ID   SYR_ANADE               Reviewed;         598 AA.
AC   Q2II14;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
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=Adeh_1524;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-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; CP000251; ABC81297.1; -; Genomic_DNA.
DR   RefSeq; YP_464734.1; -.
DR   GeneID; 3887934; -.
DR   GenomeReviews; CP000251_GR; Adeh_1524.
DR   KEGG; ade:Adeh_1524; -.
DR   HOGENOM; Q2II14; -.
DR   OMA; Q2II14; ADHHGYV.
DR   BioCyc; ADEH290397:ADEH_1524-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    598       Arginyl-tRNA synthetase.
FT                                /FTId=PRO_0000241975.
FT   MOTIF       131    141       "HIGH" region.
SQ   SEQUENCE   598 AA;  65447 MW;  3775CE051E92CDC3 CRC64;
     MVRDRVIELF RKALAQGADD GRWPAADAGF SVEAPRDPKH GDFAVNAAMV LAKQAGKPPR
     ELAQAIVEAV RAADTAGDLA GLEIAGPGFI NVRLSPDLWL RTLARAVAEG PAYGRTAVGQ
     GKKVIVEYVS ANPTGPMHVG HGRNAVVGDG VQGLLRWAGF DVSREYYVND YGAQVQTLAR
     SVHLRYQELH GRAVTMPPKS YPGEYVKDIA AGLKAEYGAR FLDAPEAEWL TLFRDHAVQH
     VLGMIREDLA AVNISFDRWS SEKALYESGT VDRFLRFLEE KDLVYVGKLP PPKSKKGQPP
     PQAQPDEEGV TAAEDLTLFR SSAYGDEVDR PVKKADGTPT YFCADIAYHW DKRQRADALV
     DVLGADHGGY VPRLEAAMEA LGASRKDLHV VLIQMVSLMR GGESVKMSKR AGTLVSLREV
     VDEVGRDATR FIFLTRRSDA PLDFDVELAK KQTLDNPVFY VQYGHARLAA IFQKAREAGH
     AVPEFDLDAA RTLGSPEEQD LIRRIAAFPD LLAAAALAYE PHRVAFYLQE TIAAFHSWYT
     QGKKSGEKVI GPDPVKTAAR LFLCRALKQV LANGLAVLGV SAPDRMESPE TRDIADDV
//