SYR_META1
ID SYR_META1 Reviewed; 541 AA.
AC B3PM19;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Arginine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00123};
DE EC=6.1.1.19 {ECO:0000255|HAMAP-Rule:MF_00123};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00123};
DE Short=ArgRS {ECO:0000255|HAMAP-Rule:MF_00123};
GN Name=argS {ECO:0000255|HAMAP-Rule:MF_00123};
GN OrderedLocusNames=MARTH_orf134;
OS Metamycoplasma arthritidis (strain 158L3-1) (Mycoplasma arthritidis).
OC Bacteria; Tenericutes; Mycoplasmoidales; Metamycoplasmataceae;
OC Metamycoplasma.
OX NCBI_TaxID=243272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=158L3-1;
RX PubMed=18573899; DOI=10.1128/iai.00516-08;
RA Dybvig K., Zuhua C., Lao P., Jordan D.S., French C.T., Tu A.H.,
RA Loraine A.E.;
RT "Genome of Mycoplasma arthritidis.";
RL Infect. Immun. 76:4000-4008(2008).
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; Evidence={ECO:0000255|HAMAP-Rule:MF_00123};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00123}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00123}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00123}.
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DR EMBL; CP001047; ACF07071.1; -; Genomic_DNA.
DR RefSeq; WP_012498028.1; NC_011025.1.
DR AlphaFoldDB; B3PM19; -.
DR SMR; B3PM19; -.
DR STRING; 243272.MARTH_orf134; -.
DR PRIDE; B3PM19; -.
DR EnsemblBacteria; ACF07071; ACF07071; MARTH_orf134.
DR KEGG; mat:MARTH_orf134; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_14; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000008812; 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..541
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000095381"
FT MOTIF 123..133
FT /note="'HIGH' region"
SQ SEQUENCE 541 AA; 61896 MW; 39FFAF7DBE0FF235 CRC64;
MITTKEIIIA SLNEALEKLE IKKPITLTEP KSYGDYSTNL ALTLQKELGK PAIEIAKEIV
NAIDLKKHKE IVKVEVANPG FINFWVSNSV LSDLVNSINS LEDHYGDMSK EGKGAVNIEF
VSANPTGFLH IGHARNAAIG ATLCNVLEKA GHRVVREYYV NDYGNQMNNL AASVFSRYQQ
IFNKDFPMPD DAYKGHDMTI FADAFFKKYG DKYRNVAYTE EVKKLFRDFG REIALENIKI
DLGRFGVWFD LYTSETQQYE KDRVWPVIRR LKSTYEKDGA TWLNTTKGGN DDKDRVIIKG
NGESTYMCAD IAYHEQKFVE LHDPEKGKII DIWGADHSGY VERIKFSFED LGWRRDQIEI
LLFQLLRVVK NGKEIKMSKR LGTSLTLREL LDLVGKDAVR YFLIERSYNS KIDFDINKVQ
KSDETNPLFL IKYAHARCYQ LLEKAQIKNP IASNLENDFA QKLTNELKEY PNLIDTMAKT
YKVNLLPPYL LKLAGAFNSF YSNVRISGDP NEQSYLALVK ATKIVLANAM KLMDLDIPNK
M