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Conserved domains on  [gi|731939|sp|P40366|]
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RecName: Full=Protein DLS1; AltName: Full=DPB3-like subunit of ISW2 complex 1

Protein Classification

histone-fold protein( domain architecture ID 19224140)

histone-fold protein such as NFYB/HAP3 family histone-like transcription factors similar to transcriptional activator hap3 that belongs to a complex that binds to the sequence CCAAT located upstream of genes involved in mitochondrial electron transport

Gene Ontology:  GO:0046982|GO:0006261|GO:0008622
PubMed:  8524779|17391511

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HFD_POLE4-like cd22929
histone-fold domain found in DNA polymerase epsilon subunit 4 (POLE4) and similar proteins; ...
 17-106 7.49e-22

histone-fold domain found in DNA polymerase epsilon subunit 4 (POLE4) and similar proteins; POLE4, also called DNA polymerase II subunit 4, or DNA polymerase epsilon subunit p12, may participate in DNA repair and in chromosomal DNA replication. It is an accessory component of the DNA polymerase epsilon complex that consists of four subunits: the catalytic subunit POLE and the accessory subunits POLE2, POLE3 and POLE4. POLE4 forms a complex with POLE3. The POLE3-POLE4 is a histone chaperone that promotes tetrasome formation and DNA supercoiling in vitro. Interaction with POLE3 is a prerequisite for further binding with POLE and POLE2. In fungi, POLE4 has been named as DNA polymerase epsilon subunit C (DPB3, also known as DNA polymerase II subunit C). It is an accessory component of the DNA polymerase epsilon (DNA polymerase II) that participates in chromosomal DNA replication. DNA polymerase epsilon is a heterotetramer consisting of POL2, DPB2, DPB3 and DPB4. DPB3 is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair. This subfamily also includes protein DLS1 (DPB3-like subunit of ISW2 complex 1). It functions as a component of the ISW2 complex, which at least consists of ISW2, ITC1, DLS1 and DPB4, and acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW2 complex is involved in coordinating transcriptional repression and in inheritance of telomeric silencing. It is involved in repression of MAT a-specific genes, INO1, and early meiotic genes during mitotic growth dependent upon transcription factor UME6 and in a parallel pathway to the RPD3-SIN3 histone deacetylase complex. DLS1 is partially required for the ISW2 complex chromatin remodeling activity and is not required for its interaction with chromatin.


:

Pssm-ID: 467054 [Multi-domain]  Cd Length: 79  Bit Score: 83.72  E-value: 7.49e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731939    17 SPKLPVEKVQRIAKNDPEYMDTSDDAFVATAFATEFFVQVLTHESLHRQQQQqqqqvpplpDELTLSYDDISAAIvhSSD 96
Cdd:cd22929   1 LPKLPLSRVKRIMKLDPDVTLVSQEAVVAIAKATELFIQLLAKEAYSVAQQS---------KRKTLQLKDIDAAI--KSD 69

                        90
                ....*....|
gi 731939    97 GHLQFLNDVI 106
Cdd:cd22929  70 DRFAFLEDVL 79
 
Name Accession Description Interval E-value
HFD_POLE4-like cd22929
histone-fold domain found in DNA polymerase epsilon subunit 4 (POLE4) and similar proteins; ...
 17-106 7.49e-22

histone-fold domain found in DNA polymerase epsilon subunit 4 (POLE4) and similar proteins; POLE4, also called DNA polymerase II subunit 4, or DNA polymerase epsilon subunit p12, may participate in DNA repair and in chromosomal DNA replication. It is an accessory component of the DNA polymerase epsilon complex that consists of four subunits: the catalytic subunit POLE and the accessory subunits POLE2, POLE3 and POLE4. POLE4 forms a complex with POLE3. The POLE3-POLE4 is a histone chaperone that promotes tetrasome formation and DNA supercoiling in vitro. Interaction with POLE3 is a prerequisite for further binding with POLE and POLE2. In fungi, POLE4 has been named as DNA polymerase epsilon subunit C (DPB3, also known as DNA polymerase II subunit C). It is an accessory component of the DNA polymerase epsilon (DNA polymerase II) that participates in chromosomal DNA replication. DNA polymerase epsilon is a heterotetramer consisting of POL2, DPB2, DPB3 and DPB4. DPB3 is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair. This subfamily also includes protein DLS1 (DPB3-like subunit of ISW2 complex 1). It functions as a component of the ISW2 complex, which at least consists of ISW2, ITC1, DLS1 and DPB4, and acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW2 complex is involved in coordinating transcriptional repression and in inheritance of telomeric silencing. It is involved in repression of MAT a-specific genes, INO1, and early meiotic genes during mitotic growth dependent upon transcription factor UME6 and in a parallel pathway to the RPD3-SIN3 histone deacetylase complex. DLS1 is partially required for the ISW2 complex chromatin remodeling activity and is not required for its interaction with chromatin.


Pssm-ID: 467054 [Multi-domain]  Cd Length: 79  Bit Score: 83.72  E-value: 7.49e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731939    17 SPKLPVEKVQRIAKNDPEYMDTSDDAFVATAFATEFFVQVLTHESLHRQQQQqqqqvpplpDELTLSYDDISAAIvhSSD 96
Cdd:cd22929   1 LPKLPLSRVKRIMKLDPDVTLVSQEAVVAIAKATELFIQLLAKEAYSVAQQS---------KRKTLQLKDIDAAI--KSD 69

                        90
                ....*....|
gi 731939    97 GHLQFLNDVI 106
Cdd:cd22929  70 DRFAFLEDVL 79
 
Name Accession Description Interval E-value
HFD_POLE4-like cd22929
histone-fold domain found in DNA polymerase epsilon subunit 4 (POLE4) and similar proteins; ...
 17-106 7.49e-22

histone-fold domain found in DNA polymerase epsilon subunit 4 (POLE4) and similar proteins; POLE4, also called DNA polymerase II subunit 4, or DNA polymerase epsilon subunit p12, may participate in DNA repair and in chromosomal DNA replication. It is an accessory component of the DNA polymerase epsilon complex that consists of four subunits: the catalytic subunit POLE and the accessory subunits POLE2, POLE3 and POLE4. POLE4 forms a complex with POLE3. The POLE3-POLE4 is a histone chaperone that promotes tetrasome formation and DNA supercoiling in vitro. Interaction with POLE3 is a prerequisite for further binding with POLE and POLE2. In fungi, POLE4 has been named as DNA polymerase epsilon subunit C (DPB3, also known as DNA polymerase II subunit C). It is an accessory component of the DNA polymerase epsilon (DNA polymerase II) that participates in chromosomal DNA replication. DNA polymerase epsilon is a heterotetramer consisting of POL2, DPB2, DPB3 and DPB4. DPB3 is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair. This subfamily also includes protein DLS1 (DPB3-like subunit of ISW2 complex 1). It functions as a component of the ISW2 complex, which at least consists of ISW2, ITC1, DLS1 and DPB4, and acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW2 complex is involved in coordinating transcriptional repression and in inheritance of telomeric silencing. It is involved in repression of MAT a-specific genes, INO1, and early meiotic genes during mitotic growth dependent upon transcription factor UME6 and in a parallel pathway to the RPD3-SIN3 histone deacetylase complex. DLS1 is partially required for the ISW2 complex chromatin remodeling activity and is not required for its interaction with chromatin.


Pssm-ID: 467054 [Multi-domain]  Cd Length: 79  Bit Score: 83.72  E-value: 7.49e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731939    17 SPKLPVEKVQRIAKNDPEYMDTSDDAFVATAFATEFFVQVLTHESLHRQQQQqqqqvpplpDELTLSYDDISAAIvhSSD 96
Cdd:cd22929   1 LPKLPLSRVKRIMKLDPDVTLVSQEAVVAIAKATELFIQLLAKEAYSVAQQS---------KRKTLQLKDIDAAI--KSD 69

                        90
                ....*....|
gi 731939    97 GHLQFLNDVI 106
Cdd:cd22929  70 DRFAFLEDVL 79
HFD_Dpb3-like cd23645
histone-fold domain found in Schizosaccharomyces pombe DNA polymerase epsilon subunit C (Dpb3) ...
 18-106 2.64e-09

histone-fold domain found in Schizosaccharomyces pombe DNA polymerase epsilon subunit C (Dpb3) and similar proteins; Schizosaccharomyces pombe Dpb3 is an accessory component of the DNA polymerase epsilon (DNA polymerase II) that is a heterotetramer consisting of cdc20/Pol2, Dpb2, Dpb3, and Dpb4, and participates in chromosomal DNA replication. Dpb3 is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair. The Dpb3-Dpb4 dimer associates with histone deacetylases, chromatin remodelers, and histones and plays a crucial role in the inheritance of histone hypoacetylation and H3K9 methylation in heterochromatin. The Dpb3-Dpb4 dimer is also required for the recruitment of sir2 to heterochromatin.


Pssm-ID: 467059 [Multi-domain]  Cd Length: 78  Bit Score: 51.08  E-value: 2.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731939    18 PKLPVEKVQRIAKNDPEYMDTSDDAFVATAFATEFFVQVLTHESLHRQQQQQqqqvpplpdELTLSYDDISAAIvhSSDG 97
Cdd:cd23645   1 TVLPLARVKRIIKADKDVKICSKDAVFLISKATELFIEYLAEQAYELAKLEK---------RKTVQYKDLAKAV--KRDD 69


                ....*....
gi 731939    98 HLQFLNDVI 106
Cdd:cd23645  70 NLEFLEDVI 78
HFD_CHRAC1-like cd22924
histone-fold domain found in chromatin accessibility complex protein 1 (CHRAC-1) and similar ...
 20-106 5.56e-09

histone-fold domain found in chromatin accessibility complex protein 1 (CHRAC-1) and similar proteins; CHRAC-1, also called chromatin accessibility complex 15 kDa protein, or CHRAC-15, or DNA polymerase epsilon subunit p15, forms a complex with DNA polymerase epsilon subunit POLE3 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome remodeling activity of ISWI/SNF2H and ACF1. Together with POLE3, ACF1 and ISWI/SNF2H proteins, CHRAC-1 forms the ISWI chromatin-remodeling complex, CHRAC. This subfamily also includes Drosophila melanogaster chromatin accessibility complex 16kD protein (CHRAC-16), which is a histone-like protein that promotes nucleosome sliding of ATP-dependent nucleosome remodeling complexes. It is part of the CHRAC, composed of CHRAC-14, CHRAC-16, ACF and ISWI, which uses energy/ATP to increase the general accessibility of DNA in chromatin. It forms a heterodimer with CHRAC-14, binds DNA, and facilitates nucleosome sliding by ACF. It is required for oogenesis.


Pssm-ID: 467049  Cd Length: 74  Bit Score: 50.25  E-value: 5.56e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731939    20 LPVEKVQRIAKNDPEYMDTSDDAFVATAFATEFFVQVLTHESLHRQQqqqqqqvpplpDELTLSYDDIsAAIVHSSDgHL 99
Cdd:cd22924   1 LPLSRVRTIMKSSPDVSSISQDAVFLITKATELFVEYLAKEAYKKSK-----------DKKKLTYKDL-ADVVNDDE-NL 67


                ....*..
gi 731939   100 QFLNDVI 106
Cdd:cd22924  68 EFLLDIV 74
HFD_NFYC-like cd22908
histone-fold domain found in nuclear transcription factor Y subunit gamma (NF-YC) and similar ...
 17-107 8.68e-04

histone-fold domain found in nuclear transcription factor Y subunit gamma (NF-YC) and similar proteins; NF-YC, also called CAAT box DNA-binding protein subunit C, or nuclear transcription factor Y subunit C, or transactivator HSM-1/2, is a component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes. NF-Y can function as both an activator and a repressor, depending on its interacting cofactors. NF-Y is a heterotrimeric transcription factor composed of three components, NF-YA, NF-YB and NF-YC. NF-YB and NF-YC must interact and dimerize for NF-YA association and DNA binding. The family also includes NF-YC homologs such as Aspergillus fumigatus CCAAT-binding complex (CBC) subunit HapE and Saccharomyces cerevisiae transcriptional activator Hap5. HapE is a component of CBC, which is composed of the histone-like subunits HapC and HapE as well as the DNA specificity conferring subunit HapB. In yeast, Hap5 is a component of the CCAT-binding factor (CBF or HAP complex II), which is a transcriptional activator and binds to the upstream activation site (UAS2) of the CYC1 gene and other genes involved in mitochondrial electron transport and activates their expression. It recognizes the sequence 5'-CCAAT-3'. Hap5 is essential for DNA-binding activity.


Pssm-ID: 467033 [Multi-domain]  Cd Length: 84  Bit Score: 36.34  E-value: 8.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731939    17 SPKLPVEKVQRIAKNDPEYMDTSDDAFVATAFATEFFVQVLTH------ESLHRQqqqqqqqvpplpdelTLSYDDISAA 90
Cdd:cd22908   5 NHELPLARIKKIMKSDEDVKMISAEAPVLFAKACELFILELTLrawihtEENKRR---------------TLQRSDIAAA 69

                        90
                ....*....|....*..
gi 731939    91 IvhSSDGHLQFLNDVIP 107
Cdd:cd22908  70 I--TSSDMFDFLIDIVP 84
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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