extracellular exonuclease ExeM; ExeM, as described in Shewanella oneidensis, is a biofilm ...
1-861
0e+00
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.
The actual alignment was detected with superfamily member NF033680:
Pssm-ID: 468138 [Multi-domain] Cd Length: 883 Bit Score: 1493.53 E-value: 0e+00
extracellular exonuclease ExeM; ExeM, as described in Shewanella oneidensis, is a biofilm ...
1-861
0e+00
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.
Pssm-ID: 468138 [Multi-domain] Cd Length: 883 Bit Score: 1493.53 E-value: 0e+00
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
468-842
9.19e-22
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.
Pssm-ID: 197338 [Multi-domain] Cd Length: 266 Bit Score: 95.93 E-value: 9.19e-22
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
22-129
4.85e-17
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.
Pssm-ID: 460003 [Multi-domain] Cd Length: 108 Bit Score: 77.46 E-value: 4.85e-17
extracellular exonuclease ExeM; ExeM, as described in Shewanella oneidensis, is a biofilm ...
1-861
0e+00
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.
Pssm-ID: 468138 [Multi-domain] Cd Length: 883 Bit Score: 1493.53 E-value: 0e+00
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
468-842
9.19e-22
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.
Pssm-ID: 197338 [Multi-domain] Cd Length: 266 Bit Score: 95.93 E-value: 9.19e-22
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
22-129
4.85e-17
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.
Pssm-ID: 460003 [Multi-domain] Cd Length: 108 Bit Score: 77.46 E-value: 4.85e-17
YhcR_OBF_like: A subfamily of OB-fold domains similar to the OB folds of Bacillus subtilis ...
228-295
5.93e-17
YhcR_OBF_like: A subfamily of OB-fold domains similar to the OB folds of Bacillus subtilis YhcR. YhcR is a sugar-nonspecific nuclease, which is active in the presence of Ca2+ and Mn2+. It cleaves RNA endonucleolytically, producing 3'-monophosphate nucleosides. YhcR appears to be the major Ca2+ activated nuclease of B. subtilis. YhcR may be localized in the cell wall.
Pssm-ID: 239932 [Multi-domain] Cd Length: 78 Bit Score: 76.15 E-value: 5.93e-17
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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