Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
122-312
5.16e-48
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family includes spermidine synthase that catalyzes the fifth (last) step in the biosynthesis of spermidine from arginine, and spermine synthase.
:
Pssm-ID: 396237 [Multi-domain] Cd Length: 183 Bit Score: 159.02 E-value: 5.16e-48
S-adenosylmethionine decarboxylase N -terminal; This is the N-terminal domain found in human ...
21-103
1.62e-23
S-adenosylmethionine decarboxylase N -terminal; This is the N-terminal domain found in human spermine synthase (EC 2.5.1.22). The N-terminal domain, which forms the major part of the dimerization interface, shows a considerable structural similarity to the AdoMetDC-like fold (S-adenosylmethionine decarboxylase, the enzyme that forms the aminopropyl donor substrate), pfam02675. Deletion of the N-terminal domain led to a complete loss of spermine synthase activity, suggesting that dimerization may be required for activity. The N-terminal domain (amino acids 1-117) includes seven beta-strands and two alpha-helices.
The actual alignment was detected with superfamily member pfam17950:
Pssm-ID: 465581 Cd Length: 96 Bit Score: 92.52 E-value: 1.62e-23
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
122-312
5.16e-48
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family includes spermidine synthase that catalyzes the fifth (last) step in the biosynthesis of spermidine from arginine, and spermine synthase.
Pssm-ID: 396237 [Multi-domain] Cd Length: 183 Bit Score: 159.02 E-value: 5.16e-48
S-adenosylmethionine decarboxylase N -terminal; This is the N-terminal domain found in human ...
21-103
1.62e-23
S-adenosylmethionine decarboxylase N -terminal; This is the N-terminal domain found in human spermine synthase (EC 2.5.1.22). The N-terminal domain, which forms the major part of the dimerization interface, shows a considerable structural similarity to the AdoMetDC-like fold (S-adenosylmethionine decarboxylase, the enzyme that forms the aminopropyl donor substrate), pfam02675. Deletion of the N-terminal domain led to a complete loss of spermine synthase activity, suggesting that dimerization may be required for activity. The N-terminal domain (amino acids 1-117) includes seven beta-strands and two alpha-helices.
Pssm-ID: 465581 Cd Length: 96 Bit Score: 92.52 E-value: 1.62e-23
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
83-304
3.17e-10
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine + S-adenosylmethioninamine = spermidine + 5'-methylthioadenosine) and is involved in polyamine biosynthesis and in the biosynthesis of spermidine from arganine. The region between residues 77 and 120 of the seed alignment is thought to be involved in binding to decarboxylated SAM. [Central intermediary metabolism, Polyamine biosynthesis]
Pssm-ID: 188048 [Multi-domain] Cd Length: 271 Bit Score: 59.75 E-value: 3.17e-10
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
153-262
1.21e-03
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: 37.79 E-value: 1.21e-03
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
122-312
5.16e-48
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family includes spermidine synthase that catalyzes the fifth (last) step in the biosynthesis of spermidine from arginine, and spermine synthase.
Pssm-ID: 396237 [Multi-domain] Cd Length: 183 Bit Score: 159.02 E-value: 5.16e-48
S-adenosylmethionine decarboxylase N -terminal; This is the N-terminal domain found in human ...
21-103
1.62e-23
S-adenosylmethionine decarboxylase N -terminal; This is the N-terminal domain found in human spermine synthase (EC 2.5.1.22). The N-terminal domain, which forms the major part of the dimerization interface, shows a considerable structural similarity to the AdoMetDC-like fold (S-adenosylmethionine decarboxylase, the enzyme that forms the aminopropyl donor substrate), pfam02675. Deletion of the N-terminal domain led to a complete loss of spermine synthase activity, suggesting that dimerization may be required for activity. The N-terminal domain (amino acids 1-117) includes seven beta-strands and two alpha-helices.
Pssm-ID: 465581 Cd Length: 96 Bit Score: 92.52 E-value: 1.62e-23
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
83-304
3.17e-10
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine + S-adenosylmethioninamine = spermidine + 5'-methylthioadenosine) and is involved in polyamine biosynthesis and in the biosynthesis of spermidine from arganine. The region between residues 77 and 120 of the seed alignment is thought to be involved in binding to decarboxylated SAM. [Central intermediary metabolism, Polyamine biosynthesis]
Pssm-ID: 188048 [Multi-domain] Cd Length: 271 Bit Score: 59.75 E-value: 3.17e-10
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
153-262
1.21e-03
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: 37.79 E-value: 1.21e-03
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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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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