ID G0SHG6_CHATD Unreviewed; 587 AA.
AC G0SHG6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=asparagine--tRNA ligase {ECO:0000256|ARBA:ARBA00012816};
DE EC=6.1.1.22 {ECO:0000256|ARBA:ARBA00012816};
DE AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029886};
GN ORFNames=CTHT_0069950 {ECO:0000313|EMBL:EGS17655.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS17655.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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:0000256|ARBA:ARBA00000422};
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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DR EMBL; GL988047; EGS17655.1; -; Genomic_DNA.
DR RefSeq; XP_006697273.1; XM_006697210.1.
DR AlphaFoldDB; G0SHG6; -.
DR STRING; 759272.G0SHG6; -.
DR GeneID; 18261033; -.
DR KEGG; cthr:CTHT_0069950; -.
DR eggNOG; KOG0555; Eukaryota.
DR HOGENOM; CLU_004553_2_10_1; -.
DR OMA; DCCLYPR; -.
DR OrthoDB; 347413at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd04323; AsnRS_cyto_like_N; 1.
DR CDD; cd00776; AsxRS_core; 1.
DR Gene3D; 3.30.1910.20; asparaginyl-tRNA synthetase, N-terminal domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR048952; AsnRS_N.
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:SF16; ASPARAGINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF20917; AsnRS_N; 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:0000313|EMBL:EGS17655.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066}.
FT DOMAIN 282..579
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 85..130
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 587 AA; 66818 MW; 1DD0567A3F9E13A9 CRC64;
MAGDQELADR TKTEAPAATC YIDPVNGKDD ETADGSESKP YQSLYHALIQ HLDKPAPTYL
TLVPPKEGAD SADGPRWEAP AKSAMKKALA RVDAYKKKLA KEQASAKQEE EERKQRLKNL
EEAKKIVLKE DPSLPPAVRI KLNNFDVELG DGESKKGTRV KVYGRIQHIR AQKHTTFITI
KDGYGILQCI FPTGPLTQNY EALLFAQETA LVVYGEMRAV PPGHKVPGNR ELHVDYFEVL
GRAPCDLDAI TNKVSMQQDV WDAQMLDNRH LVLRGENASA VMKLREAVEL AFIDTYREME
FRKVSPPAMV QTQVEGGATL FKYDYYGEEA YLTQSSQLYL ETVIQSLGNV YCIEKSFRAE
KSLTRRHLSE YTHVEAELDF IDFNDLLDHI EELISRVVDK VLADDTARGY IEKLNPGFKK
PTRPFLRMRY EEAIEWLNKQ DPPILNEEGK PHQFGDDIAE AAERKMTDII NRPILLTHFP
VEIKAFYMKK DPKDPRVTES VDVLMPGVGE IVGGSMRMDD YDELIEAYKK NGIPHEPYYW
YTDQRKYGSS PHGGYGLGLE RFLAWLANQH TVRTTCLYPR FMGRCKP
//
