ID F6DZ09_SINMK Unreviewed; 585 AA.
AC F6DZ09;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 03-APR-2013, entry version 12.
DE RecName: Full=Arginine--tRNA ligase;
DE EC=6.1.1.19;
DE AltName: Full=Arginyl-tRNA synthetase;
GN Name=argS; OrderedLocusNames=Sinme_1325;
OS Sinorhizobium meliloti (strain AK83).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=693982;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK83;
RX PubMed=21569405; DOI=10.1186/1471-2164-12-235;
RG US DOE Joint Genome Institute;
RA Galardini M., Mengoni A., Brilli M., Pini F., Fioravanti A., Lucas S.,
RA Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Land M., Hauser L.,
RA Woyke T., Mikhailova N., Ivanova N., Daligault H., Bruce D.,
RA Detter C., Tapia R., Han C., Teshima H., Mocali S., Bazzicalupo M.,
RA Biondi E.G.;
RT "Exploring the symbiotic pangenome of the nitrogen-fixing bacterium
RT Sinorhizobium meliloti.";
RL BMC Genomics 12:235-235(2011).
CC -!- CATALYTIC ACTIVITY: ATP + L-arginine + tRNA(Arg) = AMP +
CC diphosphate + L-arginyl-tRNA(Arg).
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC family.
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DR EMBL; CP002781; AEG53072.1; -; Genomic_DNA.
DR RefSeq; YP_004548686.1; NC_015590.1.
DR ProteinModelPortal; F6DZ09; -.
DR EnsemblBacteria; AEG53072; AEG53072; Sinme_1325.
DR GeneID; 10725902; -.
DR KEGG; smk:Sinme_1325; -.
DR KO; K01887; -.
DR BioCyc; SMEL693982:GJDT-1344-MONOMER; -.
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 Gene3D; 3.30.1360.70; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00123; Arg_tRNA_synth; 1; -.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR001278; Arg-tRNA-ligase_Ia.
DR InterPro; IPR015945; Arg-tRNA-synth_Ia_core.
DR InterPro; IPR005148; Arg-tRNA-synth_N.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd.
DR PANTHER; PTHR11956; PTHR11956; 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 SMART; SM01016; Arg_tRNA_synt_N; 1.
DR SMART; SM00836; DALR_1; 1.
DR SUPFAM; SSF55190; Arg-tRNA-synth_Ic_N; 1.
DR SUPFAM; SSF47323; tRNAsyn_1a_bind; 1.
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 MOTIF 131 141 "HIGH" region (By similarity).
SQ SEQUENCE 585 AA; 64781 MW; 59F31028EBB5F238 CRC64;
MNLFTDFEAR INRILESIEI IREKRSELDF GRINVEPPRD ASHGDVATNA AMVLAKPLGM
NPRALADLIV DKLGQDPEVA GVSVAGPGFI NVRLSVSYWQ KLLAAITRAG VDYGRSTFGA
GRKINVEYVS ANPTGPMHVG HCRGAVVGDA LANLLAFAGY DVTKEYYIND AGSQIEVLAR
SAFLRYRQAL GEDIAEIPAG LYPGDYLVPV GEALADEYGT SLRIMPEDKW VPLVKERVID
AMMAMIREDL AALNVNHDVF FSERALHDNG AARIRTAIND LTFKGHVYKG TLPPPKGQLP
EEWEDREQTL FRSTEVGDDI DRPLIKSDGS YTYFAADVAY FKDKFDRGFH EMIYVLGADH
GGYVKRLEAL ARAISGGTAK LTVLLCQLVK LYRNGEPVKM SKRSGDFVTL REVVDEVGRD
PVRFMMLYRK SSEPLDFDFA KVTEQSKDNP VFYVQYAHAR CRSVFRQAAE AFPDLDLSSV
DFAAAAGAIV DPTEMQLVAK LAEYPRVVEA AALSHEPHRI AFYLYDLAAV FHGHWNKGKE
NPELRFVNDK NRELSIARLG LVHAVASVLK SGLSITGTSA PDEMR
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