ID   SYR_MYCGA               Reviewed;         549 AA.
AC   Q7NC67;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   27-MAR-2024, entry version 106.
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=MYCGA0120; ORFNames=MGA_0636;
OS   Mycoplasmoides gallisepticum (strain R(low / passage 15 / clone 2))
OS   (Mycoplasma gallisepticum).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=710127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R(low / passage 15 / clone 2);
RX   PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA   Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA   Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT   "The complete genome sequence of the avian pathogen Mycoplasma
RT   gallisepticum strain R(low).";
RL   Microbiology 149:2307-2316(2003).
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; AE015450; AAP56362.2; -; Genomic_DNA.
DR   RefSeq; WP_011113241.1; NC_004829.2.
DR   AlphaFoldDB; Q7NC67; -.
DR   SMR; Q7NC67; -.
DR   KEGG; mga:MGA_0636; -.
DR   PATRIC; fig|233150.7.peg.14; -.
DR   HOGENOM; CLU_006406_0_1_14; -.
DR   OrthoDB; 9805987at2; -.
DR   Proteomes; UP000001418; 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; Arginyl tRNA synthetase N-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00456; argS; 1.
DR   PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR   PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 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..549
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151575"
FT   MOTIF           122..132
FT                   /note="'HIGH' region"
SQ   SEQUENCE   549 AA;  63613 MW;  EBFA572AEA3A2911 CRC64;
     MVFKKIKTQI DHALKQLNLP TDVEYLIQQT KNIQFGDFSS NVAMVLSKRQ NKNPQEIAKQ
     IIEQLNPNEF EKITFSKPGF INFFLSNQDK LVVLKRLQET NYSVEKLPKE EQESINIEFV
     SANPTGFLHL GHVRNAYTGD VLSNILRAVG HNVTKEYWIN DLGNQVSLFA LSTIIRYLQE
     LGINKYELPD DSYHGKEPIF VAEEMIKDFG NKYQDIKIED NKIVDSKIAN ELTQYCTNKM
     LHFIKQDLES IGVKMDVWTS EKVVYQSNTL TELLNNQLKD HIYEQDGAVW LRTTDGGDDK
     DRVIIKENKQ PTYYGTDIAN HYLKHKRGFD RLINVWGADH FGHILRTAYA AELTGIKKGK
     FVVVLIEMVK LLKDNKEIKF SKRLGNAISI PDMLEFLSKD ASRWFMLNQS WTSGIRIDVD
     LTNKKDSSNP VYYVQYAHAR IHKLLTKAEH IDLNKVNLSL LNSDVERTMV NYLASFEHYV
     HNVATTYEVN KLLNFVYTLT QSFHSWYNSH EILNQKDEIK QTRLLLAKAI KNLINYLLSL
     FGIEAVEQM
//