Protein Family Models

These are metalloenzymes that function as the ubiquitin isopeptidase/ deubiquitinase in the ubiquitin-based signaling and protein turnover pathways in eukaryotes [1]. Prokaryotic JAB domains are predicted to have a similar role in their cognates of the ubiquitin modification pathway [2]. The domain is widely found in bacteria, archaea and phages where they are present in several gene contexts in addition to those that correspond to the prokaryotic cognates of the eukaryotic Ub pathway. Other contexts in which JAB domains are present include gene neighbor associations with ubiquitin fold domains in cysteine and siderophore biosynthesis, and phage tail morphogenesis, where they are shown or predicted to process the associated ubiquitin [2,3]. A distinct family, the RadC-like JAB domains are widespread in bacteria and are predicted to function as nucleases [4]. In halophilic archaea the JAB domain shows strong gene-neighborhood associations with a nucleotidyltransferase suggesting a role in nucleotide metabolism [4]. [1]. 12183636. Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Verma R, Aravind L, Oania R, McDonald WH, Yates JR 3rd, Koonin EV, Deshaies RJ;. Science. 2002;298:611-615. [2]. 16859499. The prokaryotic antecedents of the ubiquitin-signaling system and the early evolution of ubiquitin-like beta-grasp domains. Iyer LM, Burroughs AM, Aravind L;. Genome Biol. 2006;7:R60. [3]. 16104727. Reconstitution of a new cysteine biosynthetic pathway in Mycobacterium tuberculosis. Burns KE, Baumgart S, Dorrestein PC, Zhai H, McLafferty FW, Begley TP;. J Am Chem Soc. 2005;127:11602. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

Most members of the NlpC/P60 family are lipoprotein-hydrolyzing enzymes, cleaving the D-gamma-glutamyl-meso-diaminopimelate linkage or N-acetylmuramate-l-alanine linkage. The family includes transglutaminases, papain-like cysteine peptidases, and arylamine acetyltransferases.

Date:

2024-10-16

C40 family peptidase is a cell-wall hydrolase that cleaves peptide cross-bridges between glycan chains and is essential for bacterial growth and viability; typically cleaves the linkage between D-Glu and diaminopimelic acid (or Lys) within peptidoglycan stem peptides; contains a Cys-His-His catalytic triad

Date:

2021-01-08