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 ...
1-294
7.31e-132
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: 382.83 E-value: 7.31e-132
Phospholipase B; Phospholipase B (PLB) catalyzes the hydrolytic cleavage of both acylester ...
1-294
7.31e-132
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: 382.83 E-value: 7.31e-132
Phospholipase B; Phospholipase B (PLB) catalyzes the hydrolytic cleavage of both acylester ...
1-294
7.31e-132
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: 382.83 E-value: 7.31e-132
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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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
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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(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
non-specific hits
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the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
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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