ID   SYR_MYCLE               Reviewed;         550 AA.
AC   P45840;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 3.
DT   25-MAY-2022, entry version 134.
DE   RecName: Full=Arginine--tRNA ligase;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginyl-tRNA synthetase;
DE            Short=ArgRS;
GN   Name=argS; OrderedLocusNames=ML1127;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA63099.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U15186; AAA63099.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL583920; CAC31508.1; -; Genomic_DNA.
DR   PIR; A87050; A87050.
DR   RefSeq; NP_301821.1; NC_002677.1.
DR   RefSeq; WP_010908145.1; NC_002677.1.
DR   AlphaFoldDB; P45840; -.
DR   SMR; P45840; -.
DR   STRING; 272631.ML1127; -.
DR   EnsemblBacteria; CAC31508; CAC31508; CAC31508.
DR   KEGG; mle:ML1127; -.
DR   PATRIC; fig|272631.5.peg.2049; -.
DR   Leproma; ML1127; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_11; -.
DR   OMA; NKPLHLG; -.
DR   Proteomes; UP000000806; 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; Reference proteome.
FT   CHAIN           1..550
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151577"
FT   MOTIF           130..140
FT                   /note="'HIGH' region"
FT   CONFLICT        174
FT                   /note="I -> V (in Ref. 1; AAA63099)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   550 AA;  59603 MW;  DBD8A95A9B9831BB CRC64;
     MTPADLAELL KTTAIVVLAE RGLDAAALPQ TVTVERPRNP EHGDYSSNLA MQLGKKVGAN
     PLELAGWLAE VLAQAGGIAD VEVAGPGFIN MRLDASAQAM IVNTVINADK NFGHSDDLAG
     YQINLEFVSA NPTGPIHIGG TRWAAVGDAL GRLLSTQGAA VVREYYFNDH GAQIDRFTNS
     LIAAAKGELT PADGYAGTYV TDIAAQVMQQ APYALSLPES EMHETVREIG VDLMFTHIKK
     SLHEFGTDFD VYTHEDSMHA SGRVDEAIAR LRDTGNVYEK DGALWLRTSA FGDDKDRVVI
     KSDGKPAYIA GDLAYYLDKR QRGFDLCIYM LGADHHGYIA RLKAAAAAFG DDPAIVEVLI
     GQMVNLVCDG QLVRMSKRSG NVITLDDLVE AIGVDAARYS LIRSSVDTPI DIDLALWSSS
     SNENPVYYVQ YAHARLSALA RNAAEFGLIP DTGHLELLSH DKEGALLRTV GEFPQVLKTA
     AALREPHRVC RYLEDLAGDY HRFYDSCRVL PQGDEKPTDL HTARLALCQA NRQVIANGLA
     ILGVSAPERM