Summary: Sister chromatid cohesion protein Dcc1
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Sister chromatid cohesion protein Dcc1 Provide feedback
Sister chromatid cohesion protein Dcc1 is a component of the Ctf18-RFC complex. This complex is required for the efficient establishment of chromosome cohesion during S-phase and for loading the replication clamp Pol30/PCNA, which functions in DNA replication and repair [1,2]. Ctf18-RFC loads PCNA onto DNA in an ATP-dependent manner. It may also have PCNA-unloading activity [3].
Literature references
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Mayer ML, Gygi SP, Aebersold R, Hieter P;, Mol Cell. 2001;7:959-970.: Identification of RFC(Ctf18p, Ctf8p, Dcc1p): an alternative RFC complex required for sister chromatid cohesion in S. cerevisiae. PUBMED:11389843 EPMC:11389843
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Bermudez VP, Maniwa Y, Tappin I, Ozato K, Yokomori K, Hurwitz J;, Proc Natl Acad Sci U S A. 2003;100:10237-10242.: The alternative Ctf18-Dcc1-Ctf8-replication factor C complex required for sister chromatid cohesion loads proliferating cell nuclear antigen onto DNA. PUBMED:12930902 EPMC:12930902
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Bylund GO, Burgers PM;, Mol Cell Biol. 2005;25:5445-5455.: Replication protein A-directed unloading of PCNA by the Ctf18 cohesion establishment complex. PUBMED:15964801 EPMC:15964801
This tab holds annotation information from the InterPro database.
InterPro entry IPR019128
Sister chromatid cohesion protein Dcc1 is a component of the RFC-like complex Ctf18-RFC. This complex is required for the efficient establishment of chromosome cohesion during S-phase and may load or unload Pol30/PCNA. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighbouring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA [ PUBMED:11389843 , PUBMED:15964801 ].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Cellular component | Ctf18 RFC-like complex (GO:0031390) |
Biological process | mitotic sister chromatid cohesion (GO:0007064) |
Domain organisation
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Alignments
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Seed (107) |
Full (1487) |
Representative proteomes | UniProt (2629) |
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RP15 (325) |
RP35 (750) |
RP55 (1180) |
RP75 (1557) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (107) |
Full (1487) |
Representative proteomes | UniProt (2629) |
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RP15 (325) |
RP35 (750) |
RP55 (1180) |
RP75 (1557) |
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Raw Stockholm | |||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
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Curation and family details
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Curation
Seed source: | KOGs (KOG0798) |
Previous IDs: | DUF2036; |
Type: | Family |
Sequence Ontology: | SO:0100021 |
Author: |
KOGs, Finn RD |
Number in seed: | 107 |
Number in full: | 1487 |
Average length of the domain: | 277.00 aa |
Average identity of full alignment: | 22 % |
Average coverage of the sequence by the domain: | 73.49 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 336 | ||||||||||||
Family (HMM) version: | 11 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Dcc1 domain has been found. There are 14 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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