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 24-JAN-2024, entry version 116.
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 (Social amoeba).
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.Q55FI3; -.
DR PaxDb; 44689-DDB0231334; -.
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; VPHAGWG; -.
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 CDD; cd00776; AsxRS_core; 1.
DR CDD; cd04318; EcAsnRS_like_N; 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 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 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
//
