adaptin domain-containing protein is a component of an adaptor protein (AP) complex; similar to Saccharomyces cerevisiae AP-3 complex subunit delta| HEAT repeat domain-containing protein may function as a scaffold, anchoring and/or adaptor protein
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
1-532
3.94e-154
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: 467.48 E-value: 3.94e-154
Clathrin-adaptor complex-3 beta-1 subunit C-terminal; This domain lies at the C-terminus of ...
764-909
2.33e-73
Clathrin-adaptor complex-3 beta-1 subunit C-terminal; This domain lies at the C-terminus of the clathrin-adaptor protein complex-3 beta-1 subunit. The AP-3 complex is associated with the Golgi region of the cell as well as with more peripheral structures. The AP-3 complex may be directly involved in trafficking to lysosomes or alternatively it may be involved in another pathway, but that mis-sorting in that pathway may indirectly lead to defects in pigment granules.
:
Pssm-ID: 464319 Cd Length: 148 Bit Score: 239.09 E-value: 2.33e-73
Serine-rich region of AP3B1, clathrin-adaptor complex; This short low-complexity, highly ...
682-715
3.84e-14
Serine-rich region of AP3B1, clathrin-adaptor complex; This short low-complexity, highly serine-rich region lies on clathrin-adaptor complex 3 beta-1 subunit proteins, between family Adaptin_N, pfam01602 and a C-terminal domain, AP3B1_C,pfam14796.
:
Pssm-ID: 434218 [Multi-domain] Cd Length: 111 Bit Score: 69.57 E-value: 3.84e-14
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
1-532
3.94e-154
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: 467.48 E-value: 3.94e-154
Clathrin-adaptor complex-3 beta-1 subunit C-terminal; This domain lies at the C-terminus of ...
764-909
2.33e-73
Clathrin-adaptor complex-3 beta-1 subunit C-terminal; This domain lies at the C-terminus of the clathrin-adaptor protein complex-3 beta-1 subunit. The AP-3 complex is associated with the Golgi region of the cell as well as with more peripheral structures. The AP-3 complex may be directly involved in trafficking to lysosomes or alternatively it may be involved in another pathway, but that mis-sorting in that pathway may indirectly lead to defects in pigment granules.
Pssm-ID: 464319 Cd Length: 148 Bit Score: 239.09 E-value: 2.33e-73
Serine-rich region of AP3B1, clathrin-adaptor complex; This short low-complexity, highly ...
682-715
3.84e-14
Serine-rich region of AP3B1, clathrin-adaptor complex; This short low-complexity, highly serine-rich region lies on clathrin-adaptor complex 3 beta-1 subunit proteins, between family Adaptin_N, pfam01602 and a C-terminal domain, AP3B1_C,pfam14796.
Pssm-ID: 434218 [Multi-domain] Cd Length: 111 Bit Score: 69.57 E-value: 3.84e-14
Sister chromatid cohesion protein 2 and homologs; This family includes Sister chromatid ...
63-189
9.40e-03
Sister chromatid cohesion protein 2 and homologs; This family includes Sister chromatid cohesion protein 2 (Scc2) and its homolog (Scc2 homolog, also called Nipped-B-like protein or NIPBL). Scc2/NIPBL and Scc4 form a complex that is responsible for loading the cohesin protein onto sister chromatids during mitosis and meiosis. Cohesin is a ring-shaped protein complex that encircles the sister chromatids and helps to hold them together until they are ready to be separated during cell division. In addition to its role in chromosome segregation, cohesin also plays important roles in other cellular processes such as transcription, chromosome condensation, and DNA repair.
Pssm-ID: 467937 [Multi-domain] Cd Length: 1197 Bit Score: 39.97 E-value: 9.40e-03
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
1-532
3.94e-154
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: 467.48 E-value: 3.94e-154
Clathrin-adaptor complex-3 beta-1 subunit C-terminal; This domain lies at the C-terminus of ...
764-909
2.33e-73
Clathrin-adaptor complex-3 beta-1 subunit C-terminal; This domain lies at the C-terminus of the clathrin-adaptor protein complex-3 beta-1 subunit. The AP-3 complex is associated with the Golgi region of the cell as well as with more peripheral structures. The AP-3 complex may be directly involved in trafficking to lysosomes or alternatively it may be involved in another pathway, but that mis-sorting in that pathway may indirectly lead to defects in pigment granules.
Pssm-ID: 464319 Cd Length: 148 Bit Score: 239.09 E-value: 2.33e-73
non-SMC mitotic condensation complex subunit 1; The three non-SMC (structural maintenance of ...
81-202
8.90e-17
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: 78.66 E-value: 8.90e-17
Serine-rich region of AP3B1, clathrin-adaptor complex; This short low-complexity, highly ...
682-715
3.84e-14
Serine-rich region of AP3B1, clathrin-adaptor complex; This short low-complexity, highly serine-rich region lies on clathrin-adaptor complex 3 beta-1 subunit proteins, between family Adaptin_N, pfam01602 and a C-terminal domain, AP3B1_C,pfam14796.
Pssm-ID: 434218 [Multi-domain] Cd Length: 111 Bit Score: 69.57 E-value: 3.84e-14
Sister chromatid cohesion protein 2 and homologs; This family includes Sister chromatid ...
63-189
9.40e-03
Sister chromatid cohesion protein 2 and homologs; This family includes Sister chromatid cohesion protein 2 (Scc2) and its homolog (Scc2 homolog, also called Nipped-B-like protein or NIPBL). Scc2/NIPBL and Scc4 form a complex that is responsible for loading the cohesin protein onto sister chromatids during mitosis and meiosis. Cohesin is a ring-shaped protein complex that encircles the sister chromatids and helps to hold them together until they are ready to be separated during cell division. In addition to its role in chromosome segregation, cohesin also plays important roles in other cellular processes such as transcription, chromosome condensation, and DNA repair.
Pssm-ID: 467937 [Multi-domain] Cd Length: 1197 Bit Score: 39.97 E-value: 9.40e-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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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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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(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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(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
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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