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Q3IGW8 (SYQ_PSEHT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 69. 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:PSHAa1642
OrganismPseudoalteromonas haloplanktis (strain TAC 125) [Complete proteome] [HAMAP]
Taxonomic identifier326442 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

Protein attributes

Sequence length552 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 – 552552Glutamine--tRNA ligase HAMAP-Rule MF_00126
PRO_1000095501

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
Q3IGW8 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 642BAD8C449B8213

FASTA55263,539
        10         20         30         40         50         60 
MAEIENRPSN FIRTRIDQDL ASGKHASTHT RFPPEPNGFL HIGHAKSICL NFGIAKDYNG 

        70         80         90        100        110        120 
LCNLRFDDTN PEKEDINYVN SIKEDVQWLG FNWDGEIKYS SNYFDILYDY AVELINKGLA 

       130        140        150        160        170        180 
YVCFLTADQA REYRGTLKEP GKNSPYRDTA SDENLALFEK MRNGEFKEGE CVLRAKIDMA 

       190        200        210        220        230        240 
SSFMVLRDPI IYRVRFAHHH QTADKWCIYP MYDFTHCISD ALEGITHSLC TLEFQDNRRL 

       250        260        270        280        290        300 
YDWVLDNISL ECHPQQIEFS RLNLEYTIMS KRKLSDLVVN NHVEGWDDPR MPTIAGLRRR 

       310        320        330        340        350        360 
GYTPASIREF CLRIGVTKQE NMVEMGMLEA CIREDLNENA PRAMAVLDPV KIVIENYDAD 

       370        380        390        400        410        420 
KVETLSVANH PNKEEMGRRD VPFTREIYIE REDFKEEANN KFKRLVLDKE VRLRGAYVIK 

       430        440        450        460        470        480 
AQRVEKDENG EITTIYCTYD PETLGKNPSD GRKVKGVIHW VSASEAITAE VRLYDRLFSV 

       490        500        510        520        530        540 
PNPAAADEFE STLNPDSLVI LTNAKLEPSL ANSAAEQGFQ FERTGYFSRD SKAKNIVFNQ 

       550 
TVGLRDSWSK TQ 

« Hide

References

[1]"Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125."
Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N., Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C. expand/collapse author list , Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.
Genome Res. 15:1325-1335(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TAC 125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR954246 Genomic DNA. Translation: CAI86715.1.
RefSeqYP_340158.1. NC_007481.1.

3D structure databases

ProteinModelPortalQ3IGW8.
SMRQ3IGW8. Positions 9-547.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326442.PSHAa1642.

Proteomic databases

PRIDEQ3IGW8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI86715; CAI86715; PSHAa1642.
GeneID3708249.
KEGGpha:PSHAa1642.
PATRIC32296847. VBIPseHal105694_1588.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPHAL326442:GJIU-1675-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_PSEHT
AccessionPrimary (citable) accession number: Q3IGW8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 8, 2005
Last modified: February 19, 2014
This is version 69 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