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 27-MAR-2024, entry version 117.
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 PaxDb; 186497-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 OrthoDB; 5908at2157; -.
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 CDD; cd00776; AsxRS_core; 1.
DR CDD; cd04319; PhAsnRS_like_N; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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 NCBIfam; TIGR00457; asnS; 1.
DR PANTHER; PTHR22594:SF34; ASPARAGINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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
//
