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0  structures 376  species 0  interactions 568  sequences 17  architectures

Family: CNDH2_N (PF06278)

Summary: Condensin II complex subunit CAP-H2 or CNDH2, N-terminal

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Condensin II complex subunit CAP-H2 or CNDH2, N-terminal Provide feedback

CNDH2_N is the N-terminal domain of the H2 subunit of the condensing II complex, found in eukaryotes but not in fungi. Eukaryotes carry at least two condensin complexes, I and II, each made up of five subunits. The functions of the two complexes are collaborative but non-overlapping. CI appears to be functional in G2 phase in the cytoplasm beginning the process of chromosomal lateral compaction while the CII is concentrated in the nucleus, possibly to counteract the activity of cohesion at this stage. In prophase, CII contributes to axial shortening of chromatids while CI continues to bring about lateral chromatid compaction, during which time the sister chromatids are joined centrally by cohesins. There appears to be just one condensin complex in fungi. CI and CII each contain SMC2 and SMC4 (structural maintenance of chromosomes) subunits, then CI has non-SMC CAP-D2 (CND1), CAP-G (CND3), and CAP-H (CND2). CII has, in addition to the two SMCs, CAP-D3, CAPG2 and CAP-H2. All four of the CAP-D and CAP-G subunits have degenerate HEAT repeats, whereas the CAP-H are kleisins or SMC-interacting proteins (ie they bind directly to the SMC subunits in the complex). The SMC molecules are each long with a small hinge-like knob at the free end of a longish strand, articulating with each other at the hinge. Each strand ends in a knob-like head that binds to one or other end of the CAP-H subunit. The HEAT-repeat containing D and G subunits bind side-by-side between the ends of the H subunit. Activity of the various parts of the complex seem to be triggered by extensive phosphorylations, eg, entry of the complex, in Sch.pombe, into the nucleus during mitosis is promoted by Cdk1 phosphorylation of SMC4/Cut3; and it has been shown that Cdk1 phosphorylates CAP-D3 at Thr1415 in He-La cells thus promoting early stage chromosomal condensation by CII.

Literature references

  1. Wood AJ, Severson AF, Meyer BJ;, Nat Rev Genet. 2010;11:391-404.: Condensin and cohesin complexity: the expanding repertoire of functions. PUBMED:20442714 EPMC:20442714

  2. Hirano T;, Genes Dev. 2012;26:1659-1678.: Condensins: universal organizers of chromosomes with diverse functions. PUBMED:22855829 EPMC:22855829


Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR009378

This entry represents the N-terminal domain of the H2 subunit of the condensing II complex, found in eukaryotes but not in fungi.

Eukaryotes carry at least two condensin complexes, I and II, each made up of five subunits. The functions of the two complexes are collaborative but non-overlapping. CI appears to be functional in G2 phase in the cytoplasm beginning the process of chromosomal lateral compaction while the CII is concentrated in the nucleus, possibly to counteract the activity of cohesion at this stage. In prophase, CII contributes to axial shortening of chromatids while CI continues to bring about lateral chromatid compaction, during which time the sister chromatids are joined centrally by cohesins. There appears to be just one condensin complex in fungi. CI and CII each contain SMC2 and SMC4 (structural maintenance of chromosomes) subunits, then CI has non-SMC CAP-D2 (CND1), CAP-G (CND3), and CAP-H (CND2). CII has, in addition to the two SMCs, CAP-D3, CAPG2 and CAP-H2. All four of the CAP-D and CAP-G subunits have degenerate HEAT repeats, whereas the CAP-H are kleisins or SMC-interacting proteins (ie they bind directly to the SMC subunits in the complex). The SMC molecules are each long with a small hinge-like knob at the free end of a longish strand, articulating with each other at the hinge. Each strand ends in a knob-like head that binds to one or other end of the CAP-H subunit. The HEAT-repeat containing D and G subunits bind side-by-side between the ends of the H subunit. Activity of the various parts of the complex seem to be triggered by extensive phosphorylations, eg, entry of the complex, in Sch.pombe, into the nucleus during mitosis is promoted by Cdk1 phosphorylation of SMC4/Cut3; and it has been shown that Cdk1 phosphorylates CAP-D3 at Thr1415 in He-La cells thus promoting early stage chromosomal condensation by CII [PUBMED:20442714, PUBMED:22855829].

Domain organisation

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(29)
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  Seed
(29)
Full
(568)
Representative proteomes UniProt
(910)
NCBI
(1426)
Meta
(0)
RP15
(100)
RP35
(238)
RP55
(397)
RP75
(550)
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  Seed
(29)
Full
(568)
Representative proteomes UniProt
(910)
NCBI
(1426)
Meta
(0)
RP15
(100)
RP35
(238)
RP55
(397)
RP75
(550)
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Seed source: Pfam-B_11729 (release 9.0)
Previous IDs: DUF1032;
Type: Family
Sequence Ontology: SO:0100021
Author: Moxon SJ
Number in seed: 29
Number in full: 568
Average length of the domain: 104.00 aa
Average identity of full alignment: 42 %
Average coverage of the sequence by the domain: 16.93 %

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HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 32.3 32.3
Trusted cut-off 32.3 32.6
Noise cut-off 32.1 32.1
Model length: 112
Family (HMM) version: 12
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