Vitellinogen, open beta-sheet; This entry represents the open beta-sheet domain found in ...
695-883
1.61e-13
Vitellinogen, open beta-sheet; This entry represents the open beta-sheet domain found in vitellinogen, which generally corresponds to a domain within the lipovitellin-1 peptide product. This domain adopts a structure consisting of several large open beta-sheets.
The actual alignment was detected with superfamily member pfam19444:
Pssm-ID: 472237 Cd Length: 258 Bit Score: 71.34 E-value: 1.61e-13
Lipoprotein amino terminal region; This family contains regions from: Vitellogenin, Microsomal ...
103-494
1.83e-19
Lipoprotein amino terminal region; This family contains regions from: Vitellogenin, Microsomal triglyceride transfer protein and apolipoprotein B-100. These proteins are all involved in lipid transport. This family contains the LV1n chain from lipovitellin, that contains two structural domains.
Pssm-ID: 460170 [Multi-domain] Cd Length: 582 Bit Score: 93.11 E-value: 1.83e-19
MTP large subunit, lipid-binding domain; Microsomal triglyceride transfer protein (MTP) is ...
695-883
1.61e-13
MTP large subunit, lipid-binding domain; Microsomal triglyceride transfer protein (MTP) is essential in lipid metabolism, especially in the biogenesis of very low-density lipoproteins and chylomicrons via the transfer of neutral lipids and the assembly of apoB-containing lipoproteins. It is a heterodimer consisting of a large MTP alpha-subunit and a protein disulfide isomerase (PDI) beta-subunit. The MTP large subunit has and N-terminal beta-barrel domain, a central alpha-helical domain and a C-terminal 2-beta-sheet domain. This is the highly conserved MTP C-terminal domain involved in lipid-binding and transfer activity, with preference of neutral 3 chain-containing lipids. The beta-sheets are named A and C and form a sandwich comprising the lipid-binding site between them. Half of the A-sheet interacts with the beta-barrel. This domain also interacts with a' and b' domains of PDI.
Pssm-ID: 466086 Cd Length: 258 Bit Score: 71.34 E-value: 1.61e-13
Lipoprotein amino terminal region; This family contains regions from: Vitellogenin, Microsomal ...
103-494
1.83e-19
Lipoprotein amino terminal region; This family contains regions from: Vitellogenin, Microsomal triglyceride transfer protein and apolipoprotein B-100. These proteins are all involved in lipid transport. This family contains the LV1n chain from lipovitellin, that contains two structural domains.
Pssm-ID: 460170 [Multi-domain] Cd Length: 582 Bit Score: 93.11 E-value: 1.83e-19
MTP large subunit, lipid-binding domain; Microsomal triglyceride transfer protein (MTP) is ...
695-883
1.61e-13
MTP large subunit, lipid-binding domain; Microsomal triglyceride transfer protein (MTP) is essential in lipid metabolism, especially in the biogenesis of very low-density lipoproteins and chylomicrons via the transfer of neutral lipids and the assembly of apoB-containing lipoproteins. It is a heterodimer consisting of a large MTP alpha-subunit and a protein disulfide isomerase (PDI) beta-subunit. The MTP large subunit has and N-terminal beta-barrel domain, a central alpha-helical domain and a C-terminal 2-beta-sheet domain. This is the highly conserved MTP C-terminal domain involved in lipid-binding and transfer activity, with preference of neutral 3 chain-containing lipids. The beta-sheets are named A and C and form a sandwich comprising the lipid-binding site between them. Half of the A-sheet interacts with the beta-barrel. This domain also interacts with a' and b' domains of PDI.
Pssm-ID: 466086 Cd Length: 258 Bit Score: 71.34 E-value: 1.61e-13
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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