SYR_MYCS2
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 25-MAY-2022, entry version 133.
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; Actinobacteria; Corynebacteriales; 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}.
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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.MSMEI_4832; -.
DR PRIDE; Q9X5M0; -.
DR EnsemblBacteria; ABK70921; ABK70921; MSMEG_4959.
DR EnsemblBacteria; AFP41277; AFP41277; 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 OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
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; 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_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
