sister chromatid cohesion protein PDS5 is essential for the establishment and maintenance of sister chromatid cohesion at centromere proximal and distal regions during S phase; also required for chromosomal condensation.
Sister chromatid cohesion protein PDS5 protein; This entry represents the Sister chromatid ...
30-1109
0e+00
Sister chromatid cohesion protein PDS5 protein; This entry represents the Sister chromatid cohesion protein PDS5. The large PDS5 molecule is exclusively alpha helical, composed of a large number of HEAT-like repeats and helical extensions/additions that deviate from the HEAT repeat pattern.
:
Pssm-ID: 466319 [Multi-domain] Cd Length: 1051 Bit Score: 789.48 E-value: 0e+00
Sister chromatid cohesion protein PDS5 protein; This entry represents the Sister chromatid ...
30-1109
0e+00
Sister chromatid cohesion protein PDS5 protein; This entry represents the Sister chromatid cohesion protein PDS5. The large PDS5 molecule is exclusively alpha helical, composed of a large number of HEAT-like repeats and helical extensions/additions that deviate from the HEAT repeat pattern.
Pssm-ID: 466319 [Multi-domain] Cd Length: 1051 Bit Score: 789.48 E-value: 0e+00
Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. ...
32-665
7.96e-138
Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. Together with WapI and Scc3, it is involved in the release of the cohesin complex from chromosomes during S phase. The core of the cohesin complex consists of a coiled-coiled heterodimer of Smc1 and Smc30, together with Scc1 (also called kleisin). Pds5 interacts with Scc1 via a conserved patch on the surface of its heat repeats. Pds5 also promotes the acetylation of Smc3 that protects cohesin from releasing activity in G2 phase.
Pssm-ID: 410996 [Multi-domain] Cd Length: 630 Bit Score: 435.80 E-value: 7.96e-138
Sister chromatid cohesion protein PDS5 protein; This entry represents the Sister chromatid ...
30-1109
0e+00
Sister chromatid cohesion protein PDS5 protein; This entry represents the Sister chromatid cohesion protein PDS5. The large PDS5 molecule is exclusively alpha helical, composed of a large number of HEAT-like repeats and helical extensions/additions that deviate from the HEAT repeat pattern.
Pssm-ID: 466319 [Multi-domain] Cd Length: 1051 Bit Score: 789.48 E-value: 0e+00
Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. ...
32-665
7.96e-138
Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. Together with WapI and Scc3, it is involved in the release of the cohesin complex from chromosomes during S phase. The core of the cohesin complex consists of a coiled-coiled heterodimer of Smc1 and Smc30, together with Scc1 (also called kleisin). Pds5 interacts with Scc1 via a conserved patch on the surface of its heat repeats. Pds5 also promotes the acetylation of Smc3 that protects cohesin from releasing activity in G2 phase.
Pssm-ID: 410996 [Multi-domain] Cd Length: 630 Bit Score: 435.80 E-value: 7.96e-138
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
66-398
4.46e-05
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: 47.62 E-value: 4.46e-05
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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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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