ID   A5PJC3_BOVIN            Unreviewed;       477 AA.
AC   A5PJC3; F6QRZ3;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   02-SEP-2026, entry version 110.
DE   RecName: Full=Asparaginyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00013291};
DE            EC=6.1.1.22 {ECO:0000256|ARBA:ARBA00012816};
DE   AltName: Full=Asparagine--tRNA ligase, mitochondrial {ECO:0000256|ARBA:ARBA00080216};
GN   Name=NARS2 {ECO:0000313|EMBL:AAI42046.1, ECO:0000313|VGNC:VGNC:49559};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|EMBL:AAI42046.1};
RN   [1] {ECO:0000313|EMBL:AAI42046.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Crossbred x Angus {ECO:0000313|EMBL:AAI42046.1};
RC   TISSUE=Ileum {ECO:0000313|EMBL:AAI42046.1};
RA   Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA   Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA   Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA   Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA   Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA   Holt R., Jones S.J., Marra M.A.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mitochondrial aminoacyl-tRNA synthetase that catalyzes the
CC       specific attachment of the asparagine amino acid (aa) to the homologous
CC       transfer RNA (tRNA), further participating in protein synthesis. The
CC       reaction occurs in a two steps: asparagine is first activated by ATP to
CC       form Asn-AMP and then transferred to the acceptor end of tRNA(Asn).
CC       {ECO:0000256|ARBA:ARBA00058292}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Asn) + L-asparagine + ATP = L-asparaginyl-tRNA(Asn) + AMP
CC         + diphosphate + H(+); 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:ARBA00047844};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226}.
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DR   EMBL; BC142045; AAI42046.1; -; mRNA.
DR   RefSeq; NP_001092337.1; NM_001098867.2.
DR   AlphaFoldDB; A5PJC3; -.
DR   SMR; A5PJC3; -.
DR   FunCoup; A5PJC3; 1940.
DR   STRING; 9913.ENSBTAP00000048918; -.
DR   PaxDb; 9913-ENSBTAP00000048918; -.
DR   GeneID; 504824; -.
DR   KEGG; bta:504824; -.
DR   CTD; 79731; -.
DR   VEuPathDB; HostDB:ENSBTAG00000039943; -.
DR   VGNC; VGNC:49559; NARS2.
DR   OMA; PEMAFYD; -.
DR   OrthoDB; 1931232at2759; -.
DR   Bgee; ENSBTAG00000039943; Expressed in choroid plexus and 104 other cell types or tissues.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd00776; AsxRS_core; 1.
DR   CDD; cd04318; EcAsnRS_like_N; 1.
DR   FunFam; 2.40.50.140:FF:000310; Probable asparagine--tRNA ligase, mitochondrial; 1.
DR   FunFam; 3.30.930.10:FF:000075; probable asparagine--tRNA ligase, mitochondrial isoform X1; 1.
DR   Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_00534; Asn_tRNA_synth; 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; 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   NCBIfam; NF003037; PRK03932.1; 1.
DR   PANTHER; PTHR22594:SF34; ASPARAGINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 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   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
SQ   SEQUENCE   477 AA;  53953 MW;  82D70E1E03457812 CRC64;
     MFRARCLLRA LRSCSSAPCP RQRPAARVSV RGALGVQSAN GERVKVQGWI RSIRSQKEVL
     FLHVNDGSSL ESLQVVADSS FDSRELAFGS SVEVQGQLVK SPSKKQNVEL KAEKIEVVGS
     CDAKAFPFKY KERHPLEYLR QYPHLRCRTN VLGSVLRVRS EATAAIHSFF KDSGFVHIHT
     PVITSNDCEG AGELFQVEPS SKIKVPEENF FNIPVFLTVS GQLHLEVMSG AFTQVFTFGP
     TFRAENSQSR RHLAEFYMVE AEISFLESLQ DLMQVMESLF KTTAMTVLSN CPKDVELCHK
     FLAPGQKDRL EHMLKNNFLI ISYTEAVEIL KQASQNFTFT PEWGADLHTE HEKYLVKHCG
     DIPVFVINYP LVLKPFYMRD NEDGPQHTVA AVDLLVPGVG ELFGGSLREE RYHLLEQRLA
     RLGLTEAYQW YLDLRRFGSV PHGGFGMGFE RYLQCILGID NIKDVIPFPR FTHSCLL
//