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Reviewed, UniProtKB/Swiss-Prot A8AJD6 (SYQ_CITK8)

Last modified November 3, 2009. Version 14. 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: CKO_02482
OrganismCitrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) [Complete proteome] [HAMAP]
Taxonomic identifier290338 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacter

Protein attributes

Sequence length555 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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_1000016292

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
A8AJD6-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: CD8754088DCD117D

FASTA55563,629
        10         20         30         40         50         60 
MSEAEARPTN FIRQIIDEDL ASGKHTTIHT RFPPEPNGYL HIGHAKSICL NFGIAQDYQG 

        70         80         90        100        110        120 
LCNLRFDDTN PVKEDIEYVD SIKNDVEWLG FHWAGNVCYS SDYFDQLHAY AVELITKGLA 

       130        140        150        160        170        180 
YVDELTPDQI REYRGTLKEP GKNSPFRDRS VEENLALFEK MRTGGFEEGK 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 KLVIENYPQG 

       370        380        390        400        410        420 
ESEMVTMPNH PNKPEMGSRE VPFSGEIWID RADFREEANK QYKRLVMGKE VRLRNAYVVK 

       430        440        450        460        470        480 
AERVEKDAEG NITTIFCTYD ADTLSKDPAD GRKVKGVIHW VSAAHALPVE IRLYDRLFSV 

       490        500        510        520        530        540 
PNPGAAEDFL SVINPESLVI KQGYAEPSLQ NAVAGKAYQF EREGYFCLDS RYTTADKRVF 

       550 
NRTVGLRDTW AKAGE 

« Hide

References

[1]McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R.
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000822 Genomic DNA. Translation: ABV13599.1.
RefSeqYP_001454035.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA8AJD6.

Genome annotation databases

GeneID5582767.
GenomeReviewsGene locus CKO_02482 in contig CP000822_GR.
KEGGcko:CKO_02482.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMARMPTIAG.

Family and domain databases

HAMAPMF_00126.
[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.
[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_CITK8
AccessionPrimary (citable) accession number: A8AJD6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 23, 2007
Last modified: November 3, 2009
This is version 14 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