SYR_YERP3
ID SYR_YERP3 Reviewed; 576 AA.
AC A7FID8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
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};
GN OrderedLocusNames=YpsIP31758_2043;
OS Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP 31758;
RX PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT causative agent of Far East scarlet-like fever.";
RL PLoS Genet. 3:1508-1523(2007).
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; CP000720; ABS49422.1; -; Genomic_DNA.
DR RefSeq; WP_012105133.1; NC_009708.1.
DR AlphaFoldDB; A7FID8; -.
DR SMR; A7FID8; -.
DR EnsemblBacteria; ABS49422; ABS49422; YpsIP31758_2043.
DR KEGG; ypi:YpsIP31758_2043; -.
DR HOGENOM; CLU_006406_5_1_6; -.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000002412; 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_1000057813"
FT MOTIF 122..132
FT /note="'HIGH' region"
SQ SEQUENCE 576 AA; 64108 MW; 31984FAA841051D9 CRC64;
MNIQALLSDK VSQALIAAGA PADCEAQVRQ SAKAQFGDYQ ANGVMAVAKK LGMQPRQLAE
RVVELLDLTG IASKIEIAGP GFINIFLDRQ WVAEKVEYAL TAPKLGVAPV EPQTIVVDYS
APNVAKQMHV GHLRSTIIGD AAVRTLAFLG HNVIRANHVG DWGTQFGMLI AYLEKMQNEN
ASDMGLSDLE LFYQQAKKTY DEDEEFALRA RAYVVKLQSG DEYCRQMWRK LVDITMAQNQ
VAYDRLNVTL TKDDVMGESL YNAMLPEIVA DLKAKGLAVE SEGATVVYLD EYKNKDGEPM
GVIIQKKDGG YLYTTTDIAC AKYRYETLGA DRILYYIDSR QHQHLMQAWA IVRKAGYVPE
SVPLEHHMFG MMLGKDGKPF KTRSGGTVKL SDLLDEAVER AGKLIAEKNP DMPADELKQV
INAVGIGAVK YADLSKSRTT DYIFDWDNML ALDGNTAPYM QYAYTRVVSV FRRAGVDENS
LTLPLVITED REAALATRLL QFEEIITTVA REGTPHVMCS YLYDLAGLFS SFYEHCQILN
AESEEIRQSR LKLAMLTAKT LKQGLDTLGI QTVERM