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Conserved domains on  [gi|688598943|ref|XP_005159495|]
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death domain-associated protein 6 isoform X1 [Danio rerio]

Protein Classification

DAXX_helical_bundle and DAXX_histone_binding domain-containing protein( domain architecture ID 11141896)

DAXX_helical_bundle and DAXX_histone_binding domain-containing protein

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 ...
 242-447 1.22e-88

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: 277.20  E-value: 1.22e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598943 242 ASRRQIAYLENLLKVYNEEIRRLQEGDLSLDDleKEDSSYIQEHKLKRKMMKIYEKLCELKGCNTLTGRVIEQKIPYSGT 321
Cdd:cd13150    1 KRRKQIRRLEKLLKKLSKEIRKLEEKEVDLLD--DEDSAYIQEDRLKKRFVEIYKKLCELKGESPDTGRIVEKKIHFSGT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598943 322 RYPEINKKVERFINSSEallNPPDYSDILKIVQRANERYNLQLSRKQQAQISQEAFRETGNKLQERRHLDMVYNFGSHLT 401
Cdd:cd13150   79 RYPEVNRKIEKFVNRNK---TFPDFHDILKIVQKANRKKNLGLTEYQIKRLAKEAFTQVGNLLQKRRQNDLWENFGSHLT 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 688598943 402 DpykPTLDPALMDPALHRKLRSNRDVAISSLEEVINKYANKQEDME 447
Cdd:cd13150  156 D---DEKDPALEDPELKRKLEENRKIGDKRLNEVIEKYVNKQDDLE 198
Daxx pfam03344
Daxx N-terminal Rassf1C-interacting domain; The Daxx protein (also known as the Fas-binding ...
 102-196 9.58e-54

Daxx N-terminal Rassf1C-interacting domain; The Daxx protein (also known as the Fas-binding protein) is thought to play a role in apoptosis. Daxx forms a complex with Axin. Remodelling of the family to a short domain based on the PDB:2kzs structure gives a more representative family. DAXX is a scaffold protein shown to play diverse roles in transcription and cell cycle regulation. This N-terminal domain folds into a left-handed four-helix bundle (H1, H2, H4, H5) that binds to the N-terminal residues of the tumour-suppressor Rassf1C.


:

Pssm-ID: 460889  Cd Length: 95  Bit Score: 180.35  E-value: 9.58e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598943  102 ASAKKDTHVLKVENEKLFNEFVEHCSKHSQEHPEVMTYLQTRYSKALPTFLTSVEFRNTLGRCLTRAQANAGKTFVYINE 181
Cdd:pfam03344   1 SSASGEKKCLKLENEKLFEEFLELCKKQTSDHPEVVPFLQTRQQKARPEFLASAEFRNILGRCLSRAQARPAKTFVYINE 80

                          90
                  ....*....|....*
gi 688598943  182 LCTVLKQHTPRKRSS 196
Cdd:pfam03344  81 LCTVLKAHSAKKKLN 95
 
Name Accession Description Interval E-value
DAXX_histone_binding cd13150
Histone binding domain of the death-domain associated protein (DAXX); DAXX is a nuclear ...
 242-447 1.22e-88

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: 277.20  E-value: 1.22e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598943 242 ASRRQIAYLENLLKVYNEEIRRLQEGDLSLDDleKEDSSYIQEHKLKRKMMKIYEKLCELKGCNTLTGRVIEQKIPYSGT 321
Cdd:cd13150    1 KRRKQIRRLEKLLKKLSKEIRKLEEKEVDLLD--DEDSAYIQEDRLKKRFVEIYKKLCELKGESPDTGRIVEKKIHFSGT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598943 322 RYPEINKKVERFINSSEallNPPDYSDILKIVQRANERYNLQLSRKQQAQISQEAFRETGNKLQERRHLDMVYNFGSHLT 401
Cdd:cd13150   79 RYPEVNRKIEKFVNRNK---TFPDFHDILKIVQKANRKKNLGLTEYQIKRLAKEAFTQVGNLLQKRRQNDLWENFGSHLT 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 688598943 402 DpykPTLDPALMDPALHRKLRSNRDVAISSLEEVINKYANKQEDME 447
Cdd:cd13150  156 D---DEKDPALEDPELKRKLEENRKIGDKRLNEVIEKYVNKQDDLE 198
Daxx pfam03344
Daxx N-terminal Rassf1C-interacting domain; The Daxx protein (also known as the Fas-binding ...
 102-196 9.58e-54

Daxx N-terminal Rassf1C-interacting domain; The Daxx protein (also known as the Fas-binding protein) is thought to play a role in apoptosis. Daxx forms a complex with Axin. Remodelling of the family to a short domain based on the PDB:2kzs structure gives a more representative family. DAXX is a scaffold protein shown to play diverse roles in transcription and cell cycle regulation. This N-terminal domain folds into a left-handed four-helix bundle (H1, H2, H4, H5) that binds to the N-terminal residues of the tumour-suppressor Rassf1C.


Pssm-ID: 460889  Cd Length: 95  Bit Score: 180.35  E-value: 9.58e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598943  102 ASAKKDTHVLKVENEKLFNEFVEHCSKHSQEHPEVMTYLQTRYSKALPTFLTSVEFRNTLGRCLTRAQANAGKTFVYINE 181
Cdd:pfam03344   1 SSASGEKKCLKLENEKLFEEFLELCKKQTSDHPEVVPFLQTRQQKARPEFLASAEFRNILGRCLSRAQARPAKTFVYINE 80

                          90
                  ....*....|....*
gi 688598943  182 LCTVLKQHTPRKRSS 196
Cdd:pfam03344  81 LCTVLKAHSAKKKLN 95
DAXX_helical_bundle cd13151
Helical bundle domain of the death-domain associated protein (DAXX); DAXX is a nuclear protein ...
 109-196 2.62e-38

Helical bundle 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 the N-terminal helical bundle domain of DAXX, which was shown to interact with the tumor suppressor Ras-association domain family 1C (RASSF1C).


Pssm-ID: 240522  Cd Length: 88  Bit Score: 137.24  E-value: 2.62e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598943 109 HVLKVENEKLFNEFVEHCSKHSQEHPEVMTYLQTRYSKALPTFLTSVEFRNTLGRCLTRAQANAGKTFVYINELCTVLKQ 188
Cdd:cd13151    1 GVNKLENEKLFEEFLDKCLSDSAEHPEVVTFLRNRYSRATPEFLKSVEFKNILSRCLARIAARPAKLYVYINELCTVLKA 80


                 ....*...
gi 688598943 189 HTPRKRSS 196
Cdd:cd13151   81 HTPKKKLN 88
 
Name Accession Description Interval E-value
DAXX_histone_binding cd13150
Histone binding domain of the death-domain associated protein (DAXX); DAXX is a nuclear ...
 242-447 1.22e-88

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: 277.20  E-value: 1.22e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598943 242 ASRRQIAYLENLLKVYNEEIRRLQEGDLSLDDleKEDSSYIQEHKLKRKMMKIYEKLCELKGCNTLTGRVIEQKIPYSGT 321
Cdd:cd13150    1 KRRKQIRRLEKLLKKLSKEIRKLEEKEVDLLD--DEDSAYIQEDRLKKRFVEIYKKLCELKGESPDTGRIVEKKIHFSGT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598943 322 RYPEINKKVERFINSSEallNPPDYSDILKIVQRANERYNLQLSRKQQAQISQEAFRETGNKLQERRHLDMVYNFGSHLT 401
Cdd:cd13150   79 RYPEVNRKIEKFVNRNK---TFPDFHDILKIVQKANRKKNLGLTEYQIKRLAKEAFTQVGNLLQKRRQNDLWENFGSHLT 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 688598943 402 DpykPTLDPALMDPALHRKLRSNRDVAISSLEEVINKYANKQEDME 447
Cdd:cd13150  156 D---DEKDPALEDPELKRKLEENRKIGDKRLNEVIEKYVNKQDDLE 198
Daxx pfam03344
Daxx N-terminal Rassf1C-interacting domain; The Daxx protein (also known as the Fas-binding ...
 102-196 9.58e-54

Daxx N-terminal Rassf1C-interacting domain; The Daxx protein (also known as the Fas-binding protein) is thought to play a role in apoptosis. Daxx forms a complex with Axin. Remodelling of the family to a short domain based on the PDB:2kzs structure gives a more representative family. DAXX is a scaffold protein shown to play diverse roles in transcription and cell cycle regulation. This N-terminal domain folds into a left-handed four-helix bundle (H1, H2, H4, H5) that binds to the N-terminal residues of the tumour-suppressor Rassf1C.


Pssm-ID: 460889  Cd Length: 95  Bit Score: 180.35  E-value: 9.58e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598943  102 ASAKKDTHVLKVENEKLFNEFVEHCSKHSQEHPEVMTYLQTRYSKALPTFLTSVEFRNTLGRCLTRAQANAGKTFVYINE 181
Cdd:pfam03344   1 SSASGEKKCLKLENEKLFEEFLELCKKQTSDHPEVVPFLQTRQQKARPEFLASAEFRNILGRCLSRAQARPAKTFVYINE 80

                          90
                  ....*....|....*
gi 688598943  182 LCTVLKQHTPRKRSS 196
Cdd:pfam03344  81 LCTVLKAHSAKKKLN 95
DAXX_helical_bundle cd13151
Helical bundle domain of the death-domain associated protein (DAXX); DAXX is a nuclear protein ...
 109-196 2.62e-38

Helical bundle 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 the N-terminal helical bundle domain of DAXX, which was shown to interact with the tumor suppressor Ras-association domain family 1C (RASSF1C).


Pssm-ID: 240522  Cd Length: 88  Bit Score: 137.24  E-value: 2.62e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598943 109 HVLKVENEKLFNEFVEHCSKHSQEHPEVMTYLQTRYSKALPTFLTSVEFRNTLGRCLTRAQANAGKTFVYINELCTVLKQ 188
Cdd:cd13151    1 GVNKLENEKLFEEFLDKCLSDSAEHPEVVTFLRNRYSRATPEFLKSVEFKNILSRCLARIAARPAKLYVYINELCTVLKA 80


                 ....*...
gi 688598943 189 HTPRKRSS 196
Cdd:cd13151   81 HTPKKKLN 88
 
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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