SYR_STRT1
ID SYR_STRT1 Reviewed; 563 AA.
AC Q5M1Z3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
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=str0047;
OS Streptococcus thermophilus (strain CNRZ 1066).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=299768;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNRZ 1066;
RX PubMed=15543133; DOI=10.1038/nbt1034;
RA Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT "Complete sequence and comparative genome analysis of the dairy bacterium
RT Streptococcus thermophilus.";
RL Nat. Biotechnol. 22:1554-1558(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; CP000024; AAV61664.1; -; Genomic_DNA.
DR RefSeq; WP_011226739.1; NC_006449.1.
DR AlphaFoldDB; Q5M1Z3; -.
DR SMR; Q5M1Z3; -.
DR KEGG; stc:str0047; -.
DR HOGENOM; CLU_006406_6_1_9; -.
DR OMA; NKPLHLG; -.
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_0000242102"
FT MOTIF 121..131
FT /note="'HIGH' region"
SQ SEQUENCE 563 AA; 62893 MW; 83CAFCAD12D2E2B3 CRC64;
MNTKELIAAE IAKVVPELEQ ENIQNLLEIP KNADMGDLAF PAFSLAKVLR KAPQMIAADI
AEKIDASNFE KVEAVGPYIN IFLDKSKISA DVLGQVIAQG SHYADQNIGN GRNIAFDMSS
PNIAKPFSIG HLRSTVIADA LANIVAKQGY KPVRINHLGD WGKQFGMLIV AYKKWGSEEA
VKANPINELL QLYVRINAEA EEDPSVDEEA REWFRKLEAG DEEATALWQW FRDESLVEFN
RLYDELGVSF DSYNGEAFYN DKMDEVVDIL TEKGLLQESQ GAQVVNLEKY GIEHPALIKK
SDGATLYITR DLAAALYRKR TYDFAKAIYV VGNEQSAHFK QLKAVLKEMG YNWSDDMTHV
AFGLVTKNGK KLSTRKGNVI LLEPTIAEAV NRAQAQIEAK NPNLPNKEAI AHAVGVGAIK
FYDLKTDRMN GYDFDLDAMV SFEGETGPYV QYAHARIQSI LRKADFTPSA DATYSLNDVE
SWEIIKLLQD FPRIINRASD NFEPSIVAKF AISLAQAFNK YYAHTRILDE SPERDSRLAL
CYATATVLKE ALRLLGVEAP DEM