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Protein

Peptidyl-prolyl cis-trans isomerase CYP7

Gene

CPR7

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. Plays a major role in negative regulation of the heat shock transcription factor (HSF).

Miscellaneous

Present with 3230 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

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

GO - Molecular functioni

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

GO - Biological processi

  • cellular response to heat Source: SGD
  • protein refolding Source: SGD

Keywordsi

Molecular functionIsomerase, Rotamase

Enzyme and pathway databases

BioCyciYEAST:YJR032W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase CYP7 (EC:5.2.1.8)
Short name:
PPIase CYP7
Alternative name(s):
Rotamase CYP7
Gene namesi
Name:CPR7
Ordered Locus Names:YJR032W
ORF Names:J1585
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJR032W.
SGDiS000003793. CPR7.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000641741 – 393Peptidyl-prolyl cis-trans isomerase CYP7Add BLAST393

Proteomic databases

MaxQBiP47103.
PRIDEiP47103.

Interactioni

Subunit structurei

Interacts with RPD3 and CNS1.

Binary interactionsi

Show more details

GO - Molecular functioni

  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi33785. 327 interactors.
DIPiDIP-2312N.
IntActiP47103. 11 interactors.
MINTiMINT-1540906.
STRINGi4932.YJR032W.

Structurei

Secondary structure

1393
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 13Combined sources8
Beta strandi16 – 25Combined sources10
Turni27 – 29Combined sources3
Helixi31 – 42Combined sources12
Beta strandi48 – 50Combined sources3
Beta strandi61 – 66Combined sources6
Turni67 – 69Combined sources3
Beta strandi70 – 73Combined sources4
Turni76 – 78Combined sources3
Beta strandi79 – 81Combined sources3
Turni87 – 90Combined sources4
Helixi100 – 105Combined sources6
Beta strandi111 – 113Combined sources3
Beta strandi125 – 131Combined sources7
Beta strandi134 – 136Combined sources3
Beta strandi140 – 142Combined sources3
Beta strandi144 – 149Combined sources6
Helixi152 – 154Combined sources3
Turni155 – 157Combined sources3
Beta strandi160 – 166Combined sources7
Helixi168 – 175Combined sources8
Beta strandi185 – 187Combined sources3
Beta strandi189 – 196Combined sources8
Helixi199 – 201Combined sources3
Beta strandi205 – 208Combined sources4
Helixi213 – 215Combined sources3
Helixi222 – 224Combined sources3
Helixi233 – 252Combined sources20
Helixi256 – 273Combined sources18
Turni277 – 279Combined sources3
Helixi281 – 304Combined sources24
Helixi308 – 319Combined sources12
Helixi326 – 342Combined sources17
Helixi346 – 359Combined sources14
Helixi366 – 385Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5JHEX-ray1.80A1-393[»]
ProteinModelPortaliP47103.
SMRiP47103.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini8 – 196PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST189
Repeati240 – 273TPR 1Add BLAST34
Repeati292 – 325TPR 2Add BLAST34
Repeati330 – 363TPR 3Add BLAST34

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

HOGENOMiHOG000065980.
InParanoidiP47103.
KOiK01802.
OMAiQFFITTY.
OrthoDBiEOG092C3VLQ.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
2.40.100.10. 1 hit.
InterProiView protein in InterPro
IPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiView protein in Pfam
PF00160. Pro_isomerase. 1 hit.
PF00515. TPR_1. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SMARTiView protein in SMART
SM00028. TPR. 3 hits.
SUPFAMiSSF48452. SSF48452. 1 hit.
SSF50891. SSF50891. 1 hit.
PROSITEiView protein in PROSITE
PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.

Sequencei

Sequence statusi: Complete.

P47103-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIQDPLVYLD ISIDKKPIGR IVCKLFREKA PKTTENFYKL CAGDVKSPLK
60 70 80 90 100
DQQYLSYKGN GFHRVVKNFM IQAGDIVFGT QKDSSSSSVG KGGCSIYADK
110 120 130 140 150
EEVKTDDESF CYGNFEDENL GEFVEPFTLG MANLGSPNTN NSQFFITTYA
160 170 180 190 200
APHLNGKHSI FGQVVHGKSV VRTIENCRVD SDGVPESDVR ISDCGVWEKT
210 220 230 240 250
MGVPLYNASN DQIGGDVYEE YPDDDTHFGD DDFGKALEAA NIIKESGTLL
260 270 280 290 300
FKKKDYSNAF FKYRKSLNYI NEYMPEPDVD KERNIQFINL KMKIYLNLSL
310 320 330 340 350
VLFNLERYDD AIMYATYLLE MDNVPNRDQA KAYYRRGNSY LKKKRLDEAL
360 370 380 390
QDYIFCKEKN PDDEVIEQRI EYVNRLIEEN KEKTRKNISK FFS
Length:393
Mass (Da):45,134
Last modified:November 1, 1995 - v1
Checksum:i1532F255E8016F4F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti237L → F in AAC49415 (PubMed:8873448).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48868 Genomic DNA. Translation: AAC49415.1.
Z49532 Genomic DNA. Translation: CAA89559.1.
X87297 Genomic DNA. Translation: CAA60725.1.
AY693103 Genomic DNA. Translation: AAT93122.1.
BK006943 Genomic DNA. Translation: DAA08821.1.
PIRiS57050.
RefSeqiNP_012566.1. NM_001181690.1.

Genome annotation databases

EnsemblFungiiYJR032W; YJR032W; YJR032W.
GeneIDi853489.
KEGGisce:YJR032W.

Similar proteinsi

Entry informationi

Entry nameiCYP7_YEAST
AccessioniPrimary (citable) accession number: P47103
Secondary accession number(s): D6VWK5, Q92323
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 25, 2017
This is version 152 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names