SYDM_DICDI
ID SYDM_DICDI Reviewed; 692 AA.
AC Q55C99;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Aspartate--tRNA ligase, mitochondrial;
DE EC=6.1.1.12;
DE AltName: Full=Aspartyl-tRNA synthetase;
DE Short=AspRS;
DE Flags: Precursor;
GN Name=maspS; ORFNames=DDB_G0270152;
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-aspartate + tRNA(Asp) = AMP + diphosphate + L-
CC aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660,
CC Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC ChEBI:CHEBI:456215; EC=6.1.1.12;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 1 subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72426.1; -; Genomic_DNA.
DR RefSeq; XP_646582.1; XM_641490.1.
DR AlphaFoldDB; Q55C99; -.
DR SMR; Q55C99; -.
DR STRING; 44689.DDB0231311; -.
DR PaxDb; Q55C99; -.
DR EnsemblProtists; EAL72426; EAL72426; DDB_G0270152.
DR GeneID; 8617552; -.
DR KEGG; ddi:DDB_G0270152; -.
DR dictyBase; DDB_G0270152; maspS.
DR eggNOG; KOG2411; Eukaryota.
DR HOGENOM; CLU_014330_3_2_1; -.
DR InParanoid; Q55C99; -.
DR OMA; YQLDVEM; -.
DR PhylomeDB; Q55C99; -.
DR PRO; PR:Q55C99; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; ISS:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; ISS:dictyBase.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1360.30; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00044; Asp_tRNA_synth_type1; 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; IPR004524; Asp-tRNA-ligase_1.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR004115; GAD-like_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR PANTHER; PTHR22594:SF5; PTHR22594:SF5; 1.
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; SSF55261; SSF55261; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00459; aspS_bact; 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..61
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 62..692
FT /note="Aspartate--tRNA ligase, mitochondrial"
FT /id="PRO_0000327861"
FT REGION 287..290
FT /note="Aspartate"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 309..311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 590
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 597
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 642..645
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 692 AA; 79277 MW; 0028309770FF7FD1 CRC64;
MNRVILKDSK IFLNVLNKPI IKNKNCLSLL NITTSSTTSI IKNQQINQFN KRNFTNTINN
NKNENINNKI LNIIERSHSC GEITSKDIGK EVIIYGWINS LRNLGDNVFL VIRDGHGKVQ
CYVDLKQQCI LKSSVPNIDI NERNSIEENI KLFKLESIVS IKGKVIARPE RMVNKNMSTG
EIEISVDQLQ LLNNCVDLPF TVEHDSTAVS EELRLKYRYV DLRRDKVQSN IRLRSKVAMA
ARNYLINQQF IEVETPTLFR PTPEGAREYL VPTRHQGQFY SLPQSPQQYK QLLMVGGIDR
YFQLARCYRD EDLRSDRQPE FTQIDMELSF VNTQMIYRII EGLVKTLWKE AGFNIDYEFP
FYTYEQVLST YGIDKPDTRY DMKLVDITDC FNKDETNINL FKNALSQASN NFKESKPVIK
CIKLDQVLPT LKSKHLDQIT TESNSIITVQ IKSNNEWKSL ISKSISEQEK TLITERMNLK
EGDVLLISVG PRFQVESTLG KTRIYCANLL KELNLLKLDP QQFNFLWVVD FPLFTPSDYM
NEQSALLSTH HPFTAPHPED IDLLLNPLST PSDYSKIRGQ HYDIVINGVE LGGGSIRIHN
SDVQLRVLEK VLKLEPHMVQ RFNHLLTALS MGCPPHGGIA LGFDRLCSLL VNSNSIRDVI
AFPKTSGGKE LMTSSPATVT KSELDELFLI QK
