SYN_YERP3
ID SYN_YERP3 Reviewed; 466 AA.
AC A7FJU5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
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};
GN OrderedLocusNames=YpsIP31758_2558;
OS Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP 31758;
RX PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT causative agent of Far East scarlet-like fever.";
RL PLoS Genet. 3:1508-1523(2007).
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.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00534}.
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DR EMBL; CP000720; ABS49879.1; -; Genomic_DNA.
DR RefSeq; WP_002211301.1; NC_009708.1.
DR AlphaFoldDB; A7FJU5; -.
DR SMR; A7FJU5; -.
DR EnsemblBacteria; ABS49879; ABS49879; YpsIP31758_2558.
DR GeneID; 66842129; -.
DR KEGG; ypi:YpsIP31758_2558; -.
DR HOGENOM; CLU_004553_2_0_6; -.
DR OMA; DNMDLAE; -.
DR Proteomes; UP000002412; 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..466
FT /note="Asparagine--tRNA ligase"
FT /id="PRO_1000061025"
SQ SEQUENCE 466 AA; 52074 MW; CF2D16263F6B92DD CRC64;
MSVVPVVDVL QGRAAVGSEV TVRGWVRTRR DSKAGISFVA VYDGSCFDPL QAVVNNTLPN
YQDEVLHLTT GCSVEVTGTV VASPGEGQSF EIQATAINVV GWVDDPDTYP MAAKRHSIEY
LREVAHLRPR TNLIGAVARV RHTLAQAIHR FFDENGYFWV STPLITASDT EGAGEMFRVS
TLDLENLPRT DTGAVDFSED FFGKEAFLTV SGQLNGETYA CALSKVYTFG PTFRAENSNT
SRHLAEFWMV EPEVAFASLD DVAGLAEKML KYVFQAVLNE RADDMKFFAE RVDKDAVDRL
QRFVTSDFAQ VDYTDAIEIL LASGQKFEND VSWGIDLSSE HERYLAEKHF KAPVVVKNYP
KDIKAFYMRM NEDGKTVAAM DVLAPGIGEI IGGSQREERL DVLDARLAEM GLNKEDYWWY
RDLRRYGTVP HSGFGLGFER LISYVTGVQN VRDVIPFPRT PRNASF