SYR_WIGBR
ID SYR_WIGBR Reviewed; 576 AA.
AC Q8D372;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=WIGBR1290;
OS Wigglesworthia glossinidia brevipalpis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Wigglesworthia.
OX NCBI_TaxID=36870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12219091; DOI=10.1038/ng986;
RA Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M.,
RA Aksoy S.;
RT "Genome sequence of the endocellular obligate symbiont of tsetse flies,
RT Wigglesworthia glossinidia.";
RL Nat. Genet. 32:402-407(2002).
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; BA000021; BAC24275.1; -; Genomic_DNA.
DR RefSeq; WP_011069933.1; NC_004344.2.
DR AlphaFoldDB; Q8D372; -.
DR SMR; Q8D372; -.
DR STRING; 36870.25166084; -.
DR EnsemblBacteria; BAC24275; BAC24275; BAC24275.
DR KEGG; wbr:argS; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_5_1_6; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000000562; 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 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; Reference proteome.
FT CHAIN 1..576
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000151636"
FT MOTIF 123..133
FT /note="'HIGH' region"
SQ SEQUENCE 576 AA; 67095 MW; 71AD4F8A8E87C8CA CRC64;
MNIKNILLKN VKNALKPSNL DLRNLKIKKT KFKKFGNYQI DGIFSILNKN KINLNELLNK
ILPIINMKLI NVSEKIEFVK PGYINIFLKK SWIEDNLLKI YHSNKLGISK LKKKTIIIDY
SSPNIGKEMH VGHMRSTIIG DSISLILELL GHKVIRANHI GDWGNQFGML LAYFNEKQNL
KFSEITCTDL ENYYINAKKK YDKDLEFKKK SQFFTLKLQK KEKDCINIWK KITNLSIENN
QKIYDQLNIK LNKTHIMGES LYNDFVPYII SDLPKKNLAI NKSGNIMVIL NNFKNKQGKS
MGVILKKRNG TYLYSVIDIA CIKYRYDFFK AQKIIYYTDS RQSQHLLQVF DIVRKAKYIP
NFVKLEHHKF GMVLKKDKTP FKTRSGDTIK LSDLLKKSKE KAKKLIIKKN PNTSIDEIES
LSQAIGIGSI KYFELSKNRE TDYIFNWDNI LSFNGNTAPY IQYAYTRVIS LIKKNKLKNK
NNVKFLLKKE EEIDLSICLL QFEEIINDVS KLGTPHILCN YLYDLSKTFS VFYENCSIIK
TKEESVKNSR LFLSILTSRT LKVGLELLGI PMVEKM