HMM Summary Page: TIGR03689

Functionproteasome ATPase
Gene Symbolarc
Trusted Cutoff504.75
Domain Trusted Cutoff504.75
Noise Cutoff251.60
Domain Noise Cutoff251.60
Isology Typeequivalog
EC Number3.6.4.8
HMM Length512
Mainrole CategoryProtein fate
Subrole CategoryDegradation of proteins, peptides, and glycopeptides
Gene Ontology TermGO:0000502: proteasome complex cellular_component
GO:0010498: proteasomal protein catabolic process biological_process
GO:0016887: ATPase activity molecular_function
GO:0019941: modification-dependent protein catabolic process biological_process
AuthorHaft DH
Entry DateNov 5 2008 2:44PM
Last ModifiedFeb 14 2011 3:27PM
CommentIn the Actinobacteria, as shown for Mycobacterium tuberculosis, some proteins are modified by ligation between an epsilon-amino group of a lysine side chain and the C-terminal carboxylate of the ubiquitin-like protein Pup. This modification leads to protein degradation by the archaeal-like proteasome found in the Actinobacteria. Members of this protein family belong to the AAA family of ATPases and tend to be clustered with the genes for Pup, the Pup ligase PafA, and structural components of the proteasome. This protein forms hexameric rings with ATPase activity.
ReferencesRN [1] RM PMID:15659170 RT Characterization of a Mycobacterium tuberculosis proteasomal ATPase homologue. RA Darwin KH, Lin G, Chen Z, Li H, Nathan CF RL Mol Microbiol. 2005 Jan;55(2):561-71. RN [2] RM PMID:18980670 RT Unraveling the biochemistry and provenance of pupylation: a prokaryotic analog of ubiquitination. RA Iyer LM, Burroughs AM, Aravind L RL Biol Direct. 2008 Nov 3;3(1):45. RN [3] RM PMID:9765579 RT The 20S proteasome of Streptomyces coelicolor. RA Nagy I, Tamura T, Vanderleyden J, Baumeister W, De Mot R RL J Bacteriol. 1998 Oct;180(20):5448-53.
Genome PropertyGenProp0833: proteasome-targeting modification by pupylation (HMM)