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Database: UniProt
Entry: F6TBY0_XENTR
LinkDB: F6TBY0_XENTR
Original site: F6TBY0_XENTR 
ID   F6TBY0_XENTR            Unreviewed;       548 AA.
AC   F6TBY0;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 4.
DT   27-MAR-2024, entry version 66.
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:ENSXETP00000045103};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000045103};
RN   [1] {ECO:0000313|Ensembl:ENSXETP00000045103}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000045103};
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA   Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA   Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA   Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA   Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA   Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA   Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA   Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
RN   [2] {ECO:0000313|Ensembl:ENSXETP00000045103}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUN-2011) 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   AlphaFoldDB; F6TBY0; -.
DR   Ensembl; ENSXETT00000045103; ENSXETP00000045103; ENSXETG00000027170.
DR   AGR; Xenbase:XB-GENE-965615; -.
DR   Xenbase; XB-GENE-965615; nars1.
DR   eggNOG; KOG0555; Eukaryota.
DR   HOGENOM; CLU_004553_2_10_1; -.
DR   TreeFam; TF105664; -.
DR   Bgee; ENSXETG00000027170; Expressed in brain and 14 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   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}.
FT   DOMAIN          246..540
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   COILED          74..101
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   548 AA;  63406 MW;  E7E5B8E004E723F3 CRC64;
     ISLCPLEMYV SDREGNDSTG DGTKEKPFKT ILKAMLAAGK EPFPTFYVDS QKENERWDVI
     SKSQMKNNRK LWVREQMKNE AKEKKEAEDN LRREKNLEEA KKIVITNDPS LPAPLKIRQL
     EAYRGQRVKV FGWVHRLRRQ GKTLMFIVLR DGTGYLQCVL SDQLCQCYNG LVLSTESTVA
     VYGTLNLVPD GKQAPGGHEL ACDYWEIVGL APAGGADNLL NEESDVDVQL NNRHMMIRGE
     NMSKIFKVRS TVIHCFRNHF FDRGYYEITP PTLVQTQVEG GSTLFKLDYF GEEAYLTQSS
     QLYLETCIPA MGDTFCIAQS YRAEQSRTRR HLAEYTHIEA ECPFMTFEDL LNRLEDLVCD
     VVDRVLKSPV ASLLYDLHPE FKPPKRPFRR MNYTEAITWL KEHDVKKDDG TYYEFGEDIP
     EAPERLMTDS INEPILLCRF PAEIKSFYMQ RCAEDKRLTE SVDVLMPNVG EIVGGSMRIW
     DSEELLEGYK REGIDATPYY WYTDQRKYGT CPHGGYGLGL ERFLTWILNR HHIRDVCLYP
     RFVQRCKP
//
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