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Q6AJL4 (SYE_DESPS) 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:
Glutamate--tRNA ligase

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:DP2737
OrganismDesulfotalea psychrophila (strain LSv54 / DSM 12343) [Complete proteome] [HAMAP]
Taxonomic identifier177439 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobulbaceaeDesulfotalea

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) By similarity. HAMAP-Rule MF_00022

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00022

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00022.

Sequence similarities

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

Sequence caution

The sequence CAG37466.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

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

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 491491Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119553

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif243 – 2475"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2461ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6AJL4 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: 0EAC64A7E125BF9B

FASTA49155,678
        10         20         30         40         50         60 
MTETRLRFPP SPTGYLHIGG ARTALYNWLY AKQHGGKLVL RIEDTDTERS TEESIKGIVD 

        70         80         90        100        110        120 
GLDWLGIDFD EGPYFQTDFA SDHKSAAQKL LDSGQAYKCF CSKESLDEKR EAALAAKKSL 

       130        140        150        160        170        180 
GYDGTCRNLT AEQIAEKEAA GAPYVLRFRV PECESVSYED KIAGTIRVAR SEIDDFVIVR 

       190        200        210        220        230        240 
SNGAPLYLLC NVVDDIRDRI SHVIRGQDHM TNTIKQILLY EALDAPIPVF AHMPLTLDNK 

       250        260        270        280        290        300 
RAKISKRSHG EIVAVQFYRD HGFLPWALNN FLAMLGWSAG DDKEFYTKEE LLKAFSLERI 

       310        320        330        340        350        360 
NKSSSIFNYR KGDPKFFTDP KAISMNEHYI RNMDITELGK LVQKELEADG LWDTAYADEK 

       370        380        390        400        410        420 
ADWYLATIDM IRARFHTLKD FATLGRAYFG EDYVVEEKPL KKNVLKFEGL KEWLPLLGER 

       430        440        450        460        470        480 
YASLDDFSAE ETERVARELA DELELKPGVI INGMRTAVTG QLAGPSMFDI VTTLGQERMV 

       490 
KRLREAGRLF A 

« Hide

References

[1]"The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from permanently cold Arctic sediments."
Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M., Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H., Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.
Environ. Microbiol. 6:887-902(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LSv54 / DSM 12343.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR522870 Genomic DNA. Translation: CAG37466.1. Different initiation.
RefSeqYP_066473.1. NC_006138.1.

3D structure databases

ProteinModelPortalQ6AJL4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING177439.DP2737.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG37466; CAG37466; DP2737.
GeneID2946141.
KEGGdps:DP2737.
PATRIC21715590. VBIDesPsy67261_2969.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMANKLTWIN.
OrthoDBEOG6DRPF7.
ProtClustDBCLSK2765033.

Enzyme and pathway databases

BioCycDPSY177439:GJW5-2820-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. SSF48163. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_DESPS
AccessionPrimary (citable) accession number: Q6AJL4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: February 19, 2014
This is version 69 of the entry and version 2 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