ID   SYNM_DICDI              Reviewed;         460 AA.
AC   Q55FI3;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Probable asparagine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.22;
DE   AltName: Full=Asparaginyl-tRNA synthetase;
DE            Short=AsnRS;
DE   Flags: Precursor;
GN   Name=asnS2; ORFNames=DDB_G0268100;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000003; EAL73503.1; -; Genomic_DNA.
DR   RefSeq; XP_647550.1; XM_642458.1.
DR   AlphaFoldDB; Q55FI3; -.
DR   SMR; Q55FI3; -.
DR   STRING; 44689.DDB0231334; -.
DR   PaxDb; Q55FI3; -.
DR   EnsemblProtists; EAL73503; EAL73503; DDB_G0268100.
DR   GeneID; 8616358; -.
DR   KEGG; ddi:DDB_G0268100; -.
DR   dictyBase; DDB_G0268100; asnS2.
DR   eggNOG; KOG0554; Eukaryota.
DR   HOGENOM; CLU_004553_2_0_1; -.
DR   InParanoid; Q55FI3; -.
DR   OMA; SVPHAGW; -.
DR   PhylomeDB; Q55FI3; -.
DR   PRO; PR:Q55FI3; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.930.10; -; 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   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00457; asnS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..460
FT                   /note="Probable asparagine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000327476"
SQ   SEQUENCE   460 AA;  53166 MW;  D58FDB7FC4200947 CRC64;
     MNNIIKRFYK WPIRINEINK NNKDLIGKEI KVKGWVRNIR NQKSVSFIEL GDGSSIKGLQ
     IVGDKDSFSK LKYGSSIEVN GKLINSLGND KEAIEVQLTE PYKLIGNCPD CYPLQPKNHS
     FEFLRDIAHI RSRGNSIGAL LRVRNKSTQL IHQYFNDNGF INVHTPIITA SDCEGGGEQF
     QIKSSLDTKE SMFFGQPSFL TVSGQLEAEI YACSHSRVYT FGPTFRAEKS NTPRHLSEFW
     MIEPEMAFID LNDNLDIAED FCKYLIRNLL DSCKEDIEFF NKRIDTNLLS RLEKTLSTPF
     IRLEYKDAIQ LLQNNNHPIK WGDDIQREQE KFITTHFGEI PVFVINWPKS IKPFYMRENE
     QTDHSNIMPT VSNMDLLVPT VGELIGGSIR EERYDKLLNT INEMGMDKDQ YSWYLDLRKY
     GTVPHGGFGL GFERFLQFVT GLQNIKDVIP IPRHQNYCKF