ID SYC_ALCBS Reviewed; 460 AA. AC Q0VML5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 24. DE RecName: Full=Cysteinyl-tRNA synthetase; DE EC=6.1.1.16; DE AltName: Full=Cysteine--tRNA ligase; DE Short=CysRS; GN Name=cysS; OrderedLocusNames=ABO_2135; OS Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=393595; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16878126; DOI=10.1038/nbt1232; RA Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., RA Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., RA Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., RA Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A., RA Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., RA Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.; RT "Genome sequence of the ubiquitous hydrocarbon-degrading marine RT bacterium Alcanivorax borkumensis."; RL Nat. Biotechnol. 24:997-1004(2006). CC -!- CATALYTIC ACTIVITY: ATP + L-cysteine + tRNA(Cys) = AMP + CC diphosphate + L-cysteinyl-tRNA(Cys). CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- SUBUNIT: Monomer (By similarity). 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; AM286690; CAL17583.1; -; Genomic_DNA. DR RefSeq; YP_693855.1; -. DR GeneID; 4212582; -. DR GenomeReviews; AM286690_GR; ABO_2135. DR KEGG; abo:ABO_2135; -. DR NMPDR; fig|393595.12.peg.2133; -. DR HOGENOM; Q0VML5; -. DR OMA; Q0VML5; NFVTIHD. DR BioCyc; ABOR393595:ABO_2135-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:HAMAP. DR HAMAP; MF_00041; -; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR015804; Cys-tRNA-synt_Ia_C. DR InterPro; IPR015273; Cys-tRNA-synt_Ia_DALR. DR InterPro; IPR015803; Cys-tRNA-synt_Ia_N. DR InterPro; IPR002308; Cys-tRNA-synth_1a. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1. DR PANTHER; PTHR10890; Cys_tRNA-synt_1a; 1. DR Pfam; PF09190; DALR_2; 1. DR Pfam; PF01406; tRNA-synt_1e; 1. DR PRINTS; PR00983; TRNASYNTHCYS. DR TIGRFAMs; TIGR00435; cysS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; FALSE_NEG. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc. FT CHAIN 1 460 Cysteinyl-tRNA synthetase. FT /FTId=PRO_1000006560. FT MOTIF 31 41 "HIGH" region. FT MOTIF 266 270 "KMSKS" region. FT METAL 29 29 Zinc (By similarity). FT METAL 209 209 Zinc (By similarity). FT METAL 234 234 Zinc (By similarity). FT METAL 238 238 Zinc (By similarity). FT BINDING 269 269 ATP (By similarity). SQ SEQUENCE 460 AA; 51328 MW; 156608ACA20EEFC3 CRC64; MTLRLQNTLT GKKDDFIPLD PNRITLYVCG PTVYNFVHIG NARPVVVFDV LYRLLQRLYP NVVYARNITD IDDKIIKAAA DNGEAISTLT ERFTQAFADD MASLNAKTPS IIPKATDHIP EMIQMIAILV EKGHAYEADG QVLFAVESMP DYGKLSGRKL EDMLAGARVE VADYKRHPGD FILWKPSTDE QPGWDSPWGR GRPGWHIECS AMIHKHLGDV IDIHGGGQDL IFPHHENEIA QGCCAHGTDY VRYWLHNGYI NIDGEKMSKS LGNFRLVRDL LTQYHGETLR FALLSSHYRS PLNFSADVLD NAEKGLDTLY YALLGRGETV APEAGYQLPD NHPVLDALKD DLNTSEAVSA LHAIAGELNK AELDDKPKLK AELLAAADLL GLLTVEPTAW FQNKNVSEDG LSNDAIDALV EERTQAKKDK NFARADEIRQ QLTKAGIQLE DTREGTRWSR //