SMART: Pfam domain Prok-JAB

The domain within your query sequence starts at position 125 and ends at position 258; the E-value for the Prok-JAB domain shown below is 1.2e-9.

LLDFHCHLTRSEVVGYLGGRWDINNQSGYWAWVDKGVTGAGLMASCWYPTVLTVLRAFPC
RSRLGDTDTAATVEEEIYQVLFLRGLSLVGWYHSHPHSPAVPSLQDIDAQMEYQLRLQGS
SNGFQPCLALLCSP

Prok-JAB

PFAM accession number:	PF14464
Interpro abstract (IPR028090):	This entry represents the JAB domain in prokaryotes. The domain is widely found in bacteria, archaea and phages. Its function is still not clear. However, in eukaryotes, JAB domain has been found in metalloenzymes that function as the ubiquitin isopeptidase/deubiquitinase in the ubiquitin-based signaling and protein turnover pathways [ (PUBMED:12183636) ]. Prokaryotic proteins containing JAB domains are predicted to have a similar role in their cognates of the ubiquitin modification pathway [ (PUBMED:16859499) ]. A distinct family, the RadC-like JAB domains are widespread in bacteria and are predicted to function as nucleases [ (PUBMED:21890906) ]. In halophilic archaea, the JAB domain shows strong gene-neighbourhood associations with a nucleotidyltransferase suggesting a role in nucleotide metabolism [ (PUBMED:21890906) ]. The archaeal (H. volcanii) JAB (also known as JAMM) domain containing protein, HvJAMM1, has been characterised [ (PUBMED:22970855) ]. It cleaves ubiquitin-like small archaeal modifier proteins (SAMP1/2) from protein conjugates [ (PUBMED:22970855) ].

PFAM accession number:

PF14464

Interpro abstract (IPR028090):

This entry represents the JAB domain in prokaryotes. The domain is widely found in bacteria, archaea and phages. Its function is still not clear. However, in eukaryotes, JAB domain has been found in metalloenzymes that function as the ubiquitin isopeptidase/deubiquitinase in the ubiquitin-based signaling and protein turnover pathways [ (PUBMED:12183636) ]. Prokaryotic proteins containing JAB domains are predicted to have a similar role in their cognates of the ubiquitin modification pathway [ (PUBMED:16859499) ]. A distinct family, the RadC-like JAB domains are widespread in bacteria and are predicted to function as nucleases [ (PUBMED:21890906) ]. In halophilic archaea, the JAB domain shows strong gene-neighbourhood associations with a nucleotidyltransferase suggesting a role in nucleotide metabolism [ (PUBMED:21890906) ].

The archaeal (H. volcanii) JAB (also known as JAMM) domain containing protein, HvJAMM1, has been characterised [ (PUBMED:22970855) ]. It cleaves ubiquitin-like small archaeal modifier proteins (SAMP1/2) from protein conjugates [ (PUBMED:22970855) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Prok-JAB