ID   SYR_MYCGE               Reviewed;         537 AA.
AC   P47618; Q49291; Q49444;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 138.
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=MG378;
OS   Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS   (Mycoplasmoides genitalium).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 153-255 AND 350-455.
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA   Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT   "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL   J. Bacteriol. 175:7918-7930(1993).
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; L43967; AAC71605.1; -; Genomic_DNA.
DR   EMBL; U02168; AAD12450.1; -; Genomic_DNA.
DR   EMBL; U01740; AAD10550.1; -; Genomic_DNA.
DR   PIR; H64241; H64241.
DR   RefSeq; WP_009885941.1; NZ_AAGX01000012.1.
DR   AlphaFoldDB; P47618; -.
DR   SMR; P47618; -.
DR   STRING; 243273.MG_378; -.
DR   EnsemblBacteria; AAC71605; AAC71605; MG_378.
DR   KEGG; mge:MG_378; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_14; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   BioCyc; MGEN243273:G1GJ2-472-MON; -.
DR   Proteomes; UP000000807; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd00671; ArgRS_core; 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; 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; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 1.
DR   PRINTS; PR01038; TRNASYNTHARG.
DR   SMART; SM00836; DALR_1; 1.
DR   SUPFAM; SSF47323; SSF47323; 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..537
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151576"
FT   MOTIF           113..123
FT                   /note="'HIGH' region"
FT   CONFLICT        153..154
FT                   /note="YG -> MW (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        350..355
FT                   /note="FALQLV -> MHYNWI (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   537 AA;  62406 MW;  D8080D69EDA33817 CRC64;
     MFFIINDLKE CISALKLKFD DQKELVKLVK NNSFNGFSST IIFQLKSENH KKIADSIVEW
     FLKNKKDNYQ NVFIANNNFI NFQISYQKYL EYLIKTPCFT KKNIKILIES VSANPTGRIH
     LGHVRIAFFG DVLNNLAKLL GYTTVCEYWV NDYGQQARVF SFSVYQSLQL KKNIAIQQHP
     DGYSGIVIDK IASEIENFPV DNLNFEEFCK TSFLDHFLVN CTQKVLSLIK SDLNKIHVFI
     DSWKFESEIV KKTNFNDLLE QLKPNSYFYQ DNALWLKTTL YGDDKDRVLI RSDKRASYFG
     TDVAYHLEKL QRGFDILFNV WGTDHEGHIK RMYCAFDALK NTTKTSLKIF ALQLVTLYKN
     KELVRLSKRA GNVITIETML SMISEDAARW FMLSQNNGTI IKIDLDIANL QNSANPVYYV
     QYAFARMNSI LRIANSDQLK EITDCSLLIN EKEISLLNQL VYYPFMLQKA METGELHLLT
     NFLYETASLF HSWYKVCKIN DDKNSLLSAQ RLALLRSLQF IVKQILDVLK ISTPQQM