ID A0A2K6E1P4_MACNE Unreviewed; 558 AA.
AC A0A2K6E1P4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
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 Name=NARS1 {ECO:0000313|Ensembl:ENSMNEP00000042099.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000042099.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000042099.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 RefSeq; XP_011731732.1; XM_011733430.1.
DR AlphaFoldDB; A0A2K6E1P4; -.
DR SMR; A0A2K6E1P4; -.
DR Ensembl; ENSMNET00000066601.1; ENSMNEP00000042099.1; ENSMNEG00000043822.1.
DR GeneID; 105477080; -.
DR KEGG; mni:105477080; -.
DR CTD; 4677; -.
DR GeneTree; ENSGT01030000234618; -.
DR OMA; DCCLYPR; -.
DR OrthoDB; 347413at2759; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000043822; Expressed in temporal lobe and 12 other cell types or tissues.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120}.
FT DOMAIN 259..550
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 79..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 558 AA; 63873 MW; B9EEC506E9A5CAD5 CRC64;
MSLEVTRATA GMVLELYVSD REGSDATGDG TKEKPFKTGL KALMTVGKEP FPTIYVDSQK
ENERWNVISK SQLKNIKKMW HREQMKSESR EKKEAEDSLR REKNLEEAKK ITIKNDPALP
EPKCVKISAL EGYRGQRVKV FGWVHRLRRQ GKNLMFLVLR DGTGYLQCVL ADELCQCYNG
VLLSTESSVA VYGMLNLTPK GKQAPGGHEL SCDFWELIGL APAGGADNLI NEESDVDVQL
NNRHMMIRGE NMSKILKARS MITRCFRDHF FDRGYHEITP PSLVQTQVEG GATLFKLNYF
GEEAFLTQSS QLYLETCLPA LGDVFCIAQS YRAEQSRTRR HLAEYTHVEA ECPFLTFDDL
LNRLEDLVCD VVDRILKSPA GSIVYELNPN FQPPKRPFKR MNYSDAIIWL KEHDIKKEDG
TFYEFGEDIP EAPERLMTDT INEPILLCRF PVEIKSFYMQ RCPEDSCLTE SVDVLMPNVG
EIVGGSMRTS DAEEILAGYK REGIDPAPYY WYTDQRKYGT CPHGGYGLGL ERFLTWILNR
YHIRDVCLYP RFVQRCTP
//
