SYR_RICCK
ID SYR_RICCK Reviewed; 576 AA.
AC A8EXD2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=A1E_00310;
OS Rickettsia canadensis (strain McKiel).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=293613;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=McKiel;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia canadensis.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000409; ABV73015.1; -; Genomic_DNA.
DR RefSeq; WP_012148216.1; NC_009879.1.
DR AlphaFoldDB; A8EXD2; -.
DR SMR; A8EXD2; -.
DR STRING; 293613.A1E_00310; -.
DR PRIDE; A8EXD2; -.
DR EnsemblBacteria; ABV73015; ABV73015; A1E_00310.
DR KEGG; rcm:A1E_00310; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_5; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000007056; 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..576
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000018106"
FT MOTIF 126..136
FT /note="'HIGH' region"
SQ SEQUENCE 576 AA; 65362 MW; 54CC96BD8697E14D CRC64;
MNIFNQLKQD IIAASRQLYN NQEIANIVTI ETSKDNFNGD LSSNIAMIIA AKENMPPRTV
ALKFKEILIT LPYIASIEIA GPGFINFTIK AESWQIAIKN ILQHEGKFFE IDIDKNKYIN
IEYVSANPTG PMHIGHARGA VYGDVLARIL QKVGYNVTKE YYVNDAGSQI NDLVSTVLLR
YREALGEKIT IPVGLYPGEY LIPVGQILVK EYGNKLLVMD EEERFKIVKN FAVEKMLDLN
RKDLEELGIK HDLFFSEQSL HDKGKIEEIV KLLTNMGLIY EGTLPAPKGK IHAKWDNRVQ
KLFKSTKYGD SQDRPIEKAD GSWSYFASDL AYAKDKIDRG ANHLIYVLGA DHSGYVKRIE
AIVKALGKEQ IKVDVKICQL VNFIENGVPV KMSKRLGNFA SVQDVNHEVG KDIIRFMMLT
RQNDKPLDFD LVKVKEQSRE NPIFYVQYAH VRTVSILSKA MELMPESYSS FEAGIYDLSL
LSSEEEIDII KLLAAWTKTL EVSAKYFEPH RIALYLINLA SKFHSIWNFG KENSDYRFVI
ENNKELTTAR LALAKAIQKV IASGFEVIGV EPMNKM