(data stored in SCRATCH9089 zone)

SWISSPROT: SYQ_PASMU

ID   SYQ_PASMU               Reviewed;         559 AA.
AC   P57847;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   11-DEC-2019, entry version 120.
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=PM0528;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(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; 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, ECO:0000305}.
DR   EMBL; AE004439; AAK02612.1; -; Genomic_DNA.
DR   RefSeq; WP_010906709.1; NC_002663.1.
DR   SMR; P57847; -.
DR   PRIDE; P57847; -.
DR   EnsemblBacteria; AAK02612; AAK02612; PM0528.
DR   KEGG; pmu:PM0528; -.
DR   PATRIC; fig|272843.6.peg.534; -.
DR   eggNOG; ENOG4105CX6; Bacteria.
DR   eggNOG; COG0008; LUCA.
DR   HOGENOM; HOG000259232; -.
DR   KO; K01886; -.
DR   OMA; VTHSICT; -.
DR   BioCyc; PMUL272843:G1FZ8-559-MONOMER; -.
DR   Proteomes; UP000000809; 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;
DR   PRODOM; P57847.
DR   SWISS-2DPAGE; P57847.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..559
FT                   /note="Glutamine--tRNA ligase"
FT                   /id="PRO_0000195841"
FT   NP_BIND         45..47
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   NP_BIND         51..57
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   NP_BIND         272..273
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   MOTIF           44..54
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   MOTIF           279..283
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         77
FT                   /note="L-glutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         222
FT                   /note="L-glutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
FT   BINDING         241
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00126"
SQ   SEQUENCE   559 AA;  64310 MW;  C3DBC90B65F071D1 CRC64;
     MSHPVENVVA AENTEKRPTN FIRQIIDEDL ASGKHTGVQT RFPPEPNGYL HIGHAKSICL
     NFGIAEDYQG LCNLRFDDTN PVKEDVEYVD SIKQDVEWLG FKWEGEPRYA SDYFDQLYGY
     AIELIEKGLA YVDELSPEEM REYRGTLTEP GKNSPYRDRS IEENLALFEK MKNGEIAEGK
     ACLRAKIDMA SPFIVMRDPV IYRIKFATHH QTGDKWCIYP MYDFTHCISD AIERITHSLC
     TLEFQDNRRL YDWVLENISI ARPLPHQYEF SRLNLESTLT SKRKLLQLVN EGIVDGWNDP
     RMPTISGLRR RGYTPASLRE FCRRIGVTKQ DNMVEFSALE ACIREDLNEN APRAMAVINP
     LKIVIENFSG KEMLTAPNHP NRDELGVREL PFTRELYIDQ ADFREEANKQ YKRLVLGKEV
     RLRNAYVIKA ERVEKDAEEN ITTVYCTYDP DTLGKNPADG RKVKGVIQWV SAEDYLPAEF
     RQYGRLFTVA NPGAAEDIHQ VLNPDSLVIK QGVVEKSLAN AQPEKAYQFE REGYYCADSK
     DSRPDHLVFN LTVSLKEGF
//

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