SYR_MESH2
ID SYR_MESH2 Reviewed; 534 AA.
AC Q602D8;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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}; OrderedLocusNames=mhp012;
OS Mesomycoplasma hyopneumoniae (strain 232) (Mycoplasma hyopneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX NCBI_TaxID=295358;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=232;
RX PubMed=15489423; DOI=10.1128/jb.186.21.7123-7133.2004;
RA Minion F.C., Lefkowitz E.J., Madsen M.L., Cleary B.J., Swartzell S.M.,
RA Mahairas G.G.;
RT "The genome sequence of Mycoplasma hyopneumoniae strain 232, the agent of
RT swine mycoplasmosis.";
RL J. Bacteriol. 186:7123-7133(2004).
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; AE017332; AAV27355.1; -; Genomic_DNA.
DR RefSeq; WP_011205851.1; NC_006360.1.
DR AlphaFoldDB; Q602D8; -.
DR SMR; Q602D8; -.
DR STRING; 295358.mhp012; -.
DR EnsemblBacteria; AAV27355; AAV27355; mhp012.
DR KEGG; mhy:mhp012; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_14; -.
DR OMA; NKPLHLG; -.
DR PhylomeDB; Q602D8; -.
DR Proteomes; UP000006822; 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.
FT CHAIN 1..534
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000242047"
FT MOTIF 120..130
FT /note="'HIGH' region"
SQ SEQUENCE 534 AA; 61651 MW; 020AADFBF972D3C7 CRC64;
MKKKISQAII KFFKNENLII DESKLIIEKS KNFGDYSSNV ALIFAKQNKI DSLKLAQTIK
NQLLSENLNL EKIEIAPPGF INFFISKNEY ANIVSEIIQK GENFGRYSLQ KKINLEFVSA
NPTGFLHLGH LRGAVIGDIL ANILEFSGNF VFREYYINDF GSQIDRLVGS VFSRYQQIFK
KFPLPEEAYL GEDIIWCAQK FFQIYANKFE NSSLDDLEAY KIFREKSIEI FLDEIKADLA
NLSIKFDVFS SESELFRTEK VQKNLANLPF VYKKEEAIWL KTSKFGDQKD RVLVKKNGEF
TYFSSDIAYH FEKINSNFKP DFLINIWGAD HIGYVDRMKA ALKTVNLNQK LDILLYQLVK
LFKNGQEFKM SKRMGKTFTI KDLLELVDQD AIRYFISERS YNSLVEFDIG LAAKISLQNP
LFLIQYAHAR ASKLLANSTI APEKKLKFEA ENETILISKL KQFEEIVLKI TKNYKINLLN
KYLLELANLF NSFYSNSKII GNQNQNSLLS LTKAVQIVLK NGLKLLGIKA KERI