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Database: UniProt
Entry: G2HEW3_PANTR
LinkDB: G2HEW3_PANTR
Original site: G2HEW3_PANTR 
ID   G2HEW3_PANTR            Unreviewed;       548 AA.
AC   G2HEW3; A0A2J8NDL6; A0A8I3B1Q1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 76.
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|EMBL:JAA07604.1};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|EMBL:JAA07604.1};
RN   [1] {ECO:0000313|EMBL:BAK62271.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Testis {ECO:0000313|EMBL:BAK62271.1};
RX   PubMed=21484476; DOI=10.1007/s10142-011-0220-9;
RA   Kim R.N., Kim D.W., Choi S.H., Chae S.H., Nam S.H., Kim D.W., Kim A.,
RA   Kang A., Park K.H., Lee Y.S., Hirai M., Suzuki Y., Sugano S., Hashimoto K.,
RA   Kim D.S., Park H.S.;
RT   "Major chimpanzee-specific structural changes in sperm development-
RT   associated genes.";
RL   Funct. Integr. Genomics 11:507-517(2011).
RN   [2] {ECO:0000313|EMBL:JAA07604.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA07604.1}, Skeletal muscle
RC   {ECO:0000313|EMBL:JAA35013.1}, Skin {ECO:0000313|EMBL:JAA31458.1}, and
RC   Smooth vascular {ECO:0000313|EMBL:JAA20519.1};
RA   Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT   "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT   mRNA sequences.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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; AK305277; BAK62271.1; -; mRNA.
DR   EMBL; GABC01003734; JAA07604.1; -; mRNA.
DR   EMBL; GABF01001626; JAA20519.1; -; mRNA.
DR   EMBL; GABD01001642; JAA31458.1; -; mRNA.
DR   EMBL; GABD01001641; JAA31459.1; -; mRNA.
DR   EMBL; GABE01009726; JAA35013.1; -; mRNA.
DR   RefSeq; NP_001233302.1; NM_001246373.1.
DR   AlphaFoldDB; G2HEW3; -.
DR   STRING; 9598.ENSPTRP00000017072; -.
DR   GeneID; 455438; -.
DR   KEGG; ptr:455438; -.
DR   CTD; 4677; -.
DR   eggNOG; KOG0555; Eukaryota.
DR   HOGENOM; CLU_004553_2_10_1; -.
DR   OrthoDB; 347413at2759; -.
DR   TreeFam; TF105664; -.
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   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000313|EMBL:JAA07604.1}; 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          249..540
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          69..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   548 AA;  62999 MW;  EFFC854F6166D4B4 CRC64;
     MVLAELYVSD REGSDATGDG TKEKPFKTGL KALMTVGKEP FPTIYVDSQK ENERWNVISK
     SQLKNIKKMW HREQMKNESR EKKEAEDSLR REKNLEEAKK ITIKNDPSLP EPKCVKISAL
     EGYRGQRVKV FGWVHRLRRQ GKNLMFLVLR DGTGYLQCVL ADELCQCYNG VLLSTESSVA
     VYGMLNLTPK GKQAPGGHEL SCDFWELIGL APAGGADNLI NEESDVDVQL NNRHMMIRGE
     NMSKILKARS MVTRCFRDHF FDRGYYEVTP PTLVQTQVEG GATLFKLDYF GEEAFLTQSS
     QLYLETCLPA LGDVFCIAQS YRAEQSRTRR HLAEYTHVEA ECPFLTFDDL LNRLEDLVCD
     VVDRILKSPA GSIVHELNPN FQPPKRPFKR MNYSDAIVWL KEHDVKKEDG TFYEFGEDIP
     EAPERLMTDT INEPILLCRF PVEIKSFYMQ RCPEDSRLTE SVDVLMPNVG EIVGGSMRIF
     NSEEILAGYK REGIDPTPYY WYTDQRKYGT CPHGGYGLGL ERFLTWILNR YHIRDVCLYP
     RFVQRCTP
//
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