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Q26548 (PPIE_SCHMA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Peptidyl-prolyl cis-trans isomerase E

Short name=PPIase E
EC=5.2.1.8
Alternative name(s):
Cyclophilin E
Rotamase E
OrganismSchistosoma mansoni (Blood fluke)
Taxonomic identifier6183 [NCBI]
Taxonomic lineageEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

Protein attributes

Sequence length273 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulation

Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the cyclophilin-type PPIase family. PPIase E subfamily.

Contains 1 PPIase cyclophilin-type domain.

Contains 1 RRM (RNA recognition motif) domain.

Sequence caution

The sequence AAC47317.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCyclosporin
RNA-binding
   Molecular functionIsomerase
Rotamase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: InterPro

peptide binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 273273Peptidyl-prolyl cis-trans isomerase E
PRO_0000064161

Regions

Domain1 – 4848RRM
Domain115 – 271157PPIase cyclophilin-type

Experimental info

Sequence conflict1961F → I in AAC47317. Ref.2

Secondary structure

............................... 273
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q26548 [UniParc].

Last modified January 1, 1998. Version 2.
Checksum: A3CE71D40CB0CDD1

FASTA27330,905
        10         20         30         40         50         60 
MPMDYQTEKH RGFAFVEFEE VEDAMSAIDN MNESEIFGRT IRVNVARPVR IREGWSRPVW 

        70         80         90        100        110        120 
SDENWLKKYG SAPLEGRKLD EPDIVNPSDT SENVEDLSDE EMRTKKQKRN LPRVFFDIRI 

       130        140        150        160        170        180 
GNGDAGRIVM ELRSDIVPRT AENFRALCTG ERGFGYHNCC FHRVIPQFMC QGGDFVKGDG 

       190        200        210        220        230        240 
TGGKSIYGRK FDDENFQLRH EGFGVLSMAN SGPNTNGSQF FICTTKCDWL DGKHVVFGRV 

       250        260        270 
VDGQNVVKKM ESVGSKSGKV KEPVIISRCG ELI 

« Hide

References

[1]"RNA trans-splicing in flatworms. Analysis of trans-spliced mRNAs and genes in the human parasite, Schistosoma mansoni."
Davis R.E., Hardwick C., Tavernier P., Hodgson S., Singh H.
J. Biol. Chem. 270:21813-21819(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence conservation of schistosome cyclophilins."
Klinkert M.-Q., Bugli F., Cruz J., Engels B., Cioli D.
Mol. Biochem. Parasitol. 81:239-242(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 57-273.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U30265 mRNA. Translation: AAC47543.1.
U50388 mRNA. Translation: AAC47317.1. Different initiation.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CK1X-ray1.80A102-273[»]
2CMTX-ray1.50A102-273[»]
ProteinModelPortalQ26548.
SMRQ26548. Positions 1-53, 110-273.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA5.2.1.8. 5608.

Family and domain databases

Gene3D2.40.100.10. 1 hit.
3.30.70.330. 1 hit.
InterProIPR029000. Cyclophilin-like_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR016304. Cyclophilin-type_PPIase_E.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
PIRSFPIRSF001475. PPI_cyclophilin_E. 1 hit.
PRINTSPR00153. CSAPPISMRASE.
SUPFAMSSF50891. SSF50891. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ26548.

Entry information

Entry namePPIE_SCHMA
AccessionPrimary (citable) accession number: Q26548
Secondary accession number(s): Q26558
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 1, 1998
Last modified: June 11, 2014
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references