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_000416329 951 aa linear BCT 10-SEP-2020 ACCESSION WP_000416329 VERSION WP_000416329.1 KEYWORDS RefSeq. SOURCE Salmonella ORGANISM Salmonella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae. REFERENCE 1 (residues 1 to 951) AUTHORS Fukunaga,R. and Yokoyama,S. TITLE Structural basis for non-cognate amino acid discrimination by the valyl-tRNA synthetase editing domain JOURNAL J. Biol. Chem. 280 (33), 29937-29945 (2005) PUBMED 15970591 REFERENCE 2 (residues 1 to 951) AUTHORS Tardif,K.D. and Horowitz,J. TITLE Functional group recognition at the aminoacylation and editing sites of E. coli valyl-tRNA synthetase JOURNAL RNA 10 (3), 493-503 (2004) PUBMED 14970394 REFERENCE 3 (residues 1 to 951) AUTHORS Fukai,S., Nureki,O., Sekine,S., Shimada,A., Vassylyev,D.G. and Yokoyama,S. TITLE Mechanism of molecular interactions for tRNA(Val) recognition by valyl-tRNA synthetase JOURNAL RNA 9 (1), 100-111 (2003) PUBMED 12554880 REFERENCE 4 (residues 1 to 951) AUTHORS Hountondji,C., Lazennec,C., Beauvallet,C., Dessen,P., Pernollet,J.C., Plateau,P. and Blanquet,S. TITLE Crucial role of conserved lysine 277 in the fidelity of tRNA aminoacylation by Escherichia coli valyl-tRNA synthetase JOURNAL Biochemistry 41 (50), 14856-14865 (2002) PUBMED 12475234 REFERENCE 5 (residues 1 to 951) AUTHORS Fukai,S., Nureki,O., Sekine,S., Shimada,A., Tao,J., Vassylyev,D.G. and Yokoyama,S. TITLE Structural basis for double-sieve discrimination of L-valine from L-isoleucine and L-threonine by the complex of tRNA(Val) and valyl-tRNA synthetase JOURNAL Cell 103 (5), 793-803 (2000) PUBMED 11114335 REFERENCE 6 (residues 1 to 951) AUTHORS Heck,J.D. and Hatfield,G.W. TITLE Valyl-tRNA synthetase gene of Escherichia coli K12. Primary structure and homology within a family of aminoacyl-TRNA synthetases JOURNAL J. Biol. Chem. 263 (2), 868-877 (1988) PUBMED 3275660 REFERENCE 7 (residues 1 to 951) AUTHORS Hartlein,M., Frank,R. and Madern,D. TITLE Nucleotide sequence of Escherichia coli valyl-tRNA synthetase gene valS JOURNAL Nucleic Acids Res. 15 (21), 9081-9082 (1987) PUBMED 3317277 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 :: NF004349.1 Evidence Source :: NCBI Protein Cluster (PRK) Source Identifier :: PRK05729 ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..951 /organism="Salmonella" /db_xref="taxon:590" Protein 1..951 /product="valine--tRNA ligase" /EC_number="6.1.1.9" /GO_function="GO:0000166 - nucleotide binding [Evidence IEA]" /GO_function="GO:0004812 - aminoacyl-tRNA ligase activity [Evidence IEA]" /GO_function="GO:0004832 - valine-tRNA ligase activity [Evidence IEA]" /GO_function="GO:0005524 - ATP binding [Evidence IEA]" /GO_process="GO:0006438 - valyl-tRNA aminoacylation [Evidence IEA]" /calculated_mol_wt=108045 Region 1..949 /region_name="ValS" /note="Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; COG0525" /db_xref="CDD:440291" ORIGIN 1 mektynpqdi eqplyehwek qgyfkpngde skesfcimip ppnvtgslhm ghafqqtimd 61 tmiryqrmqg kntlwqvgtd hagiatqmvv erkiaaeegk trhdygrdaf idkiwqwkae 121 sggtitrqmr rlgnsvdwer erftmdegls navkevfvrl ykedliyrgk rlvnwdpklr 181 taisdleven reskgsmwhi rypladgakt adgkdylvva ttrpetilgd tgvavnpedp 241 ryqsligkfv ilplvnrrip ivgdehadme kgtgcvkitp ahdfndyevg krhalpmini 301 ltfdgdires aevfdtkgee sdvysseipa efqklerfaa rkavvaavda lglleeikph 361 dltvpygdrg gvviepmltd qwyvradvla kpaveaveng diqfvpkqye nmyfswmrdi 421 qdwcisrqlw wghripawyd ndgnvyvgrt edevrqennl gadvalrqde dvldtwfssa 481 lwtfstlgwp entdalrqfh ptsvmvsgfd iiffwiarmi mmtmhfikde ngkpqvpfht 541 vymtglirdd egqkmskskg nvidpldmvd gislpellek rtgnmmqpqm aekirkrtek 601 qfpngiephg tdalrftlaa lastgrdinw dmkrlegyrn fcnklwnasr fvlmnteeqd 661 cgfnggemtl sladrwilae fnqtvkayrd aldsfrfdia agilyeftwn qfcdwylelt 721 kpvmtggses elrgtrhtlv tvlegllrla hpiipfitet iwqrvkvicg itadtimlqp 781 fpeynaaqvd eaaladtewl kqaivavrni raemniapgk plelllrgcs eeavrrvndn 841 rsflqtlarl esitvlpadd kgpvsvtkii dgaellipma glinkddela rlakevakie 901 geiariegkl snegfvarap eaviakerek ldgyaeakak lieqqavisa l