ID   SYR_BLOPB               Reviewed;         581 AA.
AC   Q492L0;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=BPEN_468;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ41087.1; -; Genomic_DNA.
DR   RefSeq; YP_277963.1; -.
DR   GeneID; 3562964; -.
DR   GenomeReviews; CP000016_GR; BPEN_468.
DR   KEGG; bpn:BPEN_468; -.
DR   HOGENOM; Q492L0; -.
DR   OMA; Q492L0; HMGFGTM.
DR   BioCyc; CBLO291272:BPEN_468-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:3.40.50.620; 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    581       Arginyl-tRNA synthetase.
FT                                /FTId=PRO_0000241991.
FT   MOTIF       123    133       "HIGH" region.
SQ   SEQUENCE   581 AA;  66780 MW;  37AF0870CC47F172 CRC64;
     MNIQKFLLKK IHRALLAITN ESFFHLIQVQ QSTKRKFGNY QINGLIAISK KLNIPIEEFA
     KKFIQFINLN DVAHTIKIEK PGFINIFLNT KWISNQINNI FSASHLGITP ATPKTIVIDY
     SGPNVAKEMH VGHLRSTVIG DSIARVLSFL GHNVIRANHI GDWGTQFGML IAYIEKNAQT
     RFLLNKTIQL STLEHFYREA KKKYDIDPDF AELSRNYVLK LQKGDKHYRQ IWKYLVDISI
     LNNQDIYVRL NINLKKSDII GESFYNDMLP DIVSDLKNKG LAVTSNGATV VFLENYHNKL
     GTPFGVIIQK KDGAYLYSTT DIACIKYRCK VLHADRIIYY IDSRQKQHLI QAWEIADKAG
     YIEKSVLLEH HMCGMLLGKD GKPFKTRAGN ALKLKTLLDE ALERARCLIL SKNPNLKYTE
     INKLAHIISI GAIKYSELSK NRITDYIFDW NNMLNFEGNT APYVQYACTR IFAIFKRSKQ
     PNFQLKKNDI QLETEEEILL AICLLQFEEM IVAVSNQGAP HILCSYLYKL SVLFSSFYEN
     CPIIKAHNTH IKYSRLKLAL ITMRTLKTGL NLLGIKTVRY M
//