ID D0QWD0_DROMI Unreviewed; 557 AA.
AC D0QWD0;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Asparagine--tRNA ligase, cytoplasmic {ECO:0000256|ARBA:ARBA00039867};
DE EC=6.1.1.22 {ECO:0000256|ARBA:ARBA00012816};
DE AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029886};
GN ORFNames=GA10495 {ECO:0000313|EMBL:ACN94629.1};
OS Drosophila miranda (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7229 {ECO:0000313|EMBL:ACN94629.1};
RN [1] {ECO:0000313|EMBL:ACN94629.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MSH22 {ECO:0000313|EMBL:ACN94629.1};
RX PubMed=19859648; DOI=10.1007/s00239-009-9298-2;
RA Marion de Proce S., Halligan D.L., Keightley P.D., Charlesworth B.;
RT "Patterns of DNA-sequence divergence between Drosophila miranda and D.
RT pseudoobscura.";
RL J. Mol. Evol. 69:601-611(2009).
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; FJ821025; ACN94629.1; -; Genomic_DNA.
DR RefSeq; XP_017151838.1; XM_017296349.1.
DR RefSeq; XP_017151852.1; XM_017296363.1.
DR RefSeq; XP_017151853.1; XM_017296364.1.
DR AlphaFoldDB; D0QWD0; -.
DR GeneID; 108161925; -.
DR KEGG; dmn:108161925; -.
DR OMA; DCCLYPR; -.
DR OrthoDB; 347413at2759; -.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 255..549
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 84..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 557 AA; 63435 MW; A25011120A4CE78F CRC64;
MPADLADLTL SALFTSEKSG SDESGDGSEA KPYKSILQAM RHAGKEPFPT IYVDSKDPNA
AEAFEPAAKS QLKKIQKLFV REGHKNAEKQ QREAGDAEKR QQNLEEARNV KISEDPSWPV
ARKIRIMEGT ENRGSRVKVY GWVHRLRRQG KALIFITLRD GTGFLQCVLN DQLCQTYDAL
TLSTESTVVL FGTLKLIPEG KTAPGGHELN VDYWELIGLA PPGGADAILN EEAQPDVQLD
NRHIMIRGEN TSKVLKMRSV VMQAFRAHYL ARGYNEVTPP TLVQTQVEGG STLFKLQYFS
EEAYLTQSSQ LYLETCLPAL GDVFTIAQSY RAEQSRTRRH LAEYTHIEAE CPFLTFEDLL
DRLEDLVCDV VDRVLKSPWG NLVKELNPDF KPPTKPFRRM NYSDAIKWLK ENNVTKDDGT
FYEFGEDIPE APERKMTDAI NEPIMLCRFP AEIKSFYMSR CPEDKTLTES VDVLLPNVGE
IVGGSMRIFD SEELLKGYQR EGIDPKPYYW YTDQRIYGTL PHGGYGLGLE RFLCWLLNRY
HIREVCLYPR FLDRCKP
//
