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Q8SSE4 (SYEC_ENCCU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable glutamate--tRNA ligase, cytoplasmic
EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Ordered Locus Names:ECU02_1210
OrganismEncephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite) [Reference proteome]
Taxonomic identifier284813 [NCBI]
Taxonomic lineageEukaryota › Fungi › Microsporidia › Unikaryonidae › Encephalitozoon ›

Protein attributes

Sequence length642 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Subcellular location

Cytoplasm By similarity.

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
Reference proteome
Gene Ontology (GO)
   Biological_processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 642642Probable glutamate--tRNA ligase, cytoplasmic
PRO_0000388391

Regions

Nucleotide binding382 – 3865ATP By similarity
Region152 – 1543Glutamate binding By similarity
Region326 – 3305Glutamate binding By similarity
Motif157 – 16610"HIGH" region By similarity
Motif382 – 3865"KMSKS" region By similarity

Sites

Binding site1621ATP By similarity
Binding site1881Glutamate By similarity
Binding site3441Glutamate By similarity
Binding site3471ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8SSE4 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: B2BC6D4B2C329BB2

FASTA64273,964
        10         20         30         40         50         60 
MDGKSEFKEE LINYILLKKY GKGAQDPPVY SNALKKAPQE MFPPGLVDAL DSYSINLSRS 

        70         80         90        100        110        120 
EGVEFLVLLN SLVNDIRSEE VKDIIFGMIN TNQMLTKLMK DKKEVERFPD TCKMYSEQFK 

       130        140        150        160        170        180 
ANKPLLKEFN AGSRKEQGNL EIGEPSENVV TRFPPEPNGR LHIGHARAAL LNWYFASKGN 

       190        200        210        220        230        240 
GRLLVRFDDT NPEKEEERFE RGILSDLSLL GINEYTLSHT SDYFDKIIDL GVFLIGEGKA 

       250        260        270        280        290        300 
YADNTPQEVM RDERGRGVES RCRSMDVEES KRIFKEMARG NASGYCLRAK IDMSSSNKAM 

       310        320        330        340        350        360 
RDPVIFRVNE SPHHRTGDKY KVYPTYDFAC PIVDSLEGIT LSLRANEYRD RNQQYYWFID 

       370        380        390        400        410        420 
NLRLRNRPKI HDFSRLNFEN TVLSKRKLKY YVDNGFVSGW DDPRLATIAG IKRLGMNMEA 

       430        440        450        460        470        480 
LREYILMQGV SQKTCTISWD KVWAINRKKI DPVSARYFCV QQRDAVEVSI DNTSEYTMDV 

       490        500        510        520        530        540 
PKHKKNGDLG TKEVFYSSQI LLSQEDGRVL QDNEEFTLMN WGNAIVKSKT VENGTVTKME 

       550        560        570        580        590        600 
VSLNPDGDFK LTKNKMSWVS KRGSVTVELA EYGNLMNDED TEDLALRFNR NSVKKEYWYA 

       610        620        630        640 
ESAIINVREG EVIQFERNGF YYCDGFLVFN LLPFTKQKRT GN

« Hide

References

[1]"Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi."
Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J., Vivares C.P.
Nature 414:450-453(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GB-M1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL590442 Genomic DNA. Translation: CAD25150.1.
RefSeqNP_584646.1. NM_001040835.1.

3D structure databases

HSSPHSSP built from PDB template 1NYL based on UniProtKB P00962.
ProteinModelPortalQ8SSE4.
ModBaseSearch...

Protein-protein interaction databases

STRING6035.ECU02_1210.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID858636.
KEGGecu:ECU02_1210.

Phylogenomic databases

eggNOGCOG0008.
KOK01885.

Family and domain databases

Gene3D1.10.1160.10. 1 hit.
2.40.240.10. 2 hits.
3.40.50.620. 2 hits.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR004526. Glu-tRNA-synth_Ib_arc/euk.
IPR000924. Glu/Gln-tRNA-synth_Ib.
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. Ribosomal_L25rel. 1 hit.
TIGRFAMsTIGR00463. gltX_arch. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYEC_ENCCU
AccessionPrimary (citable) accession number: Q8SSE4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: June 1, 2002
Last modified: May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

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