIIILRAQSVVVLTLLILGFSYSDLITYYSEESLYTDEIILSKQTQYQRIIVTRWKNEIRLFLNGHLQFSSRDEYRYHETLVHPALLAHPAPKKVLVLGGGDGLAVREILKHKNVESVTLVDLDSAITNLFSEHGILKELNEESLKNSKVTVINTDAFLWLEESDQTFDVVLIDFPDPSNFSLGKLYTTAFFHTLKRRMNETSVLEIQSTSPLFARSSYWCIERTIASLGFYTLPLHVYVPSFGEWGFVLAGQRPIQFKKKFPKDLKFLNIQELESIQTFPQDMSRVPVEINRLDNQALVRYYDREWNRILD
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Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1. Homodimer or homotetramer. Belongs to the spermidine/spermine synthase family. Truncated N-terminus.
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Q2W4H6
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MAAEKPSSIFRDFLDSEAAGGVILMVTAALALVIANSPLSGAYFAFLQAKFLGMSVLHGINDGLMAVFFLLVGLEIKREVLGGQLSNWSQRILPGLAALGGMVVPALVFLALNAKSPETVRGWAVPTATDIAFALGVLALLGPRVPASLKIFLTALAIIDDLGAVLVIALFYTAKLSWPALVAVAAILALLAALNRLRVRSLWPYLLVGAGLWGAMLQSGVHATVAGIALALTIPMGDEQHSPLHRLEHGLAPWVGYGIVPIFGFANAGVSFAGLEPSRVLQSLPLGIALGLLFGKQIGVFGTAWMAIWLGFAARPEGAGTAQLYGVAVLCGIGFTMSLFIGALAFGELPASSDAVKVGVLAGSALSAILGSLVLLRCRSSSS
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Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out) Belongs to the NhaA Na(+)/H(+) (TC 2.A.33) antiporter family.
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Q9FGZ1
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MADSRDDLAESLQNLFTSVSSMVKSELQGTNNHLDLLEKMNLRVASEYDDMGDVAAGLRVFAEQMKSKSGGLDEFVGQMDAIEKQVSEFEAVISVLDRYVSVLESKIRAEYRHPHHQRRSNDSVVTD
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Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1), a complex that mediates the vacuolar degradative transport via the intracellular vesicle trafficking from the endosome to the vacuole. Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) (By similarity). Interacts with BLOS1 and SNX1. Belongs to the BLOC1S2 family. The predicted gene has been split into 2 genes: At5g49550 and At5g49555.
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A0Q6Q2
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MKEISGIKVKVESGSKYTTDHGFHAVKDGIRNKKENAVHVRKPDWLKVQKQDSKEYLKVKSITKKHKLSTVCEEARCPNINECWSHGTATIMLMGSVCTRACKFCSVDTGNPKGWLDKDEPMNAAESVKLMGLEYVVLTSVDRDDLEDGGAGHYAATITAIKNLDENIKVEALTPDFAGINENIDKIINTKVDVIAQNIETVERLTHPVRDPRAGYWQTLNFLKYVKQKSPNVLTKTSIMVGLGETDEEIYKTMDDARSVGVDIITLGQYMQPTKHHLSVERFVTPQQFEEYRKVGLEKGFLEVASGPMVRSSYRADRVFKRNNLDL
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Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin] Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2. Belongs to the radical SAM superfamily. Lipoyl synthase family.
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Q80XG2
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VVIFLGTVAHKTSPQRPDRLLIRLRHLVDNVEQLKIYVNDLDPELLPAPQDVKEHCAHSAFACFQKAKLKPANTGSNKTIISDLVTQLRRRLPATKAEKKQQSLVKCPSCDSYEKKTPKEFLE
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Cytokine with immunoregulatory activity. May promote the transition between innate and adaptive immunity. Induces the production of IgG(1) and IgG(3) in B-cells. Implicated in the generation and maintenance of T follicular helper (Tfh) cells and the formation of germinal-centers. Together with IL6, control the early generation of Tfh cells and are critical for an effective antibody response to acute viral infection (By similarity). May play a role in proliferation and maturation of natural killer (NK) cells in synergy with IL15. May regulate proliferation of mature B- and T-cells in response to activating stimuli. In synergy with IL15 and IL18 stimulates interferon gamma production in T-cells and NK cells (By similarity). During T-cell mediated immune response may inhibit dendritic cells (DC) activation and maturation (By similarity). Belongs to the IL-15/IL-21 family.
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B8D9H2
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MKFIDQAIIHVIAGNGGNGCVSFRREKYIPKGGPDGGNGGDGGNIWLEANNNLNTLIDLRFKKKFQAQNGQNGSSRKSSGKKGDDIKIHVPIGTKVINYQTREIIGDLIQHKQKMLIAKGGWHGLGNARFKSSTNRTPRQSTLGSIGEKRDIQLELMLLADVGTLGMPNVGKSTLVTNISGAKTKISDYPFTTLHPVLGSVNIQKNKKFIIADIPGIIKGASYGAGLGIRFLKHLERCKLLLHIIDLVPQNNCHPSDNIKTVLNELKKYSLKLYNKPRWFIFNKIDLLSVEELNQIIKEIIFQFKIHEKYYLISSMKKIGIKKLCSDITKYLKK
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An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control. Monomer. Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.
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A9BDG0
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MSCLLIAASGTGGHLFPALAVAEALPESWKVSWLGVSDRLESSLIPKKYQLSTIGVEGVQSRGIKRIVQIFKLLAATGSVICLIRRNRIQIVLTTGGYIAVPAVLAAKLTGKKVILHESNAIPGKATRLLGRLCDKVALGWPPAKKKLPGCKVTVTGTPVRKSFLMKNKLPSWAPSGPGPLIVVIGGSQGAVGLNDMVRAVLPFLLDQGCRIVHITGKNAQSKIIHTNLVEQPFSDDIPGLLQNADLVISRSGAGALSEFAVCEVPAILVPYPYAADNHQECNAIYASQFGAALIVHQHEPEGKALRNALERLLKKNLSQADTVENLLNLMRKGMAKMAVRDAHIHLMSLLKEAS
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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). di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP Cell wall biogenesis; peptidoglycan biosynthesis. Belongs to the glycosyltransferase 28 family. MurG subfamily.
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G8SD34
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MRYDAFISYSHAADGALAPAVQRGLQRLARRWHRPRALEVFRDQTGLAVSHALWSSIKVALDQSEFFVLLASPEAAASPWVNQEIEHWLSRHSVDRLLPVVTSGEWVWDADAGDVDLERSTAVPPALRGVFGEEPRHLDLRWARAEHELDLRHGRFRDAIAELAAGMHGMSKEDLDGEDVIRHRQMLRMRRGALAVVCALLLLVAGTAVAWRNARGEVTATNVALQRQRAATAAEQHRTEEAADQARSQQQIVEAEQQRAQKAAEEARGQQAVAEAEQQRALRAAGEARRQEGIAAAEQRRAQKAAAEARRQRGVADAEKAKANRAAAEAERQRKIAADEQRKAHEAAAEAERQREEAVKQQRIAIGRRLLGQAGEARDRDPRTAIQLGIAARHIYPGPQSQAGLVETLVRTHYAGTVTGHTAVVSAVALSGDGRTLVTDGLDGTVMVWDPTDRAAPRRLAQLTSSTAPVYTVALSGDGRTLVTGSEDGTAMVWDLTDRAAPRRLAQLTGHTDVVDAVALSGDGRTLATGSFDGTAMVWDVTDRAAPRRLAQLTDHTAPVTAVALSGDGRTLATGSDDHTAMVWDLTDRAAPRRLAQLTGHTAGVDAVALSGDGRTLATGSYDGTAMLWDLTDRAAPRRLAQLTGHTAQVYTVALSRDGRTLATGSEDHTAMVWDLTDRAAPRRLAQLTGHTDAVDAVALSGDGRTLATAASITRRCCGM
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NAD(+) hydrolase (NADase) that catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide. H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity.
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Q93WV1
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MTVDIMRLPKMEDQTAIQEAASQGLKSMEHLIRVLSNRPEERNVDCSEITDFTVSKFKKVISLLNRSGHARFRRGPVHSPPSSSVPPPVKVTTPAPTQISAPAPVSFVQANQQSVTLDFTRPSVFGAKTKSSEVVEFAKESFSVSSNSSFMSSAITGDGSVSKGSSIFLAPAPAVPVTSSGKPPLSGLPYRKRCFEHDHSEGFSGKISGSGNGKCHCKKSRKNRMKRTVRVPAVSAKIADIPPDEYSWRKYGQKPIKGSPHPRGYYKCSTFRGCPARKHVERALDDSTMLIVTYEGEHRHHQSTMQEHVTPSVSGLVFGSA
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Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element (By similarity).
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A8L6D8
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MTATTAESGNLLPLVSGRSRPPRHLADLSRDERRAVATSLGLPAFRADQLARHYFTHHLRADDADLMTDLPASIRPALVEAMLPRLLTPATALDCDGGQTRKTVWRTVDGAKIESVLMRYPQRATVCVSSQAGCGMGCPFCATGQGGLTRNLSTAEIVEQVVDAARTMAARTTAEGGLPGGPGRLSNVVFMGMGEPLANYAALLAALHRLIDPAPDGLGLSARGLTVSTVGLVPAIRRLAGEGLPVTLAVSLHAPDDELRDELVPINTRWPVAEVLAAAWEYARVTGRRVSIEYALIDGVNDSPERADALAALLVGQLAHVNLIPLNPTGGSSWQASAPRGQRVFVERLRARGVAATVRDTRGREIAAACGQLAAEPPVRSRAGR
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Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue. Belongs to the radical SAM superfamily. RlmN family.
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P23728
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MATTAMRMIISIIFISTYVTHITLCQNITEEFYQSTCSAVSRGYLSALRTGWYTSVVTIELSKIQKNVCNSTDSNVKLIKQELERYNNAVVELQSLMQNEPASSSRAKRGIPELIHYKRNSTKKFYGLMGKKRKRRFLGFLLGIGSAIASGVAVSKVLHLEGEVNKIKNALLSTNKAVVSLSNGVSVLTSKVLDLKNYIDKELLPKVNNHDCKISNIATVIEFQQKNNRLLEIAREFSVNAGITTPLSTYMLTNSELLSLINDMPITNDQKKLMSSNVQIVRQQSYSIMSVVKEEVMAYVVQLPIYGVIDTPCWKLHTSPLCTTDNKEGSNICLTRTDRGWYCDNAGSVSFFPQAETCKVQSNRVFCDTMNSLTLPTDVNLCNTDIFNAKYDCKIMTSKTDISSSVITSIGAIVSCYGKTKCTASNKNRGIIKTFSNGCDYVSNRGVDTVSVGNTLYYVNKLEGKALYIKGEPIINYYDPLVFPSDEFDASIAQVNAKINQSLAFIRRSDELLHSVDVGKSTTNVVITTIIIVIVVVILMLIAVGLLFYSKTRSTPIMLGKDQLSGINNLSFSK
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Inactive precursor that is cleaved at two sites by a furin-like protease to give rise to the mature F1 and F2 fusion glycoproteins. Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the coiled coil regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs at the plasma or endosomal membrane. The trimer of F1-F2 (F protein) also facilitates the attachment and entry into the host cell. Later in infection, F protein expressed at the plasma membrane of infected cells can mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. Major determinant of the species specificity of RSV infection. The trimer of F1-F2 (F protein) also facilitates the attachment and entry into the host cell. Later in infection, F protein expressed at the plasma membrane of infected cells can mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. Homotrimer. Heterodimer with fusion protein F2; disulfide-linked. Part of a complex composed of F1, F2 and G glycoproteins. As a heterodimer with F2, interacts with host RHOA; this interaction facilitates virus-induced syncytium formation. Homotrimer. Heterodimer with fusion protein F1; disulfide-linked. Part of a complex composed of F1, F2 and G glycoproteins. As a heterodimer with F1, interacts with host RHOA; this interaction facilitates virus-induced syncytium formation. Localized at the host apical membrane. Localized at the host apical membrane. The N-terminus is a hydrophobic fusion peptide that inserts into the target host membrane (By similarity). It is buried in the center of the trimer cavity before cleavage by host furin. The coiled coil (heptad repeat) regions are probably involved in homotrimerization, heterodimerization and in the formation of a fusion-active hairpin structure (By similarity). The N-terminus is a hydrophobic fusion peptide that inserts into the target host membrane (By similarity). It is buried in the center of the trimer cavity before cleavage by host furin. The coiled coil (heptad repeat) regions are probably involved in homotrimerization, heterodimerization and in the formation of a fusion-active hairpin structure (By similarity). The F glycoprotein is synthesized as a F0 inactive precursor that is heavily N-glycosylated and processed at two sites by a host furin-like protease probably in the Golgi. The cleavage site between p27 and F1 may occur after endocytosis to yield the mature F1 and F2 proteins. Both cleavages are required for membrane fusion and p27 is released from the processed protein. Belongs to the paramyxoviruses fusion glycoprotein family. Ser-550 is present instead of the conserved Cys which is expected to bind palmitate.
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A7GTD6
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MKKFILASGSPRRKELLELANVPFEVVVSEVEETIGAYSSPADIVMALALQKASAVAETHEESIVLGADTIVTYDSRILGKPKDAAEAKEMLQLLSGKTHEVYTGVALMSKEKTVTFYERTEVTFWELTEEEIDVYIATKEPLDKAGSYGIQGKGAIFVQHIQGDYYSVVGLPIARLVRELKQFDSGASHA
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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. dTTP + H2O = diphosphate + dTMP + H(+) H2O + UTP = diphosphate + H(+) + UMP Belongs to the Maf family. YhdE subfamily.
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Q4K779
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MFDYKLLSALAAVIEQAGFERAAQVLGLSQSAISQRIKLLEARVGQPVLVRVTPPAPTEIGRRLLNHVQQVRLLERDLQSLVPALDEEGLPERLRIALNADSLATWWAGAVGDFCAEHHLLLDLVVEDQTVGLKRMRAGEVAACVCASERPVAGARSLLLGAMRYRAMASPEFIVRHFPQGVRAEQLPRTPALVFGPDDFLQHRYLASLGVDGAFEHHLCPSSEGFIRLTEAGLGWGLVPELQVREQLERGLLLELLPDKPIDVPLYWHHWRNGGQLLGLLTEHLARLSAQWLVPWEQP
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Controls the transcription of genes involved in arginine and lysine metabolism. Homodimer. Belongs to the LysR transcriptional regulatory family.
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C6DVC4
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MTALDWRSALTADEQRSVRALVTATTAVDGVAPVGEQVLRELGQQRTEHLLVAGSRPGGPIIGYLNLSPPRGAGGAMAELVVHPQSRRRGIGTAMARAALAKTAGRNQFWAHGTLDPARATASALGLVGVRELIQMRRPLRDIPEPTIPDGVVIRTYAGTSDDAELLRVNNAAFAGHPEQGGWTAVQLAERRGEAWFDPDGLILAFGDSPRERPGRLLGFHWTKVHPDHPGLGEVYVLGVDPAAQRRGLGQMLTSIGIVSLARRLGGRKTLDPAVEPAVLLYVESDNVAAVRTYQSLGFTTYSVDTAYALAGTDN
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Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol. 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol Monomer. Belongs to the acetyltransferase family. MshD subfamily.
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Q8K9R0
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MRNILTIFLLTSTFFTGILWIIDHILLIKNYFYNKKKTKNNNTILINKVILENKKCFFRSLSSLFPTFFIVFIIRSFIYEPFQIPSGSMMPTLLIGDFILVKKFSYGIKEPITNKTIIKMNLPQRGDIVVFKHPKNNIDYIKRVVGLPGDKIQYDINRKKIKICINYTNQKNCENKLFITYSKPKLSNFFQKIYLLKSRTNEEEKVYNSIYFKKVEEKINNLKHNILILDGINSKINDYYQQKGMPKLIWIVPKNKYFMMGDNRDNSLDSRYWGFVPEENLLGKATKIWMSFEKKENEWPTGIRIKRIGNIY
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Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins. Belongs to the peptidase S26 family.
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Q4R3K4
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MSLSKKLTLDKLDVRGKRVIMRVDFNVPMKKNQITNNQRIKASIPSIKYCLDNGAKAVVLMSHLGRPDGVPMPDKYSLQPVAAELKSLLGKDVLFLKDCVGAEVENACANPAPGSVILLENLRFHVEEEGKGQDPSGKKIKAEPDKIEGFRASLSKLGDVYVNDAFGTAHRAHSSMVGVNLPHKASGFLMKKELDYFAKALENPVRPFLAILGGAKVADKIQLIKNMLDKVNEMIIGGGMAYTFLKVLNNMEIGASLFDEEGAKIVKDIMTKAQKNGVRITFPVDFVTADKFDENAQVGKATVASGIPPGWMGLDCGPESNKNHAQVVAQARLIVWNGPLGVFEWDAFAKGTKALMDEIVKATSKGCITIIGGGDTATCCAKWNTEDKVSHVSTGGGASLELLEGKILPGVEALSNM
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Essential for sperm motility and male fertility but is not required for the completion of spermatogenesis. (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. Monomer. Belongs to the phosphoglycerate kinase family.
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G8H5N1
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MNQLAMVNTTITRPLANYHSSVWGNYFLSYTPQLTEISSQEKRELEELKEKVRQMLVETPDNSTQKLVLIDTIQRLGVAYHFENHIKISIQNIFDEFEKNKNKDNDDDLCVVALRFRLVRGQRHYMSSDVFTRFTNDDGKFKETLTKDVQGLLNLYEATHLRVHGEEILEEALSFTVTHLKSMSPKLDNSLKAQVSEALFQPIHTNIPRVVARKYIRIYENIESHDDLLLKFAKLDFHILQKMHQRELSELTRWWKDLDHSNKYPYARDKLVECYFWAIGVYFGPQYKRARRTLTKLIVIITITDDLYDAYATYDELVPYTNAVERCEISAMHSISPYMRPLYQVFLDYFDEMEEELTKDGKAHYVYYAKIETNKWIKSYLKEAEWLKNDIIPKCEEYKRNATITISNQMNLITCLIVAGEFISKETFEWMINESLIAPASSLINRLKDDIIGHEHEQQREHGASFIECYVKEYRASKQEAYVEARRQITNAWKDINTDYLHATQVPTFVLEPALNLSRLVDILQEDDFTDSQNFLKDTITLLFVDSVNSTSCG
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Sesquiterpene synthase involved in the biosynthesis of volatile compounds (PubMed:21818683). Mediates the conversion of (2E,6E)-farnesyl diphosphate ((EE)-FPP) into (+)-thujopsene, beta-bisabolene, alpha-cederene, beta-acoradiene, (E)-gamma-bisabolene, (Z)-alpha-bisabolene, (Z)-beta-farnesene and (E)-beta-farnesene, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into (E)-gamma-bisabolene, (E)-alpha-bisabolene, (E)-beta-farnesene, (Z)-beta-farnesene, beta-bisabolene, beta-acoradiene and alpha-acoradiene (PubMed:21818683). Can act with a low efficiency as a monoterpene synthase with geranyl diphosphate (GPP) as substrate, thus producing beta-myrcene, limonene and terpinolene (PubMed:21818683). (2E,6E)-farnesyl diphosphate = (E)-gamma-bisabolene + diphosphate (2Z,6Z)-farnesyl diphosphate = (E)-gamma-bisabolene + diphosphate (2Z,6Z)-farnesyl diphosphate = (E)-alpha-bisabolene + diphosphate (2Z,6Z)-farnesyl diphosphate = (Z)-beta-farnesene + diphosphate (2E,6E)-farnesyl diphosphate = (E)-beta-farnesene + diphosphate (2E,6E)-farnesyl diphosphate = (+)-thujopsene + diphosphate (2Z,6Z)-farnesyl diphosphate = (E)-beta-farnesene + diphosphate (2E,6E)-farnesyl diphosphate = (Z)-beta-farnesene + diphosphate (2Z,6Z)-farnesyl diphosphate = beta-acoradiene + diphosphate (2Z,6Z)-farnesyl diphosphate = alpha-acoradiene + diphosphate (2Z,6Z)-farnesyl diphosphate = beta-bisabolene + diphosphate (2E,6E)-farnesyl diphosphate = (-)-alpha-cedrene + diphosphate (2E,6E)-farnesyl diphosphate = beta-bisabolene + diphosphate (2E,6E)-farnesyl diphosphate = beta-acoradiene + diphosphate (2Z,6Z)-farnesyl diphosphate = (-)-alpha-cedrene + diphosphate (2E)-geranyl diphosphate = diphosphate + terpinolene (2E)-geranyl diphosphate = diphosphate + limonene (2E)-geranyl diphosphate = beta-myrcene + diphosphate Binds 3 Mg(2+) or Mn(2+) ions per subunit. Secondary metabolite biosynthesis; terpenoid biosynthesis. The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+). Belongs to the terpene synthase family. Tpsa subfamily.
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