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Q9VG93

- GSTT7_DROME

UniProt

Q9VG93 - GSTT7_DROME

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Protein

Glutathione S-transferase D7

Gene
GstD7, gstD26, CG4371
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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

GO - Molecular functioni

  1. glutathione transferase activity Source: FlyBase

GO - Biological processi

  1. glutathione metabolic process Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase D7 (EC:2.5.1.18)
Short name:
DmGST26
Gene namesi
Name:GstD7
Synonyms:gstD26
ORF Names:CG4371
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0010043. GstD7.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 224224Glutathione S-transferase D7PRO_0000185959Add
BLAST

Proteomic databases

PaxDbiQ9VG93.
PRIDEiQ9VG93.

Expressioni

Gene expression databases

BgeeiQ9VG93.

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

BioGridi71337. 5 interactions.
IntActiQ9VG93. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9VG93.
SMRiQ9VG93. Positions 4-211.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8382GST N-terminalAdd
BLAST
Domaini90 – 210121GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 553Glutathione binding By similarity
Regioni67 – 693Glutathione binding By similarity

Sequence similaritiesi

Belongs to the GST superfamily. Theta family.

Phylogenomic databases

eggNOGiCOG0625.
GeneTreeiENSGT00540000069741.
InParanoidiQ9VG93.
KOiK00799.
OMAiGQEYASI.
OrthoDBiEOG7V1FRJ.
PhylomeDBiQ9VG93.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VG93-1 [UniParc]FASTAAdd to Basket

« Hide

MPNLDLYNFP MAPASRAIQM VAKALGLELN SKLINTMEGD QLKPEFVRIN    50
PQHTIPTLVD NGFVIWESRA IAVYLVEKYG KPDSPLYPND PQKRALINQR 100
LYFDMGTLYD ALTKYFFLIF RTGKFGDQEA LDKVNSAFGF LNTFLEGQDF 150
VAGSQLTVAD IVILATVSTV EWFSFDLSKF PNVERWLKNA PKVTPGWEQN 200
LESLQQGKKF LQDLQAAKEK EVKA 224
Length:224
Mass (Da):25,419
Last modified:May 1, 2000 - v1
Checksum:iD4478B93C59E565A
GO

Sequence cautioni

The sequence M97702 differs from that shown. Reason: Frameshift at several positions.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M97702 Genomic DNA. No translation available.
AE014297 Genomic DNA. Translation: AAF54792.1.
BT023285 mRNA. Translation: AAY55701.1.
PIRiH46681.
RefSeqiNP_525114.1. NM_080375.2.
UniGeneiDm.27472.

Genome annotation databases

EnsemblMetazoaiFBtr0082574; FBpp0082046; FBgn0010043.
GeneIDi48340.
KEGGidme:Dmel_CG4371.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M97702 Genomic DNA. No translation available.
AE014297 Genomic DNA. Translation: AAF54792.1 .
BT023285 mRNA. Translation: AAY55701.1 .
PIRi H46681.
RefSeqi NP_525114.1. NM_080375.2.
UniGenei Dm.27472.

3D structure databases

ProteinModelPortali Q9VG93.
SMRi Q9VG93. Positions 4-211.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 71337. 5 interactions.
IntActi Q9VG93. 1 interaction.

Proteomic databases

PaxDbi Q9VG93.
PRIDEi Q9VG93.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0082574 ; FBpp0082046 ; FBgn0010043 .
GeneIDi 48340.
KEGGi dme:Dmel_CG4371.

Organism-specific databases

CTDi 48340.
FlyBasei FBgn0010043. GstD7.

Phylogenomic databases

eggNOGi COG0625.
GeneTreei ENSGT00540000069741.
InParanoidi Q9VG93.
KOi K00799.
OMAi GQEYASI.
OrthoDBi EOG7V1FRJ.
PhylomeDBi Q9VG93.

Miscellaneous databases

GenomeRNAii 48340.
NextBioi 839350.

Gene expression databases

Bgeei Q9VG93.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The glutathione S-transferase D genes. A divergently organized, intronless gene family in Drosophila melanogaster."
    Toung Y.-P.S., Hsieh T.-S., Tu C.-P.D.
    J. Biol. Chem. 268:9737-9746(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.

Entry informationi

Entry nameiGSTT7_DROME
AccessioniPrimary (citable) accession number: Q9VG93
Secondary accession number(s): Q4V3S1, Q9TX87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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