Reviewed,
UniProtKB/Swiss-Prot O13340 (CARP_PODAN)
Last modified
November 25, 2008.
Version 39.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
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: Podosporapepsin EC=3.4.23.- | ||
| Gene names |
| ||
| Organism | Podospora anserina | ||
| Taxonomic identifier | 5145 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Lasiosphaeriaceae › Podospora |
Protein attributes
| Sequence length | 425 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Induction | Expressed under carbon starvation conditions. |
| Sequence similarities | Belongs to the peptidase A1 family. |
Ontologies
Keywords | |
|---|---|
| Domain | Signal |
| Molecular function | Aspartyl protease Hydrolase Protease |
| PTM | Cleavage on pair of basic residues Glycoprotein Zymogen |
Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: InterPro |
| Molecular function | aspartic-type endopeptidase activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 28 | 28 | Potential | ||||||||
| Propeptide | 29 – 91 | 63 | Activation peptide By similarity | PRO_0000025877 | |||||||
| Chain | 92 – 425 | 334 | Podosporapepsin | PRO_0000025878 | |||||||
Sites | |||||||||||
| Active site | 126 | 1 | By similarity | ||||||||
| Active site | 310 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 184 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 273 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 370 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 346 ↔ 381 | By similarity | |||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Characterization of a gene from the filamentous fungus Podospora anserina encoding an aspartyl protease induced upon carbon starvation." Paoletti M., Clave C., Begueret J. Gene 210:45-52(1998) [PubMed: 9524217] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AF016054 Genomic DNA. Translation: AAC49997.1. | |
| PIR | JC6557. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GVU based on UniProtKB P11838. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | A01.044. |
Family and domain databases | |
| InterPro | IPR001969. Pept_Asp_AS. IPR009007. Pept_Aspartc_cat. IPR001461. Peptidase_A1. [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 | CARP_PODAN | ||||||||
| Accession | Primary (citable) accession number: O13340 | ||||||||
| 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 |

Clusters with


