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Conserved domains on  [gi|62898369|dbj|BAD97124|]
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death-associated protein 6 variant, partial [Homo sapiens]

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 ...
 183-387 5.76e-94

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: 290.29  E-value: 5.76e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62898369 183 GSRRQIQRLEQLLALYVAEIRRLQEKELDLseLDDPDSAYLQEARLKRKLIRLFGRLCELKDCSSLTGRVIEQRIPYRGT 262
Cdd:cd13150   1 KRRKQIRRLEKLLKKLSKEIRKLEEKEVDL--LDDEDSAYIQEDRLKKRFVEIYKKLCELKGESPDTGRIVEKKIHFSGT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62898369 263 RYPEVNRRIERLINKpgPDTFPDYGDVLRAVEKAAARHSLGLPRQQLQLMAQDAFRDAGIRLQERRHLDLIYNFGCHLTD 342
Cdd:cd13150  79 RYPEVNRKIEKFVNR--NKTFPDFHDILKIVQKANRKKNLGLTEYQIKRLAKEAFTQVGNLLQKRRQNDLWENFGSHLTD 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 62898369 343 DyrpGVDPALSDPVLARRLRENRSLAMSRLDEVISKYAMLQDKSE 387
Cdd:cd13150 157 D---EKDPALEDPELKRKLEENRKIGDKRLNEVIEKYVNKQDDLE 198
Daxx pfam03344
Daxx N-terminal Rassf1C-interacting domain; The Daxx protein (also known as the Fas-binding ...
 56-144 2.28e-53

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: 178.81  E-value: 2.28e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62898369    56 KKCYKLENEKLCEEFLGLCKMQTADHPEVVPFLYNRQQRAHSLFLASAEFCNILSRVLSRARSRPAKLYVYINELCTVLK 135
Cdd:pfam03344   7 KKCLKLENEKLFEEFLELCKKQTSDHPEVVPFLQTRQQKARPEFLASAEFRNILGRCLSRAQARPAKTFVYINELCTVLK 86


                  ....*....
gi 62898369   136 AHSAKKKLN 144
Cdd:pfam03344  87 AHSAKKKLN 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 ...
 183-387 5.76e-94

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: 290.29  E-value: 5.76e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62898369 183 GSRRQIQRLEQLLALYVAEIRRLQEKELDLseLDDPDSAYLQEARLKRKLIRLFGRLCELKDCSSLTGRVIEQRIPYRGT 262
Cdd:cd13150   1 KRRKQIRRLEKLLKKLSKEIRKLEEKEVDL--LDDEDSAYIQEDRLKKRFVEIYKKLCELKGESPDTGRIVEKKIHFSGT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62898369 263 RYPEVNRRIERLINKpgPDTFPDYGDVLRAVEKAAARHSLGLPRQQLQLMAQDAFRDAGIRLQERRHLDLIYNFGCHLTD 342
Cdd:cd13150  79 RYPEVNRKIEKFVNR--NKTFPDFHDILKIVQKANRKKNLGLTEYQIKRLAKEAFTQVGNLLQKRRQNDLWENFGSHLTD 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 62898369 343 DyrpGVDPALSDPVLARRLRENRSLAMSRLDEVISKYAMLQDKSE 387
Cdd:cd13150 157 D---EKDPALEDPELKRKLEENRKIGDKRLNEVIEKYVNKQDDLE 198
Daxx pfam03344
Daxx N-terminal Rassf1C-interacting domain; The Daxx protein (also known as the Fas-binding ...
 56-144 2.28e-53

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: 178.81  E-value: 2.28e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62898369    56 KKCYKLENEKLCEEFLGLCKMQTADHPEVVPFLYNRQQRAHSLFLASAEFCNILSRVLSRARSRPAKLYVYINELCTVLK 135
Cdd:pfam03344   7 KKCLKLENEKLFEEFLELCKKQTSDHPEVVPFLQTRQQKARPEFLASAEFRNILGRCLSRAQARPAKTFVYINELCTVLK 86


                  ....*....
gi 62898369   136 AHSAKKKLN 144
Cdd:pfam03344  87 AHSAKKKLN 95
DAXX_helical_bundle cd13151
Helical bundle domain of the death-domain associated protein (DAXX); DAXX is a nuclear protein ...
 57-144 2.07e-39

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: 140.32  E-value: 2.07e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62898369  57 KCYKLENEKLCEEFLGLCKMQTADHPEVVPFLYNRQQRAHSLFLASAEFCNILSRVLSRARSRPAKLYVYINELCTVLKA 136
Cdd:cd13151   1 GVNKLENEKLFEEFLDKCLSDSAEHPEVVTFLRNRYSRATPEFLKSVEFKNILSRCLARIAARPAKLYVYINELCTVLKA 80


                ....*...
gi 62898369 137 HSAKKKLN 144
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 ...
 183-387 5.76e-94

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: 290.29  E-value: 5.76e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62898369 183 GSRRQIQRLEQLLALYVAEIRRLQEKELDLseLDDPDSAYLQEARLKRKLIRLFGRLCELKDCSSLTGRVIEQRIPYRGT 262
Cdd:cd13150   1 KRRKQIRRLEKLLKKLSKEIRKLEEKEVDL--LDDEDSAYIQEDRLKKRFVEIYKKLCELKGESPDTGRIVEKKIHFSGT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62898369 263 RYPEVNRRIERLINKpgPDTFPDYGDVLRAVEKAAARHSLGLPRQQLQLMAQDAFRDAGIRLQERRHLDLIYNFGCHLTD 342
Cdd:cd13150  79 RYPEVNRKIEKFVNR--NKTFPDFHDILKIVQKANRKKNLGLTEYQIKRLAKEAFTQVGNLLQKRRQNDLWENFGSHLTD 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 62898369 343 DyrpGVDPALSDPVLARRLRENRSLAMSRLDEVISKYAMLQDKSE 387
Cdd:cd13150 157 D---EKDPALEDPELKRKLEENRKIGDKRLNEVIEKYVNKQDDLE 198
Daxx pfam03344
Daxx N-terminal Rassf1C-interacting domain; The Daxx protein (also known as the Fas-binding ...
 56-144 2.28e-53

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: 178.81  E-value: 2.28e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62898369    56 KKCYKLENEKLCEEFLGLCKMQTADHPEVVPFLYNRQQRAHSLFLASAEFCNILSRVLSRARSRPAKLYVYINELCTVLK 135
Cdd:pfam03344   7 KKCLKLENEKLFEEFLELCKKQTSDHPEVVPFLQTRQQKARPEFLASAEFRNILGRCLSRAQARPAKTFVYINELCTVLK 86


                  ....*....
gi 62898369   136 AHSAKKKLN 144
Cdd:pfam03344  87 AHSAKKKLN 95
DAXX_helical_bundle cd13151
Helical bundle domain of the death-domain associated protein (DAXX); DAXX is a nuclear protein ...
 57-144 2.07e-39

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: 140.32  E-value: 2.07e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62898369  57 KCYKLENEKLCEEFLGLCKMQTADHPEVVPFLYNRQQRAHSLFLASAEFCNILSRVLSRARSRPAKLYVYINELCTVLKA 136
Cdd:cd13151   1 GVNKLENEKLFEEFLDKCLSDSAEHPEVVTFLRNRYSRATPEFLKSVEFKNILSRCLARIAARPAKLYVYINELCTVLKA 80


                ....*...
gi 62898369 137 HSAKKKLN 144
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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