Unfortunately due to lack of commercial feasibility, the SkyBLAST service has been suspended from December 1st, 2025.
All subscriptions for paid accounts have been paused. For further information or enquiries, please email [email protected]
LOCUS WP_000195332 677 aa linear BCT 10-SEP-2020 ACCESSION WP_000195332 VERSION WP_000195332.1 KEYWORDS RefSeq. SOURCE Salmonella ORGANISM Salmonella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae. REFERENCE 1 (residues 1 to 677) AUTHORS Ochsner,U.A., Young,C.L., Stone,K.C., Dean,F.B., Janjic,N. and Critchley,I.A. TITLE Mode of action and biochemical characterization of REP8839, a novel inhibitor of methionyl-tRNA synthetase JOURNAL Antimicrob. Agents Chemother. 49 (10), 4253-4262 (2005) PUBMED 16189106 REFERENCE 2 (residues 1 to 677) AUTHORS Nakanishi,K., Ogiso,Y., Nakama,T., Fukai,S. and Nureki,O. TITLE Structural basis for anticodon recognition by methionyl-tRNA synthetase JOURNAL Nat. Struct. Mol. Biol. 12 (10), 931-932 (2005) PUBMED 16155581 REFERENCE 3 (residues 1 to 677) AUTHORS Datta,D., Vaidehi,N., Zhang,D. and Goddard,W.A. 3rd. TITLE Selectivity and specificity of substrate binding in methionyl-tRNA synthetase JOURNAL Protein Sci. 13 (10), 2693-2705 (2004) PUBMED 15388861 REFERENCE 4 (residues 1 to 677) AUTHORS Serre,L., Verdon,G., Choinowski,T., Hervouet,N., Risler,J.L. and Zelwer,C. TITLE How methionyl-tRNA synthetase creates its amino acid recognition pocket upon L-methionine binding JOURNAL J. Mol. Biol. 306 (4), 863-876 (2001) PUBMED 11243794 REFERENCE 5 (residues 1 to 677) AUTHORS Mechulam,Y., Schmitt,E., Maveyraud,L., Zelwer,C., Nureki,O., Yokoyama,S., Konno,M. and Blanquet,S. TITLE Crystal structure of Escherichia coli methionyl-tRNA synthetase highlights species-specific features JOURNAL J. Mol. Biol. 294 (5), 1287-1297 (1999) PUBMED 10600385 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: HMM Evidence Accession :: NF001100.0 Evidence Source :: NCBI Protein Cluster (PRK) Source Identifier :: PRK00133 ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..677 /organism="Salmonella" /db_xref="taxon:590" gene 1..677 /gene="metG" Protein 1..677 /product="methionine--tRNA ligase" /EC_number="6.1.1.10" /GO_function="GO:0000166 - nucleotide binding [Evidence IEA]" /GO_function="GO:0004825 - methionine-tRNA ligase activity [Evidence IEA]" /GO_function="GO:0005524 - ATP binding [Evidence IEA]" /GO_process="GO:0006431 - methionyl-tRNA aminoacylation [Evidence IEA]" /calculated_mol_wt=76143 Region 6..677 /region_name="metG" /note="methionyl-tRNA synthetase; Reviewed; PRK00133" /db_xref="CDD:234655" ORIGIN 1 mtqvakkilv tcalpyangs ihlghmlehi qadvwvryqr mrghevnfic addahgtpim 61 lkaqqlgitp eqmigemsqe hqtdfagfni sydnyhsths denrelseli ytrlkengfi 121 knrtisqlyd pekgmflpdr fvkgtcpkck sadqygdnce vcgatyspte liepksvvsg 181 atpvmrdseh fffdlpsfse mlqawtrsga lqeqvankmq ewfesglqqw disrdapyfg 241 feipnapgky fyvwldapig ymgsfknlcd krgdttsfde ywkkdsdael yhfigkdivy 301 fhslfwpaml egshfrkptn lfvhgyvtvn gakmsksrgt fikastwlkh fdadslryyy 361 taklssridd idlnledfvq rvnadivnkv vnlasrnagf inkrfdgvla aeladpqlyk 421 tftdaaavig eawesrefgk aireimalad ianryvdeqa pwvvakqegr dadlqaicsm 481 ginlfrvlmt ylkpvlptls erveaflnse lnwdaieqpl lghkvntfka lynridmkqv 541 ealvesskee vkaaaapvtg pladfpiqet itfddfakid lrvalienae fvdgsdkllr 601 ltldlggekr nvfsgirsay pdpqaligrq tvmvanlapr kmrfgvsegm vmaagpggkd 661 ifllspddga kpgqqvk