NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sorsogon / Philippines;
DOI=10.1016/0166-6851(90)90076-X; PubMed=1693415 [NCBI, ExPASy, EBI, Israel, Japan]
Henkle K.J., Davern K.M., Wright M.D., Ramos A.J., Mitchell G.F.;
"Comparison of the cloned genes of the 26- and 28-kilodalton glutathione S-transferases of Schistosoma japonicum and Schistosoma mansoni.";
Mol. Biochem. Parasitol. 40:23-34(1990).

Comments

FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
FUNCTION: GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.
CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
SUBUNIT: Homodimer.
MISCELLANEOUS: There are at least two isoenzymes of GST in S.japonicum.
SIMILARITY: Belongs to the GST superfamily. Mu family.
SIMILARITY: Contains 1 GST C-terminal domain.
SIMILARITY: Contains 1 GST N-terminal domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M26914; AAA29890.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B44941; B44941.

3D structure databases

HSSP

P30114; 1OE7. [HSSP ENTRY / PDB]

SMR

P26624; 1-206.

ModBase

P26624.

Ontologies

GO:0004364;	Molecular function: glutathione transferase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR010987; Glutathione-S-Trfase_C-like.
IPR004046; GST_C.
IPR004045; GST_N.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.1050.10; GST_C_like; 1.
G3DSA:3.40.30.10; Thioredoxin_fold; 1.

Pfam

PF00043; GST_C; 1.
PF02798; GST_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS50405; GST_CTER; 1.
PS50404; GST_NTER; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P26624.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 206`	`>206`	`Glutathione S-transferase class-mu 28 kDa isozyme.`	`PRO_0000185814`
`DOMAIN`	`<1 81`	`>81`	`GST N-terminal.`
`DOMAIN`	`83 206`	`124`	`GST C-terminal.`
`ACT_SITE`	`5 5`		`By similarity.`
`NON_TER`	`1 1`

Sequence information

Length: 206 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 23393 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: D1AD3707EDEABAA7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
VKLIYFNGRG RAEPIRMILV AAGVEFEDER IEFQDWPKIK PTIPGGRLPI VKITDKRGDV 

        70         80         90        100        110        120 
KTMSESLAIA RFIARKHNMM GDTDDEYYII EKMIGQVEDV ESEYHKTLIK PPEEKEKISK 

       130        140        150        160        170        180 
EILNGKVPIL LQAICETLKE STGNLTVGDK VTLADVVLIA SIDHITDLDK EFLTGKYPEI 

       190        200 
HKHRKHLLAT SPKLAKYLSE RHATAF

P26624 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools