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Protein

Peptidylprolyl isomerase cyp7

Gene

cyp7

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

PPIases accelerate the folding of proteins. Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in pre-mRNA splicing.

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Biological processi

mRNA processing, mRNA splicing

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidylprolyl isomerase cyp7 (EC:5.2.1.8)
Short name:
PPIase cyp7
Alternative name(s):
Complexed with cdc5 protein 27
Cyclophilin 7
Rotamase cyp7
Gene namesi
Name:cyp7
Synonyms:cwf27
ORF Names:SPBC16H5.05c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC16H5.05c.
PomBaseiSPBC16H5.05c. cyp7.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 463463Peptidylprolyl isomerase cyp7PRO_0000064178Add
BLAST

Proteomic databases

MaxQBiO42941.

Interactioni

Subunit structurei

Belongs to the 40S cdc5-associated complex (or cwf complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least brr2, cdc5, cwf2/prp3, cwf3/syf1, cwf4/syf3, cwf5/ecm2, spp42/cwf6, cwf7/spf27, cwf8, cwf9, cwf10, cwf11, cwf12, prp45/cwf13, cwf14, cwf15, cwf16, cwf17, cwf18, cwf19, cwf20, cwf21, cwf22, cwf23, cwf24, cwf25, cwf26, cyp7/cwf27, cwf28, cwf29/ist3, lea1, msl1, prp5/cwf1, prp10, prp12/sap130, prp17, prp22, sap61, sap62, sap114, sap145, slu7, smb1, smd1, smd3, smf1, smg1 and syf2.1 Publication

Protein-protein interaction databases

BioGridi276605. 37 interactions.
IntActiO42941. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliO42941.
SMRiO42941. Positions 8-171.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 166156PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi235 – 31884Ser-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000161443.
InParanoidiO42941.
KOiK12737.
OrthoDBiEOG77HDQ6.
PhylomeDBiO42941.

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]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O42941-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATLTNLEPL ATGTVILKTT RGDIQIELWC KEVPKACRNF IQLCLEGYYD
60 70 80 90 100
GTIVHRVVPE FLIQGGDPTG TGMGGESIYG EPFAVETHPR LRFIRRGLVG
110 120 130 140 150
MACTENEGNN SQFFITLGPT PEWNGKQTLF GRVVGDTIYN VVRISELELD
160 170 180 190 200
ANQRPVFPPK IISTEVIDNY FTDIKPRSTK EEREKIANEL AHQEKQKERN
210 220 230 240 250
KLLKSGRRNK AVLSFGDEVD MPIVKKPLRQ KTPVSRSSDT TTELSKDLIS
260 270 280 290 300
SSSSIHSTYS SAQTGLTSAK VSSDEYARQV DTLDTKLNSS SKSKVQEEIS
310 320 330 340 350
RLKSELRDLE KSGGSSNSKP VVVRPKKRNI LTEELEKYKK SKKVVLGKRK
360 370 380 390 400
NLENDEESTL RALSSFQSKI RNAEDEDVMD SQYGSKIEDT PCSLHNVPGC
410 420 430 440 450
FSCFDRLGEK NITETNSNWF AHRLVAENDP TRRTEELRIQ RAEELKDVPS
460
ARPKKLLMKR DII
Length:463
Mass (Da):52,174
Last modified:June 1, 1998 - v1
Checksum:iD7A3148A3CD74A83
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA17903.1.
PIRiT39621.
RefSeqiNP_595943.1. NM_001021851.2.

Genome annotation databases

EnsemblFungiiSPBC16H5.05c.1; SPBC16H5.05c.1:pep; SPBC16H5.05c.
GeneIDi2540067.
KEGGispo:SPBC16H5.05c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA17903.1.
PIRiT39621.
RefSeqiNP_595943.1. NM_001021851.2.

3D structure databases

ProteinModelPortaliO42941.
SMRiO42941. Positions 8-171.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276605. 37 interactions.
IntActiO42941. 1 interaction.

Proteomic databases

MaxQBiO42941.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC16H5.05c.1; SPBC16H5.05c.1:pep; SPBC16H5.05c.
GeneIDi2540067.
KEGGispo:SPBC16H5.05c.

Organism-specific databases

EuPathDBiFungiDB:SPBC16H5.05c.
PomBaseiSPBC16H5.05c. cyp7.

Phylogenomic databases

HOGENOMiHOG000161443.
InParanoidiO42941.
KOiK12737.
OrthoDBiEOG77HDQ6.
PhylomeDBiO42941.

Miscellaneous databases

NextBioi20801204.
PROiO42941.

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]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Proteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs."
    Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.
    Mol. Cell. Biol. 22:2011-2024(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CWF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiCYP7_SCHPO
AccessioniPrimary (citable) accession number: O42941
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: June 1, 1998
Last modified: May 11, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. 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.