SYN_VIBVU
ID SYN_VIBVU Reviewed; 466 AA.
AC Q8DAF0;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 114.
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=VV1_2254;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
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; AE016795; AAO10633.1; -; Genomic_DNA.
DR RefSeq; WP_011080125.1; NC_004459.3.
DR AlphaFoldDB; Q8DAF0; -.
DR SMR; Q8DAF0; -.
DR EnsemblBacteria; AAO10633; AAO10633; VV1_2254.
DR KEGG; vvu:VV1_2254; -.
DR HOGENOM; CLU_004553_2_0_6; -.
DR OMA; DNMDLAE; -.
DR Proteomes; UP000002275; Chromosome 1.
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_0000176476"
SQ SEQUENCE 466 AA; 52406 MW; A4577F799612F58B CRC64;
MTYAPVKDVL SGKLAVDSEV TVRGWIRTRR DSKAGISFLA IYDGSCFDPI QAVVPNNLNN
YNDEVLKLTT GCSVEVTGKI VASPAAGQAF ELAATDVKVV GWVEDADTYP MAKTRHSIEY
LREVAHLRPR TNVIGAVARV RHSLSQAIHR FYHEQGYYWL SAPLITASDC EGAGEMFRVS
TLDLANLPRT ESGDVDFNED FFGKETFLTV SGQLNGEAYA CALSKIYTFG PTFRAENSNT
SRHLAEFWMV EPEVAFADLN DIAKLAEDML KYVFAAVLEE RRDDLEFFAS RIDKDVINRL
EQFVSSDFAQ VDYTDAIQIL LDSGREFEFP VEWGIDMSSE HERFLAEEHF KAPVIVKNYP
KDIKAFYMRM NEDGKTVAAM DVLAPGIGEI IGGSQREERL DVLDARMVEM GIDPEHMNWY
RDLRRYGTVP HAGFGLGFER LVSYVTGMGN VRDVIPFPRT PRNANF
