Peptidase M35 family; Family M35 Zn2+-metallopeptidase domain, also known as the deuterolysin ...
1438-1617
6.18e-10
Peptidase M35 family; Family M35 Zn2+-metallopeptidase domain, also known as the deuterolysin family, contains fungal as well as bacterial metalloendopeptidases that include deuterolysin (EC2.4.24.39), peptidyl-Lys metalloendopeptidase (MEP), penicillolysin, as well as uncharacterized sequences. Typically, members of this family of extracellular peptidases contain a unique zinc-binding motif (the aspzincin motif), defined by the HExxH + D motif where an aspartic acid is the third zinc ligand and is found in a GTXDXXYG motif C-terminal to the His zinc ligands. Deuterolysins are highly active towards basic nuclear proteins such as histones and protamines, with a preference for a Lys or Arg residue in the P1' subsite. MEPs specifically cleave peptidyl-lysine bonds (-X-Lys-) in proteins and peptides. Penicillolysin, a thermolabile protease from Penicillium citrinum, strongly hydrolyzes nuclear proteins such as clupeine, salmine and histone. Many members of the M35 peptidases display unusual thermostabilities.
The actual alignment was detected with superfamily member cd11007:
Pssm-ID: 470810 Cd Length: 183 Bit Score: 60.16 E-value: 6.18e-10
Peptidase M35-like domain of uncharacterized proteins; This family contains proteins similar ...
1438-1617
6.18e-10
Peptidase M35-like domain of uncharacterized proteins; This family contains proteins similar to the M35 Zn2+-metallopeptidases, also known as the deuterolysin family, presumably these are bacterial metalloendopeptidases that have yet to be characterized. Typically, members of this family of extracellular peptidases contain a unique zinc-binding motif (the aspzincin motif), defined by the HExxH + D motif where an aspartic acid is the third zinc ligand; however, members of this family do not contain the GTXDXXYG motif C-terminal to the His zinc ligands that is typical for the M35 proteases. Deuterolysins are highly active towards basic nuclear proteins such as histones and protamines, with a preference for a Lys or Arg residue in the P1' subsite. MEPs specifically cleave peptidyl-lysine bonds (-X-Lys-) in proteins and peptides. Many members of the M35 peptidases display unusual thermostabilities.
Pssm-ID: 199913 Cd Length: 183 Bit Score: 60.16 E-value: 6.18e-10
Peptidase M35-like domain of uncharacterized proteins; This family contains proteins similar ...
1438-1617
6.18e-10
Peptidase M35-like domain of uncharacterized proteins; This family contains proteins similar to the M35 Zn2+-metallopeptidases, also known as the deuterolysin family, presumably these are bacterial metalloendopeptidases that have yet to be characterized. Typically, members of this family of extracellular peptidases contain a unique zinc-binding motif (the aspzincin motif), defined by the HExxH + D motif where an aspartic acid is the third zinc ligand; however, members of this family do not contain the GTXDXXYG motif C-terminal to the His zinc ligands that is typical for the M35 proteases. Deuterolysins are highly active towards basic nuclear proteins such as histones and protamines, with a preference for a Lys or Arg residue in the P1' subsite. MEPs specifically cleave peptidyl-lysine bonds (-X-Lys-) in proteins and peptides. Many members of the M35 peptidases display unusual thermostabilities.
Pssm-ID: 199913 Cd Length: 183 Bit Score: 60.16 E-value: 6.18e-10
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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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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specific hits meet or exceed a domain-specific e-value threshold
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