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Q6L0N9 (SYE_PICTO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 67. 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:PTO0878
OrganismPicrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828) [Complete proteome] [HAMAP]
Taxonomic identifier263820 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesPicrophilaceaePicrophilus

Protein attributes

Sequence length548 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

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00022.

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_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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 548548Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119724

Regions

Motif103 – 11311"HIGH" region HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
Q6L0N9 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: CE6F31A1B4261F60

FASTA54864,230
        10         20         30         40         50         60 
MSITEEIRKQ AIKNAYLHDG RADVKSVVSK LMAEFPEARK NPGDLINDVK KCVDEINSMG 

        70         80         90        100        110        120 
KDRIIEIINN EYPEFKIKEK KEEKHELPEL PNAKNGVVMR MAPSPSGPLH IGHSRMAILN 

       130        140        150        160        170        180 
DEYVKRYGGD LILRIEDTNP GNIDIDAYDM IPEDLKWLDV NVTKTVIQTS RMDLYYREAK 

       190        200        210        220        230        240 
KLIENGYMYI AETDQKRFKE LKLKSMALPD RSMDPGVHLD RFDKMLNREY REGEAVAVLK 

       250        260        270        280        290        300 
TDLNHPNPSI RDWIAFRISY KRHPLTGDEY CVYPMMNFSV AIDDHYLGLT HVIRGMDHLV 

       310        320        330        340        350        360 
NTEKQKYIFN YNNWKLPYYY HYGIIKIPGS VLKTSIIKNG IKSGKYTGWD DVRLGTIRAL 

       370        380        390        400        410        420 
RKRGYRPETF RRYWINSGMK ETGATFSWEI FDSINRQLID RDAMRFFFVN DPVLLDLNND 

       430        440        450        460        470        480 
IDLESHARYH PDIDLGYRKY IIKSHSRIYL SRRDLDDIKP DEIFRLKDLC VVKRTEDGIA 

       490        500        510        520        530        540 
YIDDDSNKRL KIIQWCPENS HEFTVQKPDG TVDSGMLEPL AYNYNGVSQF ERYGYVNIIN 


RNGYFLHR 

« Hide

References

[1]"Genome sequence of Picrophilus torridus and its implications for life around pH 0."
Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C., Schepers B., Dock C., Antranikian G., Liebl W.
Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017261 Genomic DNA. Translation: AAT43463.1.
RefSeqYP_023656.1. NC_005877.1.

3D structure databases

ProteinModelPortalQ6L0N9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING263820.PTO0878.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT43463; AAT43463; PTO0878.
GeneID2844155.
KEGGpto:PTO0878.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000073585.
KOK01885.
OMAAFRIIDT.

Enzyme and pathway databases

BioCycPTOR263820:GHA3-915-MONOMER.

Family and domain databases

Gene3D1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_A. Glu_tRNA_synth_A.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR004526. Glu-tRNA-synth_arc/euk.
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.
IPR022888. Glu_tRNA_synth_arc.
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.
TIGRFAMsTIGR00463. gltX_arch. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_PICTO
AccessionPrimary (citable) accession number: Q6L0N9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 67 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