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SYQ_CLOD6
ID   SYQ_CLOD6               Reviewed;         554 AA.
AC   Q188C8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Glutamine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00126};
DE            EC=6.1.1.18 {ECO:0000255|HAMAP-Rule:MF_00126};
DE   AltName: Full=Glutaminyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00126};
DE            Short=GlnRS {ECO:0000255|HAMAP-Rule:MF_00126};
GN   Name=glnS {ECO:0000255|HAMAP-Rule:MF_00126}; OrderedLocusNames=CD630_20590;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00126};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00126}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00126}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00126}.
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DR   EMBL; AM180355; CAJ68944.1; -; Genomic_DNA.
DR   RefSeq; WP_003428989.1; NZ_CP010905.2.
DR   RefSeq; YP_001088573.1; NC_009089.1.
DR   AlphaFoldDB; Q188C8; -.
DR   SMR; Q188C8; -.
DR   STRING; 272563.CD630_20590; -.
DR   EnsemblBacteria; CAJ68944; CAJ68944; CD630_20590.
DR   KEGG; cdf:CD630_20590; -.
DR   KEGG; pdc:CDIF630_02282; -.
DR   PATRIC; fig|272563.120.peg.2173; -.
DR   eggNOG; COG0008; Bacteria.
DR   OMA; INNFCAQ; -.
DR   PhylomeDB; Q188C8; -.
DR   BioCyc; PDIF272563:G12WB-2210-MON; -.
DR   Proteomes; UP000001978; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004819; F:glutamine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1160.10; -; 1.
DR   Gene3D; 2.40.240.10; -; 2.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00126; Gln_tRNA_synth; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR004514; Gln-tRNA-synth.
DR   InterPro; IPR022861; Gln_tRNA_ligase_bac.
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_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; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..554
FT                   /note="Glutamine--tRNA ligase"
FT                   /id="PRO_1000095482"
FT   MOTIF           33..43
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   MOTIF           266..270
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         34..36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         40..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         66
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         210
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         229
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         259..260
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         267..269
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
SQ   SEQUENCE   554 AA;  64281 MW;  E9AB923D5FAE0B4D CRC64;
     MSNETNSSNF IKNIIINDLE TGKHDSIITR FPPEPNGYLH IGHAKSICLN FGLAKEFNGK
     ANLRFDDTNP LKEDVEYVES IKEDVKWLGF DWNELNFASN YFDEMYKRAL ILIKKGKAYV
     CDLTQEEMRE YRGTLTEPGK ESPHRNRTIE ENLDLFERMK NGEFKDGEKT LRAKIDMSSP
     NINLRDPIIY RISHSTHHNT GDKWCIYPMY AFAHPIEDAI EGITHSICTL EFEDQRPLYD
     WFVKECEMEN IPRQIEFARL NINNTVMSKR KLKQLVDEGI VDGWDDPRVP TISGIRRKGY
     TAEALRNFCS EIGVSKVNST VDSQMLDYFL RENLQPKAPL TMGVLRPLKL IITNYPEDKI
     EMLEIENNAK DESQGKRLVP FSRELYIEQD DFMEEPVKKY FRFFPGNEVR LKGAYFVKCT
     DVIKDENGNV VEIHGTYDPE TKSGSGFTGR KVKSTIHWVD AKSAIPCEFR LFEPLILDDI
     PENEGKHFLE QINPNSLEIL QGFVEPTQIK DAKPFDKFQF VRNGFFSIDN KYTTDEKFVF
     NRIVPLKSSF KPGK
 
 
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