ID   SYN_PYRFU               Reviewed;         434 AA.
AC   Q8U4D3;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2002, sequence version 2.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Asparagine--tRNA ligase;
DE            EC=6.1.1.22;
DE   AltName: Full=Asparaginyl-tRNA synthetase;
DE            Short=AsnRS;
GN   Name=asnS; OrderedLocusNames=PF0155;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL80279.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE009950; AAL80279.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_014835459.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U4D3; -.
DR   SMR; Q8U4D3; -.
DR   STRING; 186497.PF0155; -.
DR   PRIDE; Q8U4D3; -.
DR   EnsemblBacteria; AAL80279; AAL80279; PF0155.
DR   GeneID; 41711945; -.
DR   KEGG; pfu:PF0155; -.
DR   PATRIC; fig|186497.12.peg.161; -.
DR   eggNOG; arCOG00407; Archaea.
DR   HOGENOM; CLU_004553_2_0_2; -.
DR   OMA; DNMDLAE; -.
DR   OrthoDB; 24864at2157; -.
DR   PhylomeDB; Q8U4D3; -.
DR   Proteomes; UP000001013; 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..434
FT                   /note="Asparagine--tRNA ligase"
FT                   /id="PRO_0000176486"
SQ   SEQUENCE   434 AA;  50114 MW;  0B9D55512F31B7A8 CRC64;
     MIEKVYCSEV KPELEGKKVK LAGWVYSNMK VGKKIFLWIR DSTGIVQTVI AKNVVGEEVF
     EKAKKLGRES SVIVEGIVKA DERAPGGAEV RVEKLEVIQA VSEFPIPENP EQASPELLLD
     YRHLHIRTPK ASAIMKVKET LIMAAREWLL KDGWHEVFPP ILVTGAVEGG ATLFKLKYFD
     KYAYLSQSAQ LYLEAAIFGL EKVWSLTPSF RAEKSRTRRH LTEFWHLELE AAWMDLWDIM
     KVEEELVSYM VQRTLELRKK EIEMFRDDLT TLKNTEPPFP RISYDEAIDI LQSKGINVQW
     GDDLGADEER VLTEEFDRPF FVYGYPKQIK AFYMKEDPND PRKVLAADML APEGYGEIIG
     GSQREDDYEK LLNRILEEGM DPKDYEWYLD LRKYGSVPHS GFGLGVERLV AWVLKLDHIR
     WASLFPRTPA RLYP