GDSL/SGNH-like Acyl-Esterase family found in Pmr5 and Cas1p; The PC-Esterase family is ...
123-406
1.67e-112
GDSL/SGNH-like Acyl-Esterase family found in Pmr5 and Cas1p; The PC-Esterase family is comprised of Cas1p, the Homo sapiens C7orf58, Arabidopsis thaliana PMR5 and a group of plant freezing resistance/cold acclimatization proteins typified by Arabidopsis thaliana ESKIMO1, animal FAM55D proteins, and animal FAM113 proteins. The PC-Esterase family has features that are both similar and different from the canonical GDSL/SGNH superfamily. The members of this family are predicted to have Acyl esterase activity and predicted to modify cell-surface biopolymers such as glycans and glycoproteins. The Cas1p protein has a Cas1_AcylT domain, in addition, with the opposing acyltransferase activity. The C7orf58 family has a ATP-Grasp domain fused to the PC-Esterase and is the first identified secreted tubulin-tyrosine ligase like enzyme in eukaryotes. The plant family with PMR5, ESK1, TBL3 etc have a N-terminal C rich potential sugar binding domain followed by PC-Esterase domain.
:
Pssm-ID: 463996 Cd Length: 281 Bit Score: 331.08 E-value: 1.67e-112
PMR5 N terminal Domain; The plant family with PMR5, ESK1, TBL3 etc have a N-terminal C rich ...
69-122
2.12e-29
PMR5 N terminal Domain; The plant family with PMR5, ESK1, TBL3 etc have a N-terminal C rich predicted sugar binding domain followed by the PC-Esterase (acyl esterase) domain.
:
Pssm-ID: 464168 [Multi-domain] Cd Length: 54 Bit Score: 108.34 E-value: 2.12e-29
GDSL/SGNH-like Acyl-Esterase family found in Pmr5 and Cas1p; The PC-Esterase family is ...
123-406
1.67e-112
GDSL/SGNH-like Acyl-Esterase family found in Pmr5 and Cas1p; The PC-Esterase family is comprised of Cas1p, the Homo sapiens C7orf58, Arabidopsis thaliana PMR5 and a group of plant freezing resistance/cold acclimatization proteins typified by Arabidopsis thaliana ESKIMO1, animal FAM55D proteins, and animal FAM113 proteins. The PC-Esterase family has features that are both similar and different from the canonical GDSL/SGNH superfamily. The members of this family are predicted to have Acyl esterase activity and predicted to modify cell-surface biopolymers such as glycans and glycoproteins. The Cas1p protein has a Cas1_AcylT domain, in addition, with the opposing acyltransferase activity. The C7orf58 family has a ATP-Grasp domain fused to the PC-Esterase and is the first identified secreted tubulin-tyrosine ligase like enzyme in eukaryotes. The plant family with PMR5, ESK1, TBL3 etc have a N-terminal C rich potential sugar binding domain followed by PC-Esterase domain.
Pssm-ID: 463996 Cd Length: 281 Bit Score: 331.08 E-value: 1.67e-112
PMR5 N terminal Domain; The plant family with PMR5, ESK1, TBL3 etc have a N-terminal C rich ...
69-122
2.12e-29
PMR5 N terminal Domain; The plant family with PMR5, ESK1, TBL3 etc have a N-terminal C rich predicted sugar binding domain followed by the PC-Esterase (acyl esterase) domain.
Pssm-ID: 464168 [Multi-domain] Cd Length: 54 Bit Score: 108.34 E-value: 2.12e-29
GDSL/SGNH-like Acyl-Esterase family found in Pmr5 and Cas1p; The PC-Esterase family is ...
123-406
1.67e-112
GDSL/SGNH-like Acyl-Esterase family found in Pmr5 and Cas1p; The PC-Esterase family is comprised of Cas1p, the Homo sapiens C7orf58, Arabidopsis thaliana PMR5 and a group of plant freezing resistance/cold acclimatization proteins typified by Arabidopsis thaliana ESKIMO1, animal FAM55D proteins, and animal FAM113 proteins. The PC-Esterase family has features that are both similar and different from the canonical GDSL/SGNH superfamily. The members of this family are predicted to have Acyl esterase activity and predicted to modify cell-surface biopolymers such as glycans and glycoproteins. The Cas1p protein has a Cas1_AcylT domain, in addition, with the opposing acyltransferase activity. The C7orf58 family has a ATP-Grasp domain fused to the PC-Esterase and is the first identified secreted tubulin-tyrosine ligase like enzyme in eukaryotes. The plant family with PMR5, ESK1, TBL3 etc have a N-terminal C rich potential sugar binding domain followed by PC-Esterase domain.
Pssm-ID: 463996 Cd Length: 281 Bit Score: 331.08 E-value: 1.67e-112
PMR5 N terminal Domain; The plant family with PMR5, ESK1, TBL3 etc have a N-terminal C rich ...
69-122
2.12e-29
PMR5 N terminal Domain; The plant family with PMR5, ESK1, TBL3 etc have a N-terminal C rich predicted sugar binding domain followed by the PC-Esterase (acyl esterase) domain.
Pssm-ID: 464168 [Multi-domain] Cd Length: 54 Bit Score: 108.34 E-value: 2.12e-29
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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of your query sequence and the protein sequences used to curate the domain model,
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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
Click on the triangle for interactive 3D structure viewing options.
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.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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Domains are color coded according to superfamilies
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Others (non-specific hits) and
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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.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
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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.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
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
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
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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