SYN_MESHJ
ID SYN_MESHJ Reviewed; 449 AA.
AC Q4A9S1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Asparagine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00534};
DE EC=6.1.1.22 {ECO:0000255|HAMAP-Rule:MF_00534};
DE AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00534};
DE Short=AsnRS {ECO:0000255|HAMAP-Rule:MF_00534};
GN Name=asnS {ECO:0000255|HAMAP-Rule:MF_00534}; OrderedLocusNames=MHJ_0414;
OS Mesomycoplasma hyopneumoniae (strain J / ATCC 25934 / NCTC 10110)
OS (Mycoplasma hyopneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX NCBI_TaxID=262719;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J / ATCC 25934 / NCTC 10110;
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-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-
CC asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659,
CC Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1.22;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00534};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00534}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00534}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00534}.
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DR EMBL; AE017243; AAZ44500.1; -; Genomic_DNA.
DR RefSeq; WP_011284172.1; NC_007295.1.
DR AlphaFoldDB; Q4A9S1; -.
DR SMR; Q4A9S1; -.
DR STRING; 262719.MHJ_0414; -.
DR EnsemblBacteria; AAZ44500; AAZ44500; MHJ_0414.
DR KEGG; mhj:MHJ_0414; -.
DR eggNOG; COG0017; Bacteria.
DR HOGENOM; CLU_004553_2_0_14; -.
DR OMA; DNMDLAE; -.
DR Proteomes; UP000000548; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00534; Asn_tRNA_synth; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004522; Asn-tRNA-ligase.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00457; asnS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..449
FT /note="Asparagine--tRNA ligase"
FT /id="PRO_1000051410"
SQ SEQUENCE 449 AA; 52301 MW; 0D22FD47AD98D5BF CRC64;
MFQTINEISI HPELYNQKKV LIQGWITNIR GNLKIIFVEL NDGSSFKNLQ CVLKKEFIDF
DKIENLALGV AVEISGIFSN TPERQQFGEV LVETLEIKGN NYNTNFPIQN QEISLEVLRQ
MPHFRHRSRL FRVIMKLRSA LFFEIHKFFR RQGFINFSAP ILTSNDGEGA GEVFIVDDEN
KDFFNKKTTL GVTGQLHAEA YALGFKKVYT FAPTFRAERS NTRRHAAEFW MIEPEVAFFT
LEQIIELAVK LLQKVIKSVI IRNKDEFIFL EKAGDKNLRK RLLQFCDSQV TQISYEKAIE
LLLEHQEKFE EKDLFFGCDL KTEHERFLTE EIFHMPVVII NYPKNLKAFY MHQNEDGQTV
AAFDLLVPGI GELIGGSQRE VRYEKLLARM SELNMNIEEF QWYLDLRKYG NPGSSGFGLG
FERLLMYITG IENIRDVIPF PRTSKNILM
