SYDC2_DICDI
ID SYDC2_DICDI Reviewed; 569 AA.
AC Q559M9; Q75JQ2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Aspartate--tRNA ligase, cytoplasmic 2;
DE EC=6.1.1.12;
DE AltName: Full=Aspartyl-tRNA synthetase 2;
DE Short=AspRS 2;
GN Name=aspS2; ORFNames=DDB_G0272304;
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
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: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 2 subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000008; EAL71304.1; -; Genomic_DNA.
DR RefSeq; XP_645305.1; XM_640213.1.
DR AlphaFoldDB; Q559M9; -.
DR SMR; Q559M9; -.
DR STRING; 44689.DDB0231309; -.
DR PaxDb; Q559M9; -.
DR EnsemblProtists; EAL71304; EAL71304; DDB_G0272304.
DR GeneID; 8618471; -.
DR KEGG; ddi:DDB_G0272304; -.
DR dictyBase; DDB_G0272304; aspS2.
DR eggNOG; KOG0556; Eukaryota.
DR HOGENOM; CLU_004553_2_1_1; -.
DR InParanoid; Q559M9; -.
DR OMA; TSLDFEM; -.
DR PhylomeDB; Q559M9; -.
DR PRO; PR:Q559M9; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:dictyBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_02075; Asp_tRNA_synth_type2; 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; IPR004523; Asp-tRNA_synthase_2.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR43450; PTHR43450; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..569
FT /note="Aspartate--tRNA ligase, cytoplasmic 2"
FT /id="PRO_0000327968"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..295
FT /note="Aspartate"
FT /evidence="ECO:0000250"
FT BINDING 314..316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 322..324
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 475
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 479
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 540..543
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 569 AA; 67218 MW; FB20FE145096432F CRC64;
MSEENNHKEK SKNEIKKEKK KIEKEKKITE LKSKKKINEK NNTINYDDDD DNDDDNFKNK
KWGEINNENY KEIIKNRFVK EWSNISDLNE SCVGKYVLIR ARVSNIRSFG NSLCFLQLRD
GLSSIQAVIS KNDENNSKSM IHFINSTITK ESIIDIEAIL TNSSTPIESC IIKNLELKIY
SLFLQSKSNS SLPLQFDDLS KPTTYQNYDD NGYTYVIPLN SRLNNRCLDL RTFYNLSIFK
IQSAISNLFR DQLLINDFIE IHSPKIIKQS INENSFKLNY FNEIAYLSES TQFYRQLAIV
SDFKRVFEIG PVYRTDLGHT HRHLNEFTSL DFEMTFKDHY HEVLDFLDNL MISIFKILET
NYENELKIIN NYQLQFEKFK FSTKTPRFTF SEVKLMLIEF SENENNKFCM ELFDYLNVQE
ERIFGKIVKE KFNVDYYIIE KPSSEYQPFY IMPDSNNEKL LNSFHIYING EKIGSGSQRI
HDWKLLEKRY KNYYINHNNN NNNNNNNNNN NNNNNNNNNI ENYINIFKFG CSQHAGCSIG
LERLVMAYLG LENIRKASFC PRDPTRLTP
