Ioc3p [Saccharomyces cerevisiae S288C]
WHIM1 domain-containing protein( domain architecture ID 10634769)
WHIM1 (WSTF, HB1, Itc1p, MBD9 motif 1) domain-containing protein similar to Saccharomyces cerevisiae ISWI one complex protein 3 that functions as a component of the ISW1A complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA
List of domain hits
Name | Accession | Description | Interval | E-value | ||
WHIM1 | pfam15612 | WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and ... |
365-411 | 4.94e-07 | ||
WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and WHIM3 motifs, and the DDT domain comprise an alpha helical module found in diverse eukaryotic chromatin proteins.Based on the Ioc3 structure, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. The conserved basic residue in WHIM1 is involved in packing with the DDT motif. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognising and DNA binding domains, some of which discriminate methylated DNA. : Pssm-ID: 464774 [Multi-domain] Cd Length: 46 Bit Score: 46.72 E-value: 4.94e-07
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PRK13808 super family | cl31642 | adenylate kinase; Provisional |
74-134 | 7.53e-03 | ||
adenylate kinase; Provisional The actual alignment was detected with superfamily member PRK13808: Pssm-ID: 172341 [Multi-domain] Cd Length: 333 Bit Score: 39.49 E-value: 7.53e-03
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Name | Accession | Description | Interval | E-value | ||
WHIM1 | pfam15612 | WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and ... |
365-411 | 4.94e-07 | ||
WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and WHIM3 motifs, and the DDT domain comprise an alpha helical module found in diverse eukaryotic chromatin proteins.Based on the Ioc3 structure, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. The conserved basic residue in WHIM1 is involved in packing with the DDT motif. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognising and DNA binding domains, some of which discriminate methylated DNA. Pssm-ID: 464774 [Multi-domain] Cd Length: 46 Bit Score: 46.72 E-value: 4.94e-07
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PRK13808 | PRK13808 | adenylate kinase; Provisional |
74-134 | 7.53e-03 | ||
adenylate kinase; Provisional Pssm-ID: 172341 [Multi-domain] Cd Length: 333 Bit Score: 39.49 E-value: 7.53e-03
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Name | Accession | Description | Interval | E-value | ||
WHIM1 | pfam15612 | WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and ... |
365-411 | 4.94e-07 | ||
WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and WHIM3 motifs, and the DDT domain comprise an alpha helical module found in diverse eukaryotic chromatin proteins.Based on the Ioc3 structure, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. The conserved basic residue in WHIM1 is involved in packing with the DDT motif. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognising and DNA binding domains, some of which discriminate methylated DNA. Pssm-ID: 464774 [Multi-domain] Cd Length: 46 Bit Score: 46.72 E-value: 4.94e-07
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PRK13808 | PRK13808 | adenylate kinase; Provisional |
74-134 | 7.53e-03 | ||
adenylate kinase; Provisional Pssm-ID: 172341 [Multi-domain] Cd Length: 333 Bit Score: 39.49 E-value: 7.53e-03
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Blast search parameters | ||||
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