ID   SYR_MYCPN               Reviewed;         537 AA.
AC   P75222;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 132.
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=MPN_556; ORFNames=MP286;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1)
OS   (Mycoplasmoides pneumoniae).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129 / Subtype 1;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB95934.1; -; Genomic_DNA.
DR   PIR; S73612; S73612.
DR   RefSeq; NP_110245.1; NC_000912.1.
DR   RefSeq; WP_010874913.1; NZ_OU342337.1.
DR   AlphaFoldDB; P75222; -.
DR   SMR; P75222; -.
DR   IntAct; P75222; 2.
DR   STRING; 272634.MPN_556; -.
DR   EnsemblBacteria; AAB95934; AAB95934; MPN_556.
DR   KEGG; mpn:MPN_556; -.
DR   PATRIC; fig|272634.6.peg.618; -.
DR   HOGENOM; CLU_006406_0_1_14; -.
DR   OrthoDB; 9805987at2; -.
DR   BioCyc; MPNE272634:G1GJ3-912-MONOMER; -.
DR   Proteomes; UP000000808; 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; 3.40.50.620; 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; 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; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 1.
DR   PRINTS; PR01038; TRNASYNTHARG.
DR   SMART; SM00836; DALR_1; 1.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 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..537
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151578"
FT   MOTIF           113..123
FT                   /note="'HIGH' region"
SQ   SEQUENCE   537 AA;  62121 MW;  099B1C0DC33A39B2 CRC64;
     MLFINTDLQE CLNALNLEFD EHKELVKLVK NNSFSGFAST VVFHLKGVNQ KETAQQIAAW
     LLKHKKAHYR RVFVANNNFI NFEISPQKYL DFLKTKPTFA PKPTKVLIEW VSANPTGELH
     LGHVRNAFFG HVLNNLMVFL GFQTVREYWV NDYGQQARVF GFSVYQALHL QQNIKVTPHP
     DGYEGELVDS IAKTITGIPL DKLSFEEFLQ QPFLDQLLAD CTAKVLEVIK QDLATIHIHF
     DSWKFESQVV KETDYKKLLT QFKDEAHYEK DGAIWLKTTL YGDDKDRVLV RQDNRPSYFG
     TDVAYHLDKA ARGFDLLYDI WGSDHEGHIK RMHCVYEGLK IHQKCQLKIT ALQLVMLYKN
     KEIVRLSKRA GNVITIKQML QMLSEDAARW FMLSQTNNSI IKIDLDTANL QNSSNPVYYV
     QYAYARMCSV LKVVDQAALA QVNDCSLLTH EKEIALLDQL VYFKSLLEKV QVSHELHLLT
     NYLYETATLF HSWYKACKIN DPAQYNLTQQ RLLLLQSLHH VFGQLLQILN ITAPQQM
//