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Protein

Peptidyl-prolyl cis-trans isomerase cyp6

Gene

cyp6

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. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

  • protein folding Source: InterPro
  • regulation of phosphorylation of RNA polymerase II C-terminal domain Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase cyp6 (EC:5.2.1.8)
Short name:
PPIase cyp6
Alternative name(s):
Rotamase cyp6
Gene namesi
Name:cyp6
ORF Names:SPBC17G9.05
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC17G9.05.
PomBaseiSPBC17G9.05.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • mitotic spindle pole body Source: PomBase
  • nuclear chromatin Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Peptidyl-prolyl cis-trans isomerase cyp6PRO_0000232980Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei206 – 2061Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UUE4.

PTM databases

iPTMnetiQ9UUE4.

Expressioni

Inductioni

Induced during the meiotic cycle.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi276486. 1 interaction.
MINTiMINT-4712691.

Structurei

3D structure databases

ProteinModelPortaliQ9UUE4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 168168PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST
Domaini244 – 32279RRMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi325 – 432108Arg-richAdd
BLAST

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000186284.
InParanoidiQ9UUE4.
KOiK12735.
OMAiDPYPDPA.
OrthoDBiEOG7CK3HG.
PhylomeDBiQ9UUE4.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF50891. SSF50891. 1 hit.
SSF54928. SSF54928. 1 hit.
PROSITEiPS50072. CSA_PPIASE_2. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UUE4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVLIETTVG DLVIDLFVKE APKTCENFLK LCKLKYYNFC PFYNIQHNYT
60 70 80 90 100
CQTGDPLGPT GDGGRCVWNV LNKGTRFFKA EFNPSLVHNK MGLVSMSTAT
110 120 130 140 150
ISSRDDKLLV CGSQFIITLS DNLEGLDERY PIYGQVAEGF DTLLKINDAI
160 170 180 190 200
CDEEGQPYRD IRIKHTIILD DPFEDPPDLV EPLRSPSPTP EQLATVRIGE
210 220 230 240 250
NEQIESETSE DKLQREKEME AEAEAVTLEM IGDLPFAHVA PPENVLFVCK
260 270 280 290 300
LNPVTQDEDL ELIFSRFGKI ISCQVIRDKE TGDSLQYAFI EFDNKESVEK
310 320 330 340 350
AYFKMQNVLI DDSRIHVDFS QSVARYRQYY NSNRDRKRSS SRSDDREYHR
360 370 380 390 400
RSDGRYDRSN YRDDYRHRRK ERDHRDDQSS FRNERFSNYY GDDRSYHKRR
410 420 430
NTGNKNCDDH LRDKSPERRY RYDRRYRDDR YR
Length:432
Mass (Da):50,776
Last modified:May 1, 2000 - v1
Checksum:i16FE19301626561C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB52803.1.
PIRiT39728.
RefSeqiNP_595894.1. NM_001021801.2.

Genome annotation databases

EnsemblFungiiSPBC17G9.05.1; SPBC17G9.05.1:pep; SPBC17G9.05.
GeneIDi2539942.
KEGGispo:SPBC17G9.05.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB52803.1.
PIRiT39728.
RefSeqiNP_595894.1. NM_001021801.2.

3D structure databases

ProteinModelPortaliQ9UUE4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276486. 1 interaction.
MINTiMINT-4712691.

PTM databases

iPTMnetiQ9UUE4.

Proteomic databases

MaxQBiQ9UUE4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC17G9.05.1; SPBC17G9.05.1:pep; SPBC17G9.05.
GeneIDi2539942.
KEGGispo:SPBC17G9.05.

Organism-specific databases

EuPathDBiFungiDB:SPBC17G9.05.
PomBaseiSPBC17G9.05.

Phylogenomic databases

HOGENOMiHOG000186284.
InParanoidiQ9UUE4.
KOiK12735.
OMAiDPYPDPA.
OrthoDBiEOG7CK3HG.
PhylomeDBiQ9UUE4.

Miscellaneous databases

PROiQ9UUE4.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF50891. SSF50891. 1 hit.
SSF54928. SSF54928. 1 hit.
PROSITEiPS50072. CSA_PPIASE_2. 1 hit.
PS50102. RRM. 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. "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.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiPPIL4_SCHPO
AccessioniPrimary (citable) accession number: Q9UUE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 107 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.