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B1IY48 (SYQ_ECOLC) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamine--tRNA ligase

EC=6.1.1.18
Alternative name(s):
Glutaminyl-tRNA synthetase
Short name=GlnRS
Gene names
Name:glnS
Ordered Locus Names:EcolC_2976
OrganismEscherichia coli (strain ATCC 8739 / DSM 1576 / Crooks) [Complete proteome] [HAMAP]
Taxonomic identifier481805 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

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-Rule MF_00126

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00126

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00126.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglutaminyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

glutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glutamine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 554554Glutamine--tRNA ligase HAMAP-Rule MF_00126
PRO_1000076254

Regions

Motif34 – 4411"HIGH" region HAMAP-Rule MF_00126
Motif268 – 2725"KMSKS" region HAMAP-Rule MF_00126

Sites

Binding site2711ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B1IY48 [UniParc].

Last modified April 29, 2008. 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]"Complete sequence of Escherichia coli C str. ATCC 8739."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Ingram L., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8739 / DSM 1576 / Crooks.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000946 Genomic DNA. Translation: ACA78601.1.
RefSeqYP_001725928.1. NC_010468.1.

3D structure databases

ProteinModelPortalB1IY48.
SMRB1IY48. Positions 9-548.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING481805.EcolC_2976.

Chemistry

BindingDBB1IY48.

Proteomic databases

PRIDEB1IY48.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA78601; ACA78601; EcolC_2976.
GeneID6065680.
KEGGecl:EcolC_2976.
PATRIC18228930. VBIEscCol82905_3176.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000259232.
KOK01886.
OMAVTHSICT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK05347.

Enzyme and pathway databases

BioCycECOL481805:GI3G-3039-MONOMER.

Family and domain databases

Gene3D1.10.1160.10. 1 hit.
2.40.240.10. 2 hits.
3.40.50.620. 2 hits.
HAMAPMF_00126. Gln_tRNA_synth.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR004514. Gln-tRNA-synth.
IPR022861. Gln_tRNA_ligase_bac.
IPR000924. Glu/Gln-tRNA-synth.
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]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF50715. SSF50715. 1 hit.
TIGRFAMsTIGR00440. glnS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYQ_ECOLC
AccessionPrimary (citable) accession number: B1IY48
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 29, 2008
Last modified: March 19, 2014
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries