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Protein

Peptidyl-prolyl cis-trans isomerase E

Gene
N/A
Organism
Schistosoma mansoni (Blood fluke)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Enzyme regulationi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Cyclosporin, RNA-binding

Enzyme and pathway databases

BRENDAi5.2.1.8. 5608.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase E (EC:5.2.1.8)
Short name:
PPIase E
Alternative name(s):
Cyclophilin E
Rotamase E
OrganismiSchistosoma mansoni (Blood fluke)
Taxonomic identifieri6183 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000641611 – 273Peptidyl-prolyl cis-trans isomerase EAdd BLAST273

Interactioni

Protein-protein interaction databases

STRINGi6183.Smp_094810__mRNA.

Structurei

Secondary structure

1273
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi113 – 120Combined sources8
Beta strandi123 – 132Combined sources10
Turni134 – 136Combined sources3
Helixi138 – 149Combined sources12
Turni150 – 152Combined sources3
Beta strandi160 – 165Combined sources6
Turni166 – 168Combined sources3
Beta strandi169 – 172Combined sources4
Turni175 – 177Combined sources3
Beta strandi178 – 181Combined sources4
Beta strandi205 – 208Combined sources4
Beta strandi220 – 225Combined sources6
Helixi228 – 230Combined sources3
Turni231 – 233Combined sources3
Beta strandi236 – 242Combined sources7
Helixi244 – 249Combined sources6
Helixi250 – 253Combined sources4
Beta strandi264 – 272Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CK1X-ray1.80A102-273[»]
2CMTX-ray1.50A102-273[»]
ProteinModelPortaliQ26548.
SMRiQ26548.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ26548.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 48RRMPROSITE-ProRule annotationAdd BLAST48
Domaini115 – 271PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST157

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0111. Eukaryota.
COG0652. LUCA.
OrthoDBiEOG091G0BGL.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
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]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001475. PPI_cyclophilin_E. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
SSF54928. SSF54928. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q26548-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPMDYQTEKH RGFAFVEFEE VEDAMSAIDN MNESEIFGRT IRVNVARPVR
60 70 80 90 100
IREGWSRPVW SDENWLKKYG SAPLEGRKLD EPDIVNPSDT SENVEDLSDE
110 120 130 140 150
EMRTKKQKRN LPRVFFDIRI GNGDAGRIVM ELRSDIVPRT AENFRALCTG
160 170 180 190 200
ERGFGYHNCC FHRVIPQFMC QGGDFVKGDG TGGKSIYGRK FDDENFQLRH
210 220 230 240 250
EGFGVLSMAN SGPNTNGSQF FICTTKCDWL DGKHVVFGRV VDGQNVVKKM
260 270
ESVGSKSGKV KEPVIISRCG ELI
Length:273
Mass (Da):30,905
Last modified:January 1, 1998 - v2
Checksum:iA3CE71D40CB0CDD1
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti196F → I in AAC47317 (PubMed:8898338).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30265 mRNA. Translation: AAC47543.1.
U50388 mRNA. Translation: AAC47317.1. Different initiation.

Genome annotation databases

GeneDBiSmp_094810.1:pep.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30265 mRNA. Translation: AAC47543.1.
U50388 mRNA. Translation: AAC47317.1. Different initiation.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CK1X-ray1.80A102-273[»]
2CMTX-ray1.50A102-273[»]
ProteinModelPortaliQ26548.
SMRiQ26548.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6183.Smp_094810__mRNA.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneDBiSmp_094810.1:pep.

Phylogenomic databases

eggNOGiKOG0111. Eukaryota.
COG0652. LUCA.
OrthoDBiEOG091G0BGL.

Enzyme and pathway databases

BRENDAi5.2.1.8. 5608.

Miscellaneous databases

EvolutionaryTraceiQ26548.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
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]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001475. PPI_cyclophilin_E. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
SSF54928. SSF54928. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPPIE_SCHMA
AccessioniPrimary (citable) accession number: Q26548
Secondary accession number(s): Q26558
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.