Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
41-551
1.28e-87
Adaptin N terminal region; This family consists of the N terminal region of various alpha, beta and gamma subunits of the AP-1, AP-2 and AP-3 adaptor protein complexes. The adaptor protein (AP) complexes are involved in the formation of clathrin-coated pits and vesicles. The N-terminal region of the various adaptor proteins (APs) is constant by comparison to the C-terminal which is variable within members of the AP-2 family; and it has been proposed that this constant region interacts with another uniform component of the coated vesicles.
The actual alignment was detected with superfamily member pfam01602:
Pssm-ID: 396262 [Multi-domain] Cd Length: 523 Bit Score: 287.59 E-value: 1.28e-87
Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure ...
727-836
2.87e-28
Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure consisting of a 5 stranded beta-sheet, flanked by one alpha helix on the outer side, and by two alpha helices on the inner side. This domain is required for binding to clathrin, and its subsequent polymerisation. Furthermore, a hydrophobic patch present in the domain also binds to a subset of D-phi-F/W motif-containing proteins that are bound by the alpha-adaptin appendage domain (epsin, AP180, eps15).
:
Pssm-ID: 198088 Cd Length: 111 Bit Score: 109.71 E-value: 2.87e-28
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
41-551
1.28e-87
Adaptin N terminal region; This family consists of the N terminal region of various alpha, beta and gamma subunits of the AP-1, AP-2 and AP-3 adaptor protein complexes. The adaptor protein (AP) complexes are involved in the formation of clathrin-coated pits and vesicles. The N-terminal region of the various adaptor proteins (APs) is constant by comparison to the C-terminal which is variable within members of the AP-2 family; and it has been proposed that this constant region interacts with another uniform component of the coated vesicles.
Pssm-ID: 396262 [Multi-domain] Cd Length: 523 Bit Score: 287.59 E-value: 1.28e-87
Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure ...
727-836
2.87e-28
Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure consisting of a 5 stranded beta-sheet, flanked by one alpha helix on the outer side, and by two alpha helices on the inner side. This domain is required for binding to clathrin, and its subsequent polymerisation. Furthermore, a hydrophobic patch present in the domain also binds to a subset of D-phi-F/W motif-containing proteins that are bound by the alpha-adaptin appendage domain (epsin, AP180, eps15).
Pssm-ID: 198088 Cd Length: 111 Bit Score: 109.71 E-value: 2.87e-28
Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure ...
725-835
1.88e-24
Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure consisting of a 5 stranded beta-sheet, flanked by one alpha helix on the outer side, and by two alpha helices on the inner side. This domain is required for binding to clathrin, and its subsequent polymerization. Furthermore, a hydrophobic patch present in the domain also binds to a subset of D-phi-F/W motif-containing proteins that are bound by the alpha-adaptin appendage domain (epsin, AP180, eps15).
Pssm-ID: 462667 Cd Length: 111 Bit Score: 98.49 E-value: 1.88e-24
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
41-551
1.28e-87
Adaptin N terminal region; This family consists of the N terminal region of various alpha, beta and gamma subunits of the AP-1, AP-2 and AP-3 adaptor protein complexes. The adaptor protein (AP) complexes are involved in the formation of clathrin-coated pits and vesicles. The N-terminal region of the various adaptor proteins (APs) is constant by comparison to the C-terminal which is variable within members of the AP-2 family; and it has been proposed that this constant region interacts with another uniform component of the coated vesicles.
Pssm-ID: 396262 [Multi-domain] Cd Length: 523 Bit Score: 287.59 E-value: 1.28e-87
non-SMC mitotic condensation complex subunit 1; The three non-SMC (structural maintenance of ...
115-287
8.99e-54
non-SMC mitotic condensation complex subunit 1; The three non-SMC (structural maintenance of chromosomes) subunits of the mitotic condensation complex are Cnd1-3. The whole complex is essential for viability and the condensing of chromosomes in mitosis.
Pssm-ID: 463677 [Multi-domain] Cd Length: 162 Bit Score: 183.43 E-value: 8.99e-54
Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure ...
727-836
2.87e-28
Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure consisting of a 5 stranded beta-sheet, flanked by one alpha helix on the outer side, and by two alpha helices on the inner side. This domain is required for binding to clathrin, and its subsequent polymerisation. Furthermore, a hydrophobic patch present in the domain also binds to a subset of D-phi-F/W motif-containing proteins that are bound by the alpha-adaptin appendage domain (epsin, AP180, eps15).
Pssm-ID: 198088 Cd Length: 111 Bit Score: 109.71 E-value: 2.87e-28
Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure ...
725-835
1.88e-24
Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure consisting of a 5 stranded beta-sheet, flanked by one alpha helix on the outer side, and by two alpha helices on the inner side. This domain is required for binding to clathrin, and its subsequent polymerization. Furthermore, a hydrophobic patch present in the domain also binds to a subset of D-phi-F/W motif-containing proteins that are bound by the alpha-adaptin appendage domain (epsin, AP180, eps15).
Pssm-ID: 462667 Cd Length: 111 Bit Score: 98.49 E-value: 1.88e-24
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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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
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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To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
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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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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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