class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to Humulus lupulus xanthohumol 4-O-methyltransferase and O-methyltransferase 3
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
174-367
3.03e-50
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
The actual alignment was detected with superfamily member pfam00891:
Pssm-ID: 473071 [Multi-domain] Cd Length: 208 Bit Score: 167.97 E-value: 3.03e-50
dimerization domain; This domain is found at the N-terminus of a variety of plant ...
48-96
1.97e-07
dimerization domain; This domain is found at the N-terminus of a variety of plant O-methyltransferases. It has been shown to mediate dimerization of these proteins.
:
Pssm-ID: 400439 Cd Length: 50 Bit Score: 47.19 E-value: 1.97e-07
dimerization domain; This domain is found at the N-terminus of a variety of plant ...
48-96
1.97e-07
dimerization domain; This domain is found at the N-terminus of a variety of plant O-methyltransferases. It has been shown to mediate dimerization of these proteins.
Pssm-ID: 400439 Cd Length: 50 Bit Score: 47.19 E-value: 1.97e-07
dimerization domain; This domain is found at the N-terminus of a variety of plant ...
48-96
1.97e-07
dimerization domain; This domain is found at the N-terminus of a variety of plant O-methyltransferases. It has been shown to mediate dimerization of these proteins.
Pssm-ID: 400439 Cd Length: 50 Bit Score: 47.19 E-value: 1.97e-07
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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(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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