ID   B5YDP0_DICT6            Unreviewed;       433 AA.
AC   B5YDP0;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   08-OCT-2025, entry version 105.
DE   RecName: Full=Asparagine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00534};
DE            EC=6.1.1.22 {ECO:0000256|HAMAP-Rule:MF_00534};
DE   AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00534};
DE            Short=AsnRS {ECO:0000256|HAMAP-Rule:MF_00534};
GN   Name=asnS {ECO:0000256|HAMAP-Rule:MF_00534,
GN   ECO:0000313|EMBL:ACI19611.1};
GN   OrderedLocusNames=DICTH_0782 {ECO:0000313|EMBL:ACI19611.1};
OS   Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12).
OC   Bacteria; Pseudomonadati; Dictyoglomota; Dictyoglomia; Dictyoglomales;
OC   Dictyoglomaceae; Dictyoglomus.
OX   NCBI_TaxID=309799 {ECO:0000313|EMBL:ACI19611.1, ECO:0000313|Proteomes:UP000001733};
RN   [1] {ECO:0000313|EMBL:ACI19611.1, ECO:0000313|Proteomes:UP000001733}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35947 / DSM 3960 / H-6-12
RC   {ECO:0000313|Proteomes:UP000001733};
RX   PubMed=24558247;
RA   Coil D.A., Badger J.H., Forberger H.C., Riggs F., Madupu R., Fedorova N.,
RA   Ward N., Robb F.T., Eisen J.A.;
RT   "Complete Genome Sequence of the Extreme Thermophile Dictyoglomus
RT   thermophilum H-6-12.";
RL   Genome Announc. 2:e00109-e00114(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Asn) + L-asparagine + ATP = L-asparaginyl-tRNA(Asn) + AMP
CC         + diphosphate + H(+); 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:0000256|HAMAP-Rule:MF_00534};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00534}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00534}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00534}.
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DR   EMBL; CP001146; ACI19611.1; -; Genomic_DNA.
DR   RefSeq; WP_012548243.1; NC_011297.1.
DR   AlphaFoldDB; B5YDP0; -.
DR   STRING; 309799.DICTH_0782; -.
DR   PaxDb; 309799-DICTH_0782; -.
DR   KEGG; dth:DICTH_0782; -.
DR   eggNOG; COG0017; Bacteria.
DR   HOGENOM; CLU_004553_2_0_0; -.
DR   OrthoDB; 9762036at2; -.
DR   Proteomes; UP000001733; 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   Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 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   NCBIfam; NF003037; PRK03932.1; 1.
DR   NCBIfam; NF003483; PRK05159.1; 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 {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00534};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00534}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00534};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00534};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00534};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00534}; Reference proteome {ECO:0000313|Proteomes:UP000001733}.
FT   DOMAIN          133..423
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   433 AA;  50409 MW;  19C10E0BB473F299 CRC64;
     MSAPWVYIED IPKIQEGEIE VRGWLFNKRS SGKIVFLIIR DGTGYIQGVA TLDNFTQDQL
     ESLEKIPIES SLIVVGDLKK EPRAPGGYEL LLKSVNVVSY SEEYPIQKKD HSIDFLLERR
     HLWIRSRKQN AILRIRSEVV KAIRDFLDEK GFVLIDAPIL TPSACEGTTT LFELDYFDLG
     KAYLSQSGQL YMEAACMAFG KVYCFGPAFR AEKSKTRRHL TEFWMVEPEM AFWDWQDNMR
     LQEELVSYIV QRVLEKRKRE LEILERDTKP LEKVVPPFPR ITYREAIEIL KRNGQNVEYG
     DDFGGDEETI ISSQFDRPVF IHHYPAKIKP FYMQPDPENP EEVLNNDLLA PEGYGEIIGG
     SQRIHDLKLL EKKLEEYNLP KEAFEWYLDL RRYGSVPHSG FGLGIERTVA WICGLKHVRE
     AIPFPRMIYR IYP
//