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P0C1I9 (CYP11_RHIOR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase cyp11

Short name=PPIase cyp11
EC=5.2.1.8
Alternative name(s):
Cyclophilin cyp11
Rotamase cyp11
Gene names
Name:cyp11
ORF Names:RO3G_13323
OrganismRhizopus oryzae (Rhizopus delemar)
Taxonomic identifier64495 [NCBI]
Taxonomic lineageEukaryotaFungiFungi incertae sedisBasal fungal lineagesMucoromycotinaMucoralesMucoraceaeRhizopus

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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).

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
   Molecular functionIsomerase
Rotamase
Gene Ontology (GO)
   Biological processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 338338Peptidyl-prolyl cis-trans isomerase cyp11
PRO_0000244722

Regions

Domain7 – 172166PPIase cyclophilin-type
Compositional bias217 – 2204Poly-Glu
Compositional bias234 – 2418Poly-Lys

Sequences

Sequence LengthMass (Da)Tools
P0C1I9 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: 4500A1482E987432

FASTA33839,077
        10         20         30         40         50         60 
MINPRVFFDI DVDGNRIGRI VIELFADQVP KTAENFRALC TGEKGIGKVS NMPLHYKGSI 

        70         80         90        100        110        120 
FHRIIKGFMC QGGDFTHRTG KGGESIYGAN FPDESFSRKH DTHGLLSMAN RGPNTQTSQF 

       130        140        150        160        170        180 
FITTRPTPHL DGKHVVFGRV VSGYNVVEMM ENEPVDDQDR PLHNVMIANC GELVLKLPPG 

       190        200        210        220        230        240 
ALLKKASAVS DESEDEIKNR KRSRSSDDDS SSDEDSEEEE RKRTKKKRSR KHSKKDKKKK 

       250        260        270        280        290        300 
KRESSNRKRS PEANRHVSRE RRDISREKRD NSRERRLSRK EDDRRSPSDK RKEDRRSLSP 

       310        320        330 
EKRSSERRVA RPVRPRLNYN DPNVEVKGRG RFKYRPTY 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Rhizopus oryzae RA 99-880."
Lander E.S., Birren B.W., Ma L.-J., Ibrahim A.S., Skory C.D., Wickes B.L., Lang F.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC 9543 / RA 99-880.
[2]Pemberton T.J.
Submitted (MAY-2006) to UniProtKB
Cited for: REVISION OF GENE MODEL.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACW02000245 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortalP0C1I9.
SMRP0C1I9. Positions 3-173.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR002130. Cyclophilin-like_PPIase_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
[Graphical view]
Gene3DG3DSA:2.40.100.10. PPIase_cyclophilin. 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...

Entry information

Entry nameCYP11_RHIOR
AccessionPrimary (citable) accession number: P0C1I9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 27, 2006
Last modified: January 25, 2012
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families