DUF862PPPDE putative peptidase domain |
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| SMART accession number: | SM01179
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| Description: |
The PPPDE superfamily (after Permuted Papain fold Peptidases of DsRNA viruses and Eukaryotes), consists of predicted thiol peptidases with a circularly permuted papain-like fold. The inference of the likely DUB function of the PPPDE superfamily proteins is based on the fusions of the catalytic domain to Ub-binding PUG (PUB)/UBA domains and a novel alpha-helical Ub-associated domain (the PUL domain, after PLAP, Ufd3p and Lub1p) (PUBMED:15483401). |
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| Family alignment: |
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There are 437
DUF862 domains in 437 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Iyer LM, Koonin EV, Aravind L
- Novel predicted peptidases with a potential role in the ubiquitin signalingpathway.
- Cell Cycle. 2004; 3: 1440-50
- Display abstract
A multi-pronged strategy including extensive sequence searches, structuralmodeling, and analysis of contextual information extracted from domainarchitectures, genetic screens, and large-scale protein-protein interactionanalyses was employed to predict previously undetected components of theeukaryotic ubiquitin (Ub) signaling system. Two novel groups of proteins that arelikely to function as de-ubiquitinating and de-SUMOylating peptidases (DUBs) wereidentified. The first group of putative DUBs, designated PPPDE superfamily (afterPermuted Papain fold Peptidases of DsRNA viruses and Eukaryotes), consists ofpredicted thiol peptidases with a circularly permuted papain-like fold. Theinference of the likely DUB function of the PPPDE superfamily proteins is basedon the fusions of the catalytic domain to Ub-binding PUG (PUB)/UBA domains and a novel alpha-helical Ub-associated domain (the PUL domain, after PLAP, Ufd3p andLub1p). The presence of the PPPDE superfamily proteins in most eukaryoticlineages, including basal ones, such as Giardia, suggests a role indeubiquitination of highly conserved proteins involved in key cellular functions,such as cell cycle control. In addition to eukaryotic proteins, the PPPDEsuperfamily includes predicted proteases from several groups of double-strandedRNA viruses and one single-stranded DNA virus. The apparent recruitment of DUBsfor viral polyprotein processing seems to represent a common theme in evolutionof viruses. The second group of putative DUBs identified in this study is the WLM(Wss1p-like metalloproteases) family of the Zincin-like superfamily ofZn-dependent peptidases, which are linked to the Ub-system by virtue of fusionswith the UB-binding PUG (PUB), Ub-like, and Little Finger domains. Morespecifically, genetic evidence implicates the WLM family in de-SUMOylation. Ifvalidated experimentally, the WLM family proteins will represent the first caseof a Zincin-like metalloprotease involvement in Ub-signaling.
- Structure (3D structures containing this domain)
3D Structures of DUF862 domains in PDB
| PDB code | Main view | Title | | 3ebq |  | Crystal structure of human pppde1 |
- Links (links to other resources describing this domain)
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