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P0C1J2 (CWC27_RHIOR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl isomerase cwc27

Short name=PPIase cwc27
EC=5.2.1.8
Alternative name(s):
Rotamase cwc27
Gene names
Name:cwc27
ORF Names:RO3G_04513
OrganismRhizopus oryzae (Rhizopus delemar)
Taxonomic identifier64495 [NCBI]
Taxonomic lineageEukaryotaFungiFungi incertae sedisBasal fungal lineagesMucoromycotinaMucoralesMucoraceaeRhizopus

Protein attributes

Sequence length524 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. Involved in pre-mRNA splicing By similarity.

Catalytic activity

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

Subunit structure

Associated with the spliceosome By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

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
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 componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

spliceosomal complex

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 – 524524Peptidyl-prolyl isomerase cwc27
PRO_0000244725

Regions

Domain11 – 166156PPIase cyclophilin-type
Compositional bias183 – 389207Glu/Lys-rich
Compositional bias482 – 4865Poly-Ser
Compositional bias488 – 52437Arg-rich

Sequences

Sequence LengthMass (Da)Tools
P0C1J2 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: 087BDD7CF342A2D5

FASTA52461,050
        10         20         30         40         50         60 
MSNIYALEPH TNAKVILHTT SGDIEIELWG KEAPRATRNF IQLCLEGYYD NTIFHRIVPG 

        70         80         90        100        110        120 
FLVQGGDPTG TGQGGESVYE DGFPDEFHSR LRFNRRGLVG VANTGQNDNG SQFFITLDRA 

       130        140        150        160        170        180 
DELTKRHTLF GRVAGDTLFN VMKMTELEID ENERPLYPPR IKRTEIVINP FDDILPRITE 

       190        200        210        220        230        240 
REKRQQKELE KKKMLEEAKK KKAPKKKQLN LLSFGEEAAE LEPPSHTVEK TKMKSAYDFM 

       250        260        270        280        290        300 
ETSAPTPTEL IEELKKPVKE ESTVISEKKD DAKQEEENKK AEEEERKRKK ALEEERKRQK 

       310        320        330        340        350        360 
EEEKKKMQEN TSESRASAIE KLKQDIRNLS KTSSNTSDEL IPKKDKKRSL VELEREKYAS 

       370        380        390        400        410        420 
QKRKKMKKGD DTDVFNKLMS FQKKLSTAKE DEDAAAAKRD QPPCEIHGIP GCESCRDTTQ 

       430        440        450        460        470        480 
DAEEDVSDAG WISHKLIFEK DLKGKDLMKR RETVDDYVVI DPRDREAKAK QEEYERKKGI 

       490        500        510        520 
KSSSSSQRRD RMDHDDKRYR TEKRSRSDRH RRSRSRDRYD DRRR 

« Hide

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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACW02000073 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortalP0C1J2.
SMRP0C1J2. Positions 8-172.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

PhylomeDBP0C1J2.

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 nameCWC27_RHIOR
AccessionPrimary (citable) accession number: P0C1J2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 27, 2006
Last modified: January 25, 2012
This is version 23 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