SMART: Pfam domain RMMBL

The domain within your query sequence starts at position 527 and ends at position 569; the E-value for the RMMBL domain shown below is 1.2e-14.

ESIEIKARVTYIDYEGRSDGDSIKKIINQMKPRQLIIVHGPPE

RMMBL

PFAM accession number:	PF07521
Interpro abstract (IPR011108):	The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in IPR001279 and are common to all metallo-beta-lactamases. This, the fifth motif [ (PUBMED:12177301) ], appears to be specific to Zn-dependent metallohydrolases such as ribonuclease J 2 [ (PUBMED:21764917) ] which are involved in the processing of mRNA [ (PUBMED:17128255) (PUBMED:20544974) ]. This domain adds essential structural elements to the CASP-domain and is unique to RNA/DNA-processing nucleases, showing that they are pre-mRNA 3'-end-processing endonucleases [ (PUBMED:17128255) (PUBMED:20544974) (PUBMED:21764917) ].

PFAM accession number:

PF07521

Interpro abstract (IPR011108):

The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in IPR001279 and are common to all metallo-beta-lactamases. This, the fifth motif [ (PUBMED:12177301) ], appears to be specific to Zn-dependent metallohydrolases such as ribonuclease J 2 [ (PUBMED:21764917) ] which are involved in the processing of mRNA [ (PUBMED:17128255) (PUBMED:20544974) ]. This domain adds essential structural elements to the CASP-domain and is unique to RNA/DNA-processing nucleases, showing that they are pre-mRNA 3'-end-processing endonucleases [ (PUBMED:17128255) (PUBMED:20544974) (PUBMED:21764917) ].

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