SYR_STRP6
ID SYR_STRP6 Reviewed; 563 AA.
AC Q5X9F1;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=M6_Spy1827;
OS Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=286636;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-946 / MGAS10394;
RX PubMed=15272401; DOI=10.1086/422697;
RA Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT "Progress toward characterization of the group A Streptococcus metagenome:
RT complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL J. Infect. Dis. 190:727-738(2004).
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; CP000003; AAT87962.1; -; Genomic_DNA.
DR RefSeq; WP_011185081.1; NC_006086.1.
DR AlphaFoldDB; Q5X9F1; -.
DR SMR; Q5X9F1; -.
DR EnsemblBacteria; AAT87962; AAT87962; M6_Spy1827.
DR KEGG; spa:M6_Spy1827; -.
DR HOGENOM; CLU_006406_6_1_9; -.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000001167; 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; 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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..563
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000151622"
FT MOTIF 121..131
FT /note="'HIGH' region"
SQ SEQUENCE 563 AA; 63151 MW; 16D333B38A720D13 CRC64;
MDTKTLIASE IAKVVPELEQ DAIFNLLETP KNSDMGDLAF PAFSLAKVLR KAPQMIASEL
AEQIDESQFE KVVAVGPYIN FFLDKAKISS QVLEQVITAG SDYAQQDEGQ GRNVAIDMSS
PNIAKPFSIG HLRSTVIGDS LAHIFAKMGY KPVKINHLGD WGKQFGMLIV AYKKWGDETA
VQAHPIDELL KLYVRINAEA ETDPTVDEEA REWFRKLEDG DKEATELWQW FRDESLLEFN
RLYDQLHVTF DSYNGEAFYN DKMDEVLDLL EAKNLLVESK GAQVVNLEKY GIEHPALIKK
SDGATLYITR DLAAALYRKR TYDFAKSVYV VGNEQAAHFK QLKAVLKEMG YDWSDDMTHV
AFGLVTKGGA KLSTRKGNVI LLEPTVAEAI NRAASQIEAK NPNLADKEAV AHAVGVGAIK
FYDLKTDRMN GYDFDLEAMV SFEGETGPYV QYAHARIQSI LRKADFTPSA TTTYSLADAE
SWEIIKLIQD FPRIIKRTSD NFEPSIMAKF AINLAQSFNK YYAHTRILDD NSERDNRLAL
CYATATVLKE ALRLLGVDAP NEM