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Q5QXQ2 (SYQ_IDILO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. 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:IL1478
OrganismIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]
Taxonomic identifier283942 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina

Protein attributes

Sequence length561 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 – 561561Glutamine--tRNA ligase HAMAP-Rule MF_00126
PRO_1000095492

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
Q5QXQ2 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: E48E5B3DFE2AF8F2

FASTA56164,529
        10         20         30         40         50         60 
MADTDSRPSN FIRQIIDKDL ASGKHATVHT RFPPEPNGYL HIGHAKSIVL NFGIAEDYNG 

        70         80         90        100        110        120 
TCNLRFDDTN PLKEKVDYVN SIKKDVEWLG YHWEGEPRYS SNYFDQLHGF AVELIEKGLA 

       130        140        150        160        170        180 
YVDFSSQDKM REMRGTLKEP GVNSPYRDTS VEENLKHFAD MTAGKHEEGT AALRAKIDMS 

       190        200        210        220        230        240 
SPFMCMRDPV IYRVRFVHHH QTGDKWCVYP MYDFTHCISD ALEGITHSLC TLEFQDNRRL 

       250        260        270        280        290        300 
YDWVLDNISI DCHPQQIEFS RLNLQYTVMS KRIINTLVDE NKVSGWDDPR IASIAGLRRR 

       310        320        330        340        350        360 
GYTPDSVREF CRRIGVTKMD NQVEMSMLEA CIRDDLNVNA PRAMAVMDPV KIVIENYPEG 

       370        380        390        400        410        420 
EQELLDAPNH PNDPEMGSRQ VTFSREIWIE REDFRESANK KFKRLVLDKE VRLRNAYVIR 

       430        440        450        460        470        480 
ADRIETDDNG EIQTIYCHYD ADTLGKDPAD GRKVKGVIHW VSAETAKAAE FRVYDRLFQV 

       490        500        510        520        530        540 
PNPAAEEDLF STLNPESLVI KKGFVEANLA SAKLGENFQF ERLGYYCLDQ DAETEGRLIF 

       550        560 
NQTVGLRDSW AKIEQEQTTG S 

« Hide

References

[1]"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy."
Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. expand/collapse author list , Aizawa S., Shibata S., Malahoff A., Alam M.
Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017340 Genomic DNA. Translation: AAV82318.1.
RefSeqYP_155867.1. NC_006512.1.

3D structure databases

ProteinModelPortalQ5QXQ2.
SMRQ5QXQ2. Positions 9-549.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283942.IL1478.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV82318; AAV82318; IL1478.
GeneID3172053.
KEGGilo:IL1478.
PATRIC22141037. VBIIdiLoi21852_1481.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycILOI283942:GI0U-1488-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_IDILO
AccessionPrimary (citable) accession number: Q5QXQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 4, 2005
Last modified: February 19, 2014
This is version 65 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