ID   SYDC_ENCCU              Reviewed;         473 AA.
AC   Q8SRQ8;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Probable aspartate--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.12;
DE   AltName: Full=Aspartyl-tRNA synthetase;
DE            Short=AspRS;
GN   OrderedLocusNames=ECU06_0790;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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; AL590446; CAD25439.1; -; Genomic_DNA.
DR   RefSeq; NP_585835.1; NM_001041457.1.
DR   AlphaFoldDB; Q8SRQ8; -.
DR   SMR; Q8SRQ8; -.
DR   STRING; 284813.Q8SRQ8; -.
DR   PRIDE; Q8SRQ8; -.
DR   GeneID; 859259; -.
DR   KEGG; ecu:ECU06_0790; -.
DR   VEuPathDB; MicrosporidiaDB:ECU06_0790; -.
DR   HOGENOM; CLU_004553_2_1_1; -.
DR   InParanoid; Q8SRQ8; -.
DR   OMA; WVHEIRD; -.
DR   OrthoDB; 677307at2759; -.
DR   Proteomes; UP000000819; Chromosome VI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-EC.
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; IEA:InterPro.
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   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   PANTHER; PTHR43450; PTHR43450; 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; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00458; aspS_nondisc; 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..473
FT                   /note="Probable aspartate--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000388405"
FT   REGION          224..227
FT                   /note="Aspartate"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         246..248
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         254..256
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         396
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         399
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         403
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         444..447
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   473 AA;  54062 MW;  3A97D2A80BEB0772 CRC64;
     MEERLSKISV DGMREIRDLD GSLDGRCVSV RGFVFKSSCT GKYIFIVLRD GGCTVQCMCE
     KPTDGSGGLT MPEFSSLRKV THESYIEIRG RVVKQGMEIS GCSKKDIEVR ILGFRVLSIA
     DKSLPFAMKD VSATAEEREK NPTLQNVAYH IRLDNRAMDL RAPQTRATFR VVDGVMFFFR
     TYLRQNGFME IKTSKLIGSS SEGGANLFSV DYFKRKAFMA QSPQLYKQMA IVGGFKRVYE
     IGHVYRAEES NINRYLSEFV GLDMEMEICT DYNDVIRFIH SMLVSIFDNL KKEYGEELET
     IRAFHAFEDL KYRRDPVVLT HRECVDLLLN EGVEMGYEDD FNSESEKKLG SVVRRMHGVD
     IFVIKDYPIS TRPFYTYRDE EKGITRSYDF ILRGQEILSG AQRVSIYKDL VKYVEEHGIS
     PSSLGGYLES FKYGAPPHGG CGIGLERLMK AYFGMGDIRC FSLFPRDPNR LYP