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Reviewed, UniProtKB/Swiss-Prot A7MQT2 (SYQ_ENTS8)

Last modified February 9, 2010. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutaminyl-tRNA synthetase
    EC=6.1.1.18
Alternative name(s):
    Glutamine--tRNA ligase
      Short name=GlnRS
Gene names
Name: glnS
Ordered Locus Names: ESA_02658
OrganismEnterobacter sakazakii (strain ATCC BAA-894) [Complete proteome] [HAMAP]
Taxonomic identifier290339 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCronobacter

Protein attributes

Sequence length555 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

Subunit structure

Monomer By similarity. HAMAP MF_00126

Subcellular location

Cytoplasm HAMAP 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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

glutamine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 555555Glutaminyl-tRNA synthetase HAMAP MF_00126
PRO_1000016296

Regions

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

Sites

Binding site2711ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A7MQT2-1 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: 5155349AA1AA2D16

FASTA55563,639
        10         20         30         40         50         60 
MSEAEARPTN FIRQIIDEDL ASGKHTTICT RFPPEPNGYL HIGHAKSICL NFGIAQDYHG 

        70         80         90        100        110        120 
QCNLRFDDTN PVKEDLEFVE SIKNDVQWLG FHWSGDVRYS SDYFDQLYNY AVELINKGLA 

       130        140        150        160        170        180 
YVDELSPEQI REYRGTLTAP GKNSPFRDRS 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 NTVEMAALEA CIREDLNENA PRAMAVIDPV KLVIENYPQG 

       370        380        390        400        410        420 
HSEMVSMPNH PNKPEMGNRD VPFSGEIWID RADFREEANK QYKRLVLGKE VRLRNAYVIK 

       430        440        450        460        470        480 
AERVEKDDAG EITTIYCTYD AETLSKDPAD GRKVKGVIHW VSAAHALPVE IRLYDRLFSV 

       490        500        510        520        530        540 
PNPGAAEDFL TTINKDSLVI KQGYAEPGLK NAEAGKAWQF EREGYFCLDS RHANGDKLVF 

       550 
NRTVGLRDTW AKIGE 

« Hide

References

[1]McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Fulton B., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000783 Genomic DNA. Translation: ABU77898.1.
RefSeqYP_001438733.1.

3D structure databases

SMRA7MQT2. Positions 9-549.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7MQT2.

Genome annotation databases

GeneID5550573.
GenomeReviewsGene locus ESA_02658 in contig CP000783_GR.
KEGGesa:ESA_02658.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG334108.
OMARMPTIAG.

Family and domain databases

HAMAPMF_00126. Gln_tRNA_synth.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR004514. Gln-tRNA-synth_Ic.
IPR000924. Glu/Gln-tRNA-synth_Ic.
IPR020061. Glu/Gln-tRNA-synth_Ic_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ic_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ic_codon-bd.
IPR020060. Glu/Gln-tRNA-synth_Ic_N.
IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
[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. 1 hit.
PANTHERPTHR10119:SF3. GlnS. 1 hit.
PTHR10119. Glu_tRNA-synt_1c. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
TIGRFAMsTIGR00440. glnS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYQ_ENTS8
AccessionPrimary (citable) accession number: A7MQT2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 2, 2007
Last modified: February 9, 2010
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents