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Probable histone-binding protein Caf1 (Chromatin assembly factor 1 p55 subunit) (CAF-1 p55 subunit) (Nucleosome-remodeling factor 55 kDa subunit) (NURF-55) (dCAF-1)

 CAF1_DROME              Reviewed;         430 AA.
Q24572; A0AP04; Q9VFB4;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 175.
RecName: Full=Probable histone-binding protein Caf1;
AltName: Full=Chromatin assembly factor 1 p55 subunit;
Short=CAF-1 p55 subunit;
AltName: Full=Nucleosome-remodeling factor 55 kDa subunit;
Short=NURF-55;
AltName: Full=dCAF-1;
Name=Caf1; ORFNames=CG4236;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 256-268; 301-313;
322-334 AND 354-376, FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
STAGE.
STRAIN=Canton-S;
PubMed=8887645; DOI=10.1128/MCB.16.11.6149;
Tyler J.K., Bulger M., Kamakaka R.T., Kobayashi R., Kadonaga J.T.;
"The p55 subunit of Drosophila chromatin assembly factor 1 is
homologous to a histone deacetylase-associated protein.";
Mol. Cell. Biol. 16:6149-6159(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL186, ZBMEL191, ZBMEL229,
ZBMEL377, ZBMEL384, ZBMEL398, ZBMEL82, ZBMEL84, and ZBMEL95;
PubMed=16951084; DOI=10.1534/genetics.106.058008;
Proeschel M., Zhang Z., Parsch J.;
"Widespread adaptive evolution of Drosophila genes with sex-biased
expression.";
Genetics 174:893-900(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
PROTEIN SEQUENCE OF 64-80; 256-269; 301-310; 314-339 AND 354-368,
FUNCTION, IDENTIFICATION IN THE NURF COMPLEX, ASSOCIATION WITH
CHROMATIN, AND SUBCELLULAR LOCATION.
PubMed=9419341; DOI=10.1073/pnas.95.1.132;
Martinez-Balbas M.A., Tsukiyama T., Gdula D., Wu C.;
"Drosophila NURF-55, a WD repeat protein involved in histone
metabolism.";
Proc. Natl. Acad. Sci. U.S.A. 95:132-137(1998).
[7]
CHARACTERIZATION OF THE CAF-1 COMPLEX.
PubMed=8524837; DOI=10.1073/pnas.92.25.11726;
Bulger M., Ito T., Kamakaka R.T., Kadonaga J.T.;
"Assembly of regularly spaced nucleosome arrays by Drosophila
chromatin assembly factor 1 and a 56-kDa histone-binding protein.";
Proc. Natl. Acad. Sci. U.S.A. 92:11726-11730(1995).
[8]
CHARACTERIZATION OF THE CAF-1 COMPLEX.
PubMed=8622682; DOI=10.1128/MCB.16.3.810;
Kamakaka R.T., Bulger M., Kaufman P.D., Stillman B., Kadonaga J.T.;
"Postreplicative chromatin assembly by Drosophila and human chromatin
assembly factor 1.";
Mol. Cell. Biol. 16:810-817(1996).
[9]
FUNCTION, AND INTERACTION WITH ISWI AND NURF-38.
PubMed=9784495; DOI=10.1101/gad.12.20.3206;
Gdula D.A., Sandaltzopoulos R., Tsukiyama T., Ossipow V., Wu C.;
"Inorganic pyrophosphatase is a component of the Drosophila nucleosome
remodeling factor complex.";
Genes Dev. 12:3206-3216(1998).
[10]
IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z) AND RPD3.
PubMed=11124122;
Tie F., Furuyama T., Prasad-Sinha J., Jane E., Harte P.J.;
"The Drosophila polycomb group proteins ESC and E(Z) are present in a
complex containing the histone-binding protein p55 and the histone
deacetylase RPD3.";
Development 128:275-286(2001).
[11]
INTERACTION WITH CAF1-105 AND CAF1-180.
PubMed=11533245; DOI=10.1128/MCB.21.19.6574-6584.2001;
Tyler J.K., Collins K.A., Prasad-Sinha J., Amiott E., Bulger M.,
Harte P.J., Kobayashi R., Kadonaga J.T.;
"Interaction between the Drosophila CAF-1 and ASF1 chromatin assembly
factors.";
Mol. Cell. Biol. 21:6574-6584(2001).
[12]
IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z); RPD3 AND
SU(Z)12.
PubMed=12408863; DOI=10.1016/S0092-8674(02)00975-3;
Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., Pirrotta V.;
"Drosophila Enhancer of zeste/ESC complexes have a histone H3
methyltransferase activity that marks chromosomal Polycomb sites.";
Cell 111:185-196(2002).
[13]
IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z) AND SU(Z)12.
PubMed=12408864; DOI=10.1016/S0092-8674(02)00976-5;
Mueller J., Hart C.M., Francis N.J., Vargas M.L., Sengupta A.,
Wild B., Miller E.L., O'Connor M.B., Kingston R.E., Simon J.A.;
"Histone methyltransferase activity of a Drosophila Polycomb group
repressor complex.";
Cell 111:197-208(2002).
[14]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN
THE DREAM COMPLEX.
PubMed=12490953; DOI=10.1038/nature01228;
Beall E.L., Manak J.R., Zhou S., Bell M., Lipsick J.S., Botchan M.R.;
"Role for a Drosophila Myb-containing protein complex in site-specific
DNA replication.";
Nature 420:833-837(2002).
[15]
IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z) AND RPD3.
PubMed=12533794; DOI=10.1002/gene.10173;
Furuyama T., Tie F., Harte P.J.;
"Polycomb group proteins ESC and E(Z) are present in multiple distinct
complexes that undergo dynamic changes during development.";
Genesis 35:114-124(2003).
[16]
IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z); PCL; RPD3 AND
SU(Z)12.
PubMed=12697833; DOI=10.1128/MCB.23.9.3352-3362.2003;
Tie F., Prasad-Sinha J., Birve A., Rasmuson-Lestander A., Harte P.J.;
"A 1-megadalton ESC/E(Z) complex from Drosophila that contains
polycomblike and RPD3.";
Mol. Cell. Biol. 23:3352-3362(2003).
[17]
IDENTIFICATION IN THE NURD COMPLEX, AND SELF-ASSOCIATION.
PubMed=15516265; DOI=10.1186/1471-2199-5-20;
Marhold J., Brehm A., Kramer K.;
"The Drosophila methyl-DNA binding protein MBD2/3 interacts with the
NuRD complex via p55 and MI-2.";
BMC Mol. Biol. 5:20-20(2004).
[18]
IDENTIFICATION IN THE DREAM COMPLEX.
PubMed=15479636; DOI=10.1016/j.cell.2004.09.034;
Korenjak M., Taylor-Harding B., Binne U.K., Satterlee J.S.,
Stevaux O., Aasland R., White-Cooper H., Dyson N., Brehm A.;
"Native E2F/RBF complexes contain Myb-interacting proteins and repress
transcription of developmentally controlled E2F target genes.";
Cell 119:181-193(2004).
[19]
IDENTIFICATION IN THE DREAM COMPLEX.
PubMed=15545624; DOI=10.1101/gad.1255204;
Lewis P.W., Beall E.L., Fleischer T.C., Georlette D., Link A.J.,
Botchan M.R.;
"Identification of a Drosophila Myb-E2F2/RBF transcriptional repressor
complex.";
Genes Dev. 18:2929-2940(2004).
[20]
FUNCTION, AND INTERACTION WITH RBF AND RBF2.
PubMed=15456884; DOI=10.1128/MCB.24.20.9124-9136.2004;
Taylor-Harding B., Binne U.K., Korenjak M., Brehm A., Dyson N.J.;
"p55, the Drosophila ortholog of RbAp46/RbAp48, is required for the
repression of dE2F2/RBF-regulated genes.";
Mol. Cell. Biol. 24:9124-9136(2004).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=17372656; DOI=10.1039/b617545g;
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,
Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
"An integrated chemical, mass spectrometric and computational strategy
for (quantitative) phosphoproteomics: application to Drosophila
melanogaster Kc167 cells.";
Mol. Biosyst. 3:275-286(2007).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- FUNCTION: Core histone-binding subunit that may target chromatin
assembly factors, chromatin remodeling factors and histone
deacetylases to their histone substrates in a manner that is
regulated by nucleosomal DNA. Component of several complexes which
regulate chromatin metabolism. These include the chromatin
assembly factor 1 (CAF-1) complex, which is required for chromatin
assembly following DNA replication and DNA repair; the nucleosome
remodeling and deacetylase complex (the NuRD complex), which
promotes transcriptional repression by histone deacetylation and
nucleosome remodeling; the nucleosome remodeling factor (NURF)
complex, which catalyzes ATP-dependent nucleosome sliding and
facilitates transcription of chromatin; and the polycomb group
(PcG) repressor complex ESC-E(Z), which promotes repression of
homeotic genes during development. Also required for
transcriptional repression of E2F target genes by E2f2 and Rbf or
Rbf2. {ECO:0000269|PubMed:12490953, ECO:0000269|PubMed:15456884,
ECO:0000269|PubMed:8887645, ECO:0000269|PubMed:9419341,
ECO:0000269|PubMed:9784495}.
-!- SUBUNIT: Probably binds directly to helix 1 of the histone fold of
histone H4, a region that is not accessible when H4 is in
chromatin. Self associates. Associates with chromatin. Component
of the CAF-1 complex, composed of Caf1, Caf1-105 and Caf1-180.
Within the CAF-1 complex, Caf1-180 interacts directly with both
Caf1 and Caf1-105. Component of the NuRD complex, composed of at
least Caf1, Mi-2, MTA1-like and Rpd3. Within the NuRD complex,
Caf1 may interact directly with Mi-2, MTA1-like and Rpd3. The NuRD
complex may also associate with the methyl-DNA binding protein
MBD-like via Caf1 and Mi-2. Component of the NURF complex,
composed of Caf1, E(bx), Nurf-38 and Iswi. Component of the
Esc/E(z) complex, composed of Caf1, esc, E(z), Su(z)1, and
possibly Pho1. The Esc/E(z) complex may also associate with Pcl
and Rpd3 during early embryogenesis. Interacts with Rbf and Rbf2.
Component of the DREAM complex at least composed of Myb, Caf1,
mip40, mip120, mip130, E2f2, Dp, Rbf, Rbf2, lin-52, Rpd3 and
l(3)mbt. {ECO:0000269|PubMed:11124122,
ECO:0000269|PubMed:11533245, ECO:0000269|PubMed:12408863,
ECO:0000269|PubMed:12408864, ECO:0000269|PubMed:12490953,
ECO:0000269|PubMed:12533794, ECO:0000269|PubMed:12697833,
ECO:0000269|PubMed:15456884, ECO:0000269|PubMed:15479636,
ECO:0000269|PubMed:15516265, ECO:0000269|PubMed:15545624,
ECO:0000269|PubMed:9419341, ECO:0000269|PubMed:9784495}.
-!- INTERACTION:
Q9V6Q2:cid; NbExp=6; IntAct=EBI-75924, EBI-129287;
P42124:E(z); NbExp=7; IntAct=EBI-75924, EBI-112315;
Q24338:esc; NbExp=11; IntAct=EBI-75924, EBI-88911;
Q94517:Rpd3; NbExp=4; IntAct=EBI-75924, EBI-302197;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8887645,
ECO:0000269|PubMed:9419341}.
-!- DEVELOPMENTAL STAGE: Highest level during early embryogenesis and
then decreases in larvae, pupae and adults.
{ECO:0000269|PubMed:8887645}.
-!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
{ECO:0000305}.
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EMBL; U62388; AAB37257.1; -; mRNA.
EMBL; AM294392; CAL26322.1; -; Genomic_DNA.
EMBL; AM294393; CAL26323.1; -; Genomic_DNA.
EMBL; AM294394; CAL26324.1; -; Genomic_DNA.
EMBL; AM294395; CAL26325.1; -; Genomic_DNA.
EMBL; AM294396; CAL26330.1; -; Genomic_DNA.
EMBL; AM294397; CAL26335.1; -; Genomic_DNA.
EMBL; AM294398; CAL26337.1; -; Genomic_DNA.
EMBL; AM294399; CAL26338.1; -; Genomic_DNA.
EMBL; AM294400; CAL26339.1; -; Genomic_DNA.
EMBL; AM294401; CAL26340.1; -; Genomic_DNA.
EMBL; AM294402; CAL26341.1; -; Genomic_DNA.
EMBL; AM294403; CAL26342.1; -; Genomic_DNA.
EMBL; AE014297; AAF55146.1; -; Genomic_DNA.
EMBL; AY061408; AAL28956.1; -; mRNA.
RefSeq; NP_524354.1; NM_079630.4.
UniGene; Dm.1657; -.
PDB; 2XYI; X-ray; 1.75 A; A=1-430.
PDB; 2YB8; X-ray; 2.30 A; B=1-418.
PDB; 2YBA; X-ray; 2.55 A; A/B=1-418.
PDB; 3C99; X-ray; 2.90 A; A=1-430.
PDB; 3C9C; X-ray; 3.20 A; A=1-430.
PDBsum; 2XYI; -.
PDBsum; 2YB8; -.
PDBsum; 2YBA; -.
PDBsum; 3C99; -.
PDBsum; 3C9C; -.
ProteinModelPortal; Q24572; -.
SMR; Q24572; -.
BioGrid; 66900; 58.
DIP; DIP-23697N; -.
IntAct; Q24572; 25.
MINT; Q24572; -.
STRING; 7227.FBpp0082511; -.
iPTMnet; Q24572; -.
PaxDb; Q24572; -.
PRIDE; Q24572; -.
EnsemblMetazoa; FBtr0083052; FBpp0082511; FBgn0263979.
GeneID; 41836; -.
KEGG; dme:Dmel_CG4236; -.
CTD; 41836; -.
FlyBase; FBgn0263979; Caf1.
eggNOG; KOG0264; Eukaryota.
eggNOG; ENOG410XNU9; LUCA.
GeneTree; ENSGT00570000079069; -.
InParanoid; Q24572; -.
KO; K10752; -.
OrthoDB; EOG091G0A20; -.
PhylomeDB; Q24572; -.
Reactome; R-DME-212300; PRC2 methylates histones and DNA.
Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
Reactome; R-DME-3214815; HDACs deacetylate histones.
Reactome; R-DME-3214847; HATs acetylate histones.
Reactome; R-DME-8943724; Regulation of PTEN gene transcription.
Reactome; R-DME-8951664; Neddylation.
Reactome; R-DME-8953750; Transcriptional Regulation by E2F6.
SignaLink; Q24572; -.
EvolutionaryTrace; Q24572; -.
GenomeRNAi; 41836; -.
PRO; PR:Q24572; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0263979; Expressed in 45 organ(s), highest expression level in embryo.
ExpressionAtlas; Q24572; baseline and differential.
Genevisible; Q24572; DM.
GO; GO:0033186; C:CAF-1 complex; IDA:FlyBase.
GO; GO:0035098; C:ESC/E(Z) complex; IDA:FlyBase.
GO; GO:0035097; C:histone methyltransferase complex; IDA:FlyBase.
GO; GO:0031523; C:Myb complex; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0016581; C:NuRD complex; IDA:FlyBase.
GO; GO:0016589; C:NURF complex; IDA:FlyBase.
GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
GO; GO:0070822; C:Sin3-type complex; IDA:FlyBase.
GO; GO:0005667; C:transcription factor complex; IPI:FlyBase.
GO; GO:0035035; F:histone acetyltransferase binding; ISS:FlyBase.
GO; GO:0042393; F:histone binding; IDA:FlyBase.
GO; GO:0042826; F:histone deacetylase binding; IDA:FlyBase.
GO; GO:0042803; F:protein homodimerization activity; IPI:FlyBase.
GO; GO:0031497; P:chromatin assembly; IDA:FlyBase.
GO; GO:0006342; P:chromatin silencing; IPI:FlyBase.
GO; GO:0006281; P:DNA repair; TAS:FlyBase.
GO; GO:0007307; P:eggshell chorion gene amplification; IC:FlyBase.
GO; GO:0016573; P:histone acetylation; IDA:FlyBase.
GO; GO:0070734; P:histone H3-K27 methylation; IEA:GOC.
GO; GO:0051567; P:histone H3-K9 methylation; IEA:GOC.
GO; GO:0016571; P:histone methylation; IDA:FlyBase.
GO; GO:0000281; P:mitotic cytokinesis; IMP:FlyBase.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:FlyBase.
GO; GO:0006334; P:nucleosome assembly; IDA:FlyBase.
GO; GO:0042766; P:nucleosome mobilization; IDA:FlyBase.
GO; GO:0016584; P:nucleosome positioning; IDA:FlyBase.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:FlyBase.
GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:FlyBase.
GO; GO:0007379; P:segment specification; IMP:FlyBase.
GO; GO:0006351; P:transcription, DNA-templated; IDA:FlyBase.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR022052; Histone-bd_RBBP4_N.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF12265; CAF1C_H4-bd; 1.
Pfam; PF00400; WD40; 5.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 6.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 3.
PROSITE; PS50082; WD_REPEATS_2; 5.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Chromatin regulator; Complete proteome;
Direct protein sequencing; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; WD repeat.
CHAIN 1 430 Probable histone-binding protein Caf1.
/FTId=PRO_0000050895.
REPEAT 126 159 WD 1.
REPEAT 179 210 WD 2.
REPEAT 229 260 WD 3.
REPEAT 275 306 WD 4.
REPEAT 319 350 WD 5.
REPEAT 376 407 WD 6.
MOD_RES 11 11 Phosphoserine.
{ECO:0000269|PubMed:17372656}.
MOD_RES 100 100 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
HELIX 12 35 {ECO:0000244|PDB:2XYI}.
STRAND 36 43 {ECO:0000244|PDB:2XYI}.
STRAND 51 53 {ECO:0000244|PDB:2XYI}.
STRAND 66 73 {ECO:0000244|PDB:2XYI}.
STRAND 77 79 {ECO:0000244|PDB:2XYI}.
STRAND 81 90 {ECO:0000244|PDB:2XYI}.
STRAND 119 129 {ECO:0000244|PDB:2XYI}.
STRAND 132 137 {ECO:0000244|PDB:2XYI}.
STRAND 140 147 {ECO:0000244|PDB:2XYI}.
STRAND 149 151 {ECO:0000244|PDB:2XYI}.
STRAND 153 157 {ECO:0000244|PDB:2XYI}.
HELIX 158 160 {ECO:0000244|PDB:2XYI}.
STRAND 174 178 {ECO:0000244|PDB:2XYI}.
STRAND 187 189 {ECO:0000244|PDB:2XYI}.
STRAND 191 193 {ECO:0000244|PDB:2YB8}.
STRAND 196 200 {ECO:0000244|PDB:2XYI}.
STRAND 206 210 {ECO:0000244|PDB:2XYI}.
HELIX 217 219 {ECO:0000244|PDB:2XYI}.
STRAND 220 222 {ECO:0000244|PDB:2XYI}.
STRAND 224 227 {ECO:0000244|PDB:2XYI}.
STRAND 234 239 {ECO:0000244|PDB:2XYI}.
STRAND 246 251 {ECO:0000244|PDB:2XYI}.
STRAND 254 260 {ECO:0000244|PDB:2XYI}.
STRAND 266 268 {ECO:0000244|PDB:2XYI}.
STRAND 270 274 {ECO:0000244|PDB:2XYI}.
STRAND 280 285 {ECO:0000244|PDB:2XYI}.
STRAND 292 297 {ECO:0000244|PDB:2XYI}.
STRAND 300 306 {ECO:0000244|PDB:2XYI}.
HELIX 307 309 {ECO:0000244|PDB:3C99}.
STRAND 314 318 {ECO:0000244|PDB:2XYI}.
STRAND 324 329 {ECO:0000244|PDB:2XYI}.
STRAND 336 341 {ECO:0000244|PDB:2XYI}.
STRAND 342 344 {ECO:0000244|PDB:2YB8}.
STRAND 347 350 {ECO:0000244|PDB:2XYI}.
HELIX 351 353 {ECO:0000244|PDB:2XYI}.
HELIX 360 365 {ECO:0000244|PDB:2XYI}.
STRAND 370 373 {ECO:0000244|PDB:2XYI}.
STRAND 381 386 {ECO:0000244|PDB:2XYI}.
STRAND 388 390 {ECO:0000244|PDB:2XYI}.
STRAND 393 398 {ECO:0000244|PDB:2XYI}.
STRAND 401 408 {ECO:0000244|PDB:2XYI}.
HELIX 410 413 {ECO:0000244|PDB:2XYI}.
SEQUENCE 430 AA; 48635 MW; 90C5FB959F1660D5 CRC64;
MVDRSDNAAE SFDDAVEERV INEEYKIWKK NTPFLYDLVM THALEWPSLT AQWLPDVTKQ
DGKDYSVHRL ILGTHTSDEQ NHLLIASVQL PSEDAQFDGS HYDNEKGEFG GFGSVCGKIE
IEIKINHEGE VNRARYMPQN ACVIATKTPS SDVLVFDYTK HPSKPEPSGE CQPDLRLRGH
QKEGYGLSWN PNLNGYLLSA SDDHTICLWD INATPKEHRV IDAKNIFTGH TAVVEDVAWH
LLHESLFGSV ADDQKLMIWD TRNNNTSKPS HTVDAHTAEV NCLSFNPYSE FILATGSADK
TVALWDLRNL KLKLHSFESH KDEIFQVQWS PHNETILASS GTDRRLHVWD LSKIGEEQST
EDAEDGPPEL LFIHGGHTAK ISDFSWNPNE PWIICSVSED NIMQVWQMAE NVYNDEEPEI
PASELETNTA


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