SYR_MESH7
ID SYR_MESH7 Reviewed; 534 AA.
AC Q4A900;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=MHP7448_0012;
OS Mesomycoplasma hyopneumoniae (strain 7448) (Mycoplasma hyopneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX NCBI_TaxID=262722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7448;
RX PubMed=16077101; DOI=10.1128/jb.187.16.5568-5577.2005;
RA Vasconcelos A.T.R., Ferreira H.B., Bizarro C.V., Bonatto S.L.,
RA Carvalho M.O., Pinto P.M., Almeida D.F., Almeida L.G.P., Almeida R.,
RA Alves-Junior L., Assuncao E.N., Azevedo V.A.C., Bogo M.R., Brigido M.M.,
RA Brocchi M., Burity H.A., Camargo A.A., Camargo S.S., Carepo M.S.,
RA Carraro D.M., de Mattos Cascardo J.C., Castro L.A., Cavalcanti G.,
RA Chemale G., Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P.,
RA Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S.S.,
RA Fiorentin L., Franco G.R., Freitas N.S.A., Frias D., Grangeiro T.B.,
RA Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A.,
RA Laurino J.P., Lima L.F.A., Lopes M.I., Loreto E.L.S., Madeira H.M.F.,
RA Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R.B.,
RA Moreira M.A.M., Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C.,
RA Paixao R.F.C., Pedrosa F.O., Pena S.D.J., Pereira M., Pereira-Ferrari L.,
RA Piffer I., Pinto L.S., Potrich D.P., Salim A.C.M., Santos F.R., Schmitt R.,
RA Schneider M.P.C., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N.,
RA Silva D.W., Silva R., Silva S.C., Soares C.M.A., Souza K.R.L., Souza R.C.,
RA Staats C.C., Steffens M.B.R., Teixeira S.M.R., Urmenyi T.P.,
RA Vainstein M.H., Zuccherato L.W., Simpson A.J.G., Zaha A.;
RT "Swine and poultry pathogens: the complete genome sequences of two strains
RT of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae.";
RL J. Bacteriol. 187:5568-5577(2005).
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; AE017244; AAZ53389.1; -; Genomic_DNA.
DR RefSeq; WP_011289935.1; NC_007332.1.
DR AlphaFoldDB; Q4A900; -.
DR SMR; Q4A900; -.
DR EnsemblBacteria; AAZ53389; AAZ53389; MHP7448_0012.
DR KEGG; mhp:MHP7448_0012; -.
DR HOGENOM; CLU_006406_0_1_14; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000000553; 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_0000242048"
FT MOTIF 120..130
FT /note="'HIGH' region"
SQ SEQUENCE 534 AA; 61716 MW; 49C70EA57E41D80D CRC64;
MKKKISQAII KFFKNENLII DESKLIIEKS KNFGDYSSNV ALMFAKQNKI DSLKLAQTIK
NQLLSENLNL EKIEIAPPGF INFFISKNEY ANIVSEIIQK GENFGRYSLQ KKINLEFVSA
NPTGFLHLGH LRGAVIGDIL ANILEFSGNF VFREYYINDF GSQIDRLVSS VFSRYQQIFK
KFALPEEAYL GEDIIWCAQK FFQIYANKFE NSSLDDLETY KIFREKSIEI FLDEIKADLA
NLSIKFDVFS SESELFRTEK VQKNLANLPF VYKKEEAIWL KTSKFGDQKD RVLVKKNGEF
TYFSSDIAYH FEKINSNFKP DFLINIWGAD HIGYVDRMKA ALKTVNLNQK LDILLYQLVK
LFKNGQEFKM SKRMGKTFTI KDLLELVDQD AIRYFISERS YNSLVEFDIG LAAKISLQNP
LFLIQYAHAR ASKLLANSTI VPEKILKFEA ENETILISKL KQFEEIVLKI TKNYKINLLN
KYLLELANLF NSFYSNSKII GNQNQNSLLS LTKAVQIVLK NGLKLLGIKA KERI