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P46426 (GSTP_DIRIM) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Glutathione S-transferase

EC=2.5.1.18
Alternative name(s):
GST class-pi
OrganismDirofilaria immitis (Canine heartworm)
Taxonomic identifier6287 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaSpiruridaFilarioideaOnchocercidaeDirofilaria

Protein attributes

Sequence length208 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

Catalytic activity

RX + glutathione = HX + R-S-glutathione.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the GST superfamily. Pi family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Molecular functionTransferase
Gene Ontology (GO)
   Molecular_functionglutathione transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 208208Glutathione S-transferase
PRO_0000185913

Regions

Domain1 – 7878GST N-terminal
Domain80 – 200121GST C-terminal
Region49 – 502Glutathione binding By similarity
Region62 – 632Glutathione binding By similarity

Sites

Binding site71Glutathione By similarity
Binding site421Glutathione By similarity

Sequences

Sequence LengthMass (Da)Tools
P46426 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 698510856385AE6B

FASTA20824,146
        10         20         30         40         50         60 
MSYKLTYFPI RGLAEPIRLL LVDQGIKFTD EHIPKDDFVS IKSQFQFGQL PCFYDGDQQI 

        70         80         90        100        110        120 
VQSGAILRHL ARKFNLNGEN NAETSYVDMF YEGIRDLHSK YTRMIYEAYE TQKDPFIKNI 

       130        140        150        160        170        180 
LPQELAKLEK LLATRDNGKN FILGDKISFA DYVLFEELDV QQILDPHCLE KFPLLKAFHQ 

       190        200 
RLGDKPKIKE YCAKRNASKM PVNGNGKQ 

« Hide

References

[1]James E.R., McLean D.C., Venkatakrishnaiah L.
Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14753 mRNA. Translation: AAA21585.1.

3D structure databases

ProteinModelPortalP46426.
SMRP46426. Positions 1-208.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01268. GSTRNSFRASEP.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSTP_DIRIM
AccessionPrimary (citable) accession number: P46426
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 16, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families