phospholipase B family protein may catalyze the hydrolytic cleavage of acylester bonds in glycerophospholipids; similar to Drosophila melanogaster phospholipase B-like lamina ancestor involved in the regulation of cellular plasticity in imaginal disks
Phospholipase B; Phospholipase B (PLB) catalyzes the hydrolytic cleavage of both acylester ...
78-654
2.57e-99
Phospholipase B; Phospholipase B (PLB) catalyzes the hydrolytic cleavage of both acylester bonds of glycerophospholipids. This family of PLB enzymes has been identified in mammals, flies and nematodes but not in yeast. In Drosophila this protein was named LAMA for laminin ancestor since it is expressed in the neuronal and glial precursors that surround the lamina.
The actual alignment was detected with superfamily member pfam04916:
Pssm-ID: 461479 Cd Length: 483 Bit Score: 312.34 E-value: 2.57e-99
Phospholipase B; Phospholipase B (PLB) catalyzes the hydrolytic cleavage of both acylester ...
78-654
2.57e-99
Phospholipase B; Phospholipase B (PLB) catalyzes the hydrolytic cleavage of both acylester bonds of glycerophospholipids. This family of PLB enzymes has been identified in mammals, flies and nematodes but not in yeast. In Drosophila this protein was named LAMA for laminin ancestor since it is expressed in the neuronal and glial precursors that surround the lamina.
Pssm-ID: 461479 Cd Length: 483 Bit Score: 312.34 E-value: 2.57e-99
Phospholipase B; Phospholipase B (PLB) catalyzes the hydrolytic cleavage of both acylester ...
78-654
2.57e-99
Phospholipase B; Phospholipase B (PLB) catalyzes the hydrolytic cleavage of both acylester bonds of glycerophospholipids. This family of PLB enzymes has been identified in mammals, flies and nematodes but not in yeast. In Drosophila this protein was named LAMA for laminin ancestor since it is expressed in the neuronal and glial precursors that surround the lamina.
Pssm-ID: 461479 Cd Length: 483 Bit Score: 312.34 E-value: 2.57e-99
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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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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(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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(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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