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Protein

Peptidyl-prolyl cis-trans isomerase

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

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase (EC:5.2.1.8)
Short name:
PPIase
Alternative name(s):
Cyclophilin
Cyclosporin A-binding protein
Rotamase
Smp17.7
p17.7
OrganismiSchistosoma mansoni (Blood fluke)
Taxonomic identifieri6183 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 161161Peptidyl-prolyl cis-trans isomerasePRO_0000064127Add
BLAST

Expressioni

Tissue specificityi

Found mainly in the tegument, gut epithelium, and muscle layers. Also found in the interior of the parasite.

Interactioni

Protein-protein interaction databases

STRINGi6183.Smp_040130__mRNA.

Structurei

3D structure databases

ProteinModelPortaliQ26565.
SMRiQ26565. Positions 3-160.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 160155PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0865. Eukaryota.
COG0652. LUCA.
HOGENOMiHOG000065981.
OMAiFRELCTH.
PhylomeDBiQ26565.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q26565-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAKAFFDIK AGDERLGRII FELFNDVPDT TRNFRELCTH KNNFGYKGSV
60 70 80 90 100
FHRIIPGFMC QGGDFTNGDG TGGKSIYGNK FKDENFNHKH EAFSLSMANA
110 120 130 140 150
GPNTNGSQFF ITTVPCSWLD GKHVVFGKVV SGIDVVKKME SLGSTSGKPS
160
KKIIIEDCGE C
Length:161
Mass (Da):17,671
Last modified:November 1, 1996 - v1
Checksum:iBB3D3C4EF874F527
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L46884 mRNA. Translation: AAB41257.1.

Genome annotation databases

EnsemblMetazoaiSmp_040130.1; Smp_040130.1:pep; Smp_040130.
GeneDBiSmp_040130.1:pep.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L46884 mRNA. Translation: AAB41257.1.

3D structure databases

ProteinModelPortaliQ26565.
SMRiQ26565. Positions 3-160.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6183.Smp_040130__mRNA.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiSmp_040130.1; Smp_040130.1:pep; Smp_040130.
GeneDBiSmp_040130.1:pep.

Phylogenomic databases

eggNOGiKOG0865. Eukaryota.
COG0652. LUCA.
HOGENOMiHOG000065981.
OMAiFRELCTH.
PhylomeDBiQ26565.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Identification and characterization of Schistosoma mansoni p17.7, a cyclophilin."
    Kiang D., El Ghazalie N.E., Medhat A.M., Abdel-Fattah M., Karim A.M., Loverde P.T.
    Mol. Biochem. Parasitol. 76:73-82(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Strain: NMRI.

Entry informationi

Entry nameiPPIA_SCHMA
AccessioniPrimary (citable) accession number: Q26565
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: November 1, 1996
Last modified: January 20, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. 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.