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Protein

Peptidyl-prolyl cis-trans isomerase

Gene

CyP3

Organism
Triticum aestivum (Wheat)
Status
Unreviewed-Annotation score: Annotation score: 2 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.UniRule annotation

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).UniRule annotationSAAS annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, RotamaseUniRule annotationSAAS annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase (EC:5.2.1.8)
Gene namesi
Name:CyP3Imported
Synonyms:CyP1Imported, TaBWCyp A-1Imported
OrganismiTriticum aestivum (Wheat)Imported
Taxonomic identifieri4565 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeTriticum
ProteomesiUP000019116 Componenti: Unassembled WGS sequence

Organism-specific databases

GrameneiQ93W25.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4E1QX-ray1.25A1-171[»]
4HY7X-ray1.20A1-171[»]
ProteinModelPortaliQ93W25.
SMRiQ93W25. Positions 1-171.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.UniRule annotation

Phylogenomic databases

OMAiSINCEIN.

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.

Q93W25-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANPRVFFDM TVGGAPAGRI VMELYKDAVP RTVENFRALC TGEKGVGKSG
60 70 80 90 100
KPLHYKGSAF HRVIPDFMCQ GGDFTRGNGT GGESIYGEKF ADEKFVHKHT
110 120 130 140 150
KPGILSMANA GPNTNGSQFF ICTVPCNWLD GKHVVFGEVV EGMDVVKNIE
160 170
KVGSRSGTCS KQVVIADCGQ L
Length:171
Mass (Da):18,391
Last modified:December 1, 2001 - v1
Checksum:i62D45AF2BC55FC6F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF262982 mRNA. Translation: AAK49426.1.
AF262984 mRNA. Translation: AAK49428.1.
JQ678695 mRNA. Translation: AFS50133.1.
AB711117 mRNA. Translation: BAN09078.1.

Genome annotation databases

EnsemblPlantsiTraes_6AS_82E93D872.1; Traes_6AS_82E93D872.1; Traes_6AS_82E93D872.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF262982 mRNA. Translation: AAK49426.1.
AF262984 mRNA. Translation: AAK49428.1.
JQ678695 mRNA. Translation: AFS50133.1.
AB711117 mRNA. Translation: BAN09078.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4E1QX-ray1.25A1-171[»]
4HY7X-ray1.20A1-171[»]
ProteinModelPortaliQ93W25.
SMRiQ93W25. Positions 1-171.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiTraes_6AS_82E93D872.1; Traes_6AS_82E93D872.1; Traes_6AS_82E93D872.

Organism-specific databases

GrameneiQ93W25.

Phylogenomic databases

OMAiSINCEIN.

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. "Isolation and characterisation of cDNAs encoding protein disulphide isomerases and cyclophilins in wheat."
    Johnson J.C., Clarke B.C., Bhave M.
    J. Cereal Sci. 34:159-171(2001)
    [AGRICOLA] [Europe PMC]
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: EndospermImported.
  2. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: cv. Chinese SpringImported.
  3. "A unique calmodulin binding cyclophilin (TaCyPA-1) from an Indian elite wheat cultivar - Punjab Pread Wheat (PBW-343)."
    Singh K., Kaur H., Dutta T., Kumari S., Singla-Pareek S.L., Singh P., Pareek A.
    Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  4. "cDNA sequences derived from Triticum aestivum cv. Bobwhite."
    Haque M.E., Abe F., Mori M., Oyanagi A., Komatsu S., Kawaguchi K.
    Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  5. "Structural and biochemical characterization of the cytosolic wheat cyclophilin TaCypA-1."
    Sekhon S.S., Kaur H., Dutta T., Singh K., Kumari S., Kang S., Park S.G., Park B.C., Jeong D.G., Pareek A., Woo E.J., Singh P., Yoon T.S.
    Acta Crystallogr. D 69:555-563(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS).
  6. EnsemblPlants
    Submitted (FEB-2015) to UniProtKB
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiQ93W25_WHEAT
AccessioniPrimary (citable) accession number: Q93W25
Entry historyi
Integrated into UniProtKB/TrEMBL: December 1, 2001
Last sequence update: December 1, 2001
Last modified: May 27, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.