Accession | TIGR03686 |
Name | pupylate_PafA |
Function | Pup--protein ligase |
Gene Symbol | pafA |
Trusted Cutoff | 551.30 |
Domain Trusted Cutoff | 551.30 |
Noise Cutoff | 429.85 |
Domain Noise Cutoff | 429.85 |
Isology Type | equivalog |
EC Number | 6.3.2.- |
HMM Length | 457 |
Mainrole Category | Protein fate |
Subrole Category | Degradation of proteins, peptides, and glycopeptides |
Gene Ontology Term | GO:0010498: proteasomal protein catabolic process biological_process |
| GO:0016879: ligase activity, forming carbon-nitrogen bonds molecular_function |
| GO:0019941: modification-dependent protein catabolic process biological_process |
Author | Haft DH |
Entry Date | Nov 5 2008 9:39AM |
Last Modified | Feb 14 2011 3:27PM |
Comment | Members of this family are the Pup--protein ligase PafA (proteasome accessory factor A), a protein shown to regulate steady-state levels of certain proteasome targets in Mycobacterium tuberculosis. Iyer, et al (2008) first suggested that PafA is the ligase for Pup, a ubiquitin analog attached to an epsilon-amino group of a Lys side-chain to direct the target to the proteasome. |
References | RN [1]
RM PMID:17277063
RT Characterization of the proteasome accessory factor (paf) operon in Mycobacterium tuberculosis.
RA Festa RA, Pearce MJ, Darwin KH
RL J Bacteriol. 2007 Apr;189(8):3044-50.
RN [2]
RM PMID:22910360
RT Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification pathway.
RA Ozcelik D, Barandun J, Schmitz N, Sutter M, Guth E, Damberger FF, Allain FH, Ban N, Weber-Ban E
RL Nat Commun. 2012;3:1014. doi: 10.1038/ncomms2009. |
Genome Property | GenProp0833: proteasome-targeting modification by pupylation (HMM) |