SYR_SALCH
ID SYR_SALCH Reviewed; 577 AA.
AC Q57N89;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=SCH_1916;
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
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; AE017220; AAX65822.1; -; Genomic_DNA.
DR RefSeq; WP_001025358.1; NC_006905.1.
DR AlphaFoldDB; Q57N89; -.
DR SMR; Q57N89; -.
DR EnsemblBacteria; AAX65822; AAX65822; SCH_1916.
DR KEGG; sec:SCH_1916; -.
DR HOGENOM; CLU_006406_5_1_6; -.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000000538; 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..577
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000242088"
FT MOTIF 122..132
FT /note="'HIGH' region"
SQ SEQUENCE 577 AA; 64246 MW; A5B1F54519BF47D0 CRC64;
MNIQALLSEK VSQAMIAAGA PADCEPQVRQ SAKVQFGDYQ ANGMMAVAKK LGMAPRQLAE
QVLTHLDLSG IASKVEIAGP GFINIFLEPA FLAEQVQQAL ASDRLGVSQP TRQTIVVDYS
APNVAKEMHV GHLRSTIIGD AAVRTLEFLG HHVIRANHVG DWGTQFGMLI AWLEKQQQEN
AGDMALADLE GFYRDAKKHY DEDEAFAERA RNYVVKLQSG DAYFREMWRK LVDITMTQNQ
ITYDRLNVTL TRDDVMGESL YNPMLPGIVA DLKAKGLAVE SEGATVVFLD EFKNKEGDPM
GVIIQKKDGG YLYTTTDIAC AKYRYETLHA DRVLYYIDSR QHQHLMQAWT IVRKAGYVPD
SVPLEHHMFG MMLGKDGKPF KTRAGGTVKL ADLLDEALER ARRLVAEKNP DMPADELEKL
ANAVGIGAVK YADLSKNRTT DYIFDWDNML AFEGNTAPYM QYAYTRVLSV FRKADIDEQA
LASAPVIISE DREAQLAARL LQFEETLTVV AREGTPHVMC AYLYDVAGLF SGFYEHCPIL
SAENDAVRNS RLKLAQLTAK TLKLGLDTLG IETVERM