ID   SYR_ALCBS               Reviewed;         584 AA.
AC   Q0VMA8;
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=Arginyl-tRNA synthetase;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginine--tRNA ligase;
DE            Short=ArgRS;
GN   Name=argS; OrderedLocusNames=ABO_2242;
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-arginine + tRNA(Arg) = AMP +
CC       diphosphate + L-arginyl-tRNA(Arg).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; AM286690; CAL17690.1; -; Genomic_DNA.
DR   RefSeq; YP_693962.1; -.
DR   GeneID; 4213484; -.
DR   GenomeReviews; AM286690_GR; ABO_2242.
DR   KEGG; abo:ABO_2242; -.
DR   NMPDR; fig|393595.12.peg.2242; -.
DR   HOGENOM; Q0VMA8; -.
DR   OMA; Q0VMA8; HMGFGTM.
DR   BioCyc; ABOR393595:ABO_2242-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00123; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR001278; Arg-tRNA-synth_Ic.
DR   InterPro; IPR015945; Arg-tRNA-synth_Ic_core.
DR   InterPro; IPR005148; Arg-tRNA-synth_Ic_N.
DR   InterPro; IPR008909; DALR_anticod_bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.30.1360.70; Arg-tRNA-synth_Ic_N; 1.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR11956; Arg_tRNA-synt_1c; 1.
DR   Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 1.
DR   PRINTS; PR01038; TRNASYNTHARG.
DR   TIGRFAMs; TIGR00456; argS; 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    584       Arginyl-tRNA synthetase.
FT                                /FTId=PRO_1000017983.
FT   MOTIF       127    137       "HIGH" region.
SQ   SEQUENCE   584 AA;  64882 MW;  149D458D7B2E61F5 CRC64;
     MKERLISLIE SALDTLITDG TLPADAKRPV QIDRTRDKSH GDFATNIALM LAKPAGMKPR
     DLAEKLIAAL PNDSAVAKVD IAGPGFINFF QADDWLTGLL DSALADDFLG ISRPEQPQTV
     VVDYSSPNLA KEMHVGHLRS TIIGDAVVRT LEFLGHTVIR QNHVGDWGTQ FGMLLAYLEE
     QKTEEGEREL SRELANLETF YRAAKQRFDE SDSFADRARA LVVKLQSGDD YCLTLWAEFN
     QVSLSHCQAI YDRLGVSLTP ADVHGESAYN DDLAQVVADL DSKGLLSESQ GAQCVFMDAF
     KNKEGEPLPV IVRKADGGYL YATSDLAALR YRASTLRADR MLYFVDQRQA LHFQQMFTLA
     KLAGFVPEQT ELAHMGFGTM NGPDGRPFKT RDGGTVKLVD LLDEAEQRAF ALVQEKNPQL
     DDEELRNIAR SVGIGAVKYA DLSKNRSSDY IFNFEQMLSF EGNTAPYLLY AYTRVASVFR
     KAELDMANVS GDFLLNEDAE HTLAARLVQF GEVLQNVADK GQPHLLSAYL YDVAGLFSSF
     YEHCPILSSE DERIRQSRLK LAALTARTLK HGMELLGLSP LERM
//