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Conserved domains on  [gi|1002243079|ref|XP_015625771|]
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uncharacterized protein At1g51745 [Oryza sativa Japonica Group]

Protein Classification

PWWP domain-containing protein( domain architecture ID 10467275)

PWWP domain-containing protein similar to Arabidopsis thaliana protein At1g51745

Gene Ontology:  GO:0003677|GO:0000166|GO:0005515
PubMed:  28510146|10802047|25277115

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 25-122 2.85e-12

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: 63.21  E-value: 2.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002243079  25 GTIVWVRRRNGSWWPGRILGPDELPPSQIMSPRSGT--PVKLLG-REDASVdwynieKSKRVKAFRCGEFDACIEKAeat 101
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVVDPEELPENVLKPKKKDGeyLVRFFGdSEFAWV------KPKDLKPFDEGDEFEYLKKK--- 71

                          90       100
                  ....*....|....*....|.
gi 1002243079 102 EGTSVKKREKYARREdAILHA 122
Cdd:pfam00855  72 KKKKKKKAFKKALEE-AEEAL 91
 
Name Accession Description Interval E-value
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 25-122 2.85e-12

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: 63.21  E-value: 2.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002243079  25 GTIVWVRRRNGSWWPGRILGPDELPPSQIMSPRSGT--PVKLLG-REDASVdwynieKSKRVKAFRCGEFDACIEKAeat 101
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVVDPEELPENVLKPKKKDGeyLVRFFGdSEFAWV------KPKDLKPFDEGDEFEYLKKK--- 71

                          90       100
                  ....*....|....*....|.
gi 1002243079 102 EGTSVKKREKYARREdAILHA 122
Cdd:pfam00855  72 KKKKKKKAFKKALEE-AEEAL 91
PWWP cd05162
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
 25-100 1.93e-11

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: 60.59  E-value: 1.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002243079  25 GTIVWVRRRNGSWWPGRILGPDELPPSQIMSPRSG-TPVKLLGreDASVDWYnieKSKRVKAFRCGE------------- 90
Cdd:cd05162     1 GDLVWAKLKGYPWWPARVVDPEELPEEVGKKKKKGgVLVQFFG--DNDYAWV---KSKNIKPFEEGFkkefkkkkkkskk 75

                          90
                  ....*....|
gi 1002243079  91 FDACIEKAEA 100
Cdd:cd05162    76 FKKAVEEAEE 85
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 23-58 7.59e-03

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 35.78  E-value: 7.59e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1002243079   23 SPGTIVWVRRRNGSWWPGRILGPdELPPSQIMSPRS 58
Cdd:smart00293   2 KPGDLVWAKMKGFPWWPALVISP-KMTPDNIMKRKS 36
 
Name Accession Description Interval E-value
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 25-122 2.85e-12

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: 63.21  E-value: 2.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002243079  25 GTIVWVRRRNGSWWPGRILGPDELPPSQIMSPRSGT--PVKLLG-REDASVdwynieKSKRVKAFRCGEFDACIEKAeat 101
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVVDPEELPENVLKPKKKDGeyLVRFFGdSEFAWV------KPKDLKPFDEGDEFEYLKKK--- 71

                          90       100
                  ....*....|....*....|.
gi 1002243079 102 EGTSVKKREKYARREdAILHA 122
Cdd:pfam00855  72 KKKKKKKAFKKALEE-AEEAL 91
PWWP cd05162
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
 25-100 1.93e-11

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: 60.59  E-value: 1.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002243079  25 GTIVWVRRRNGSWWPGRILGPDELPPSQIMSPRSG-TPVKLLGreDASVDWYnieKSKRVKAFRCGE------------- 90
Cdd:cd05162     1 GDLVWAKLKGYPWWPARVVDPEELPEEVGKKKKKGgVLVQFFG--DNDYAWV---KSKNIKPFEEGFkkefkkkkkkskk 75

                          90
                  ....*....|
gi 1002243079  91 FDACIEKAEA 100
Cdd:cd05162    76 FKKAVEEAEE 85
PWWP_NSD_rpt2 cd05838
second PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
 25-109 1.23e-06

second PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein family consists of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1, that are critical in maintaining chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising in suppressing cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play nonredundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (C5HCH). This model corresponds to the second PWWP domain. The family also includes Drosophila melanogaster maternal-effect sterile 4 (dMes4) that may act as a histone-lysine N-methyltransferase required for wing morphogenesis. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438963 [Multi-domain]  Cd Length: 96  Bit Score: 47.23  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002243079  25 GTIVWVRRRNGSWWPGRILGPDELPPS-QIMSPRSGT-PVKLLGREDasVDWYNiekSKRVKAFRCGefDACIEKAEATE 102
Cdd:cd05838     3 GDIVWVKLGNYRWWPAEILHPREVPDNiQSLPHPPGEfPVRFFGSHD--YYWVH---RGRVFLFEEG--DKGSKEKSKKS 75


                  ....*..
gi 1002243079 103 GTSVKKR 109
Cdd:cd05838    76 LDKSFKR 82
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 23-58 7.59e-03

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 35.78  E-value: 7.59e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1002243079   23 SPGTIVWVRRRNGSWWPGRILGPdELPPSQIMSPRS 58
Cdd:smart00293   2 KPGDLVWAKMKGFPWWPALVISP-KMTPDNIMKRKS 36
 
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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