HAMAP rule MF_04059
General rule information
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| Accession | MF_04059 |
| Dates | 16-MAR-2017 (Created) 4-JUN-2021 (Last updated, Version 7) |
| Name | ADV_PRO |
| Scope | Viruses; Adenoviridae |
| Template | P03252 (PRO_ADE02) |
| Triggered by |
Propagated annotation
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Identifier, protein and gene names
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| Identifier |
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| Protein name |
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| Gene name |
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Comments
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| Function | Cleaves viral precursor proteins (pTP, pIIIa, pVI, pVII, pVIII, and pX) inside newly assembled particles giving rise to mature virions. Protease complexed to its cofactor slides along the viral DNA to specifically locate and cleave the viral precursors. Mature virions have a weakened organization compared to the unmature virions, thereby facilitating subsequent uncoating. Without maturation, the particle lacks infectivity and is unable to uncoat. Late in adenovirus infection, in the cytoplasm, may participate in the cytoskeleton destruction. Cleaves host cell cytoskeletal keratins K7 and K18. |
| Catalytic activity | Reaction=Cleaves proteins of the adenovirus and its host cell at two consensus sites: -Yaa-Xaa-Gly-Gly-|-Xaa- and -Yaa-Xaa-Gly-Xaa-|-Gly- (in which Yaa is Met, Ile or Leu, and Xaa is any amino acid).; EC=3.4.22.39; |
| Activity regulation | Requires DNA and protease cofactor for maximal activation. Inside nascent virions, becomes partially activated by binding to the viral DNA, allowing it to cleave the cofactor that binds to the protease and fully activates it. Actin, like the viral protease cofactor, seems to act as a cofactor in the cleavage of cytokeratin 18 and of actin itself. |
| Subunit | Interacts with protease cofactor pVI-C; this interaction is necessary for protease activation. |
| Subcellular location | Virion. Host nucleus. Note=Present in about 10 copies per virion. |
| Induction | Expressed in the late phase of the viral replicative cycle. |
| Miscellaneous | All late proteins expressed from the major late promoter are produced by alternative splicing and alternative polyadenylation of the same gene giving rise to non-overlapping ORFs. A leader sequence is present in the N-terminus of all these mRNAs and is recognized by the viral shutoff protein to provide expression although conventional translation via ribosome scanning from the cap has been shut off in the host cell. |
| Similarity | Belongs to the peptidase C5 family. |
Keywords
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Autocatalytic cleavage
Disulfide bond
DNA-binding
Host nucleus
Hydrolase
Late protein
Protease
Thiol protease
Virion
Disulfide bond
DNA-binding
Host nucleus
Hydrolase
Late protein
Protease
Thiol protease
Virion
Gene Ontology
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GO:0042025; Cellular component: host cell nucleus.
GO:0044423; Cellular component: virion component.
GO:0004197; Molecular function: cysteine-type endopeptidase activity.
GO:0008234; Molecular function: cysteine-type peptidase activity.
GO:0003677; Molecular function: DNA binding.
GO:0044423; Cellular component: virion component.
GO:0004197; Molecular function: cysteine-type endopeptidase activity.
GO:0008234; Molecular function: cysteine-type peptidase activity.
GO:0003677; Molecular function: DNA binding.
Cross-references
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| Pfam | PF00770; Peptidase_C5; 1; |
| PRINTS | PR00703; ADVENDOPTASE; 1; |
| PIRSF | PIRSF001218; Protease_ADV; 1; |
Features
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| From: PRO_ADE02 (P03252) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| ACT_SITE | 54 | 54 | H | |||||||||
| ACT_SITE | 71 | 71 | [DE] | |||||||||
| ACT_SITE | 122 | 122 | C | |||||||||
| SITE | 51 | 52 | Cleavage; by autolysis | G-x | ||||||||
| DISULFID | 104 | 104 | Interchain (with C-10 in cleaved protease cofactor pVI-C) | C | ||||||||
Additional information
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| Size range | 196-214 amino acids |
| Related rules | None |
| Fusion | None |