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Reviewed, UniProtKB/Swiss-Prot Q02770 (CWC27_YEAST)

Last modified January 19, 2010. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptidyl-prolyl isomerase CWC27
    EC=5.2.1.8
Alternative name(s):
    Complexed with CEF1 protein 27
Gene names
Name: CWC27
Synonyms: CYP7
Ordered Locus Names: YPL064C
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length301 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Catalytic activity

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

Subunit structure

Belongs to the CWC complex (or PRP19-associated complex), a spliceosome subcomplex composed of the U2, U5 and U6 snRNAs and at least BUD13, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2.

Subcellular location

Cytoplasm. Nucleus Ref.3.

Miscellaneous

Present with 2360 molecules/cell in log phase SD medium. Ref.4

Sequence similarities

Belongs to the cyclophilin-type PPIase family. CWC27 subfamily.

Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentCytoplasm
Nucleus
Spliceosome
   Molecular functionIsomerase
Rotamase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processRNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

protein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentU2-type spliceosomal complex Ref.2

Inferred from direct assay. Source: SGD

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 301301Peptidyl-prolyl isomerase CWC27
PRO_0000064189

Regions

Domain9 – 159151PPIase cyclophilin-type

Sequences

Sequence LengthMass (Da)Tools
Q02770-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 131A4138F6C993B8

FASTA30135,026
        10         20         30         40         50         60 
MSSNIEPQTT AKCILYTTKG NIAIELWAKE CPETCKRFLS MLSDGTFTNG EFKELKPTQW 

        70         80         90        100        110        120 
LMFNANSTGE YRTVAEEKNP RIRFNRDGLL GWDRRRNTWF ITVLADSKHV LNDCNVFGKI 

       130        140        150        160        170        180 
VGKSIYIFRE ILGGEIEASS RDNDVKRFMY PAVLKDVEIT IPFFEDIFGS KRRLEDNEKK 

       190        200        210        220        230        240 
EQEPAKKLVK SAKVKMVYED EQEDDDGDVQ KLKPRKRMIL PAWIKDDSRS EGIKLDASLD 

       250        260        270        280        290        300 
QPQEALIREK TELHDNVDEA TTKETESQEN IKEEPMDKRE RETLAMLSKF QERIKNKNIL 


K 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed: 9169875] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[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: 11884590] [Abstract]
Cited for: MASS SPECTROMETRY, IDENTIFICATION IN THE CWC COMPLEX.
[3]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U39205 Genomic DNA. Translation: AAB68301.1.
PIRS60926.
RefSeqNP_015261.1.

3D structure databases

SMRQ02770. Positions 2-185.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2778N.
IntActQ02770. 5 interactions.
STRINGQ02770.

Proteomic databases

PeptideAtlasQ02770.

Genome annotation databases

EnsemblYPL064C; YPL064C; YPL064C; Saccharomyces cerevisiae. [Genome view]
GeneID856041.
KEGGsce:YPL064C.
NMPDRfig|4932.3.peg.6394.

Organism-specific databases

CYGDYPL064c.
SGDS000005985. CWC27.

Phylogenomic databases

eggNOGfuNOG06026.
OMAELWAKEC.
OrthoDBEOG9T1K3P.
PhylomeDBQ02770.

Enzyme and pathway databases

BRENDA5.2.1.8. 250.

Gene expression databases

ArrayExpressQ02770.
GenevestigatorQ02770.
GermOnlineYPL064C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR015891. Cyclophilin-like.
IPR002130. PPIase_cyclophilin.
[Graphical view]
Gene3DG3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PROSITEPS00170. CSA_PPIASE_1. False negative.
PS50072. CSA_PPIASE_2. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio980983.

Entry information

Entry nameCWC27_YEAST
AccessionPrimary (citable) accession number: Q02770
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: November 1, 1996
Last modified: January 19, 2010
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents