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29  structures 313  species 1  interaction 449  sequences 4  architectures

Family: ASF1_hist_chap (PF04729)

Summary: ASF1 like histone chaperone

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This is the Wikipedia entry entitled "ASF1 like histone chaperone". More...

ASF1 like histone chaperone Edit Wikipedia article

ASF1_hist_chap
PDB 2io5 EBI.jpg
crystal structure of the cia- histone h3-h4 complex
Identifiers
Symbol ASF1_hist_chap
Pfam PF04729
Pfam clan CL0463
InterPro IPR006818
SCOP 1roc
SUPERFAMILY 1roc

In molecular biology, the ASF1 like histone chaperone family of proteins includes the yeast and human ASF1 proteins. These proteins have histone chaperone activity.[1] ASF1 participates in both the replication-dependent and replication-independent pathways. The three-dimensional structure has been determined as a compact immunoglobulin-like beta sandwich fold topped by three helical linkers.[2]

References[edit]

  1. ^ Daganzo SM, Erzberger JP, Lam WM, Skordalakes E, Zhang R, Franco AA, Brill SJ, Adams PD, Berger JM, Kaufman PD (December 2003). "Structure and function of the conserved core of histone deposition protein Asf1". Curr. Biol. 13 (24): 2148–58. doi:10.1016/j.cub.2003.11.027. PMID 14680630. 
  2. ^ Munakata T, Adachi N, Yokoyama N, Kuzuhara T, Horikoshi M (March 2000). "A human homologue of yeast anti-silencing factor has histone chaperone activity". Genes Cells 5 (3): 221–33. doi:10.1046/j.1365-2443.2000.00319.x. PMID 10759893. 

This article incorporates text from the public domain Pfam and InterPro IPR006818

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

ASF1 like histone chaperone Provide feedback

This family includes the yeast and human ASF1 protein. These proteins have histone chaperone activity [1]. ASF1 participates in both the replication-dependent and replication-independent pathways. The structure three-dimensional has been determined as a a compact immunoglobulin-like beta sandwich fold topped by three helical linkers [2].

Literature references

  1. Munakata T, Adachi N, Yokoyama N, Kuzuhara T, Horikoshi M; , Genes Cells 2000;5:221-233.: A human homologue of yeast anti-silencing factor has histone chaperone activity. PUBMED:10759893 EPMC:10759893

  2. Daganzo SM, Erzberger JP, Lam WM, Skordalakes E, Zhang R, Franco AA, Brill SJ, Adams PD, Berger JM, Kaufman PD; , Curr Biol 2003;13:2148-2158.: Structure and function of the conserved core of histone deposition protein Asf1. PUBMED:14680630 EPMC:14680630

  3. Malay AD, Umehara T, Matsubara K, Padmanabhan B, Yokoyama S; , J Biol Chem. 2008; [Epub ahead of print]: Crystal structures of fission yeast histone chaperone Asf1 complexed with the Hip1 B domain or the Cac2 C-terminus. PUBMED:18334479 EPMC:18334479

  4. Umehara T, Otta Y, Tsuganezawa K, Matsumoto T, Tanaka A, Horikoshi M, Padmanabhan B, Yokoyama S; , Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005;61:971-973.: Purification, crystallization and preliminary X-ray diffraction analysis of the histone chaperone cia1 from fission yeast. PUBMED:16511210 EPMC:16511210

  5. Umehara T, Chimura T, Ichikawa N, Horikoshi M; , Genes Cells. 2002;7:59-73.: Polyanionic stretch-deleted histone chaperone cia1/Asf1p is functional both in vivo and in vitro. PUBMED:11856374 EPMC:11856374

  6. Yamaki M, Umehara T, Chimura T, Horikoshi M; , Genes Cells. 2001;6:1043-1054.: Cell death with predominant apoptotic features in Saccharomyces cerevisiae mediated by deletion of the histone chaperone ASF1/CIA1. PUBMED:11737265 EPMC:11737265


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR006818

This family includes the yeast and human ASF1 protein. These proteins have histone chaperone activity [PUBMED:14680630]. ASF1 participates in both the replication-dependent and replication-independent pathways. The structure three-dimensional has been determined as a compact immunoglobulin-like beta sandwich fold topped by three helical linkers [PUBMED:10759893].

Gene Ontology

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Domain organisation

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Alignments

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  Seed
(24)
Full
(449)
Representative proteomes NCBI
(425)
Meta
(2)
RP15
(115)
RP35
(168)
RP55
(246)
RP75
(308)
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  Seed
(24)
Full
(449)
Representative proteomes NCBI
(425)
Meta
(2)
RP15
(115)
RP35
(168)
RP55
(246)
RP75
(308)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

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Curation and family details

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Curation View help on the curation process

Seed source: Pfam-B_3167 (release 7.5)
Previous IDs: Anti-silence;
Type: Family
Author: Mifsud W
Number in seed: 24
Number in full: 449
Average length of the domain: 145.60 aa
Average identity of full alignment: 53 %
Average coverage of the sequence by the domain: 66.27 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.7 20.7
Trusted cut-off 22.8 23.8
Noise cut-off 20.6 19.9
Model length: 154
Family (HMM) version: 8
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Species distribution

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Interactions

There is 1 interaction for this family. More...

Histone

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 ASF1_hist_chap domain has been found. There are 29 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 seqence.

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