|SMART accession number:||SM00232|
|Description:||Domain in Jun kinase activation domain binding protein and proteasomal subunits. Domain at Mpr1p and Pad1p N-termini. Domain of unknown function.|
|Interpro abstract (IPR000555):|
This domain is known as the MPN domain [(PUBMED:9644972)], PAD-1-like domain [(PUBMED:10369758)], JABP1 domain [(PUBMED:20838651)] or JAMM domain [(PUBMED:12183636)]. Proteins with this domain include proteasome regulatory subunits, eukaryotic initiation factor 3 (eIF3) subunits and regulators of transcription factors. They are metalloenzymes that function as the ubiquitin isopeptidase/ deubiquitinase in the ubiquitin-based signaling and protein turnover pathways in eukaryotes [(PUBMED:12183636)]. Versions of the domain in prokaryotic cognates of the ubiquitin-modification pathway are predicted to have a similar role [(PUBMED:16859499)].
The archaeal (H. volcanii) JAMM domain containing protein, HvJAMM1, cleaves ubiquitin-like small archaeal modifier proteins (SAMP1/2) from protein conjugates [(PUBMED:22970855)]. The bacterial JAMM domain containing protein QbsD from Pseudomonas fluorescens cleaves the C-terminal amino acid residues of the sulfur carrier protein QbsE prior to the formation of the carboxy-terminal thiocarboxylate [(PUBMED:17209031)].
|GO function:||protein binding (GO:0005515)|
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- Evolution (species in which this domain is found)
- Cellular role (predicted cellular role)
- Literature (relevant references for this domain)
- Metabolism (metabolic pathways involving proteins which contain this domain)
- Structure (3D structures containing this domain)
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