ID   SYR_BORAP               Reviewed;         585 AA.
AC   Q0SMR4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=BAPKO_0625;
OS   Borrelia afzelii (strain PKo).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M.,
RA   Suehnel J., Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(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; CP000395; ABH01864.1; -; Genomic_DNA.
DR   RefSeq; YP_710040.1; -.
DR   GeneID; 4227928; -.
DR   GenomeReviews; CP000395_GR; BAPKO_0625.
DR   KEGG; baf:BAPKO_0625; -.
DR   NMPDR; fig|390236.5.peg.650; -.
DR   HOGENOM; Q0SMR4; -.
DR   OMA; Q0SMR4; SHITELL.
DR   BioCyc; BAFZ390236:BAPKO_0625-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    585       Arginyl-tRNA synthetase.
FT                                /FTId=PRO_1000017992.
FT   MOTIF       127    137       "HIGH" region.
SQ   SEQUENCE   585 AA;  67115 MW;  75FBFA12A2D3B3B8 CRC64;
     MTKNVKKNIK DEINIIVTNL ALSKNIKLDE ININIQKPPK SDLGDISILI FELSKTLKLP
     IETISEEIIK ALKAKYEIKA MGPYLNIKIP RKEYIHNTIQ MVNAQKDTYG TSKYLDNKKI
     ILEFSSPNTN KPLHVGHLRN DVIGESLSRI LKAVGAKIIK LNLINDRGVH ICKSMLAYKK
     FGNEITPEKA FKKGDHFIGD FYVQYNKYAQ ENENAEEEIQ DLLLKWEQKD ASTIELWKKL
     NNWAIEGIKE TYKITNTSFD KIYLESEIFE IGKNVVLEGL EKGFCYKRED GAICIDLPLD
     SDEKTDTKVK QKVLIRSNGT SIYLTQDLGN IAVRIKEFNF EEMIYVVGSE QIQHFKNLFF
     VSEKLGISKN KKLFHLSHGM VNLVDGKMKS REGNVIDGDN LILDLMESIL PEITQKIENK
     ENAKKNALDI ALGAIHYYLL KSAIHKDIVF NKKESLSFTG NSGPYIQYVG ARINSILEKY
     NTLSIPIIKK INFELLEHEK EWDIIKIISE LEENIIKAAK DLNPSILTSY SYSLAKHFSA
     YYQEVRVIDI NNIDLTAARI EFLKAILQTI KNCMYLLNIP YMLKM
//