SYR_STRGG
ID SYR_STRGG Reviewed; 594 AA.
AC B1VTB7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Arginine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00123};
DE EC=6.1.1.19 {ECO:0000255|HAMAP-Rule:MF_00123};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00123};
DE Short=ArgRS {ECO:0000255|HAMAP-Rule:MF_00123};
GN Name=argS {ECO:0000255|HAMAP-Rule:MF_00123}; OrderedLocusNames=SGR_4178;
OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=455632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 4626 / NBRC 13350;
RX PubMed=18375553; DOI=10.1128/jb.00204-08;
RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA Yamashita A., Hattori M., Horinouchi S.;
RT "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT griseus IFO 13350.";
RL J. Bacteriol. 190:4050-4060(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-
CC tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215;
CC EC=6.1.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_00123};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00123}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00123}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00123}.
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DR EMBL; AP009493; BAG21007.1; -; Genomic_DNA.
DR RefSeq; WP_012380409.1; NC_010572.1.
DR AlphaFoldDB; B1VTB7; -.
DR SMR; B1VTB7; -.
DR STRING; 455632.SGR_4178; -.
DR EnsemblBacteria; BAG21007; BAG21007; SGR_4178.
DR GeneID; 6209259; -.
DR KEGG; sgr:SGR_4178; -.
DR PATRIC; fig|455632.4.peg.4255; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_5_1_11; -.
DR OMA; HHIGDWG; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000001685; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00671; ArgRS_core; 1.
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.
DR InterPro; IPR005148; Arg-tRNA-synth_N.
DR InterPro; IPR036695; Arg-tRNA-synth_N_sf.
DR InterPro; IPR035684; ArgRS_core.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_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; SSF47323; SSF47323; 1.
DR SUPFAM; SSF55190; SSF55190; 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; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..594
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000095408"
FT MOTIF 127..137
FT /note="'HIGH' region"
SQ SEQUENCE 594 AA; 64757 MW; D572DB562773B6BA CRC64;
MASVPSLAST LQQQLADALT AALPDAGAAD PLLRRSDRAD FQANGILALA KKLKGNPREL
AAQVTAALPA GGLIKDIEVS GPGFLNVTLT DRAIVETLAA RAADGEGRLG VPLKDDAGTT
VIDYAQPNVA KEMHVGHLRS AVIGDAVVRI LEFTGENVVR RHHIGDWGTQ FGMLIQYLIE
HPGALQHEGG PGDGASDGEA AMSTLNRVYK ESRALFDSDE EFKARSRDRV VALQAGDPGT
LELWHRFVDE SKIYFHSVFD KLDMEIRDPD IVGESGYNDM LEETCRILEE TGVAVRSEGA
LCVFFDDVKG PDGNRVPLIV KKTNGGYGYA ATDLSAVRNR VQDLKADTLL YVVDARQSLH
FRMVFETARR AGWLGDDVKA VQLAFGTVLG KDGKPFKTRE GETVRLEDLL DEAVQRATAV
VRDKAEKVGL SEEEIVENGR YVGIGAVKYA DLSTSAVRDY KFDLDQMVAL HGDTSVYLQY
AYARIRSILR KAGDAVPAAH PELELAPAER ALGLHLDQFG EVLAEVGTGY EPHKLAAYLY
QLASHLTTFY DQCQVLSPDN APEVVENRLF LVELTARTLH RGMALLGIRT PERL