SYR_BUCAT
ID SYR_BUCAT Reviewed; 574 AA.
AC B8D7E4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=BUAPTUC7_240;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain Tuc7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=561501;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuc7;
RX PubMed=19150844; DOI=10.1126/science.1167140;
RA Moran N.A., McLaughlin H.J., Sorek R.;
RT "The dynamics and time scale of ongoing genomic erosion in symbiotic
RT bacteria.";
RL Science 323:379-382(2009).
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; CP001158; ACL30059.1; -; Genomic_DNA.
DR RefSeq; WP_012619482.1; NC_011834.1.
DR AlphaFoldDB; B8D7E4; -.
DR SMR; B8D7E4; -.
DR KEGG; bau:BUAPTUC7_240; -.
DR HOGENOM; CLU_006406_5_1_6; -.
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; 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..574
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000198880"
FT MOTIF 121..131
FT /note="'HIGH' region"
SQ SEQUENCE 574 AA; 66685 MW; 95D43367FCA81DD7 CRC64;
MNLKNTIKKD IQDALIKIAI INCDPVITLN KKTKIGHYQL NNLIKIANIS NLKPFELANR
IILNIKKKYM YKEITFSQPG FINFLINPYW ISEQLEKIFL SPRLGINHVN AQNIVIDYSS
PNIAKEMHIG HLRSTIIGDV MARILDFLGH NVIRANHIGD WGTQFGMLIA YLEVKKLVNS
PLSLMKLEEY YCKAKKKYDI DQLFAEKSRE YVVKLQNGDQ YCYSIWKKLV SITMLENCKI
YKRLHVTLKK KHTMGESIYN KMLPNIIEDL KNKKIAIEKN GSTIVFLKEF KNRLGEPMGV
VIQKKDKGFL YSTTDIACLK YRYQVLHADR IIYYTDSRQH QHLLQAWTIA KKALYISQNL
LLEHHIFGMM LSKDKRPFKT RDGDTIKLSA LLDEATERAM RLIKNKQPNL SKKKLNQLSN
IIGVGAVKYA DLSKNRNTNY IFDWNEMLSF EGNTAPYIQY AYTRIVSILK KSNMPIKKLK
EKIFLTKESE INLAIKILEF EEIILLISQK GTPHILCKYL YHLATSFSHF YENCSILFPK
KIKTCKSRLK LSILTAKTLK KGLNMLGIRV VKKM