O91466 (CATV_GVCPM) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 67.
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: Viral cathepsin Short name=V-cath EC=3.4.22.50 Alternative name(s): Cysteine proteinase Short name=CP | ||||
| Gene names |
| ||||
| Organism | Cydia pomonella granulosis virus (isolate Mexico/1963) (CpGV) (Cydia pomonella granulovirus) [Reference proteome] | ||||
| Taxonomic identifier | 654905 [NCBI] | ||||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Baculoviridae › Betabaculovirus › ![]() | ||||
| Virus host | Cydia pomonella (Codling moth) [TaxID: 82600] |
Protein attributes
| Sequence length | 333 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Cysteine protease that plays an essential role in host liquefaction to facilitate horizontal transmission of the virus. May participate in the degradation of foreign protein expressed by the baculovirus system By similarity. |
| Catalytic activity | Endopeptidase of broad specificity, hydrolyzing substrates of both cathepsin L and cathepsin B. |
| Post-translational modification | Synthesized as an inactive proenzyme and activated by proteolytic removal of the inhibitory propeptide By similarity. |
| Sequence similarities | Belongs to the peptidase C1 family. |
Ontologies
| Keywords | |
|---|---|
| Domain | Signal |
| Molecular function | Hydrolase Protease Thiol protease |
| PTM | Disulfide bond Glycoprotein Zymogen |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | proteolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | cysteine-type peptidase 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 – 20 | 20 | Potential | ||||||||
| Propeptide | 21 – 124 | 104 | Activation peptide Potential | PRO_0000322218 | |||||||
| Chain | 125 – 333 | 209 | Viral cathepsin | PRO_0000050588 | |||||||
Sites | |||||||||||
| Active site | 148 | 1 | By similarity | ||||||||
| Active site | 280 | 1 | By similarity | ||||||||
| Active site | 300 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 170 | 1 | N-linked (GlcNAc...); by host Potential | ||||||||
| Disulfide bond | 145 ↔ 186 | By similarity | |||||||||
| Disulfide bond | 179 ↔ 219 | By similarity | |||||||||
| Disulfide bond | 272 ↔ 321 | By similarity | |||||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Identification and characterization of the Cydia pomonella granulovirus cathepsin and chitinase genes." Kang W., Tristem M., Maeda S., Crook N.E., O'Reilly D.R. J. Gen. Virol. 79:2283-2292(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Mexican 1. |
| [2] | "The complete sequence of the Cydia pomonella granulovirus genome." Luque T., Finch R., Crook N., O'Reilly D.R., Winstanley D. J. Gen. Virol. 82:2531-2547(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Mexican 1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U53466 Genomic DNA. Translation: AAK70678.1. |
| RefSeq | NP_148795.1. NC_002816.1. |
3D structure databases | |
| ProteinModelPortal | O91466. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | C01.047. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 921370. |
Phylogenomic databases | |
| ProtClustDB | CLSP2509984. |
Family and domain databases | |
| InterPro | IPR025661. Pept_asp_AS. IPR000169. Pept_cys_AS. IPR025660. Pept_his_AS. IPR013128. Peptidase_C1A. IPR000668. Peptidase_C1A_C. IPR013201. Prot_inhib_I29. [Graphical view] |
| PANTHER | PTHR12411. PTHR12411. 1 hit. |
| Pfam | PF08246. Inhibitor_I29. 1 hit. PF00112. Peptidase_C1. 1 hit. [Graphical view] |
| PRINTS | PR00705. PAPAIN. |
| SMART | SM00848. Inhibitor_I29. 1 hit. SM00645. Pept_C1. 1 hit. [Graphical view] |
| PROSITE | PS00640. THIOL_PROTEASE_ASN. 1 hit. PS00139. THIOL_PROTEASE_CYS. 1 hit. PS00639. THIOL_PROTEASE_HIS. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CATV_GVCPM | ||||||||
| Accession | Primary (citable) accession number: O91466 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Viral Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
