ID   SYEC_ENCCU              Reviewed;         642 AA.
AC   Q8SSE4;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=Probable glutamate--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.17;
DE   AltName: Full=Glutamyl-tRNA synthetase;
DE            Short=GluRS;
GN   OrderedLocusNames=ECU02_1210;
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-glutamate + tRNA(Glu) = AMP + diphosphate + L-
CC         glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663,
CC         Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC         ChEBI:CHEBI:456215; EC=6.1.1.17;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       Glutamate--tRNA ligase type 2 subfamily. {ECO:0000305}.
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DR   EMBL; AL590442; CAD25150.1; -; Genomic_DNA.
DR   RefSeq; NP_584646.1; NM_001040835.1.
DR   AlphaFoldDB; Q8SSE4; -.
DR   SMR; Q8SSE4; -.
DR   STRING; 284813.Q8SSE4; -.
DR   GeneID; 858636; -.
DR   KEGG; ecu:ECU02_1210; -.
DR   VEuPathDB; MicrosporidiaDB:ECU02_1210; -.
DR   HOGENOM; CLU_001882_1_2_1; -.
DR   InParanoid; Q8SSE4; -.
DR   OMA; ANRYFFV; -.
DR   OrthoDB; 934at2759; -.
DR   Proteomes; UP000000819; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00807; GlnRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR004526; Glu-tRNA-synth_arc/euk.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR   InterPro; IPR020061; Glu_tRNA_lig_a-bdl.
DR   InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N.
DR   InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR049437; tRNA-synt_1c_C2.
DR   NCBIfam; TIGR00463; gltX_arch; 1.
DR   PANTHER; PTHR43097:SF5; GLUTAMATE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   Pfam; PF03950; tRNA-synt_1c_C; 1.
DR   Pfam; PF20974; tRNA-synt_1c_C2; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..642
FT                   /note="Probable glutamate--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000388391"
FT   MOTIF           157..166
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000250"
FT   MOTIF           382..386
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000250"
FT   BINDING         152..154
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         326..330
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         344
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         347
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         382..386
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   642 AA;  73964 MW;  B2BC6D4B2C329BB2 CRC64;
     MDGKSEFKEE LINYILLKKY GKGAQDPPVY SNALKKAPQE MFPPGLVDAL DSYSINLSRS
     EGVEFLVLLN SLVNDIRSEE VKDIIFGMIN TNQMLTKLMK DKKEVERFPD TCKMYSEQFK
     ANKPLLKEFN AGSRKEQGNL EIGEPSENVV TRFPPEPNGR LHIGHARAAL LNWYFASKGN
     GRLLVRFDDT NPEKEEERFE RGILSDLSLL GINEYTLSHT SDYFDKIIDL GVFLIGEGKA
     YADNTPQEVM RDERGRGVES RCRSMDVEES KRIFKEMARG NASGYCLRAK IDMSSSNKAM
     RDPVIFRVNE SPHHRTGDKY KVYPTYDFAC PIVDSLEGIT LSLRANEYRD RNQQYYWFID
     NLRLRNRPKI HDFSRLNFEN TVLSKRKLKY YVDNGFVSGW DDPRLATIAG IKRLGMNMEA
     LREYILMQGV SQKTCTISWD KVWAINRKKI DPVSARYFCV QQRDAVEVSI DNTSEYTMDV
     PKHKKNGDLG TKEVFYSSQI LLSQEDGRVL QDNEEFTLMN WGNAIVKSKT VENGTVTKME
     VSLNPDGDFK LTKNKMSWVS KRGSVTVELA EYGNLMNDED TEDLALRFNR NSVKKEYWYA
     ESAIINVREG EVIQFERNGF YYCDGFLVFN LLPFTKQKRT GN
//