accession stringlengths 6 10 | name stringlengths 6 11 | Full Name stringlengths 1 147 ⌀ | taxon stringlengths 3 46 ⌀ | sequence stringlengths 16 2.75k | function stringlengths 6 5.51k | AlphaFoldDB stringlengths 6 10 |
|---|---|---|---|---|---|---|
Q043R6 | TRMFO_LACGA | Folate-dependent tRNA(M-5-U54)-methyltransferase | Lactobacillus | MVKNVTVIGGGLAGSEAAWQLAKRGIEVELYEMRPKKTTPAHETANFAELVCTNSMRSNQLSNAVGLLKEEMRQLDSLIMKAADETAVPAGGALAVDRDKFSSVVTQTLKDLPNVHVHEEEITKIPKDGITIIATGPLTSDTLAEQIKDFCGTDSLHFFDAAAPIVAASSIDRDIVYKKSRYDKGEAAYLNCPMTKEEFFNFYKNLVSAETATLHGFEDKNVFEGCMPIEVMAKRGEKTMLFGPLKPVGLEDPKTGKTPYAVVQLRQDNAASTMYNIVGFQTHLKYGEQKRVFSMIPGLENAKFVRYGKMHRNTYIASPEVLNANYEARKQAGLFFAGQMTGVEGYVESAGSGLIAGINAARETVGEETLVFPKSTALGSMAHYITTTSAKHFQPMNASYALLPKLDYKVRNKQERHLEISKRALKDLETFKEEKKLD | Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs. | Q043R6 |
A9N0K6 | THIC_SALPB | Thiamine biosynthesis protein ThiC | Salmonella | MSTTTLTRREQRAKAQHFIDTLEGTAFPNSKRIYVTGSQHDIRVPMREIQLSPTLIGGSKDNPQFEENEAVPVYDTSGPYGDPEVAINVQQGLAKLRQPWIDARNDSEELDDRSSAYTRERLADDGLDDLRFTGLLTPKRAKAGKRVTQLHYARQGIVTPEMEFIAIRENMGRERIRSEVLRHQHPGMNFGARLPENITPEFVRDEVAAGRAIIPANINHPESEPMIIGRNFLVKVNANIGNSAVTSSIEEEVEKLVWSTRWGADTVMDLSTGRYIHETREWILRNSPVPIGTVPIYQALEKVNGIAEDLTWEAFRDTLLEQAEQGVDYFTIHAGVLLRYVPMTAKRLTGIVSRGGSIMAKWCLSHHKENFLFEHFREICEICAAYDVSLSLGDGLRPGSIQDANDEAQFSELHTLGELTKIAWEYDVQVMIEGPGHVPMHMIQRNMTEELESCHEAPFYTLGPLTTDIAPGYDHFTSGIGAAMIGWFGCAMLCYVTPKEHLGLPNKEDVKQGLITYKIAAHAADLAKGHPGAQIRDNAMSKARFEFRWEDQFNLALDPFTARAYHDETLPQESGKVAHFCSMCGPKFCSMKISQEVRDYAAAQAIEVGMADMSENFRAKGGEIYLKREEA | Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. | A9N0K6 |
Q0P5I6 | PR38A_BOVIN | Pre-mRNA-splicing factor 38A | Bos | MANRTVKDAHSIHGTNPQYLVEKIIRTRIYESKYWKEECFGLTAELVVDKAMELRFVGGVYGGNIKPTPFLCLTLKMLQIQPEKDIIVEFIKNEDFKYVRMLGALYMRLTGTAIDCYKYLEPLYNDYRKIKSQNRNGEFELMHVDEFIDELLHSERVCDIILPRLQKRYVLEEAEQLEPRVSALEEDMDDVESSEEEEEEDEKLERVPSPDHRRRSYRDLDKPRRSPTLRYRRSRSRSPRRRSRSPKRRSPSPRRERHRSKSPRRHRSRSRDRRHRSRSKSPGHHRSHRHRSHSKSPERSKKSHKKSRRGNE | Involved in pre-mRNA splicing as a component of the spliceosome. | Q0P5I6 |
B8H729 | PAND_PSECP | Aspartate 1-decarboxylase alpha chain | Pseudarthrobacter | MNRTMFKSKIHRATVTHADLHYVGSVTVDLDLLEAADILPGELVSIVDITNGARLETYTIAGERGSGVIGINGAAAHLMHENDLVILITYAQMTTEEAKAYEPKVVHVDQDNRIIQLGNDPAEGIAPGMTRPPFALNNAAL | Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. | B8H729 |
Q66KB7 | UEVLD_XENTR | EV and lactate/malate dehydrogenase domain-containing protein | Silurana | MEFSAETLRQQLGKYKFRDLTIEELKDLNRTFPSFIFSMETYTFRDGSQKDLLNLTGTVPMKHQGTTYNIPICLWILDSHPFAPPLCFLKPSGNMGIRVGRHIDAQGRIYLPYLQNWSHPKSTVTGLIREMAVKFEEELPLYSLSAEDGARQRELLSYIAQVTDGVSSMDVKAPSRAKVTVIGGGDMALACLLAVSAKGTAGKLLLLDPTDGEAAGGAAADLEIFSLPNVQVTKDFSAIAGSAIVIVTVNSWSNSQSYVGVLQSNVELLRGILPAVAHHCPKCLLLVASQPVEIMTYATWKLSGFPHNRVLGIGCNLDSGRFRHVIEKLADSEEGAQGAWIIGEQSDNKVAVWGAPDSSANRQTPCKLYPKIFQEQLTSRALEILKGKGQRSWSVGLSVADITDTLVQNKGKVHSVSALCKGQFGVQEEVFLSIPCVLGSAGVTGAVQTLQDEAQIWETLQRSAAAIESVQQQLRL | Possible negative regulator of polyubiquitination. | Q66KB7 |
O88588 | PACS1_RAT | Phosphofurin acidic cluster sorting protein 1 | Rattus | MAERGGAGGGPGGAGGGSSQRGSGVAQSPQQQPPQQPSQPQQPTPPKLAQATSSSSSTSAAAASSSSSSTSTSMAVAVASGSAPPGGPGPGRTPAPVQMNLYATWEVDRSSSSCVPRLFSLTLKKLVMLKEMDKDLNSVVIAVKLQGSKRILRSNEIILPASGLVETELQLTFSLQYPHFLKRDANKLQIMLQRRKRYKNRTILGYKTLAVGLINMAEVMQHPNEGALVLGLHSNVKDVSVPVAEIKIYSLSSQPIDHEGIKSKLSDRSPDIDNYSEEEEESFSSEQEGSDDPLHGQDLFYEDEDLRKVKKTRRKLTSTSAITRQPNIKQKFVALLKRFKVSDEVGFGLEHVSREQIREVEEDLDELYDSLEMYNPSDSGPEMEETESILSTPKPKLKPFFEGMSQSSSQTEIGSLNSKGSLGKDTTSPMELAALEKVKSTWIKNQDDSLTETDTLEITDQDMFGDASTSLVVPEKVKTPMKSSKADLQGSASPSKVEGTHTPRQKRSTPLKERQLSKPLSERTNSSDSERSPDLGHSTQIPRKVVYDQLNQILVSDAALPENVILVNTTDWQGQYVAELLQDQRKPVVCTCSTVEVQAVLSALLTRIQRYCNCNSSMPRPVKVAAVGSQSYLSSILRFFVKSLASKTPDWLGHMRFLIVPLGSHPVAKYLGSVDSRYSSTFLDSAWRDLFSRSEPPVSEPLDVVGRVMQYVNGATTTHQLPVAEAMLTCRHKFPDEDSYQKFIPFIGVVKVGLVEDSPSTAGDGDDSPVVSLTVPSTSPPSSSGLSRDATATPPSSPSMSSALAIVGSPNSPYGDVIGLQVDYWLGHPGERRREGDKRDASSKNTLKSVFRSVQVSRLPHAGEAQLSGTMAMTVVTKEKNKKVPTIFLSKKPREKEVDSKSQVIEGISRLICSAKQQQTMLRVSIDGVEWSDIKFFQLAAQWPTHVKHFPVGLFSGSKPT | Coat protein that is involved in the localization of trans-Golgi network (TGN) membrane proteins that contain acidic cluster sorting motifs. Controls the endosome-to-Golgi trafficking of furin and mannose-6-phosphate receptor by connecting the acidic-cluster-containing cytoplasmic domain of these molecules with the adapter-protein complex-1 (AP-1) of endosomal clathrin-coated membrane pits. | O88588 |
B4S9J3 | HYPA_PROA2 | Hydrogenase maturation factor HypA | Prosthecochloris | MHEMSIALSVVDAITARAREEQAEKVTAIELVAGKLSGVEIESLKFCFSAAVRGTIMEDAELMVTVPLSEGLCEVCGERFAVDGYYTQCPSCGSYKVRIVSGKELSIRSITLE | Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. | B4S9J3 |
A7H7I2 | GLMU_ANADF | Glucosamine-1-phosphate N-acetyltransferase | unclassified Anaeromyxobacter | MSHSPTPLAAIVLAAGKGTRMKSQKAKVLHEVGGRPLAWFPTRRALEIGANPVVAVVGHQAEAVEAALAATLPGAPLRFAVQREQLGTAHAVLSAREALGRYQGAVLILSGDTPLLRAETLSRVVAARAGATLSLATMRLADPHGYGRIVRDPAGTPARVVEEKDATDAERALDEVNAGLYCADAAFLWEALSKVGSANAQREFYLTDLVAMAARAGGVVAVPVPPEEASGVNDREELARAGRVLLRRRASELMRSGVTIEDPERFDCDEGVEIGADAVIEPNVRLKGRTRIGAGCRLGAGAILTDAVLADGVTVKPYTVIEEATVAARAILGPFSRLRPGSDIGEEAHVGNFVETKKARLGKGAKANHLTYLGDATIGAGANVGAGTITCNYDGEKKHPTTIGEGAFIGSDSILVAPIEIGAGAYVAAGSTLTESVPPGALALGRAKQVTKEGWVARRKAEAQNKGAAEAAPAPSPADSPRGGRAS | Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. | A7H7I2 |
Q61080 | FOXF1_MOUSE | Hepatocyte nuclear factor 3 forkhead homolog 8 | Mus | MSAPDKQQPPHGGGTGGGGGAGGQAMDPAAAGPTKAKKTNAGVRRPEKPPYSYIALIVMAIQSSPSKRLTLSEIYQFLQARFPFFRGAYQGWKNSVRHNLSLNECFIKLPKGLGRPGKGHYWTIDPASEFMFEEGSFRRRPRGFRRKCQALKPVYSMVNGLGFNHLPDTYGFQGSGGLSCAPNSLALEGGLGMMNGHLAGNVDGMALPSHSVPHLPSNGGHSYMGGCGGSAAGEYPHHDSSVPASPLLPAGAGGVMEPHAVYSSSAAAWPPAASAALNSGASYIKQQPLSPCNPAANPLSGSISTHSLEQPYLHQNSHNGPAELQGIPRYHSQSPSMCDRKEFVFSFNAMASSSMHTTGGGSYYHQQVTYQDIKPCVM | Probable transcription activator for a number of lung-specific genes. | Q61080 |
P82874 | TO203_ARATH | Translocase of outer membrane 20 kDa subunit 3 | Arabidopsis | MDTETEFDRILLFEQIRQDAENTYKSNPLDADNLTRWGGVLLELSQFHSISDAKQMIQEAITKFEEALLIDPKKDEAVWCIGNAYTSFAFLTPDETEAKHNFDLATQFFQQAVDEQPDNTHYLKSLEMTAKAPQLHAEAYKQGLGSQPMGRVEAPAPPSSKAVKNKKSSDAKYDAMGWVILAIGVVAWISFAKANVPVSPPR | Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the translocation pore. | P82874 |
Q4PEF9 | H2A_USTMA | Histone H2A | Ustilago | MSSGGKSGGKAGDASSKAQSRSAKAGLQFPVGRIHRLLRKGNYAQRVGAGAPVYLAAVLEYLAAEILELAGNAARDNKKSRIIPRHLQLAIRNDEELNKLLGGVTISQGGVLPFIQSELLPAKSGKPKKAGGSQDI | Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | Q4PEF9 |
Q6MQU0 | TRMB_BDEBA | tRNA(m7G46)-methyltransferase | Bdellovibrio | MALNGEYAHVAFDELRAPLNKGKWRSDVFKADAAMPLDVEVGTGNGTYFAHHAKTHSDRLLVGLELKYKPLIQSIRRAVNAGCKNAAITRFHAFNIDHLFAEGEIDNVYIHFPDPWTSPKKPKNRFVCKENLELLFRLQKPGSFINFKTDSLVYFLWAMDEIRQSPYKIIFETQDLHNSDMKDQNFETAFEKIFLREGIKINFVRLQKI | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | Q6MQU0 |
P73788 | PSTB3_SYNY3 | Phosphate-transporting ATPase 3 | unclassified Synechocystis | MTNLSGSMPSSTAADLQPALRVEGLGFYYGTKKVLEGVTMAIPVGKVTAMIGPSGCGKSTLLKAFNRIAELEGRVKVTGKIEFFGQNIYDQKVNINSLRREIGMVFQRPNPFPTSIYDNIVYGVKLCCNVSRAELDEIVERSLTRAVLWDEVKDSLKKSALGLSGGQQQRLCIARALAVNPKVLLMDEPCSALDPISTLKIEELINSLRENVTITIVTHNMQQALRVSDYTAFFNTDESRIGQLVEFDTTQNIFSSPQETQTRDYVAGRFG | Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system. | P73788 |
P02128 | HBE_CHICK | Hemoglobin epsilon chain | Gallus | MVHWSAEEKQLITSVWSKVNVEECGAEALARLLIVYPWTQRFFASFGNLSSPTAIMGNPRVRAHGKKVLSSFGEAVKNLDNIKNTYAKLSELHCDKLHVDPENFRLLGDILIIVLASHFARDFTPACQFAWQKLVNVVAHALARKYH | Beta-type chain found in early embryos. | P02128 |
Q329T0 | MNMG_SHIDS | Glucose-inhibited division protein A | Shigella | MFYPDPFDVIIIGGGHAGTEAAMAAARMGQQTLLLTHNIDTLGQMSCNPAIGGIGKGHLVKEVDALGGLMAKAIDQAGIQFRILNASKGPAVRATRAQADRVLYRQAVRTALENQPNLMIFQQAVEDLIVENDRVVGAVTQMGLKFRAKAVVLTVGTFLDGKIHIGLDNYSGGRAGDPPSIPLSRRLRELPLRVGRLKTGTPPRIDARTIDFSVLAQQHGDNPMPVFSFMGNASQHPQQVPCYITHTNEKTHDVIRSNLDRSPMYAGVIEGVGPRYCPSIEDKVMRFADRNQHQIFLEPEGLTSNEIYPNGISTSLPFDVQMQIVRSMQGMENAKIVRPGYAIEYDFFDPRDLKPTLESKFLQGLFFAGQINGTTGYEEAAAQGLLAGLNAARLSADKEGWAPARSQAYLGVLVDDLCTLGTKEPYRMFTSRAEYRLMLREDNADLRLTEIGRELGLVDDERWARFNEKLENIERERQRLKSTRVTPSAEAAAEVNAHLTAPLSREASGEDLLRRPEMTYEKLTTLTPFAPALTDEQAAEQVEIQVKYEGYIARQQDEIEKQLRNENTLLPATLDYRQVSGLSNEVIAKLNDHKPASIGQASRISGVTPAAISILLVWLKKQGMLRRSA | NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. | Q329T0 |
O34817 | NAGR_BACSU | N-acetylglucosamine utilization regulator | Bacillus | MNINKQSPIPIYYQIMEQLKTQIKNGELQPDMPLPSEREYAEQFGISRMTVRQALSNLVNEGLLYRLKGRGTFVSKPKMEQALQGLTSFTEDMKSRGMTPGSRLIDYQLIDSTEELAAILGCGHPSSIHKITRVRLANDIPMAIESSHIPFELAGELNESHFQSSIYDHIERYNSIPISRAKQELEPSAATTEEANILGIQKGAPVLLIKRTTYLQNGTAFEHAKSVYRGDRYTFVHYMDRLS | Main transcriptional repressor of genes involved in N-acetylglucosamine (GlcNAc) transport and utilization . Represses the expression of the nagAB and nagP operons by binding directly within their upstream regions . Binds to the DNA consensus sequence 5'-ATTGGTATAGACAACT-3' . Also acts as a weak repressor of mapB expression . | O34817 |
Q0MQ95 | NDUA3_GORGO | NADH-ubiquinone oxidoreductase B9 subunit | Gorilla | MAARVGAFLKNAWDKEPVLVVSFVVGGLAVILPPLSPYFKYSVMINKATPYNYPVPVRDDGNMPDVPSHPQDPQGPSLEWLKKL | Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. | Q0MQ95 |
Q8G8B6 | CARAA_PSERE | Carbazole 1,9a-dioxygenase, terminal oxygenase component CarAa | Pseudomonas | MANVDEAILKRVKGWAPYVDAKLGFRNHWYPVMFSKEIDEGEPKTLKLLGENLLVNRIDGKLYCLKDRCLHRGVQLSVKVECKTKSTITCWYHAWTYRWEDGVLCDILTNPTSAQIGRQKLKTYPVQEAKGCVFIYLGDGDPPPLARDTPPNFLDDDMEILGKNQIIKSNWRLAVENGFDPSHIYIHKDSILVKDNDLALPLGFAPGGDRKQQTRVVDDDVVGRKGVYDLIGEHGVPVFEGTIGGEVVREGAYGEKIVANDISIWLPGVLKVNPFPNPDMMQFEWYVPIDENTHYYFQTLGKPCANDEERKNYEQEFESKWKPMALEGFNNDDIWAREAMVDFYADDKGWVNEILFEVDEAIVAWRKLASEHNQGIQTQAHVSG | Part of the multicomponent carbazole 1,9a-dioxygenase (CARDO), that converts carbazole (CAR) into 2-aminobiphenyl-2,3-diol. Catalyzes the dioxygenation at the angular (C-9a) and adjacent (C-1) positions of carbazole to yield a highly unstable cis-hydrodiol intermediate which is spontaneously converted to 2-aminobiphenyl-2,3-diol. It is also able to attack the angular position adjacent of hetero atom of heterocyclic aromatic compounds such as polychlorinated dibenzo-p-dioxin (DD) and dibenzofuran (DBF). It was also shown that CARDO has the ability to metabolize biphenyl and polycyclic aromatic hydrocarbons, such as naphthalene and phenanthrene. | Q8G8B6 |
A0R2E6 | GPGS_MYCS2 | Glucosyl-3-phosphoglycerate synthase | Mycolicibacterium | MGHRWLTDHSWNRPSWTVADLEAAKAGRTVSVVLPALNEEETVGSVVETIKPLLGGLVDELIVLDSGSTDETEIRAVAAGAKVVSREAALPEVPPQPGKGEVLWRSLAATTGDIIAFVDSDLIDPDPMFVPKLLGPLLTCDGVHLVKGFYRRPLKVSGAEDANGGGRVTELVARPLLASLRPELNCVLQPLGGEYAGTRELLTSVPFAPGYGVEIGLLVDTYDRLGLDGIAQVNLGVRAHRNRPLTELASMSRQVIATLLSRCGISDSGVGLTQFFADGDDFTPRVSSVSLADRPPMTTLRPR | Involved in the biosynthesis of 6-O-methylglucose lipopolysaccarides (MGLPs) . Catalyzes the transfer of the glucose moiety from a nuleotide sugar such as UDP-alpha-D-glucose to the position 2 of 3-phospho-D-glycerate (3-PGA) to form glucosyl-3-phosphoglycerate (GPG). It can use UDP-glucose, ADP-glucose and GDP-glucose as sugar donor substrates with decreasing affinity and with 3-PGA as an acceptor. D-glycerate can only be an acceptor with ADP-glucose and at a very low rate . | A0R2E6 |
Q185S7 | PYRH_CLOD6 | Uridine monophosphate kinase | Clostridioides | MDKPMYKRVLLKLSGEALAGERGFGINNDVVNDIAIAIKKIQEIGVEVAVVVGGGNFWRGRTSEGMDRTTADYIGMLATVMNAMALQDALENIDVATRVQTAIDMRQIAEPYIRRRAVRHLEKERVVIFGAGTGNPYFTTDTTAALRAAEMEAEVILLAKNVDAVYDKDPKVHADAKKFTELSYMEVIQKELKVMDSTATSLCMDNKIPIKVFELTTENIIRAVKGENIGTTVK | Catalyzes the reversible phosphorylation of UMP to UDP. | Q185S7 |
Q9FLB5 | LAC12_ARATH | Urishiol oxidase 12 | Arabidopsis | MTTVHTFSILLFFCSLFSASLIIAKVQHHDFVIQETPVKRLCKTRNAITVNGMFPGPTLEVNNGDTLEVKVHNRARYNITIHWHGVRQIRTGWADGPEFVTQCPIRPGKSYTYRFTIQGQEGTLWWHAHSSWLRATVYGALIIHPTPGSSFPFPKPDRQTALMLGEWWNANPVDVINQATRTGAAPNISDAYTINGQPGDLYNCSTKETVVVPINSGETSLLRVINAALNQPLFFTVANHKLTVVGADASYLKPFTTKVLMLGPGQTTDVLLTADQPPKRYYIAARAYQSAQNAPFDNTTTTAILQYKKTTTTSKPIMPVLPAFNDTNTVTSFSRKFKSLRNVVVPKTIDDNLFFTIGLGLDNCPKKFPKSRCQGLNGTRFTASMNNVSFVLPSNFSLLQAHSNGIPGVFTTDFPSKPPVKFDYTGNNISRALFQPVKGTKLYKLKYGSRVQVVLQDTNIVTSENHPIHLHGYDFYIVGEGFGNFNPKKDTSKFNLVDPPLRNTVAVPVNGWAVIRFVADNPGVWLMHCHLDVHIKWGLAMAFLVDNGVGELETLEAPPHDLPIC | Lignin degradation and detoxification of lignin-derived products. | Q9FLB5 |
Q7MA42 | NUOI_WOLSU | NDH-1 subunit I | Wolinella | MDLKQKYIFIEGTNCPVTVRGRLLQVFRRSVSGELFKGLWLVLREMLRFNIHTTQYPKEKLPLSPRYRAIHELLRLLESGNERCIGCGLCEKICISNCIRMETSYGEDGRKKVHEYTINFGRCIFCGFCAEVCPELAIVHGGRYENASEQRAHFGLKEDMLTPMERFMNQGQKEFPGFGALSQDADSKVKKTPLAYFTPKGEENV | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. | Q7MA42 |
Q4I5Z5 | CGR1_GIBZE | rRNA-processing protein CGR1 | Fusarium | MSDTENTNLTPAPAAEKTLGMRKNGKQWHAPKKAFRPTSGLKSYEKRSQERAIMIQVKAKEKEMKEEKEEERQRKVQAIKEKRAKKEEKERYEKMAEKMHKKRVERLKRKEKRNKLINS | Involved in nucleolar integrity and required for processing of the pre-rRNA for the 60S ribosome subunit. | Q4I5Z5 |
P0DSN9 | SAA4_PIG | Serum amyloid A-4 protein | Sus | MKLFIGLIFCSLVMGVSSDGWFSFFKEAVQGASDLWRAYWDMKEANYQNSGRYFRARGNYEAAQRGPGGIWAAKIISNVGEYFQGLLQYLGSSSEREEDQVSNRRAEEWGRSGQDPDHFRPAGLPKKY | Major acute phase reactant. | P0DSN9 |
Q8N531 | FBXL6_HUMAN | FBL6A | Homo | MAAPASRQVRRRARAAPRPRSAEDWWWDRLAPRGSGYHLLQSDSMLLVLSEPGPARPRAQRRASRRTPRQPPRGPSAAAKPKAGLRSEAAAAPAPAPAPTPTPEEGPDAGWGDRIPLEILVQIFGLLVAADGPMPFLGRAARVCRRWQEAASQPALWHTVTLSSPLVGRPAKGGVKAEKKLLASLEWLMPNRFSQLQRLTLIHWKSQVHPVLKLVGECCPRLTFLKLSGCHGVTADALVMLAKACCQLHSLDLQHSMVESTAVVSFLEEAGSRMRKLWLTYSSQTTAILGALLGSCCPQLQVLEVSTGINRNSIPLQLPVEALQKGCPQLQVLRLLNLMWLPKPPGRGVAPGPGFPSLEELCLASSTCNFVSNEVLGRLLHGSPNLRLLDLRGCARITPAGLQDLPCRELEQLHLGLYGTSDRLTLAKEGSPFLTQKWCHTLRELDLSGQGFSEKDLEQALAAFLSTPGGSHPALCSLNLRGTRVTPSTVSSVISGCPGLLYLNLESCRCLPRGLKRAYRGLEEVQWCLEQLLTSPSPS | Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. | Q8N531 |
A1KVH5 | ACPS_NEIMF | 4'-phosphopantetheinyl transferase AcpS | Neisseria | MIYGIGTDIVSLKRIIRLNKKFGQAFAGRILTPEELLEFPQAGKPVNYLAKRFAAKEAFAKAVGTGIRGAVSFRNIGIGHDALGKPEFFYGPALSKWLEEQGISRVSLSMSDEEDTVLAFVVAEK | Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein. | A1KVH5 |
Q9XP73 | CYB_SMIYO | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Sminthopsis | MINLRKTHPLMKIINHSFIDLPAPSNISAWWNFGSLLGICLVIQILTGLFLAMHYTSDTLTAFSSVAHICRDVNYGWLIRNLHANGASMFFMCLFLHVGRGIYYGSYLYKETWNIGVMLLLTVTATAFVGYVLPWGQMSFWGATVTTNLFSAIPYIGQTLVEWAWGGFSVDKATLTRFFALHFLLPFVIAGLTLVHLTFLHETGSNNPLGIPSDCDKIPFHPYYSIKDILGLMFLLLVLLSLALFSPDLLGDPDNFSPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALLASILILLVIPFLHTANQRSMMFRPISQTLFWILTANLITLTWIGGQPVEQPFIIIGQPASILYFPLIHHPMPSAGLFENYMPKPKW | Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis. | Q9XP73 |
Q9D3H2 | OBP1A_MOUSE | Odorant-binding protein IA | Mus | MAKFLLLALTFGLAHAAMEGPWKTVAIAADRVDKIERGGELRIYCRSLTCEKECKEMKVTFYVNENGQCSLTTITGYLQEDGKTYKTQFQGNNRYKLVDESPENLTFYSENVDRADRKTKLLFILGHGPLTSEQKEKFAELAEEKGIPAGNIREVLITDYCPE | Binds the chemical odorant 2-isobutyl-3-methoxypyrazine. | Q9D3H2 |
Q3J8S9 | RL6_NITOC | 50S ribosomal protein L6 | Nitrosococcus | MSRIADNPVSIPKGVEVTLSGDNDIKVKGAKGSLAFAIHPLIQVVQDGETLRFSAKSTDKRVNALRGTTRALINNMVQGVSQGFERRLQLVGVGYRAQLQGRKLVLSLGYSHPVEFTAPEGLTIEVPSPTEIIVKGYDKQQVGQAAANIRRFRPPEPYKGKGVRYADEVVVRKEAKKK | 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. | Q3J8S9 |
P16890 | H2BL4_STRPU | Late histone H2B.L4 | Strongylocentrotus | HASRATDGKKRRKRRKESYGIYIYKVLKQVHPDTGISSRAMSIMNSFVNDVFERIAGEASRLAQYNKKSTISSREVQTAVRLLLPGELAKHAVSEGTKAVTKYTTSK | Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | P16890 |
Q9LKI5 | XPF_ARATH | Ultraviolet hypersensitive 1 | Arabidopsis | MALKYHQQIISDLLEDSNGGLLILSSGLSLAKLIASLLILHSPSQGTLLLLLSPAAQSLKSRIIHYISSLDSPTPTEITADLPANQRYSLYTSGSPFFITPRILIVDLLTQRIPVSSLAGIFILNAHSISETSTEAFIIRIVKSLNSSAYIRAFSDRPQAMVSGFAKTERTMRALFLRKIHLWPRFQLDVSQELEREPPEVVDIRVSMSNYMVGIQKAIIEVMDACLKEMKKTNKVDVDDLTVESGLFKSFDEIVRRQLDPIWHTLGKRTKQLVSDLKTLRKLLDYLVRYDAVSFLKFLDTLRVSESYRSVWLFAESSYKIFDFAKKRVYRLVKASDVKSKEHVKNKSGKKRNSKGETDSVEAVGGETATNVATGVVVEEVLEEAPKWKVLREILEETQEERLKQAFSEEDNSDNNGIVLVACKDERSCMQLEDCITNNPQKVMREEWEMYLLSKIELRSMQTPQKKKQKTPKGFGILDGVVPVTTIQNSEGSSVGRQEHEALMAAASSIRKLGKTTDMASGNNNPEPHVDKASCTKGKAKKDPTSLRRSLRSCNKKTTNSKPEILPGPENEEKANEASTSAPQEANAVRPSGAKKLPPVHFYALESDQPILDILKPSVIIVYHPDMGFVRELEVYKAENPLRKLKVYFIFYDESTEVQKFEASIRRENEAFESLIRQKSSMIIPVDQDGLCMGSNSSTEFPASSTQNSLTRKAGGRKELEKETQVIVDMREFMSSLPNVLHQKGMKIIPVTLEVGDYILSPSICVERKSIQDLFQSFTSGRLFHQVEMMSRYYRIPVLLIEFSQDKSFSFQSSSDISDDVTPYNIISKLSLLVLHFPRLRLLWSRSLHATAEIFTTLKSNQDEPDETRAIRVGVPSEEGIIENDIRAENYNTSAVEFLRRLPGVSDANYRSIMEKCKSLAELASLPVETLAELMGGHKVAKSLREFLDAKYPTLL | Seems to be involved in nucleotide excision repair (NER) of damaged DNA (dark repair mechanism). Involved in repair of UV light, and probably oxidative damage. The UVH1/RAD1-ERCC1/RAD10 complex may act as an endonuclease making DNA incision 5' to the lesion site. In vitro, is implicated in double strand breaks (DSBs) repair and is required for homologous recombination in the presence of non-homologous overhangs. May mediate the induction of a DNA-damage sensitive cell-cycle checkpoint during the G2 phase. | Q9LKI5 |
Q75JL2 | RECAM_DICDI | Recombinase A homolog | Dictyostelium | MSINKILSSTYKITQRSNNNNILFNGLKINSFSLCNTKTNLFTNKTNINLYNNYSKSSKSGKKSKKDEDDEDGEIETSKTSKKSASSSSMENVLKELEKSFGKGTLMKLGSQFSTQKVEVIPSGSMGLDIALGVGGLPKGRVTEIFGPESSGKTTLALHVIAQAQKAGGNCTFIDAEHALNPQWAARLGVNLDELFVSQPDNGEQALEIVDSLLRSKTMSVIVVDSVAALVPRVEIEGEMGDSHLGVQARLMSQALRKLSPTLKDSNCVLIFINQIRMKIGVMFGNPEVTSGGNALKFFSSIRIDIRKVGTVKKGDDIIASQVKAKVVKNKLAPPFKEAIFDIDFQSGINKTGEIIDLAVAEGIIDKMGSWYSYNDIKLDQGREKTKYLLEKTQPNLLVEIENKLRDKLIKSKPLINQQQEEEGNDQTSDEFDIENDDEIIEEDIDDETIKK | Involved in DNA recombination ability. Important for survival following exposure to DNA damaging agents. | Q75JL2 |
Q04732 | ARP_EUGGR | Calcium-binding acidic-repeat protein | Euglena | MSHLWCWLFLVLCLACLVLSIEAKDSDGDGLLDVDEINVYFTDPYNADSDQDGLTDGLEVNRHQTHPQDKDTDDDSIGDGVEVNNLGTNPKDPDSDDDGLTDGAEVNLYRTDPLDADSTTTGCPMGGGAEVRHRPQNGDTDDDGLTDGAEVNVHRTNPQDGDSDDDGLSDGAEVNTYHSNPKDGDSDDDGVSDGAEVNPKLKDSDGDGLTDEEEIKLYRTDPFCADSDFDGLLDGEEVKVHKTNPLDGDSDDDGLGDGAEVTHFNTNPLDADSDNDGLDDGEEINVHGTDPEDPDSDNDGLNDGDEVNVYNTDPEEDDSDEDGVCDGAEVNVHHTNPKDEDSDNDGIPDGAEINTHKTDPNDEDSDDDGIADGAEVTLTDSDGDGLPDEDEVALYNTNPANADSDYDGLTDGAEVKRYQSNPLDKDTDDDGLGDGVEVTVGTDPHDATVTTTGSRTAVEINVHGSDPNDEDTDDDGLTDGAEVNLHRTDPEDADTDDDGLTDGAEVNTYRTNPKLADSDGDGLSDGAEVNTHKSDPNDGDSDDDGVPDAAEAKVKDSDGDGLSDTDEVRFRTNPKLADTDFDGLTDGAEILKHKTDPRNRDTDGDGVADGLEVNTYGSDPKDADTDDDGLTDGAEINVHDTNPTDADSDDDGLSDGAEVMTYHTNAKDGDSDDDGKADGAEVSASTDPWRSDHSV | May function as a calcium-binding protein. | Q04732 |
C9RZ55 | SPL_GEOSY | Spore photoproduct lyase | unclassified Geobacillus | MKPFVPKLVYFEPEALSYPLGQELYEKFTQMGIEIRETTSHNQVRGIPGETELARYRNAKSTLVVGVRRTLKFDSSKPSAEYAIPLATGCMGHCHYCYLQTTLGSKPYIRVYVNLDDIFAQAQKYIDERAPEITRFEAACTSDIVGIDHLTHSLKKAIEFIGATDYGRLRFVTKYEHVDHLLDAKHNGKTRFRFSVNSRYVINHFEPGTSSFDARLQAARKVAGAGYKLGFVVAPIYRHDGWEQGYFELFQELARQLEGVDLSDLTFELIQHRFTKPAKRVIEQRYPKTKLDLDESKRKYKWGRYGIGKYVYRDKEARELEETMRSYIARFFPSAQVQYFT | Involved in repair of UV radiation-induced DNA damage during spore germination. Can repair thymine dimer 5-thyminyl-5,6-dihydrothymine (known as spore photoproduct (SP)) by in situ monomerization of SP to two thymines. | C9RZ55 |
Q9ZZY5 | COX3_HIPAM | Cytochrome c oxidase polypeptide III | Hippopotamus | MTHQTHAYHMVNPSPWPLTGALSALLMSSGLTMWFHFNSLILLTTGLVTNILTMYQWWRDVIRESTFQGHHTPVVQKGLRYGMVLFIISEVLFFTGFFWAFYHSSLAPTPELGGCWPPTGINPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKQMLQALFITIALGVYFTLLQASEYHEASFTISDGVYGSTFFVATGFHGLHVIIGSTFLIVCFLRQLKFHFTSDHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS | Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. | Q9ZZY5 |
Q1K4R6 | ITPA_NEUCR | Nucleoside-triphosphate pyrophosphatase | Neurospora | MSAPSQARHIVNFITGNANKLGEVKAILEPAIQVENQALDLLEIQGTLEEVTLDKCRRAADLVQGPVLVEDTCLCFNALKGLPGPYIKWFMNSLGHEGLNNLLAAYEDKSAKAVCTFGYSAGPGHEPILFQGITDGKIVPPRGPPNFGWDAIFEYEGQTYAEMDKAEKNKISHRAKALAKLQEWFAKEMTA | Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. | Q1K4R6 |
B7UFP4 | UBIG_ECO27 | 3-demethylubiquinone-8 3-O-methyltransferase | Escherichia | MNAEKSPVNHNVDHEEIAKFEAVASRWWDLEGEFKPLHRINPLRLGYIAERAGGLFGKKVLDVGCGGGILAESMAREGATVTGLDMGFEPLQVAKLHALESGIQVDYVQETVEEHAAKYAGQYDVVTCMEMLEHVPDPQSVVRACAQLVKPGGDVFFSTLNRNGKSWLMAVVGAEYILRMVPKGTHDVKKFIKPAELLGWVDQTSLKERHMTGLHYNPITNTFKLGPGVDVNYMLHTQNK | O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. | B7UFP4 |
Q74GA6 | NUOC_GEOSL | NDH-1 subunit C | Geobacter | MAENNRAVIKLKEKFAASILDVREFRGEVTVTVAREKVVDICRFLKESLQYNLCTDVTAVDYLGKQEPRFMVVYNLYSIPNKDRLRLKAGVPDADCSIDTVSCVWNSANWLEREVYDLMGVQFNNHPDLRRILMTDDWVGHPLRKDYPLQGPDREPYKGRLS | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. | Q74GA6 |
Q5LJ70 | MIAB_BACFN | tRNA-i(6)A37 methylthiotransferase | Bacteroides | MNELTGADFKSATADDNKKLFIETYGCQMNVADSEVIASVMQMAGYSVAETLEEADAVFMNTCSIRDNAEQKILNRLEFFHSMKKKKKHLIVGVLGCMAERVKDDLIEHHHVDLVVGPDAYLTLPELIASVEAGEKAMNVELSTTETYRDVIPSRICGNHISGFVSIMRGCNNFCTYCIVPYTRGRERSRDVESILNEVADLVSKGYKEITLLGQNVNSYRFEKEGGEVVTFPMLLRLVAEAAPGIRVRFTTSHPKDMSDETLEVIAQVPNVCKHIHLPVQSGSSRILKLMNRKYTREWYLDRVAAIKRIVPDCGLTTDIFSGFHSETEEDHRESLSLMEACGYDAAFMFKYSERPGTYASKHLEDNVPEEIKVRRLNEIIALQNRLSAESNNRCIGKTYEVLVEGVSKRSRDQLFGRTEQNRVVVFDRGTHRIGDFVNVRITEASSATLKGEEVFS | Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | Q5LJ70 |
B1L935 | RPOB_THESQ | Transcriptase subunit beta | unclassified Thermotoga | MKEISCGRRTRVSFGKSREPLPIPDLVEIQKISYRRFLEEGLLEVLKKFSPIYSQATRSDLKKSDRGFALEFVSTRIGEPVVDPLECKAKGLTYSVPIYATARLTDMKSGEMKEEEVFLGYIPYMTDRGTFIINGAERVVVNQIVVSPGLYFSSEYIDREEYGGYFLPSRGAWLEVILDPYDGVLYAGLDGKKVNLFLFLKTIGYEKDEDILSLYPTYLDADDEDSLLLHVGSILLEDIYDGDRKIAEKWDILTKDLAERILMIDDINQIKIVHPIAQNTFEKMLELVSSSGEEGEEEEEKTKIYGLNEVTVVDAYLEIFRRLRPEELPRINAAKRYLHDLFFNPERYDLSEVGRYKVNERLRNAYIRYLIEVEGEDPEEARKKVYNETSLVLKPLDIVLASRILFDYFERRYVNDFEIDSYELKNLIRIFKEEYLEKRKTAPYDLRKLVSVFRRNYGVTSDLGVFAAIRYVSNINKELPSIPFDTKDHLGNKRVRTVGELVQREFERLFARAQKAIQERLTLINSLSKVSIQSLINIKSIISTVNQFFAMNQLSQFMDQVNPLSELTHKRRVSAVGPGGLRRESKVFEARNVHYSQYGRLCPIETPEGANIGFITSLAIYAKIDEYGFLMTPYRKVVNGKVTDEVVYLRANEEEEYKIIPATTPVDEEGNIIPERVVARMGEDIRLVPKEEVDFMDVSTKQPFSVSASLIPFLEHDDASRALMGSNMQRQAVPLLKTEAPLVGTGMEWEAAKNSGYVVLAEHDGIVKEVDAARVVVHRTDENGNLMYDDKGNPVVDEYRLLKFVRSNQDTMINQKPIVNEGDFVKKGDPIADGPATDMGELALGRNILVAFMPWEGYNYEDAILVSQELLEEDVFTSIHIEVYETQARETRLGPEEITADIPNVSKELLKNLDENGIIRVGAYVVSDYGVGSQAILVGKVTPKGEGDTTPEEKIIRSVFGERGRDVKDTSLRLPHGVEGRVIRVDVYDQNDIAELGAGVLKLVRVYVASRKTLDIGDKLAGRHGNKGVVSNILPKEDMPFLPDGTPVQMVLNPLGIPSRMNVGQILETHLGWLAKLTGKWFATPVFEGAKEDEILRPLYEERKKRGLHLGDDENNPNGKVVLRDGRTGEPFDNPVVVGYMYMLKLIHIAKEKIHARSTGPYSLIHQQPLGGKSHFGGQRLGEMEVWALEAYGAAHTLAEMLTIKSDDIKGRNEAYKAILKNMNIPEPGVPESFRVLIKELRGLALDVRLYDENGNEIDIDKY | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | B1L935 |
Q0I2W9 | MNMC_HAES1 | FAD-dependent cmnm(5)s(2)U34 oxidoreductase | Histophilus | MFTVTPAKIYLNQEKTPVSEQFNDVYFSNQDGLAESEYVFQQGNHLWERWIVYQEKHFVIAETGFGTGLNFLAVTSLFRQFRQQYPDFPLKRLFFISFEKYPLPKDQLQQIHRLYPQFSALSQQLCDYCLDAIQGCQRFHFAETTLDLWFGDIADNLPQLGDYMQNRIDAWFLDGFSPSKNPQMWNDKLYQQIFYYSKPQGTFATFTAASAVRKGLISAGFEVQKRKGYGKKRECLCGIKNSTQQQNAKFPWYLNQPASLLSEDIAIIGGGIASLFTALSLLKRGAKVTLYCEDEQLALNASGNKQGAFYPQLSDDDDRNIRFYVHAFFYALQQLQWAIKQGIEFEHEFCGVALCAYDHKSAVKLAKISSYQWSKSLYQNLNKEQLSEKIGLPLDCAGGFIPQGAWLAPRQFVQNAFSYLQQLGLEIKTSQKITALDYRNLQWVLTNEQNETFNHQVVVLANGYQITDFVQTAKLPLYPVRGQVSQIPTSANLLKLKSVLCYDGYLTPADKMKQSHCLGASHIRNNKDRHFSHQEQRENQQKIQQNLASTDTDKNMDWLQDIDISANIARIGVRCSVRDRVPIMGNVPHFEQQCLDYRNIFNLRRRKQPIPDAAQWKNLYLIGALGSRGLTSAALLGETLASLIYAEPLPLSEDILHNLSPNRSWIRKLLKGTEIK | Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34. | Q0I2W9 |
Q1QZS5 | METE_CHRSD | Methionine synthase, vitamin-B12 independent isozyme | Chromohalobacter | MALAHILGYPRIGANRELKKAVEAYWKGDIDQAELERRGQALRAEHWQASRDAGLDFVTVGDFAFYDQVLNVSAMLGAVPPRFGAIDGDVDLDTTFRMARGRAPSGTPAAACEMTKYFDTNYHYLVPELHAGQRFRVASTRLFDEVAEAQAAGHPVKVALLGPVSWLWLGKEKSAGLDRLTLLDDVLSVYGEILERLAAQGVEWVQLDEPALVQDLPRDWRQAFESAYNKLQSAPVKLLLATYFGALGDNLGLAAGLPVAGLHIDTVRAPEQLDAVLDRLPTYKVLSLGAIDGRNIWRADLAALRERLQVARARLGERLWISASCSLLHVPVDLDAETDLDAELKSWLAFARQKLDEIVTLAHLLDGRATPEDTARLEAATSALDARRQSPRIHKPAVGERLAAVSADDAERASPYATRAKAQHRHLDLPLFPTTTIGSFPQTQDIRAARRAFKSGELSRDDYEARMRDEIAHAVERQEALAIDVPVHGEPERNDMVEYFGELLDGFAFTRFGWVQSYGSRCVKPPVIFGDVSRPGPMTVRWSEYAQSLTDKPMKGMLTGPVTILQWSFVRDDQPRDATCRQIALSLRDEVADLEAAGIKIIQIDEPALREGLPLRQGEWQEYLDWAVKSFKLSAAVARDETQIHTHMCYSEFNDIIAAIAALDADVITIETSRSDMELLDAFQDFAYPNEIGPGVYDIHSPNIPEVEWMVSLMEKAAEKIPAERLWVNPDCGLKTRGWAEVEPALANMVEAARELRRRYG | Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation. | Q1QZS5 |
A2RKR1 | LEUD_LACLM | Isopropylmalate isomerase | Lactococcus cremoris subsp. cremoris | MEKFTIYKGTSVPLMNDNIDTDQIIPKQFLKAIDKKGFGKNLFYEWRYSKDYEENPDFMLNKPQYRKASLLISGDNFGSGSSREHAAWALADYGFRAIIAGSYSDIFYNNSLKNGLLPIVQPKEALKSLAQLSSQEEITIDLPHQLIQTSTENFYFEIDPIWKDKLINGLDDIGITLQYEQAITAYEQKHQ | Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. | A2RKR1 |
Q1D0S7 | MRAY_MYXXD | UDP-MurNAc-pentapeptide phosphotransferase | Myxococcus | MLYLLYEVIQNSEAGRVLNFLRYPTFRIIAAGVFALLLGMLIGPKLIARLRLKQHGQSNVREDTPDSHQKKKGTPTMGGALILLCIAAGTLLFADLKSRAVWVMLLLTLGYGFIGFLDDWLKLSKRNSKGLAGRKKMVLQTFFFLVAVFGLLTTWTLPDGSFGPTLLINTKLTLPFIPTRWFNPDLGWFYVFFAWIVVVGTSNAVNLTDGLDGLAIVPTIVSAITFAVLCYVAGTTLSIADYEVVGGASKLVATPLYQYLGILQVPGGAELAVFCAAIVGAGISFLWFNTYPASVFMGDIGSLALGGALGGLAMLSKNEVVSAIIHGIFFAEILSVMIQVTSFKMTGKRVFKMAPVHHHFELKGMAEPKIIVRFWIVSILCGGVALLSLKLR | Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I. | Q1D0S7 |
B0BU72 | TRPB_ACTPJ | Tryptophan synthase beta chain | Actinobacillus | MSDTLLNPYFGEFGGMYVPEILVPVLKQLEETFVAAQNDPLFQAEFTDLLKNYAGRPTALTLCRNLTKGSKTKLYLKREDLLHGGAHKTNQVLGQALLAKRMGKTRIIAETGAGQHGVATALACAMLDLPCVIYMGAKDVERQSPNVFRMRLMGAEVIPVQKGSCSLKDACCEAMRDWAANYETTHYLIGTAAGPHPFPTMVREFQKMIGEETKRQILEKENRLPDAVIAAVGGGSNAIGMFAGFIEEKSVQLIGVEPAGKGIETGEHGAPLKHGTTGIYFGMKSPIMQTKDGQIEESYSISAGLDFPSVGPQHAYLNSIGRAEYVSITNQEALDAFQALAQHEGIIPALESSHALAYALKLIAQNPDKEQLLVVNLSGRGDKDIFTVDKILNGGN | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | B0BU72 |
Q39WF4 | SYY_GEOMG | Tyrosyl-tRNA synthetase | Geobacter | MSVAEQMAIIKRGATEILLEKELEEKIEKSLSTGVPLRIKAGFDPTAPDLHLGHTVLLHKMRQFQQLGHEVCFLIGDFTGMIGDPTGKSETRKALTREDVLKNAETYKEQVFKILDPKKTRVVFNSEWLGKMTASDMIGLAAQSTVARMLERDDFGKRFANQLPISIHEFLYPLIQGYDSVALKADVELGGTDQKFNLLVGRELQRVWKQSPQSVITMPLLEGLDGVNKMSKSLGNYIGINEPADEIFGKIMSISDELMLRYYELLSDLTLAEIEKLKAAMRDGDVHPMAAKKQLAREIVARYHGAVAADNAEESFVRRFRDNQTPEEMPECILSAEEGKVLLGRLLAEAGLVKSNSEGRRAINQGGVKVNGEKVTNDMLELPGVGEYVLQFGKRRFARIVFK | Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). | Q39WF4 |
Q6R8G4 | PHO16_ARATH | Protein PHO1 homolog 6 | Arabidopsis | MKFGKDFSSEWQQAYVDYKYLKTLVKDINRFKRKTNLHGGQISLSSTVLEIEDGITTATIQVSSTASQRYETTFLMTAEKGGEYELVFFRRLDDEFNKVEKFYREKVDEVVKEAAVLNKQMDALIAFRLKMKEESTVEMARFALHGVVSPAELAKNPSMKVHMEAIEEGGSSRAGRRSDEDDYYTDEEDHNDVFFTPANNLSKMKSSSSAFIEVLDSIKINNTKEALQSNTKSVLKVSNHTELKFSRDNLRKIEEKLICAFVEFHRKLWYLKSYSFLNVLALSKILTKYDKITSRDAAKSYMKMVDKSCLGSSDEVMKLMENVEATFIKQFTNGNRTKGMNILRPKPKRERHRLTFSTGFLGGCMFSLIVALVAIVRTRNILQDDGQKQYMNTMFPLYSLFGFIMLHMTMYAANIYFWRQYRVNYSFIFGFKQGTELGYKQVLFVGFSIGALALLCVLANLDMETDPKTKDYQALTELLPLFLLIAMFVVLVVPFNIFYRSSRFFFLTTLFHMLAAPLYKVTLPDFFLADQLCSQAQTLRSIEFYICYYGWGDFKQRKNTCKDSQVFNTFLFIVSAFPFFSRFLQCMRRMLEEKNIEQGYNGFKYIVIVVAVCLGMAYEVDDEKDRQIIWRLLGGITSAMAVVFCTYWDLVYDWGLLNRTSKNPWLRDNLLIPHKEVYVLAMILNVVLRFAWMQTVLDFKFESIHTQTVVAVVASLEIIRRGIWNFFRLENEHLNNVGKYRAFKAVSLPFNYEVDH | May transport inorganic phosphate (Pi). | Q6R8G4 |
Q41014 | FENR2_PEA | Ferredoxin--NADP reductase, root isozyme, chloroplastic | Pisum | MSHLAVSQMAVTVPVSSDFSVRRSAFKSSNLNFRDKSWAPVFTLGMKAKNCGWRNHNVICMSVQQASVPKVTVSPLELENPSEPPLNLHKPKEPYTATIVSVERLVGPKAPGETCHIVINHDGNVPYWEGQSYGVIPPGENPKKPGSPHNVRLYSIASTRYGDNFDGKTASLCVRRAVYYDPVTGKEDPSKNGVCSNFLCDSKPGDKIKIAGPSGKIMLLPEDDPNATHIMIATGTGVAPYRGYLRRMFMESVPTFKFGGLAWLFLGVANVDSLLYDDEFTKYLKDYPDNFRYNRALSREEKNKNGGKMYVQDKIEEYSDEIFKLLDNGAHIYFCGLRGMMPGIQETLKRVAEKRGESWEEKLSQLKKNKQWHVEVY | May play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power. Is involved in nitrate assimilation. | Q41014 |
Q8W4B2 | APEM9_ARATH | Protein DAYU | Arabidopsis | MEATDIWGEIERSESYLVCSMYEEAESLSSSILKRIFGNIDVLSDEASQGDHQFHDMLESAGMVLVQSLHGIGRTVEIVNELRDVFGEVAAIPVQVLLTGVCLQISNGSYLGVRDILEEFFRIWVYKDNHYILNDAGVSTKGFHAKNCLDIDEYMEVVELYTFGVLAKFSNDMGLAISWVEKAALPEERRQGILRRLHSLLSLKTASSFEENSKDSSYAVVNNKKSLGNEKNDEIDSFLKLSKQHEPWSLWSSHPLSLKVGNTQFSMSRGKVAVSLVGLIICYALKRKRAALIRIIRRQMESTRKAIVDFWKLAFSYQVNPLAAIQSIPSTTT | Involved in peroxisome biogenesis and matrix protein import . Required for pollen maturation and in vivo germination via its role in peroxisomal function, which partially involves jasmonic acid biosynthesis . Transported to peroxisomes via the interaction with PEX19-1 . Required for peroxisomal protein import by acting as an anchoring protein for the AAA ATPase complex, which consists of PEX1 and PEX6 . | Q8W4B2 |
Q32GQ6 | RIBA_SHIDS | GTP cyclohydrolase II | Shigella | MQLKRVVEAKLPTPWGDFLMVGFEELATGHDHVALVYGDISGHTPVLARVHSECLTGDALFSLRCDCGFQLEAALTQIAEEGRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLGVNEVRLLTNNPKKVEILTEAGINIVERVPLIVGRNPNNEHYLDTKAEKMGHLLNK | Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate. | Q32GQ6 |
A3DE48 | RIMP_ACET2 | Ribosome maturation factor RimP | Acetivibrio | MTRKEIEEIVTEIANPVVNKHSFELVDVEFIKEGSSWYLRIYIDKPGGITIDDCQVVSEEISDILDKEDPIPHSYFLEVSSPGLDRPLKKESDFERFKGELVEVKVFKPIEGKKIFEGELVGYKDNKIIIKKNGNELMEFERDKVALVRRVIKF | Required for maturation of 30S ribosomal subunits. | A3DE48 |
Q605G9 | PANC_METCA | Pantoate-activating enzyme | Methylococcus | MKIVSTKTELEAVLAPWRAADDSIAFVPTMGNLHAGHLHLVDTAKTKARRVVVSIFVNPTQFGPDEDLAAYPRTPEQDIERLRAHQADLLYLPDAADVYPDDGQPATFVEVPGLSEQLCGKFRPGHFRGVATVVCKLLNRVRPDLALFGEKDFQQLTVIRKMVRDLDMAVTIMGVPTVREPSGLAMSSRNAYLSPEQKERASLIFRTLNQAAEAVRAGERDYARIEQEASATLEAGGFSVDYVSIRRQQDLAAPSADDSALVILAAAHLGRARLIDNVLISLDTTR | Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. | Q605G9 |
Q58030 | END3_METJA | DNA-(apurinic or apyrimidinic site) lyase | Methanocaldococcus | MELIEILLKKLNKNAVVTEIAKDKDPFKVLISTIISARTKDEVTEEVSKKLFKEIKDVDDLLNIDEEKLADLIYPAGFYKNKAKNLKKLAKILKENYNGKVPDSLEELLKLPGVGRKTANLVITLAFNKDGICVDTHVHRICNRWEIVDTETPEETEFELRKKLPKKYWKVINNLLVVFGREICSSKSKCDKCFKEIKEKCPYYEKIKHFENILKKFNFRKVSKNKIPNEKGTYILKIRLKEGKKIKFGKTERFFKKGYYFYIGSAFGNSMNLKNRIERHLKDDKKMHWHIDYLLKYGKIEEIYITNERVECEVANEFIKKFDFVENFGCSDCKCKSHLFYLKP | DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. | Q58030 |
Q18CG4 | RL16_CLOD6 | 50S ribosomal protein L16 | Clostridioides | MLMPKRVKRRRVHRGSMAGQAHKGNKVTYGEFGLVALEASWITSNQIEAARIAMTRYIKRGGKVWIKIFPHKPVTRKPAETRMGAGKGSPEYWVAVVKPGRVMFELAGVSEDKAREAMRLAAHKLPIKCKFVKKEDLEVKGGE | Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. | Q18CG4 |
B8FUL3 | YBEY_DESHD | Endoribonuclease YbeY | Desulfitobacterium | MYLDINWEEDSIPENERGSLTGLLEQGIAKAVHLSAESEEAEVSLTLVDDARIHELNRDYRGVDRPTDVLSFALQEERSDEPDILDYEDHLLGDIIISVERARAQAIDYGHSFERELVYLAVHGTLHLLGYDHMEEEDKEEMRRQEEAVMSQIGLLR | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | B8FUL3 |
Q9ZM66 | FTSH_HELPJ | ATP-dependent zinc metalloprotease FtsH | Helicobacter | MKPTNEPKKPFFQSPIVLAVLGGILLIFFLRSFNSDGSFSDNFLASSTKNVSYHEIKQLISNNEVENVSIGQTLIKASHKEGNNRVIYIAKRVPDLTLVPLLDEKKINYSGFSESNFFTDMLGWLMPILVILGLWMFMANRMQKNMGGGIFGMGSAKKLINAEKPNVRFNDMAGNEEAKEEVVEIVDFLKYPERYANLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAHVPFFSMGGSSFIEMFVGLGASRVRDLFETAKKQAPSIIFIDEIDAIGKSRAAGGMISGNDEREQTLNQLLAEMDGFGSENAPVIVLAATNRPEILDPALMRPGRFDRQVLVDKPDFNGRVEILKVHIKGVKLANDVNLQEVAKLTAGLAGADLANIINEAALLAGRNNQKEVKQQHLKEAVERGIAGLEKKSRRISPKEKKIVAYHESGHAVISEMTKGSTRVNKVSIIPRGMAALGYTLNTPEENKYLMQKHELIAEIDVLLGGRAAEEVFLEEISTGASNDLERATDIIKGMVSYYGMSSVSGLMVLEKQRNAFLGGGYGSSREFSEKTAEEMDLFIKNLLEERYQHVKQTLSDYREAIEIMVKELFDKEVITGERVREIISEYEAANNLESRLIPLEEQAS | Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. | Q9ZM66 |
Q82WB9 | MDH_NITEU | Malate dehydrogenase | Nitrosomonas | MSSPIRIAVTGAAGQISYSLLFRIAAGDMLGSSQPVILQLLDIPESGKVLDGVLMELQDCAFPLLTDIIVTHDPMIAFDQADIAILVGARPRGKGMERKDLLQTNGEIFREQGRALNQVVKRDAKILVVGNPANTNTLITMKNAPDLSPENFSGMLRLDHNRALSQVAMKLNQPVSHIRKMIVWGNHSSTQFPDLSHAEIDHQKVIDLIKDQTWVENSFIPTVQNRGAVVIEARGLSSAASAANAIIDHMRDWIFGTRDDDWITMGILSDGSYKIPKGVIYGFPVVCKNGGRKIVQGLEISPFSRTRLDIAYDELTQELDSIKHLLL | Catalyzes the reversible oxidation of malate to oxaloacetate. | Q82WB9 |
Q8XZJ6 | DEF2_RALSO | Polypeptide deformylase 2 | Ralstonia | MIRPILKMGDSRLLRVAKPVQRFQTPELTALIEDMFDTMDAARGAGLAAPQIGVDLQVVIFGFDRNDRYPDAPAVPKTVLINPTIEPLSDAMEDGWEGCLSVPGLRGVVPRYTRLRYTGYDQHGHAIDRIAEGFHARVVQHECDHLQGILYPMRVQDFTRFGFTEILFPELPAHHND | Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Q8XZJ6 |
A9ITN0 | NADD_BORPD | Nicotinate mononucleotide adenylyltransferase | Bordetella | MKRIGLLGGSFDPVHLAHLALARAAAAELRLDSVQLIPAANPWQRAPLRASAGHRLRMIELAIDGEPQLAVNPVELERGGPTYTIDTVRALPADAHYVWLLGTDQLANFCTWRQWQAIAGHVDLAVAARPGAPLAAPAELASWLAAHRRRLIRLPFSPMAISASDIRGRLARGASTAGLLPATVARYIARHGLYR | Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). | A9ITN0 |
P42472 | EFTU_CHLAU | Elongation factor Tu | Chloroflexus | HVDHGKTTLTAAITKVMSLKGAAQFMAYDQIDNAPEERARGITIAIRHVEYQTDKRHYAHVDCPGHADYIKNMITGAAQMDGAILVVSAPDGPMPQTREHILLARQVQVPAIVVFLNKVDMMDDPELLELVELELRELLSKYGFPGDEIPIVRGTARNALESPSKDINAPEYKCILELMNAVDEYIPTPQRAVDQPFLMPIEDVFGIKGRGTVVTGRIERGKVKVGDTVEIVGMTNDAPRRTVVTGVEMFQKTLDEGIAGDNVGCLLRGIERTDVERGQVLCAPGSIKPHKKFEAQVYVLKKEEGGRHTPFFSGYRPQFYIRTTDVTGAIGLPAGMEMVMPGDNVVMTIELIVPVAIEEGLRFAIREGGRTVGAGVVTKILD | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. | P42472 |
P50132 | GPR4_PIG | G-protein coupled receptor 4 | Sus | MGNGTWEGCHVDSRVDHLFPPSLYIFVIGVGLPTNCLALWAAYRQVRQRNELGVYLMNLSIADLLYICTLPLWVDYFLHHDNWIHGPGSCKLFGFIFYTNIYISIAFLCCISVDRYLAVAHPLRFARLRRVKTAVAVSSVVWATELGANSVPLFHDELFRDRYNHTFCFEKFPMEGWVAWMNLYRVFVGFLFPWALMLLSYRGILRAVRGSVSTERQEKAKIKRLALSLIAIVLVCFAPYHVLLLSRSAVYLGHPWDCGFEERVFSAYHSSLAFTSLNCVADPILYCLVNEGARSDVAKALHNLLRFLTSDKPQEMASASLTLDTPLTSKRNSMARAVAAGWVASPPSQGDQVQLKMLPPPAP | Proton-sensing G-protein coupled receptor couples to multiple intracellular signaling pathways, including GNAS/cAMP, GNAQ/phospholipase C (PLC), and GNA13/Rho pathways. Acidosis-induced GPR4 activation increases paracellular gap formation and permeability of vascular endothelial cells through the GNA12/GNA13/Rho GTPase signaling pathway. In the brain may mediate central respiratory sensitivity to CO(2)/H(+). | P50132 |
P03052 | KORA2_ECOLX | Regulatory protein KorA | Escherichia | MKKRLTESQFQEAIQGLEVGQQTIEIARGVLVDGKPQATFATSLGLTRGAVSQAVHRVWAAFEDKNLPEGYARVTAVLPEHQAYIVRKWEADAKKKQETKR | In conjunction with KorB, inhibits the transcription of kilA, trfA and korAB operons. In conjunction with KorC is responsible for the negative control of kilC and kilE operons. | P03052 |
B1KI55 | LEPA_SHEWM | Ribosomal back-translocase LepA | Shewanella | MKHIRNFSIIAHIDHGKSTLSDRLIQECGGLSDREMAAQVLDSMDIERERGITIKAQSVTLDYKALDGETYQLNFIDTPGHVDFSYEVSRSLAACEGALLVVDAGQGVEAQTLANCYTALEMDMDVVPVLNKIDLPQADPERVADEIEDIVGIEAADAVRCSAKTGIGIKDVLEVIVAQIPPPEGDTEGPLQALIIDSWFDSYLGVVSLVRIKNGILKKGDKFKVMSTGQTYNADRVGIFTPKQTDTAELKTGEVGFVIAGIKEIHGAPVGDTLTHAKHGAEKPLGGFKKVKPQVYAGVFPISTDDYESFRDALNKLSLNDASLFFEPETSSALGFGFRIGFLGLLHMEIIQERLEREYNLDLITTAPTVVYEIVKTSGDTIYVDNPSDLPAINNIAEMREPIVETNILVPKDYLGNVITLCVEKRGVQKNMVYHGNQVAITYELPMAEVVMDFFDRLKSTSRGYASLEYNFVRFEPADMVRLDILINGDRVDALAMIIHKGLIRTKGLALVNKMKELIPRQMFDIAVQAAVGSQIIARSSIKAMRKDVTAKCYGGDVSRKKKLLNKQKEGKKRMKSVGNVEVPQEAFLAVLKLND | Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner. | B1KI55 |
P11017 | GBB2_BOVIN | Transducin beta chain 2 | Bos | MSELEQLRQEAEQLRNQIRDARKACGDSTLTQITAGLDPVGRIQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNICSIYSLKTREGNVRVSRELPGHTGYLSCCRFLDDNQIITSSGDTTCALWDIETGQQTVGFAGHSGDVMSLSLAPDGRTFVSGACDASIKLWDVRDSMCRQTFIGHESDINAVAFFPNGYAFTTGSDDATCRLFDLRADQELLMYSHDNIICGITSVAFSRSGRLLLAGYDDFNCNIWDAMKGDRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN | Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. | P11017 |
A8EST5 | RUVA_ALIB4 | Holliday junction ATP-dependent DNA helicase RuvA | Aliarcobacter | MIVGLIGKIIKKEPTQLNVNVNGVIYEVFVSLNCSSKIVSDDVKLEITHIIREDAQSLYGFLDSNEKKLFDTVIKINGVGPKVALAICSTFTPTSFAQIVSSNDVSMLKRVPGIGPKGASRILVELSGFIIDSNDETSGSSSALEAALALESLGFKKDLVSSVLKTCVNSNTSDLVKEALKKLQK | The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. | A8EST5 |
Q04J70 | SECA_STRP2 | Protein translocase subunit SecA | Streptococcus | MANILKTIIENDKGEIRRLEKMADKVFKYEDQMAALTDDQLKAKTVEFKERYQNGESLDSLLYEAFAVVREGAKRVLGLFPYKVQVMGGIVLHHGDVPEMRTGEGKTLTATMPVYLNALSGKGVHVVTVNEYLSERDATEMGELYSWLGLSVGINLATKSPMEKKEAYECDITYSTNSEIGFDYLRDNMVVRAENMVQRPLNYALVDEVDSILIDEARTPLIVSGANAVETSQLYHMADHYVKSLNKDDYIIDVQSKTIGLSDSGIDRAESYFKLENLYDIENVALTHFIDNALRANYIMLLDIDYVVSEEQEILIVDQFTGRTMEGRRYSDGLHQAIEAKEGVPIQDETKTSASITYQNLFRMYKKLSGMTGTGKTEEEEFREIYNIRVIPIPTNRPVQRIDHSDLLYASIESKFKAVVEDVKARYQKGQPVLVGTVAVETSDYISKKLVAAGVPHEVLNAKNHYREAQIIMNAGQRGAVTIATNMAGRGTDIKLGEGVRELGGLCVIGTERHESRRIDNQLRGRSGRQGDPGESQFYLSLEDDLMKRFGSERLKGIFERLNMSEEAIESRMLTRQVEAAQKRVEGNNYDTRKQVLQYDDVMREQREIIYAQRYDVITADRDLAPEIQAMIKRTIERVVDGHARAKQDEKLEAILNFAKYNLLPEDSITMEDLSGLSDKAIKEELFQRALKVYDSQVSKLRDEEAVKEFQKVLILRVVDNKWTDHIDALDQLRNAVGLRGYAQNNPVVEYQAEGFRMFNDMIGSIEFDVTRLMMKAQIHEQERPQAERHISTTATRNIAAHQASMPEDLDLNQIGRNELCPCGSGKKFKNCHGKRQ | Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. | Q04J70 |
Q9ZKR8 | QUED_HELPJ | Queuosine biosynthesis protein QueD | Helicobacter | MVIRRLYKFCASHVVRNCSSLKCAQNIHGHNYEVEVFIETNRLDNANMALDFGLMQQEMQTFIDSFDHAHHFWDKESPEFQRFIENHCVRYVKCSFNLSAESYALMFLYYLTKILQKSVFSNNEGELKVSSVRVHETKNGYAESFLKDLENPHFKSLVHDHCVSFSQGIQSLWHDKDFFHKIISDEKQCFFHAKPLHQIP | Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde. | Q9ZKR8 |
Q85FK2 | PSAJ_ADICA | PSI-J | Adiantum | MQHVKIYLSTAPVVATIWFGLLAGLLIEINRFFPDALLFPFP | May help in the organization of the PsaE and PsaF subunits. | Q85FK2 |
Q31BV1 | DCUP_PROM9 | Uroporphyrinogen decarboxylase | Prochlorococcus | MGENLPLLLSAALGKKVTRPPVWMMRQAGRYMKIYRDLRERYPSFRERSENPELSYEISMQPFHAFKPDGVILFSDILTPLPGMGINFEIIESKGPIIEDPIRTLSQIESLKELNPSESLSFVGQVLSSLKKDVNNEATVLGFVGAPWTLAAYVVEGKSSKNYSLIKSMAFKEPDLLHKLLDHFAKSIGEYLKFQIKSGAQVVQIFDSWAGQLSPQDYDIFAGPYQKKVVDIVKEEYPDTPVILYISGSAGVIERMAKTGVDIISLDWTVDIEEACKRIPDEIGIQGNVDPGILFGNKESIKERIDDTFNKIKDRKYILNLGHGILPGTPEENAQTFFEHGKKLTY | Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | Q31BV1 |
Q0HGL4 | GRPE_SHESM | HSP-70 cofactor | Shewanella | MSNESIKAEQDLIQEGVESEVSTEEASLIDELTQANFRIEELEQLLADALAKVEEQKDSVIRAAAEVDNIRRRAAMDVEKANKFALEKFANELLPVLDNMERALQGTNPQDETTKAIYEGVELTQKSLLTAVAKFGVKPIDPQGQAFNPDQHQAIGMQPSAEFPANTVMLVMQKGYELNSRLLRPAMVMVSQGGPSQEINIEA | Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. | Q0HGL4 |
Q8ZVM8 | RRP4_PYRAE | Exosome complex component Rrp4 | Pyrobaculum | MYYVTPRQLVFPGDVIATADSKVEGPVYLDNGKYRSLVVGLVEFREDVVVVVPLEGTYKPKKGDLVIGYVTDVLATGWEVDVRSFMPAYLPVGEALHRHVDLETTPLTTFLNIGDVVVAKVKDVDLTDEYPIILTLKDEKVGKVESGTVVEITPVKVPRVIGKRGSMLNTLMELGCDIVVGQNGRIWVKCKDPRDEVFLASLIRKIEAESHVMGLTDRIRAEIENYKTSKQQGTV | 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. | Q8ZVM8 |
B2X205 | YCF12_OEDCA | Photosystem II reaction center protein Ycf12 | Oedogonium | MNIDILSQLIAIAVTLFLGPVVVILIASRNGNL | A core subunit of photosystem II (PSII). | B2X205 |
A7Z268 | GATB_BACVZ | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B | Bacillus amyloliquefaciens group | MNFETVIGLEVHVELKTKSKIFSSSPTPFGAEANTQTSVIDLGYPGVLPVLNKEAVEFAMKAAMALNCEIATDTKFDRKNYFYPDNPKAYQISQFDKPIGENGWIEIEVGGKTKKIGITRLHLEEDAGKLTHTGDGYSLVDFNRQGTPLVEIVSEPDIRTPEEAYAYLEKLKSIIQYTGVSDCKMEEGSLRCDANISLRPIGQEKFGTKTELKNLNSFAFVQKGLEHEEKRQEQVLLSGGVIQQETRRYDEATKKTILMRVKEGSDDYRYFPEPDLVELYIDDEWKERVRATIPELPDERRKRYIEELGLPAYDAMVLTLTKEMADFFEETVNKGAEAKQASNWLMGEVSAYLNAEQKELEDVALTPEGLAGMIKLIEKGTISSKIAKKVFKELIEKGGDAEKIVKEKGLVQISDESVLLKLVTDALDSNPQSIEDFKNGKDRAIGFLVGQIMKASKGQANPPMVNKILLEEIKKR | Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln). | A7Z268 |
Q92SK4 | IXTPA_RHIME | Nucleoside-triphosphate pyrophosphatase | Sinorhizobium | MRRLIDKTLVVASHNAGKIREIRDLIGPLGFEAKSAADLNFVEPDETGTTFEENATIKALASAKASGLPALSDDSGLAVDALGGAPGVYTANWAEREDGSRDFQMAMEKVEEALRAKGAVKPESRTARFVSVLCLAWPDGHVELFRGEVEGYVVWPPRGTSGFGYDPVFQPKGYDTTFGEMSAEEKHGWKPGDSEALSHRARAFKLFAETCLGA | Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. | Q92SK4 |
Q96P50 | ACAP3_HUMAN | Centaurin-beta-5 | Homo | MTVEFEECVKDSPRFRATIDEVETDVVEIEAKLDKLVKLCSGMVEAGKAYVSTSRLFVSGVRDLSQQCQGDTVISECLQRFADSLQEVVNYHMILFDQAQRSVRQQLQSFVKEDVRKFKETKKQFDKVREDLELSLVRNAQAPRHRPHEVEEATGALTLTRKCFRHLALDYVLQINVLQAKKKFEILDSMLSFMHAQSSFFQQGYSLLHQLDPYMKKLAAELDQLVIDSAVEKREMERKHAAIQQRTLLQDFSYDESKVEFDVDAPSGVVMEGYLFKRASNAFKTWNRRWFSIQNSQLVYQKKLKDALTVVVDDLRLCSVKPCEDIERRFCFEVLSPTKSCMLQADSEKLRQAWVQAVQASIASAYRESPDSCYSERLDRTASPSTSSIDSATDTRERGVKGESVLQRVQSVAGNSQCGDCGQPDPRWASINLGVLLCIECSGIHRSLGVHCSKVRSLTLDSWEPELLKLMCELGNSAVNQIYEAQCEGAGSRKPTASSSRQDKEAWIKDKYVEKKFLRKAPMAPALEAPRRWRVQKCLRPHSSPRAPTARRKVRLEPVLPCVAALSSVGTLDRKFRRDSLFCPDELDSLFSYFDAGAAGAGPRSLSSDSGLGGSSDGSSDVLAFGSGSVVDSVTEEEGAESEESSGEADGDTEAEAWGLADVRELHPGLLAHRAARARDLPALAAALAHGAEVNWADAEDEGKTPLVQAVLGGSLIVCEFLLQNGADVNQRDSRGRAPLHHATLLGRTGQVCLFLKRGADQHALDQEQRDPLAIAVQAANADIVTLLRLARMAEEMREAEAAPGPPGALAGSPTELQFRRCIQEFISLHLEES | GTPase-activating protein for the ADP ribosylation factor family. | Q96P50 |
A1ATU9 | SYA_PELPD | Alanyl-tRNA synthetase | Pelobacter | MTGSEIRRRFLTFFAERGHTIVPSSGIIPKNDPTLMFANAGMNQFKDCFLGMEKRDYTRACSSQKCVRAGGKHNDLENVGRTARHHTFFEMLGNFSFGDYFKKEAIAFAWEFLTRDLKLDKNRLYVSVYTDDQEAADIWHQQEGVPLERIFRFGEKDNFWSMGDTGPCGPCSEIFYDQGEAAGCGSPDCTVGCDCDRYMEIWNNVFMQFDRSTDGVLTPLPKPSVDTGMGLERISAVMQGVTSNYDTDLIQGIIRHVERLSGKTYGKDERDDVSMRVIADHARAVTFLICDGALPSNEGRGYVLRRIMRRAARHAKMLGLADPMLCHMVDAVRDMMGAAYPELVEREEYIKKVILAEEQRFAETLDRGLAMLNDEVARMRAAGSTVIPGDVLFRLYDTYGFPIDLTADIVESEGFTIDEAGFEQCMERQREQAREHWKGSGAEGIGRVYKELYSRGIRGEFVGYDGLSALSPVLAIIRDGVEVESATAGETIELVTESTPFYGESGGQKGDCGSISTGNSHLEVSGASRPYSDLIVHHATVREGIIRKGDGADLRVSRPERSATARNHTATHLLQAALRRVLGEHVKQAGSLVSPDRLRFDFIHFTAMTTEEIRRVETLVNGFVMDNQPVVITQMDMASAIEAGATALFDEKYGDNVRVVRAGEVSMELCGGTHVRATGEIGLFKIITETGIAAGVRRIEAQTGGGALSFVRQMEDEQRALAGLLKAEGGNLPERLEKLLARQREMQREIESLQGKLNAAASGDLLSGVEEVGGIKLLAAEVRVEDVKALRDLSDTLKERIGQGVIVLGAAIGGKANLLVAVTRELSGTVKAGDLVKKLAPLVGGSGGGKPELAQAGGSRPENLAEALAAARQVLAEQ | Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | A1ATU9 |
B2VGQ6 | RAPA_ERWT9 | ATP-dependent helicase HepA | Erwinia | MPFTLGQRWISDTESELGLGTVVAVDTRMVTLLFPATGENRLYARNDSPITRVVFNPGDTITSHEGWQLDVDEITTANGVVSYIGTRLDTSETGVVLREVMLDSKLVFGKPQDRLFAGQLDRMDRFALRFRARKYQSEQYRLATSGLRGMRTSLIPHQLHIAHDVGRRHAPRVLLADEVGLGKTIEAGMIIHQQLQAGRAERVLIVVPETLQHQWLVEMLRRFNLRFALFDDDRYAQAQLDSDNPFDTEQMIICSLDFVRRNKQRLEKLADAEWDLMVVDEAHHLVWSEDAPSREYQVIEQLAEQVPGILLLTATPEQLGMESHFARLRLLDPDRFHDFAQFVEEQKHFSPIADAVTLLLADQKIGNDELNLLNDLMGEQDIEPLLQTANSDREGKLAARQELISMLMDRHGTSRVLFRNTRNGVKGFPKRELHQIRLPLPTQYQTAIKVSGIMSARKTADERAQDMLYPEQIYQEFEGDSGTWWNFDPRVEWLMGYLTSNRDKKVLVICAKAATALQLEQVLREREGIRAAVFHEGLSIIERDRAAAWFASEEDGAQVLLCSEIGSEGRNFQFASQMVMFDLPFNPDLLEQRIGRLDRIGQVHDIQIHVPYLEKTAQAVLVQWYHEGLDAFEHTCPTGRAVYDSVYTQLIAYLAAPENSEGLEAFIQHCRKQHDTLKAQLEQGRDRLLELNSNGGEKGQALADMIAEQDNNIELVNFALNLFDIVGINQEDRSDNLIVLTPGDHMLVPDFPGLPEDGCTITFDRNQALSREDAQYVSWEHPIIRNGLDLILSGDTGSCAISLLKNKALPVGTLLVELIYVVEAQAPKHLQLTRFLPPTPIRMMVDRKGNNLAAKVEFESFNRQLNAVNRHTGSKLVNAVQSDVHEIITLSEDQAAAEARKVIDAARQEADEKLSAELSRLQALSAVNPNIRQDEIDALESNRQQVLSNLDEAGWRLDALRLIVVTHQ | Transcription regulator that activates transcription by stimulating RNA polymerase (RNAP) recycling in case of stress conditions such as supercoiled DNA or high salt concentrations. Probably acts by releasing the RNAP, when it is trapped or immobilized on tightly supercoiled DNA. Does not activate transcription on linear DNA. Probably not involved in DNA repair. | B2VGQ6 |
B8F3L6 | SECA_GLAP5 | Protein translocase subunit SecA | Glaesserella | MFTKLMTAIFGSSNDRTLRRLNKRVAQINRLEAEFEKLTDEQLQAKTAEFKQRLAEGATLDSLLHEAFATVREASKRVLGMRHFDVQLIGGMVLTERNIAEMRTGEGKTLTATLPCYLNALTGKGVHVVTVNDYLARRDAETNRPLFEFLGMTVAVNIPGLPSDVKRQAYLADITYATNSELGFDYLRDNLAHSKEERFQRPLHYALVDEVDSILIDEARTPLIISGPAEDATQIYQAIDKVIPHLIAQDKEDTEEYTGDGDFTLDLKSKQAHLTERGQVKVENILTKMGLMHEGESLYHPARISLLHHVYAALRAHKLFEVNVDYIVKDGEIVIIDEHTGRTMAGRRWSDGLHQAIEAKEGVNIQGENQTVASITYQNYFRLYEKLAGMTGTADTEAFEFQQIYGLDTVVIPTNRPMIRDDKTDLMFKSEPEKFQAVIKDIQDCIARKQPVLVGTISIEKSEALSEALKQAGIPHKVLNAKFHAQEAEIVADAGYPGAVTIATNMAGRGTDIVLGGNWKAEIAKLENPTQEQIDEIKAKWQERHDIVMQAGGLHIIGTERHESRRIDNQLRGRSGRQGDPGSSRFYLSLDDALMRIYLNEGKLNMMRKAFTEEGEAMESKLLTKVIASAQAKVEAYNFDGRKQLLQYDDVANEQRKAIYEQRNYLLETDDISAMINTVREDVFNAVIDQYIPPQSIEEMWDVPALENRLKQEFGMELPIVKWLEAEDDLHEETLRERIINIAKEQYQAKEAMVGAEVMRSFEKGVMLQNLDELWKEHLSAMDYLRKGIHLRGYAQKDPKQEYKKESFAMFTDMLDHLKSNVISVLSRIQVRSQEEVEQAERERQAHAEQESSHYHAEGEGQDFSDLHIGRNEPCPCGSGKKYKHCHGSKAKYS | Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. | B8F3L6 |
Q6HBC2 | UVRB_BACHK | Excinuclease ABC subunit B | Bacillus cereus group | MERQFEIVSAYSPQGDQPVAIEKLVEGINSGKKKQVLLGATGTGKTFTISNVIKEVQKPTLVMAHNKTLAGQLYSELKDFFPNNAVEYFVSYYDYYQPEAYVPQTDTFIEKDAQINDEIDKLRHSATSALFERDDVIIVASVSCIYGLGSPEEYRELVVSLRVGMEKDRNQLLRELVDVQYGRNDIDFKRGTFRVRGDVVEIFPASLDEHCIRIEFFGDEIDRIREVNALTGEVLAERDHVAIFPASHFVTREEKMKVAIENIEKELEERLKELNDNGKLLEAQRIEQRTRYDLEMMREMGFCSGIENYSRHLTLRPAGATPYTLLDYFPEDFLIVMDESHVSVPQVRAMYNGDQARKQVLVDHGFRLPSALDNRPLTFDEFEEKTNQVIYVSATPGPYELEQSPEVIEQIIRPTGLLDPPIDIRPIEGQIDDLLGEIQDRIAKNERVLITTLTKKMSEDLTDYLKDVGIKVNYLHSEVKTLERIEIIRDLRLGKFDVLVGINLLREGLDIPEVSLVAILDADKEGFLRSERSLIQTIGRAARNENGRVIMYADRITRSMGIAIEETKRRRSIQEAYNEEHGITPKTIQKGVRDVIRATTAAEEPETYEATPAKKMTKKEREKTIAKMEAEMKEAAKALDFERAAELRDLLLELKAEG | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage. | Q6HBC2 |
A8YXI6 | PTH_LACH4 | Peptidyl-tRNA hydrolase | Lactobacillus | MKIIAGLGNPGQKYDKTKHNTGFMTLDHYLNEKGLSLDKDKFEGHWTKQKINGEDVILLEPQTYMNESGRSVSQIANFFKVAPEDVLIIQDDMDMPIGKIRIRANGKSGGHNGIKSIIRDLGTEKFNRLKIGIRHPKNTTVVSWVLTPFNDEQQKLMDDAFDTSVKIIDDFIAGRDSQYLMNKYN | The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. | A8YXI6 |
P0CV49 | RL120_PLAVT | Secreted RxLR effector protein 120 | Plasmopara | MRGAYYVITALLVVASSQTSADSGHRLHVYDHDVVAAENAAAKTLPQQSLRGSRDVPDDLAHEERAIISELVEEGAKLIPRAAENVEEMPRVTEAVGKRPRVAEKDALEKASGADEASKKPRNTATDDAFQGMSTEWELELPFKEWNTEIEPMREMPEPKWSWEKRKLVHEAFVKLCAEDLNPTVYETARLWSLFDGKAKSRPATFHRQVLIQLAKENVRRDVLIMKSVESEWDRWNEVSILSRVDVLNMLLNVHFQRWKRMYNAFGEQRSKLIAL | Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins. | P0CV49 |
B2JI54 | RL24_PARP8 | 50S ribosomal protein L24 | Paraburkholderia | MNKIRKGDEVIVITGKDKGKRGVVLAVGENRVTVEGLNIAKKHVKPNPMKGTTGGVEAKAMPLNISNVALVDANGKPSRVGIKVEGDKKVRFLKTTGAVLSA | One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. | B2JI54 |
P41621 | RBL_PINTH | Ribulose bisphosphate carboxylase large chain | Pinus subgen. Pinus | MSPKTETKASVGFKAGVKDYRLTYYTPEYQTKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYDIEPVPGEETQFIAYVAYPLDLFEEGSVTNLFTSIVGNVFGFKALRALRLEDLRIPPSYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEALNKAQAETGEIKGHYLNATAGTCEEMMKRAIFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQRNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGERDVTLGFVDLLRDDFIEKDRSRGIYFTQDWVSMPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEVIREACKWSPELAAACEIWKEIKFEFDVIDRL | RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | P41621 |
O94418 | MUG87_SCHPO | Meiotically up-regulated gene 87 protein | Schizosaccharomyces | MTVASDDSPKEARGIPFLDQKSRKLANELLEPCLPFIQFNLGEIEQRAKHYLNTVPTSKDGNTKAHYLLAGSGINAEQTWKKIESLSLQVRPPTTLELSFTDVDMFLKYHREKNVLNSLEALVQNTQIAFDQYLEEEWRSKAAKSRPSFDNILLENKKRVSFYPFSVQRSQKFASTLKMCLEEEALHGFQSKLVSSFCEVAREFAHDTKSLLLYESWKLLSSVILDKDSVTVFGNKGIISKAFDIETEDGSVNSRFYQRISDCSRKFLEAQFFEVLNKEIAKTPQAALVGGVPSIRNKIRAYLNIRLLRNGVWINPDLEIIQDVPIWAFIFYLLRCGFLKEAVDFTEENRDLFEKVAEKFPFYINAYAKAPNGILPRQLRSQLFSEFNQTIRLQESSDPYKYAVYKIIGRCDLSKTSCPSICSVTEDYIWFQLILSREFTEKSVSAHEFFSLEDVQHILLSYGSDYFTNNGSNPVMYFFLLMLCGLYERAINFLYPYFPTDAVHFAITCAYYGLLRTAPSSSVVSNEPGKIQSMLVETKSGKPSLEFDRLLIDYTQTCQELSPVMSACYLIPMCKIDKYISMCHKSLCSLVLSTRDYVNLLGDIRGDGERTPSFLENHRSLIGLSSVKEYLSKITLTAAKQADDQGLLSDAILLYHLAEDYDAAVTVINRRLGSALLRFLDQFVFPDKLISLTKSMMDVYNRNPSLYAKVDYKNRETTNLLLLTVEAFNAYTNKDYEQALSSLQQLEILPLDPLDSDCETFVVRKLAKEFRFLNENLLQNVPGIVLIAMNSLKELYAKQKSSSFGNDAISVDKLRLYRQKARRIVMYSFLIEYRMPSQILEQLNRCEIEMT | Has a role in meiosis. | O94418 |
Q873B7 | SPC25_NEUCR | Kinetochore protein 4 | Neurospora | MSRKSVMSSTFEPSLSTSRQPLGPSLADTLPSINFGFDELRDRMAKFTAKFDAFIEQGRKRVLEERNQFRMNVAELQEDQRMKKKDIEILQLKTNTYQQTMAKEAAETREMQAAIASLTEQRDKQAAMRDALKEQIAATQREIDARLAAQRAHAAQLEAQARYNVPELDFWVTNLCMRIEGAGAEDRLKFVYTHIDERNWEREAWFELSMSGRDYDVRHCRPKLEREKVEKVLDRVNETRELVVLLKGMRELFVEAMKS | Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. | Q873B7 |
Q9FMB0 | GL19_ARATH | Putative germin-like protein subfamily 1 member 9 | Arabidopsis | MKSFSFLAVLSILAITLSLSKASDPSSLQDFCVGVNTPADGVFVNGKFCKDPKLVTVEDFFFTGLHEARPPNPKTGSNVTAVNVNNLPGLNTLGISLVRIDYGVYGQNPPHTHPRASEVLYVAVGTLFVGFVTSNPENRLFSKTLYEGDVFVFPQGLIHFQVNVGKYPAVAFAGLSSQNPGVITIADTVFGSNPQIDPSFLASAFQVDPKIVMDLQTKFIKP | May play a role in plant defense. Probably has no oxalate oxidase activity even if the active site is conserved. | Q9FMB0 |
A0KHU1 | RUVC_AERHH | Holliday junction resolvase RuvC | Aeromonas | MSIILGIDPGSRITGYGVIRIVAGKAEYLGSGCIRTDLGELPSRLKQVYDGVSEIITQFKPDEFAIERVFMARNADSALKLGQARGSAIVAAVNALLPVSEYSATQIKQAVVGTGGAAKEQVQHMVTHLLKLSATPQADAADALGVALCHFHTRQILIKMAGRSTGSVRGRYR | 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. | A0KHU1 |
O09108 | LSHB_MOUSE | Luteinizing hormone subunit beta | Mus | MERLQGLLLWLLLSPSVVWASRGPLRPLCRPVNATLAAENEFCPVCITFTTSICAGYCPSMVRVLPAALPPVPQPVCTYRELAFASVRLPGCPPGVDPIVSFPVALSCRCGPCRLSSSDCGGPRTQPMACDLPHLPGLLLL | Promotes spermatogenesis and ovulation by stimulating the testes and ovaries to synthesize steroids. | O09108 |
Q749X2 | QUEA_GEOSL | Queuosine biosynthesis protein QueA | Geobacter | MLVTEFDYHLPPELIAQEPLVQRDATRLMTVERDGGGIGEIPFRGIVDLFRPGDLLVINDTRVIPARLLGRKESGGKTEIFLVRRRPGDHETWHCLIRSSKPPRPGVTVLLPEGVRAVVREPGDGETWLVSFTPGEGFQEWLDRNGAMPLPPYIRREADAADRDRYQTVFARNRGAVAAPTAGLHMTAGLLDEIAGRGVRVAPVTLHVGLGTFMPIRVERLEDHRMHRERYHIPPATADAINGCRREGGRVIALGTTVCRTLEQAAAADGTIAAGEGEADIFIYPGYRFKAVDALITNFHLPKSTLLMLVSAFAGRDLLFRAYGEAVARRFRFFSYGDAMFIF | Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). | Q749X2 |
A6X0C2 | RS19_BRUA4 | 30S ribosomal protein S19 | Brucella | MARSVWKGPFVDGYLLTKAEKVREGGRNEVIKMWSRRSTILPQFVGLTFGVYNGNKHVPVSISEEMVGHKFGEFAPTRTYYGHGADKKSKRK | Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. | A6X0C2 |
A1KUD6 | RLMN_NEIMF | tRNA m2A37 methyltransferase | Neisseria | MKTNLLNYDLQGLTRHFADMGEKPFRAKQVMRWMHQSGAQNFNEMTDLAKSLRHKLNEQAGIEIPKLMMSQKSSDGTRKWLLDVGTGNGVETVFIPESDRGTLCISSQVGCALECTFCSTGRQGFNRNLTAAEIIGQLWWANKAMGVTPKNERVISNVVMMGMGEPMANFDNVVTALSIMLDDHGYGLSRRRVTVSTSGMVPQMDRLRDVMPVALAVSLHASNDEVRNQIVPLNKKYPLKELMAACQRYLVKAPRDFITFEYVMLDGINDKAQHARELIELVKDVPCKFNLIPFNPFPNSGYERSSNENIRVFRDILQQAGFVVTVRKTRGDDIDAACGQLAGQVQDKTRRQQKWQQILIGQQG | Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. | A1KUD6 |
Q7W575 | TPIS_BORPA | Triose-phosphate isomerase | Bordetella | MTTAENRARLVLGNWKMHGNLAENAALLAELRAADAAAHCEMGVCVPFPYLAQTAAALQGSAIGWGAQDVSAHAKGAYTGEVAAPMLAEFGCRWVLVGHSERRTLHAESDQLVADKARAALEAGLTPVVCVGESLQEREGGNTLGVIERQLEPVLALGRDALVRMVLAYEPVWAIGTGRTASPEQAQEVHSAIRVALDGLQASQVRVLYGGSVKGANAASLFAMPDIDGGLVGGASLVAEEFLRIAAA | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | Q7W575 |
Q97N13 | DCDB_CLOAB | DCD-DUT | Clostridium | MILSGKQIKDSLGKDIVIEPFNEKQINPNSYNLKLHNELLVYDEEVLDMKKPNKTKKLIIPEEGIVLEPRKLYLGRTLEYTETDKYVPMLEGRSSIGRLGVFIHVTAGFGDVGFKGYWTLEIFCVEPIRIYSGVEICQIYYHDVGGDYEKYSSGKYQNNKGIQPSLLYKDFIN | Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate. | Q97N13 |
Q17078 | PBP2_ANTPE | APR-2 | Antheraea | MIRKVLLSVLLAVLMTINLGQASPEVMKNLCMNYGKAMDQCKQELNLPDSVIADLYNFWKDDYVMTDRLAGCAINCLSTKLDIVDPDGNLHHGNAKEFAMKHGADDGMAHELVDIIHGCEKSSPPNDDKCIKTMDIAMCFKKEIHKLNWVPNMDLVVGEVLAEV | This major soluble protein in olfactory sensilla of male moths might serve to solubilize the extremely hydrophobic pheromone molecules and to transport pheromone through the aqueous lymph to receptors located on olfactory cilia. | Q17078 |
B7KAE8 | PLAS_GLOC7 | Plastocyanin | Gloeothece citriformis | MLKKLGVLLSAIVLVIASFFVTVTPALAETYTVKMGSDQGLLKFDPPQLTIKAGDTVKWVNNKLAPHNAVFDNSKVPDSVSATKISHKALVFSPGESFTTTFDEPGTYTYYCEPHRGAGMVGTITVE | Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. | B7KAE8 |
B1XHZ7 | ISPG_SYNP2 | 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase | unclassified Synechococcus | MQAVERPVQTTDSLVDTTIHRRKTRAVKVGNVTIGSDYPVVVQSMINEDTLDIEGSVAAIRRLHEIGCEIVRVTVPSMAHARSLAQIKAKLAETYQAVPIVADVHHNGMKIALEVAKHVDKVRINPGLYVFEQASGDRTGYTEAEFAAIGEKIRETLEPLVVSLRDQGKAMRIGVNHGSLAERMLFTYGDTPEGMVESALEFIRICQSLDFHNLIISMKASRVPVMLAAYRLMAKRMDELGMDYPLHLGVTEAGDGEYGRIKSTAGIGTLLAEGIGDTIRVSLTEAPEKEIPVCYSILQALGLRKTMVEYVACPSCGRTLFNLEEVLHKVREATNHLTGLDIAVMGCIVNGPGEMADADYGYVGKTPGVISLYRGREEIRKVPEAQGVEELINLIKADGRWVDPPQ | Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. | B1XHZ7 |
B4F111 | MURG_PROMH | Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase | Proteus | MSERKRRLMVMAGGTGGHVFPGLAVAHYLQSQGWDIRWLGTADRMEAQLVPKHGIEIEYIRISGLRGKGVKALIAAPIRIIKAIFQARRIMKRYQPDAVLGMGGYVSGPGGVAAWSCGIPVVLHEQNGIAGLTNRWLSKIAKRVLQAFPGAFANAPVVGNPVRDDVLALEAPAERLKGREGAVRVLVIGGSQGARILNHTMPVVAGLLGERVTIWHQAGKGSESDTKLRYQNELSKNSVKSEYKVTEFIDDIAQAYQWADVVVCRSGALTVSEIAAAGLPAIFVPFQHKDRQQYWNALPLENAGAARIIEQNDLTPEAIADTLENWDRHQLMLMAEKAQSVAITDATERVANVIIEVAKK | 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). | B4F111 |
A6X1H1 | COBS_BRUA4 | Cobalamin-5'-phosphate synthase | Brucella | MQRNSLIGDTIRSLGFLSRLPLPQRWFEDGDDSLPRNARAFPLAGAVLGLLAGAVLFMAYKVNLPPLACAMLAIGALAAMTGALHEDGLGDTADGFFGASSPDRRLDIMKDSRIGTFAALTLIVFVGLKAALLMTIIDRAGAGYAALALVGCEAASRSGMLAFWHALPSARPGGLSDSVGQPQWETVVCGFGIGLAFLVFTLIPAGGFLSLINALVLATGLLFGFARLCIAKIGGQTGDTLGAAQQIGSVAVLAGLVMAL | Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate. | A6X1H1 |
B2HZM2 | RL3_ACIBC | 50S ribosomal protein L3 | Acinetobacter calcoaceticus/baumannii complex | MHMAIGLVGRKCGMTRIFTDAGVSVPVTVIEVDPNRITQIKTLETDGYQAVQVTTGERRESRVTNAQKGHFAKAGVAAGRLVKEFRVTEAELEGREVGGTIGVDLFTVGQIVDVTGQSKGKGFQGGVKRWNFRTQDATHGNSVSHRVLGSTGQNQTPGRVFKGKKMAGHLGDERVTVQGLEIVSVDTERSVLVVKGAIPGATGGDVIVRPTIKA | 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. | B2HZM2 |
Q63R14 | PHNN_BURPS | Ribose 1,5-bisphosphokinase | pseudomallei group | MSAERLVYVMGPSGAGKDSLLAYARKHVREPRIAFAHRYITRKSDGHENHVELTRDEFAARAQLGFFALEWSSHGFRYGVGVEIDAWLAAGSVVVVSGSRAHLPAALERYPQMCVVHIDAAPHVLAERLATRGRETADEIRARLARSVRWAVPDGVALTAIDNSGTLDDAGRVLVALLEGLARS | Catalyzes the phosphorylation of ribose 1,5-bisphosphate to 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP). | Q63R14 |
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