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Q09928 (PPIL2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase cyp8
Short name=PPIase cyp8
EC=5.2.1.8
Alternative name(s):
Rotamase cyp8
Gene names
Name:cyp8
ORF Names:SPAC21E11.05c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces ›

Protein attributes

Sequence length516 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity.

Catalytic activity

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

Subcellular location

Nucleus Ref.3.

Induction

Induced during the meiotic cycle. Ref.3

Sequence similarities

Belongs to the cyclophilin-type PPIase family. PPIL2 subfamily.

Contains 1 PPIase cyclophilin-type domain.

Contains 1 U-box domain.

Sequence caution

The sequence CAA91964.1 differs from that shown. Reason: Frameshift at position 27.

Ontologies

Keywords
   Cellular componentNucleus
   DomainCoiled coil
   Molecular functionIsomerase
Rotamase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

protein peptidyl-prolyl isomerization

Inferred from electronic annotation. Source: GOC

protein ubiquitination

Non-traceable author statement. Source: PomBase

   Cellular_componentnucleus

Inferred from direct assay PubMed 16823372. Source: PomBase

   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 – 516516Peptidyl-prolyl cis-trans isomerase cyp8
PRO_0000064179

Regions

Domain45 – 10864U-box
Domain274 – 428155PPIase cyclophilin-type
Coiled coil433 – 46129 Potential
Compositional bias502 – 5054Poly-Lys

Sequences

Sequence LengthMass (Da)Tools
Q09928 [UniParc].

Last modified June 13, 2006. Version 3.
Checksum: ED4B90E68B4A01D4

FASTA51658,626
        10         20         30         40         50         60 
MGKNTDKLYI TQTEHSGVHG WHGGMSGIAQ KNSTTSYKQL PFNYCSLSLQ PFNHPCCLVD 

        70         80         90        100        110        120 
ETKQAIIFDF RFIVPWLRKH GTNPINGQKA SMSDLIKLKF AKNSAEEYCD PVTMKSFTRF 

       130        140        150        160        170        180 
SHIVAIRSTG NCFSWDTIER LNIKPKHWRD LVNEEQFTRD DIITIQDPHN VENRDFSAIQ 

       190        200        210        220        230        240 
KQKETARDEK ITKAKIALQA SRAKSTESTS SPELSHSLDS SKSIASDMPI HRASHTTGYA 

       250        260        270        280        290        300 
AASLTSTSFT PVTKNERAII AEEDYMLNHT RIKHKGYARI VTNHGEINIE LHTDYAPHAV 

       310        320        330        340        350        360 
YNFVQLAKQG YYRNTIFHRN IARFMIQGGD PSGTGRGGQS IWGKPFKDEF CNPLKHDDRG 

       370        380        390        400        410        420 
IISMANRGKN TNGSQFFILY GPAKHLDNKH TIFGRVVGGL NVLDALEKVP TNSNDHPKLP 

       430        440        450        460        470        480 
IKLEDIIIFV DPFEEWKKDE REKEKRKRQE EEEENNLDRT SWTGRDLSAS STDHSLNASV 

       490        500        510 
GKYLKKEVSL EEKTFTSTVN PKKKKARTGF GNFDAW

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Pemberton T.J.
Submitted (MAY-2006) to UniProtKB
Cited for: SEQUENCE REVISION TO 27, IDENTIFICATION OF FRAMESHIFT.
[3]"The cyclophilin repertoire of the fission yeast Schizosaccharomyces pombe."
Pemberton T.J., Kay J.E.
Yeast 22:927-945(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329670 Genomic DNA. Translation: CAA91964.1. Frameshift.
PIRS62590.
RefSeqNP_594502.2. NM_001019931.3.

3D structure databases

ProteinModelPortalQ09928.
ModBaseSearch...

Protein-protein interaction databases

STRING4896.SPAC21E11.05c-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC21E11.05c.1; SPAC21E11.05c.1:pep; SPAC21E11.05c.
GeneID2541969.
KEGGspo:SPAC21E11.05c.

Organism-specific databases

PomBaseSPAC21E11.05c.

Phylogenomic databases

eggNOGCOG0652.
HOGENOMHOG000177172.
KOK10598.
OMALQPFEYP.
OrthoDBEOG4QVGM8.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR002130. Cyclophilin-like_PPIase_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR026951. PPIL2.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERPTHR11071:SF39. PTHR11071:SF39. 1 hit.
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
SUPFAMSSF50891. CSA_PPIase. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20803051.

Entry information

Entry namePPIL2_SCHPO
AccessionPrimary (citable) accession number: Q09928
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: June 13, 2006
Last modified: May 1, 2013
This is version 96 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

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