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C8TKJ0 (C8TKJ0_ECO26) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutamine--tRNA ligase HAMAP MF_00126
EC=6.1.1.18 HAMAP MF_00126
Alternative name(s):
Glutaminyl-tRNA synthetase HAMAP MF_00126
Gene names
Name:glnS HAMAP MF_00126 EMBL BAI24071.1
Ordered Locus Names:ECO26_0744
OrganismEscherichia coli O26:H11 (strain 11368 / EHEC) [Complete proteome] [HAMAP]
Taxonomic identifier573235 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length554 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln). HAMAP MF_00126 SAAS SAAS020059

Subunit structure

Monomer By similarity. HAMAP MF_00126 SAAS SAAS020059

Subcellular location

Cytoplasm By similarity HAMAP MF_00126.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. HAMAP MF_00126 RuleBase RU003489

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Motif34 – 4411"HIGH" region By similarity HAMAP MF_00126
Motif268 – 2725"KMSKS" region By similarity HAMAP MF_00126

Sites

Binding site2711ATP By similarity HAMAP MF_00126

Sequences

Sequence LengthMass (Da)Tools
C8TKJ0 [UniParc].

Last modified November 3, 2009. Version 1.
Checksum: E720164EF990F335

FASTA55463,478
        10         20         30         40         50         60 
MSEAEARPTN FIRQIIDEDL ASGKHTTVHT RFPPEPNGYL HIGHAKSICL NFGIAQDYKG 

        70         80         90        100        110        120 
QCNLRFDDTN PVKEDIEYVE SIKNDVEWLG FHWSGNVRYS SDYFDQLHAY AIELINKGLA 

       130        140        150        160        170        180 
YVDELTPEQI REYRGTLTQP GKNSPYRDRS VEENLALFEK MRAGGFEEGK ACLRAKIDMA 

       190        200        210        220        230        240 
SPFIVMRDPV LYRIKFAEHH QTGNKWCIYP MYDFTHCISD ALEGITHSLC TLEFQDNRRL 

       250        260        270        280        290        300 
YDWVLDNITI PVHPRQYEFS RLNLEYTVMS KRKLNLLVTD KHVEGWDDPR MPTISGLRRR 

       310        320        330        340        350        360 
GYTAASIREF CKRIGVTKQD NTIEMASLES CIREDLNENA PRAMAVIDPV KLVIENYQGE 

       370        380        390        400        410        420 
GEMVTMPNHP NKPEMGSRQV PFSGEIWIDR ADFREEANKQ YKRLVLGKEV RLRNAYVIKA 

       430        440        450        460        470        480 
ERVEKDAEGN ITTIFCTYDA DTLSKDPADG RKVKGVIHWV SAAHALPVEI RLYDRLFSVP 

       490        500        510        520        530        540 
NPGAADDFLS VINPESLVIK QGFAEPSLKD AVAGKAFQFE REGYFCLDSR HSTAEKPVFN 

       550 
RTVGLRDTWA KVGE

« Hide

References

[1]"Comparative genomics reveal the mechanism of the parallel evolution of O157 and non-O157 enterohemorrhagic Escherichia coli."
Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., Hayashi T.
Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009) [PubMed: 19815525] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 11368 EMBL BAI24071.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP010953 Genomic DNA. Translation: BAI24071.1.
RefSeqYP_003227811.1. NC_013361.1.

3D structure databases

ProteinModelPortalC8TKJ0.
SMRC8TKJ0. Positions 9-548.
ModBaseSearch...

Protein-protein interaction databases

STRINGC8TKJ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000175137; EBESCP00000160822; EBESCG00000171806.
GeneID8481928.
GenomeReviewsGene locus ECO26_0744 in contig AP010953_GR.
KEGGeoj:ECO26_0744.
PATRIC18396972. VBIEscCol24965_0758.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000009048.
ProtClustDBPRK05347.

Family and domain databases

HAMAPMF_00126. Gln_tRNA_synth.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR004514. Gln-tRNA-synth_Ib.
IPR022861. Gln_tRNA_synth_bac.
IPR000924. Glu/Gln-tRNA-synth_Ib.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:2.40.240.10. Rbsml_L25/Gln-tRNA_synth_b-brl. 2 hits.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
KOK01886.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF50715. Ribosomal_L25rel. 1 hit.
TIGRFAMsTIGR00440. GlnS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC8TKJ0_ECO26
AccessionPrimary (citable) accession number: C8TKJ0
Entry history
Integrated into UniProtKB/TrEMBL: November 3, 2009
Last sequence update: November 3, 2009
Last modified: January 25, 2012
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info