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Database: UniProt
Entry: CHD1_YEAST
LinkDB: CHD1_YEAST
Original site: CHD1_YEAST 
ID   CHD1_YEAST              Reviewed;        1468 AA.
AC   P32657; D3DM72;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   26-FEB-2020, entry version 202.
DE   RecName: Full=Chromo domain-containing protein 1;
DE            EC=3.6.4.-;
DE   AltName: Full=ATP-dependent helicase CHD1;
GN   Name=CHD1; OrderedLocusNames=YER164W; ORFNames=SYGP-ORF4;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX.
RX   PubMed=10026213; DOI=10.1074/jbc.274.9.5895;
RA   Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M., Workman J.L.;
RT   "Expanded lysine acetylation specificity of Gcn5 in native complexes.";
RL   J. Biol. Chem. 274:5895-5900(1999).
RN   [4]
RP   FUNCTION.
RX   PubMed=10811623; DOI=10.1093/emboj/19.10.2323;
RA   Tran H.G., Steger D.J., Iyer V.R., Johnson A.D.;
RT   "The chromo domain protein chd1p from budding yeast is an ATP-dependent
RT   chromatin-modifying factor.";
RL   EMBO J. 19:2323-2331(2000).
RN   [5]
RP   INTERACTION WITH POB3 AND SPT16.
RX   PubMed=12242279; DOI=10.1128/mcb.22.20.6979-6992.2002;
RA   Krogan N.J., Kim M., Ahn S.H., Zhong G., Kobor M.S., Cagney G., Emili A.,
RA   Shilatifard A., Buratowski S., Greenblatt J.F.;
RT   "RNA polymerase II elongation factors of Saccharomyces cerevisiae: a
RT   targeted proteomics approach.";
RL   Mol. Cell. Biol. 22:6979-6992(2002).
RN   [6]
RP   IDENTIFICATION IN THE SLIK COMPLEX.
RX   PubMed=12446794; DOI=10.1128/mcb.22.24.8774-8786.2002;
RA   Pray-Grant M.G., Schieltz D., McMahon S.J., Wood J.M., Kennedy E.L.,
RA   Cook R.G., Workman J.L., Yates J.R. III, Grant P.A.;
RT   "The novel SLIK histone acetyltransferase complex functions in the yeast
RT   retrograde response pathway.";
RL   Mol. Cell. Biol. 22:8774-8786(2002).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RTF1 AND SPT5.
RX   PubMed=12682017; DOI=10.1093/emboj/cdg179;
RA   Simic R., Lindstrom D.L., Tran H.G., Roinick K.L., Costa P.J.,
RA   Johnson A.D., Hartzog G.A., Arndt K.M.;
RT   "Chromatin remodeling protein Chd1 interacts with transcription elongation
RT   factors and localizes to transcribed genes.";
RL   EMBO J. 22:1846-1856(2003).
RN   [8]
RP   FUNCTION.
RX   PubMed=14585955; DOI=10.1128/mcb.23.22.7937-7946.2003;
RA   Robinson K.M., Schultz M.C.;
RT   "Replication-independent assembly of nucleosome arrays in a novel yeast
RT   chromatin reconstitution system involves antisilencing factor Asf1p and
RT   chromodomain protein Chd1p.";
RL   Mol. Cell. Biol. 23:7937-7946(2003).
RN   [9]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [10]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1144, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=SUB592;
RX   PubMed=12872131; DOI=10.1038/nbt849;
RA   Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA   Roelofs J., Finley D., Gygi S.P.;
RT   "A proteomics approach to understanding protein ubiquitination.";
RL   Nat. Biotechnol. 21:921-926(2003).
RN   [11]
RP   IDENTIFICATION IN THE SAGA COMPLEX, IDENTIFICATION IN THE SLIK COMPLEX,
RP   FUNCTION IN SUBSTRATE RECOGNITION OF THE SLIK COMPLEX, INTERACTION WITH
RP   HISTONE H3, AND MUTAGENESIS OF GLU-220; HIS-222; LEU-314 AND TYR-316.
RX   PubMed=15647753; DOI=10.1038/nature03242;
RA   Pray-Grant M.G., Daniel J.A., Schieltz D., Yates J.R. III, Grant P.A.;
RT   "Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-
RT   dependent acetylation.";
RL   Nature 433:434-438(2005).
RN   [12]
RP   FUNCTION.
RX   PubMed=16606615; DOI=10.1074/jbc.m600682200;
RA   Stockdale C., Flaus A., Ferreira H., Owen-Hughes T.;
RT   "Analysis of nucleosome repositioning by yeast ISWI and Chd1 chromatin
RT   remodeling complexes.";
RL   J. Biol. Chem. 281:16279-16288(2006).
RN   [13]
RP   FUNCTION.
RX   PubMed=16468993; DOI=10.1111/j.1365-2958.2005.05031.x;
RA   Xella B., Goding C., Agricola E., Di Mauro E., Caserta M.;
RT   "The ISWI and CHD1 chromatin remodelling activities influence ADH2
RT   expression and chromatin organization.";
RL   Mol. Microbiol. 59:1531-1541(2006).
RN   [14]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=17949749; DOI=10.1016/j.jmb.2007.09.059;
RA   Ferreira H., Flaus A., Owen-Hughes T.;
RT   "Histone modifications influence the action of Snf2 family remodelling
RT   enzymes by different mechanisms.";
RL   J. Mol. Biol. 374:563-579(2007).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [16]
RP   INTERACTION WITH RTF1.
RX   PubMed=17576814; DOI=10.1128/mcb.00772-07;
RA   Warner M.H., Roinick K.L., Arndt K.M.;
RT   "Rtf1 is a multifunctional component of the Paf1 complex that regulates
RT   gene expression by directing cotranscriptional histone modification.";
RL   Mol. Cell. Biol. 27:6103-6115(2007).
RN   [17]
RP   FUNCTION.
RX   PubMed=17620414; DOI=10.1128/mcb.00978-07;
RA   Biswas D., Dutta-Biswas R., Stillman D.J.;
RT   "Chd1 and yFACT act in opposition in regulating transcription.";
RL   Mol. Cell. Biol. 27:6279-6287(2007).
RN   [18]
RP   ASSOCIATION WITH RDNA, AND FUNCTION.
RX   PubMed=17259992; DOI=10.1038/nsmb1199;
RA   Jones H.S., Kawauchi J., Braglia P., Alen C.M., Kent N.A., Proudfoot N.J.;
RT   "RNA polymerase I in yeast transcribes dynamic nucleosomal rDNA.";
RL   Nat. Struct. Mol. Biol. 14:123-130(2007).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1364, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [20]
RP   FUNCTION.
RX   PubMed=18245327; DOI=10.1534/genetics.107.084202;
RA   Biswas D., Takahata S., Xin H., Dutta-Biswas R., Yu Y., Formosa T.,
RA   Stillman D.J.;
RT   "A role for Chd1 and Set2 in negatively regulating DNA replication in
RT   Saccharomyces cerevisiae.";
RL   Genetics 178:649-659(2008).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-987; SER-989;
RP   SER-1336 AND SER-1372, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-72; SER-987; SER-989
RP   AND SER-1336, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [23]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [24]
RP   3D-STRUCTURE MODELING OF THE SAGA COMPLEX.
RX   PubMed=15260971; DOI=10.1016/j.molcel.2004.06.005;
RA   Wu P.Y., Ruhlmann C., Winston F., Schultz P.;
RT   "Molecular architecture of the S. cerevisiae SAGA complex.";
RL   Mol. Cell 15:199-208(2004).
RN   [25]
RP   STRUCTURE BY NMR OF 172-252, AND DOMAIN.
RX   PubMed=17098252; DOI=10.1016/j.jmb.2006.10.039;
RA   Okuda M., Horikoshi M., Nishimura Y.;
RT   "Structural polymorphism of chromodomains in Chd1.";
RL   J. Mol. Biol. 365:1047-1062(2007).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 174-339, DOMAIN, INTERACTION WITH
RP   HISTONE H3K4ME3, AND MUTAGENESIS OF GLU-220.
RX   PubMed=17433364; DOI=10.1016/j.jmb.2007.03.024;
RA   Flanagan J.F., Blus B.J., Kim D., Clines K.L., Rastinejad F.,
RA   Khorasanizadeh S.;
RT   "Molecular implications of evolutionary differences in CHD double
RT   chromodomains.";
RL   J. Mol. Biol. 369:334-342(2007).
CC   -!- FUNCTION: ATP-dependent chromatin-remodeling factor which functions as
CC       substrate recognition component of the transcription regulatory histone
CC       acetylation (HAT) complexes SAGA and SLIK. It recognizes H3K4me. SAGA
CC       is involved in RNA polymerase II-dependent transcriptional regulation
CC       of approximately 10% of yeast genes. At the promoters, SAGA is required
CC       for recruitment of the basal transcription machinery. It influences RNA
CC       polymerase II transcriptional activity through different activities
CC       such as TBP interaction (SPT3, SPT8 and SPT20) and promoter
CC       selectivity, interaction with transcription activators (GCN5, ADA2,
CC       ADA3 and TRA1), and chromatin modification through histone acetylation
CC       (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone
CC       H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA
CC       interacts with DNA via upstream activating sequences (UASs). SLIK is
CC       proposed to have partly overlapping functions with SAGA. It
CC       preferentially acetylates methylated histone H3, at least after
CC       activation at the GAL1-10 locus. Acts in opposition to the FACT complex
CC       in regulating polymerase II transcription. Also required for efficient
CC       transcription by RNA polymerase I, and more specifically the pol I
CC       transcription termination step. Regulates negatively DNA replication.
CC       Not only involved in transcription-related chromatin-remodeling, but
CC       also required to maintain a specific chromatin configuration across the
CC       genome. {ECO:0000269|PubMed:10026213, ECO:0000269|PubMed:10811623,
CC       ECO:0000269|PubMed:12682017, ECO:0000269|PubMed:14585955,
CC       ECO:0000269|PubMed:15647753, ECO:0000269|PubMed:16468993,
CC       ECO:0000269|PubMed:16606615, ECO:0000269|PubMed:17259992,
CC       ECO:0000269|PubMed:17620414, ECO:0000269|PubMed:17949749,
CC       ECO:0000269|PubMed:18245327}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=10.2 nM for ATP {ECO:0000269|PubMed:17949749};
CC   -!- SUBUNIT: Component of the 1.8 MDa SAGA complex, which consists of at
CC       least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12,
CC       TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and
CC       SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2
CC       copies. SAGA is built of 5 distinct domains with specialized functions.
CC       Domain I (containing TRA1) probably represents the activator
CC       interaction surface. Domain II (containing TAF5 and TAF6, and probably
CC       TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and
CC       ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing
CC       HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily
CC       an architectural role. Domain III also harbors the HAT activity. Domain
CC       V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-
CC       interacting module, which may be associated transiently with SAGA.
CC       Component of the SLIK complex, which consists of at least TRA1, CHD1,
CC       SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2,
CC       SPT3, SGF29, TAF10 and TAF9. Interacts with RTF1, SPT5 and with the
CC       FACT subunits POB3 and SPT16. {ECO:0000269|PubMed:12242279,
CC       ECO:0000269|PubMed:12446794, ECO:0000269|PubMed:12682017,
CC       ECO:0000269|PubMed:15647753, ECO:0000269|PubMed:17433364,
CC       ECO:0000269|PubMed:17576814}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:12682017}.
CC   -!- MISCELLANEOUS: Present with 1620 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
DR   EMBL; U18917; AAB64691.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07826.1; -; Genomic_DNA.
DR   PIR; S30818; S30818.
DR   RefSeq; NP_011091.1; NM_001179054.1.
DR   PDB; 2DY7; NMR; -; A=172-252.
DR   PDB; 2DY8; NMR; -; A=279-347.
DR   PDB; 2H1E; X-ray; 2.20 A; A/B=174-339.
DR   PDB; 2XB0; X-ray; 2.00 A; X=1009-1274.
DR   PDB; 3MWY; X-ray; 3.70 A; W=142-939.
DR   PDB; 3TED; X-ray; 2.00 A; A=1006-1274.
DR   PDB; 5J70; X-ray; 2.96 A; A/B=1006-1274.
DR   PDB; 5O9G; EM; 4.80 A; W=1-1468.
DR   PDB; 6FTX; EM; 4.50 A; W=175-1269.
DR   PDB; 6G0L; EM; 4.50 A; M/W=1-1468.
DR   PDBsum; 2DY7; -.
DR   PDBsum; 2DY8; -.
DR   PDBsum; 2H1E; -.
DR   PDBsum; 2XB0; -.
DR   PDBsum; 3MWY; -.
DR   PDBsum; 3TED; -.
DR   PDBsum; 5J70; -.
DR   PDBsum; 5O9G; -.
DR   PDBsum; 6FTX; -.
DR   PDBsum; 6G0L; -.
DR   SMR; P32657; -.
DR   BioGrid; 36917; 481.
DR   ComplexPortal; CPX-656; SAGA complex.
DR   ComplexPortal; CPX-675; SLIK (SAGA-like) complex.
DR   DIP; DIP-6362N; -.
DR   IntAct; P32657; 44.
DR   MINT; P32657; -.
DR   STRING; 4932.YER164W; -.
DR   iPTMnet; P32657; -.
DR   MaxQB; P32657; -.
DR   PaxDb; P32657; -.
DR   PRIDE; P32657; -.
DR   EnsemblFungi; YER164W_mRNA; YER164W; YER164W.
DR   GeneID; 856911; -.
DR   KEGG; sce:YER164W; -.
DR   EuPathDB; FungiDB:YER164W; -.
DR   SGD; S000000966; CHD1.
DR   HOGENOM; CLU_000315_29_2_1; -.
DR   InParanoid; P32657; -.
DR   KO; K11367; -.
DR   OMA; PAWQETF; -.
DR   BioCyc; YEAST:G3O-30325-MONOMER; -.
DR   SABIO-RK; P32657; -.
DR   EvolutionaryTrace; P32657; -.
DR   PRO; PR:P32657; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P32657; protein.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0000790; C:nuclear chromatin; IDA:SGD.
DR   GO; GO:0030874; C:nucleolar chromatin; IDA:SGD.
DR   GO; GO:0000124; C:SAGA complex; IDA:SGD.
DR   GO; GO:0046695; C:SLIK (SAGA-like) complex; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0031490; F:chromatin DNA binding; IDA:SGD.
DR   GO; GO:0003677; F:DNA binding; IDA:SGD.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; IDA:SGD.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0035064; F:methylated histone binding; IDA:SGD.
DR   GO; GO:0070615; F:nucleosome-dependent ATPase activity; IDA:SGD.
DR   GO; GO:0000182; F:rDNA binding; IDA:SGD.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:SGD.
DR   GO; GO:0043044; P:ATP-dependent chromatin remodeling; IDA:SGD.
DR   GO; GO:0071894; P:histone H2B conserved C-terminal lysine ubiquitination; IMP:SGD.
DR   GO; GO:2000104; P:negative regulation of DNA-dependent DNA replication; IGI:SGD.
DR   GO; GO:1900050; P:negative regulation of histone exchange; IMP:SGD.
DR   GO; GO:0071441; P:negative regulation of histone H3-K14 acetylation; IMP:SGD.
DR   GO; GO:2000616; P:negative regulation of histone H3-K9 acetylation; IMP:SGD.
DR   GO; GO:0042766; P:nucleosome mobilization; IDA:SGD.
DR   GO; GO:0034728; P:nucleosome organization; IMP:SGD.
DR   GO; GO:0016584; P:nucleosome positioning; IDA:SGD.
DR   GO; GO:1902275; P:regulation of chromatin organization; IMP:SGD.
DR   GO; GO:0060303; P:regulation of nucleosome density; IGI:SGD.
DR   GO; GO:0001178; P:regulation of transcriptional start site selection at RNA polymerase II promoter; IGI:SGD.
DR   GO; GO:0006363; P:termination of RNA polymerase I transcription; IGI:SGD.
DR   GO; GO:0006369; P:termination of RNA polymerase II transcription; IMP:SGD.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IGI:SGD.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   InterPro; IPR041150; Cdh1_DBD.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR023779; Chromodomain_CS.
DR   InterPro; IPR025260; DUF4208.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF18196; Cdh1_DBD_1; 1.
DR   Pfam; PF00385; Chromo; 2.
DR   Pfam; PF13907; DUF4208; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01176; DUF4208; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF54160; SSF54160; 2.
DR   PROSITE; PS00598; CHROMO_1; 2.
DR   PROSITE; PS50013; CHROMO_2; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Chromatin regulator; DNA-binding; Helicase;
KW   Hydrolase; Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..1468
FT                   /note="Chromo domain-containing protein 1"
FT                   /id="PRO_0000080237"
FT   DOMAIN          195..257
FT                   /note="Chromo 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT   DOMAIN          285..350
FT                   /note="Chromo 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT   DOMAIN          388..562
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          699..860
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   NP_BIND         401..408
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           513..516
FT                   /note="DEAH box"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:17330950,
FT                   ECO:0000244|PubMed:18407956, ECO:0000244|PubMed:19779198"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:19779198"
FT   MOD_RES         987
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18407956,
FT                   ECO:0000244|PubMed:19779198"
FT   MOD_RES         989
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18407956,
FT                   ECO:0000244|PubMed:19779198"
FT   MOD_RES         1336
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18407956,
FT                   ECO:0000244|PubMed:19779198"
FT   MOD_RES         1364
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:17287358"
FT   MOD_RES         1372
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18407956"
FT   CROSSLNK        1144
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:12872131"
FT   MUTAGEN         220
FT                   /note="E->L,W: No interaction with methylated histone H3
FT                   'K-4'."
FT                   /evidence="ECO:0000269|PubMed:15647753,
FT                   ECO:0000269|PubMed:17433364"
FT   MUTAGEN         222
FT                   /note="H->Y: Confers interaction with methylated histone H3
FT                   'K-4'."
FT                   /evidence="ECO:0000269|PubMed:15647753"
FT   MUTAGEN         314
FT                   /note="L->Y: No effect on interaction with methylated
FT                   histone H3 'K-4'."
FT                   /evidence="ECO:0000269|PubMed:15647753"
FT   MUTAGEN         316
FT                   /note="Y->E: Disrupts interaction with methylated histone
FT                   H3 'K-4'; abrogates histone acetylation activity of SLIK."
FT                   /evidence="ECO:0000269|PubMed:15647753"
FT   STRAND          179..187
FT                   /evidence="ECO:0000244|PDB:2H1E"
FT   TURN            190..192
FT                   /evidence="ECO:0000244|PDB:2DY7"
FT   HELIX           193..196
FT                   /evidence="ECO:0000244|PDB:2H1E"
FT   HELIX           204..210
FT                   /evidence="ECO:0000244|PDB:2H1E"
FT   STRAND          211..217
FT                   /evidence="ECO:0000244|PDB:2H1E"
FT   HELIX           222..224
FT                   /evidence="ECO:0000244|PDB:2H1E"
FT   STRAND          226..228
FT                   /evidence="ECO:0000244|PDB:2H1E"
FT   HELIX           230..233
FT                   /evidence="ECO:0000244|PDB:2H1E"
FT   STRAND          234..237
FT                   /evidence="ECO:0000244|PDB:2DY7"
FT   HELIX           239..249
FT                   /evidence="ECO:0000244|PDB:2H1E"
FT   HELIX           251..258
FT                   /evidence="ECO:0000244|PDB:2H1E"
FT   HELIX           264..283
FT                   /evidence="ECO:0000244|PDB:2H1E"
FT   STRAND          286..297
FT                   /evidence="ECO:0000244|PDB:2H1E"
FT   STRAND          299..301
FT                   /evidence="ECO:0000244|PDB:2DY8"
FT   STRAND          303..311
FT                   /evidence="ECO:0000244|PDB:2H1E"
FT   STRAND          320..323
FT                   /evidence="ECO:0000244|PDB:2H1E"
FT   HELIX           324..330
FT                   /evidence="ECO:0000244|PDB:2H1E"
FT   HELIX           332..338
FT                   /evidence="ECO:0000244|PDB:2H1E"
FT   HELIX           1012..1025
FT                   /evidence="ECO:0000244|PDB:2XB0"
FT   HELIX           1029..1031
FT                   /evidence="ECO:0000244|PDB:3TED"
FT   HELIX           1032..1037
FT                   /evidence="ECO:0000244|PDB:2XB0"
FT   HELIX           1046..1091
FT                   /evidence="ECO:0000244|PDB:2XB0"
FT   STRAND          1092..1094
FT                   /evidence="ECO:0000244|PDB:2XB0"
FT   STRAND          1096..1098
FT                   /evidence="ECO:0000244|PDB:3TED"
FT   STRAND          1101..1103
FT                   /evidence="ECO:0000244|PDB:3TED"
FT   HELIX           1104..1112
FT                   /evidence="ECO:0000244|PDB:2XB0"
FT   STRAND          1119..1122
FT                   /evidence="ECO:0000244|PDB:3TED"
FT   STRAND          1125..1129
FT                   /evidence="ECO:0000244|PDB:3TED"
FT   HELIX           1130..1150
FT                   /evidence="ECO:0000244|PDB:2XB0"
FT   HELIX           1155..1157
FT                   /evidence="ECO:0000244|PDB:2XB0"
FT   STRAND          1171..1173
FT                   /evidence="ECO:0000244|PDB:2XB0"
FT   HELIX           1177..1190
FT                   /evidence="ECO:0000244|PDB:2XB0"
FT   HELIX           1195..1200
FT                   /evidence="ECO:0000244|PDB:2XB0"
FT   TURN            1202..1204
FT                   /evidence="ECO:0000244|PDB:2XB0"
FT   HELIX           1207..1209
FT                   /evidence="ECO:0000244|PDB:2XB0"
FT   HELIX           1250..1264
FT                   /evidence="ECO:0000244|PDB:2XB0"
FT   TURN            1265..1268
FT                   /evidence="ECO:0000244|PDB:2XB0"
SQ   SEQUENCE   1468 AA;  168241 MW;  78BDB74C7FEC6BE5 CRC64;
     MAAKDISTEV LQNPELYGLR RSHRAAAHQQ NYFNDSDDED DEDNIKQSRR KRMTTIEDDE
     DEFEDEEGEE DSGEDEDEED FEEDDDYYGS PIKQNRSKPK SRTKSKSKSK PKSQSEKQST
     VKIPTRFSNR QNKTVNYNID YSDDDLLESE DDYGSEEALS EENVHEASAN PQPEDFHGID
     IVINHRLKTS LEEGKVLEKT VPDLNNCKEN YEFLIKWTDE SHLHNTWETY ESIGQVRGLK
     RLDNYCKQFI IEDQQVRLDP YVTAEDIEIM DMERERRLDE FEEFHVPERI IDSQRASLED
     GTSQLQYLVK WRRLNYDEAT WENATDIVKL APEQVKHFQN RENSKILPQY SSNYTSQRPR
     FEKLSVQPPF IKGGELRDFQ LTGINWMAFL WSKGDNGILA DEMGLGKTVQ TVAFISWLIF
     ARRQNGPHII VVPLSTMPAW LDTFEKWAPD LNCICYMGNQ KSRDTIREYE FYTNPRAKGK
     KTMKFNVLLT TYEYILKDRA ELGSIKWQFM AVDEAHRLKN AESSLYESLN SFKVANRMLI
     TGTPLQNNIK ELAALVNFLM PGRFTIDQEI DFENQDEEQE EYIHDLHRRI QPFILRRLKK
     DVEKSLPSKT ERILRVELSD VQTEYYKNIL TKNYSALTAG AKGGHFSLLN IMNELKKASN
     HPYLFDNAEE RVLQKFGDGK MTRENVLRGL IMSSGKMVLL DQLLTRLKKD GHRVLIFSQM
     VRMLDILGDY LSIKGINFQR LDGTVPSAQR RISIDHFNSP DSNDFVFLLS TRAGGLGINL
     MTADTVVIFD SDWNPQADLQ AMARAHRIGQ KNHVMVYRLV SKDTVEEEVL ERARKKMILE
     YAIISLGVTD GNKYTKKNEP NAGELSAILK FGAGNMFTAT DNQKKLEDLN LDDVLNHAED
     HVTTPDLGES HLGGEEFLKQ FEVTDYKADI DWDDIIPEEE LKKLQDEEQK RKDEEYVKEQ
     LEMMNRRDNA LKKIKNSVNG DGTAANSDSD DDSTSRSSRR RARANDMDSI GESEVRALYK
     AILKFGNLKE ILDELIADGT LPVKSFEKYG ETYDEMMEAA KDCVHEEEKN RKEILEKLEK
     HATAYRAKLK SGEIKAENQP KDNPLTRLSL KKREKKAVLF NFKGVKSLNA ESLLSRVEDL
     KYLKNLINSN YKDDPLKFSL GNNTPKPVQN WSSNWTKEED EKLLIGVFKY GYGSWTQIRD
     DPFLGITDKI FLNEVHNPVA KKSASSSDTT PTPSKKGKGI TGSSKKVPGA IHLGRRVDYL
     LSFLRGGLNT KSPSADIGSK KLPTGPSKKR QRKPANHSKS MTPEITSSEP ANGPPSKRMK
     ALPKGPAALI NNTRLSPNSP TPPLKSKVSR DNGTRQSSNP SSGSAHEKEY DSMDEEDCRH
     TMSAIRTSLK RLRRGGKSLD RKEWAKILKT ELTTIGNHIE SQKGSSRKAS PEKYRKHLWS
     YSANFWPADV KSTKLMAMYD KITESQKK
//
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