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
//
