transferase family protein such as Penicillium simplicissimum O-acetyltransferase ptmV, Arabidopsis thaliana protein ENHANCED PSEUDOMONAS SUSCEPTIBILITY 1, and Triticum aestivum agmatine coumaroyltransferase
Transferase family; This family includes a number of transferase enzymes. These include ...
4-436
1.85e-42
Transferase family; This family includes a number of transferase enzymes. These include anthranilate N-hydroxycinnamoyl/benzoyltransferase that catalyzes the first committed reaction of phytoalexin biosynthesis. Deacetylvindoline 4-O-acetyltransferase EC:2.3.1.107 catalyzes the last step in vindoline biosynthesis is also a member of this family. The motif HXXXD is probably part of the active site. The family also includes trichothecene 3-O-acetyltransferase.
The actual alignment was detected with superfamily member pfam02458:
Pssm-ID: 460564 [Multi-domain] Cd Length: 434 Bit Score: 155.30 E-value: 1.85e-42
Transferase family; This family includes a number of transferase enzymes. These include ...
4-436
1.85e-42
Transferase family; This family includes a number of transferase enzymes. These include anthranilate N-hydroxycinnamoyl/benzoyltransferase that catalyzes the first committed reaction of phytoalexin biosynthesis. Deacetylvindoline 4-O-acetyltransferase EC:2.3.1.107 catalyzes the last step in vindoline biosynthesis is also a member of this family. The motif HXXXD is probably part of the active site. The family also includes trichothecene 3-O-acetyltransferase.
Pssm-ID: 460564 [Multi-domain] Cd Length: 434 Bit Score: 155.30 E-value: 1.85e-42
Transferase family; This family includes a number of transferase enzymes. These include ...
4-436
1.85e-42
Transferase family; This family includes a number of transferase enzymes. These include anthranilate N-hydroxycinnamoyl/benzoyltransferase that catalyzes the first committed reaction of phytoalexin biosynthesis. Deacetylvindoline 4-O-acetyltransferase EC:2.3.1.107 catalyzes the last step in vindoline biosynthesis is also a member of this family. The motif HXXXD is probably part of the active site. The family also includes trichothecene 3-O-acetyltransferase.
Pssm-ID: 460564 [Multi-domain] Cd Length: 434 Bit Score: 155.30 E-value: 1.85e-42
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.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
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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
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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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