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Protein

Peptidyl-prolyl cis-trans isomerase cyp8

Gene

cyp8

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

Functioni

May catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides thereby assisting the folding of proteins. May also function as a chaperone, playing a role in intracellular transport of proteins. May also have a protein ubiquitin ligase activity acting as an E3 ubiquitin protein ligase or as a ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on proteins.By similarity

Catalytic activityi

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

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.By similarity
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Ligase, Rotamase

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase cyp8Curated (EC:5.2.1.8By similarity, EC:6.3.2.-By similarity)
Short name:
PPIase cyp8
Alternative name(s):
Rotamase cyp8
Gene namesi
Name:cyp8
ORF Names:SPAC21E11.05c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC21E11.05c.
PomBaseiSPAC21E11.05c. cyp8.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 516516Peptidyl-prolyl cis-trans isomerase cyp8PRO_0000064179Add
BLAST

Proteomic databases

MaxQBiQ09928.

Expressioni

Inductioni

Induced during the meiotic cycle.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi278454. 2 interactions.
MINTiMINT-4696509.

Structurei

3D structure databases

ProteinModelPortaliQ09928.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 11578U-boxAdd
BLAST
Domaini274 – 428155PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili433 – 46129Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi502 – 5054Poly-Lys

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation
Contains 1 U-box domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOGENOMiHOG000177172.
InParanoidiQ09928.
KOiK10598.
OMAiFEYPVCT.
OrthoDBiEOG77HDQ6.
PhylomeDBiQ09928.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR003613. Ubox_domain.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SMARTiSM00504. Ubox. 1 hit.
[Graphical view]
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS51698. U_BOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q09928-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKNTDKLYI TQTEHSGVHG WHGGMSGIAQ KNSTTSYKQL PFNYCSLSLQ
60 70 80 90 100
PFNHPCCLVD ETKQAIIFDF RFIVPWLRKH GTNPINGQKA SMSDLIKLKF
110 120 130 140 150
AKNSAEEYCD PVTMKSFTRF SHIVAIRSTG NCFSWDTIER LNIKPKHWRD
160 170 180 190 200
LVNEEQFTRD DIITIQDPHN VENRDFSAIQ KQKETARDEK ITKAKIALQA
210 220 230 240 250
SRAKSTESTS SPELSHSLDS SKSIASDMPI HRASHTTGYA AASLTSTSFT
260 270 280 290 300
PVTKNERAII AEEDYMLNHT RIKHKGYARI VTNHGEINIE LHTDYAPHAV
310 320 330 340 350
YNFVQLAKQG YYRNTIFHRN IARFMIQGGD PSGTGRGGQS IWGKPFKDEF
360 370 380 390 400
CNPLKHDDRG IISMANRGKN TNGSQFFILY GPAKHLDNKH TIFGRVVGGL
410 420 430 440 450
NVLDALEKVP TNSNDHPKLP IKLEDIIIFV DPFEEWKKDE REKEKRKRQE
460 470 480 490 500
EEEENNLDRT SWTGRDLSAS STDHSLNASV GKYLKKEVSL EEKTFTSTVN
510
PKKKKARTGF GNFDAW
Length:516
Mass (Da):58,626
Last modified:June 13, 2006 - v3
Checksum:iED4B90E68B4A01D4
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA91964.1. Frameshift.
PIRiS62590.
RefSeqiNP_594502.2. NM_001019931.3.

Genome annotation databases

EnsemblFungiiSPAC21E11.05c.1; SPAC21E11.05c.1:pep; SPAC21E11.05c.
GeneIDi2541969.
KEGGispo:SPAC21E11.05c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA91964.1. Frameshift.
PIRiS62590.
RefSeqiNP_594502.2. NM_001019931.3.

3D structure databases

ProteinModelPortaliQ09928.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278454. 2 interactions.
MINTiMINT-4696509.

Proteomic databases

MaxQBiQ09928.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC21E11.05c.1; SPAC21E11.05c.1:pep; SPAC21E11.05c.
GeneIDi2541969.
KEGGispo:SPAC21E11.05c.

Organism-specific databases

EuPathDBiFungiDB:SPAC21E11.05c.
PomBaseiSPAC21E11.05c. cyp8.

Phylogenomic databases

HOGENOMiHOG000177172.
InParanoidiQ09928.
KOiK10598.
OMAiFEYPVCT.
OrthoDBiEOG77HDQ6.
PhylomeDBiQ09928.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

PROiQ09928.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR003613. Ubox_domain.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SMARTiSM00504. Ubox. 1 hit.
[Graphical view]
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS51698. U_BOX. 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. 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.

Entry informationi

Entry nameiPPIL2_SCHPO
AccessioniPrimary (citable) accession number: Q09928
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: June 13, 2006
Last modified: June 8, 2016
This is version 121 of the entry and version 3 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.