PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family includes HUA2-like proteins 1-3 (HULK1-3), which are probable transcription factors that act with partial redundancy with each other. They may play diverse and essential roles in the control of plant development, physiology and flowering time. The PWWP domain specifically recognizes DNA and histone methylated lysines.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065802441   29 GDLVLAKVKGFPAWPAAVSEPEKWGASTDLKKVFVHFFGTQQIAFCNHTDVEAFTDERKQSLLTK--RHAKGSDFVRAVK 106
Cdd:cd20147      1 GDLVLAKVKGFPAWPAQVSEPEDWGSAPDPKKVFVHFFGTQQIGFCNPGELSEFTEEIKQSLLARtlKKKKGSDFSRAVK 80

                           90
                   ....*....|..
gi 2065802441  107 EIIESYEKLKQQ 118
Cdd:cd20147     81 EICELYEERKGQ 92

PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family includes HUA2-like proteins 1-3 (HULK1-3), which are probable transcription factors that act with partial redundancy with each other. They may play diverse and essential roles in the control of plant development, physiology and flowering time. The PWWP domain specifically recognizes DNA and histone methylated lysines.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065802441   29 GDLVLAKVKGFPAWPAAVSEPEKWGASTDLKKVFVHFFGTQQIAFCNHTDVEAFTDERKQSLLTK--RHAKGSDFVRAVK 106
Cdd:cd20147      1 GDLVLAKVKGFPAWPAQVSEPEDWGSAPDPKKVFVHFFGTQQIGFCNPGELSEFTEEIKQSLLARtlKKKKGSDFSRAVK 80

                           90
                   ....*....|..
gi 2065802441  107 EIIESYEKLKQQ 118
Cdd:cd20147     81 EICELYEERKGQ 92

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065802441   29 GDLVLAKVKGFPAWPAAVSEPEKWGASTDLKK-----VFVHFFGTQQIAFCNHTDVEAFTDERKQSLLTKRHAKGS--DF 101
Cdd:pfam00855    1 GDLVWAKLKGYPWWPARVVDPEELPENVLKPKkkdgeYLVRFFGDSEFAWVKPKDLKPFDEGDEFEYLKKKKKKKKkkAF 80

                           90
                   ....*....|..
gi 2065802441  102 VRAVKEIIESYE 113
Cdd:pfam00855   81 KKALEEAEEALK 92

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 2065802441    27 KVGDLVLAKVKGFPAWPAAVSEPEKWGASTDLKK-----VFVHFFGT 68
Cdd:smart00293    2 KPGDLVWAKMKGFPWWPALVISPKMTPDNIMKRKsdenlYPVLFFGD 48

PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family includes HUA2-like proteins 1-3 (HULK1-3), which are probable transcription factors that act with partial redundancy with each other. They may play diverse and essential roles in the control of plant development, physiology and flowering time. The PWWP domain specifically recognizes DNA and histone methylated lysines.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065802441   29 GDLVLAKVKGFPAWPAAVSEPEKWGASTDLKKVFVHFFGTQQIAFCNHTDVEAFTDERKQSLLTK--RHAKGSDFVRAVK 106
Cdd:cd20147      1 GDLVLAKVKGFPAWPAQVSEPEDWGSAPDPKKVFVHFFGTQQIGFCNPGELSEFTEEIKQSLLARtlKKKKGSDFSRAVK 80

                           90
                   ....*....|..
gi 2065802441  107 EIIESYEKLKQQ 118
Cdd:cd20147     81 EICELYEERKGQ 92

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065802441   29 GDLVLAKVKGFPAWPAAVSEPEKWGASTDLKK-----VFVHFFGTQQIAFCNHTDVEAFTDERKQSLLTKRHAKGS--DF 101
Cdd:pfam00855    1 GDLVWAKLKGYPWWPARVVDPEELPENVLKPKkkdgeYLVRFFGDSEFAWVKPKDLKPFDEGDEFEYLKKKKKKKKkkAF 80

                           90
                   ....*....|..
gi 2065802441  102 VRAVKEIIESYE 113
Cdd:pfam00855   81 KKALEEAEEALK 92

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065802441   29 GDLVLAKVKGFPAWPAAVSEPEKWGASTDLKK----VFVHFFGTQQIAFCNHTDVEAFTDERKQsLLTKRHAKGSDFVRA 104
Cdd:cd05162      1 GDLVWAKLKGYPWWPARVVDPEELPEEVGKKKkkggVLVQFFGDNDYAWVKSKNIKPFEEGFKK-EFKKKKKKSKKFKKA 79

                   ....*.
gi 2065802441  105 VKEIIE 110
Cdd:cd05162     80 VEEAEE 85

CID domain; This domain binds to the phosphorylated C-terminal domain (CTD) of RNA polymerase II. This domain is known as the CTD-interacting domain (CID).

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065802441  857 EDALSSLVRTKESIGRATRLAMDLMKFgvsAKAM-EILAHTLeSESNLKRRVDLFFLVDSIAQCSKGlKGDTgcVYLSAI 935
Cdd:pfam04818    4 EKKLSSLNNSQESIQTLSKWILFHRKH---AKAIvEVWEKYL-KKAKPEKKLHLLYLANDVLQNSRK-KGKS--EFADAF 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2065802441  936 QVILPRLLAAAVPAGAttQENRKQCLKVLKLWLERRILPESIV 978
Cdd:pfam04818   77 EPVLPEAFASAYKKCD--EKLKKKLERLLNIWEERNVFSPEVI 117

PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like proteins ATX1, ATX2, and similar proteins; This family includes A. thaliana ATX1 and ATX2, which are sister paralogs originating from a segmental chromosomal duplication. They are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1, also called protein SET domain group 27, or trithorax-homolog protein 1 (TRX-homolog protein 1), is a methyltransferase that trimethylates histone H3 at lysine 4 (H3K4me3). It also acts as a histone modifier and as a positive effector of gene expression. ATX1 regulates transcription from diverse classes of genes implicated in biotic and abiotic stress responses. It is involved in dehydration stress signaling in both abscisic acid (ABA)-dependent and ABA-independent pathways. ATX2, also called protein SET domain group 30, or trithorax-homolog protein 2 (TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). Both ATX1 and ATX2 are multi-domain containing proteins that consist of an N-terminal PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical plant homeodomain (PHD) domain, a non-canonical extended PHD (ePHD) domain, and a C-terminal SET domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065802441   28 VGDLVLAKVKGFPAWPAAV---SEPEKWGASTDLKK----VFVHFFGTQQIAFCNHTDVEAFTDERKQSLLTKRHAKgsD 100
Cdd:cd20142      2 PGDVVWAKVKGYPMWPALVideEHAERCGLEANRPGkkgtVPVQFFGTYEVARLNPKKVVGFSKGLDLKYHSKCKAP--V 79

                           90
                   ....*....|....*....
gi 2065802441  101 FVRAVKEiIESYekLKQQE 119
Cdd:cd20142     80 FRQALEE-AERY--LKEGK 95

PWWP domain found in Hepatoma-derived growth factor-related protein 3 (HDGFL3); HDGFL3, also called HDGF-related protein 3 (HRP-3), is the only hepatoma-derived growth factor (HDGF)-related protein (HRP) family member whose expression is almost restricted to the nervous tissue. It enhances DNA synthesis and may play a role in cell proliferation. It contains a PWWP domain, which is necessary for DNA binding.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065802441   25 KWKVGDLVLAKVKGFPAWPAAVSEPEKWGASTDLKKVFVHFFGTQQIAFCNHTDVEAFTDERKQ 88
Cdd:cd20150      5 EYKAGDLVFAKMKGYPHWPARIDELPEGAVKPPANKYPIFFFGTHETAFLGPKDLFPYKEYKDK 68

PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar proteins; ScIOC4 functions as a component of the ISW1B complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW1B complex acts within coding regions to control the amount of RNA polymerase II released into productive elongation and to coordinate elongation with termination and pre-mRNA processing. The family also includes Schizosaccharomyces pombe PWWP domain-containing proteins 1 and 2 (SpPDP1 and SpPDP2). SpPDP1 associates with Set9 to regulate its chromatin localization and methyltransferase activity towards H4K20. Members of this family contain a PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065802441   29 GDLVLAKVKGFPAWPA----------AVSEPEKWGASTDLKKVFVHFFGTQQIAFCNHTDVEAFTDERKQSLLTKRHAKG 98
Cdd:cd05840      1 GDLVLAKVKGYPPWPAmvlpeellpkNVLKAKKRKPKSKKTVYPVQFFPDNEYYWVSPSSLKPLTKEEIDKFLSKSKRKN 80

                           90
                   ....*....|....*
gi 2065802441   99 sdfvravKEIIESYE 113
Cdd:cd05840     81 -------KDLIEAYE 88

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 2065802441    27 KVGDLVLAKVKGFPAWPAAVSEPEKWGASTDLKK-----VFVHFFGT 68
Cdd:smart00293    2 KPGDLVWAKMKGFPWWPALVISPKMTPDNIMKRKsdenlYPVLFFGD 48

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065802441   27 KVGDLVLAKVKGFPAWPAAVsepekWGASTDLKKVFVHFFGT--QQIAFCNHTD-VEAFTDERKQSLLT--KRHAKGSDF 101
Cdd:cd06080      2 SKGDIVWAKYRKYPYWPAVV-----KSVYKKPKKASVLFLELppEKKGIKVSLKkLKPFDCKEKEELLEegKESPYSEDF 76

                           90
                   ....*....|....
gi 2065802441  102 VRAVKEIIESYEKL 115
Cdd:cd06080     77 KEAVELAEDYLIKK 90

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065802441   28 VGDLVLAKVKGFPAWPAAVSEPEK-----WGASTDLKKVFVHFFGTQQIAFCNHTDVEAFTDERKQSLLTKRHAKGSDFV 102
Cdd:cd05838      2 YGDIVWVKLGNYRWWPAEILHPREvpdniQSLPHPPGEFPVRFFGSHDYYWVHRGRVFLFEEGDKGSKEKSKKSLDKSFK 81

                           90
                   ....*....|....*
gi 2065802441  103 RAVKEIIESYEKLKQ 117
Cdd:cd05838     82 RALKEANEAFRELKA 96

PWWP domain found in the DNA (cytosine-5)-methyltransferase 3 (DNMT3) family; The DNMT3 family includes DNMT3A and DNMT3B, which are required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNMT3A, also called DNA methyltransferase HsaIIIA, DNA MTase HsaIIIA, or M.HsaIIIA, modifies DNA in a non-processive manner and also methylates non-CpG sites. It may preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. DNMT3A is recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. DNMT3B, also called DNA methyltransferase HsaIIIB, DNA MTase HsaIIIB, or M.HsaIIIB, may preferentially methylate nucleosomal DNA within the nucleosome core region. DNMT3B may function as a transcriptional co-repressor by associating with CBX4 and independently of DNA methylation. Members of this family contains a PWWP domain that is responsible for establishing DNA methylation patterns during embryogenesis and gametogenesis. In tumorigenesis, DNA methylation by DNMT3B is known to play a role in the inactivation of tumor suppressor genes. In addition, a point mutation in the PWWP domain of DNMT3B has been identified in patients with ICF (immunodeficiency, centromeric instability, and facial anomalie) syndrome , a rare autosomal recessive disorder characterized by hypomethylation of classical satellite DNA.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065802441   27 KVGDLVLAKVKGFPAWPAAVSEPEKWGASTDLK-KVFVHFFGTQQIAFCNHTDVEAFTDERKQslLTKRHAKGSDFVRAV 105
Cdd:cd05835      1 KIGDLVWAKLKGSPWWPGIVVSHKDCGQKPPAEgSVWVFWFGDHKVSEVPLDKILPFAEFFNK--FYISKNSSKLYKKAV 78

                   ....*....
gi 2065802441  106 KEIIESYEK 114
Cdd:cd05835     79 YEALKEAAE 87

PWWP domain found in the bromodomain and PHD finger-containing (BRPF) protein family; The BRPF family of proteins includes BRPF1, BRD1/BRPF2, and BRPF3. They are scaffold proteins that form monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complexes with other regulatory subunits, such as inhibitor of growth 5 (ING5) and Esa1-associated factor 6 ortholog (EAF6). BRPF proteins have multiple domains, including a plant homeodomain (PHD) zinc finger followed by a non-canonical extended PHD (ePHD) finger, C2HC5HC2H, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. The PHD finger binds to lysine 4 of histone H3 (K4H3), the bromodomain interacts with acetylated lysines on N-terminal tails of histones and other proteins, and the PWWP domain shows histone-binding and chromatin association properties.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065802441   26 WKVGDLVLAKVKGFPAWPAAVSEP----------------EKWGASTDlKKVFVHFFGTQqiafcnHT------------ 77
Cdd:cd05839      1 LEPGDLVWAKCRGYPWYPAEIVDPkdpkegngvpipvppdRVLKKSNE-KLYLVLFFDAK------RTwgwlprnklrpl 73

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2065802441   78 DVEAFTDERKQSLLTKRHAKgsdfvravKEIIESYEK 114
Cdd:cd05839     74 GVDEELDKLKLSEAKKSKRR--------KEVRKAYER 102

CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing proteins; This family is composed of Regulation of nuclear pre-mRNA domain-containing proteins 1A (RPRD1A), 1B (RPRD1B), 2 (RPRD2), yeast Rtt103, and similar proteins. RPRD1A, RPRD1B, and RPRD2 are CID (CTD-Interacting Domain) containing proteins that co-purify with RNA polymerase (Pol) II (RNAP II) and three other RNAP II-associated proteins, RPAP2, GRINL1A and RECQL5, but not with the Mediator complex. Yeast transcription termination factor Rtt103 is a CID containing protein that functions in DNA damage response. CID binds tightly to the carboxy-terminal domain (CTD) of RNAP II. During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065802441  900 ESNLKRRVDLFFLVDSIAQCSKGlKGDTgcVYLSAIQVILPRLLAAAVPAGatTQENRKQCLKVLKLWLERRILPESIVR 979
Cdd:cd16981     45 KAKPERKLTLLYLANDVLQNSRR-KGAP--EFVEAFKKVLPEALALVRSEG--DESVRKKVLRVLNIWEERNVFGSEFLA 119

first 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 the 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 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, through 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 first PWWP domain. This 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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2065802441   28 VGDLVLAKVKGFPAWPAAVSEPEKWGASTDLKKVF--------VHFFG 67
Cdd:cd20144      1 VGDLVWAKVSGHPWWPCMVTYDPESGLYTKIKGSGgrtyrqyhVQFFG 48