(data stored in ACNUC7421 zone)

SWISSPROT: SYQ_ECO57

ID   SYQ_ECO57               Reviewed;         554 AA.
AC   Q8X9H8;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   30-AUG-2017, entry version 105.
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};
GN   OrderedLocusNames=Z0827, ECs0710;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamine + tRNA(Gln) = AMP +
CC       diphosphate + L-glutaminyl-tRNA(Gln). {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
CC       family. {ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000305}.
DR   EMBL; AE005174; AAG55002.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34133.1; -; Genomic_DNA.
DR   PIR; F85567; F85567.
DR   PIR; F90717; F90717.
DR   RefSeq; NP_308737.1; NC_002695.1.
DR   RefSeq; WP_001287136.1; NZ_MWVM01000011.1.
DR   ProteinModelPortal; Q8X9H8; -.
DR   SMR; Q8X9H8; -.
DR   STRING; 155864.Z0827; -.
DR   EnsemblBacteria; AAG55002; AAG55002; Z0827.
DR   EnsemblBacteria; BAB34133; BAB34133; BAB34133.
DR   GeneID; 917079; -.
DR   KEGG; ece:Z0827; -.
DR   KEGG; ecs:ECs0710; -.
DR   PATRIC; fig|386585.9.peg.824; -.
DR   eggNOG; ENOG4105CX6; Bacteria.
DR   eggNOG; COG0008; LUCA.
DR   HOGENOM; HOG000259232; -.
DR   KO; K01886; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 1.10.1160.10; -; 1.
DR   Gene3D; 2.40.240.10; -; 2.
DR   Gene3D; 3.40.50.620; -; 3.
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; IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl.
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_b-brl.
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; Q8X9H8.
DR   SWISS-2DPAGE; Q8X9H8.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    554       Glutamine--tRNA ligase.
FT                                /FTId=PRO_0000195835.
FT   NP_BIND      35     37       ATP. {ECO:0000255|HAMAP-Rule:MF_00126}.
FT   NP_BIND      41     47       ATP. {ECO:0000255|HAMAP-Rule:MF_00126}.
FT   NP_BIND     261    262       ATP. {ECO:0000255|HAMAP-Rule:MF_00126}.
FT   NP_BIND     269    271       ATP. {ECO:0000255|HAMAP-Rule:MF_00126}.
FT   REGION      317    324       Interaction with tRNA.
FT                                {ECO:0000255|HAMAP-Rule:MF_00126}.
FT   MOTIF        34     44       "HIGH" region. {ECO:0000255|HAMAP-
FT                                Rule:MF_00126}.
FT   MOTIF       268    272       "KMSKS" region. {ECO:0000255|HAMAP-
FT                                Rule:MF_00126}.
FT   BINDING      67     67       L-glutamine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00126}.
FT   BINDING     212    212       L-glutamine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00126}.
FT   BINDING     231    231       ATP. {ECO:0000255|HAMAP-Rule:MF_00126}.
SQ   SEQUENCE   554 AA;  63510 MW;  A484939DB8B4EC67 CRC64;
     MSEAEARPTN FIRQIIDEDL ASGKHTTVHT RFPPEPNGYL HIGHAKSICL NFGIAQDYKG
     QCNLRFDDTN PVKEDIEYVD SIKNDVEWLG FHWSGNVRYS SDYFDQLHAY AIELINKGLA
     YVDELTPEQI REYRGTLTQP GKNSPYRDRS VEENLALFEK MRTGGFEEGK ACLRAKIDMA
     SPFIVMRDPV LYRIKFAEHH QTGNKWCIYP MYDFTHCISD ALEGITHSLC TLEFQDNRRL
     YDWVLDNITI PVHPRQYEFS RLNLEYTVMS KRKLNLLVTD KHVEGWDDPR MPTISGLRRR
     GYTAASIREF CKRIGVTKQD NTIEMASLES CIREDLNENA PRAMAVIDPV KLVIENYQGE
     GEMVTMPNHP NKPEMGSRQV PFSGEIWIDR SDFREEANKQ YKRLVLGKEV RLRNAYVIKA
     ERVEKDAEGN ITTIFCTYDA DTLSKDPADG RKVKGVIHWV SAAHALPVEI RLYDRLFSVP
     NPGAADDFLS VINPESLVIK QGFAEPSLKD AVAGKAFQFE REGYFCLDSR HSTAEKPVFN
     RTVGLRDTWA KVGE
//

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