Histone-lysine N-methyltransferase, H3 lysine-79 specific [Caenorhabditis elegans]
Protein Classification
class I SAM-dependent methyltransferase( domain architecture ID 106779)
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
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| AdoMet_MTases super family | cl17173 | S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
140-341 | 1.36e-67 | ||||
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 pfam08123: Pssm-ID: 473071 Cd Length: 205 Bit Score: 212.16 E-value: 1.36e-67
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| Name | Accession | Description | Interval | E-value | ||||
| DOT1 | pfam08123 | Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ... |
140-341 | 1.36e-67 | ||||
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating histone H3. H3 methylation by DOT1 has been shown to be required for the DNA damage checkpoint in yeast. Pssm-ID: 149273 Cd Length: 205 Bit Score: 212.16 E-value: 1.36e-67
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| AdoMet_MTases | cd02440 | S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
180-290 | 2.74e-04 | ||||
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.). Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 40.11 E-value: 2.74e-04
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| Name | Accession | Description | Interval | E-value | ||||
| DOT1 | pfam08123 | Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ... |
140-341 | 1.36e-67 | ||||
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating histone H3. H3 methylation by DOT1 has been shown to be required for the DNA damage checkpoint in yeast. Pssm-ID: 149273 Cd Length: 205 Bit Score: 212.16 E-value: 1.36e-67
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| AdoMet_MTases | cd02440 | S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
180-290 | 2.74e-04 | ||||
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.). Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 40.11 E-value: 2.74e-04
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| Blast search parameters | ||||
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