ID   SYDC_ENTBH              Reviewed;         474 AA.
AC   B7XHQ4;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Probable aspartate--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.12;
DE   AltName: Full=Aspartyl-tRNA synthetase;
DE            Short=AspRS;
GN   ORFNames=EBI_21705;
OS   Enterocytozoon bieneusi (strain H348) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC   Enterocytozoon.
OX   NCBI_TaxID=481877;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H348;
RX   PubMed=18060071; DOI=10.1371/journal.pone.0001277;
RA   Corradi N., Akiyoshi D.E., Morrison H.G., Feng X., Weiss L.M., Tzipori S.,
RA   Keeling P.J.;
RT   "Patterns of genome evolution among the microsporidian parasites
RT   Encephalitozoon cuniculi, Antonospora locustae and Enterocytozoon
RT   bieneusi.";
RL   PLoS ONE 2:E1277-E1277(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H348;
RX   PubMed=19132089; DOI=10.1371/journal.ppat.1000261;
RA   Akiyoshi D.E., Morrison H.G., Lei S., Feng X., Zhang Q., Corradi N.,
RA   Mayanja H., Tumwine J.K., Keeling P.J., Weiss L.M., Tzipori S.;
RT   "Genomic survey of the non-cultivatable opportunistic human pathogen,
RT   Enterocytozoon bieneusi.";
RL   PLoS Pathog. 5:E1000261-E1000261(2009).
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; ABGB01000015; EED44551.1; -; Genomic_DNA.
DR   RefSeq; XP_002649532.1; XM_002649486.1.
DR   AlphaFoldDB; B7XHQ4; -.
DR   SMR; B7XHQ4; -.
DR   STRING; 481877.B7XHQ4; -.
DR   EnsemblFungi; EED44551; EED44551; EBI_21705.
DR   VEuPathDB; MicrosporidiaDB:EBI_21705; -.
DR   HOGENOM; CLU_004553_2_1_1; -.
DR   InParanoid; B7XHQ4; -.
DR   Proteomes; UP000001742; Unassembled WGS sequence.
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: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   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   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..474
FT                   /note="Probable aspartate--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000388406"
FT   REGION          225..228
FT                   /note="Aspartate"
FT                   /evidence="ECO:0000250"
FT   BINDING         203
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         247..249
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         255..257
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         397
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         400
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         404
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         445..448
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   474 AA;  55228 MW;  2F9358FCE20032B4 CRC64;
     MTENSELNNK ISTIKLKKLI EIQNLTDNMN GTVIRIRGFI ESITSCSSQI FILLRDRLEK
     VQCIIFKSTN VSSIYEFSRL KKLPLESFIE IEGQVVFAEI PIKRATKQNI EIVISTLNIL
     GPVVSKLPFQ LKDCKIAGKE SDTNTITVGY NLRLDNRFLD FRLPVTQSII KIIDQTMYTF
     RTYLRTHEFI EIKTSKIIQS GSEGGANLFS LNYFNKPAYL AQSPQLYKQL AIIGGLKRVY
     EIGHVYRAEV SNINRYLSEF VGLDIEMEME TTYIDFIHFL HSLFINIFES FKNEMKKELE
     IIRQYYEFVD LKYRSTPIII TYKDAVDMLK SKNIQIDYGC DFSREHERIL GKIIKDKEDI
     DIFTIIDYPS SIRAFYSYID ETTKLTRSYD FIVRGEEILS GAQRENRYDY LKNAVIDKGL
     NPENLKNYLE AFKYGAPPHI GCGIGLERFL KAYFGFDDIR YFSLFPRDPN RIFP