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Protein

Peptidyl-prolyl cis-trans isomerase

Gene
N/A
Organism
Paramecium primaurelia
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 (By similarity).By similarity

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
OrganismiParamecium primaurelia
Taxonomic identifieri5886 [NCBI]
Taxonomic lineageiEukaryotaAlveolataCiliophoraIntramacronucleataOligohymenophoreaPeniculidaParameciidaeParamecium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 162162Peptidyl-prolyl cis-trans isomerasePRO_0000064126Add
BLAST

Proteomic databases

PRIDEiO00845.

Structurei

3D structure databases

ProteinModelPortaliO00845.
SMRiO00845. Positions 1-161.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 161157PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

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.

O00845-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANVFFDVQF GGDAPKKIVF KLYDDVVPKT AANFRELATG SRGFGYKGSV
60 70 80 90 100
FHRVITDFMA QGGDFTNFNG TGGKSIYGEK FADENFKLKH TKPALLSMAN
110 120 130 140 150
AGPNTNGSQF FITFVPCPWL DGKHVVFGEV VDGFDTLELF KKNSSQQGKP
160
KTTIKIVDSG VV
Length:162
Mass (Da):17,704
Last modified:July 1, 1997 - v1
Checksum:i22F0862E7129247A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13117 Genomic DNA. Translation: CAA73578.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13117 Genomic DNA. Translation: CAA73578.1.

3D structure databases

ProteinModelPortaliO00845.
SMRiO00845. Positions 1-161.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO00845.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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. "Sequence-specific epigenetic effects of the maternal somatic genome on developmental rearrangements of the zygotic genome in Paramecium primaurelia."
    Meyer E., Butler A., Dubrana K., Duharcourt S., Caron F.
    Mol. Cell. Biol. 17:3589-3599(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 156.

Entry informationi

Entry nameiPPIA_PARPR
AccessioniPrimary (citable) accession number: O00845
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: July 1, 1997
Last modified: October 14, 2015
This is version 62 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.