ID   SYQ_NOSCE               Reviewed;         695 AA.
AC   C4V819;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 56.
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   ORFNames=NCER_100619;
OS   Nosema ceranae (strain BRL01) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae; Nosema.
OX   NCBI_TaxID=578460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRL01;
RX   PubMed=19503607; DOI=10.1371/journal.ppat.1000466;
RA   Cornman R.S., Chen Y.P., Schatz M.C., Street C., Zhao Y., Desany B.,
RA   Egholm M., Hutchison S., Pettis J.S., Lipkin W.I., Evans J.D.;
RT   "Genomic analyses of the microsporidian Nosema ceranae, an emergent
RT   pathogen of honey bees.";
RL   PLoS Pathog. 5:E1000466-E1000466(2009).
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; ACOL01000036; EEQ82641.1; -; Genomic_DNA.
DR   RefSeq; XP_002996312.1; XM_002996266.1.
DR   AlphaFoldDB; C4V819; -.
DR   SMR; C4V819; -.
DR   STRING; 578460.C4V819; -.
DR   EnsemblFungi; EEQ82641; EEQ82641; NCER_100619.
DR   KEGG; nce:NCER_100619; -.
DR   VEuPathDB; MicrosporidiaDB:NCER_100619; -.
DR   HOGENOM; CLU_001882_2_3_1; -.
DR   InParanoid; C4V819; -.
DR   OMA; FAWRIMG; -.
DR   Proteomes; UP000009082; Unassembled WGS sequence.
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..695
FT                   /note="Probable glutamine--tRNA ligase"
FT                   /id="PRO_0000388383"
FT   MOTIF           201..211
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000250"
FT   MOTIF           446..450
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000250"
FT   BINDING         202..204
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         208..214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         234
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         391
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         410
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         439..440
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
FT   BINDING         447..449
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P00962"
SQ   SEQUENCE   695 AA;  81524 MW;  B37230F4F506F579 CRC64;
     MFDVESLLKK LNVSEDKKEN ILQKEQLKKN LETLYTNFDT DNKLLFTLAC TAPKKIDILI
     FGILINENVI KNDATLRASM KFAIKNTDVT YEELKDFILK NTKSKEEVSE IINKACLSGK
     SKKEVYIILK NKLPFEDSKY LMDEVNKFEI DTSKSKKVKD WLEEGEVSML HKPGDNPQLN
     EKILKDHLER TGGKVVTRFP PEPNGILHIG HAKAINLDFG YAEKYNGICY LRFDDTNPRN
     EEDYYFESII EDVKWLGFEP YAITSSSKYF GDMCELAEKL ILKDKAYICE LSNEELKKRR
     RMLSEAFETD KDKSIEELGL ILSPYRNREI SENLKIFREM VEKKHKEGDY TLRFKMDIRS
     KNPMMFDLVG MRIIDCDHVV TKDKYNLYPS YEFALCVSDS LEDVTHSFCT REFFTRQESY
     KWLLDALEIY KPVQWEFSRL NISNTVLSKR KIVPLKKYGI ELDDPRLYTI KGMRRRGIPP
     QAINNFVKSL GITYAETIID NKKFESFIRD ELNKTTQRVM CVMDPLKIYI RNAKEQEISI
     PNSNQKIIFK PYIYIEKSDF KMEDDDKDFL RFTPNQSVGL YMFGAIKFIK FDNDMIIAEL
     TNETPKKFIH WVSCDSIKVT IRLYDPLFRS FNPEEGNYLD NINLDSLKTV VGYCDDRIKG
     CEVEDKFQFQ RVGYFCVDPD TTPENIVFNR IITLI