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Conserved domains on  [gi|967506645|ref|XP_014983440|]
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PWWP domain-containing DNA repair factor 3B [Macaca mulatta]

Protein Classification

PWWP domain-containing protein( domain architecture ID 10149510)

PWWP domain-containing protein similar to Homo sapiens hepatoma-derived growth factor that may act as a transcriptional repressor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PWWP_MUM1-like cd06080
PWWP domain found in mutated melanoma-associated antigen 1 (MUM-1) and similar proteins; MUM-1, ...
 387-476 2.83e-34

PWWP domain found in mutated melanoma-associated antigen 1 (MUM-1) and similar proteins; MUM-1, also called PWWP domain-containing DNA repair factor 3A (PWWP3A), or protein expandere (EXPAND1), is a melanoma-associated antigen (MAA) that belongs to the mutated or aberrantly expressed type of MAAs, along with antigens such as CDK4, beta-catenin, gp100-in4, p15, and N-acetylglucosaminyltransferase V. It is highly expressed in several types of human cancers and involved in the DNA damage response pathway by contributing to the maintenance of chromatin architecture. MUM-1 is recruited to the vicinity of DNA breaks by TP53BP1 and plays an accessory role to facilitate damage-induced chromatin changes and promoting chromatin relaxation. It is required for efficient DNA repair and cell survival following DNA damage. This subfamily also includes mutated melanoma-associated antigen 1-like protein 1 (MUM1L1), also called MUM1-like protein 1, or PWWP domain-containing DNA repair factor 3B (PWWP3B). Its biological function remains unclear. The PWWP domain specifically recognizes DNA and histone methylated lysines.


:

Pssm-ID: 438967  Cd Length: 90  Bit Score: 125.44  E-value: 2.83e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967506645 387 FEAGMIVWFKYQKYPFWPAVIKSIRRKERKASVLFIEAnmNSEKKGIRVNFRRLKKFDCKEKQMLVNKARED-YSESIDW 465
Cdd:cd06080    1 FSKGDIVWAKYRKYPYWPAVVKSVYKKPKKASVLFLEL--PPEKKGIKVSLKKLKPFDCKEKEELLEEGKESpYSEDFKE 78

                         90
                 ....*....|.
gi 967506645 466 CISLICDYRVR 476
Cdd:cd06080   79 AVELAEDYLIK 89
 
Name Accession Description Interval E-value
PWWP_MUM1-like cd06080
PWWP domain found in mutated melanoma-associated antigen 1 (MUM-1) and similar proteins; MUM-1, ...
 387-476 2.83e-34

PWWP domain found in mutated melanoma-associated antigen 1 (MUM-1) and similar proteins; MUM-1, also called PWWP domain-containing DNA repair factor 3A (PWWP3A), or protein expandere (EXPAND1), is a melanoma-associated antigen (MAA) that belongs to the mutated or aberrantly expressed type of MAAs, along with antigens such as CDK4, beta-catenin, gp100-in4, p15, and N-acetylglucosaminyltransferase V. It is highly expressed in several types of human cancers and involved in the DNA damage response pathway by contributing to the maintenance of chromatin architecture. MUM-1 is recruited to the vicinity of DNA breaks by TP53BP1 and plays an accessory role to facilitate damage-induced chromatin changes and promoting chromatin relaxation. It is required for efficient DNA repair and cell survival following DNA damage. This subfamily also includes mutated melanoma-associated antigen 1-like protein 1 (MUM1L1), also called MUM1-like protein 1, or PWWP domain-containing DNA repair factor 3B (PWWP3B). Its biological function remains unclear. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438967  Cd Length: 90  Bit Score: 125.44  E-value: 2.83e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967506645 387 FEAGMIVWFKYQKYPFWPAVIKSIRRKERKASVLFIEAnmNSEKKGIRVNFRRLKKFDCKEKQMLVNKARED-YSESIDW 465
Cdd:cd06080    1 FSKGDIVWAKYRKYPYWPAVVKSVYKKPKKASVLFLEL--PPEKKGIKVSLKKLKPFDCKEKEELLEEGKESpYSEDFKE 78

                         90
                 ....*....|.
gi 967506645 466 CISLICDYRVR 476
Cdd:cd06080   79 AVELAEDYLIK 89
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 390-464 1.17e-03

PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain binds to Histone-4 methylated at lysine-20, H4K20me, suggesting that it is methyl-lysine recognition motif. Removal of two conserved aromatic residues in a hydrophobic cavity created by this domain within the full-length protein, Pdp1, abolishes the interaction o f the protein with H4K20me3. In fission yeast, Set9 is the sole enzyme that catalyzes all three states of H4K20me, and Set9-mediated H4K20me is required for efficient recruitment of checkpoint protein Crb2 to sites of DNA damage. The methylation of H4K20 is involved in a diverse array of cellular processes, such as organizing higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression.


Pssm-ID: 459964 [Multi-domain]  Cd Length: 92  Bit Score: 38.56  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967506645  390 GMIVWFKYQKYPFWPAVI----------KSIRRKERKASVLFIEANMNSekkgiRVNFRRLKKFDCKE-----KQMLVNK 454
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVvdpeelpenvLKPKKKDGEYLVRFFGDSEFA-----WVKPKDLKPFDEGDefeylKKKKKKK 75

                          90
                  ....*....|
gi 967506645  455 AREDYSESID 464
Cdd:pfam00855  76 KKKAFKKALE 85
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 387-421 7.27e-03

domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 35.40  E-value: 7.27e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 967506645   387 FEAGMIVWFKYQKYPFWPAVI---KSIR---RKERKASVLF 421
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVispKMTPdniMKRKSDENLY 41
 
Name Accession Description Interval E-value
PWWP_MUM1-like cd06080
PWWP domain found in mutated melanoma-associated antigen 1 (MUM-1) and similar proteins; MUM-1, ...
 387-476 2.83e-34

PWWP domain found in mutated melanoma-associated antigen 1 (MUM-1) and similar proteins; MUM-1, also called PWWP domain-containing DNA repair factor 3A (PWWP3A), or protein expandere (EXPAND1), is a melanoma-associated antigen (MAA) that belongs to the mutated or aberrantly expressed type of MAAs, along with antigens such as CDK4, beta-catenin, gp100-in4, p15, and N-acetylglucosaminyltransferase V. It is highly expressed in several types of human cancers and involved in the DNA damage response pathway by contributing to the maintenance of chromatin architecture. MUM-1 is recruited to the vicinity of DNA breaks by TP53BP1 and plays an accessory role to facilitate damage-induced chromatin changes and promoting chromatin relaxation. It is required for efficient DNA repair and cell survival following DNA damage. This subfamily also includes mutated melanoma-associated antigen 1-like protein 1 (MUM1L1), also called MUM1-like protein 1, or PWWP domain-containing DNA repair factor 3B (PWWP3B). Its biological function remains unclear. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438967  Cd Length: 90  Bit Score: 125.44  E-value: 2.83e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967506645 387 FEAGMIVWFKYQKYPFWPAVIKSIRRKERKASVLFIEAnmNSEKKGIRVNFRRLKKFDCKEKQMLVNKARED-YSESIDW 465
Cdd:cd06080    1 FSKGDIVWAKYRKYPYWPAVVKSVYKKPKKASVLFLEL--PPEKKGIKVSLKKLKPFDCKEKEELLEEGKESpYSEDFKE 78

                         90
                 ....*....|.
gi 967506645 466 CISLICDYRVR 476
Cdd:cd06080   79 AVELAEDYLIK 89
PWWP cd05162
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
 390-473 2.44e-06

PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, is a small domain consisting of 100-150 amino acids and is composed of a five-stranded antiparallel beta-barrel followed by a helical region. It is found in numerous proteins that are involved in cell division, growth, and differentiation. Most PWWP-domain proteins seem to be nuclear, often DNA-binding, proteins that function as transcription factors regulating a variety of developmental processes. PWWP domains specifically recognize DNA and histone methylated lysines at the level of the nucleosome. Based on the fact that other regions of PWWP-domain proteins are responsible for nuclear localization and DNA-binding, is likely that the PWWP domain acts as a site for protein-protein binding interactions, influencing chromatin remodeling and thereby regulating transcriptional processes. Some PWWP-domain proteins have been linked to cancer or other diseases; some are known to function as growth factors.


Pssm-ID: 438958 [Multi-domain]  Cd Length: 86  Bit Score: 45.95  E-value: 2.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967506645 390 GMIVWFKYQKYPFWPAVIKSIR---------RKERKASVLFIEANMNSEkkgirVNFRRLKKFDCKEKQMLVNKARedYS 460
Cdd:cd05162    1 GDLVWAKLKGYPWWPARVVDPEelpeevgkkKKKGGVLVQFFGDNDYAW-----VKSKNIKPFEEGFKKEFKKKKK--KS 73

                         90
                 ....*....|...
gi 967506645 461 ESIDWCISLICDY 473
Cdd:cd05162   74 KKFKKAVEEAEEA 86
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 390-464 1.17e-03

PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain binds to Histone-4 methylated at lysine-20, H4K20me, suggesting that it is methyl-lysine recognition motif. Removal of two conserved aromatic residues in a hydrophobic cavity created by this domain within the full-length protein, Pdp1, abolishes the interaction o f the protein with H4K20me3. In fission yeast, Set9 is the sole enzyme that catalyzes all three states of H4K20me, and Set9-mediated H4K20me is required for efficient recruitment of checkpoint protein Crb2 to sites of DNA damage. The methylation of H4K20 is involved in a diverse array of cellular processes, such as organizing higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression.


Pssm-ID: 459964 [Multi-domain]  Cd Length: 92  Bit Score: 38.56  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967506645  390 GMIVWFKYQKYPFWPAVI----------KSIRRKERKASVLFIEANMNSekkgiRVNFRRLKKFDCKE-----KQMLVNK 454
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVvdpeelpenvLKPKKKDGEYLVRFFGDSEFA-----WVKPKDLKPFDEGDefeylKKKKKKK 75

                          90
                  ....*....|
gi 967506645  455 AREDYSESID 464
Cdd:pfam00855  76 KKKAFKKALE 85
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 387-421 7.27e-03

domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 35.40  E-value: 7.27e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 967506645   387 FEAGMIVWFKYQKYPFWPAVI---KSIR---RKERKASVLF 421
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVispKMTPdniMKRKSDENLY 41
 
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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