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 |
|---|---|---|---|---|---|---|
C0ZB86 | RECO_BREBN | Recombination protein O | Brevibacillus | MLVKWEGIVIRSVDYGESSKVVTMFTRENGKLGVMARGAKKTKSRLAAVSQLFSHSYYLCKAGPGTGMPDLSQGDMLDSFRDMRQSLTATAYAAYIAELLDRLTQEREPNPYLFQLLLHTFRHLDEGRDAEILCRIFETKMLIVAGISPQLTACANCGEQREPYAISVGQGGLLCPVCLPSDPYAMAVTPSTWKLLRLFQVFDLERLGDIEVKPATRNQLKHVLRSFMDEYLDLRLKSRSFLEQLERMERMTQSDQD | Involved in DNA repair and RecF pathway recombination. | C0ZB86 |
Q96T53 | MBOA4_HUMAN | Membrane-bound O-acyltransferase domain-containing protein 4 | Homo | MEWLWLFFLHPISFYQGAAFPFALLFNYLCIMDSFSTRARYLFLLTGGGALAVAAMGSYAVLVFTPAVCAVALLCSLAPQQVHRWTFCFQMSWQTLCHLGLHYTEYYLHEPPSVRFCITLSSLMLLTQRVTSLSLDICEGKVKAASGGFRSRSSLSEHVCKALPYFSYLLFFPALLGGSLCSFQRFQARVQGSSALHPRHSFWALSWRGLQILGLECLNVAVSRVVDAGAGLTDCQQFECIYVVWTTAGLFKLTYYSHWILDDSLLHAAGFGPELGQSPGEEGYVPDADIWTLERTHRISVFSRKWNQSTARWLRRLVFQ... | Catalyzes ghrelin acylation at 'Ser-3' using preferentially octanoyl-CoA, hexanoyl-CoA and decanoyl-CoA as acyl-CoA donors leading to ghrelin activity . In vitro uses also acyl-CoA donors of different lengths from short-chain (C2) to long-chain fatty acids (C16) knowing that acyl-CoA donors from butanoyl-CoA (C4) to do... | Q96T53 |
P84272 | DAH56_RANDH | Dahlein-5.6 | Ranoidea | GLLASLGKVFGGYLAEKLKPK | Has no antimicrobial activity. Strongly inhibits the formation of NO by neuronal nitric oxide synthase at micromolar concentrations. | P84272 |
B5RFJ0 | THIC_SALG2 | Thiamine biosynthesis protein ThiC | Salmonella | MSTTTLTRREQRAKAQHFIDTLEGTAFPNSKRIYVTGSQHDIRVPMREIQLSPTLIGGSKDNQQFEENEAVPVYDTSGPYGDPEVAINVQQGLAKLRQPWIDARNDSEELDDRSSAYTRERLADDGLDDLRFTGLLTPKRAKAGKRITQLHYARQGIVTPEMEFIAIRENMGRERICSEVLRHQHPGMSFGARLPENITPEFVRDEVAAGRAIIPANINHPESEPMIIGRNFPVKVNANIGNSAVTSSIEEEVEKLVWSTRWGADTVMDLSTGRYIHETREWILRNSPVPIGTVPIYQALEKVNGIAEDLTWEAFRDTLL... | 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. | B5RFJ0 |
A8MAJ5 | RS8_CALMQ | 30S ribosomal protein S8 | Caldivirga | MVMLDVLSNALMSVKNAESRGDRQVIIWPSSKLIGNVLRVMQRYGYVGEFEYVYDGRGGKYVVQLLGRINDIGAIKPRFHVKVDELQKWEEKYLPARQVGILILTTSKGVVSHLEARENRVGGILVAYVY | 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. | A8MAJ5 |
Q9TR30 | CX7A2_SHEEP | Cytochrome c oxidase subunit VIIa-liver/heart | Ovis | FENKVPEKQKLFQEDNGIPVHLKG | Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CII... | Q9TR30 |
Q4WDA4 | CD123_ASPFU | Cell division cycle protein 123 | Aspergillus subgen. Fumigati | MPLLDPNTQTLAESSAAQPQRLPFPPVTYSHILHCSYHQWQPRYRTLTPKSRAIPLTPSFVSYLRANGIVLPPETTRPHGDDDIDTFSDDGADEESDPSVEWQEIHSQIKSTISEFGGKVTPKLNWSAPKDAVWMSATNDLQCRTPNDIYLLLKSSDFITHDLEHPFDGCVPDPDDSSEAPATQPDIPYYLVLRKYVNFNPSLEFRCFVRNRVLLCMCQRDQNHFDFLFSLRDTLRSRIQAFFDEKLKDTFPDPNFVFDVYIPEPHQRVWLIDINPWADRTDPLLFSWLEILQMKDPIGIKEEDTDAPEESFVRLSLNGA... | Regulates the cell cycle in a nutrient dependent manner. | Q4WDA4 |
A6UP51 | VATE_METVS | V-ATPase subunit E | Methanococcus | MGAEKITSKIMEDAKIQANVILAEAQKEKEALIKKAHEEAEKKKQAILKKGEKDAEMTRNRILAEARLSAKKNSLEERERTIAKAIQKLEEDLVKLPQKDEYKDILLKMIITGVYSVGGGELDLQLNKNDWKLIDDSTLWALEKEMEDRLKKVTVLKKGESLPIIGGCVVKTADKTKVSDNSLEATFERNLDIIRAKIAEMLF | Produces ATP from ADP in the presence of a proton gradient across the membrane. | A6UP51 |
Q2RSE3 | RL13_RHORT | 50S ribosomal protein L13 | Rhodospirillum | MKTYSAKPSEVDRKWYVIDAEGVVLGRLAVIIADLLRGKNKTIYTPHIDTGDHVVVINAEKVHLTGNKAANERFFWHTGHPGGIKSRSLGQIRDGAHPERLIEKAVERMMPRGPLARAQFKKLRVYGGEAHPHDAQQPVVLDVAALNPKNKRSA | 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. | Q2RSE3 |
P44707 | DSBB_HAEIN | Disulfide oxidoreductase | Haemophilus | MLALLKQFSEKRFVWFLLAFSSLALESTALYFQYGMGLQPCVLCVYERLAMIGLFVAGTIALLQPRVFILRLIALALGLFSSIKGLLISFRHLDLQMNPAPWKQCEFIPNFPETLPFHQWFPFIFNPTGSCNESQWSLFGLTMVQWLVVIFSLYVVILTLLLIAQVIKTRKQRRLFN | Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein. | P44707 |
Q9LVJ7 | NFYA6_ARATH | Nuclear transcription factor Y subunit A-6 | Arabidopsis | MQEFHSSKDSLPCPATSWDNSVFTNSNVQGSSSLTDNNTLSLTMEMKQTGFQMQHYDSSSTQSTGGESYSEVASLSEPTNRYGHNIVVTHLSGYKENPENPIGSHSISKVSQDSVVLPIEAASWPLHGNVTPHFNGFLSFPYASQHTVQHPQIRGLVPSRMPLPHNIPENEPIFVNAKQYQAILRRRERRAKLEAQNKLIKVRKPYLHESRHLHALKRVRGSGGRFLNTKKHQESNSSLSPPFLIPPHVFKNSPGKFRQMDISRGGVVSSVSTTSCSDITGNNNDMFQQNPQFRFSGYPSNHHVSVLM | Stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters. | Q9LVJ7 |
Q5XDK8 | SYM_STRP6 | Methionyl-tRNA synthetase | Streptococcus | MKKPFYITTPIYYPSGKLHIGSAYTTIACDVLARYKRLMGHEVFYLTGLDEHGQKIQTKAKEAGITPQTYVDNMAKDVKALWQLLDISYDTFIRTTDDYHEEVVAAVFEKLLAQDDIYLGEYSGWYSVSDEEFFTESQLKEVFRDEDGQVIGGIAPSGHEVEWVSEESYFLRLSKYADRLVAFFKERPDFIQPDGRMNEMVKNFIEPGLEDLAVSRTTFTWGVPVPSDPKHVVYVWIDALLNYATALGYGQANHANFDKFWNGTVFHMVGKDILRFHSIYWPILLMMLDLPMPDRLIAHGWFVMKDGKMSKSKGNVVYPE... | Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | Q5XDK8 |
Q3MA19 | RL11_TRIV2 | 50S ribosomal protein L11 | Trichormus | MAKKVVAVIKLALNAGKANPAPPVGPALGQHGVNIMMFCKEYNAKTADQAGMVIPVEISVYEDRSFTFVLKTPPASVLIRKAAKIERGSNEPNKKKVGTITTAQLREIAQTKLPDLNANDIDAAMKIVAGTARNMGVTVTD | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | Q3MA19 |
Q9D1I5 | MCEE_MOUSE | DL-methylmalonyl-CoA racemase | Mus | MRRVVKAAALAAGATGLFSRVQTSVAIGRSFSTPQSQFQESSPVWKLGRLNHVAVAVPDLEKASSFYRDVLGAQVSEVVPLPEHGVSVVFVNLGNTKMELLHPLGSDSPITGFLQKNKAGGMHHVCIEVDNISAAVMDLKKKKIRSLSDEAKIGAHGKPVIFLHPKDCGGVLVELEQA | Methylmalonyl-CoA epimerase involved in propionyl-CoA metabolism. | Q9D1I5 |
Q01563 | GSPB_DICD3 | General secretion pathway protein B | Dickeya | MKNTPEVKASPQTGYRIPGYLLVVYALLLFTLGWFGHQRWADISPIPLSTSAAAIAAPPTKVGMVPASTAVTADENHPGSLHAAAENSATQTAASGSQTSASSQEATPDTKPAKLVTGWQTAKPGELPYIAFSAHVYTSAPDKRSVTLNGERYREGDSPYQGLVIEQIEQDMVIFSFNGEPFILDSLQDWPGGKPGDDAAQGNEQEPTSKPEQTVRTTKK | Out proteins are required for the translocation of pectate lyases and cellulases across the outer membrane. | Q01563 |
P16563 | CRIS2_MOUSE | Testis-specific protein TPX-1 | Mus | MAWFQVMLFVFALLLRSPLTEGKDPDFTSLLTNQLQVQREIVNKHNELRRSVNPTGSDILKMEWSIQATTNAQKWANKCILEHSSKDDRKINIRCGENLYMSTDPTLWSTVIQSWYNENEDFVYGVGAKPNSAVGHYTQLVWYSSFKIGCGIAYCPNQDNLKYFYVCHYCPMGNNVMKKSTPYQQGTPCASCPNNCENGLCTNSCDFEDLLSNCESLKTSAGCKHELLKTKCQATCLCEDKIH | May regulate some ion channels' activity and therebye regulate calcium fluxes during sperm capacitation. | P16563 |
A1UD96 | NUOI_MYCSK | NDH-1 subunit I | unclassified Mycobacterium | MPKLWDAVAGFAVTFGTLFKKPITEEYPEKPGPVAPRYHGRHQLNRYPDGLEKCIGCELCAWACPADAIYVEGDDNTADERYSPGERYGRVYQINYLRCIGCGLCIEACPTRALTMTNDYEMADDNRADLIWGKDKLLAPLQDGMLAPPHPMAPGATDDDYYLGRIGPATEDVR | 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 menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are ... | A1UD96 |
Q6FW42 | DRS1_CANGA | ATP-dependent RNA helicase DRS1 | Nakaseomyces/Candida clade | MSLKMKGKKYTDLDFVPTISDSEEDVPDLDSDEEKPKPETKGKKKNKSVDEESADMNSGFRFNTDDGEINTNFDGWEFLGDEKDEEKKDVDLDKIIRKKGGLIGMAHVDEAEKSESEESESDDEDLAMDGFGMGAQEQPEGEEEDEDASNSEQESNDEEEDDDEETYDVGDAGDAEEKVEEDTAEEMQAFYAPESESENAKKEVHKTFNDLALSRPVMKGLSNLGYVKPSPIQSATIPIALLGKDIIAGAVTGSGKTAAFMIPIIERLLYKPAKVASTRVIVLTPTRELAIQVADVGKKIGQFVSNLTFGLAVGGLNLRQ... | ATP-binding RNA helicase involved in ribosome assembly. | Q6FW42 |
A9MHF3 | RL7_SALAR | 50S ribosomal protein L7/L12 | Salmonella | MSITKDQIIEAVAAMSVMDVVELITAMEEKFGVSAAAAVAVAGAGAAAEAAEEKTEFDVILKAAGANKVAVIKAVRGATGLGLKEAKDLVESAPAALKEGVSKDDAEALKKSLEEAGAEVEVK | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation. | A9MHF3 |
B7M0I6 | RSXC_ECO8A | Rsx electron transport complex subunit C | Escherichia | MLKLFSAFRKNKIWDFNGGIHPPEMKTQSNGTPLRQVPLAQRFVIPLKQHIGAEGELCVSVGDKVLRGQPLTRGRGKMLPVHAPTSGTVTAIAPHSTAHPSALAELSVIIDADGEDCWIPRDGWADYRTRSREELIERIHQFGVAGLGGAGFPTGVKLQGGGDKIETLIINAAECEPYITADDRLMQDCAAQVVEGIRILAHILQPREILIGIEDNKPQAISMLRAVLADSNDISLRVIPTKYPSGGAKQLTYILTGKQVPHGGRSSDIGVLMQNVGTAYAVKRAVIDGEPITERVVTLTGEAIARPGNVWARLGTPVRH... | Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR. | B7M0I6 |
Q9KWS6 | DNAJ_PARTM | Chaperone protein DnaJ | Parageobacillus | MAKRDYYEILGVSKNATKEEIKKAYRKLSKKYHPDINKEPDAAEKFKEIKEAYEVLSDDQKRAHYDQFGHADPNQGFGGFRSDDFDFGGFSGFSGFDDIFSTFFGGGRRRDPNAPRAGADLQYTMTLTFEEAVFGKETDIEIPREETCNTCHGTGAKPGTKKETCSYCHGTGQISTEQSTPFGRIVNRRTCPYCGGTGQYIKERCTTCGGTGRVKRRKKIHVKIPAGIDDGQQLRVAGQGEPGINGGPPGDLYIVFHVEPHEFFERDGDDIYCEIPLTFAQAALGDEIEVPTLHGKVRLKIPAGTQTGTKFRLKGKGVPN... | Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bou... | Q9KWS6 |
Q9Z1P6 | NDUA7_MOUSE | NADH-ubiquinone oxidoreductase subunit B14.5a | Mus | MASATRVIQKLRNWASGQDLQAKLQLRYQEIAKRTQPPPKLPVGPSHKLSNNYYCTRDGRREVVPPSIIMSSQKALVSGKAAESSAMAATEKKAVTPAPPMKRWELSKDQPYL | 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. | Q9Z1P6 |
B4S817 | HSLV_PROA2 | ATP-dependent protease subunit HslV | Prosthecochloris | MNRSEKPQLRATTVLGVIRNGKAALGSDGQMTLGNTVIKHSTKKIRRIQHANLITGFAGATADAVTLLDRFDEKLQAFGGQLERSAVELARDWRTDKYLRRLEAMLAVVSADKALIISGTGDVIEPEDGIVAIGSGSMYALSAARALIRYTDLSAREIVTESLKIAADICIYTNDHIVVEEV | Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | B4S817 |
E9Q8Q8 | SACA6_MOUSE | Sperm acrosome membrane-associated protein 6 | Mus | MTSQRSLSSPQTRRPSVMGLISLVGSIVLLFLLIFRASTWACLFCFTTYEERLRVCQLFVGREETKINLCRNELEGAFEDLKDMKINYDERSYLHDEFTQMTVSLQEKAARRREPFWLAFKDAAAKLKRTIEHLKKAPACIPPCGLQEVARLFHCSGCFSKLCDLPLDCPVQDMLVNRGDQALFSCIVAFELPESEITYSWKFVGGVRTKDVTYFRDMPGAHGYLARIRPVQPKHGGTFSCVILHDQRPLARLYFYLNVTGPPPPEDTELQVTFREVMNRTPAEPEMIQPWSPSLGELLTNPQALTLGNLFLLAATAALG... | Sperm protein required for fusion of sperm with the egg membrane during fertilization. | E9Q8Q8 |
P81377 | KAP1_RAT | cAMP-dependent protein kinase type I-beta regulatory subunit | Rattus | MASPSCFHSEDEDSLKGCEMYVQKHGIQQVLKECIVHLCVAKPDRPLRFLREHFEKLEKEENRQILARQKSNSQCDSHDEEISPTPPNPVVKARRRRGGVSAEVYTEEDAVSYVRKVIPKDYKTMTALAKAISKNVLFSHLDDNERSDIFDAMFPVTHIDGETVIQQGNEGDNFYVIDQGEVDVYVNGEWVTNISEGGSFGELALIYGTPRAATVKAKTDLKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLQRRSPNEEYVEVGRLGP... | Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. | P81377 |
C1D6I2 | DNAA_LARHH | Chromosomal replication initiator protein DnaA | Laribacter | MTDLSAFWPQCLARFEAELSAQQFNTWIKPLVCVAGEDAIALYAANRFSLGFVKERFLSRIETFAEDILGRPVTIELRIGGAQAGASAPAAASPRSPGRPAPAPVAATPTTGSLADSIVSDVPLPNVKLTAPKPAIGGGHESTRLNPAFTFESLVTGKGNQLARAAALQIADNPGDSTYNPFFVYGGVGLGKTHLIQAIGNHVYQKNPQAKIRYIHAERYVADIMRAYQHKAFDEFKRYYHSLDLLLIDDIQFFAGKNRTMEEFFYAFNALLEGGKQVIMTCDSYPKQIEGMDERLISRFSWGLTVEIQPPELEMRVAIL... | Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. | C1D6I2 |
Q8NX83 | PT1_STAAW | Phosphotransferase system, enzyme I | Staphylococcus | MSKLIKGIAASDGVAIAKAYLLVEPDLTFDKNEKVTDVEGEVAKFNSAIEASKVELTKIRNNAEVQLGADKAAIFDAHLLVLDDPELIQPIQDKIKNENANAATALTDVTTQFVTIFESMDNEYMKERAADIRDVSKRVLSHILGVELPNPSMIDESVVIVGNDLTPSDTAQLNKEFVQGFATNIGGRTSHSAIMSRSLEIPAIVGTKSITQEVKQGDMIIVDGLNGDVIVNPTEDELIAYQDKRERYFADKKELQKLRDADTVTVDGVHAELAANIGTPNDLPGVIENGAQGIGLYRTEFLYMGRDQMPTEEEQFEAYK... | General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phos... | Q8NX83 |
P9WMA8 | DATIN_MYCTO | Dormancy associated translation inhibitor | Mycobacterium tuberculosis complex | MEPKRSRLVVCAPEPSHAREFPDVAVFSGGRANASQAERLARAVGRVLADRGVTGGARVRLTMANCADGPTLVQINLQVGDTPLRAQAATAGIDDLRPALIRLDRQIVRASAQWCPRPWPDRPRRRLTTPAEALVTRRKPVVLRRATPLQAIAAMDAMDYDVHLFTDAETGEDAVVYRAGPSGLRLARQHHVFPPGWSRCRAPAGPPVPLIVNSRPTPVLTEAAAVDRAREHGLPFLFFTDQATGRGQLLYSRYDGNLGLITPTGDGVADGLA | Involved in translation regulation. Can also stimulate macrophages and peripheral blood mononuclear cells (PBMC) to secrete important cytokines that may be significant in granuloma formation and its maintenance. Increases secretion of IFN-gamma, TNF-alpha, IL-1 beta and IL-8 through human Toll-like receptor 2 (TLR2) si... | P9WMA8 |
C7Z638 | MTNA_FUSV7 | Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein | Fusarium vanettenii | MSTLQAVKYIRGKLEVLDQLRLPHEFHYDEVSNRTEAFDSIYTMRVRGAPAIAIVAALGLAVELHNGSCTASSAEETIGQIEEALDYLKESRPTAVDLTNAINQLKARIREVGSTATKEAIISAFIEEAEKIFEKDLKTNLSIGDFGAEWLRAQVGASPEQQISVLTHCNTGSLATSGHGTALGIIRTLQAKKLLHHAFCTETRPYNQGSRLTAFELVFEGIPSTLITDSMAASLFRTRKQEKNIAAVIVGADRVVRNGDTANKIGTYQLAVLAKHHGVKFIVAAPTTSIDLETETGDGIKIEERKKEELTQVTGAVIKP... | Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). | C7Z638 |
Q32BC5 | MTGA_SHIDS | Peptidoglycan glycosyltransferase MtgA | Shigella | MSKSRLTVFSFVRRFLLRLMVVLAVFWGGGIALFSVAPVPFSAVMVERQVSAWLHGNFRYVAHSDWVSMDQISPWMGLAVIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLTLGIETVWSKKRILTVYLNIAEFGDGVFGVEAAAQRYFHKPASKLTRSEAALLAAVLPNPLRFKVSAPSGYVRSRQAWILRQMYQLGGEPFMQQHQLD | Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors. | Q32BC5 |
A7IAU6 | VATD_METB6 | V-ATPase subunit D | Methanoregula | MALRDIKPTRSELINLKRKIQLSQRGYKILKMKRDGLIMEFFKILSEAKDSRGELLRRYKHAVEMMAVANTVEGALGVKAAAFSVKETPEITLKSKNIMGVVVPEIESSKVKKTLADRGYGVLGTSPVIDETASSFEDLVEAIIESAEIETTMKRLLDEIEKTKRRVNALEFKVIPELTEARDFIKMRLDEMEREELFRMKKIKARGSS | Produces ATP from ADP in the presence of a proton gradient across the membrane. | A7IAU6 |
Q8EBS1 | SYA_SHEON | Alanyl-tRNA synthetase | Shewanella | MYQTTAALRSAFLEFFRSNGHQVVDSSSLVPGNDPTLLFTNAGMNQFKDVFLGMDKRSYTRATTAQRCVRAGGKHNDLDNVGYTARHHTFFEMLGNFSFGDYFKEDAIRFGWTFLTEVLMLPKERLCVTIYQTDDEAFEIWNKKIGVAAENIIRIGDNKGAPYASDNFWQMGDTGPCGPCTEIFYDHGDHIWGGRPGSPEEDGDRFIEIWNIVFMQYNRQASGEMLPLPKPSVDTGMGIERIAAIMQGVHSNYEIDIFRALIAKAAEIIGVADLSNKSLRVIADHIRSCAFLVADGVMPSNEGRGYVLRRIIRRAVRHGN... | 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. | Q8EBS1 |
Q8YHU3 | CBID_BRUME | Cobalt-precorrin-6A synthase | Brucella | MNDETTPANKNPEKAELRCGWTTGACATAATKAALTALITGEFPDPVGIILPKGEVPYFQLAYEGLGEGYAMAGIVKDAGDDPDVTHGATIISTVYPAPPGTGIIFRAGEGVGTVTREGLAIPPPGEAAINPVPRRMMTEICEAICAEYGLPADLVITISVPGGEEIAQKTWNPRLGIIGGISILGTTGVVHPFSCSAWIHSIHRGIDVARAAGQKHVLGATGSTSEDAAQALYNLPDFAILDMGDFAGGVLKYLREHPIDRLTIAGGFAKLTKLAQGALDLHSSRSQVDKGFLWQIAERAGAPADMKERILLANTAMEV... | Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A. | Q8YHU3 |
Q9V2N1 | COBS_PYRAB | Cobalamin-5'-phosphate synthase | Pyrococcus | MRNILPFLTRIPVKGDFEKARNELWAFPLVSLVSSIIPIAILYLRIPLANVLALLSLYFVIGLLHLDGLADWADGIMVKGDRERKIKAMKDLNTGIAGVFAVVVVLFLQVYSLSMLPFYAIYIAELNSKFSMLLGLATKKPLGQGLGAYFMEGMNGRQLAIGVVLYVLLYLPVVIYDPSALFGVMGLVFAWYVIRLSLENFGGINGDCLGAMAEITRAGTLVILSFSLCFTT | Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate. | Q9V2N1 |
P02600 | MYL1_RAT | Myosin light chain alkali 1/2 | Rattus | MAPKKDVKKPAAAAPAPAPAPAPAPAKPKEEKIDLSAIKIEFSKEQQEEFKEAFLLFDRTGECKITLSQVGDVLRALGTNPTNAEVKKVLGNPSNEEMNAKKIEFEQFLPMMQAISNNKDQGGYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALLAGQEDSNGCINYEAFVKHIMSV | Non-regulatory myosin light chain required for proper formation and/or maintenance of myofibers, and thus appropriate muscle function. | P02600 |
Q5P0Z8 | OTC_AROAE | Ornithine carbamoyltransferase | Aromatoleum | MTKPRHYLQFKDFTRDDYRHVFDRTRWIKDKFKRYEPYHPLFDRTLVMIFEKASTRTRLSFEAGMQQLGGSAIYLNTRDSQLGRGEPVEDAAQVISRMSDVVMIRTFEQDIIERFAAHSRVPVINGLTNEYHPCQILADIYTFIEHRGSIQGRTVAWVGDSNNMCNTWLQAAELLDFNVHVSTPPGYEVEPERAGLYGTGHFEQFADPMEACKGADLVTTDVWTSMGFEAENDERMKDFADWCVDAEMMAAARADAVFMHCLPAHRGEEVTADVIDGAQSVVWDEAENRLHVQKALMEYLVLGKVED | Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. | Q5P0Z8 |
Q81D33 | DDLA_BACCR | D-alanylalanine synthetase A | Bacillus cereus group | MLLWAGYASEKQVSIMTGNEMIAHLDKNKYEIVPITLNEKMDLIEKAKDIDFALLALHGKYGEDGTVQGTLESLGIPYSGSNMLSSSICMDKNISKKILRYEGVETPDWIELTKMEDLNLDELDKLGFPLVVKPNSGGSSVGVKIVYNKNELISMLETVFEWDSEVVIEKYIKGDEITCSILDGKQLPIVSIRHAAEFFDYNAKYDDTSTVEEVIELPAQIKERVNKASLTCYKALKCSVYARVDMMVKDGIPYVMEINTLPGMTQSSLLPKSAEAAGISYSKLLDMIIETSLKVRNEEGF | Cell wall formation. | Q81D33 |
O27129 | RS12_METTH | 30S ribosomal protein S12 | Methanothermobacter | MPGLFAAKKLKSKRQKFKWKDTHYKRRSLRLDVKADPLEGAPQARGIVIEKVGIEAKQPNSAIRKCVRVQLIKNGKQITAFAPGDGAIGFIDEHDEVVVEGIGGPSGRSMGDIPGVRWKVTKVNNVSLQEMVKGKIEKPVR | With S4 and S5 plays an important role in translational accuracy. Located at the interface of the 30S and 50S subunits. | O27129 |
B3DWG1 | HYPA_METI4 | Hydrogenase maturation factor HypA | Methylacidiphilum | MHELSLCESLVSLLEEEMQKLGCGALKKVVLQVGPLALIEEGAMRFAFEVASKGTVVEGAELFIEWIAVRGYCLDCQKEALVYKIGESCPCCGGVMILSEEGKDLKVASIEVE | Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. | B3DWG1 |
A6L028 | RIMP_PHOV8 | Ribosome maturation factor RimP | Phocaeicola | MIDKNVVTRIVDEWLEGKDYFLVDVTVSPDDKIVVEIDHAEGVWIDDCVELSRYIESKLDREEEDYELEVGSAGIGQPFKVLQQYLIHIGKEVEILTKEGKKLEGVLKDANEENFTVTIEKKVKPEGAKRPKLVEEDITFAYDEIKYTKYLISFK | Required for maturation of 30S ribosomal subunits. | A6L028 |
Q5E7A2 | SYDP_ALIF1 | Protein Syd | Aliivibrio | MPLSVEQALANFSQRYVEAWKAQHDCLPINEELVGLASPCIEETRDLEISWQPIVRDEAIRLHNIEQGIELDLHDDFHAFYGTQYSADMTAKFEDMNIELLQVWSDEDLERLQGNMLGHLVMQRRLKLVPTLFVAVTDDEMEVVSICNQSGEVILDRVGTKNRTVLAANMAEFLNKLEPVIAA | Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function. | Q5E7A2 |
A9WIN9 | COBQ_CHLAA | Cobyric acid synthase | Chloroflexus | MQAPVLMVVGTASSVGKSTLVTALCRLAYRRGLRVAPFKAQNMSNNAAVTADGKEIARSTAVQAAAAGIAPTVAMNPILIKPEGQRRSQIIVEGRPWQSLTATDFWQRKAQLWSVVTRNLDHLRATYDLVIAEGAGSPVELNLKPGDIVNMRVARYAQAQTILVGDIDRGGIFAQLLGTLMLLEPEERQLITGCIVNRFRGDPSLFADGVTILEERSGLPVLGVIPWLDDLGLPEEDAVALEQPPVAPAHGLIIAVIRLPTIANFDDFDPLAREPGVVVRYIDHPLELTGAAAVILPGVKHTLAARHWLHERGFDNALRE... | Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. | A9WIN9 |
A3CV35 | PAN_METMJ | Proteasome regulatory particle | Methanoculleus | MGDIARQAPDKDTGEDIYQYLLERITNLENRNLELREQFRQMESEKRYVETQKIRYERELRKLKSEIEQLRSPPLVIGTVTDVIDNSRVIVRSSAGPRFLVRTSQLIDPDLLKPGVRCTLNQQSLAIVDVLPTSYDAQIYGMELVESPEETYENIGGLEPQIEEIREAVELPLTKPQLFEKVGISPPKGVLLYGPPGTGKTLLARAVAHQTNAHFLRVVGSELVQKYIGEGARLVRELFDLAKQRAPSIIFIDEIDAIGAHRNDSTTSGDREVQRTLMQLLAEMDGFDNRGDVKIVAATNRIDILDRALLRPGRFDRMIE... | ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. ... | A3CV35 |
A1AV04 | UPPP_PELPD | Undecaprenyl pyrophosphate phosphatase | Pelobacter | MNLLHALILGALQGVTEVLPISSSAHLILVPWLLGWPESGLTFDVALHLGTFLALVVYFRRDIVDMAVSTIDAVKHRSLDTPARRLPFLVIASAVPAALVGKLFETQIEELFRSRPLLIGLFLILFGVGLGLADLFGRKRRFMAQVTVSHALVIGLFQCLALIPGVSRSGITITAGLMLGFNRVGAARFSFLMSLPIVAGAALFKMLHLLDQGIPAGEGLPLAAGIVSSAVTGYISVAFLLRFVQKRSIAPFVWYRLIAGGAVVSVILTGISG | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | A1AV04 |
Q68XI5 | RECN_RICTY | Recombination protein N | typhus group | MFYSLSVKNFILIDELEIEFNKGLCVITGETGAGKSILLDAILFCLGYKTSNNVIKHGKDYTVVNIIFSLNDEIKKFLIQNFIEPEELLLVKCLQKVEGRKNFFINNQIVTKTLMKQLANYLFELHGQNNNITLLEASTQRDILDSYGNLLEFRVQLAKCYQIWQNTRKEIEEITVKQNEIEQEIDYLSFVTEELTKLNIQIGEEETLTNIRKDLQNKGKNLQLIRDIIAEINNPEINISINRACKLLARQDYNDRFNAVVTSLEEAYNNLEVARQELSNILGSFTYEEYNLEETEERLFLIKAISRKYNVPANELGIFL... | May be involved in recombinational repair of damaged DNA. | Q68XI5 |
B3DQN2 | MURC_BIFLD | UDP-N-acetylmuramoyl-L-alanine synthetase | Bifidobacterium | MSQDQPIVLDPTYASFDAAARPADLGATHFIGIGGAGMSVLAEMLHAEGVAVDGSDRAHSAKTDRLETLGITVEFGQRAENVAQAETVVYSSAIKPDNPEIVAAHAAGKRIVHRSDILALLMNGKRAVTVAGAHGKTTTSSMLSHILVNAGADPSYAIGGFIQGPDGTTLDGGHAGKGDILVAEADESDGSFAKYHPTIAIITNCEADHLDHYGDEAHYRAAFVAHAGRATGHVIISIDDPDGLAVLEALPADVKSHTVAYGTTARESLPDLGGAAYVWIASESETAGSGVEQLTLHLPAAVTAGEPVSQSVALKVPGVH... | Cell wall formation. | B3DQN2 |
Q12MQ7 | SEQA_SHEDO | Negative modulator of initiation of replication | Shewanella | MKYIEVDEELYRFIASKTERIGESASDILRRLLTLPVDTVTPFEPNAIDEPSLDVAHHQASNFAASNQEQQTGHGHAGEPSAVQTPESNDYAKAQPHSSGYQPGQLEGHKSEPQTLAQLNSQPLAVGQSSQSATSQVDFNALVNEHLLSQQKGAVGRFMWLLEGLAALAPSQFNKVLLVQGKGRLYFARSKDELLASSASANPKEIGTTGYWVTTNNNTAKKQAILVEVLTKLHCDETLASAIADRICDKVAG | Negative regulator of replication initiation, which contributes to regulation of DNA replication and ensures that replication initiation occurs exactly once per chromosome per cell cycle. Binds to pairs of hemimethylated GATC sequences in the oriC region, thus preventing assembly of replication proteins and re-initiati... | Q12MQ7 |
Q07ZQ7 | AROC_SHEFN | 5-enolpyruvylshikimate-3-phosphate phospholyase | Shewanella | MSGNSIGQNFVVTTFGESHGVALGCIIDGCPPGLELTVEDMQHDLDRRRPGTSRYTTARREADEVRILSGVFEGKTTGTSIGLLIENTDQRSQDYSDIKDTFRPGHADYTYQQKYGMRDYRGGGRSSARETAMRVAAGAVAKKYLKQVHGIEIHGYLAQLGPISADTIDLTQIEQNAFFFPDASKLEALDEYMRGLRKSGDSIGAKITVAATGVPVGLGEPVFDRLDADIAHALMGINAVKGVEIGDGFGVVTQKGSQGRDLMSPQGFASNHAGGVLGGISSGQPVVAHIALKPTSSISVPGQSMTVQGETIDMITKGRH... | 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... | Q07ZQ7 |
A0A2H5AIY2 | TYDC2_NARPS | Tyrosine decarboxylase 2 | Narcissus | MEESLKPMDAEQLRENAHKMVDFIADYYKSIESFPVLSQVKPGYLRDLLPDSAPDHPESLEDVLEDIRQKIVPGVTHWQSPNYFAYYPSNSSVAGFLGEMISAGFNIVGFNWIASPAATELEVIVLDWLAKMLNLPNQFLSSGQGGGVIQGTASEANLVVLLAARDKFLNRFGKRSLEKLVVYASDQTHAAMKKACQIAGIYPENFRVLNADHTSNYALVPEALSDAISNDLSAGLIPFFLCATVGTTSSAAVDPLSELGKISKVNDMWFHVDAAYAGSACICPEYRHYIDGIEEAASFNMNAHKWFLTNFDCSLLWIKD... | Catalyzes the decarboxylation of L-tyrosine to tyramine, which is converted to norbelladine, a precursor to all Amaryllidaceae alkaloids such as galanthamine, lycorine and haemanthamine, and including haemanthamine- and crinamine-type alkaloids, promising anticancer agents. | A0A2H5AIY2 |
B9JZ26 | LGT_AGRVS | Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase | Agrobacterium | MNTVASLFAILPYPQIDPIALSIGPVAIRWYGLAYVTGILIGWWLARRMIANLSLWPGNTTPITEKHLDDFLVWAAIGIVLGGRIGYILFYDLQPVLDNPLVALEIWRGGMSFHGGLTGATLAMIVFARRNGLPVWMLFDLVACVAPIGLFFGRIANFINGELWGRVSDVAWAMQFPTGGPFTRHPSQLYEAALEGLVLFVLLQVLARQFHALKTSGVISGVFICGYALARIFVEFFREPDEQLGYLVGGWLTMGMLLSLPMLALGLWAIWRARRAGRSQEPSGLKG | Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins. | B9JZ26 |
Q9LY41 | ATL4_ARATH | RING-type E3 ubiquitin transferase ATL4 | Arabidopsis | MESLINPSHGGGNYDSHSSSLDSLKPSVLVIILILLMTLLISVSICFLLRCLNRCSHRSVLPLSSSSSVATVTSDSRRFSGHRVSPETERSSVLDSLPIFKFSSVTRRSSSMNSGDCAVCLSKFEPEDQLRLLPLCCHAFHADCIDIWLVSNQTCPLCRSPLFASESDLMKSLAVVGSNNGGGENSFRLEIGSISRRRQTPIPESVEQHRTYSIGSFDYIVDDVDSEISESNFNRGKQEDATTTTATATAVTTNPTSFEASLAADIGNDGSRSWLKDYVDRLSRGISSRAMSFRSSGRFFTGSSRRSEELTVMDLEANHA... | E3 ubiquitin-protein ligase able to catalyze polyubiquitination with ubiquitin-conjugating enzyme E2 UBC8 in vitro. | Q9LY41 |
P68250 | 1433B_BOVIN | 14-3-3 protein beta/alpha, N-terminally processed | Bos | MTMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTERNEKKQQMGKEYREKIEAELQDICNDVLQLLDKYLIPNATQPESKVFYLKMKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGDEGDAGEGEN | Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negative regu... | P68250 |
A9L543 | AC4CH_SHEB9 | N(4)-acetylcytidine amidohydrolase | Shewanella | MLLNKITFFERFEHDILSGAKTITLRDEAESHVIVGQILPVSTFETERWFCDIQIIDVTPVKLTELTEVHAKQENMTLPQLRDVIAEIYPGLEQLFMIRFRILSQ | Catalyzes the hydrolysis of N(4)-acetylcytidine (ac4C). | A9L543 |
Q67N85 | TDH_SYMTH | L-threonine 3-dehydrogenase | Symbiobacterium | MAETMRALRKLEAGPGATLQEVPIPTIGPRDVLVKVRAASICGTDYHIYTWDPWSAGRVKPPLTIGHELAGEVVAVGREVTACKVGDYVSAETHIVCNRCPRCHMGEYHLCENTKILGVDTDGAFAEYVAVPEQNIWVNDKDIPFELQSIQEPLGNAVHTALNGDLTARSVLITGCGPIGIMSVPVAKMAGAEIVMAMDINEYRLQLAGQLGADVLINPTKQDPVEVVRSYTRGYGADVVLEMSGNPTAIRQGLKAARNGARISLLGLPGRPLELDLAADVIMRGLVLQGITGRRMWQTWYQVRSLYRAGLAERLRPLVT... | Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate. | Q67N85 |
Q09715 | TUP11_SCHPO | Transcriptional repressor tup11 | Schizosaccharomyces | MASVEDATKVQEMLDALKAEYNALAHHSFASKARGNDYESSMIQSQIQEIEAFRKTVDDMYEKQKSIRETYEKDINKLKRELEELGVEANTASYRNRGERSELAASNNQVTHIDQEHPSQTKSTSQPPSNHLPAFQQIPPIHQSAYPQNNVAEVLMPPIPPSVEASSGQNFNQGIASQNPAISTSNLPSTTPLYIPPVNYGANQVSQQPNPQLPGVSNYYNPSATSKPAVNVQPPRIPTKATPSAEPSMTASANAGSISQAGPDGEYQGREQIAPVSDTEAARKTTSQSWYVTYNPACKRVFNINLVHTLEHPSVVCCVK... | Transcriptional repressor. | Q09715 |
A4WUM8 | ATPG_CERS5 | F-ATPase gamma subunit | Cereibacter | MPSLKDLKNRIGSVKNTRKITKAMQMVAAAKLRRAQEAAEAARPFAERMTAVMTGLAGSVGSSESAPRLLAGTGSDKVQLLVVMTAERGLCGGFNSSIVRLARAHAAKLLAEGKTVKILTVGKKGREQLRRDLGQHFIGHVDLSEVKRMGYPVAQGIARDVLDRFDKGEFDVATIFFARFQSVISQIPTAQQVIPAVFEGEGEVNSLYDYEPSEEGVLADLLPRGVATQIFTALLENGASEQGARMSAMDNATRNAGDMINRLTIQYNRSRQAAITKELIEIISGAEAL | Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. | A4WUM8 |
Q94FA5 | METK4_BRAJU | Methionine adenosyltransferase 4 | Brassica | METFLFTSESVNEGHPDKLCDQVSDAILDACLEQDPESKVACETCTKTNMVMVFGEITTSAKVDYEKIVRSTCREIGFISADVGLDADKCNVLVNIEQQSPDIAQGVHGHLTKKPEDIGAGDQGHMFGYATDETPELMPLTHVLATKLGAKLTEVRKNKTCPWLRPDGKTQVTVEYKNEGGAMIPIRVHTVLISTQHDETVTNDEIAVDLKEHVIKPVIPAKYLDENTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSVVATGLARRCIVQVSYAIGVPEPLSVFV... | Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate. | Q94FA5 |
Q39F31 | DAPE_BURL3 | N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase | Burkholderia cepacia complex | MSATLALTEQLIARASVTPDDQHCQQIMTERLTALGFECETIASHGVTNLWAVKRGTDGRDGKLLAFAGHTDVVPTGPLEQWSSPPFIPAHRDGKLYGRGAADMKTSLAAFVVASEEFVAAHPGHRGTIAFLITSDEEGPATDGTVKVVELLEARGERMDYCIVGEPTSTTELGDVVKNGRRGSMSGELVVKGVQGHIAYPHLAKNPIHLLAPALAELAAEQWDEGNEYFPPTTWQVSNLHAGTGASNVIPGHADLLFNFRFSTASTVEGLQARVHAILDKHGLEYTLKWSVSGLPFLTPRGELSGALENAIRTETGITT... | Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls. | Q39F31 |
Q60764 | MKRN3_MOUSE | Zinc finger protein 127 | Mus | MEESTAPIEAHAAAGAEAGAEGGEGVSVPPPPQFEAAGASAGVSSAPLQQASGLAPLLVTPGPAIRRAASLRPAPAEGGGARSGPERNSGSWTKQILCRYYLHGQCKEGDNCRYSHDLSGRRRSRGGQDAQPRASADRGPKMATRWEPPTQEVAEAPPAASSSSLPLIGSAAERGFTEAEIDNAGIRSAAERGFSEAEIDNASLAAGAAAGAGAEGWEGAIEFVPGQPYRGRMVPPHGPEAPLQSPAIEREHMAMGMGMPMPVPMPMPVPMPVPMPLPLCRYAARGQCLRGDRCAYPHGEICDMCGQQALHPWDAAQQEA... | E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. | Q60764 |
Q14L37 | DNLJ_SPICI | Polydeoxyribonucleotide synthase [NAD(+)] | Spiroplasma | MTFEQAKKRSLVLKEQLEKWNYEYYVNDNPSVSDQEYDRALQELIAIEQQYSELITIDSPTQRVSGQISEKFNKYVHTSPMLSLGNAFNYDDLIHFDEQIKEFTALPEIEYTCELKIDGLSISLVYDNHVLVMGATRGDGLTGEDVTINIKQIKSIPLRIDQPTLIVRGEVYLSVEEFNKINEERVKNGEFKFANPRNAAAGTLRQLDSTIVAKRKLNAFLYYYVNALQDGIQSQYEALQRLEQLKFKINPEYRYCSNIAAVWAYIQEYEPKRNQLGYEIDGIVIKVNNLNLYNRIGYTAKNPKWAIAYKFPAEVVVTKL... | DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. | Q14L37 |
Q06J19 | RPOC2_BIGNA | Plastid-encoded RNA polymerase subunit beta'' | Bigelowiella | MEKIFFNYPFNKGKLKTLLIWSILNTGQYNMINLVENLKKVGFQYATTAGISLGIDDLKTISTKYDLIEKTNDNIKDITNHLNLAVLNEVEHSQKLINSWQKISEILKININKKFKTVNKLNPIYMMAFSGARGNISQVRQLIGMRGLMADPNGQIIHLPIKSNFREGLTVTEYLISCYGARKGVVDTALRTATAGYLTRRLVDTAQHVIISQLDCGTKQGIFLSNLYQGTDILLALKDQLYGRVLGKDIKINSLMYLKNQQIDDSLSILLANHLKRVFIRSPLTCKASNSTLCQLCYGWNLSHSKLISLGEIVGVIAAQ... | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Q06J19 |
Q9V2W8 | FLAB4_THEKO | Flagellin B4 | Thermococcus | MRRRGAIGIGTLIVFIAMVLVAAVAAGVIIGTAGYLEQKAQAAGRQTTQEVASGIKVLNVYGYTNATPPSNGTIERMAIFITPNAGSEGIDLSNVKIVLSDGRRLVVYNYSGSFQNAESVKDLFNMTYVGVWNSTNGTASFGIAVINDIGSEMQGTHPTLEFGDMVALCVWTTMFEYEDKDGIGPSTRITGKVIPERGAAGVLDFTTPATFSYNVMVLQ | Flagellin is the subunit protein which polymerizes to form the filaments of archaeal flagella. | Q9V2W8 |
Q9KMU6 | PRTV_VIBCH | 18 kDa metalloprotease PrtV | Vibrio | MKTIKKTLLAAAIASFFSSGLYAQTPIDLGVVNEDKLIEMLVRTGQIPADASDVDKRIALERYLEEKIRSGFKGDAQFGKKALEQRAKILKVIDKQKGPHKARVFALDVGQKRTDKVLALLIDFPDLPWDDNRLTKEHTEMLYDRYEPSHYQDLLFSDKGYTGPNGENFISMRQYYESESGNSYSVSGQAAGWYRASKNAAYYGGNSPGTNNDMNARELVREALDQLARDPNINLADYDIEDRYDYNGNGNFREPDGVIDHLMIFHASVGEEAGGGVLGADAIWSHRFNLGRYHVLEGTKSNVPGRFNGQFAAFDYTIQP... | Metalloprotease that exhibits a cytotoxic effect leading to cell death. In host tissues, it could play a role in pathogenesis by modulating the stability of the extracellular matrix components such as fibronectin and fibrinogen. Also able to cleave plasminogen. | Q9KMU6 |
A0QKV0 | IF1_MYCA1 | Translation initiation factor IF-1 | Mycobacterium avium complex (MAC) | MAKKDGAIEVEGRVVEPLPNAMFRIELENGHKVLAHISGKMRQHYIRILPEDRVVVELSPYDLSRGRIVYRYK | One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-... | A0QKV0 |
Q56A73 | SPIN4_HUMAN | Spindlin-4 | Homo | MSPPTVPPMGVDGVSAYLMKKRHTHRKQRRKPTFLTRRNIVGCRIQHGWKEGNEPVEQWKGTVLEQVSVKPTLYIIKYDGKDSVYGLELHRDKRVLALEILPERVPTPRIDSRLADSLIGKAVEHVFEGEHGTKDEWKGMVLARAPVMDTWFYITYEKDPVLYMYTLLDDYKDGDLRIIPDSNYYFPTAEQEPGEVVDSLVGKQVEHAKDDGSKRTGIFIHQVVAKPSVYFIKFDDDIHIYVYGLVKTP | Exhibits H3K4me3-binding activity. | Q56A73 |
B1W0N3 | HIS3_STRGG | Phosphoribosyl-AMP cyclohydrolase | Streptomyces | MTSTPGATPPASSLDPAVAARLKRGADGLVPAIAQQYDTGEVLMLGWMDDEALHRTLTTGRCTYWSRSRQEYWVKGDTSGHVQHVKSVALDCDADTVLVKVDQTGAACHTGDRTCFDADALPLGK | Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP. | B1W0N3 |
Q7V1D9 | RLMH_PROMP | rRNA (pseudouridine-N3-)-methyltransferase RlmH | Prochlorococcus | MLQTNRLSINAIGKIKKNWIREGINQYKKRMPDLIINESKSFNIDNIRVNNIIICLTEEGQSFNSIELTSLLLNFKNKKINFLIGDADGIPSDIKDKSNLLLSLSPLTFPHELARLILIEQIYRAISISNNSPYHRA | Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. | Q7V1D9 |
Q252Y9 | COAE_CHLFF | Dephosphocoenzyme A kinase | Chlamydia | MLDLLKVSITGDLSSGKTEACRVFQDLGAYVISADKVSHSFLVPHSHIGHRVIDLLGSDVVVDNAFDRKVIAEKVFDNLVLLQALEAILHPEVCRIIEEQYCLVAKENKYPLFIAEVPLLYEIQYANKFDRVILITADENTRRERFTRKTNCSDLNFYQRCARFSSNEEKMMHADIIIENNGTKEELRHKVEEYFYALKGAL | Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. | Q252Y9 |
B7IHG0 | CBID_THEAB | Cobalt-precorrin-6A synthase | Thermosipho | MKKELRYGYTTGSCATAAAKAATYMLFNDEILKSIKIDLPIGKEIELDIFYIERKEGEVICGVRKDAGDDPDVTHNMIIYAKAEKSKEFLITGGEGIGVVTKKGLPLQVGDYAINPVPRKMIESEVKKVLPEGKNVKITIFAPEGKYIAKRTLNPKLGIIGGISILGTTGIVEPLSDEAYKKTIDLEISMASSESNEICLVFGNYGKNFTTLSSKMPLVTMGNYVGFALESACKHRIKKVYLVGQIGKMIKVAGGIFNTYSYIADARNEIFTAYLSLYGLDRGILEKVMSANTTEEILDLIEGKVGKDFFENLALRIKEK... | Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A. | B7IHG0 |
Q5E3F1 | LPXA_ALIF1 | Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase | Aliivibrio | MIHETAKIHPSAVIEGNVTIEANVSVGPFTYISGNVTIGEGTEVMSHVVIKGDTTIGKDNRIFAFAIIGEESQDKKYGGEATTVVIGDRNVIRESVQIHRGTVQDRGVTTVGSDNLLCVNVHIAHDCVVGDNIIMGNNATLAGHVTVEDFAIVSALSPVHQFCTVGAHSFIGGASVVVQDVPPFVMAQGNHCKPFGINIEGLKRRGFEKAEIHAIRRAYKALYRNGNTLEEAKVEINKEIEAFPVLQGFLDLFEKSTRGIIR | Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | Q5E3F1 |
Q9BQ70 | TCF25_HUMAN | Nuclear localized protein 1 | Homo | MSRRALRRLRGEQRGQEPLGPGALHFDLRDDDDAEEEGPKRELGVRRPGGAGKEGVRVNNRFELINIDDLEDDPVVNGERSGCALTDAVAPGNKGRGQRGNTESKTDGDDTETVPSEQSHASGKLRKKKKKQKNKKSSTGEASENGLEDIDRILERIEDSTGLNRPGPAPLSSRKHVLYVEHRHLNPDTELKRYFGARAILGEQRPRQRQRVYPKCTWLTTPKSTWPRYSKPGLSMRLLESKKGLSFFAFEHSEEYQQAQHKFLVAVESMEPNNIVVLLQTSPYHVDSLLQLSDACRFQEDQEMARDLVERALYSMECAF... | May play a role in cell death control. Acts as a transcriptional repressor. Has been shown to repress transcription of SRF in vitro and so may play a role in heart development. | Q9BQ70 |
Q9Y6Z9 | SOU1_SCHPO | Sorbitol utilization protein sou1 | Schizosaccharomyces | MTSMFSLKGKTTLITGGSGGIGFSIAKAFAAAGSNVGLLYGRNKKALEYAAELRDKHGVQAKAYSCPIENRSAVIETTNQAVEELGGRLDVMIANAGIAIPHLSLEDKNEDIWTKVVGINLNGAYYTAQAAGHHFKKQGKGSLIFTASMSGHIANWPQQWASYHATKAAVKHLARALAVEWAPFARVNSVSPGYIDTDLTLYADENLRKKWKEYTPQARIGLPDELPGAYLYLASDASSYCTGSDIIVDGGYCSR | Catalyzes the NADP dependent reduction of L-sorbose to D-glucitol. | Q9Y6Z9 |
D5CE33 | RUTB_ENTCC | Ureidoacrylate amidohydrolase RutB | Enterobacter cloacae complex | MTTLNARPEAITFSAPQSALIVVDMQNAYASPGGYLDLAGFDVSATRPVIENIKTAVAAARAAGMLIIWFQNGWDDQYVEAGGPGSPNFHKSNALKTMRKRPELQGKLLAKGGWDYQLVDELVPEAGDIVLPKPRYSGFFNTPLDSLLRSRGIRHLVFTGIATNVCVESTLRDGFFLEYFGVVLEDATHQAGPEFAQKAALFNIETFFGWVSNVADFCDALNPPLARIA | Hydrolyzes ureidoacrylate to form aminoacrylate and carbamate. The carbamate hydrolyzes spontaneously, thereby releasing one of the nitrogen atoms of the pyrimidine ring as ammonia and one of its carbon atoms as CO2. | D5CE33 |
P62877 | RBX1_HUMAN | E3 ubiquitin-protein transferase RBX1, N-terminally processed | Homo | MAAAMDVDTPSGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH | E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleot... | P62877 |
Q46HD3 | TRMB_PROMT | tRNA(m7G46)-methyltransferase | Prochlorococcus | MRQHVNPLSQFFQLPLSLPSKNILFEKSHYPIHLDIGSAKGEFLIELATKCPDWNFVGLEIREPLVSLCEKKRRKLELTNLKFLFCNVNVSLDEWLSDLDFGQLKRVSIQFPDPWFKRKHFKRRVLKTNILNSIAKAMSKNGEIFIQSDIFELIEYMTNTIDENRYFTRKNVGDLRSINKNPYNVMTDREILSLKKNLLIYRVMYIRNSLLFTN | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | Q46HD3 |
P27615 | SCRB2_RAT | Scavenger receptor class B member 2 | Rattus | MARCCFYTAGTLSLLLLVTSVTLLVARVFQKAVDQTIEKNMVLQNGTKVFDSWEKPPLPVYIQFYFFNVTNPEEILQGEIPLLEEVGPYTYRELRNKANVQFGENGTTISAVTNKAYIFERNQSVGDPTVDLIRTINIPLLTVVEMAQQPFLREIIEAMLKAYQQTLFVTHTVHELLWGYKDEVLSLVHIFRPDVSPNFGLFYERNGTNDGEYVFLTGEDNYLNFTKIVEWNGKTSLDWWTTDTCNMINGTDGDSFHPLISKDETLYIFPSDFCRSVYITFSSFENVEGLPAFRYKVPAEILANSSENAGFCIPEGNCMD... | Acts as a lysosomal receptor for glucosylceramidase (GBA1) targeting. | P27615 |
Q30TI8 | FLIW_SULDN | Flagellar assembly factor FliW | Sulfurimonas | MKFDVCVPILGFENVKEVTLEKIDDAFMRMESSNDEHISFTLINPFALREYDFEIPDATQKLLEIDEKSNILILNIAIIQTPVEDTVVNFIGPMIFNTDNNKAAQLVLSESTKYGVAEKISLYLKK | Acts as an anti-CsrA protein, binds CsrA and prevents it from repressing translation of its target genes, one of which is flagellin. Binds to flagellin and participates in the assembly of the flagellum. | Q30TI8 |
Q67KC5 | ARGJ_SYMTH | Arginine biosynthesis bifunctional protein ArgJ beta chain | Symbiobacterium | MEWLAGGVTAPAGFVAAGACADIKGNGAGKKDVALLASRVPCAAAGVYTTNLVKAAPVVLTRGRTETGELQAVVANSGNANACTGEQGMRDAAEMARLAAEALGIRPELMGVASTGVIGVPLPMDRVSAGIRAAAAALSPEGGADAAEAIMTTDTFPKQAAARLEIGGATVTIGAMAKGSGMIHPNMATMLGFVTTDAAVDAAALREALREATDRSFNMITVDGDTSTNDMVLVLANGLAGNPRIMPGSAHYRAFADALAAVLIHLAKEIARDGEGATKLIEVRVKGAATLSDARKAARAVCGSNLVKAAVFGEDANWGR... | Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate. | Q67KC5 |
Q8TKX4 | PTH_METAC | Peptidyl-tRNA hydrolase | Methanosarcina | MSEYKQCIVTRDDLKLSKGKFAVQVAHAALSAAEWASKSDLEKWKEGGQKKIVLRVPTIKDLYELKEKARREGLPTALIQDAGLTEIPAGTVTVLGIGPAKEEVIDKVTRDLKLV | The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. | Q8TKX4 |
Q9CKC8 | ZIPA_PASMU | Cell division protein ZipA | Pasteurella | MDLNTILIILGIIALIILVVHGLWANRREKSQYFKSANTFTRDSRLREPPAHIQSASEEKKDANTSTPTAEVSPAQRTFAFEAEKQFAHEQQAVEQAIENIKITLPKEEQPYQAKIEPDTPPTSPALTTIAEVENYANQEEGIDTHSEQLRQQLADLAQQSPSVTLAALQEEQALMESQAQQQASEDVRQDTDATFIMMYVVAPENYQFQGARLAKILDELGFLFGEHNIYHRHSDLSVNSPVLFSVANIEQPGTFDYNMHDFSTVGIALFMQLPSEGNDLMNLRMMIRAAKSIAEDLGGFVLTDQQAIFDDQAEKAYLD... | Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins. | Q9CKC8 |
Q6AR67 | TAL_DESPS | Probable transaldolase | Desulfotalea | MKFFIDTANLDEIREGVELGLVDGVTTNPSLIARENLPFEELIAEICKIVDGPVSAEVISLDAPGMVAEAKKLASIDEKVVIKVPMTAEGLKAVRQLSAAGIKTNVTLIFSANQALLAAKAGASYVSPFVGRLDDIGVNSADLISDILTIFDNYGYASEVIVASVRGPQHVLDSALLGADIATIPLKTIKQLTKHPLTDKGMEQFLADWEKRTQ | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | Q6AR67 |
Q749B2 | RS4_GEOSL | 30S ribosomal protein S4 | Geobacter | MARYTGPSCRLCRRENMELFLKGERCYTDKCAIKRRNYPPGQHGQGRPKVSNYGVQLREKQKVRRIYGILEKQFRSYFQEADRLKGVTGENLLSLLERRLDNVVYRLGFAASRTEARILVRHNHFTLNGKKANIPSIQLRAGDVVELKEKSRKIACINESLDAVVRRGIPQWLELEKDAYKGVVKTLPVREDITMPIQEQLIVELYSK | With S5 and S12 plays an important role in translational accuracy. | Q749B2 |
Q5H0A7 | G6PI_XANOR | Phosphohexose isomerase | Xanthomonas | MTQTNGFDALHAHAQRLRGAAIPALLAAEPERPTQYAWQVGPLYFNFARQKYDRAALDALFAIARERDLAGAFQRLFRGEQVNVTEQRAALHTALRGDLTDAPVASEAYATAAEVRQRMGALIQQLEATDVTDIVSVGIGGSDLGPRLVADALRPVSGARLRVHFVSNVDGAAMQRTLATLDPARTAGILISKTFGTQETLLNGSILHAWLGGSERLYAVSANPERAAKAFDIAPGRVLPMWDWVGGRYSLWSAVGFPIALAIGFERFEQLLEGAAQFDAHALNTPLEENVAVLHGLTAVWNRNLLGSATHAVMTYDQRL... | Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. | Q5H0A7 |
A5EVK4 | COAX_DICNV | Pantothenic acid kinase | Dichelobacter | MYLLIDVGNSRIKWLYGNKVPSTIEAVSYKQDWQMKLIRAWHLLPEPEAIALSSVNKAEITTTIEEIVRQLWHKTVKIFVSQKQTNHTLTVVYQKPEKLGSDRYLAMLGARSLCHDPLCVVGCGTAITLDAVDGDGRHLGGFILPGMRLAENALLQNTQKLVPMRWTPHLLGNDTASCISAGIHHALPAGVDHIIDELEGQCGYYFKRFAFGGDAQILFGNRPTYRIEPDLIFGGMFAHLSPPKQV | Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. | A5EVK4 |
A3DEU4 | NADD_ACET2 | Nicotinate mononucleotide adenylyltransferase | Acetivibrio | MEVNVKRIGILGGTFDPIHNGHLIMAEIIRGAFELDRVLFIPSGNPPHKKNQTVTDAEHRYNMVCEALKGNPYFEKSRIEVDREGYTYTIDTLGILNEQYRGIADLYYIIGADVLYDLLTWKDYEKVFGICKFIAALRPGTGKEGFRERIKYLEDRFSASILEAEIPLIEISSTMIRNRVKEGKSIKYLVPETVENYIKKEGLYLK | Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). | A3DEU4 |
Q3AU08 | RECA_CHLCH | Recombinase A | Chlorobium | MTMDNPKVEQAGHAVDSAKLKQLNLAVDALEKQFGKGTIMRMGDGSAGLTVQAISTGSMALDFALGVGGLPRGRVTEIYGPESSGKTTLALHVIAEAQKEGGITAIVDAEHAFDPSYARKLGVDINALLISQPESGEQALSIVETLVRSGAVDVVVVDSVAALVPQAELEGEMGDSSMGLQARLMSQALRKLTGAISKSSTVCIFINQLRDKIGVMYGSPETTTGGKALKFYSSVRLDIRKIAQLKDGDELTGSRTRVKVVKNKVAPPFKMAEFDILYGEGISALGELIDLGVEFGVIKKAGSWFSYGTEKLGQGRESVK... | Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage. | Q3AU08 |
A1QZM2 | DNAA_BORT9 | Chromosomal replication initiator protein DnaA | Borrelia | MQEGKNIWSLILAAIRKELSEEEFYIWFENLYFIDATDESIKISAPNSFHKNQVEKRFSKRIKEILTEKGHNTINVEFINPPKEPKTHSMELKNTSLKDISIQQDSPEKRTILNTHTKNIIEHTKHYVIKEDIHTKYRNPFLKKKYTFENFIIGPNNKLAYNASLSIAKNPGKKYNPCLIYGGVGLGKTHLLQSIGNKTEELHKEFKILYVTAENFLNEFVESIKTNETKRFKKKYRHLDMLLIDDIHDLQKKEGIQEELFHTFNALYEDNKQMVFTCDRQPSELINFTDRLKSRFTRGLNVDISKPNFELRVAIIEKKA... | Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. | A1QZM2 |
O13297 | CET1_YEAST | mRNA 5'-triphosphate monophosphatase | Saccharomyces | MSYTDNPPQTKRALSLDDLVNHDENEKVKLQKLSEAANGSRPFAENLESDINQTETGQAAPIDNYKESTGHGSHSQKPKSRKSSNDDEETDTDDEMGASGEINFDSEMDFDYDKQHRNLLSNGSPPMNDGSDANAKLEKPSDDSIHQNSKSDEEQRIPKQGNEGNIASNYITQVPLQKQKQTEKKIAGNAVGSVVKKEEEANAAVDNIFEEKATLQSKKNNIKRDLEVLNEISASSKPSKYRNVPIWAQKWKPTIKALQSINVKDLKIDPSFLNIIPDDDLTKSVQDWVYATIYSIAPELRSFIELEMKFGVIIDAKGPD... | First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end. | O13297 |
Q8DK88 | METK_THEVB | Methionine adenosyltransferase | Thermosynechococcus | MRYLFSSESVTEGHPDKICDQIADAILDALLTQDPQSRVAAEVVVNTGLVLITGEITTKAQVNYVNLARQKIHEIGYTDANNGFAANSCAVLVALDEQSPDIARGVDTAQEAREQLSDAELDRIGAGDQGIMFGYACNETPEYMPLPISLAHRMARRLAAVRKTGQLPYLRPDGKTQVTVIYEDGKPVGIDTILISTQHTATIDDISEESAVQAKIKADLWEAVVKPVFADLTLQPDGNTRFLVNPTGKFVIGGPQGDSGLTGRKLVVDTYGGYARHGGGAFSGKDPTKVDRSAAYMARYIAKNIVAAGLADKCELQISY... | Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | Q8DK88 |
B5BIA8 | CLSA_SALPK | Cardiolipin synthase A | Salmonella | MTTFYTVVSWLVILGYWVLIAGVTLRILMKRRAVPSAMAWLLIIYILPLVGIIAYLSVGELHLGKRRAERARAMWPSTAKWLNDLKACKHIFAQENSSVASSLFKLCERRQGIAGVKGNQLQLLTDSDDVMQALIRDIQLARHNIEMVFYIWQPGGMADQVAESLMAAARRDIHCRLMLDSAGSVAFFRSPWAAMMRNAGIEVVEALKVNLMRVFLRRMDLRQHRKMVMIDNYIAYTGSMNMVDPRFFKQDAGVGQWVDLMARMEGPVATAMGIVYSCDWEIETGKRILPPPPDVNIMPFEQASGHTIHTIASGPGFPED... | Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. | B5BIA8 |
Q7SXE8 | CDK9_DANRE | Cell division protein kinase 9 | Danio | MSKYYDGVEFPFCDEFSKYEKLAKIGQGTFGEVFKAKHRQTGKKVALKKVLMENEKEGFPITALREIKILQLLKHENVVNLIEICRTKGEATQFNRYKGSIYLVFDFCEHDLAGLLSNANVKFTLAEIKRVMQMLLNGLYYIHRNKILHRDMKAANVLITRDGVLKLADFGLARAFSLAKNSQGNRYTNRVVTLWYRPPELLLGERDYGPPIDLWGAGCIMAEMWTRSPIMQGNTEQHQLTLISQLCGSITPEVWPGVDKKYELYQKMELPKGQKRKVKDRLKAYVKDPYALDLIDKLLVLDPAQRIDSDDALNHDFFWS... | Protein kinase involved in the regulation of transcription. Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor b (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the l... | Q7SXE8 |
C0MFA6 | DEF_STRS7 | Polypeptide deformylase | Streptococcus | MSAQDKLIKAQHLIDMNDIIREGNPTLRAVAKEVEFPLSDDDIILGEKMMQFLKHSQDPVMGEKLGLRAGVGLAAPQIDVSKRIIAVLVPNPEDSEGNPPKEAYSMEEVLYNPKIVSHSVQDAALADGEGCLSVDRVVEGYVVRHARVTVEYYDKHNEKHRIKLKGYNAIVVQHEIDHINGVLFYDRINAKKPFEAKEGMLILE | 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. | C0MFA6 |
Q1GZA1 | CYNS_METFK | Cyanate lyase | Methylobacillus | MSRLDVTEKIITAKVMKGLKWADVAAKLNLSKEWVTAACLGQMTLNAEQAKIIAEIFDLSDEDQKWLMVTPCKGSLPTAVPTDPLIYRFYEMINVYGTTIKQLIHEEFGDGIMSAIDFKMDLQRVADPMGDRVNIVLNGKFLPYKQF | Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. | Q1GZA1 |
A4YSK8 | RL18_BRASO | 50S ribosomal protein L18 | unclassified Bradyrhizobium | MSRAKVTNARRKQRVRLSLRRSAGGRPRLSVFRSSKHIYAQVIDDQKGETIASASSMEKEMRSAGNTGADIDAAKAVGKLLAERAVKAGIKEVVFDRGGYLYHGRVKALADAARESGLSF | This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. | A4YSK8 |
B8EFD7 | TAL_SHEB2 | Transaldolase | Shewanella | MANTLEQLKLYTTIVADTGDIEAIKRYQPEDATTNPSLILKAAQIPEYESLIDNAIDWAKSQSDDLAQQLDDASDKLAVNIGVEILKLVPGRISTEVDARLSFDKEQSIAKAHKLVRLYKEAGVDKSRILIKLASTWEGICAAKELEKEGINCNLTLLFSFAQARACAEAGAYLISPFVGRILDWYKKDTGKDYDAVNDPGVVSVTEIYNYYKQHGFNTVVMGASFRNIGEIIELAGCDRLTIGPSLLEELANSQIDITPKLVAATSTVAAEAPLTEAQFRWDFNQDPMAVDKLAEGIRNFAIDQGKLEVMLTAKLAN | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | B8EFD7 |
Q3IYX7 | PGSA_CERS4 | Phosphatidylglycerophosphate synthase | Cereibacter | MNWSIPNILTVLRLLAAPGVAVMFLYFHRPWADWFALTLFILAAVTDFFDGYLARLWKQESKFGAMLDPIADKAMVVIALVIITGYSGMNPWLILPVTLILFREVFVSGLREFLGAKASLLKVTKLAKWKTTAQMVAIAILFLGTGLEHLEGIARQGMTWEQYARAVSAGEADPIRSCGMHGCSSYATWLGLALIWIAAALTFITGWDYFRKALPYLKDEK | This protein catalyzes the committed step to the synthesis of the acidic phospholipids. | Q3IYX7 |
Q2GIJ7 | YBEY_ANAPZ | Endoribonuclease YbeY | phagocytophilum group | MPVEVSTIDRKWYRIIRKPKATSQEIVLFALRELKVDRYNPIVSVVLAHDALLLELNHKYRNINKPTNVLSFNYEALSHNCCLGEIFLSIDRLTYESKTLGVEVHAHFTHMLIHGVLHILGYDHEVPEDAQEMQALEIDLLSKRSIENPYLIQE | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | Q2GIJ7 |
Q9KA72 | DPO3_HALH5 | DNA polymerase III PolC-type | Halalkalibacterium (ex Joshi et al. 2022) | MNEEQRVRQERFKLLMEQLLIPEDVTANHLKDGKIEKLTIKKDERRWHFQLSIPTVLPASIYELLADRLVQTFSHIAKVSFQIQYGQPDLSEQVWQSYWPLIVAKLTNISQPLKEMLEKQTPRFDGKRLVIQVGNETEAIALKRKLTEPLQQAVQSFGFPAVQLDAEVKESKQAFEKFVEQRKQEDHSKVVEAILEKKKLEQQVEKKMKEEKLTIGYPIKDEPVPLETIVEEERRITVQGYIFAAETKELRSGRTLLTFKITDYTDSILVKMFSRDKEDIPLLQAVKKGMWVKVRGGVQNDTFVRDLVMIANDVNEVSGK... | Required for replicative DNA synthesis. This DNA polymerase also exhibits 3' to 5' exonuclease activity. | Q9KA72 |
Q057C6 | RS13_BUCCC | 30S ribosomal protein S13 | Buchnera | MTRIAGINISDKKHILVALTSIYGIGISLSKKICFSIGIRCDVKINSLTKEKIESLRSIISKFLVEGDLRREKTINIKRLMDIGCYRGLRHRKHLPVRGQRTKTNARTRKGPRKLIKSR | 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. Contacts the tRNAs in the A and P-sites. | Q057C6 |
Q1LI61 | RS11_CUPMC | 30S ribosomal protein S11 | Cupriavidus | MAKGPNNAAQRARKKVKKNVADGIAHVHASFNNTIITITDRQGNALSWATAGGQGFKGSRKSTPFAAQVAAENAGRVAQDQGIKNLEVRIKGPGPGRESAVRALNALGIKIAVIEDVTPVPHNGCRPPKRRRI | Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome. | Q1LI61 |
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