Reviewed,
UniProtKB/Swiss-Prot P43232 (CARP5_RHINI)
Last modified
June 16, 2009.
Version 55.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Rhizopuspepsin-5 EC=3.4.23.21 Alternative name(s): Aspartate protease |
| Organism | Rhizopus niveus |
| Taxonomic identifier | 4844 [NCBI] |
| Taxonomic lineage | Eukaryota › Fungi › Fungi incertae sedis › Basal fungal lineages › Mucoromycotina › Mucorales › Mucoraceae › Rhizopus |
Protein attributes
| Sequence length | 392 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1'. Clots milk and activates trypsinogen. Does not cleave 4-Gln-|-His-5, but does cleave 10-His-|-Leu-11 and 12-Val-|-Glu-13 in B chain of insulin. |
| Sequence similarities | Belongs to the peptidase A1 family. |
Ontologies
| Keywords | |
|---|---|
| Domain | Signal |
| Molecular function | Aspartyl protease Hydrolase Protease |
| PTM | Disulfide bond Zymogen |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: InterPro |
| Molecular function | aspartic-type endopeptidase 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 21 | 21 | Potential | ||||||||
| Propeptide | 22 – 69 | 48 | Activation peptide Potential | PRO_0000025891 | |||||||
| Chain | 70 – 392 | 323 | Rhizopuspepsin-5 | PRO_0000025892 | |||||||
Sites | |||||||||||
| Active site | 103 | 1 | By similarity | ||||||||
| Active site | 286 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 116 ↔ 119 | By similarity | |||||||||
| Disulfide bond | 320 ↔ 353 | By similarity | |||||||||
Sequences
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References
| [1] | Horiuchi H., Nakamura H., Okazaki T., Yano K., Takagi M. Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: IFO 4810 / AS 3.4817. |
Cross-references
Sequence databases | |
|---|---|
| X56993 Genomic DNA. Translation: CAA40310.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 2APR based on UniProtKB P06026. |
| SMR | P43232. Positions 70-392. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | A01.012. |
Enzyme and pathway databases | |
| BRENDA | 3.4.23.21. 18853. |
Family and domain databases | |
| InterPro | IPR001461. Peptidase_A1. IPR001969. Peptidase_aspartic_AS. IPR009007. Peptidase_aspartic_catalytic. [Graphical view] |
| Gene3D | G3DSA:2.40.70.10. Pept_Aspartc_cat. 1 hit. |
| PANTHER | PTHR13683. Peptidase_A1. 1 hit. |
| Pfam | PF00026. Asp. 1 hit. [Graphical view] |
| PRINTS | PR00792. PEPSIN. |
| PROSITE | PS00141. ASP_PROTEASE. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CARP5_RHINI | ||||||||
| Accession | Primary (citable) accession number: P43232 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

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