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Database: UniProt
Entry: M3WDZ9_FELCA
LinkDB: M3WDZ9_FELCA
Original site: M3WDZ9_FELCA 
ID   M3WDZ9_FELCA            Unreviewed;       613 AA.
AC   M3WDZ9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 4.
DT   27-MAR-2024, entry version 69.
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:ENSFCAP00000010053.6,
GN   ECO:0000313|VGNC:VGNC:68416};
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000010053.6, ECO:0000313|Proteomes:UP000011712};
RN   [1] {ECO:0000313|Ensembl:ENSFCAP00000010053.6, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000010053.6,
RC   ECO:0000313|Proteomes:UP000011712};
RX   PubMed=17975172; DOI=10.1101/gr.6380007;
RA   Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA   Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA   Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA   Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA   Tesler G., O'Brien S.J.;
RT   "Initial sequence and comparative analysis of the cat genome.";
RL   Genome Res. 17:1675-1689(2007).
RN   [2] {ECO:0000313|Ensembl:ENSFCAP00000010053.6, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000010053.6,
RC   ECO:0000313|Proteomes:UP000011712};
RA   Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT   "Sequence assembly of the Felis catus genome version 6.2.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSFCAP00000010053.6}
RP   IDENTIFICATION.
RC   STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000010053.6};
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   EMBL; AANG04003548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; M3WDZ9; -.
DR   STRING; 9685.ENSFCAP00000010053; -.
DR   PaxDb; 9685-ENSFCAP00000010053; -.
DR   Ensembl; ENSFCAT00000010824.6; ENSFCAP00000010053.6; ENSFCAG00000010822.6.
DR   VGNC; VGNC:68416; NARS1.
DR   eggNOG; KOG0555; Eukaryota.
DR   GeneTree; ENSGT01030000234618; -.
DR   HOGENOM; CLU_004553_2_10_1; -.
DR   InParanoid; M3WDZ9; -.
DR   OMA; DCCLYPR; -.
DR   Proteomes; UP000011712; Chromosome D3.
DR   Bgee; ENSFCAG00000010822; Expressed in prefrontal cortex and 9 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0031728; F:CCR3 chemokine receptor binding; IEA:Ensembl.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:Ensembl.
DR   GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR   GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
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:UP000011712}.
FT   DOMAIN          287..576
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          108..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          582..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..613
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   613 AA;  69428 MW;  704E961BD3524083 CRC64;
     MCVVLMQRPS RGILRCTLGS QGGSALQAMS LEVTGPTAGM VLELYVSDRE GNDATGDGTK
     EKPFKTGLKA LMTVGKEPFP TIYIDSQKEN ERWDVISKSQ MKNIKKMWHR EQMKSESREK
     KEAEDNLRRE KNLEEAKKIT IKNDPSLPEP KCVKIHALEG YRGQRVKVFG WVHRLRRQGK
     NLMFLVLRDG TGYLQCVLSD DLCQCYNGVV LATESSVAVC GMLNLTPKGK QAPGGHELSC
     DFWELIGLAP AGGADNLINE ESDVDVQLNN RHMMIRGENM SKILKARSVV TRCFRDHFFD
     RGYYEVTPPT LVQTQVEGGA TLFKLDYFGE EAFLTQSSQL YLETCIPALG DVFCIAQSYR
     AEQSRTRRHL AEYTHVEAEC PFLTFEELLN RLEDLVCDVV DRVLKSPAAS IVRDLNPNFK
     PPKRPFKRMN YSDAIVWLKE HDIKKEDGTF YEFGEDIPEA PERLMTDTIN EPILLCRFPV
     EIKSFYMQRC PEDSRLTESV DVLMPNVGEI VGGSMRIWDS EEMLAGYKRE GIDPTPYYWY
     TDQRKYGTCP HGGYGLGLER FLTWILNSGA WKLKGPPTME GPVDWSHGGS CHRNSPAYQK
     PRTSSSTGEE VGI
//
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