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Conserved domains on  [gi|5231105|gb|AAD41072|]
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DAXX protein, partial [Danio rerio]

Protein Classification

Atrophin-1 and DAXX_histone_binding domain-containing protein( domain architecture ID 10192128)

protein containing domains PTZ00449, Atrophin-1, and DAXX_histone_binding

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DAXX_histone_binding cd13150
Histone binding domain of the death-domain associated protein (DAXX); DAXX is a nuclear ...
 1-185 3.61e-74

Histone binding domain of the death-domain associated protein (DAXX); DAXX is a nuclear protein that modulates transcription of various genes and is involved in cell death and/or the suppression of growth. DAXX is also a histone chaperone conserved in Metazoa that acts specifically on histone H3.3. This alignment models a functional domain of DAXX that interacts with the histone H3.3-H4 dimer, and in doing so competes with DNA binding and interactions between the histone chaperone ASF1/CIA and the H3-H4 dimer.


:

Pssm-ID: 240523  Cd Length: 198  Bit Score: 222.88  E-value: 3.61e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5231105    1 RLQEGDLSLDDleKEDSSYIQEHKLKRKMMKIYEKLCELKGCNTLTGRVIEQKIPYSGTRYPEINKKVERFINSSEallN 80
Cdd:cd13150  22 KLEEKEVDLLD--DEDSAYIQEDRLKKRFVEIYKKLCELKGESPDTGRIVEKKIHFSGTRYPEVNRKIEKFVNRNK---T 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5231105   81 PPDYSDILKIVQRANERYNLQLSRKQQAQISQEAFRETGNKLQERRRLDMVYNFGSHLTDpykPTLDPALMDPALHRKLR 160
Cdd:cd13150  97 FPDFHDILKIVQKANRKKNLGLTEYQIKRLAKEAFTQVGNLLQKRRQNDLWENFGSHLTD---DEKDPALEDPELKRKLE 173

                       170       180
                ....*....|....*....|....*
gi 5231105  161 SNRDVAISSLEEVINKYANKQEDME 185
Cdd:cd13150 174 ENRKIGDKRLNEVIEKYVNKQDDLE 198
 
Name Accession Description Interval E-value
DAXX_histone_binding cd13150
Histone binding domain of the death-domain associated protein (DAXX); DAXX is a nuclear ...
 1-185 3.61e-74

Histone binding domain of the death-domain associated protein (DAXX); DAXX is a nuclear protein that modulates transcription of various genes and is involved in cell death and/or the suppression of growth. DAXX is also a histone chaperone conserved in Metazoa that acts specifically on histone H3.3. This alignment models a functional domain of DAXX that interacts with the histone H3.3-H4 dimer, and in doing so competes with DNA binding and interactions between the histone chaperone ASF1/CIA and the H3-H4 dimer.


Pssm-ID: 240523  Cd Length: 198  Bit Score: 222.88  E-value: 3.61e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5231105    1 RLQEGDLSLDDleKEDSSYIQEHKLKRKMMKIYEKLCELKGCNTLTGRVIEQKIPYSGTRYPEINKKVERFINSSEallN 80
Cdd:cd13150  22 KLEEKEVDLLD--DEDSAYIQEDRLKKRFVEIYKKLCELKGESPDTGRIVEKKIHFSGTRYPEVNRKIEKFVNRNK---T 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5231105   81 PPDYSDILKIVQRANERYNLQLSRKQQAQISQEAFRETGNKLQERRRLDMVYNFGSHLTDpykPTLDPALMDPALHRKLR 160
Cdd:cd13150  97 FPDFHDILKIVQKANRKKNLGLTEYQIKRLAKEAFTQVGNLLQKRRQNDLWENFGSHLTD---DEKDPALEDPELKRKLE 173

                       170       180
                ....*....|....*....|....*
gi 5231105  161 SNRDVAISSLEEVINKYANKQEDME 185
Cdd:cd13150 174 ENRKIGDKRLNEVIEKYVNKQDDLE 198
 
Name Accession Description Interval E-value
DAXX_histone_binding cd13150
Histone binding domain of the death-domain associated protein (DAXX); DAXX is a nuclear ...
 1-185 3.61e-74

Histone binding domain of the death-domain associated protein (DAXX); DAXX is a nuclear protein that modulates transcription of various genes and is involved in cell death and/or the suppression of growth. DAXX is also a histone chaperone conserved in Metazoa that acts specifically on histone H3.3. This alignment models a functional domain of DAXX that interacts with the histone H3.3-H4 dimer, and in doing so competes with DNA binding and interactions between the histone chaperone ASF1/CIA and the H3-H4 dimer.


Pssm-ID: 240523  Cd Length: 198  Bit Score: 222.88  E-value: 3.61e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5231105    1 RLQEGDLSLDDleKEDSSYIQEHKLKRKMMKIYEKLCELKGCNTLTGRVIEQKIPYSGTRYPEINKKVERFINSSEallN 80
Cdd:cd13150  22 KLEEKEVDLLD--DEDSAYIQEDRLKKRFVEIYKKLCELKGESPDTGRIVEKKIHFSGTRYPEVNRKIEKFVNRNK---T 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5231105   81 PPDYSDILKIVQRANERYNLQLSRKQQAQISQEAFRETGNKLQERRRLDMVYNFGSHLTDpykPTLDPALMDPALHRKLR 160
Cdd:cd13150  97 FPDFHDILKIVQKANRKKNLGLTEYQIKRLAKEAFTQVGNLLQKRRQNDLWENFGSHLTD---DEKDPALEDPELKRKLE 173

                       170       180
                ....*....|....*....|....*
gi 5231105  161 SNRDVAISSLEEVINKYANKQEDME 185
Cdd:cd13150 174 ENRKIGDKRLNEVIEKYVNKQDDLE 198
 
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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