entry stringlengths 6 10 | entry_name stringlengths 5 11 | protein_name stringlengths 3 2.44k | sequence stringlengths 2 35.2k | function stringlengths 7 11k |
|---|---|---|---|---|
Q9UYJ4 | PFDB_PYRAB | Prefoldin subunit beta (GimC subunit beta) | MQNIPPQVQAMLGQLESYQQQLQLVIQQKQKVQADLNEAKKALEEIEALPDDAQVYKTVGTLIVKTTKEKALQELKEKVETLEVRLNALNRQEQKINEKVKELTQKIQAALRPPTAG | Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding (By similarity). |
Q9UYK5 | SAHH_PYRAB | Adenosylhomocysteinase (EC 3.13.2.1) (S-adenosyl-L-homocysteine hydrolase) (AdoHcyase) | MVNCTSDYCVKDISLAPEGMKKIDWVSRFMPVLQHIRREFEEKKPFKGVRIAATLHLEMKTAFLLLTLKAGGAKVSAAASNPLSTQDDVVAALAKEGVKVYAIRGESKEEYYEFMNKALDIRPNIIIDDGADMVSLVHTERKELLDEIWGASEETTTGVIRLRAMERDKVLRFPVIAVNDSYMKYLFDNRYGTGQSTWDGIMRATNLLVAGKNVVVVGYGWCGRGIAMRARGLGATVIVVEVDPIKALEARMDGFLVMSMKEAAKIGDIFVTATGNIKCIRREHFELMKDGAIMANAGHFDVEIWKPDLEELAVEISNPR... | May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine. {ECO:0000255|HAMAP-Rule:MF_00563}. |
Q9UYL3 | FLAB4_PYRAB | Flagellin B4 | MHRKGAIGIGTLIVFIAMVLVAAVAAGVIIGTAGYLQQKAQATGMQTTQEVSSGIKIINIYGYVNSSVPSNGTITKMAIFVSPNAGSGGISLSNVKIVLSDGKKLVVYNYSKGLLYDKQISDLFNDSIVTIWNNITDTTFGIAVINDSGNKMDKDYPNLEWGDTVALLLRTTVFETEDNRRGIGPGTRIVGKVIPEVGAAGVIDFTTPSTYNYRVMVLQ | Flagellin is the subunit protein which polymerizes to form the filaments of archaeal flagella. |
Q9UYL4 | FLAB5_PYRAB | Flagellin B5 | MRRGAIGIGTLIVFIAMVLVAAVAAGVLISTSGYLQQRAMSVGLETTRDVSSGLRIISIWGYAPKNTTGNTTIQSNITKLAIYIAPNAGSEPINLNQTRIILTVKSTMVIFTFGGEDTVADWTNGAVNVFNETIWENINGTKFGVGVVVDSDKSMLSNKASPGMNSGDLAVLLINTKLAFNKYGGIPPNTKVVGKILPPHGAGTVIDLITPATYSSEGIELQ | Flagellin is the subunit protein which polymerizes to form the filaments of archaeal flagella. |
Q9UYR5 | NIKR_PYRAB | Putative nickel-responsive regulator | MDLVRFSISIPAELLEKFDRIIEEIGYENRSEAIRDLIRDFIIRREWEVGNEEVAGTITIVYNHDEGDVVKELLDLQHEYLDEIISTLHVHMDEHNCLEVIVVKGKAKRIKMIASRLMSLKGVKHGKLVMTSTGKELL | Transcriptional regulator. {ECO:0000255|HAMAP-Rule:MF_00476}. |
Q9UYR6 | IF2B_PYRAB | Translation initiation factor 2 subunit beta (aIF2-beta) (eIF-2-beta) | MEIDYYDYEKLLEKAYEELPENVKHHKSRFEVPGALVTIEGNKTIIENFKDIAEALNRDPQHLLKFLLREIATAGTLEGKRVVLQGRFTPYLIANKIKKYIKEYVICPVCGSPDTKIIKRDRFYFLKCEACGAETPIQHL | eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. |
Q9UYS6 | TFE_PYRAB | Transcription factor E (TFE) (TFIIE subunit alpha homolog) (Transcription initiation factor TFIIE) | MSRKNKALLEIAKDIGGDEAVEIVKALEKKGEATDEELAEITGIRVNTVRKILYALYDEKLADFKRIKDEETGWYYYYWHLETKRLPEIIRARKLRELERLKKMLQEETSEVYYHCGNPEHPKLTFDEAFEYGFTCPICGEILQEYDNSAVIEELKKRIEELEIELGLRPSPKKEKKKTRAKAKRKTRKK | Transcription factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Facilitates transcription initiation by enhancing TATA-box recognition by TATA-box-binding protein (Tbp), and transcription factor B (Tfb) and RNA polymerase recruitment. Not absolutely required for transcription i... |
Q9UYV6 | Y1401_PYRAB | Putative phosphate permease PYRAB14010 | MDMDPWLLLTLILGLAMAWAIGANDAANSMSTAVGAGAITPKQAVLIAGILEFTGAYFFGKTVTETIRKGIIDPSRISDPNVLVYGSLAALLGATIWLVIATKYGLPVSTTHSIIGGIVGYGVVYAGLEIVNWGKMASVVLSWILSPIVGAIFAFFIFKAIRRTVLESEDPIRSAKRWSPVWIGLAFVVIGTMFYIKVLHGKSLYMGVLKLGIPVGLVVFLITSMILRVKFPKVDPYLGAEFIFRRVQVITSGYVALAHGANDVANAIGPVAAVYTIATMGMAGAKVPVPRWILALGGLGIAIGVATYGYRVMETVGKKI... | Potential transporter for phosphate. |
Q9UZ06 | LEUD1_PYRAB | 3-isopropylmalate dehydratase small subunit 1 (EC 4.2.1.33) (Alpha-IPM isomerase 1) (IPMI 1) (Isopropylmalate isomerase 1) | MRVRGRAWKYGDNIDTDVIIPARYLNTSDPKELAKHVLEDLDPEFRSKMKPGDIIVAGENFGCGSSREHAPLAIKAAGVSCVIAKSFARIFYRNAINIGLPILEAPQAVDRIETGDELEVDFSSGEIRNLTKGEVYRANPFPDFIMEIIKAGGLVEWAKRRLKG | Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. |
Q9UZ16 | MTNA_PYRAB | Putative methylthioribose-1-phosphate isomerase (M1Pi) (MTR-1-P isomerase) (EC 5.3.1.23) (MTNA-like protein) (aMTNA) (S-methyl-5-thioribose-1-phosphate isomerase) | MEVRYKPEELTKLPRSVEYKERTVYMINQRLLPREFKVEAFRTVESVAEAIKNMTVRGAPAIGAAAAFGLALYAETSKAKSKDEFMDGFYKAYETLKNTRPTAVNLFWALNRIKKLVEEHLEDPLDEIKSLIVNEAQKIADEDVEANLRMGHYGAEVLPEGNLLTHCNAGSLATVHLGTVGAVVRVMHKDGSLKLLWLDETRPVLQGARLSAWEYSYDGLNVKLIADNAAAFVMQQGLVDAIIVGADRIVANGDFANKIGTYMLAVLAREHGIPFFAVAPLSSIDMSLKSGKEIPIEERSPEEVLTCGGCRIAPDVPVYN... | Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). {ECO:0000255|HAMAP-Rule:MF_01678}. |
Q9UZ54 | Y1300_PYRAB | Putative transcriptional regulatory protein PYRAB13000 | MKTFLTEQQIKVLVLRAKGLKQSEIARILKTTRANVSILEKRALEKIEKARNTLLLWEQINSKVSVSVKAGEDIFTIPDRLFKEADKAGVKVPYSTAEIIAFLVEHAPIEDRLAKRDFVIFLDSKNRLRISECLINFVEEGIGND | Putative transcriptional regulator. {ECO:0000255|HAMAP-Rule:MF_00620}. |
Q9UZ56 | IORB_PYRAB | Indolepyruvate oxidoreductase subunit IorB (IOR) (EC 1.2.7.8) (Indolepyruvate ferredoxin oxidoreductase subunit beta) | MKEYNIVITGVGGQGILTAANLLGWAALRAGYKVRVGEVHGMSQRFGSVIAYVRFGEDVYGAMVPEGKADVILSFEPVEALRYINYLKKGGLVFTNARPIPPVQVSMGLASYPSMEEIRKIVEEDFGGKFLAFDAEKLAIEAGNVITTNVVLIGALTQTPGFPLSAEHVKEVIRISVPPKAVDVNMRAFELGVKAAKEMLNL | Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates. |
Q9UZ61 | FTSZ2_PYRAB | Cell division protein FtsZ 2 | MVFDKLLEQAGINLDLDGKDMMDSEMLGDVSDLIKIAVIGVGGSGNNTITRLYDLGVQGADLIAMNTDAQHLHYVKAHKKLLLGRSITHGKGSGGDPRVGYRAAEASASEIAEVVKGYDLIFLTAGMGNGTGTGATPVIARIIKETARNNGLPQEPLVISVVTFPFKMEGRVRIEKAKAGIEMLLEYSDTVIIIQNDKLKELVPKLPIQIAFRFADEIIARMVKGIVETIKLPSMVNIDYADIYSVMKGGGPALIGIGESDSNNRAVDAVMEALNNKMLDVEFGSGDKALVHFTVGPDVSLEEITKAMEIVYERLGEKSE... | Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new ce... |
Q9UZ81 | NTPTH_PYRAB | Nucleoside-triphosphatase THEP1 (NTPase THEP1) (EC 3.6.1.15) (Nucleoside triphosphate phosphohydrolase) | MRFFVSGMPGVGKTTLAKRIADEIRREGYKVGGIITQEIRTGPKRSGFRVIALDTGEIGRLAYVGQGYPRVGRYVVDIEGFDRVAIPAISRALRDADIIIIDEIGPMEFKSNEFLKALGLVLKSEKPLLATVHRKLVDRYRPLGRYYWLTPENRNEVFAEILMEIRKVLGRNENAGNKA | Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency. {ECO:0000255|HAMAP-Rule:MF_00796}. |
Q9UZC1 | MPGS_PYRAB | Mannosyl-3-phosphoglycerate synthase (MPG synthase) (MPGS) (EC 2.4.1.217) | MLLEAPVYKEIFGAVTIHEVQKVIKMDTETEDVPVYTISNIPREKIYNLLGKMAIIVPMKNEKLHLVDGVLKAIPHKCPIIIVSNSKREGPNRYKLEVDLVRHFYNLTHSKVIMIHQKDPGLAKAFKEVGYTDILDGKGKVRSGKGEGMIIGMLLAKAIGAEYIGFVDADNYIPGSVNEYVKDYAAGFLMSESDYTMVRLHWRHKPKVTKGTLYFKKWGRVSEITNHYLNLLISEHTAFETTIMVTGNAGEHAMTMKLAEIMPFSTGYSVEPYEIVYLLERFGKWENVDEFKEVFDQGIEIFQIETLNPHFHEDKGQEHV... | Transfers a mannosyl group from GDP-mannose to phosphoglycerate to form mannosyl-3-phosphoglycerate (MPG). |
Q9UZC8 | RAD50_PYRAB | DNA double-strand break repair Rad50 ATPase | MKIEEVKVYNFRSHEETVVRFRKGINLIIGQNGSGKSSLLDAILVGLYWSKKLRLRGLKKDEFRRIGGKGGTRIEIKFENDDSKYVLFRDFSRNVAYLKVQENGKWRHASEPSMESVSSYIERILPYNVFLNAIYIRQGQIDAILESDETRDKVVREILNLDKLESAYENLKRIKTNINLLIESKKSFIARTENIEELIKANEDELTKKLSEINEISSKLPPIRGELEKVRENVKELESIKGKISELKIQVEKLKGRKKGLEEKIVQIERSIEEKKAKISELEEIVKDIPKLQEKEKEYRKLKGFRDEYESKLRRLEKEL... | Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Rad50 controls the balance between DNA end bridging and DNA resection via ATP-dependent structural rearr... |
Q9UZD5 | MFNA_PYRAB | Probable L-aspartate decarboxylase (ADC) (EC 4.1.1.11) | MSKFPEKGLPREEVLNLLEDKTKVDLTFSSGKILGSMCTMPHELAIEVFARYIDRNLGDPGLHPGTRKIEEEVIEMLSDLLHLEKGYGHIVSGGTEANILAVRAFRNISDAERPELILPKSAHFSFIKAGEMLGVKLVWAELKQDYAVDVKDVEAKISDNTIGIVGIAGTTGLGVVDDIPALSDLAREYGIPLHVDAAFGGFVIPFAKSLGYDLPDFDFKLKGVESITIDPHKMGMAPIPAGGIIFRRKKYLKAISVLAPYLAGGKVWQATITGTRPGASVLAVWALIKHLGFEGYREIVRKAMELSRWFAEEIKKLNNA... | Catalyzes the decarboxylation of L-aspartate to produce beta-alanine. {ECO:0000255|HAMAP-Rule:MF_01610}. |
Q9UZK4 | KAD6_PYRAB | Putative adenylate kinase (AK) (EC 2.7.4.3) (ATP-AMP transphosphorylase) | MLIAITGTPGVGKTTIAKLLAEKLGYEYVNLRDFALEKGCGREVDGEVEVEIDELAYFVEKELKDRNVVLDGHLSHLMPVDLVVVLRAHPRIIGERLRERGYSKEKIGENVEAELVDAILIEAIDEHENVIEVDTTNKTPEEIVEEIIGLIKSGVKRRVGIVDWSEVYDEIIPYLRLGGE | Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. {ECO:0000255|HAMAP-Rule:MF_00039}. |
Q9UZP8 | GCST_PYRAB | Probable aminomethyltransferase (EC 2.1.2.10) (Glycine cleavage system T protein) | MAKRVHLFDWHKEHAKKIEEFAGWEMPIWYSSIKEEHLAVRNAVGLFDVSHMGEIYFRGKDALKFLQYVTTNDISKPPAISGIYTLVLNERGAIKDETLIFNMGNNEYLMICDSDAFEKLYAWFTYLKKTIEQFTKLDLEIELKTYDIAMFAVQGPKARDLARDLFGIDINEMWWFQARWVELDGIKMLLSRSGYTGENGFEVYIEDANPYHPDESKRGEPEKALHVWERILEEGKKYGIKPAGLGARDTLRLEAGYTLYGNETKELQLLSTDIDEVTPLQANLEFAIYWDKDFIGKDALLKQKERGLGRKLVHFKMVDK... | The glycine cleavage system catalyzes the degradation of glycine. {ECO:0000255|HAMAP-Rule:MF_00259}. |
Q9UZV7 | KHSE_PYRAB | Homoserine kinase (HK) (HSK) (EC 2.7.1.39) | MKKRIYAPATIANFGPGFDVFGMAIEEPGDEVIVKESDSFEIEVEGYDVPRDENNVAVISAKALFKMVGEEGGVKIRLKKGVRPKSGLGSSGASSVAGALAAARVLGVDNDELIIMAALEGEKAASGSPHGDNVIPSYYGGFNILESLNPLRVHRVDVELNVVVVLPEVEVPTKEARRIVPEKVPLKDAIKNLAMASSLVLALKEGDIETVGRLLDDNLALPYRKKLMPWFDEVRKAGLEAGAYGVTVSGSGPSLFAIGENLKDIGKAMKEKFEELGIRAEFWITKTGRGAKWY | Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. {ECO:0000255|HAMAP-Rule:MF_00384}. |
Q9V005 | PXPA_PYRAB | 5-oxoprolinase subunit A (5-OPase subunit A) (EC 3.5.2.9) (5-oxoprolinase (ATP-hydrolyzing) subunit A) | MRVDLNSDLGESFGRYKLGLDEEVMRYITSANIACGWHAGDPIVMRRTVKLAKENNVQVGAHPGYPDLMGFGRRYMKLTPEEARNYILYQIGALYAFAKAEGVELQHVKPHGALYNAMVKEEELARAVIEGILDFDKNLILVTLSNSRVAEIAEEMGLKVAHEVFADRAYNPDGTLVPRGKPGAVIEDKEEIAERVISMVKDGGVRAINGEWVELRVDTICVHGDNPKALEITSHIRKILEEEGVKVVPLKDFIG | Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate. {ECO:0000255|HAMAP-Rule:MF_00691}. |
Q9V022 | SYP_PYRAB | Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase) (ProRS) | MVERKRWSENFSEWFNEVIEEAGILDKRYPVKGMNVWLPYGLKIMKNIEKFIHEEMERTGHQEVLFPALIPETEFKKEAEHIAGFEGEVFWITHAGHEPLDVKLILRPTSETAMYSMFALWIRSHADLPFKVYQIVNVYRYETKHTRPLIRVREISRFFEAHTAHADFEDAERQIKEDLEIFDNLMKRLAIAYIISKRPEWDKFPGAFYSLGAEVVMPDGRTLQIGTMHNYKQNFAKAYNILYEKEDGTHDYVHQTTFGMSERLLAAVIAIHGDDRGMVLPPTIAPIQVVIVPIPKKEKQEIVYEYAREIEEELRTAGIR... | 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). {ECO:0000255|HAMAP-Rule:MF_01571}. |
Q9V024 | TBP_PYRAB | TATA-box-binding protein (Box A-binding protein) (BAP) (TATA sequence-binding protein) (TBP) (TATA-box factor) | MVDTNNVKLRIENIVASVDLFAQLDLEKVLDICPNSKYNPEEFPGIICRFDDPKVALLIFSSGKLVVTGAKSIHDIERAVAKLIEKLKGIGVKFKRAPLIDIQNMVFSGDIGREFNLDNVALTLPNCEYEPEQFPGVIYRVKDPRAVILLFSSGKIVCSGAKSEADAWEAVRKLLRELEKYGLIEEEEEEL | General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation (By similarity). |
Q9V030 | UBIX_PYRAB | Flavin prenyltransferase UbiX (EC 2.5.1.129) | MRVVVAITGASGTIYGIKLYETLRDLGHEVILLASKTGIKVAKYETGIEVKPDFSEDELFAPIASGSYPFDAMVIAPCSMKTLSAIANGFSNNLITRAADVALKERRKLVLLIRETPLNLIHIQNMLKITQAGGIIMPASPAFYHKPGTIDDMIKFIIGKILDVLGINHNLYKRWGMDYND | Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN. {ECO:0000... |
Q9V074 | TYW31_PYRAB | tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-demethylwyosine(37)-N(4))-methyltransferase 1 (EC 2.1.1.282) (tRNA wyosine derivatives biosynthesis protein Taw3 1) | MRFTENFERAKKEALISLEIALRRGEVDEDIIPLLKKINEKPNYFTTSSCSGRISIMEMPDFGDKVNAKWLGKWHREVSLDEVLEAIRKHREGQLWLLVRSPILHVGARTLEDGIKLLNLGVSCGFKYSNIKSISDRKLIVEIRSTERLDALLGENGEILVSDDYMRKLVEIANAQVRRFKRKLKRFEERIEEL | S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wyosine derivatives biosynthesis pathway. Probably methylates N-4 position of wybutosine-86 to produce wybutosine-72. {ECO:0000255|HAMAP-Rule:MF_00266}. |
Q9V085 | METE_PYRAB | Methionine synthase (EC 2.1.1.-) (Homocysteine methyltransferase) | MELPILPTSVIGSYPKPRWLLRMYKLRELGKIPEEDFKEAVKDASVAVLREHERAGVDIPWDGEMWRSEMTEHFTAKISGFKFYGPVRVWGNAYFNKAAAVDKLEYKEPLVLEEFLWVRENTTREIVKVPITGPYTIAEWSFNEYYPDKESFVMDLAKIINKELKTLEEHGATYIQLDEPAMLNHPDEVPLAVEAINRAVKGIKIKVGLHVCYSNYYLLADYFDDIRVTQFALEFANRQFRDMDFLKKLSGKELGFGVVDVHNPRIETVDEIVRAIKKAFNYLEPEWLYINPDCGLKLLDRRIAYQKLVNMVKAVRIVRK... | Catalyzes the transfer of a methyl group to L-homocysteine resulting in methionine formation. The physiological methyl donor is unknown. {ECO:0000255|HAMAP-Rule:MF_00288}. |
Q9V098 | SOR_PYRAB | Superoxide reductase (SOR) (EC 1.15.1.2) | MLKDTIKSGDWKGEKHVPVIEYEKEGDLVKVEVSVGKEIPHPNTPEHHIAWIELYFHPEDGQFPILVGRVAFTSHDDPLTEPRAVFFFKTKKKGKLYALSYCNIHGLWENEVQLE | Uses electrons from reduced NADP, by way of rubredoxin and an oxidoreductase, to catalyze the reduction of superoxide to hydrogen peroxide. |
Q9V099 | RUBR_PYRAB | Rubredoxin (Rd) | MAKWRCKICGYIYDEDEGDPDNGISPGTKFEDLPDDWVCPLCGAPKSEFERIE | Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule (By similarity). |
Q9V0D9 | APBC_PYRAB | Iron-sulfur cluster carrier protein | MTIKAPALNLPGLGADPLTQRIKEKEKKWKYKVAVLSGKGGVGKSTVAVNLTAALAKMGYFVGILDADIHGPNVAKMLGVEKEEIYAEKFDDGHFEMIPPMADFMGQVTPIKVMSMGMMVPEDQPIIWRGALVTKAIKQLLGDVKWGSLDFMIIDFPPGTGDEILTVVQSIQLDAAIIVTTPQEVALLDTGKAVNMMKKMEVPYIAVVENMSYLICPHCGNKIDIFGEGGGEKLAEKEGVDFLGKIPIDLKAREASDLGIPIVLYGDTPAAKAFMEIAEKLVNKLKEMKGDEKKE | Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP. {ECO:0000255|HAMAP-Rule:MF_02040}. |
Q9V0E3 | NOP10_PYRAB | Ribosome biogenesis protein Nop10 | MRFRIRKCPKCGRYTLKETCPVCGEKTKVAHPPRFSPEDPYGEYRRRLKRELLGIGRKEK | Involved in ribosome biogenesis more specifically in 18S rRNA pseudouridylation and in cleavage of pre-rRNA. |
Q9V0E4 | IF2A_PYRAB | Translation initiation factor 2 subunit alpha (aIF2-alpha) (eIF-2-alpha) | MPRRAREYPEEGEFVVATVKRIHNYGAFLELDEYPGKEAFMHISEVASTWVRNIRDYLKEGQKVVAKVIRVDPRKGHIDLSLRRVTQQQRKAKLQEFKRAQKAENLLKLAAEKLGKDFETAWREVWVPLEEEWGEVYAAFEDAAKDGIDVLKGHVPDEWLPVLKEIIDNYVEVPTVTIDAEFEITVPKPNGVEIIKEALIRARDRANKEKDVEVKFTYLGAPRYRIDITAPDYYKAEEVLESIAEEILRVIKEAGGEATLLRKEKRIKKVKKRKK | eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. |
Q9V0G1 | GCSH_PYRAB | Probable glycine cleavage system H protein | MIEVGEYKVKEGLYYTKEHEWAQVLEDGTVLVGITDYAQKELGDIAYVELPEVGKEVKKGEVLCEVESVKAVSEVYAPVSGEVIEVNEELSDSPEKINEDPYGAWIAKIKPNNLEEELKELMDAEKYAEFLKSL | The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. {ECO:0000255|HAMAP-Rule:MF_00272}. |
Q9V0G8 | RS19E_PYRAB | Small ribosomal subunit protein eS19 (30S ribosomal protein S19e) | MATVYDVPGDLLVERVAQRLKEIPEIKPPEWAPFVKTGRHKERLPEQEDWWYYRVASILRRVYLDGPVGIERLRTYYGGRKNRGHAPERFYKAGGSIIRKALQQLEAAGFVEKVPGKGRVITPKGRSFLDKIATELKKELEEIIPELKKY | May be involved in maturation of the 30S ribosomal subunit. |
Q9V0H5 | CETZ_PYRAB | Tubulin-like protein CetZ | MRAIIIGIGQCGGKIADIFSLVDFEAIAINTSRGDLEYLKHIPQDKRILIGESIVGGKGVNANPVLGREAMKRDLPMVMKKINSMVGYEDVDIFFLTFGFGGGTGAGGTPVLAEALKEEYPDSLVVAIGALPLKEEGIRPTINAAITIDKLSKVVDSIIAIDNNKLKESDEDISQAYERINYTIVERIASLLALIDVPGEQTLDASDLKFVLRAMGSFATVGYAKADAEKVKSLSRLIIRSFENEGLYLDVSLESALYGLVAIHGPPEVLKAKDIFEALNELTQRIRGKQIFRGFYPDPRERSVEVVTLLSGIYESKSIE... | Involved in cell shape control. {ECO:0000255|HAMAP-Rule:MF_01946}. |
Q9V0I7 | GUAAB_PYRAB | GMP synthase [glutamine-hydrolyzing] subunit B (EC 6.3.5.2) (GMP synthetase) | MNWEKFVEEKVKEIRETVGDSKAIIALSGGVDSSTAAVLAYKAIGDKLHAVFVNTGFLRKGEPEFVVKTFRDEFGMNLHYVDAQDRFFSALKGVTDPEEKRKIIGRVFIEVFEEVAREIGAEYLIQGTIAPDWIESQGKIKSHHNVGGLPERLNLKLIEPLRDLYKDEVRELAKFLGLPEKIYNRMPFPGPGLAVRVIGEVTPEKIRIVREANAIVEEEVERAGLRPWQAFAVLLGVKTVGVQGDIRAYKETIAVRIVESLDGMTANAMNVPWEVLQRIAFRITSEIPEVGRVLYDITNKPPATIEFE | Catalyzes the synthesis of GMP from XMP. |
Q9V0M0 | NEP1_PYRAB | Ribosomal RNA small subunit methyltransferase Nep1 (EC 2.1.1.-) (16S rRNA (pseudouridine-N1-)-methyltransferase Nep1) | MSEKKRLHLIIADAELETVPEQILDHPAIVNYAKRRKRKPEKIILDSTYHHAALKQLEDGERRGRPDIVHICLLNALDSILNKEDRLRVYVHTRNDYVIYIKPETRLPRNYNRFIGLMESLFEKGAVPEDLELLRLERKTLQELINEINPDAVFVMHEEGELMIPKNFGKLLDKFKKPAVIIGGFPHGDFRSRVEGVKISLYKEPLMAWTIVNEVIVSYEWEVIKKFSTKFI | Methyltransferase involved in ribosomal biogenesis. Specifically catalyzes the N1-methylation of the pseudouridine corresponding to position 914 in M.jannaschii 16S rRNA (By similarity). |
Q9V0N5 | DHYS_PYRAB | Probable deoxyhypusine synthase (DHS) (EC 2.5.1.46) | MKAKDIVLKKSEEIEGLAIEGPWLDEVESLEGVISYYEKIGFQATHLGKAVKIWRKVEEKRKGGEEVRVFLGYTSNIVSSGLREIIAWLVKERKVDVIVTTAGGIEEDFIKTLKPFILGDWEVNDAELREKGINRIGNIFVPNDRYIEFEKYMVPFFERILDIERKLKRPLTASEFIYEMGRYMDEVLGKEKEKSIIYWAYKRDVPIFCPAITDGSIGDMLYFFKEERHDSKLVIDIANDIVKLNNLAITAKETASIILGGSLPKHAIINANLFRGGTDYAIYISTAVPWDGSLSGAPPSEGVSWGKIKAKADYVEIWAD... | Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue. |
Q9V0N8 | TRMY_PYRAB | tRNA (pseudouridine(54)-N(1))-methyltransferase (EC 2.1.1.257) | MRVFIIKANEAHTANDFSLKDLPGTSGRIDLICRALNSAFHLSHSFRKNVRVYVTLLGPPDPPKSLRFEGPELKPKILNPDELSTAKIIGKALERGKDIKRKSTEEIKVLPGIYVSNMSFEDVIRVVIKRFPLYILEEDGKDITEVEFPKNNVAFVLGDHIGLSSEDLSFLESVGMKVSIGPKAYLTSHVIAYVNIYLDRLGIP | Specifically catalyzes the N1-methylation of pseudouridine at position 54 (Psi54) in tRNAs. {ECO:0000255|HAMAP-Rule:MF_00587}. |
Q9V0Q4 | PGP_PYRAB | Phosphoglycolate phosphatase (PGP) (PGPase) (EC 3.1.3.18) | MKIKAISIDIDGTITYPNRMIHEKALEAIRKAESLGIPVMLVTGNTVQFAEAASILIGTSGPVVAEDGGAISYRKKRIFLANMDEEWILWNEIRKRFPNARTSHTMPDRRAGLVIMRETIDVETVRKIIHELGLNLVAVDSGFAIHVKKPWINKGAGIEKACELLGIKPREVAHIGDGENDLDAFKVVGYRIAIAQAPDVLKENADYVTEKEYGEGGAEAIFHVLRVSGYMDF | Catalyzes the dephosphorylation of 2-phosphoglycolate. {ECO:0000255|HAMAP-Rule:MF_01419}. |
Q9V0V3 | PELO_PYRAB | Protein pelota homolog (EC 3.1.-.-) | MEVLEEKPKEGKVKLKVETLDDLWHLYHVISPGDIVYAKTLRKQAQRSDSLRPEKVEAIPVFLGVRAEKINLHRFANQLRVTGPIVYASRDDVPLGKYHTIAVEPGMTITIQKERWRSHHVERIKEAVEASKRAKVMIVAMEDGEAEVAIVREYGLDFIASIRHNIGGKRYNVKREDEEKKFFHDVAKTIKDLIERENVQKVIVAGPGFYKENFYGFLRENYPELAGKVVLDDTSMGGRVGVYEVIKRGTVDKVYTETRVAQEIKLVEKVIERIAKDEPVAYGLKDVEEAVNYGAVDTLLVLDELLKGDDRERIEEIMEM... | May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity. {ECO:0000255|HAMAP-Rule:MF_01853}. |
Q9V0V4 | RNP2_PYRAB | Ribonuclease P protein component 2 (RNase P component 2) (EC 3.1.26.5) (Pop5) | MKLKTLPPTLRDKNRYIAFEIISDDEFTKDEVKSLIWEASLRVLGELGTALAKPWFIKYDPKTKTGIVRCDREYVEHLRFALMLATDFNGKRLIIRTLGVSGTIKRLKKKFLSQYGWK | Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. {ECO:0000255|HAMAP-Rule:MF_00755}. |
Q9V0V5 | TF2B_PYRAB | Transcription initiation factor IIB (TFIIB) | MTKQRVCPVCGSTEFIYDPERGEIVCARCGYVIEENIVDMGPEWRAFDASQREKRSRTGAPESILLHDKGLSTDIGIDRSLTGLMREKMYRLRKWQSRLRVSDAAERNLAFALSELDRITAQLKLPKHVEEEAARLYREAVRKGLIRGRSIESVIAACVYAACRLLKVPRTLDEISDIARVEKKEIGRSYRFIARNLNLTPKKLFVKPTDYVNKFADELGLSEKVRRRAIEILEEAYKRGLTSGKSPAGLVAAALYIASLLEGEKRTQREVAEVARVTEVTVRNRYKELVEKLGIKVPVT | Stabilizes TBP binding to an archaeal box-A promoter. Also responsible for recruiting RNA polymerase II to the pre-initiation complex (DNA-TBP-TFIIB). {ECO:0000255|HAMAP-Rule:MF_00383}. |
Q9V0V6 | RS10_PYRAB | Small ribosomal subunit protein uS10 (30S ribosomal protein S10) | MQKARIKLASTNVRSLEEVANQIKQIAERTGVRMSGPIPLPTKRIRIVTRKSPDGEGSATFDRWELRIHKRLIDIEADERAMRQIMRIRVPEDVTIEIELIS | Involved in the binding of tRNA to the ribosomes. {ECO:0000255|HAMAP-Rule:MF_00508}. |
Q9V0V7 | EF1A_PYRAB | Elongation factor 1-alpha (EF-1-alpha) (Elongation factor Tu) (EF-Tu) | MPKEKPHVNIVFIGHVDHGKSTTIGRLLYDTGNIPETIIKKFEEMGEKGKSFKFAWVMDRLKEERERGITIDVAHTKFETPHRYITIIDAPGHRDFVKNMITGASQADAAVLVVAATDGVMPQTKEHAFLARTLGIKHIIVTINKMDMVNYDQKVFEKVKAQVEKLLRTLGYKDFPVIPTSAWNGDNIVKKSDKMPWYNGPTLIEALDQIPEPEKPVDKPLRIPIQDVYSIKGVGTVPVGRVETGKLKVGDVVIFEPASTIFHKPIQGEVKSIEMHHEPLQEALPGDNIGFNVRGVSKNDIKRGDVAGHPDKPPTVVRTK... | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00118}. |
Q9V0X2 | FLUC_PYRAB | Fluoride-specific ion channel FluC | MNLKTTLLLIIGGGLGALARYYISGILPVYKDFPLGTLLVNSIASFILGYLYGLLFFGFEVSSEWRIFLGTGFCGGLSTFSTFSYETFSLLREGEYLLAFMNVVANVLVTITLVFLGFILARR | Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. {ECO:0000255|HAMAP-Rule:MF_00454}. |
Q9V0Y5 | MTAD_PYRAB | 5-methylthioadenosine/S-adenosylhomocysteine deaminase (MTA/SAH deaminase) (EC 3.5.4.28) (EC 3.5.4.31) | MVSLSVLLRGGLVLYGRDYKLTRADVLIEGDKIVEVKRNINKPADEVLDVSKSLVIPSFINAHTHSPMVILRGLAEDVPLMEWLQEYIWPVERKLRRKDVYWGSKLALIEMAHSGTSTFVDMYFHMEEIAKATEEVGLRAYLGYGMVDLDDEEKRKIEMRETEKLYEFIKKLDSSKVNFILAPHAPYTCSFDCLRWVSEKSREWNSLVTIHLAETQDEIKIIREKYGKSPVDVLEDVGLLNEKLIAAHGIWLSDEDIRKISSAGATIAHCPASNMKLGSGVFPMKKALENNVNVALGTDGAASNNTLDILREMRLASLLQ... | Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine. {ECO:0000255|HAMAP-Rule:MF_01281}. |
Q9V0Y9 | REG6_PYRAB | HTH-type transcriptional regulator FL11 (Feast/famine regulatory protein FL11) (FFRP FL11) | MRVSLDEIDRRIIKILQKDGKAPLREISKITGLAESTIHERIKKLRESGVIRKFTAIVNPEALGYSMLAFILIKVKAGKYAEVASNLVKYEEIMEVYETTGDYDMVVKIRTKNSEELNSFLDVIGSIPGVEGTHTMIVLKTHKETTELPIK | DNA-binding protein involved in the repression of transcription of a large number of genes, thereby arresting growth, in response to environmental changes. |
Q9V0Z2 | NAC_PYRAB | Nascent polypeptide-associated complex protein | MMPMNPKQLKKLMKQLDMKQLDGVKEVIIKLENKEIVIKEPVVTVIRAMGEKMYQIAGGTEEERVVLKISEEDIKLVMEQAGVDYETAKKALEEAGGDLAEAILRLTDQ | Contacts the emerging nascent chain on the ribosome. {ECO:0000255|HAMAP-Rule:MF_00814}. |
Q9V0Z6 | RTCA_PYRAB | RNA 3'-terminal phosphate cyclase (RNA cyclase) (RNA-3'-phosphate cyclase) (EC 6.5.1.4) | MITIDGSYGEGGGQILRTSIALSAITGEPVRIINIRANRPNPGLRPQHLHGILALKHLANADVKGAHVGSRELVFIPKRLEAKKVEVNIGTAGSITLVLQALLPAMAFAKNRVEFKITGGTDVPWSPPVDYLANVTLFALEKLGIMAGIKIVRRGHYPKGGGIIEGYVEPWKERRELVATKYSSIAKVEGISHATNLPAHVAERQAKAAKEELSKLEVPVKIKTEVSKSLGPGSGIVVWAETDCLRLGGDALGKRGKPAEVVGKEAAQELLEQLKPGYCVDKFLGDQLIPFLAFSGGEIWVSEVTNHLKTNIWVVENFLG... | Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in t... |
Q9V105 | ARCH_PYRAB | Protein archease (tRNA m5C methyltransferase chaperone) | MKRWEHYEHTADIGIRGYGDSLEEAFEAVAIALFDVIVNVNKVEKKEVREVEVEGEDLESLLYNFLEELLVIHDIEGLVFRDFEVKIEKTEKGYKLKAKAYGEKLDPEKHEPKEEVKAITYHDMKIEKLPDGRWMAQLVPDI | Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity). Chaperone or modu... |
Q9V108 | PTH_PYRAB | Peptidyl-tRNA hydrolase (PTH) (EC 3.1.1.29) | MFKFKQVIVVRKDLKLSKGKLAVQVAHGAVTAAFKAYKEKREWFEKWFHEGQKKVVVKVESLDELFKLKAEAEKLNLPTALIQDAGLTEIPPGTITVLAIGPGPSEIIDKVTGHLKLL | The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. {ECO:0000255|HAMAP-Rule:MF_00628}. |
Q9V109 | RS7_PYRAB | Small ribosomal subunit protein uS7 (30S ribosomal protein S7) | MAKPLSERFFIPHEIKVMGRWSTEDVEVRDPSLKPYINLEPRLLPHTHGRHAKKHFGKANVHIVERLINKIMRSGGSHYKVAGHFMRREHRSLNSKKVKAYEVVKEAFKIIEKRTGKNPIQVLVWAIENAAPREDTTSVMFGGIRYHVAVDISPMRRLDVALRNIALGASAKCYRTKMSFAEALAEEIILAANKDPKSYAYSKKLEIERIAESSR | 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. Is located at the subunit interface close to the decoding center. {ECO:0000255|HAMAP-Rule:MF_00480}. |
Q9V118 | RRP42_PYRAB | Exosome complex component Rrp42 | MSDNEIVAGIMRDHIINLLKEGKRIDDRGFEDYRPIEIEVGVIEKAEGSALVKLGSTQVLVGIKTSLGEPFPDTPNMGVMTTNVELVPLASPTFEPGPPDERAIELARVIDRGIRESKALNLEKMVIVPGKIVRVVFIDVHVLDHDGNLMDAIGIAAIAALLNARVPKVRYNEETGEVETLDETEPLPVEKIPVPVTFAKIGNILVVDPSLDEELVMDGKITITTDETGHISAVQKSEGGAFKLEEVMYAVETAFKKAEEIRKLILEAVEKAKQ | Non-catalytic component of the exosome, which is a complex involved in RNA degradation. Contributes to the structuring of the Rrp41 active site. {ECO:0000255|HAMAP-Rule:MF_00622}. |
Q9V120 | RRP4_PYRAB | Exosome complex component Rrp4 | MKRIFVQNRELVVPGTLLAQGPYKNGRGTFREGSRIYSTVIGLVDIKGNTIRVIPLEGPYIPEVGDNVIGKIVDVKFSSWVVDIGAPYPANLKIQDFTDEKIDLLRTDLRKFFDIGDIIYAKVKAITEVNNIDLTTKGMPFNGGPLKGGQIVKITPSRVPRVIGRGGSMINMIKKLTMTRIIVGQNGWIWVSGKNDALEKLAIEAILKIDKESHTRGLTDRIKALLLSRLQELKEKGVIEEIPKLEEEPQGEDEVNGNDGEARGA | Non-catalytic component of the exosome, which is a complex involved in RNA degradation. Increases the RNA binding and the efficiency of RNA degradation. Confers strong poly(A) specificity to the exosome. {ECO:0000255|HAMAP-Rule:MF_00623}. |
Q9V122 | PSA_PYRAB | Proteasome subunit alpha (20S proteasome alpha subunit) (Proteasome core protein PsmA) | MAFVPPQAGYDRAITVFSPDGRLFQVNYAREAVKRGATAVGVKCKDGVVLAVEKRITSRLIEPESYEKIFQIDDHIAAASSGIIADARVLVNRARLEAQIHRLTYGEPAPLAVIVKKICDLKQMHTQYGGVRPFGAALLMAGVNDKPELYETDPSGAYFAWKAVAIGSGRNTAMAIFEDKYRDDMTLDEAIKLAIFALAKTMEKPSAENIEVAVITVKDKKFRKLSKEEIEKFLGEVMKEVEEEEVKEKEEDYSELDSHY | Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. {ECO:0000255|HAMAP-Rule:MF_00289}. |
Q9V138 | IF1A_PYRAB | Translation initiation factor 1A (aIF-1A) | MPKKERKVEGDEVIRVPLPEGNQLFGVVEQALGAGWMDVRCEDGKIRRCRIPGKLRRRVWIRVGDLVIVQPWPVQSDKRGDIVYRYTQTQVDWLLRKGKITQEFLTGGSLLVE | Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits (By similarity). |
Q9V148 | HYPA_PYRAB | Hydrogenase maturation factor HypA | MHEWALADAIVRTALDYAQKENASKILAIKVVLGELQDVNAEVVEFAMKELLRGTIGEGAEIIFEEEEAVFRCRNCGHEWKLKEVKDKLDERIREDIHFIPEVVHAFISCPNCGSHDFEVVKGRGVYIAGIKIEKEEGE | Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. {ECO:0000255|HAMAP-Rule:MF_00213}. |
Q9V151 | RF1_PYRAB | Peptide chain release factor subunit 1 (Translation termination factor aRF1) | MTRHDAQLYELKKKIEELKKIRGRGTELISLYIPAGYDLSKVMQQLREEYSTAQNIKSKTTRKNVLGALERAMQHLKLYKQTPENGLALFVGNVSEMEGNTDIRLWAIVPPEPLNVRLYRCDQTFVTEPLEEMLRVKDAYGLITVEKNEATIGLLRGKRIEVLDELTSNVPGKTRAGGQSARRYERIREQETHEFMKRIGEHANRVFLPLLEKGELKGIIVGGPGPTKEDFVEGDYLHHELKKKIIGVVDISYHGEYGLRELVEKASDILRDHEVIREKKLVNEFLKHVVKDTGLATYGEREVRRALEIGAVDTLLISEG... | Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA. |
Q9V159 | REG7_PYRAB | HTH-type transcriptional regulator LrpA | MVDERDKIILDILSKDARTPFTEIAKILGISETAVRKRVKALEEKGIIEGYTIKINPKKLGYSLVTITGVDTRPEKLFEVAEKLKEFEFVRELYLSSGDHMIMAVIWAKDGEDLADIISNKIGKIDGVTKVCPAIILERLK | DNA-binding protein that negatively regulates its own transcription. Interferes with RNA polymerase (RNAP) recruitment by inhibiting the association of RNAP with the TBP-TFB promoter complex. |
Q9V196 | RL13_PYRAB | Large ribosomal subunit protein uL13 (50S ribosomal protein L13) | MRIINAEGLILGRLASRVAKMLLEGEEVVIVNAEKAVITGNREVIFSKYKQRTGLRTLTNPRRGPFYPKRSDEIVRRTIRGMLPWKTDRGRKAFKRLKVYVGIPKEFKDKQLETIVEAHVSRLSRPKYVTVGEVAKFLGGKF | This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. {ECO:0000255|HAMAP-Rule:MF_01366}. |
Q9V1A0 | RS13_PYRAB | Small ribosomal subunit protein uS13 (30S ribosomal protein S13) | MADFRHIVRVAGVDLDGNKQLRWALTAIKGVGINFATMVCRVAGLDPFMKAGYLTDEQVKKIEEILQDPVAHGIPRWAVNRPKDYETGRDLHLITAKLDMAIREDIMRLRRIRAYRGIRHELGLPVRGQRTRSNFRRGQTVGVSRKKK | Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits these bridges are implicated in subunit movement. {ECO:0000255|HAMAP-Rule:MF_01315}. |
Q9V1B3 | G3PP_PYRAB | Glyceraldehyde 3-phosphate phosphatase (EC 3.1.3.-) | MIKVIFFDLDDTLVDTTKLAELARRNAIENMIRHGLPVDFETAYSELMELIKEYGSNFPHHFDYLLRRLDLPYNPKWVSAGVIAYHNTKFAYLREVPGARKVLIRLRELGYRLGIITDGNPVKQWEKILRLEIDDFFEHVIISDFEGVKKPHPKIFKKALKAFNVDAQEALMVGDRLYSDIYGAKNVGMKTVWFKYGKYSKEELEYREYADYEIEKLQDLLKVIENENGSNKEVHPAR | Catalyzes the dephosphorylation of D,L-glyceraldehyde 3-phosphate in vitro. |
Q9V1E3 | SYE_PYRAB | Glutamate--tRNA ligase (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS) | MEVERIALKYALINAIEHGGKANPKAVIGKVLGENPELRSKAREIVPIINKVVEEVNSLSLDEQKAKLMEIYPEYFEKKEEKKEEKKGLPPLPKAEKGKVVTRFAPNPDGAFHLGNARAAILSYEYAKMYGGKFILRFDDTDPKVKRPEPIFYEMIIEDLEWLGIKPDEIVYASDRLELYYKYAEELIKMGKAYVCTCKPEKFRELRDKGIPCPHRDEPVEVQLERWRKMLNGEYKEGEAVVRIKTDLNHPNPAVRDWPALRIVDNPNHPRAGNKYRVWPLYNFASAIDDHELGVTHIFRGQEHAENETRQRYIYEYFGW... | Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). {ECO:0000255|HAMAP-Rule:MF_02076}. |
Q9V1F5 | HARB_PYRAB | Archaeal histone B (Archaeal histone A2) | MAELPIAPVDRLIRKAGAQRVSEKAAKLLAEHLEEKALEIAKKAVDLAKHAGRKTVKVEDIKLAIRS | Binds and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. Increases the resistance of DNA to thermal denaturation (in vitro). |
Q9V1G4 | TRPD_PYRAB | Anthranilate phosphoribosyltransferase (EC 2.4.2.18) | MLEKIINRENLSFEEAYNLFKELMNESDVRIAAYLAAFQTKGYTAEEIAGLAKAMRDYAIKLELGEVADTAGTGGDGSSSINVSTASALILSAFTKVAKHGNVSITSKSGSANVLEALGLNIKIPPEKARKMIEKTNFTFIFAPMYHPALKRIMPVRRELKVKTVFNILGPLANPAEPKFQVLGVNSPDLVEKMAEALSFLGVERALVVHGMGLDEVNPRGETIVAEVNGEDIDMYTLTPEDFGVERVKVVPCNSPQESAERIKAVLRGEGKVEDRNFILINASAALYASKVAEDFREGVELVKGILGEPMSKKLEEIIC... | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). {ECO:0000255|HAMAP-Rule:MF_00211}. |
Q9V1G8 | TRPB1_PYRAB | Tryptophan synthase beta chain 1 (EC 4.2.1.20) | MWFGKFGGQYVPETLMEPLRELEKAYKRLKNDEEFNRQLDYYLRTWAGRPTPLYYAERLTKKVGGAKIYLKREDLLHGGAHKTNNAIGQALLAKFMGKTRLIAETGAGQHGVATAMAGALLGMKVDIYMGAEDVERQKMNVFRMKLLGANVIPVHTGSKTLKDAINEALRDWVATFEYSHYLIGSVVGPHPYPIIVRDFQSVIGREAREQILEAEGDLPDVIVACVGGGSNAMGIFYPFVKDKSVRLIGVEAGGKGIESGKHSASLNAGEIGVFHGMLSYFLQDEEGQIRTTHSIAPGLDYPGVGPEHAYLKESGRAEYV... | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. |
Q9V1G9 | TRPA_PYRAB | Tryptophan synthase alpha chain (EC 4.2.1.20) | MFRDGSLIPYLTAGDPSAKATLRFLLAIEEYSGAIELGIPFSDPIADGKTIQQSHFRALKGGFKLEHAFNIVREFRKHSDVPIVLMTYYNPVFRVGLREFIGKAKDSGVDGMLIVDLPVMHASEFLEVAREEGIKTVFLAAPNTPDERLKEIDKASTGFVYLISLYGTTGARDKIPETAFNLLKRAKRICKNKVAVGFGVSKREHVEMLLNAGANGVVVGSALINIIAEHGENAEEKLREKVRELAGL | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. |
Q9V1H0 | AROC_PYRAB | Chorismate synthase (CS) (EC 4.2.3.5) (5-enolpyruvylshikimate-3-phosphate phospholyase) | MRGRVLSFTLFGESHGKGVGVVITGIPPGIKVSHEELVKELERRKGIPGLSTARSEPDNPIILSGIFRGYTTGTPIAVLFENKDVDSSYYEDIKDKPRPGHADYPARIKYFGYNDYRGGGHFSGRLTVGIVTAGYFAKKILEKYGIRIRAYIKRIGRVEAKQLTLEEILSSENPFCPDEEAFEKMVEEIELARREGDSVGGIVEVVAVNVPPGLGGPYEEDIEADLASAFFRIPAVKGVEFGLGFKVAEKRGSEVNDPYVIRDGKVVTKTNNHGGVLGGITTGMPIIARIAFKPTPSIYLPQRTVDLREMKEVEIKLRGR... | Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a s... |
Q9V1I9 | LEUD2_PYRAB | 3-isopropylmalate dehydratase small subunit 2 (EC 4.2.1.33) (Alpha-IPM isomerase 2) (IPMI 2) (Isopropylmalate isomerase 2) | MITTGRVWKFWDNVSTDEITPGRYNLTKDPQELARIAFIEVRPEFAEKVRRGDVVVGGKNFGIGSSRESAALALKAAGVSGIIAKSFGRIFYRNAVNLGIPLLIGDTDELEDGDVITVNWETGEVRKNGQTLQFEPLPGFLLEIVREGGILEFIRRRGDLCIG | Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. |
Q9V1J9 | SRP19_PYRAB | Signal recognition particle 19 kDa protein (SRP19) | MSKFVIWTSELDSRLSKKYGRVVPRNLAVERPSIEEIEEAAKSLGFKVLQVEREKLNPKLSGIDEDLRTYGRIIIESPYGKAKTLKIIAQKIRELRRRR | Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP. {ECO:0000255|HAMAP-Rule:MF_00305}. |
Q9V1N3 | ALBA_PYRAB | DNA/RNA-binding protein Alba | MTEEHVVYIGKKPVMNYVLAVITQFHEGAKEVSIKARGRAISRAVDVAEIVRNRFLKDDVDVKEIKIGTEELPTADGRTTNTSTIEIVLARKA | Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stabili... |
Q9V1N4 | RFRNP_PYRAB | RNA-free ribonuclease P (RNA-free RNase P) (EC 3.1.26.5) (Protein-only RNase P) | MIRFVLDTSIFVNPDVRKKFGETPTKAMKTFLKYAESLFGHVEFYMPPGIYREVMHFVEEEEVSPDIELYIIKKPPNVHDIKIPAFVVYELIEDIRRRVDKGLRVAEKAVRESVIDTSNVDKIIQKLRRNYRKALREGILDSKEDFELILLAKELDGIIVSADVGILTWAEKMGIKWVDAFKFKEVLEELVEKLKRSESEKERK | RNA-free RNase P that catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. {ECO:0000255|HAMAP-Rule:MF_01078}. |
Q9V1P3 | TRM1_PYRAB | tRNA (guanine(26)-N(2))-dimethyltransferase (EC 2.1.1.216) (tRNA 2,2-dimethylguanosine-26 methyltransferase) (tRNA(guanine-26,N(2)-N(2)) methyltransferase) (tRNA(m(2,2)G26)dimethyltransferase) | MELVEVLEGKAKILTPKAESIYDAPVFYNPRMALNRDIAVVLLNVLKPRIVLDALSATGIRGIRFALETPAEEIWMNDISEDAYNLMKKNVLLNFKGELEESNGRAVLKSEKTLVVNHDDANRLMAEKHRYFHFIDLDPFGSPMEFLDTALRSVKRKGILGITATDGAPLCGAHPKACMRKYLAVPLRGELCHEVGTRILVGVVARYAAKYDLGIEVILAYYKDHYFRAFIKLKDGARKGDESLENLGYIYFDESTGKFEVERSFLPSKPNAYGPVWLGPLKSQEIVEEMLEISQQLSLARKKQAVKLLKILKDELDVPL... | Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups. {ECO:0000255|HAMAP-Rule:MF_00290}. |
Q9V1P8 | RSMA_PYRAB | Probable ribosomal RNA small subunit methyltransferase A (EC 2.1.1.-) (16S rRNA dimethyladenosine transferase) (16S rRNA dimethylase) (S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase) | MRDRLFFLLSKYGIRPNDRIGQHFLIVKDVIDKAIEVAEVSKSDVVLEVGPGLGFLTDELSKRAKKVFTIELDRRIIEILRNEYSWNNVEIIQGDAVKVEWPSFNKVVSNIPYQISSPFTFKLLKMEFERAVVMYQLEFALRMTAKPGDRNYSRLSLMTQALADVEIVMRIGKGAFYPKPKVDSALVLITPKKDRIELNESLVKALFQHRRKVVSKALRESAHMLGIKDVKTVKDILSSVPHSNKRVFHLTPEEVKEIEEYLREHRIIS | Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. {ECO:0000255|HAMAP-Rule:MF_00607}. |
Q9V1Q1 | AMZA_PYRAB | Archaemetzincin (EC 3.4.-.-) | MMGMIIIVPIGEVPGDVLAFLQNSLSGFYAKYGIEVRLVGGLSLSKFQHAFDFERRQFLARYFLPVLSYIRKDFNAKAALGVVNVDIYELGLNFIFGLAHPGLRVAIISLYRLYPEFYGNPPDRKLLKERALKEAMHELGHVFGLEHCPNPKCVMHFSNSIIDTDIKSWMYCEKCLRKLEKNLTRSYV | Probable zinc metalloprotease whose natural substrate is unknown. {ECO:0000255|HAMAP-Rule:MF_01842}. |
Q9V1Q4 | Y373_PYRAB | Putative ABC transporter ATP-binding protein PYRAB03730 (EC 7.-.-.-) | MNIIEVENVSFKYGNSKAYSLRDVNLNVKKGEFLGIIGPSGSGKSTFCLTLNGLIPHSINGEFEGNVFVDGLNTREHSVAELSTRVGLVFQNPDSQLFNMTVLEEVAFALENLGVEREEMWRRIRWALKLVKLWDKREEFPPNLSGGEKQRLAIASVLVMKPKVLVLDEPTSQLDPLGREEVLSLVRLLNKEEKITIILVEHNTDFLLEHADRIVVFDGGRVVMEGKPEEVFENVEFLERIGIRIPTRVKIGYELKKRGITRRAVLSYEEIIAEIAKQLR | Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity). |
Q9V1R3 | HMDH_PYRAB | 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase) (EC 1.1.1.34) | MNVEDIIEKVANGEIKLHQVEKYVNGDKRLATEIRRKALERKLGISLKHIGHYSIDPNELIGRNIENMIGVVQIPMGVAGPLKINGEYAKGEFYIPLATTEGALVASVNRGCSALTEAGGVVTTILDDKMTRAPLIRCPNARRAREVAEWVKENLNYLQEKAVAKVTRHGKLRDVKPFIVGNNLYLRFEFETGDAMGMNMVTIASEEIMKVIEEEFPDVRYLALSGNLCVDKKPNAVNFILGRGKTVVAEAIVPREIVEKKLKTTPELIAEVNYFKNLVGSAQAGSYGFNAHFGNIVGAIFLATGQDEAQITEGSHGITI... | Converts HMG-CoA to mevalonate. |
Q9V1T5 | RL3_PYRAB | Large ribosomal subunit protein uL3 (50S ribosomal protein L3) | MGKVHRPRRGSLAFSPRKRAKSIVPRIRSWPKETEVRMLGFAGYKAGMTHILMIDDEPGLTNGKEIFMPVTIIETPPLRVFGIRAYRQGYLGLETATEVIVPDFELDNYVSKKAKGRKFTFYQLLKRRIATLPKNYTKDDFEQKLGNLEDMIKEGEIVEVRALVATQPWVIKLKKKPEVMEYAIGGTSVEEKFNYIKEKLGKELRVGEVLKEGELLDVIAVTKGKGTQGPVKRWGIKLRAHKDSKGRRKVGSIGPWHPARVMWTVPMAGQMGFHHRTELNKRLIAIGENGKLVIDGNEIEITPKGGFPHYGIVRSDFMMI... | One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. {ECO:0000255|HAMAP-Rule:MF_01325}. |
Q9V1T6 | RL4_PYRAB | Large ribosomal subunit protein uL4 (50S ribosomal protein L4) | MKVKVFDLNGQPVDEIELPKVFFTPFRPDLIRRAVIASWTHRIQPQGRDPMAGKRRVTENIGKGHGMARVERLKTPPRYAAFVPFARGGRRTHPPKVEKIIWEGINKKERRLAIMSAIAATANYDIVKARGHIIDNVPQLPLIVVDDLQKVSKTRETREIFKKLGIWDDIERAKEKTGIRAGKGKMRGRRYKKAKGPLIVVGKNEGIVFGARNHPGVDVVVVDNLGVEHLAPGTHPGRLTVWTVSAIERLKEIYG | One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. {ECO:0000255|HAMAP-Rule:MF_01328}. Forms part of t... |
Q9V1T7 | RL23_PYRAB | Large ribosomal subunit protein uL23 (50S ribosomal protein L23) | MDPYKVIIRPVITDKAISLIEKENKLTFIVDRRATKQDIKRAIEEIFNVKVEKVNTLITPKGEKKAYVKLKPEYSASEIAARLGLF | Binds to 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. {ECO:0000255|HAMAP-Rule:MF_01369}. |
Q9V1T8 | RL2_PYRAB | Large ribosomal subunit protein uL2 (50S ribosomal protein L2) | MGKSLIQQRRGKGSPTFRSPSHRFRGAVKYIPLNYTQDKTLRGVVEEIMHDPGRTAPVARVRFENGMEKLIIAPEGLLVGQEIYIGPDAPIAIGNTLPLAKIPEGTYVYNIEGIPGDGGKYVRAGGTYALVVSREKDKVIVQLPSGELKAFNPNCRATIGVVAGGGRLEKPLVKAGKAYYKYKARNRFWPTPRGVKMNAVNHPFGGKEHHPGKPTTTSRRAPPGRKVGHIAARRTGRRK | One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. {... |
Q9V1T9 | RS19_PYRAB | Small ribosomal subunit protein uS19 (30S ribosomal protein S19) | MARKEFRYRGYTLEQLMNMSLEELAKLLPARQRRSLKRGLTPEQKKLLRKIRLAKKGKYNKPIRTHCRDMIVLPEMVGLTIYVHNGKEFVPVEIKPEMIGHYLGEFAPTRKRVQHGAPGIGATRSSMFVAVK | Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. |
Q9V1U0 | RL22_PYRAB | Large ribosomal subunit protein uL22 (50S ribosomal protein L22) | MGRRFDYSFQNFDPERMARASGRDLRISPKLAVEVCRELRGMMLNDALRYLDDVIALRRPVPLKRYNDSQGHKPGKGFGPGRYPVKVAKAIKKVLLNAQNNAKQKGLDPDKLRIIHIAAHRGPVLRGWYPRAFGRPTPFNEQTTHIEVVVEEVRR | This protein binds specifically to 23S rRNA. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. {ECO:0000255|HAMAP-Rule:MF_01331}. The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended bet... |
Q9V1U1 | RS3_PYRAB | Small ribosomal subunit protein uS3 (30S ribosomal protein S3) | MAIERYFIREAVKEMLIDEFLEKELRRAGYGGLDIKKTPLGTKVIIFAANPGYVIGRGGRRIRELTRILERQFGLENPQIDVQEIKNPYLNAKVQAVRIAQALERGIHFRRAAYAAMRAIMSNGARGVEIRISGKLTGERAKSVRFYQGYLAKVGNPAETLVSKGYAQALLKLGVIGVKVAIMPPDARLPDEIEIIEKPVEEEVSSNEAE | Binds the lower part of the 30S subunit head. {ECO:0000255|HAMAP-Rule:MF_01309}. |
Q9V1U4 | RNP1_PYRAB | Ribonuclease P protein component 1 (RNase P component 1) (EC 3.1.26.5) (Rpp29) | MRRNGKERKDRTSGGSQRPYQEIVGRTWIFRGSHRGRVTKRNIIWHELIGLKVRVVNSMHPGFVGIEGYVVDETRNMLVIVGDKVWKVPKDVCIFEFETEDGAKIKIPGERLVGRPEMRLKKRWRKW | Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. {ECO:0000255|HAMAP-Rule:MF_00754}. |
Q9V1U5 | RS17_PYRAB | Small ribosomal subunit protein uS17 (30S ribosomal protein S17) | MVRDIGLRIQPPAEKCDDPKCPWHGHLKIHGRVFEGIVVSDKPRKTVTVERQYYHYLKKYERYELRRSRIHAHNPPCINAKVGDRVLIAETRPLSKTKHFVVVAVLERAEERR | One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. {ECO:0000255|HAMAP-Rule:MF_01345}. |
Q9V1U6 | RL14_PYRAB | Large ribosomal subunit protein uL14 (50S ribosomal protein L14) | MAKKGAGATRGITPVRPTRAIPVGAYLTVADNSGAKVIQVIGVVEYHGTRRRLASAGVGDMVVATVKKGRPDMRHQVVRAVIIRQRKEYRRLDGMRIKFEDNAAVIVTPEGVPRGTEIRGPVAREAAERWVRIGSIASIIV | Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01367}. |
Q9V1U7 | RL24_PYRAB | Large ribosomal subunit protein uL24 (50S ribosomal protein L24) | MRLNSKQPRKQRKFLYNAPLHLRQKMMAAPLSKELREKYKIRNLPVRVGDKVRIMRGDFKGHEGKVVEVDLKRYRIYVEGATLRKTNGTEVFYPIHPSNVMIIELNLDDERRKKIIERRAG | One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. {ECO:0000255|HAMAP-Rule:MF_01326}. Located at the polypeptide exit tunnel on the outside of the subunit. {ECO:0000255|HAMAP-Rule:MF_01326}. |
Q9V1U9 | RL5_PYRAB | Large ribosomal subunit protein uL5 (50S ribosomal protein L5) | MAITIPNREEILADWEAHPMRKPRIEKVTINIGVGESGERLTKAEIMLERLTGQKPIRRKAKKTNRDFGIRRGEPIAVKVTLRGPKAYEMLKRLLAAVDNRLKASSFDEHGNVCFGIDEHINIPGVEYDPEIGIFGMDVCVTLERPGFRVARRKRKRAKIPTRHKLTKEEGMVYMMEEFGVEIVEEEG | This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits this bridge is implicated in subunit movement.... |
Q9V1V0 | RS8_PYRAB | Small ribosomal subunit protein uS8 (30S ribosomal protein S8) | MTLLDPLANALSHITNSERVGKREVYIKPASKLIGEVLRVMQKYGYIGEFEFIDDGRAGVYRVQLLGKINKAGAIKPRFPVKARDYERWEKRFLPAFEFGILIVSTSQGVMSHKEAREKGIGGRLIAYVY | One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. {ECO:0000255|HAMAP-Rule:MF_01302}. |
Q9V1V1 | RL6_PYRAB | Large ribosomal subunit protein uL6 (50S ribosomal protein L6) | MPVDAWVREEIEIPEGVEVSVQGNTVKVKGPKGEVERELFWPGVKIFVEGGKVVIYKDFPRRKDVAIVRTFKAHINNMIKGVTEGFTYKLKVVYSHFPITVKVQGDEVIIENFLGEKAPRRAKILPGVTVKVKGQEIIVEGIDKEAVGQTAANIEQATRITKWDRRVFQDGIYIVEKAGKPITF | This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. {ECO:0000255|HAMAP-Rule:MF_01365}. |
Q9V1V3 | RL19E_PYRAB | Large ribosomal subunit protein eL19 (50S ribosomal protein L19e) | MKTLKMQRRVAAELLKCGENRIWIDPERVDDVASAITREDIRRLIKEGVIKKKPVKGQSRYRARIRHEQKKKGRHRGPGSRKGKKTARMGKKELWIKTIRALRKELRKLKEQKKIDRRTYRMLYIRAKGGQFKSKHQLYMFLEEHNLLKKR | Binds to the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01475}. |
Q9V1V4 | RL18_PYRAB | Large ribosomal subunit protein uL18 (50S ribosomal protein L18) | MAHGPRYRVPFRRRREGKTNYRKRLKLLKSGKPRLVVRKSLNHHIAQIIVYDPKGDRTLVSAHTRELIRDFGWKGHCGNTPSAYLLGLLIGYKAKKAGIEEAILDIGLHPPVRGSSVFAVLKGAVDAGLNVPHSPEIFPEDYRIRGEHIAEYARMLKEQDEEKFRRQFGGYLEKGLDPEKLPEHFDEVKARIIEKFESEGARE | This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. {ECO:0000255|HAMAP-Rule:MF_01337}. |
Q9V1V5 | RS5_PYRAB | Small ribosomal subunit protein uS5 (30S ribosomal protein S5) | MSQEWKEYAKRVLDEWQPKTKLGMLVKEGQITDIHEIFRKGYQIKEPEIIDVLLPEVNARENQEILDIALTVRMTDSGRRVRFRVLAAVGNRDGYVGLGIGHGREVGIAIRKAINYAKLNIIEIKRGCGSWECRCRRPHSVPFTVEGKEGSVRVKLIPGPRGLGLVIGDVGKKILRLAGIQDVWSQTLGETRTTVNFAKAVFNALYNTNKVVVTPEMIERYGIVVGRAMPASFTLE | With S4 and S12 plays an important role in translational accuracy. {ECO:0000255|HAMAP-Rule:MF_01307}. |
Q9V1V7 | RL15_PYRAB | Large ribosomal subunit protein uL15 (50S ribosomal protein L15) | MIRRRKKVRKLRGSHTHGWGCKKKHRGGGSKGGRGMAGTGKRNKSKWTWTIKYAPDHLGKRGFSRPPEVQREVRTVTLKSIDENLDELLQKGIAYEEEGKIIVDTTQFADKVLGTGKITKPLVIKARAFSSKAEEKIKAAGGEAVLV | Binds to the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01341}. |
Q9V1V8 | SECY_PYRAB | Protein translocase subunit SecY (Protein transport protein SEC61 subunit alpha homolog) | MGARDIIYAIEKWFPEVERPKKHVPLKEKFMWTGLALILYYVLAEIPVYGIPERIQDYFQFLRVVLAGRNGSILTLGIGPIVTAGIILQLLVGSEIIKLDLANPEDRRFYQALQRVFSVFMCFLEAAIWVLGGAFGRVGVDVTYAIAALMILQLAFGGIILIVLDELVSKWGIGSGISLFIAAGVSQRILTRSLNPLTDPNIIDPLTGKPAIVGAIPYFIQHILKGDLKGALYRGGTAPDMMAVIATIIVFLVVVYFESMRVEIPLGYRGVTIRGRYPIRFLYVSNIPIILTFALYANIQLWARVLDRLGHPWLGTFDPT... | The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydr... |
Q9V1Y5 | TYW32_PYRAB | tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-demethylwyosine(37)-N(4))-methyltransferase 2 (EC 2.1.1.282) (tRNA wyosine derivatives biosynthesis protein Taw3 2) | MKAKREALISLFTAIKEGKVDEDIIDLLMLINSIKGVYTTSSCSGRIGIIEEPSLGAKPLSRWLIKVHRPMEFEEAIDALKKANKGIIFLKSQPPILHVVAENLEMAKLLHQIGLSSGFKYTTFKVISNRYLVEINGTEYLTVPLGRDGKVLVSEEYLKFAVEIGNEMLRRGKSRLPRLYKNFQELKEKVGEDELFIALKREILGT | S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wyosine derivatives biosynthesis pathway. Probably methylates N-4 position of wybutosine-86 to produce wybutosine-72. {ECO:0000255|HAMAP-Rule:MF_00266}. |
Q9V1Z8 | EF2_PYRAB | Elongation factor 2 (EF-2) | MGRREEMIAKIKELMLQPERIRNIGIAAHIDHGKTTLSDNLLAGAGMISEELAGKQLVLDFDEQEQARGITINAANVSMVHNYEGKDYLINLIDTPGHVDFGGDVTRAMRAIDGVIIVVDAVEGVMPQTETVVRQALREYVKPVLFINKVDRLIRELKLTPQQMMERFSKIIMDVNRLIQRYAPEEYKKQWMVKVEDGSVAFGSAYYNWALSVPFMKRTGVKFNEIIDLTLKGDHKTLRQKAPLHVVVLDMVVKHLPNPIEAQKYRIPHLWQGDINSDVGQAMLNCDPKGKMVMVVTKIIIDKHAGEVATGRVWSGTVKS... | Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respective... |
Q9V225 | Y249_PYRAB | Putative GTPase PYRAB02490 (EC 3.6.-.-) | MIDELIERMKKGDRRATARLITLVENDEEKAREIIRKIYPLTGNAYIVGITGPPGAGKSTLLDKLIKEARKEGLIVGVIAIDPTSPFTGGALLGDRIRMQRHSTDPGVFIRSMATRGSLGGLAKATNDAIKVLDAYGCDVIFVETVGVGQVEVDIVKTADTVVLVTVPGLGDDVQTIKAGLMEIADIFVINKADKEGADATYFELNLALDLESDKWRELGWRPPVVETVATMNKGIKELWDKIKEHREFLERSGRLKEKRRKRIEEEIKTIVSGIIAGKVEASIKRGEFEEIIRRVSQKDIDPYSAADMILKEIIGGGLS... | May have GTPase activity. May also bind and hydrolyze ATP. May function as chaperone (By similarity). |
Q9V233 | RADA_PYRAB | DNA repair and recombination protein RadA | MGKKSSDPAVVEINDVDELELEVGEEVTSKKKKKEKEIRTIEDLPGVGPATAEKLREAGFDTLEAIAVASPIELKEVAGISEGAALKIIQAARKAANLGTFMRADEYLKKRESIGRISTGSKSLDKLLGGGIETQAITEVFGEFGSGKTQLAHTLAVMVQLPPEEGGLNGSVIWIDTENTFRPERIREIAKNRGLDPDEVLKHIYVARAFNSNHQMLLVQQAEDKIKELLNTDKPVKLLIVDSLTSHFRSEYIGRGALAERQQKLAKHLADLHRLANLYEIAVFVTNQVQARPDAFFGDPTRPIGGHILAHSATLRVYLR... | Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules (By similarity). |
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