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26  structures 403  species 2  interactions 420  sequences 8  architectures

Family: ANAPC_CDC26 (PF10471)

Summary: Anaphase-promoting complex APC subunit CDC26

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Anaphase-promoting complex APC subunit CDC26 Provide feedback

The anaphase-promoting complex (APC) or cyclosome is a cell cycle-regulated ubiquitin-protein ligase that regulates important events in mitosis such as the initiation of anaphase and exit from telophase. The APC, in conjunction with other enzymes, assembles multi-ubiquitin chains on a variety of regulatory proteins thereby targeting them for proteolysis by the 26S proteasome. CDC26 is one of the nine or so subunits identified within APC but its exact function is not known [1]. The APC/C becomes active at the metaphase/anaphase transition and remains active during G1 phase. One mechanism linked to activation of the APC/C is phosphorylation. The yeast APC/C is composed of at least 13 subunits, but the function of many of the subunits is unknown. Hcn1 is the smallest subunit of the S. pombe APC/C, and is found to be essential for cell viability, APC/C integrity, and proper APC/C regulation. In addition, Hcn1 phosphorylation indicates a specific role for the phosphorylation of this subunit late in the cell cycle [2].

Literature references

  1. Gmachl M, Gieffers C, Podtelejnikov AV, Mann M, Peters JM; , Proc Natl Acad Sci U S A. 2000;97:8973-8978.: The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are sufficient to ubiquitinate substrates of the anaphase-promoting complex. PUBMED:10922056 EPMC:10922056

  2. Yoon HJ, Feoktistova A, Chen JS, Jennings JL, Link AJ, Gould KL;, J Biol Chem. 2006;281:32284-32293.: Role of Hcn1 and its phosphorylation in fission yeast anaphase-promoting complex/cyclosome function. PUBMED:16950791 EPMC:16950791


This tab holds annotation information from the InterPro database.

InterPro entry IPR018860

The anaphase-promoting complex (APC) or cyclosome is a multi-subunit E3 protein ubiquitin ligase that regulates important events in mitosis, such as the initiation of anaphase and exit from telophase. The APC, in conjunction with other enzymes, assembles multi-ubiquitin chains on a variety of regulatory proteins, thereby targeting them for proteolysis by the 26S proteasome.

This entry represents subunit CDC26, whose exact function is not known [PUBMED:10922056].

Gene Ontology

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Domain organisation

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Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(37)
Full
(420)
Representative proteomes UniProt
(602)
NCBI
(691)
Meta
(0)
RP15
(87)
RP35
(207)
RP55
(325)
RP75
(426)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(37)
Full
(420)
Representative proteomes UniProt
(602)
NCBI
(691)
Meta
(0)
RP15
(87)
RP35
(207)
RP55
(325)
RP75
(426)
Alignment:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(37)
Full
(420)
Representative proteomes UniProt
(602)
NCBI
(691)
Meta
(0)
RP15
(87)
RP35
(207)
RP55
(325)
RP75
(426)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download    
Gzipped Download   Download   Download   Download   Download   Download   Download   Download    

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

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.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Treefam_TF101057
Previous IDs: APC_CDC26;
Type: Family
Sequence Ontology: SO:0100021
Author: Buljan M , Coggill P
Number in seed: 37
Number in full: 420
Average length of the domain: 75.60 aa
Average identity of full alignment: 24 %
Average coverage of the sequence by the domain: 52.31 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild --amino -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 24.5 24.5
Trusted cut-off 24.5 24.5
Noise cut-off 24.4 24.3
Model length: 74
Family (HMM) version: 9
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 2 interactions for this family. More...

TPR_1 TPR_1

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 ANAPC_CDC26 domain has been found. There are 26 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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