ID SYK_ROSDO Reviewed; 527 AA. AC Q16AV0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 1. DT 03-NOV-2009, entry version 27. DE RecName: Full=Lysyl-tRNA synthetase; DE EC=6.1.1.6; DE AltName: Full=Lysine--tRNA ligase; DE Short=LysRS; GN Name=lysS; OrderedLocusNames=RD1_1246; OS Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter OS sp. (strain OCh 114)) (Roseobacter denitrificans). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=375451; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17098896; DOI=10.1128/JB.01390-06; RA Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., RA Ramos H., Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., RA Shah M.K., O'Huallachain M.E., Lince M.T., Blankenship R.E., RA Beatty J.T., Touchman J.W.; RT "The complete genome sequence of Roseobacter denitrificans reveals a RT mixotrophic rather than photosynthetic metabolism."; RL J. Bacteriol. 189:683-690(2007). CC -!- CATALYTIC ACTIVITY: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate CC + L-lysyl-tRNA(Lys). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000362; ABG30893.1; -; Genomic_DNA. DR RefSeq; YP_681579.1; -. DR STRING; Q16AV0; -. DR GeneID; 4197453; -. DR GenomeReviews; CP000362_GR; RD1_1246. DR KEGG; rde:RD1_1246; -. DR NMPDR; fig|375451.6.peg.1163; -. DR HOGENOM; Q16AV0; -. DR OMA; AFSDDMD; -. DR BioCyc; RDEN375451:RD1_1246-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:HAMAP. DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:HAMAP. DR HAMAP; MF_00177; -; 1. DR InterPro; IPR008925; aa-tRNA-synth_I_codon-bd. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002904; Lys-tRNA-synth_Ic_arc-type. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1. DR Gene3D; G3DSA:1.10.10.350; tRNA_synt_bd; 1. DR Pfam; PF01921; tRNA-synt_1f; 1. DR TIGRFAMs; TIGR00467; lysS_arch; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis. FT CHAIN 1 527 Lysyl-tRNA synthetase. FT /FTId=PRO_1000040354. FT MOTIF 44 52 "HIGH" region. FT MOTIF 290 294 "KMSKS" region. FT BINDING 293 293 ATP (By similarity). SQ SEQUENCE 527 AA; 59384 MW; 23D33C5964D04CA1 CRC64; MSDTRTAAMT SKAWPFEEAR RVLKRYEKNP PEKGYVLFET GYGPSGLPHI GTFGEVARTS MVMRAFQEIS DIPTRLICFS DDLDGMRKVP GNVPNPDALT EHLQRPLTSV PDPFGTHASF GAHNNAMLRR FLDTFGFEYE FISATEFYNT GQFDEILLRA AAKYDEIMAV MLKSLREERR QTYSIFLPIH PESGRVMYVP MKEVNAQAGT ITFDSEDGEE MTLPVTGGAV KLQWKPDFGA RWAALGVDFE MYGKDHSTNT PIYDKICRIL GQRPPEHFTY ELFLDENGQK ISKSSGNGVS IDEWLTYAST ESLSYFMYQK PKTAKRMYFD VIPKAVDEYH QQLRAYAGQD TAQRLNNPVW HIHGGDVPAS NMLVPFSMLL NLASVSSAED KSQLWGFIQR YAPESNPENN PDMDAAADFA VRYFNDFVKP KKVYRAASDL EREALEDLRD QLKAYDGPVD DEALQSIVYA CGRERFDPLR GWFTALYEVL LGASQGPRFG GFIALYGVQE TVALIDAALA GELLSDD //