ID   SYQ_ENCCU               Reviewed;         697 AA.
AC   Q8SR10;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Probable glutamine--tRNA ligase;
DE            EC=6.1.1.18 {ECO:0000250|UniProtKB:P47897};
DE   AltName: Full=Glutaminyl-tRNA synthetase;
DE            Short=GlnRS;
GN   OrderedLocusNames=ECU10_1460;
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-glutamine + tRNA(Gln) = AMP + diphosphate + L-
CC         glutaminyl-tRNA(Gln); Xref=Rhea:RHEA:20121, Rhea:RHEA-COMP:9662,
CC         Rhea:RHEA-COMP:9681, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:78442, ChEBI:CHEBI:78521,
CC         ChEBI:CHEBI:456215; EC=6.1.1.18;
CC         Evidence={ECO:0000250|UniProtKB:P47897};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AL590449; CAD25865.1; -; Genomic_DNA.
DR   RefSeq; NP_586261.1; NM_001042094.1.
DR   AlphaFoldDB; Q8SR10; -.
DR   SMR; Q8SR10; -.
DR   STRING; 284813.Q8SR10; -.
DR   GeneID; 859911; -.
DR   KEGG; ecu:ECU10_1460; -.
DR   VEuPathDB; MicrosporidiaDB:ECU10_1460; -.
DR   HOGENOM; CLU_001882_2_3_1; -.
DR   InParanoid; Q8SR10; -.
DR   OMA; FAWRIMG; -.
DR   OrthoDB; 809861at2759; -.
DR   Proteomes; UP000000819; Chromosome X.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004819; F:glutamine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 2.40.240.10; -; 2.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR004514; Gln-tRNA-synth.
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; IPR020056; Rbsml_L25/Gln-tRNA_synth_N.
DR   InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   Pfam; PF03950; tRNA-synt_1c_C; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF50715; SSF50715; 1.
DR   TIGRFAMs; TIGR00440; glnS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..697
FT                   /note="Probable glutamine--tRNA ligase"
FT                   /id="PRO_0000388381"
FT   MOTIF           204..214
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000250"
FT   MOTIF           441..445
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000250"
FT   BINDING         205..207
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         211..217
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         237
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         386
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         405
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         434..435
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         442..444
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
SQ   SEQUENCE   697 AA;  81248 MW;  045C9353A142AE04 CRC64;
     MADLEKILER LGISPEKRCQ VIKKEQVVRN MEKIFLGRDL SNRLLYTLAC IAPKNADLGL
     LADLVDARVI KHESMLKECL RYTEKKDVSM EEMTRFVKRN EVSSEDVRKF VAKMRSDRVA
     KKDMVSKARK AMPCADFRVV VEEINKVPDD VDGGDEKRPL EGGWLEEGEI KKLPKPSEIP
     QINEEIRQAH LRRTGGRVVT RFPPEPNGIL HIGHAKAINL NFEYAKKFGG YTYLRYDDTN
     PKNEEAEYFD SIYEDVRWLG FEPYKVTASS DYFDKMTEFG FQLIRKGKAY VCHLSQDEIC
     ERRRQYVSDG TNDRSHLSQY RDRPVSENLR LFQEMVDGKW EEGKACLRFK MDTDTKNPLM
     LDLVGIRILD VVHPRKNVKY TVYPTYEFAL CVSDSLEDVT HSFCTREFYT RQESYNWLLV
     QLEIYKPIQW EFSRLNISNT VLSKRKLLPL KKYGIELDDP RLFTIKGMRR RGFPPEAINQ
     FCRSLGFTFA ETTVDVKKLE NFVRDNLNRT SRRIMCVKEP LKVTIMNSTP CSISIPDLPG
     SSVVRDVPFT PVIYIEKSDF MEKGDKDFLR LTPEQPVGLY MLYPIRVVKV TPDGIVAERW
     DGVPRKFIHW VSEDSVEVEM RMYSSLWTSF SPKDATYLEE MNKDSLKVFH GLCDKRISDA
     RIEDRFQFQR IGYFCVDKDT TKENIVVNLT IPLKNIA