SYR_MYCPN
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 03-AUG-2022, entry version 126.
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) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
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; NC_000912.1.
DR AlphaFoldDB; P75222; -.
DR SMR; P75222; -.
DR IntAct; P75222; 2.
DR STRING; 272634.MPN_556; -.
DR PRIDE; P75222; -.
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 OMA; NKPLHLG; -.
DR BioCyc; MPNE272634:G1GJ3-912-MON; -.
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; -; 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_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
