ExeM/NucH family extracellular endonuclease.

Predicted extracellular nuclease [General function prediction only].

Mycoplasma pulmonis MnuA nuclease-like. This subfamily includes Mycoplasma pulmonis MnuA, a membrane-associated nuclease related to Deoxyribonuclease 1 (DNase1 or DNase I, EC 3.1.21.1). The in vivo role of MnuA is as yet undetermined. This subfamily belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.

extracellular exonuclease ExeM. ExeM, as described in Shewanella oneidensis, is a biofilm formation-associated exonuclease that cleaves extracellular DNA (eDNA), a biofilm component. Members of the ExeM family contain two or three pairs of Cys residues, presumed to form disulfide bonds, and a C-terminal GlyGly-CTERM membrane-anchoring segment. Strangely, engineered removal of the GlyGly-CTERM region did not result in net export from the cell and appearance of the enzyme in culture supernatants.

Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1. This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, EEP, domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds. Their substrates range from nucleic acids to phospholipids and perhaps, proteins.