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 |
|---|---|---|---|---|---|---|
Q8R5T7 | CH60_CALS4 | Chaperonin-60 | Caldanaerobacter | MAKQIKYGEEARKALERGVNAVANTVKVTLGPRGRNVVLDKKYGTPTVTNDGVTIAREIELEDPFENQGAQLLKEAATKTNDVAGDGTTTATLLAQVMVLEGLKNLAAGANPMLLRRGMAKAVEAAVEGLRRISKPIDNKESIAHVAAISAADEEIGQLIAEAMEKVGKDGVITVEESKTIGTTLEVVEGMQFDRGYISPYMVTDAEKMEAVLEEPVILITDKKLSSVQDLLPLLEQIVQHGKKLLIIADDVEGEALATLVVNKLRGTFSCVAVKAPGFGDRRKEMLQDIAILTGGQVISEELGYDLKDVTLDMLGRARQ... | Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. | Q8R5T7 |
Q53QV2 | LBH_HUMAN | Limb bud and heart development protein homolog | Homo | MSIYFPIHCPDYLRSAKMTEVMMNTQPMEEIGLSPRKDGLSYQIFPDPSDFDRCCKLKDRLPSIVVEPTEGEVESGELRWPPEEFLVQEDEQDNCEETAKENKEQ | Transcriptional activator which may act in mitogen-activated protein kinase signaling pathway. | Q53QV2 |
Q9JKU0 | T2R16_RAT | T2R3 | Rattus | MVPTQVTIFSIIMYVLESLVIIVQSCTTVAVLFREWMHFQRLSPVEIILISLGISHFCLQWTSMLYNFGTYSRPVLLFWKVSVVWEFMNVLTFWLTSLLAVLYCVKVSSFSHPVFLWLRLKILKLVLWLLLGALIASCLSIIPSVVKYHIQMELLTLDHLPKNSSLILRLQMFEWYFSNPFKMIGFGVPFLVFLISIILLTVSLVQHWGQMKHYSSSSSSLRAQCTVLKSLATFFIFFTSYFLTIVVSFIGTVFDKKSWFWVCEAVIYGLVCIHFTSLMMSNPTLKKALRLQFWSPESS | Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5. | Q9JKU0 |
A9M5W0 | CBID_BRUC2 | Cobalt-precorrin-6A synthase | Brucella | MNDETTPANKNPEKAELRCGWTTGACATAATKAALTALITGEFPDPVGIILPKGEVPYFQLAYEGLGEGYAMAGIVKDAGDDPDVTHGATIISTVYPAPPGTGIIFRAGEGVGTVTREGLAIPPGEAAINPVPRRMMTEICEAICAEYGLPADLVITISVPGGEEIAQKTWNPRLGIIGGISILGTTGVVHPFSCSAWIHSIHRGIDVARAAGQKHVLGATGSTSEDAAQALYNLPDFAILDMGDFAGGVLKYLREHPIDRLTIAGGFAKLTKLAQGALDLHSSRSQVDKGFLWQIAERAGAPADMKERILLANTAMEVL... | Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A. | A9M5W0 |
Q8CX49 | CH10_SHEON | Chaperonin-10 | Shewanella | MNIRPLHDRVIVKRLEVESTSAGGIVLTGSAAEKSTRGEVLAVGNGRILENGTVRPLDVKVGDVVIFNEGYGVKKEKIDGQEVLILSEADLMAIVG | Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of ... | Q8CX49 |
A0A1B4XBH5 | SDNK_SORAA | Sordarin/hypoxysordarin biosynthesis cluster protein K | Sordaria | MVQFNGPHGKVTVSYLRQGGLNPPAPAPKGSFTGKTVLITGCSSGIGYQAALQIASLNPKRLILGTRTLAKGEAAKQEILATVGPSLDSSIIEVIPIECSDLSSVRQFTTTVRKTTPPGTLDCVLLSAGLALPTREVVTDESGHEWPTTFVVNVLAPALLALEFLPLLQSTPGSVVESVNSISYCNVTSEDISPLLSSQDEATGTTSALDFFNNPERWTTQRAYYEAKLMLMFVLEGLVQDQAQQQASQPGEDRKVLFLACCPGQCRTNLYRQFGLGVRAFMTLFNAVIARTAEQGARTLVTGLLLQGEEAMGKMWVNDR... | Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of sordarin and hypoxysordarin, glycoside antibiotics with a unique tetracyclic diterpene aglycone structure . First, the geranylgeranyl diphosphate synthase sdnC constructs GGDP from farnesyl diphosphate and isopentenyl diphosphate . Th... | A0A1B4XBH5 |
A1JSN7 | GLME_YERE8 | Methylaspartate mutase | Yersinia | MELRNKKISLDDFMSERFHVLKTWHTGKDVENFEDGVKYQQTIPESKNFARALFEADCNGITLSQPRAGVALIEEHIELLKTLQKDCDLLPTTIDAYTRLNRYEEAAVGIQKSIEAGTSKLNGLPVVNHGVKACRRITESLSKPLQIRHGTPDARLLAEIAMASGFTSYEGGGISYNIPYAKRVTLEKSIRDWQYCDRLIGVYEEHGIRINREPFGPLTGTLIPPFVSHAVAIIEGLLALEQGVKSVTVGYGQVGNIVQDIAAIQSLRELAHEYFRANGYENYELSTVFHQWMGGFPEDESRAFAVISWGAAVAGMAGAT... | Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate). | A1JSN7 |
Q7UN03 | RS5_RHOBA | 30S ribosomal protein S5 | Rhodopirellula | MSNARNKRNNKNEEQGLEAGLLDRVVKIKRCAAVVKGGRRFSFAAMVVVGNGSGQVGWGYGKANEVPPSVQKAQKQASRSMIHVPLVEGSIPHQVWGRYGAARVVLIPAGAGTGIIAGQAVRAVCEACGIHDILTKSYGTNNPVTLVKATLDAMSKLRTREQIAALRGLNPDDLIEA | Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. | Q7UN03 |
B4RD11 | DCUP_PHEZH | Uroporphyrinogen decarboxylase | Phenylobacterium | MSTPPPKLLRALAGETLERPPIWFMRQAGRSLPEYRELRSRAKDFIAFCLDPEMAAEATLQPMRRFPMDGAIVFADILLIPLALGQDVWFEAGEGPKLGELPPIEALRDQVEASTGRLSAVGETLARVRAELEPDRALIGFAGAPWTVATYMLERKGSEREAARAYAYAHPDELDALLDVLVDATARYLVMQAKAGAQALKLFESWAESLSEDVFERIVVRPHAAIVEKVRAAGVTVPIIGFPRGAGAQVETYAEGVPVEGIALDVQATAALGRRLQAQGRCIQGALDNLLLREGGPALDARVDQLLAQWGDGPWIFNLG... | Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | B4RD11 |
A5CVN5 | PYRE_VESOH | Orotate phosphoribosyltransferase | Candidatus Vesicomyosocius | MEQYQEDFVEFILDSGALKFGNFTLKSGRISPYFFNVGVFNTGQYLSQLGKFYAIAIENSGLDFDVLFGPSYKGIPLVTATAVAFNNNFNKDVSYSFNRKEVKTYGEGGGIVGHSLEGNILIIDDVITAGTAIHEAVDIIKANGATVKGVIVAVDRQEKGKSGQSAIQEVEQNFGISVFSIINLSNVVDYLKQGNNHALIDRIEVQR | Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). | A5CVN5 |
Q2YAY2 | RL6_NITMU | 50S ribosomal protein L6 | Nitrosospira | MSRVGKNPVSVPANVEVRLSGSEVEVKGPLGMLRHELVSDISIERKGESLLVKAADDSKHANAMWGTTRALLANMVKGVTTGFEKRLILVGVGYRAQAADNVLNLTLGFSHPIAHKMPEGIKVETPSQTEVVIKGMDKQQVGQVAADVRAYREPEPYKGKGVRYADEVIVLKETKKK | 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. | Q2YAY2 |
C4L7Q5 | RDGC_TOLAT | Recombination-associated protein RdgC | Tolumonas | MWFKNLQLYRFTRPFEHDADSLEKMLQSHLFSPCGSQEMSKFGWISPLGKHAEVLVHEAQGQMLLCAKKEEKVLPAAVIKDMLQEKIDEMEAAQGRALKKKEKESLKEEILHTLLPRAFPRSSQTFLWINPAENYLVVDAGSAKKADDVLSLLRKCTGSLPVVPFALQNPPEITMTEWLNAGAAPGGFVLEDEAELRSALEHGGIIRCKEQDLVTEEIKAHLLADKMVTKLALNWSDTVSFVLADDLSIKRLKFSEELREQNEDVISEDHVARMDADFALMTGELAKFVPELVAALGGEKAE | May be involved in recombination. | C4L7Q5 |
Q1C5B1 | UREF_YERPA | Urease accessory protein UreF | Yersinia | MNASDLIRIMQFGDSVLPVGAFTFSNGVESAIQTGIVHDVATLKGFVLTALKQAASCDGMGVVVAHRAVVADDRDGIIRADWAVNNRKLNEESRLMATRMGKKLAEMSIHVVEHPLISWWLEQIKNGNTAGTYPVTQAVVMAAQGIGQREVVVMHQYGVAMTILSAAMRLMRVTHFDTQHILFELNHDIEKFCDIAEIGDINQMSSYVPIVDVLAAVHVKAHVRLFSN | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | Q1C5B1 |
P34925 | RYK_HUMAN | Tyrosine-protein kinase RYK | Homo | MRGAARLGRPGRSCLPGARGLRAPPPPPLLLLLALLPLLPAPGAAAAPAPRPPELQSASAGPSVSLYLSEDEVRRLIGLDAELYYVRNDLISHYALSFSLLVPSETNFLHFTWHAKSKVEYKLGFQVDNVLAMDMPQVNISVQGEVPRTLSVFRVELSCTGKVDSEVMILMQLNLTVNSSKNFTVLNFKRRKMCYKKLEEVKTSALDKNTSRTIYDPVHAAPTTSTRVFYISVGVCCAVIFLVAIILAVLHLHSMKRIELDDSISASSSSQGLSQPSTQTTQYLRADTPNNATPITSYPTLRIEKNDLRSVTLLEAKGKV... | May be a coreceptor along with FZD8 of Wnt proteins, such as WNT1, WNT3, WNT3A and WNT5A. Involved in neuron differentiation, axon guidance, corpus callosum establishment and neurite outgrowth. In response to WNT3 stimulation, receptor C-terminal cleavage occurs in its transmembrane region and allows the C-terminal int... | P34925 |
A7FZ73 | RS7_CLOB1 | 30S ribosomal protein S7 | Clostridium | MPRKGHIAKRDVLPDPLYNSKVVTKLINSIMLDGKRGVAQKICYDAFEIIAEKSGKDAMEVFETAMNNIMPLLEVKARRIGGATYQVPIEVRPERRQTLGIRWMLIAARKRGERSMRERLAGELLDASNNTGAAVKKREDTHKMAEANKAFAHYRY | One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA. | A7FZ73 |
Q21LG1 | RL19_SACD2 | 50S ribosomal protein L19 | Saccharophagus | MSSKNKIIQELEAEQLKQDVPEFSPGDTVVVQVKVKEGNRERLQAFEGVVIARRNRGLDSAFTVRKISHGIGVERTFQTHSKQVDSVAVKRRGDVRQAKLYYLRELTGRAARIKEKLG | This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site. | Q21LG1 |
B0SCC0 | CH60_LEPBA | Chaperonin-60 | Leptospira | MAKTIEFDETARRKLLSGVNKLANAVKVTLGPKGRNVVIDKKFGSPTITKDGVTVAKEIELEDAIENMGAQMVKEVSTKTNDIAGDGTTTATILAQAIINEGLKNVTAGANPMALKHGIDKAVVVAVEEIKKHAIKINSKAEYANVATISANNDPEIGNLIAQAFDKVGKEGVITVDEAKSIETTLDIVEGMQFDRGYVSPYMVTDPEAMIATFNDPFILIYDKKIASMKDLLPVLEKIAQAGRPLVIIAEEVEGEALATIVVNTLRKTIQCVAVKAPGFGDRRKAMLEDIAILTGGQVISEDLGMKLENADVKMLGRAK... | Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. | B0SCC0 |
A7MEA1 | RUVC_CROS8 | Holliday junction resolvase RuvC | Cronobacter | MSIILGIDPGSRVTGYGVIRQTGRQLTYLGSGCIRTSVTDLPSRLKLIYAGVSEIITQFRPDYFAIEQVFMAKNADSALKLGQARGAAIVAAVNHDLPVFEYAARQVKQTVVGIGSAEKSQVQHMVRTLLKLSANPQADAADALAIAITHCHVSQNATQVSESRLNLARGRLR | 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. | A7MEA1 |
Q58539 | RNP3_METJA | Rpp30 | Methanocaldococcus | MRIDINRIEKEEDIKLLKELKWNGFVFYQYDDEFSKDRYEEVKAIAESYKLKVYSGVKIKTESSKQLRDKVKKFRNKCHIILIEGGVLKINRAAVELHDVDILSTPELGRKDSGIDHVLARLASNHRVAIELNFKTLLNKDGYERARTLLFFRNNLKLAKKFDVPVVISTDAENKYQIKNPYDLRAFLNTLVEPLYAKKIMETAYKICDFRDYLMRDNVVRYGVEIIKEEKE | Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. | Q58539 |
Q9SIW2 | CHR35_ARATH | Protein DEFECTIVE IN RNA-DIRECTED DNA METHYLATION 1 | Arabidopsis | MGFVYIVMTGYYKNVHKRKQNQVDDGPEAKRVKSSAKVIDYSNPFAVSNMLEALDSGKFGSVSKELEEIADMRMDLVKRSIWLYPSLAYTVFEAEKTMDNQQVVEGVINLDDDDDDDTDVEKKALCVVPSSSEIVLLDSDDEDNERQRPMYQFQSTLVQHQKNQGDVTPLIPQCSFEEVDLGRGKEMPSAIKAIVEGQTSRGKVLPIENGVVNEKGVYVGVEEDDSDNESEAADEDLGNIWNEMALSIECSKDVARETSHKEKADVVEDCEHSFILKDDMGYVCRVCGVIEKSILEIIDVQFTKAKRNTRTYASETRTKR... | Subunit of the chromatin-remodeling complex (DDR complex) that mediates RNA polymerases IV and V (Pol IV and Pol V) recruitment to chromatin . Cooperates with Pol IV and Pol V to regulates RNA- and RNAi- (RNA interference) directed non-CpG de novo DNA methylation on cytosine of genes targeted for silencing and enhancer... | Q9SIW2 |
Q9SAJ7 | MTP9_ARATH | Metal tolerance protein 9 | Arabidopsis | MAATEHRGLSGGDYNVDLLPIDQDDSPPSSWRLSLDTFRLPSSSPLSSGRHNGRTRLSRYLRTPKKERKVSEYYKQQEKLLEGFNEMETINETGFVSGAPTEEELKKLAKSERLAVHISNAANLVLFVAKVYASVESRSMAVIASTLDSLLDLLSGFILWFTANAMRTPNNFRYPIGKRRMQPVGIIVFASVMATLGLQVILESTRLLVSKNGSHMSSTEEKWMIGIMASATVVKFLLMLYCRSFQNEIVRAYAQDHLFDVITNSVGLATAVLAVKFYWWIDPSGAILIALYTISTWARTVLENVHSLIGRSAPPDFLAK... | Involved in sequestration of excess metal in the cytoplasm into vacuoles to maintain metal homeostasis. | Q9SAJ7 |
A2C733 | RL21_PROM3 | 50S ribosomal protein L21 | Prochlorococcus | MAEKPAAKPKAAAAKAEAKDQSDSYAIVEASGQQFWLQPNRYYDLDRLQAAVDDTVTLENVLLIKDGKNDTTVGQPYVKGASVELKVMDHRRGPKIIVYKMRPKKKTRRKNGHRQELTRVMVQSISIDGKALS | This protein binds to 23S rRNA in the presence of protein L20. | A2C733 |
Q2YAZ1 | RS3_NITMU | 30S ribosomal protein S3 | Nitrosospira | MGQKIHPTGFRLSVLKNWSSKWYANGKSFPGMLNEDIKVREYLKKKLAHASVGRVVIERPSKNARITIYSSRPGVVIGKKGEDIEVLRGALQKLMGVPVHVNIEEIRKPEIDAQLIADNIAQQLEKRIMFRRAMKRAMQNAMRLGAQGIKIMSSGRLNGIEIARTEWYREGRVPLHTLRADLDYGVSEAKTTYGVIGIKVWVFKGEVIGRGEQAGAGTAAPQVLPPAGEPETRRPPRRPAGRADARSDGKAGEKKGPRKSDNSSEESATKPAKKPVKPGVNDAAAS | Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation. | Q2YAZ1 |
P17648 | ADH_FRAAN | Alcohol dehydrogenase | Fragaria | MSSTEGKVICCRAAVAWEAGKPLVIEEVEVAPPQANVVRVKILYTSLCHTDVYFWEAKGQNPLFPRIYGHEAGGIVESVGEGVTDLKAGDHVLPVFTGECKECDHCKSEESNMCDLLRINTDRGVMLNDGKSRFSIKGKPIYHFVGTSTFSVYTVTHVGCLAKINPQSPLDKVCILSCGISTGLGATLNVRKPKKGSTVAVFGLGAVGLAAAEGARMAGASRIIGVDLNSNRFEEAKKFGITEFVNPKDHKKPVQEVIAELTNGGVDRSIECTGNIQAMIPAFECVHDGWGVAVLVGVPHKDAVFTTHPMNFLNERTLKG... | This protein is responsible for the conversion of alcohols to aldehydes in plants and is important for NAD metabolism during anaerobic respiration. | P17648 |
A0A224AKZ9 | 708G2_CITUN | CuCGT | Citrus | MSDSGGFDSHPHVALIPSAGMGHLTPFLRLAASLVQHHCRVTLITTYPTVSLAETQHVSHFLSAYPQVTEKRFHLLPFDPNSANATDPFLLRWEAIRRSAHLLAPLLSPPLSALITDVTLISAVLPVTINLHLPNYVLFTASAKMFSLTASFPAIVASKSTSSGSVEFDDDFIEIPGLPPIPLSSVPPAVMDSKSLFATSFLENGNSFVKSNGVLINSFDALEADTLVALNGRRVVAGLPPVYAVGPLLPCEFEKRDDPSTSLILKWLDDQPEGSVVYVSFGSRLALSMEQTKELGDGLLSSGCRFLWVVKGKIVDKEDE... | UDP-glucose-dependent glucosyltransferase catalyzing the C-glucosylation of 2-hydroxyflavanones (2-hydroxylnaringenin and 2-hydroxypinocembrin) and phloretin . No activity with flavanones, flavones or flavonols . Exhibits C-glucosylation activity toward 2-phenyl-2',4',6'-trihydroxyacetophenone . Can use UDP-xylose as s... | A0A224AKZ9 |
Q971J0 | RL11_SULTO | 50S ribosomal protein L11 | Sulfurisphaera | MPTKSIKIVVEGGNVKPGPPLAPTLSQLGLNVGEVVKKINDATSQFKGMSVPVTLEVDTDTKKYEIKVGIPTTTSLLLKFANASEPSGDPAHKKVGDIKFEDIIQVAIMKKPQITAKTLKAAVKSILGTAHSIGLTVDKKSPKELVKAVDEGKYDDLLAKYEQKWNEAEG | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | Q971J0 |
B3DZP5 | CH60_METI4 | Chaperonin-60 | Methylacidiphilum | MAAKQLIFDESARHALLRGVEKLSKAVKCTLGPAGRNVILDKKFGSPTITKDGVTVAKEVELEDPWENMGAQLVKEVASKTSDVAGDGTTTATVLAESIYKEGLKNVTAGANPMDLKRGVDKAVQAVVKQLKEISHIVKGKEEIKQVATVSANWDTSIGEIIADALDKVGKDGTVTVEEAKHIETTLEVVEGMQFDRGYISPYFVTNAEELEAVLENAYILIHEKKISNLKDLLPLLEKIAKAGRPLLIIAEDVEGEALATLVVNKLRGTLQVCAVKAPGFGDRRKAMLEDIAILTGGRCLTEDLGIKLENVQLEDLGRA... | Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. | B3DZP5 |
Q2G9W6 | PYRE_NOVAD | Orotate phosphoribosyltransferase | Novosphingobium | MLEDEILSEFRASQALLEGHFLLSSGRHSAHYLQCARVLMDPMRASRLAAATAAKIPRDLRHQIQKVVSPAMGGVIIGHEMGRALGVEAMFVERPTGTFELRRGFALNPGEKVLMVEDVVTTGLSSREAIKAIEQAGGEVIAAAALVDRSAGAVDLGVPFFPLVALNFPTYAPDELPPELAATEAVKPGSRAKP | Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). | Q2G9W6 |
P41040 | CALM_MAIZE | Calmodulin | Zea | MADQLTDEQIAEFKEAFSLFDKDGDGCITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPELLNLMARKMKDTDSEEELKEAFRVFDKDQNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKVMMAK | Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. | P41040 |
A2BP63 | ISPH_PROMS | 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | Prochlorococcus | MDTQAFRRSLHHSDRYNRRGFDSPTKRAQALEEAYQSDLISSIRDNGFTYTKGRLNIKLAQAFGFCWGVERAVAMAYETRRHYPNENIWITNEIIHNPSVNDHLRKMNVKFISAKNGIKDFSLVSNGDVVILPAFGATVQEMKLLHEKGCHIIDTTCPWVSKVWHTVEKHKKHVFTSIIHGKFKHEETLATSSFAGKYLVVLDLEEANYVSEYILGKGNRNEFMNKFSKAFSNGFDPDKDLDRVGVANQTTMLKSETEEIGKVFERTMLKKFGPENLNSHFLAFNTICDATEERQDAMFSLVDEDLDILVVIGGFNSSNT... | Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. | A2BP63 |
P36601 | RAD51_SCHPO | RAD51 homolog | Schizosaccharomyces | MADTEVEMQVSAADTNNNENGQAQSNYEYDVNVQDEEDEAAAGPMPLQMLEGNGITASDIKKIHEAGYYTVESIAYTPKRQLLLIKGISEAKADKLLGEASKLVPMGFTTATEYHIRRSELITITTGSKQLDTLLQGGVETGSITELFGEFRTGKSQICHTLAVTCQLPIDMGGGEGKCLYIDTEGTFRPVRLLAVADRYGLNGEEVLDNVAYARAYNADHQLELLQQAANMMSESRFSLLVVDSCTALYRTDFSGRGELSARQMHLARFMRTLQRLADEFGIAVVITNQVVAQVDGISFNPDPKKPIGGNILAHSSTTR... | Required both for recombination and for the repair of DNA damage caused by X-rays. Binds to single and double-stranded DNA, in the presence of magnesium, and exhibits DNA-dependent ATPase activity. Promotes DNA strand annealing and strand exchange via DNA recombinase activity and forms helical nucleoprotein filaments. | P36601 |
A0QJA9 | UNG_MYCA1 | Uracil-DNA glycosylase | Mycobacterium avium complex (MAC) | MTARPLSELVEPGWARALQPVAEQVARMGQFLRAEIAAGRRYLPAGPNVLRAFTYPFDEVKVLIVGQDPYPTPGHAVGLSFSVAPDVSPLPRSLANIFQEYTADLGHPPPSCGDLTPWAQRGVLLLNRVLTVRPSNPASHRGKGWEPVTECAIRALTARQQPLVAILWGRDASTLKPILAQGNCVAIESPHPSPLSASRGFFGSRPFSRANKLLAEMGADEIDWRLP | Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | A0QJA9 |
B6YUJ5 | PCP_THEON | Pyroglutamyl-peptidase I | Thermococcus | MKVLITGFEPFGGEEINPSWEAVRRLPDEIAGAELIKRQLPVTFRGVRELLPRLIVETKPDLVILTGQAGGRPNITVERVAINVMDSTMPDNEGYTPEDEPIFEGAPDAYFATLPIKAIVKALREAKIPAAVSNTAGTYVCNTAMYTVLHTIAVAGMETKAGFIHVPFIHEQALDKPRPSMALETVVKAYEVIIKTSLKA | Removes 5-oxoproline from various penultimate amino acid residues except L-proline. | B6YUJ5 |
P37303 | GLY1_YEAST | Low specificity L-threonine aldolase | Saccharomyces | MTEFELPPKYITAANDLRSDTFTTPTAEMMEAALEASIGDAVYGEDVDTVRLEQTVARMAGKEAGLFCVSGTLSNQIAIRTHLMQPPYSILCDYRAHVYTHEAAGLAILSQAMVVPVVPSNGDYLTLEDIKSHYVPDDGDIHGAPTRLISLENTLHGIVYPLEELVRIKAWCMENGLKLHCDGARIWNAAAQSGVPLKQYGEIFDSISICLSKSMGAPIGSVLVGNLKFVKKATHFRKQQGGGIRQSGMMARMALVNINNDWKSQLLYSHSLAHELAEYCEAKGIPLESPADTNFVFINLKAARMDPDVLVKKGLKYNVK... | Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | P37303 |
Q9UKY4 | POMT2_HUMAN | Dolichyl-phosphate-mannose--protein mannosyltransferase 2 | Homo | MPPATGGGLAESELRPRRGRCGPQAARAAGRDVAAEAVARSPKRPAWGSRRFEAVGWWALLALVTLLSFATRFHRLDEPPHICWDETHFGKMGSYYINRTFFFDVHPPLGKMLIGLAGYLSGYDGTFLFQKPGDKYEHHSYMGMRGFCAFLGSWLVPFAYLTVLDLSKSLSAALLTAALLTFDTGCLTLSQYILLDPILMFFIMAAMLSMVKYNSCADRPFSAPWWFWLSLTGVSLAGALGVKFVGLFIILQVGLNTIADLWYLFGDLSLSLVTVGKHLTARVLCLIVLPLALYTATFAVHFMVLSKSGPGDGFFSSAFQ... | Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient . Essentially dedicated to O-mannosylation of alpha-DAG1 and few other proteins but not of cadherins and pro... | Q9UKY4 |
P05482 | CM3C_CONGE | Mu-conotoxin GIIIC | Gastridium | RDCCTPPKKCKDRRCKPLKCCA | Mu-conotoxins block voltage-gated sodium channels (Nav). This toxin shows potent activity on Nav1.4/SCN4A (IC(50)=286 nM), and weak activity on mNav1.6/SCN8A. | P05482 |
A8ZUJ6 | GCH4_DESOH | GTP cyclohydrolase FolE2 | Desulfosudis | MKDIQKERDFRNMPIDKVGIKNLKYPIRVLDRKNGCQQTVGTINMYVDLPHESKGTHMSRFVEMLHILQPEISPKTFSVILDQMKKDLDAASAHMEVTFPYFIEKAAPVSGTPGFMEYTCKLMGTSRADGRVDLVSEVVVPISSVCPCSKEISDGGAHNQRGEVRLAIRSKKFVWIEDLIQLVEAAASCELYSVLKRVDEKWVTEKGYQNPKFVEDIVRDVAVALKNDTNITWFNISVENFESIHNHSAYATITCGRINP | Converts GTP to 7,8-dihydroneopterin triphosphate. | A8ZUJ6 |
C4L618 | CODY_EXISA | GTP-sensing transcriptional pleiotropic repressor CodY | unclassified Exiguobacterium | MNLLEKTRQLNTMLQQEASAHVDFKEMADKMREVLESNTFIVSRRGRLLGFAIKQQIENDRMKAFLVDRQFPEPYASNLFNVKETTANIDIDSEYTAFPVENHDLFLNSKTTIVPIIGGGERLGTLVLGRLANEFTEDDLVLAEYSATVVGMEILREKAAEAETSARKKAVVQMAINSLSYSELEAIEHIFEELGGNEGLLVASKIADRVGITRSVIVNALRKLESAGVIESRSLGMKGTYIKILNDNFLFELQKLKSN | DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer b... | C4L618 |
B4NXF7 | MOCS3_DROYA | Sulfurtransferase MOCS3 | Sophophora | MMESEVDSEQSRLKREIAELRAALNRKEQCLRELEASVSSDASAEEQVVGNALESPGRAVHTKLTNDDIARYSRQLILPDFGVQGQLKLKNSSVLIVGLGGLGCPAAQYLAAAGCGRLGLIDYDEVERSNFHRQILHSESRCGMSKAESARIALLELNPHCEIHCHSRLLYSQNALHIIRGYDVVLDCSDNVPTRYLLSDACVMLRKPLVSGSALKMDGQLTVYNYGNGPCYRCIYPVPPPPEAVTNCGDGGVLGAVTGTIGAMQALEAIKVIVGLGDVLAGRLLIFDGSSGLFRNIRIRSKRPNCHVCSAQPLITELID... | Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS... | B4NXF7 |
Q9CCZ4 | Y2640_MYCLE | Putative S-adenosyl-L-methionine-dependent methyltransferase ML2640 | Mycobacterium | MRTHDDTWDIKTSVGTTAVMVAAARAAETDRPDALIRDPYAKLLVTNTGAGALWEAMLDPSMVAKVEAIDAEAAAMVEHMRSYQAVRTNFFDTYFNNAVIDGIRQFVILASGLDSRAYRLDWPTGTTVYEIDQPKVLAYKSTTLAEHGVTPTADRREVPIDLRQDWPPALRSAGFDPSARTAWLAEGLLMYLPATAQDGLFTEIGGLSAVGSRIAVETSPLHGDEWREQMQLRFRRVSDALGFEQAVDVQELIYHDENRAVVADWLNRHGWRATAQSAPDEMRRVGRWGDGVPMADDKDAFAEFVTAHRL | Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity. | Q9CCZ4 |
Q6MGM6 | ATPG_BDEBA | F-ATPase gamma subunit | Bdellovibrio | MASLKDIRAQIESTKNTQQITKAMKLVSAAKLRKAQNNIVNMRPYALALRQVIADIAVTNKVSHPLMEKKEQVKNVLLVVITSDRGLCGAFNSNINKFAEAYYNSNKASLEKIDFLFVGRRGHDYFARRGIKAVDYITKLDKDISYELASKVANRVMNDYLEGSYDEVRIVHNEFKSAISQVVTAETLLPIDLGMTTFKKEADTASNFAVDMIFEPAPEQIIKELLEKHFELQVYRCMSESVAGEHGARMSAMENATNNAKEMINKLTLTYNKLRQEKITTELIEIVSGAEALKG | 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. | Q6MGM6 |
C1DCE9 | PLSX_LARHH | Phosphate-acyl-ACP acyltransferase | Laribacter | MTLTVAVDAMGGDVGVGVTVPAAVDFLDRHPDVRLILVGQPDAIEDELTRLARPRSGRLTVHAASQVVAMDDSPQSALKNKKDSSMRVAINLVKEGQAQAAVSAGNTGALMATARFVLKTIPGIDRPAIAKLLPTMKGESCVLDLGANVDCTPEQLLQFGIMGATLIEGVTGRNNPTVGLLNIGSEEIKGNDTVKQAAELLRNSSLNFYGNVEGNDIYLGTVDVIVTDGFTGNVALKTSEGLAHMVGALLKQEFGRNLFTRLSALAALPVLKHFKKRLDSPALQWRQSGRPARHRGQEPRRHRQPRFWLCHRRGRRRSPR... | Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. | C1DCE9 |
I1L3T1 | 708D1_SOYBN | UDP-glucose:2-hydroxyflavanone C-glucosyltransferase | Glycine subgen. Soja | MSSSEGVVHVAFLPSAGMGHLNPFLRLAATFIRYGCKVTLITPKPTVSLAESNLISRFCSSFPHQVTQLDLNLVSVDPTTVDTIDPFFLQFETIRRSLHLLPPILSLLSTPLSAFIYDITLITPLLSVIEKLSCPSYLYFTSSARMFSFFARVSVLSASNPGQTPSSFIGDDGVKIPGFTSPIPRSSVPPAILQASSNLFQRIMLEDSANVTKLNNGVFINSFEELEGEALAALNGGKVLEGLPPVYGVGPLMACEYEKGDEEGQKGCMSSIVKWLDEQSKGSVVYVSLGNRTETRREQIKDMALGLIECGYGFLWVVKL... | UDP-glucose-dependent glucosyltransferase catalyzing the c-glucosylation of the A ring of 2-hydroxynaringenin. Also active toward phloretin, but not toward naringenin and apigenin. | I1L3T1 |
O82018 | CALM_MOUSC | Calmodulin | Mougeotia | MADQLTEEQIAEFKEAFSLFDKDGDGSITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLNLMARKMKDTDSEEELKEAFKVFDKDQNGYISAADWRHVMTNLGEKLTDEEVDEMIREADVDGDGQVNYEEFVKMMMAK | Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. | O82018 |
Q1ELU9 | LAT5_LACTA | Latarcin-5 | Lachesana | MKYCVVILALLVALVCITESRSTETGYAVAETLEDNDLDELQAYLEEIAEASEMEDFSNIEEARGFFGKMKEYFKKFGASFKRRFANLKKRLG | Has antimicrobial activity against. Gram-positive bacteria (A.globiformis VKM Ac-1112 (MIC=1.1 uM), and B.subtilis VKM B-501 (MIC=0.6 uM)), Gram-negative bacteria (E.coli DH5-alpha (MIC=0.6 uM), E.coli MH1 (MIC=0.6 uM), and P.aeruginosa PAO1 (MIC=18 uM)), and yeasts (P.pastoris GS115 (MIC>37 uM), and S.cerevisiae Y190 ... | Q1ELU9 |
P57126 | GYRB_BUCAI | DNA gyrase subunit B | Buchnera | MKNIYDSSNIKILRGLDAVRKRPGMYIGDTDDGSGLHHMVFEIVDNSIDEALSGYCKEIIVTIHSDNSVSVKDDGRGIPTDIHPEENISAAEVILTVLHSGGKFDNASYQISGGLHGVGISVVNALSEKLELIIDKNKKKYQQIYRHGKPENPLSIIGTTDTTGTYIRFWPSYKTFTNNIKFQYEILSKRLRELSFLNSNIAIYLEDNRTSIKNCYHYKGGIKAFIKFLNAKKTPIHTHIFYFRSTKDQIELEIAMQWNNSHQENILCFTNNIPQKDGGTHLAGFRSGMTRTLNLHIEREGYNKKNKTTIIGEDVREGLT... | A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which invo... | P57126 |
Q9W5Y0 | NEP3_DROME | Neprilysin-3 | Sophophora | MTRYKQTEFTEDDSSSIGGIQLNEATGHTGMQIRYHTARATWNWRSRNKTEKWLLITTFVMAITIFTLLIVLFTDGGSSDATKHVLHVQPHQKDCPSGNELPCLNKHCIFASSEILKSIDVTVDPCDDFYGYSCNQWIKNNPIPEGKSTWGTFGKLEQMNQLIIRNVLEKPAKSFKSDAERKAKVYYESCLDADEHMEKLGAKPMNDLLLQIGGWNVTKSGYNVANWTMGHTLKILHNKYNFNCLFGWAIGEDDKNSSRHVIQIDQGGLTLPTADYYNNKTDNHRKVLNEYIEYMTKVCVLLGANESDARAQMIGVINFE... | Metalloendoprotease which is required in the dorsal paired medial neurons for the proper formation of long-term (LTM) and middle-term memories (MTM). Also required in the mushroom body neurons where it functions redundantly with neprilysins Nep2 and Nep4 in normal LTM formation. | Q9W5Y0 |
Q9RLM4 | MTD1_NEIMC | Probable modification methylase NmeDIP | Neisseria | MMSLKIQPAVPKKSDKPSATNRDCQNFKREKNNLPFQLTDKSCNLDISIRQERKKTLIFSFFSGAGFLDLGFELSGFDIAFVNEVHPPFLEAYKYSRSRMDIPKPKYGYFKGSIDECLYAEKAKDLAGWVKKEKQNGIIVGFIGGPPCPDFSIAGKNKGKDGENGKLSQSYVDLICKNQPDFFVFENVKGLYRTAKHREFFNALKRQLSDFGYVCTEKLINAIEYGVPQDRERIILVGFLSQHVDALQKFDWDAHISFPDALEKDWPTTEEVGRVVSQPANIYPELTVQYWFNRNGVDTHPNASKHFQPRAGLEKFQTIS... | A methylase that recognizes the double-stranded sequence 5'-RCCGGB-3', methylates C-2 on both strands, and protects the DNA from cleavage by the NmeDI endonuclease. | Q9RLM4 |
B5YEQ1 | OBG_DICT6 | GTP-binding protein Obg | Dictyoglomus | MFIDRAKIYVKAGDGGNGCVAFRREKFVPRGGPAGGDGGKGGDVIIEADENLDTLLDFHYKRHYYAERGEHGKGKNQKGKDGEDLIIKVPTGTLIFDAETGELIADLVSHGQRVVVARGGKGGRGNTHFATSTRQAPYFAEKGEKGEERWLYLELKLLADVGLVGLPNAGKSTLLSKISNANPEIAPYPFTTKTPNLGVVEREDITFTVADIPGLIEGAHENKGMGDEFLRHIERTLVLVFVIDAADLVTPPQKAYEILKKELYLYSPKLLEKPRIIAINKIDLPEAQERLPEIEKWLKNEGVPYVFISAKEGINIDKLL... | An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control. | B5YEQ1 |
Q9VGB5 | CP135_DROME | CYPCCCXIIIA5 | Sophophora | MLTLQIFEAFAIILCVYFLWSRRRFYIMMLKLPGPMGFPFIGLAFEYIRLKRKIRLRTILFKIYGKTVLTWIGLTPVLVTCEPKILEDIFTSPNCSNRSSVVDKAISSCLGLGLLTLKNNHWNERRKLLLPSFKNNAVLSFVPVLNNEANFLVTLLAEFVDGGDINLLPELNKWSFKIAAQITMGDEVRNQANYQNGNLLESYKALNNLIPIGVVMPWLRNKYLGKLFSYEKRRLEAATQSNAFIKDIIDKKLSSTDNSSEPALIDRILNLVRIGELSYDDVMGEFSNIIFAASDTLSITVNNVLILMAMFPKYQDNVFE... | May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. | Q9VGB5 |
O69082 | COAE_PSEPG | Dephosphocoenzyme A kinase | Pseudomonas | MATAAFTPWILGLTGGIGSGKSAAAERFVELGVHLVDADQAARWVVEPGRPALASIVERFGPGVLQADGQLDRAALRQLIFADPAQRKWLEQLLHPLIGQEIFSYLAKAQSPYAIYVSPLLIESGQYHKTQRVLVIDAPQELQIARTLARDNTSAEQVQAILQAQLAREERLRHADDVLVNDGDLAALHEQIDRLHHFYLTLKGGQP | Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. | O69082 |
Q8G5L9 | UVRB_BIFLO | Excinuclease ABC subunit B | Bifidobacterium | MGFNIERADKPFVVKSPYKPSGDQPQAIAELAERIENGENDVVLMGATGTGKTATTAWLIEKLQRPTLIIEPNKTLAAQLCAEFRELMPDNAVSYFVSYYDYYQPEAYIPQTDTYIEKDSNINDDVERLRHQATANLLTRRDCVVVATVSCIYGLGTPEEYAGRMLFLKVGQEINRDDLLRQFVAMQYKRNDIAFTRGTFRVRGDTVEIIPVYEELAVRIEFFGDEIDRISTLHPLTGDEIDEENEVHIFPASHYVAGPERMERALKTIREELEERLAELRKQGKELEAQRLNMRTTYDLEMLTQVGVCSGVENYSRHFD... | 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 bindi... | Q8G5L9 |
P81730 | ACLY_ACHLY | Achromolysin | Achromobacter | AQVGTGPGGNQKIGQYEYGSGGRPFLDVAQSGSTYTFNTTNLTVNLNHGTSGSTAYSYTGPRNTINGAYSPLNDAHYFGRDYWTPSTNFNQGGQGVRQAAADLGYSTADVIDAFRQVGV | Has staphylolytic activity. | P81730 |
Q1HN32 | BDNF_ERYJO | Brain-derived neurotrophic factor | Eryx | SCMKAAPMKEVSIRGQGSLAYPGLRTQGNLETLSGPNDATRGLTSLADTFEHVIEELLDEQQAIQPSKENKDADLYSTRVMLSSQVPLEPPLLFLLEEYKNYLDAANMSMRVRRHSDPARRGELSVCDSTSEWVTAAEKKTAVDMSGATVTVLEKVPVPKGQLKQYFYETKCSSKGYAKEGCRGIDKRYWNSQCRTTQSFVRALTMDNKKRVGWRFIRIDTSC | Promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. | Q1HN32 |
A1TA72 | DER_MYCVP | GTP-binding protein EngA | Mycolicibacterium | MTDDGTWSDESDWELGPDDISDAIEEVSAPPPVVAVVGRPNVGKSTLVNRILGRREAVVQDVPGVTRDRVSYDASWSGQRFMVQDTGGWEPDAKGLQQLVAEQASVAMRTADAIIFVVDSVVGATAADEAAAKLLQRSGKPVFLAANKVDNERGEADAAALWSLGLGEPHPISAMHGRGVADLLDAVVDALPTISEVAGAGGGGPRRVALVGKPNVGKSSLLNRLSGDERSVVHDVAGTTVDPVDSLIEMDGKLWRFVDTAGLRRKVGQASGHEFYASVRTHGAIDAAEVAIVLVDASQPLTEQDQRVLSMVVEAGRALV... | GTPase that plays an essential role in the late steps of ribosome biogenesis. | A1TA72 |
Q8CXT8 | SSRP_LEPIN | Small protein B | Leptospira | MVKKKEESGHSPLVNKKAKFNFELISFIEAGIVLSGSEVKSLRDKKGNLTDAFAKIKNGEVFLENFSIAPYKNGGYANHPEIRPRKLLLHKKEIEKLERQVKEKGLVLVATKVYFKNNLRVKVEIAVGKPKKLHDKRDDLQKKDAQQEIARALKSSNRYQ | Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemb... | Q8CXT8 |
O24738 | BARX_STRVG | 2-oxo-3-(phosphooxy)propyl 3-oxoalkanoate synthase | Streptomyces | MTSTVPRELVHRAAVAEVFLTGWSRTAENRFALTAQWPRAHSYFTPVNGCYDPLLASETIRQVGTLLSHAEFGVSFGDQFLMWDLHHSVRPEQAGVGAAPADLELDVICSDIRRRGRRLAGMRYEVTLYCGGQVIATGGAAFDCTSPAVYQRLRGDRVGATGVRPLPQPLAPASVGRFLTTDVVLSATERPLEWQLRVDEQHPVLFDHPVDHVPGMVLMESARQAAQAIDPSRPFLPTTMRSEFSRYAELDRPCWIQAEPLPAADNGDRQVRVTGHQDDTTVFSCLIGTRGAAE | Involved in the biosynthesis of virginiae butanolide (VB), a gamma-butyrolactone autoregulator that triggers the production of the streptogramin antibiotic virginiamycin. | O24738 |
Q9NR64 | KLHL1_HUMAN | Kelch-like protein 1 | Homo | MSGSGRKDFDVKHILRLRWKLFSHPSPSTGGPAGGGCLQQDGSGSFEHWGPSQSRLLKSQERSGVSTFWKKPSSSSSSSSSPSSSSSSFNPLNGTLLPVATRLQQGAPGQGTQQPARTLFYVESLEEEVVPGMDFPGPHEKGLVLQELKVEPDNSSQATGEGCGHRLSSTGHSMTPQSDLDSSSSEEFYQAVHHAEQTFRKMESYLKQQQLCDVILIVGNRKIPAHRLVLSSVSDYFAAMFTSDVCEAKQEEIKMEGIDPNALWDLVQFAYTGCLELKEDTIENLLAAACLLQLPQVVEVCCHFLMKLLHPSNCLGIRAF... | May play a role in organizing the actin cytoskeleton of the brain cells. | Q9NR64 |
A0JVC9 | LIPB_ARTS2 | Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase | Arthrobacter | MTLEFSTLGLAPDFVDYMKGWDTQRELHDKVVAAEAPSTVLLLEHAAVYTAGKLTEDHERPFDGTPVVAVDRGGKLTWHGPGQLIAYPILKLKNRSGIRDYVERLEAVMIAVMADYGINAERIKGRAGVWIKADSKGPDRKIAAIGIRVLDGVTMHGIAINCNNDLAPYAQIIACGITDAGVTTMSIEAGRTITPGDIAERVVEEFRKHEEALVSSPEGALL | Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | A0JVC9 |
Q87WV2 | MURA_PSESM | UDP-N-acetylglucosamine enolpyruvyl transferase | Pseudomonas | MDKLIITGGVRLDGEIRISGAKNSALPILAATLLADGPVTVQNLPHLHDITTMIELFGRMGIEPVIDEKLSVEIDPRTIKTLIAPYELVKTMRASILVLGPMVARFGEAEVALPGGCAIGSRPVDLHIRGLEAMGAIIDVEGGYIKAKAPEGGLRGAHFFFDTVSVTGTENIMMAASLANGRSVLENAAREPEVVDLANFLIAMGAKIHGAGTDTITIDGVKRLGSATYKVMPDRIETGTYLVAAAVTGGRVKVKDTDPTILEAVLLKLQEAGAEVTTGEDWIELNMHGKRPKAVNVRTAPYPAFPTDMQAQFISLNAIA... | Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. | Q87WV2 |
Q746Y5 | GATC_GEOSL | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C | Geobacter | MKITRTDVEHVATLARLELTEDEKDRFTGQLDAILAYVEKLNELDTDGIIPTSHAVPVENAFREDEVRPSIGVENALANAPDRVEGFFRVPRVIE | 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 ... | Q746Y5 |
A6V4E8 | NUOB_PSEA7 | NDH-1 subunit B | Pseudomonas | MQYKLTRIDPDAANDQYPIGERETVADPLVEGQVHKNIFMGKLEDVLNSTVNWGRKNSLWPYNFGLSCCYVEMTTAFTAPHDIARFGAEVIRASPRQADFMVIAGTCFIKMAPVIQRLYEQMLEPKWVISMGSCANSGGMYDIYSVVQGVDKFLPVDVYIPGCPPRPEAFLQGLMLLQESIGQERRPLSWVVGDQGVYRADMPAQKDLKREQRIQVTNLRSPDEV | 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 t... | A6V4E8 |
B9KIW9 | EFTS_ANAMF | Elongation factor Ts | Anaplasma | MKVGVEAIRELRQITGAGLGDCKEALETCSGDMEKAKVYLREKGLSKAYKKSHRDAADGLVAVRVEGDKGAILKLGSETDFVARNEKFRSLAAELVSSLLKHGAEDLSSFSASPYDGGSGVSVADEVVNAAAVLGEHIVLSGIGFLELGGPGVIGSYIHGAVGEGIGRAGALVALEATTAKTEALLEFARQLAMHIVAAKPESVSVETLSNDIVEREREIVAKQVEALGKPESVASKIVDGRMQKFFEDMVLLEQTFIMDGSTKIRDLLHNKGQDLGCEVRIVAYRLFSVG | Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. | B9KIW9 |
A1KB36 | RL10_AZOSB | 50S ribosomal protein L10 | Azoarcus | MGLNLDDKKAVVAEVSAQVANAQTIAVAEYRGIAVGDLTALRAKARESGVYLRVLKNTLVRRAIAETPFAGLADQLTGPLIYGISEDPVAAAKVLNDFAKGNDKLVLKAGSYAGNVLDKAGVQALASIPSREELLAKLLGVMQAPVSGFAGALAALAKKREEEGAAA | Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. | A1KB36 |
Q58403 | Y996_METJA | Metalloprotease MJ0996 | Methanocaldococcus | MLNLEKIEKLLEVGDYADIRINFGESNTITLKDGKIEEISSGFGNGVAVRVLYKNGWGFVTSNIVSEEEIEKLINKAYKMAKISNEYSEKEIILKDYKAIIDNYKMIGKINPTDVDIEEKKEIIIDTYKNMTDEKIKSISVSYSDVFGKRIFMISEGSRIEGEITRCIMYMNCVAKENGNLQYGAERTGGFGFEKIKDNYLNLALEAKNRALRLLKAKPCPKGKFKVILDPELAGVFIHEAVGHASEADLVLQNDSVFKDKLGERVGSEYVTVIDDATIEGAFGSYKYDDEGVEGKKTVIIENGILKTYLHSRETAGRMD... | Probable metalloprotease. | Q58403 |
Q8K441 | ABCA6_MOUSE | ATP-binding cassette sub-family A member 6 | Mus | MKELSVHVRQQTRALLHKILLKKWRRKRESLLEWSIPIIIGLHMGLFSYLARNIQVLEVPPQDLGSLNEFNGSSLVVVYTPISNITQQIMNKTTFAPTMKGTRIIGVPSIEDLDEVLLHNIPDALGVIFNDSFSYQLKVLRMYGNPFLKEDLLAHCWDTHSQAFCSLSKYWERGFVALQTAINAGIIEVTTNHSVMEELMSIDGINMKTLPFIPRDLSDYEIFILFCLLYFSSFIYFASSNVTKERKQCKEVMKVMGLQDSAFWLSWGLIYVGFIFIISIFIAIIITSTQIIMMTGFLVIFTLFFLYGLSLIAVTFLMAV... | Probable transporter which may play a role in macrophage lipid transport and homeostasis. | Q8K441 |
P00614 | PA2TA_OXYSC | Phosphatidylcholine 2-acylhydrolase | Oxyuranus | NLLQFGFMIRCANRRSRPVWHYMDYGCYCGKGGSGTPVDDLDRCCQVHDECYGEAVRRFGCAPYWTLYSWKCYGKAPTCNTKTRCQRFVCRCDAKAAECFARSPYQNSNWNINTKARCR | Monomer (alpha chain): Snake venom phospholipase A2 (PLA2) alpha chain that possesses the same high enzymatic activity as the heterotrimer. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. | P00614 |
C6DDH3 | CYSI2_PECCP | Sulfite reductase [NADPH] hemoprotein beta-component 2 | Pectobacterium | MSEKYVFSEKHPGPLVVEGKLTDAERMKTESNFLRGTIAEDLNDGLTGGFKGDNFLLIRFHGMYQQDDRDIRAERAEQKLEPRHAMLLRCRLPGGVMTPEQWLRIDKFAGESTIYGSIRITNRQTFQYHGILKSNVKPVHQMLNSIGLDALATANDMNRNVLCTSNPIESELHQQAYEWAKKISEHLLPRTRAYAEIWMDQEKVATTDEEPILGSTYLPRKFKTTVVVPPQNDVDLHANDLNFIAIADNGRLVGFNVLVGGGLSIAHGDKATYPRTASELGYISIEHTLAIAEAVVTTQRDWGNRTNRKNAKTKYTLERV... | Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. | C6DDH3 |
Q4ULR3 | ILVE_RICFE | Probable branched-chain-amino-acid aminotransferase | spotted fever group | MTMIKLEQIFWHVWINGDLVPYQFARIHVLTHSLHYSGSVFEGERAYNGKVFKLKEHTERLIKSAEALGLKVPYSVDEIIKAHELVIKQNNIKDAYIRPLIWCGDESLNITNPDLSTNLLIAGIPSMPRSFEKGINLHVGRWRKAIPDSTPVQSKSAAQYNMAITSKKEAKALGYDDALLLDYEGYIAECTTTNIFFVKDKTLYTPIADRFLNGITRQTIIEIAKDLGLEVKEERLKLEQIENFTGCFVTGTAIEVQNIDSIDLGNKKITFDDHQIADRLKKEYGRIVRE | Acts on leucine, isoleucine and valine. | Q4ULR3 |
C5A1L9 | AMPPA_THEGJ | Nucleoside monophosphate phosphorylase | Thermococcus | MRAKVRILDVFSGRYSVFINEEEAKKAKLHPDDLVKVESGKKTIYGSLAISNLVGPGEVGVSRDVLQLHSLSEGEVVTLTPVGTPESVRYIKKKMHGEKLRKVEIEAIVRDIVDRKLRDIEISSFVTALEINGLDMDEIAALTIAMAETGDMLDIDRKPIMDVHSIGGVPGNKTNILVVPIVAAAGLTIPKTSSRAITSAAGTADVVEVFTNVSFSLDEIKRIVEKVGACLVWGGALNLAPADDITIKAERALSVDPRGLMLASIMSKKYAMGSQYVLIDIPTGKGVKVETMDEARALARDFIELGKRLGQYVEVAITYG... | Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. | C5A1L9 |
Q8YVQ3 | BIOB_NOSS1 | Biotin synthase | Nostoc | MSVGRIRYDWHKAEIRAVYDTPLLELIYQAASVHRQFHNPKQIQVCKLISIKTGACPEDCSYCAQSSRYQTEVKPQALLDKQTVVEIAQNAKQKGVSRVCMGAAWREVRDNSQFDRVLEMVKDVTDMGLEVCCTLGMLTSEQAKKLETAGLYAYNHNLDTSSDYYSTIITTRTYGDRLNTIENVRQTNVTVCSGGILGLGESIDDRVAMLQTLATLNPHPESVPINILSQVEGTPLEDQPDVPVWDVVRMIATARIVMPTSDVRLSAGRARLSQVEQAFCFMAGANSIFSSDDNKMLTVTTPCPDYDADQEMLNLLGLEM... | Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. | Q8YVQ3 |
C3MZY6 | RNP4_SULIA | Rpp21 | Sulfolobus | MRIKNKIKKRIIELIDLAYITARKGDLELAREYIKLAEMYSRKGRVKIPLKYKRMFCRKCYTPLITGVTERRRIRSKILIRTCLICNWQRRYVLSRNKGSNKEN | Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. | C3MZY6 |
Q8NGP6 | OR5M8_HUMAN | Olfactory receptor OR11-194 | Homo | MRRNCTLVTEFILLGLTSRRELQILLFTLFLAIYMVTVAGNLGMIVLIQANAWLHMPMYFFLSHLSFVDLCFSSNVTPKMLEIFLSEKKSISYPACLVQCYLFIALVHVEIYILAVMAFDRYMAICNPLLYGSRMSKSVCSFLITVPYVYGALTGLMETMWTYNLAFCGPNEINHFYCADPPLIKLACSDTYNKELSMFIVAGWNLSFSLFIICISYLYIFPAILKIRSTEGRQKAFSTCGSHLTAVTIFYATLFFMYLRPPSKESVEQGKMVAVFYTTVIPMLNLIIYSLRNKNVKEALIKELSMKIYFS | Odorant receptor. | Q8NGP6 |
Q4JC35 | KDGA_SULAC | 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase | Sulfolobus | MEIISPIITPFDKQGKVNVDALKTHAKNLLEKGIDAIFVNGTTGLGPALSKDEKRQNLNALYDVTHKLIFQVGSLNLNDVMELVKFSNEMDILGVSSHSPYYFPRLPEKFLAKYYEEIARISSHSLYIYNYPAATGYDIPPSILKSLPVKGIKDTNQDLAHSLEYKLNLPGVKVYNGSNTLIYYSLLSLDGVVASFTNFIPEVIVKQRDLIKQGKLDDALRLQELINRLADILRKYGSISAIYVLVNEFQGYDVGYPRPPIFPLTDEEALSLKREIEPLKRKIQELVH | Involved in the degradation of glucose and galactose via the Entner-Doudoroff pathway. Catalyzes the reversible cleavage of 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-3-deoxygluconate (KDG) forming pyruvate and glyceraldehyde 3-phosphate or glyceraldehyde, respectively. It is also able to catalyze the reversib... | Q4JC35 |
O19000 | MT1_CANLF | Metallothionein-I | Canis | MDPDCSCSTGGSCTCAGSCKCKECKCTSCKKSCCSCCPVGCAKCAQGCICKGASDKCSCCA | Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. | O19000 |
Q8EK81 | EFTU1_SHEON | Elongation factor Tu 1 | Shewanella | MAKAKFERSKPHVNVGTIGHVDHGKTTLTAAISHVLAKTYGGEAKDFSQIDNAPEERERGITINTSHIEYDTPSRHYAHVDCPGHADYVKNMITGAAQMDGAILVVASTDGPMPQTREHILLSRQVGVPFIIVFMNKCDMVDDAELLELVEMEVRELLSEYDFPGDDLPVIQGSALKALEGEPEWEAKILELAAALDSYIPEPERDIDKPFLMPIEDVFSISGRGTVVTGRVERGIVRVGDEVEIVGIRTTTKTTCTGVEMFRKLLDEGRAGENCGILLRGTKRDDVERGQVLSKPGSINPHTTFESEVYVLSKEEGGRH... | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. | Q8EK81 |
Q1D651 | GLGE_MYXXD | (1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase | Myxococcus | MTERLGSVFIEGVSPELDAGRHAVKRVVGERCTVKADVFKEGHDVLVAVIRWRQVTPRAQQTDWEEVPMRFLGNDRWEGEFPLTRNGRYEYTIEAWPDLFRTWTSELKRKVDAGRDVRSELLEGAALLEGAVARARTAKQPDDARVLGEAAVRLRQPPSPDLLAVALAPELADVASTHPDRSLARRYDKVLEVFADREKARFSAWYEFFPRSAKRDGVTHATFRDAEGWLPYIQQLGFDTVYLPPIHPIGRTARKGKNNSLAAAADDVGSPWAIGASEGGHKAVHPKLGTLEDFRHFVETAQAHGIEVALDLAFQCSPDH... | Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB. | Q1D651 |
A5E5I9 | MAP2_LODEL | Peptidase M | Lodderomyces | MSTDTSIKAGIDSIRAKADDLHLAEDSSNGTQANLDKHQIKATTAVGQDNGNNAGVADHKNDKNNKNNKNNNDDDDDDEDDDVAAAAAAVGDAGSDKKKKKKKSSNKKKKKKLVSIDQSYPDGVFPEGEWQEYGLDSNKYRTTSEEMRYLDRQQNNKWEDFRKGAEIHRRVRAKAKSSIRPGMTMIEIADLIENSVRAYASADHTLKAGIGFPTGLSLNHVAAHYTPNTGDKLTLGKDDLMKVDIGVHVNGRICDSAFTMTFNEDGKYDSIMQAVKEATNTGVKEAGIDVRLNDIGAAVQEVMESYEMELDGKTYPIKCI... | Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | A5E5I9 |
Q4JC68 | XPD_SULAC | ATP-dependent DNA helicase Saci_0192 | Sulfolobus | MLKLRDWQEKLKDKVIEGLRNNFLVALNAPTGSGKTLFSLLVSLEVKPKVLFVVRTHNEFYPIYRDLTKIREKRNITFSFLVGKPSSCLYAEKGAESEDIPCKYCELKGSIVEVKTDDSPLSLVKKLKKDGLQDKFCPYYSLLNSLYKADVIALTYPYFFIDRYREFIDIDLREYMIVIDEAHNLDKVNELEERSLSEITIQMAIKQSKSEESRRILSKLLNQLREVVLPDEKYIKVENVPKLSKEELEILADDYEDIRKDSLKQGKVNKIHIGSILRFFSLLSIGSFIPFSYSKRLVIKNPEISYYLNLLNDNELSIIL... | ATP-dependent 5'-3' DNA helicase involved in nucleotide excision repair (NER) of DNA. | Q4JC68 |
B8I5A9 | ILVD_RUMCH | Dihydroxy-acid dehydratase | Ruminiclostridium | MRSDIVKKGIEKAPHRSLFKAMGYTDEELERPLIGVANSKSEIIPGHIHLDKLTEAVKAGIRMAGGTPIEFGAIGVCDGIAMGHTGMKYSLATRELIADSCEAMSKAHSFDGMVFIPNCDKIVPGMLMAAARINIPSIVISGGPMLSLNRDGKQLDLNSLFEAVGSYKAGTMTKEEVDDIEDHACPGCGSCSGMFTANSMNCLTEVLGMGLTGNGTIPAVYAERIRLAKYAGMKIMELVEKDIKPSDILTNEAFENALTVDMALGCSTNSVLHLPAIANELGIEINLDIINEISSRTPNLCKLAPAGKYHIQDLYSAGGV... | Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (... | B8I5A9 |
C1D0H8 | NUOH_DEIDV | NDH-1 subunit H | Deinococcus | MPDWLLTLLITVVKAVAVILALLTTFAYMTLVERKLLGRFQIRVGPNRVGPMGLLQPAADAIKSIFKEDLQVTLADKLVYTLAPIIAIGMALTAFGGIPAGPEGSLFGENPWVYNLDAGVLALLALTSMGVYGIFLGGWASGSKYPMLGGLRSSAQMISYELGMGLSILGLLMLVGSTRFTDIVLWQGANGWMILFQSLGFALFLISSFAETNRTPFDLVEAEQELVAGYLTEYSAIKWALFQMAEYVNMITASALMSTLFFGGWRGPGFLNGIIPGIADIPILWLVVKIGFFLFVFIWVRATLPRLRYDQLMRFGWKLL... | 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 t... | C1D0H8 |
B7NPE1 | FPG_ECO7I | DNA-(apurinic or apyrimidinic site) lyase MutM | Escherichia | MPELPEVETSRRGIEPYLVGATILHAVVRNGRLRWPVSEEIYRLSDQPVLSVQRRAKYLLLELPEGWIIIHLGMSGSLRILPEELPPEKHDHVDLVMSNGKVLRYTDPRRFGAWLWTKELEGHNVLAHLGPEPLSDDFNGEYLHQKCAKKKTAIKPWLMDNKLVVGVGNIYASESLFAAGIHPDRLASSLSLAECELLARVIKAVLLRSIEQGGTTLKDFLQSDGKPGYFAQELQVYGRKGEPCRVCGTPIVATKHAQRATFYCRQCQK | Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. ... | B7NPE1 |
P59097 | P2OX_TRAHI | Pyranose:oxygen 2-oxidoreductase | Trametes | MSASSSDPFHSFAKTSFTSKAAKRATAHSLPPLPGPGDLPPGMNVEYDVAIVGSGPIGCTYARELVEAGFNVAMFEIGEIDSGLKIGSHKKNTVEYQKNIDKFVNVIQGQLMPVSVPVNTMVVDTLSPASWQASTFFVRNGANPEQDPLRNLSGQAVTRVVGGMSTHWTCATPRFEKLQRPLLVKNDSKADDAEWDRLYKKAESYFKTGTTQFAESIRHNLVLKKLQEEYKGVRDFQQIPLAATRQSPTFVEWSSAHTVFDLENRPNKDAPKQRFNLFPAVACTNVRRDNANSEIVGLDVRDLHGGKSITIKAKVYILTA... | Catalyzes the oxidation of various aldopyranoses and disaccharides on carbon-2 to the corresponding 2-keto sugars concomitant with the reduction of O(2) to H(2)O(2). Plays an important role in lignin degradation of wood rot fungi by supplying the essential cosubstrate H(2)O(2) for the ligninolytic peroxidases, lignin p... | P59097 |
A2RFN2 | RF2_STRPG | Peptide chain release factor 2 | Streptococcus | MEVAEIRQKIVENKEKLTSFRRSLDLDRLEEEIALLENHMTEPDFWNDNIAAQKTSQELNELKGKYDTFHNMQELSDETELLLEMLDEDDSLKEELEENLMQLDKIMGAYEMTLLLSEPYDHNNAILEIHPGSGGTEAQDWGDLLLRMYTRFGNANGFKVEVLDYQAGDEAGIKSVTLSFEGPNAYGLLKSEMGVHRLVRISPFDSAKRRHTSFASVEVMPELDNTIEVEVRDDDIKMDTFRSGGAGGQNVNKVSTGVRLTHIPTGIVVSSTVDRTQYGNRDRAMKMLQAKLYQLEQEKKAQEVDALKGDKKEITWGSQI... | Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA. | A2RFN2 |
F1Q8J0 | RNPC3_DANRE | RNA-binding protein 40 | Danio | MAETDEADVQTKKSKTLIIRHLPRELSRDEKEDLLKYFGASSVRVLSEKGPLKHMAFATFSSETSASKALNRLHQLRILGRTLVVEFAKDQDSASILKDPPVSDRTAAAVAEKEKKEKQQPSVPLMDTSIAPSLGLKFQTNPTLKYLYPPPSSGILTNITHTLLSVPKFYVQVLHLMNKMNLPSPFRPVTAPPPMFEMPSGPLPPPFPPENPPLPEHDESGSEEESEYESEDEEERERMIRLMGLVNQPCKRPLRTKTSSKRKKPKLKDLLFIPKPDSHGPSGPVLQPADVFEQPHALGQKKIEFHISSEVSAILEGPGQ... | Participates in pre-mRNA U12-dependent splicing, performed by the minor spliceosome which removes U12-type introns. U12-type introns comprise less than 1% of all non-coding sequences. | F1Q8J0 |
Q6LTK3 | FADJ_PHOPR | 3-hydroxyacyl-CoA dehydrogenase | Photobacterium | MTQHESANSQPSAFSLTFGDNGVAWLKIDVPNERMNTLQSAFVDQVTDVLAQLKDKKDIKGMVVYSGKPDNFIAGADIRMLAACQTADEAQQLAAKGQELFGQLEALPFHVVAAIHGPCLGGGLELALACHSRVCSDDDKTRLGLPEVQLGLLPGSGGTQRLPRLIGVANALDMILTGKQLRAKKAKNLGLVEEAVPLSILLDIAEKQALKGKPKRKGSFQEWAMGGNALGRSVVFDQAAKKTHEKTRGNYPAADAILDVIKYGLQHGMKKGLDQEAKRFGELVMTSESAALRSIFFATTAMKKESGSDALPATIKKVGV... | Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities. | Q6LTK3 |
B4T8Y4 | CBID_SALHS | Cobalt-precorrin-6A synthase | Salmonella | MSELSFDAPVWHHGKALRKGYTTGSCATAAAKVAALMVLRQHLIHQVSIVTPSGVTLCLNVESPHIEGQQAIAAIRKDGGDDVDATHGMLIFARVTLNDSGEITLTGGEGIGTVTRKGIGLPLGSAAINRTPRHTIESAVREAIGPARGADVEIFAPEGEVRAQKTYNSRLGILGGISIIGTTGIVTPMSEESWKRSLSLELEIKRASGLTRVILVPGNHGERFVREQMGVDTQAVVTMSNFVGYMIEEAVRLGFCQIVLVGHPGKLIKIAAGIFHTHSHIADARMETLVAHLALLGAPLELLTLVSDCDTTEAAMEHIE... | Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A. | B4T8Y4 |
B1VZM3 | LIPA_STRGG | Sulfur insertion protein LipA | Streptomyces | MSAVAPDGRKMLRLEVRNSQTPIERKPEWIKTRAKMGPEYKQLQQLVKGEGLHTVCQEAGCPNIFECWEDREATFLIGGDQCTRRCDFCQIDTGKPQALDRDEPRRVGESVVTMDLNYATITGVARDDLEDGGAWLYAETVRQIHTLTAEREAGATKVELLIPDFNAEPEQLAEVFSSRPEVLAHNVETVPRIFKRIRPGFRYERSLEVITRAREAGLITKSNLILGMGETREEVSEALQDLYDAGCELITITQYLRPSVRHHPVERWVKPHEFVELKDEADAIGYSGVMSGPLVRSSYRAGRLFQQAMEARGVAAAGSA... | Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | B1VZM3 |
A8ZRQ3 | RS6_DESOH | 30S ribosomal protein S6 | Desulfosudis | MRRYETIFIADPDLSPENQAQLFEKATTLIDANSGVLVEFDEWGTRRLAYEIRKKPRGHYVRLDFCGDGATVQGLENAFRIDERVLKFMTVFLSENADPEALRQAIAEEKEKKAEGQAAADAAPADGDDEAPKQPAPASDDDAPKQPETEAGSDETEAAAADKSDDNA | Binds together with S18 to 16S ribosomal RNA. | A8ZRQ3 |
Q9JRN7 | TLD_AGGAC | GDP-4-keto-6-deoxy-D-mannose reductase | Aggregatibacter | MKILVTGGSGFIGKNLIYLLREKREFEVFGATVEETMDLTNPCSVQSVLEKTKPDFIVHLAALTFVPNNNPITFYLVNTIGTENLLRSIVDLNVAKLGVLCFSTAGIYGIQETKLLSESLTPKPVNHYSMSKHCMEHIVNKYRCFRGITVVRPFNVLGLGQNINFLVPKMVSAFVKKDKTIELGNLDSVRDFISVNDCCDIIYRLISKLIENETINICTGIGYSVYQIFQLLCEISMHQMEIKQNELFVRHDDIPQMIGDPSKLLNVLGNDYRFTSVRAILEEMYKNRLLELSI | Catalyzes the conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-6-deoxy-D-talose. | Q9JRN7 |
A6X0K1 | LPXA_BRUA4 | Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase | Brucella | MKETFIHPTALVEQGVELGQGVSVGPFCHIQSGAVIGDNSELMSHVVVTGATTLGTGGKVYPHAVLGCDPQNNKHKGGPTKLNIGANCLIREGVTMHKGSDSARGYTSVGDNCSFLAYAHVAHDCDIGDYVTFSNNVMIGGHTTIGHHAILGGGAAIHQFVRVGHHAFVGGMAAVVSDLIPYGMAIGVHAHLGGLNIVGMKRSGMERKEIHNLRHAVRMLFDRTKPIRDRAKDVLTAIPDSPAVIDMIDFINVDTKRAYCTPPLDAVHGGAGHDSGED | Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | A6X0K1 |
Q2F5J3 | PYM_BOMMO | Protein wibg homolog | Bombyx | MSTPTAYEHDADGSKFIPATQRPDGTWRKPRRIKEGYVPQEEVPLYESKGKQFRARQNDGLPVGLTPEIVAQAQKKKGQRSTIQPIPGMIITVEKKKKKKKTVTGVEEAAEKLAKCEIQEPTLPSQSVPTESISQSDPTKRLKNLRKKLREIEFLEEKIKAGLLKSPDKDQKEKMSKKNEILNEIDILKNSIL | Regulator of the exon junction complex (EJC), a multiprotein complex that associates immediately upstream of the exon-exon junction on mRNAs and serves as a positional landmarks for the intron exon structure of genes and directs post-transcriptional processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA... | Q2F5J3 |
B2HWT2 | RUVA_ACIBC | Holliday junction ATP-dependent DNA helicase RuvA | Acinetobacter calcoaceticus/baumannii complex | MIGCLIGEVFALEAPTVLLNVNGVGYEIDTPLSTFCQLQKGQKVTLWTHLVVREDAQQLYGFSDAQEKTIFRTLLKVNGVGPKMALGILSTLNVELLVHTIEHDDVNTLVKVPGVGKKTAERLMIELRDRFKTLAQGTSSAAALPQIQFVSNSPVAEAEAALQSLGYKPLEAQKAVAAVKADYTESADIIRAALKSMMK | 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... | B2HWT2 |
Q0K391 | ASPD_CUPNH | L-aspartate dehydrogenase | Cupriavidus | MLHVSMVGCGAIGRGVMELLKSDPEVVFDVVIVPEHTMDEARDAVTALAPGARVATHLDDQRPDLLVECAGHHALEEHIVPALERGIPCMVVSVGALSEPGMAERLEAAARRGGTQVQLLSGAIGAIDALAAARVGGLDEVIYTGRKPARAWAGTPAEQLFDLDALTEATVIFEGTARDAARLYPKNANVAATVSLAGLGLDRTSVKLLADPHAVENVHHVEARGAFGGFELTMRGKPLAANPKTSALTVFSVVRALGNRAHAVSI | Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate. | Q0K391 |
Q8FNP5 | LIPB_COREF | Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase | Corynebacterium | MTAPRAPFFPADRSIRASDDPIEVQHLGTVDYRDSWDLQASLAEQRARDEIADQILVLEHPSVYTAGKRTQPEDLPTNGLPVIEVDRGGRITWHGPGQLVMYPIIKLAEPIDVVDYVRRLEEALIQTVRTFGVPEAGRVDGRSGVWVPAHDGYPDSKVAALGIRVTRGVTMHGLALNCNNTLEFYDHIIACGIEDAGLTTLSRELGRDVPTTELVDPLISDLDDAFAGRLTVADHSFASAPDPTRALPKRG | Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | Q8FNP5 |
Q2SU71 | AROK_BURTA | Shikimate kinase | pseudomallei group | MQARDPHVNVIFVGLMGAGKTTVGRAVARRLDRPFFDSDHEIEARTGARIPVIFELEGESGFRDREAQMIAELTQRENIVLATGGGAILRPENRKLLHERGLVVYLRANPHDLWLRTRKDKNRPLLQTDDPKAKLEALYEARDPLYRECAHFVIETGRPSVNGLVNMVLMQLEMAGIVAKPLQA | Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. | Q2SU71 |
Q0PBB6 | COAX_CAMJE | Pantothenic acid kinase | Campylobacter | MLLCDIGNSNANFLDDNKYFTLNIDQFLEFKNEQKIFYINVNEHLKEHLKNQKNFINLEPYFLFDTIYQGLGIDRIAACYTIEDGVVVDAGSAITIDIISNSIHLGGFILPGIANYKKIYSHISPRLKSEFNTQVSLDAFPQKTMDALSYGVFKGIYLLIKDAAQNKKLYFTGGDGQFLANYFDHAIYDKLLIFRGMKKIIKENPNLLY | Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. | Q0PBB6 |
P59732 | RLMH_ENTFA | rRNA (pseudouridine-N3-)-methyltransferase RlmH | Enterococcus | MKIKLVTVGKLKEKYLIQGINEYLKRLNSYAKMEIIEVPDEKAPEKLSDAEMLQVKEKEGQRILGKINDNEYVFVLAINGKQLSSEEFSKEIEQLGISGKSNLTFVIGGSLGLSDSVLQRSNQQISFGRLTYPHQLMRLVLVEQIYRGFRIMKGEPYHK | Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. | P59732 |
O88484 | PDP2_RAT | Pyruvate dehydrogenase phosphatase catalytic subunit 2 | Rattus | MSSTASYRIFNFARNRIAVLRGGRRLYSRAATSRNQVKWRLFSPASLAVNDSSPHGGFALRKAYRHTSTEEEDFHLQLSPEQVSDLLRAGESSHKVLDFNSGVPNSVLRFESNQLAANSPVEDRQGVASCVQTRGTVFGIFDGHGGHACAQAVSERLFYYMAVSLMSHKTLEQMEEAMENMKPLLPILQWLKHPGDSIYKDITSVHLDHLRVYWQELLDLHMETGLSTEEALMYSFQRLDSDISLEIQAPLEDEVTKNLSLQVAFSGATACMAHVDGVHLHIANAGDCRAILGVQGDNGAWSCLPLTCDHNAWNEAELSR... | Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex. | O88484 |
Q0BRP0 | SYT_GRABC | Threonyl-tRNA synthetase | Granulibacter | MPAITLPDGSVRHYDAPVTGTTIAADIGPGLARAALAMKVDGRMMDLSRAIAADAQVVFVTRKDEAALEMIRHDAAHVLAEAVQELFPGTQVTIGPSIENGFYYDFARNEPFTPEDLPAIEAKMREIIARNAPFEREVWDRQDAIRFFQDKGEKYKAQLIQDLPDTETITVYRQGEWLDLCRGPHMRSTGDIGPAFRLMKVAGAYWRGDHRNAMLSRIYGTAWRDQKELDAYLHQLEEAERRDHRRLGKEMDLFHIQEEAVGSIFWHKKGWRLYRALENYMRRRQIEAGYEEVRTPQLVDRSLWEDSGHWDKYREHMFIA... | Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). | Q0BRP0 |
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