ID   SYR_MYCS2               Reviewed;         550 AA.
AC   Q9X5M0; A0R223; I7G6F4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   27-MAR-2024, entry version 141.
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=MSMEG_4959, MSMEI_4832;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Pavelka M.S. Jr., Jacobs W.R. Jr.;
RT   "A comparison of the construction of unmarked deletion mutations in
RT   Mycobacterium smegmatis, M. bovis bacille Calmette-Guerin (BCG) and M.
RT   tuberculosis H37Rv by allelic exchange.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(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;
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF126720; AAD32590.1; -; Genomic_DNA.
DR   EMBL; CP000480; ABK70921.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP41277.1; -; Genomic_DNA.
DR   RefSeq; WP_011730214.1; NZ_SIJM01000019.1.
DR   RefSeq; YP_889211.1; NC_008596.1.
DR   AlphaFoldDB; Q9X5M0; -.
DR   SMR; Q9X5M0; -.
DR   STRING; 246196.MSMEG_4959; -.
DR   PaxDb; 246196-MSMEI_4832; -.
DR   GeneID; 66736280; -.
DR   KEGG; msg:MSMEI_4832; -.
DR   KEGG; msm:MSMEG_4959; -.
DR   PATRIC; fig|246196.19.peg.4838; -.
DR   eggNOG; COG0018; Bacteria.
DR   OrthoDB; 9803211at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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; cd07956; Anticodon_Ia_Arg; 1.
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..550
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151579"
FT   MOTIF           130..140
FT                   /note="'HIGH' region"
FT   CONFLICT        149
FT                   /note="A -> T (in Ref. 1; AAD32590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        232
FT                   /note="D -> N (in Ref. 1; AAD32590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        255..257
FT                   /note="EDS -> GDW (in Ref. 1; AAD32590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        331
FT                   /note="L -> V (in Ref. 1; AAD32590)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   550 AA;  59429 MW;  4DAB7844FFFCFCEC CRC64;
     MTPADLAELL KATAAAVLTE HDLDVAALPA TVTVERPRNP EHGDYATNLA LQLGKKVGVN
     PRELAGWLAT ALTAADGIAV AEVAGPGFVN LRIEASAQGV IITNVLAAEG SYGSSDQYAG
     RNVNLEFVSA NPTGPIHIGG TRWAAVGDAL GRLLATQGAA VTREYYFNDH GAQIDRFVNS
     LIASAKGEPT PEDGYAGDYI VDIAQQVIAK APDVLGLPED QQRETFRAIG VDLMFTHIKQ
     SLHDFGTDFD VYTHEDSMHT SGRVDQAITQ LREAGSIYEK DGAVWLRTTD FGDDKDRVVI
     KSDGNAAYIA GDLAYYLDKR KRGFDLCIYM LGADHHGYIA RLKAAAAALG DDPDTVEVLI
     GQMVNLVRDG QPVRMSKRAG TVITLDDLVE AIGVDAARYA LIRSSVDTPI DIDLELWSSA
     SNENPVYYVQ YAHARLCALA RNAADLGVSV NTDHLDLLTH EKEGALIRNL GEFPRVLKTA
     ASLREPHRVC RYLEDLAGDY HRFYDSCRVL PQGDEEPGDL HSARLALCRA TRQVIANGLA
     ILGVSAPERM
//