SYR_MYCCT
ID SYR_MYCCT Reviewed; 554 AA.
AC Q2SSA3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=MCAP_0376;
OS Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS / NCTC 10154).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=340047;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL Submitted (SEP-2005) 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; CP000123; ABC01557.1; -; Genomic_DNA.
DR RefSeq; WP_011387261.1; NC_007633.1.
DR AlphaFoldDB; Q2SSA3; -.
DR SMR; Q2SSA3; -.
DR EnsemblBacteria; ABC01557; ABC01557; MCAP_0376.
DR GeneID; 23778668; -.
DR KEGG; mcp:MCAP_0376; -.
DR HOGENOM; CLU_006406_0_1_14; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR PhylomeDB; Q2SSA3; -.
DR Proteomes; UP000001928; 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..554
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000242046"
FT MOTIF 123..133
FT /note="'HIGH' region"
SQ SEQUENCE 554 AA; 63494 MW; DCB6C2770006D705 CRC64;
MNRTIIEMFY DDLKNICQKF NITKEPIIEI NKNNTPGLLS SSICLISSKQ VNKKPLDLAN
DFKEQLLLTN NYSSIQIANP GFLNVLVKPE ILSNVISNVL TLKSKYGNLE KQNKIINIEY
VSANPTGYLH VGHARNAVIG SVLVNLFKKA GYKVQTEYYV NDAGNQINVL AVTVFVHYLQ
ALNIDAKKPE NCYAGEMYDD LAKIIINKYN DQFKDIKYTD NKILDDNVHS LFKQISIDYF
LKIIKQQLAD FNVKIRHWSS EQEVYDTHQI EKVLKLYKSK DASYYKDGAE FLKTTQFGDD
KDRVLVKSDK TYTYILPDLA THHLRIKRTK ADKLINVWGG DHHGYIKRMQ AGLALLGNDP
DILEIQMVQM VRLIKDGSEY KMSKRKGTAV WLVDILELVG VDALRYMLAS KSSNSHMDLD
LDLITLKNSS NPIYYAQYAT ARCHSILNQA KIKKITPLVK ETNLLNNPKE IELLLILDNF
KEVIKNSANN RSTQQICDYI QNICKIFHSY YAEIKIIDEN NLELTKLRLG FIKAILQVLK
NAFFIIGIQP VVEM