SYQ_SHISS
ID SYQ_SHISS Reviewed; 554 AA.
AC Q3Z4C0;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=SSON_0634;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ87392.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3Z4C0; -.
DR SMR; Q3Z4C0; -.
DR EnsemblBacteria; AAZ87392; AAZ87392; SSON_0634.
DR KEGG; ssn:SSON_0634; -.
DR HOGENOM; CLU_001882_2_3_6; -.
DR OMA; INNFCAQ; -.
DR Proteomes; UP000002529; 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.
FT CHAIN 1..554
FT /note="Glutamine--tRNA ligase"
FT /id="PRO_0000242877"
FT REGION 317..324
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT MOTIF 34..44
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT MOTIF 268..272
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 35..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 41..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 67
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 212
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 261..262
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT BINDING 269..271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
SQ SEQUENCE 554 AA; 63478 MW; E720164EF990F335 CRC64;
MSEAEARPTN FIRQIIDEDL ASGKHTTVHT RFPPEPNGYL HIGHAKSICL NFGIAQDYKG
QCNLRFDDTN PVKEDIEYVE SIKNDVEWLG FHWSGNVRYS SDYFDQLHAY AIELINKGLA
YVDELTPEQI REYRGTLTQP GKNSPYRDRS VEENLALFEK MRAGGFEEGK ACLRAKIDMA
SPFIVMRDPV LYRIKFAEHH QTGNKWCIYP MYDFTHCISD ALEGITHSLC TLEFQDNRRL
YDWVLDNITI PVHPRQYEFS RLNLEYTVMS KRKLNLLVTD KHVEGWDDPR MPTISGLRRR
GYTAASIREF CKRIGVTKQD NTIEMASLES CIREDLNENA PRAMAVIDPV KLVIENYQGE
GEMVTMPNHP NKPEMGSRQV PFSGEIWIDR ADFREEANKQ YKRLVLGKEV RLRNAYVIKA
ERVEKDAEGN ITTIFCTYDA DTLSKDPADG RKVKGVIHWV SAAHALPVEI RLYDRLFSVP
NPGAADDFLS VINPESLVIK QGFAEPSLKD AVAGKAFQFE REGYFCLDSR HSTAEKPVFN
RTVGLRDTWA KVGE
