[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Duffieux F., Peyret P., Roe B.A., Vivares C.P.; "Putative trehalose 6-phosphate phosphatase from the chromosome I of Encephalitozoon cuniculi (Microspora)."; Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=GB-M1; DOI=10.1101/gr.164301; PubMed=11157783 [NCBI, ExPASy, EBI, Israel, Japan] Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M., Weissenbach J., Saurin W., Vivares C.P.; "Sequence and analysis of chromosome I of the amitochondriate intracellular parasite Encephalitozoon cuniculi (Microspora)."; Genome Res. 11:198-207(2001).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=GB-M1; DOI=10.1038/35106579; PubMed=11719806 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi."; Nature 414:450-453(2001).

Comments

CATALYTIC ACTIVITY: Trehalose 6-phosphate + H₂O = trehalose + phosphate.
SIMILARITY: In the N-terminal section; belongs to the glycosyltransferase 20 family.
SIMILARITY: In the C-terminal section; belongs to the trehalose phosphatase family.

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

AJ006825; CAA07262.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391737; CAD24957.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_965922.1; -.

3D structure databases

ModBase

Q8SSL0.

Ontologies

GO:0004805;	Molecular function: trehalose-phosphatase activity (inferred from electronic annotation from EC).
GO:0005992;	Biological process: trehalose biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001830; Glyco_trans_20.
IPR006379; HAD-SF_hydro_IIB.
IPR003337; Trehalose_PPase.
Graphical view of domain structure.

Pfam

PF00982; Glyco_transf_20; 1.
PF02358; Trehalose_PPase; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01484; HAD-SF-IIB; 1.
TIGR00685; T6PP; 1.

ProtoNet

Q8SSL0.

Genome annotation databases

GeneID

860263; -.

GenomeReviews

AL391737_GR; ECU01_0870.

KEGG

ecu:ECU01_0870; -.

NMPDR

fig|6035.1.peg.1922; -.

Phylogenomic databases

HOGENOM

Q8SSL0; -.

Other

UniRef

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

Keywords

Complete proteome; Hydrolase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 718`	`718`	`Probable trehalose-phosphatase.`	`PRO_0000122507`
`CONFLICT`	`421 421`		`R -> K (in Ref. 1; CAA07262).`

Sequence information

Length: 718 AA [This is the length of the unprocessed precursor]

Molecular weight: 82064 Da [This is the MW of the unprocessed precursor]

CRC64: B82FC7D318854CD5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKIIVAAEEL PICASRMEPS EAIKNWISTP LKKIPHPDKA SKIQIEFGDR SKESLHLFAK 

        70         80         90        100        110        120 
PHFMVPDMLD DDEMFFVGAP GFYSPEEFSD EDCRRIEESM KAYRCYPIFQ KRVKYSKMIE 

       130        140        150        160        170        180 
EILGKNTYEF VQSNFDHANM FARYKEYNTR WHEKIMEIYE EGDVVWVMDH SLFLLPGMLG 

       190        200        210        220        230        240 
NSIPVGMSAS VPFSSLLKCI PFWEQIFSSI LCCRYIEFNE SSSKESFDLL VSQKTGFCMG 

       250        260        270        280        290        300 
DPGYKDIREP LTCVGKKGID KDVLLKMSSE VHEFEGLGKG KVILLPSDSQ THLLGVEAYL 

       310        320        330        340        350        360 
SRYGKEITVL FLRTRVLNGD SDKQAEVMRL REYLEINYKV LSREFTPASD PEFISMLKRC 

       370        380        390        400        410        420 
DLCHCPEVAD VCSLFGIPVV RNNPYDFFDI ADEINENLMQ RGEGSKEGSS EVIGKMEWKK 

       430        440        450        460        470        480 
RFMTSLLSIS GMEYDVDLEP KEPRIRSSLS MDQTGHKKVD AKKKPGIRKK NREKEEAVEI 

       490        500        510        520        530        540 
ILNNKEDANA ARIVNDFKKS KARTLVMDYD GTLTNIVARP PMAAPTQEIK DLLIRLGKIC 

       550        560        570        580        590        600 
RVVISTGRSV EDCDKFFPKE IEVFAEHGAC HRIDGKWKEG GTFPQKDLAW RIGQFFLART 

       610        620        630        640        650        660 
PGSELERKKT GYAFHFRNVS PLIGVKQARA LFELLMRVCK DYVKKGNHVI EVRSSKKSCA 

       670        680        690        700        710 
MEKIEEGFVL CAGDDVADED MFDVCKGYTI KVGDQSTSAA YRVKDPENFR MLLGRLLE

Q8SSL0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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