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Protein

Peptidyl-prolyl cis-trans isomerase CPR6

Gene

CPR6

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 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).

GO - Molecular functioni

  • peptidyl-prolyl cis-trans isomerase activity Source: SGD
  • ribosome binding Source: SGD
  • unfolded protein binding Source: SGD

GO - Biological processi

  • protein folding Source: SGD
  • protein refolding Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Enzyme and pathway databases

BioCyciYEAST:YLR216C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase CPR6 (EC:5.2.1.8)
Short name:
PPIase CPR6
Alternative name(s):
Rotamase CPR6
Gene namesi
Name:CPR6
Ordered Locus Names:YLR216C
ORF Names:L8167.24
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR216C.
SGDiS000004206. CPR6.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 371371Peptidyl-prolyl cis-trans isomerase CPR6PRO_0000064173Add
BLAST

Proteomic databases

MaxQBiP53691.

Interactioni

Subunit structurei

Interacts with RPD3.

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP82P028292EBI-5429,EBI-8659
RPD3P325612EBI-5429,EBI-15864

GO - Molecular functioni

  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi31484. 81 interactions.
DIPiDIP-1274N.
IntActiP53691. 11 interactions.
MINTiMINT-393160.

Structurei

3D structure databases

ProteinModelPortaliP53691.
SMRiP53691. Positions 2-365.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 174168PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST
Repeati219 – 25234TPR 1Add
BLAST
Repeati270 – 30334TPR 2Add
BLAST
Repeati308 – 34134TPR 3Add
BLAST

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation
Contains 3 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

GeneTreeiENSGT00550000074595.
HOGENOMiHOG000065980.
InParanoidiP53691.
KOiK05864.
OMAiEVSWWMD.
OrthoDBiEOG757D7G.

Family and domain databases

Gene3Di1.10.150.160. 1 hit.
1.25.40.10. 1 hit.
2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR023114. Elongated_TPR_rpt_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SMARTiSM00028. TPR. 1 hit.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
SSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50005. TPR. 1 hit.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53691-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRPKTFFDI SIGGKPQGRI VFELYNDIVP KTAENFLKLC EGNAGMAKTK
60 70 80 90 100
PDVPLSYKGS IFHRVIKDFM CQFGDFTNFN GTGGESIYDE KFEDENFTVK
110 120 130 140 150
HDKPFLLSMA NAGPNTNGSQ AFITCVPTPH LDGKHVVFGE VIQGKRIVRL
160 170 180 190 200
IENQQCDQEN NKPLRDVKID DCGVLPDDYQ VPENAEATPT DEYGDNYEDV
210 220 230 240 250
LKQDEKVDLK NFDTVLKAIE TVKNIGTEQF KKQNYSVALE KYVKCDKFLK
260 270 280 290 300
EYFPEDLEKE QIEKINQLKV SIPLNIAICA LKLKDYKQVL VASSEVLYAE
310 320 330 340 350
AADEKAKAKA LYRRGLAYYH VNDTDMALND LEMATTFQPN DAAILKAIHN
360 370
TKLKRKQQNE KAKKSLSKMF S
Length:371
Mass (Da):42,072
Last modified:October 1, 1996 - v1
Checksum:i188666D94866DDDD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121I → V in AAS56285 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48867 mRNA. Translation: AAC49414.1.
U14913 Genomic DNA. Translation: AAB67445.1.
AY557959 Genomic DNA. Translation: AAS56285.1.
BK006945 Genomic DNA. Translation: DAA09533.1.
PIRiS48567.
RefSeqiNP_013317.1. NM_001182103.1.

Genome annotation databases

EnsemblFungiiYLR216C; YLR216C; YLR216C.
GeneIDi850914.
KEGGisce:YLR216C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48867 mRNA. Translation: AAC49414.1.
U14913 Genomic DNA. Translation: AAB67445.1.
AY557959 Genomic DNA. Translation: AAS56285.1.
BK006945 Genomic DNA. Translation: DAA09533.1.
PIRiS48567.
RefSeqiNP_013317.1. NM_001182103.1.

3D structure databases

ProteinModelPortaliP53691.
SMRiP53691. Positions 2-365.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31484. 81 interactions.
DIPiDIP-1274N.
IntActiP53691. 11 interactions.
MINTiMINT-393160.

Proteomic databases

MaxQBiP53691.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR216C; YLR216C; YLR216C.
GeneIDi850914.
KEGGisce:YLR216C.

Organism-specific databases

EuPathDBiFungiDB:YLR216C.
SGDiS000004206. CPR6.

Phylogenomic databases

GeneTreeiENSGT00550000074595.
HOGENOMiHOG000065980.
InParanoidiP53691.
KOiK05864.
OMAiEVSWWMD.
OrthoDBiEOG757D7G.

Enzyme and pathway databases

BioCyciYEAST:YLR216C-MONOMER.

Miscellaneous databases

PROiP53691.

Family and domain databases

Gene3Di1.10.150.160. 1 hit.
1.25.40.10. 1 hit.
2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR023114. Elongated_TPR_rpt_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SMARTiSM00028. TPR. 1 hit.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
SSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50005. TPR. 1 hit.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of two CyP-40-like cyclophilins in Saccharomyces cerevisiae, one of which is required for normal growth."
    Duina A.A., Marsh J.A., Gaber R.F.
    Yeast 12:943-952(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPPID_YEAST
AccessioniPrimary (citable) accession number: P53691
Secondary accession number(s): D6VYL7, Q6Q5K7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 18600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

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.