methyltransferase-like protein 23 isoform X1 [Benincasa hispida]
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; ... |
47-190 | 3.66e-19 | |||
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 pfam10294: Pssm-ID: 473071 Cd Length: 172 Bit Score: 81.61 E-value: 3.66e-19
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Name | Accession | Description | Interval | E-value | |||
Methyltransf_16 | pfam10294 | Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ... |
47-190 | 3.66e-19 | |||
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins. Pssm-ID: 313513 Cd Length: 172 Bit Score: 81.61 E-value: 3.66e-19
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L-AlaDH | cd05305 | Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
80-118 | 5.38e-03 | |||
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms. Pssm-ID: 240630 [Multi-domain] Cd Length: 359 Bit Score: 37.38 E-value: 5.38e-03
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Name | Accession | Description | Interval | E-value | |||
Methyltransf_16 | pfam10294 | Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ... |
47-190 | 3.66e-19 | |||
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins. Pssm-ID: 313513 Cd Length: 172 Bit Score: 81.61 E-value: 3.66e-19
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L-AlaDH | cd05305 | Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
80-118 | 5.38e-03 | |||
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms. Pssm-ID: 240630 [Multi-domain] Cd Length: 359 Bit Score: 37.38 E-value: 5.38e-03
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Blast search parameters | ||||
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