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Conserved domains on  [gi|52631084|gb|AAU84992|]
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death domain-associated protein, partial [Mus musculus]

Protein Classification

DAXX_helical_bundle and DAXX_histone_binding domain-containing protein( domain architecture ID 11055901)

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 ...
 73-277 2.61e-93

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: 275.27  E-value: 2.61e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631084  73 GSRRQIQRLEQLLALYVAEIRRLQEKELDLseLDDPDSSYLQEARLKRKLIRLFGRLCELKDCSSLTGRVIEQRIPYRGT 152
Cdd:cd13150   1 KRRKQIRRLEKLLKKLSKEIRKLEEKEVDL--LDDEDSAYIQEDRLKKRFVEIYKKLCELKGESPDTGRIVEKKIHFSGT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631084 153 RYPEVNRRIERLINKPglDTFPDYGDVLRAVEKAATRHSLGLPRQQLQLLAQDAFRDVGVRLQERRHLDLIYNFGCHLTD 232
Cdd:cd13150  79 RYPEVNRKIEKFVNRN--KTFPDFHDILKIVQKANRKKNLGLTEYQIKRLAKEAFTQVGNLLQKRRQNDLWENFGSHLTD 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 52631084 233 DyrpGVDPALSDPTLARRLRENRTLAMNRLDEVISKYAMMQDKTE 277
Cdd:cd13150 157 D---EKDPALEDPELKRKLEENRKIGDKRLNEVIEKYVNKQDDLE 198
DAXX_helical_bundle super family cl23986
Helical bundle domain of the death-domain associated protein (DAXX); DAXX is a nuclear protein ...
 1-34 1.21e-15

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).


The actual alignment was detected with superfamily member pfam03344:

Pssm-ID: 474122  Cd Length: 95  Bit Score: 71.34  E-value: 1.21e-15
                          10        20        30
                  ....*....|....*....|....*....|....
gi 52631084     1 RVLARSRKRPAKIYVYINELCTVLKAHSIKKKLN 34
Cdd:pfam03344  62 RCLSRAQARPAKTFVYINELCTVLKAHSAKKKLN 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 ...
 73-277 2.61e-93

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: 275.27  E-value: 2.61e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631084  73 GSRRQIQRLEQLLALYVAEIRRLQEKELDLseLDDPDSSYLQEARLKRKLIRLFGRLCELKDCSSLTGRVIEQRIPYRGT 152
Cdd:cd13150   1 KRRKQIRRLEKLLKKLSKEIRKLEEKEVDL--LDDEDSAYIQEDRLKKRFVEIYKKLCELKGESPDTGRIVEKKIHFSGT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631084 153 RYPEVNRRIERLINKPglDTFPDYGDVLRAVEKAATRHSLGLPRQQLQLLAQDAFRDVGVRLQERRHLDLIYNFGCHLTD 232
Cdd:cd13150  79 RYPEVNRKIEKFVNRN--KTFPDFHDILKIVQKANRKKNLGLTEYQIKRLAKEAFTQVGNLLQKRRQNDLWENFGSHLTD 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 52631084 233 DyrpGVDPALSDPTLARRLRENRTLAMNRLDEVISKYAMMQDKTE 277
Cdd:cd13150 157 D---EKDPALEDPELKRKLEENRKIGDKRLNEVIEKYVNKQDDLE 198
Daxx pfam03344
Daxx N-terminal Rassf1C-interacting domain; The Daxx protein (also known as the Fas-binding ...
 1-34 1.21e-15

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: 71.34  E-value: 1.21e-15
                          10        20        30
                  ....*....|....*....|....*....|....
gi 52631084     1 RVLARSRKRPAKIYVYINELCTVLKAHSIKKKLN 34
Cdd:pfam03344  62 RCLSRAQARPAKTFVYINELCTVLKAHSAKKKLN 95
DAXX_helical_bundle cd13151
Helical bundle domain of the death-domain associated protein (DAXX); DAXX is a nuclear protein ...
 1-34 1.09e-12

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: 62.89  E-value: 1.09e-12
                        10        20        30
                ....*....|....*....|....*....|....
gi 52631084   1 RVLARSRKRPAKIYVYINELCTVLKAHSIKKKLN 34
Cdd:cd13151  55 RCLARIAARPAKLYVYINELCTVLKAHTPKKKLN 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 ...
 73-277 2.61e-93

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: 275.27  E-value: 2.61e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631084  73 GSRRQIQRLEQLLALYVAEIRRLQEKELDLseLDDPDSSYLQEARLKRKLIRLFGRLCELKDCSSLTGRVIEQRIPYRGT 152
Cdd:cd13150   1 KRRKQIRRLEKLLKKLSKEIRKLEEKEVDL--LDDEDSAYIQEDRLKKRFVEIYKKLCELKGESPDTGRIVEKKIHFSGT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631084 153 RYPEVNRRIERLINKPglDTFPDYGDVLRAVEKAATRHSLGLPRQQLQLLAQDAFRDVGVRLQERRHLDLIYNFGCHLTD 232
Cdd:cd13150  79 RYPEVNRKIEKFVNRN--KTFPDFHDILKIVQKANRKKNLGLTEYQIKRLAKEAFTQVGNLLQKRRQNDLWENFGSHLTD 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 52631084 233 DyrpGVDPALSDPTLARRLRENRTLAMNRLDEVISKYAMMQDKTE 277
Cdd:cd13150 157 D---EKDPALEDPELKRKLEENRKIGDKRLNEVIEKYVNKQDDLE 198
Daxx pfam03344
Daxx N-terminal Rassf1C-interacting domain; The Daxx protein (also known as the Fas-binding ...
 1-34 1.21e-15

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: 71.34  E-value: 1.21e-15
                          10        20        30
                  ....*....|....*....|....*....|....
gi 52631084     1 RVLARSRKRPAKIYVYINELCTVLKAHSIKKKLN 34
Cdd:pfam03344  62 RCLSRAQARPAKTFVYINELCTVLKAHSAKKKLN 95
DAXX_helical_bundle cd13151
Helical bundle domain of the death-domain associated protein (DAXX); DAXX is a nuclear protein ...
 1-34 1.09e-12

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: 62.89  E-value: 1.09e-12
                        10        20        30
                ....*....|....*....|....*....|....
gi 52631084   1 RVLARSRKRPAKIYVYINELCTVLKAHSIKKKLN 34
Cdd:cd13151  55 RCLARIAARPAKLYVYINELCTVLKAHTPKKKLN 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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