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Conserved domains on  [gi|285811725|tpg|DAA07753|]
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TPA: Ies5p [Saccharomyces cerevisiae S288C]

Protein Classification

IES5 domain-containing protein( domain architecture ID 13879701)

IES5 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IES5 pfam17335
Ino80 complex subunit 5; The INO80 chromatin remodeling complex is known to be related to DNA ...
 11-123 1.31e-42

Ino80 complex subunit 5; The INO80 chromatin remodeling complex is known to be related to DNA repair in yeast, mammals, and plants. In yeast, the INO80 complex is recruited to the DSBs (DNA double-strand breaks) through the direct interaction of its Nhp10 (non-histone protein 10) or Arp4 (Actin-Related Protein) subunits with phosphorylated histone H2A. However, the ortholog of yeast Nhp10 does not exist in mammals. The Nhp10 module consists of Nhp10, Ies1, Ies3, and Ies5. These yeast-specific subunits cross-link to the N terminus of Ino80 and form a stable complex in-vitro, which helps high-affinity targeting of INO80 to nucleosome-binding.


:

Pssm-ID: 407440  Cd Length: 110  Bit Score: 135.99  E-value: 1.31e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811725   11 DKEIRKISARNDELIKQDGTLKREYTTLLRKVSSVITVLNSIDDadtgSAETELPRLISQATVEKVPELKWYNDQISLIT 90
Cdd:pfam17335   2 EKEYQKLVSRNDELIKQEATLRKEYTTLLRKISSLFAVLEQLEP----ELENEEPKLISEETLAKVPGLQWYNEQISLVS 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 285811725   91 EKLEDDEDIEVPEELMDAYTLYKETPLLYNDTH 123
Cdd:pfam17335  78 ESSQDKEEIEIPEELMDSYELYKDTPLLYKDNQ 110
 
Name Accession Description Interval E-value
IES5 pfam17335
Ino80 complex subunit 5; The INO80 chromatin remodeling complex is known to be related to DNA ...
 11-123 1.31e-42

Ino80 complex subunit 5; The INO80 chromatin remodeling complex is known to be related to DNA repair in yeast, mammals, and plants. In yeast, the INO80 complex is recruited to the DSBs (DNA double-strand breaks) through the direct interaction of its Nhp10 (non-histone protein 10) or Arp4 (Actin-Related Protein) subunits with phosphorylated histone H2A. However, the ortholog of yeast Nhp10 does not exist in mammals. The Nhp10 module consists of Nhp10, Ies1, Ies3, and Ies5. These yeast-specific subunits cross-link to the N terminus of Ino80 and form a stable complex in-vitro, which helps high-affinity targeting of INO80 to nucleosome-binding.


Pssm-ID: 407440  Cd Length: 110  Bit Score: 135.99  E-value: 1.31e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811725   11 DKEIRKISARNDELIKQDGTLKREYTTLLRKVSSVITVLNSIDDadtgSAETELPRLISQATVEKVPELKWYNDQISLIT 90
Cdd:pfam17335   2 EKEYQKLVSRNDELIKQEATLRKEYTTLLRKISSLFAVLEQLEP----ELENEEPKLISEETLAKVPGLQWYNEQISLVS 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 285811725   91 EKLEDDEDIEVPEELMDAYTLYKETPLLYNDTH 123
Cdd:pfam17335  78 ESSQDKEEIEIPEELMDSYELYKDTPLLYKDNQ 110
 
Name Accession Description Interval E-value
IES5 pfam17335
Ino80 complex subunit 5; The INO80 chromatin remodeling complex is known to be related to DNA ...
 11-123 1.31e-42

Ino80 complex subunit 5; The INO80 chromatin remodeling complex is known to be related to DNA repair in yeast, mammals, and plants. In yeast, the INO80 complex is recruited to the DSBs (DNA double-strand breaks) through the direct interaction of its Nhp10 (non-histone protein 10) or Arp4 (Actin-Related Protein) subunits with phosphorylated histone H2A. However, the ortholog of yeast Nhp10 does not exist in mammals. The Nhp10 module consists of Nhp10, Ies1, Ies3, and Ies5. These yeast-specific subunits cross-link to the N terminus of Ino80 and form a stable complex in-vitro, which helps high-affinity targeting of INO80 to nucleosome-binding.


Pssm-ID: 407440  Cd Length: 110  Bit Score: 135.99  E-value: 1.31e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811725   11 DKEIRKISARNDELIKQDGTLKREYTTLLRKVSSVITVLNSIDDadtgSAETELPRLISQATVEKVPELKWYNDQISLIT 90
Cdd:pfam17335   2 EKEYQKLVSRNDELIKQEATLRKEYTTLLRKISSLFAVLEQLEP----ELENEEPKLISEETLAKVPGLQWYNEQISLVS 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 285811725   91 EKLEDDEDIEVPEELMDAYTLYKETPLLYNDTH 123
Cdd:pfam17335  78 ESSQDKEEIEIPEELMDSYELYKDTPLLYKDNQ 110
 
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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