ID   SYR_BURCM               Reviewed;         593 AA.
AC   Q0BBE9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=Bamb_2968;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia
OS   cepacia (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T.,
RA   Konstantinidis K., Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000440; ABI88524.1; -; Genomic_DNA.
DR   RefSeq; YP_774858.1; -.
DR   GeneID; 4310555; -.
DR   GenomeReviews; CP000440_GR; Bamb_2968.
DR   KEGG; bam:Bamb_2968; -.
DR   NMPDR; fig|339670.3.peg.196; -.
DR   OMA; Q0BBE9; ADHHGYV.
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:3.40.50.620; 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    593       Arginyl-tRNA synthetase.
FT                                /FTId=PRO_1000017999.
FT   MOTIF       138    148       "HIGH" region.
SQ   SEQUENCE   593 AA;  64289 MW;  5441A622104ACDCC CRC64;
     MLPAHKQTLE ALLADSVTQV AHALKGADAA FVAPAITLER PKVAAHGDVA CNVAMQLAKP
     LGTNPRQLAE KIVAALTAQP AAQGLVDAAD IAGPGFINLR LTAAAKQAVI AAVFEQGRAF
     GTSDREKGKQ VLLEFVSANP TGPLHVGHGR QAALGDVLAN VIASQGYAVH REFYYNDAGV
     QIGNLAISTQ ARARGLKPGD AGWPEAAYNG EYIADIARDY LNRETVAAKD GEPVTGAGDI
     DDLDAIRKFA VAYLRHEQDM DLQAFGVKFD QYYLESSLYS EGRVEKTVDA LVKAGMTYEQ
     DGALWLRTTD EGDDKDRVMR KSDGTYTYFV PDVAYHVTKW ERGFTQVINI QGSDHHGTIA
     RVRAGLQGLH VGIPKGYPDY VLHKMVTVMR DGQEVKLSKR AGSYVTVRDL IEWSGGAAPG
     QEAAPDLIDE ATITRGRDAV RFFLISRKAD TEFVFDIDLA LKQNDENPVY YVQYAHARIC
     SVLNELKSRY NVDVAQLPGA DLSQLTSAQA VSLMQKLAEY PDMLTHAAKE LAPHAVAFYL
     RDLAGEFHSF YNAERVLVDD EAPRNARAAL LAATRQVLEN GLAVLGVSAP AKM
//