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Database: UniProt
Entry: A0A340WRB3_LIPVE
LinkDB: A0A340WRB3_LIPVE
Original site: A0A340WRB3_LIPVE 
ID   A0A340WRB3_LIPVE        Unreviewed;       559 AA.
AC   A0A340WRB3;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=NARS {ECO:0000313|RefSeq:XP_007450167.1};
OS   Lipotes vexillifer (Yangtze river dolphin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Lipotidae; Lipotes.
OX   NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007450167.1};
RN   [1] {ECO:0000313|RefSeq:XP_007450167.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-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_007450167.1; XM_007450105.1.
DR   AlphaFoldDB; A0A340WRB3; -.
DR   STRING; 118797.A0A340WRB3; -.
DR   GeneID; 103080463; -.
DR   KEGG; lve:103080463; -.
DR   CTD; 4677; -.
DR   InParanoid; A0A340WRB3; -.
DR   OrthoDB; 347413at2759; -.
DR   Proteomes; UP000265300; Unplaced.
DR   GO; GO:0031090; C:organelle membrane; IEA:UniProt.
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, ECO:0000313|RefSeq:XP_007450167.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265300}.
FT   DOMAIN          260..551
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   559 AA;  64411 MW;  676CDBECA2CB1C77 CRC64;
     MSLEVTRATA GMVLAELYVS DREGSDATGD GTKEKPFKTG LKALMTVGKE PFPTIYVDSQ
     KENERWDVIS KSQMKNIRKL WHREQMKSES REKKEVEDNL RREKNLEEAK KITIKNDPSL
     PEPNCVKIRE LEGYRGQRVK VFGWVHRLRR QGKNLMFLVL RDGTGYLQCV LSDDLCQCYN
     GVVLSTESSV AVYGMLNLTP KGKQAPGGHE LNCDFWELVG LAPAGGADNL INEESDVDVQ
     LNNRHMMIRG ENMSKILKAR SVVTRCFRDH FFDRGYYEIS PPTLVQTQVE GGATLFKLDY
     FGEEAYLTQS SQLYLETCIP ALGDVFCIAQ SYRAEQSRTR RHLAEYTHVE AECPFLTFEE
     LLNRLEDLVC DVVDRVLKSP AASIVHDLNP NFKPPKRPFK RMNYSDAVMW LKEHNIKKED
     GTFYEFGEDI PEAPERLMTD TINEPILLCR FPVEIKSFYM QRCPEDSRLT ESVDVLMPNV
     GEIVGGSMRI WDNEEILAGY KREGIDPTPY YWYTDQRKYG TCPHGGYGLG LERFLTWILN
     RYHIRDVCLY PRFVQRCKP
//
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