SYN_PASMU
ID SYN_PASMU Reviewed; 467 AA.
AC Q9CN06;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 25-MAY-2022, entry version 123.
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=PM0643;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK02727.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE004439; AAK02727.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_005726506.1; NC_002663.1.
DR AlphaFoldDB; Q9CN06; -.
DR SMR; Q9CN06; -.
DR STRING; 747.DR93_1473; -.
DR EnsemblBacteria; AAK02727; AAK02727; PM0643.
DR KEGG; pmu:PM0643; -.
DR HOGENOM; CLU_004553_2_0_6; -.
DR OMA; DNMDLAE; -.
DR Proteomes; UP000000809; 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; Reference proteome.
FT CHAIN 1..467
FT /note="Asparagine--tRNA ligase"
FT /id="PRO_0000176438"
SQ SEQUENCE 467 AA; 52856 MW; 91EDD9ABCFF30E23 CRC64;
MTKVASIVDV LQGKIAIGET VTVRGWIRTR RDSKAGLSFL AIYDGSCFDP IQAIVNNDIE
NYETEVLRLT TGCSVIVTGT VVESPAEGQA VELQAEKVEV AGWVEDPETY PMAAKRHSIE
YLREVAHLRP RTNIIGAVAR VRHCLAQAIH RFFHEQGFYW VATPLITASD TEGAGEMFRV
STLDLENLPR DDKGAVDFSQ DFFGKESFLT VSGQLNGETY ACALSKIYTF GPTFRAENSN
TTRHLAEFWM VEPEIAFATL ADNAKLAEDM LKYVFRAVLE ERKDDLKFFE KHVDNDVISR
LENFINSDFA QIDYTDAIEV LLQSGKKFEF PVSWGIDLSS EHERYLAEEH FKSPVVVKNY
PKDIKAFYMR LNDDGKTVAA MDVLAPGIGE IIGGSQREER LDVLDKRMIE MGLNPEDYWW
YRDLRRYGTV PHAGFGLGFE RLIVYVTGVQ NIRDVIPFPR SPRNANF