SYN_THEGJ
ID SYN_THEGJ Reviewed; 430 AA.
AC C5A4R8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=TGAM_0728;
OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=593117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT the most radioresistant organism known amongst the Archaea.";
RL Genome Biol. 10:R70.1-R70.23(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 -!- 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; CP001398; ACS33230.1; -; Genomic_DNA.
DR RefSeq; WP_015858348.1; NC_012804.1.
DR AlphaFoldDB; C5A4R8; -.
DR SMR; C5A4R8; -.
DR STRING; 593117.TGAM_0728; -.
DR PaxDb; C5A4R8; -.
DR EnsemblBacteria; ACS33230; ACS33230; TGAM_0728.
DR GeneID; 7987702; -.
DR KEGG; tga:TGAM_0728; -.
DR PATRIC; fig|593117.10.peg.728; -.
DR eggNOG; arCOG00407; Archaea.
DR HOGENOM; CLU_004553_2_0_2; -.
DR OMA; DNMDLAE; -.
DR OrthoDB; 24864at2157; -.
DR Proteomes; UP000001488; 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..430
FT /note="Asparagine--tRNA ligase"
FT /id="PRO_1000211907"
SQ SEQUENCE 430 AA; 49646 MW; DBC7726F274F7A97 CRC64;
MIDKVYCADV KPEMEGKRVK LAGWVYRKRE VGKKVFIVLR DSSGIVQVVF SKELNEEAYR
EAKKLGIESS VIIEGTVKAD PRAPTGAEVQ ADKLQVIQNV DFFPITKDAS PEFLLDVRHL
HLRSPKVASI MKVKGTLMQA AREWLLQDGW YEVFPPILVT GAVEGGSTLF KLKYFDKTAY
LSQSAQLYLE AAIFGLEKVW SLTPSFRAEK SRTRRHLTEF WHLELEAAWM DLWDIMKVEE
ELVSYMVQRT LELRRSEIET FRKDLTTLKN AVPPFPRISY DEAIDILQSK GVEIEWGEDM
GADEERVLTE EFEAPFFVYG YPKHIKAFYM KEDPEDPRKV LAADMLAPEG YGEIIGGSQR
EDNYDKLIQR ILEEGMDPKD YEWYLDLRKY GSVPHSGFGL GLERLVAWVL KLDHVRWATL
FPRTPSRLYP