P0C1J2 (CWC27_RHIOR) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 23.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Peptidyl-prolyl isomerase cwc27 Short name=PPIase cwc27 EC=5.2.1.8 Alternative name(s): Rotamase cwc27 | ||||
| Gene names |
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| Organism | Rhizopus oryzae (Rhizopus delemar) | ||||
| Taxonomic identifier | 64495 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Fungi incertae sedis › Basal fungal lineages › Mucoromycotina › Mucorales › Mucoraceae › Rhizopus |
Protein attributes
| Sequence length | 524 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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 | |
| Sequence similarities | Belongs to the cyclophilin-type PPIase family. CWC27 subfamily. Contains 1 PPIase cyclophilin-type domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | mRNA processing mRNA splicing |
| Cellular component | Cytoplasm Nucleus Spliceosome |
| Molecular function | Isomerase Rotamase |
| Gene Ontology (GO) | |
| Biological process | RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW mRNA processingInferred from electronic annotation. Source: UniProtKB-KW protein foldingInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell spliceosomal complexInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 524 | 524 | Peptidyl-prolyl isomerase cwc27 | PRO_0000244725 | |||||
Regions | |||||||||
| Domain | 11 – 166 | 156 | PPIase cyclophilin-type | ||||||
| Compositional bias | 183 – 389 | 207 | Glu/Lys-rich | ||||||
| Compositional bias | 482 – 486 | 5 | Poly-Ser | ||||||
| Compositional bias | 488 – 524 | 37 | Arg-rich | ||||||
Sequences
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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 | |
| ProteinModelPortal | P0C1J2. |
| SMR | P0C1J2. Positions 8-172. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| PhylomeDB | P0C1J2. |
Family and domain databases | |
| InterPro | IPR002130. Cyclophilin-like_PPIase_dom. IPR020892. Cyclophilin-type_PPIase_CS. [Graphical view] |
| Gene3D | G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit. |
| Pfam | PF00160. Pro_isomerase. 1 hit. [Graphical view] |
| PRINTS | PR00153. CSAPPISMRASE. |
| SUPFAM | SSF50891. CSA_PPIase. 1 hit. |
| PROSITE | PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CWC27_RHIOR | ||||||||
| Accession | Primary (citable) accession number: P0C1J2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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