SYN_THEKO
ID SYN_THEKO Reviewed; 431 AA.
AC Q5JHC1;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 101.
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=TK0759;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(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 -!- 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; AP006878; BAD84948.1; -; Genomic_DNA.
DR RefSeq; WP_011249710.1; NC_006624.1.
DR AlphaFoldDB; Q5JHC1; -.
DR SMR; Q5JHC1; -.
DR STRING; 69014.TK0759; -.
DR EnsemblBacteria; BAD84948; BAD84948; TK0759.
DR GeneID; 3235715; -.
DR KEGG; tko:TK0759; -.
DR PATRIC; fig|69014.16.peg.739; -.
DR eggNOG; arCOG00407; Archaea.
DR HOGENOM; CLU_004553_2_0_2; -.
DR InParanoid; Q5JHC1; -.
DR OMA; DNMDLAE; -.
DR OrthoDB; 24864at2157; -.
DR PhylomeDB; Q5JHC1; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004816; F:asparagine-tRNA ligase activity; IBA:GO_Central.
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; IBA:GO_Central.
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..431
FT /note="Asparagine--tRNA ligase"
FT /id="PRO_0000176488"
SQ SEQUENCE 431 AA; 49838 MW; 775B3ABD9BC00591 CRC64;
MIDKVYCADV TPEMEGKKVK LAGWVYRKRE VGKKVFIVLR DSSGIVQVVF SKDLNEEAYR
EAKKVGIESS VIIEGTVKAD PRAPTGAEVQ GEKLQIIQNV DFFPITKDAS DEFLLDVRHL
HLRSPKVAAI MKVKGTLMQA AREWLLQDGW YEVFPPILVT GAVEGGATLF KLKYFDRYAY
LSQSAQLYLE AAIFGLEKVW SLTPSFRAEK SRTRRHLTEF WHLELEAAWM DLWDIMKVEE
ELVSYMVQRT LELRKKEIEL YRKDDIKTLK NAVPPFPRIS YDEAIDILQS KGVNIEWGED
MGADEERVLT EEFESPFFVY GYPKHIKAFY MKEDPEDPRK VLAADMLAPE GYGEIIGGSQ
REDDYDKLVQ RILEEGMKPE DYEWYLDLRK YGSVPHSGFG LGLERLVAWV LKLDHVRWAT
LFPRTPSRLY P