PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ubiquitin-protein ligase (G2E3); PHF7, also termed testis development protein NYD-SP6, is a testis-specific plant homeodomain (PHD) finger-containing protein that associates with chromatin and binds histone H3 N-terminal tails with a preference for dimethyl lysine 4 (H3K4me2). It may play an important role in stimulating transcription involved in testicular development and/or spermatogenesis. PHF7 contains a canonical Cys4HisCys3 PHD finger and a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, both of which may be involved in activating transcriptional regulation. G2E3 is a dual function ubiquitin ligase (E3) that may play a possible role in cell cycle regulation and the cellular response to DNA damage. It is essential for prevention of apoptosis in early embryogenesis. It is also a nucleo-cytoplasmic shuttling protein with DNA damage responsive localization. G2E3 contains two distinct RING-like ubiquitin ligase domains that catalyze lysine 48-linked polyubiquitination, and a C-terminal catalytic HECT domain that plays an important role in ubiquitin ligase activity and in the dynamic subcellular localization of the protein. The RING-like ubiquitin ligase domains consist of a PHD finger and an ePHD finger. This model corresponds to the Cys4HisCys3 canonical PHD finger.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 809279653 186 RCDVRRCRCKEGRDYNAPDSKWEIKRCQCCGSSGTHLACSSLRSWEQNWECLEC 239
Cdd:cd15496    1 RCDARKCLCPQGREYNEPEGKWELVLCQSCGSRGTHRACSSLRSWEQSWECVEC 54

PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ubiquitin-protein ligase (G2E3); PHF7, also termed testis development protein NYD-SP6, is a testis-specific plant homeodomain (PHD) finger-containing protein that associates with chromatin and binds histone H3 N-terminal tails with a preference for dimethyl lysine 4 (H3K4me2). It may play an important role in stimulating transcription involved in testicular development and/or spermatogenesis. PHF7 contains a canonical Cys4HisCys3 PHD finger and a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, both of which may be involved in activating transcriptional regulation. G2E3 is a dual function ubiquitin ligase (E3) that may play a possible role in cell cycle regulation and the cellular response to DNA damage. It is essential for prevention of apoptosis in early embryogenesis. It is also a nucleo-cytoplasmic shuttling protein with DNA damage responsive localization. G2E3 contains two distinct RING-like ubiquitin ligase domains that catalyze lysine 48-linked polyubiquitination, and a C-terminal catalytic HECT domain that plays an important role in ubiquitin ligase activity and in the dynamic subcellular localization of the protein. The RING-like ubiquitin ligase domains consist of a PHD finger and an ePHD finger. This model corresponds to the Cys4HisCys3 canonical PHD finger.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 809279653 186 RCDVRRCRCKEGRDYNAPDSKWEIKRCQCCGSSGTHLACSSLRSWEQNWECLEC 239
Cdd:cd15496    1 RCDARKCLCPQGREYNEPEGKWELVLCQSCGSRGTHRACSSLRSWEQSWECVEC 54

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809279653   365 EFLSLLMQHLENSS--LFEGSLSKNL----SLNSQALKENL--YYEAGKMLAISLVHGGPSPGFFSKTLFNCLVygpeNT 436
Cdd:smart00119  25 EFFFLLSKELFNPDygLFRYSPNDYLlypnPRSGFANEEHLsyFRFIGRVLGKALYDNRLLDLFFARPFYKKLL----GK 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809279653   437 QPILDDVSDFDVA-----QIIIRINTATTVADLKSIINEC-----YNYLELI--GCLRLITTlSDKYMLVKDILGYHVIQ 504
Cdd:smart00119 101 PVTLHDLESLDPElykslKWLLLNNDTSEELDLTFSIVLTsefgqVKVVELKpgGSNIPVTE-ENKKEYVHLVIEYRLNK 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809279653   505 RVHTPFESFKQGLKTLGVLEKIQAY-PEAFCSILCHKPEsLSAKILSElFTV------HTLPDVKAlgFWnsylQAVEdg 577
Cdd:smart00119 180 GIEKQLEAFREGFSEVIPENLLKLFdPEELELLICGSPE-IDVDDLKS-NTEykggysANSQTIKW--FW----EVVE-- 249

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 809279653   578 kSTTTME--DILIFATGCSSIPPAGFKPT-PSIeCLHVD------FPVGNKCNNCLAIPITNTYKEFQENMDFTIRNT 646
Cdd:smart00119 250 -SFTNEErrKLLQFVTGSSRLPVGGFAALsPKF-TIRKAgsdderLPTAHTCFNRLKLPPYSSKEILREKLLLAINEG 325

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809279653 317 RLYINKANIWNSALDAFRNR-NFNPSYAIEVAYVIENdnfGSEHPGSKQEFLSLLMQHLENSS--LFE--GSLSKNLSLN 391
Cdd:cd00078    2 KITVRRDRILEDALRQLSKVsSSDLKKVLEVEFVGEE---GIDAGGVTREFFTLVSKELFNPSygLFRytPDDSGLLYPN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809279653 392 SQA----LKENLYYEAGKMLAISLVHGGPSPGFFSKTLFNCLVYGPentqPILDDVSDFDvaqiiirintATTVADLKSI 467
Cdd:cd00078   79 PSSfadeDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKP----LSLEDLEELD----------PELYKSLKEL 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809279653 468 INecYNYLELIGCLRLITTLSDKYMLVKDI-----------------------LGYHVIQRVHTPFESFKQGLKTLGVLE 524
Cdd:cd00078  145 LD--NDGDEDDLELTFTIELDSSFGGAVTVelkpggrdipvtnenkeeyvdlyVDYRLNKGIEEQVEAFRDGFSEVIPEE 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809279653 525 KIQA-YPEAFCSILCHKPEslsakilselFTVHTLPDV-KALG-----------FWnsylQAVEdgkSTTTME--DILIF 589
Cdd:cd00078  223 LLSLfTPEELELLICGSED----------IDLEDLKKNtEYKGgyssdsptiqwFW----EVLE---SFTNEErkKFLQF 285

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 809279653 590 ATGCSSIPPAGFKPTP---SIECLHVD---FPVGNKCNNCLAIPITNTYKEFQENMDFTIRNT 646
Cdd:cd00078  286 VTGSSRLPVGGFADLNpkfTIRRVGSPddrLPTAHTCFNLLKLPPYSSKEILREKLLYAINEG 348

PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ubiquitin-protein ligase (G2E3); PHF7, also termed testis development protein NYD-SP6, is a testis-specific plant homeodomain (PHD) finger-containing protein that associates with chromatin and binds histone H3 N-terminal tails with a preference for dimethyl lysine 4 (H3K4me2). It may play an important role in stimulating transcription involved in testicular development and/or spermatogenesis. PHF7 contains a canonical Cys4HisCys3 PHD finger and a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, both of which may be involved in activating transcriptional regulation. G2E3 is a dual function ubiquitin ligase (E3) that may play a possible role in cell cycle regulation and the cellular response to DNA damage. It is essential for prevention of apoptosis in early embryogenesis. It is also a nucleo-cytoplasmic shuttling protein with DNA damage responsive localization. G2E3 contains two distinct RING-like ubiquitin ligase domains that catalyze lysine 48-linked polyubiquitination, and a C-terminal catalytic HECT domain that plays an important role in ubiquitin ligase activity and in the dynamic subcellular localization of the protein. The RING-like ubiquitin ligase domains consist of a PHD finger and an ePHD finger. This model corresponds to the Cys4HisCys3 canonical PHD finger.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 809279653 186 RCDVRRCRCKEGRDYNAPDSKWEIKRCQCCGSSGTHLACSSLRSWEQNWECLEC 239
Cdd:cd15496    1 RCDARKCLCPQGREYNEPEGKWELVLCQSCGSRGTHRACSSLRSWEQSWECVEC 54

Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the two ePHD fingers of PFH6 and the single ePHD finger of PFH11. PHF6, also termed the X-linked mental retardation disorder Borjeson-Forssman-Lehmann syndrome-associated protein, is a nucleolus, ribosomal RNA promoter-associated protein that regulates cell cycle progression by suppressing ribosomal RNA synthesis. It has been implicated in cell cycle control, genomic maintenance, and tumor suppression. PHF6 shows transcriptional repression activity through directly interacting with the nucleosome remodeling and deacetylation complex component RBBP4. PHF6 contains two non-canonical ePHD fingers. PHF11, also termed BRCA1 C-terminus-associated protein, or renal carcinoma antigen NY-REN-34, is a transcriptional co-activator of the Th1 effector cytokine genes, interleukin-2 (IL2) and interferon-gamma (IFNG), co-operating with nuclear factor kappa B (NF-kappaB). It is involved in T-cell activation and viability. Polymorphisms within PHF11 are associated with total IgE, allergic asthma and eczema.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809279653   2 SSGIWQRGKE-EEGVYGFLIEDIRKEVNRASKLKCCVCKKNGASIGCVAPRCKRSYHFPCGLQRECIFQF---TGNFASF 77
Cdd:cd15673   33 SSGLVQYVSPnENDFGGFDIEDVKKEIKRGRKLKCNLCKKTGATIGCDVKQCKKTYHYHCAKKDDAKIIErnsQGIYRVY 112

                 ....
gi 809279653  78 CWDH 81
Cdd:cd15673  113 CKNH 116

Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. PHF6 contains two non-canonical ePHD fingers, this model corresponds to the first ePHD finger. PHF6, also termed the X-linked mental retardation disorder Borjeson-Forssman-Lehmann syndrome-associated protein, is a nucleolus, ribosomal RNA promoter-associated protein that regulates cell cycle progression by suppressing ribosomal RNA synthesis. It has been implicated in cell cycle control, genomic maintenance, and tumor suppression. PHF6 shows transcriptional repression activity through directly interacting with the nucleosome remodeling and deacetylation complex component RBBP4. .

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 809279653   2 SSGIWQRGKEEEGVYGFLIEDIRKEVNRASKLKCCVCKKNGASIGCVAPRCKRSYHFPCGL 62
Cdd:cd15710   33 SSALVSSHSDSENLGGFSIEDVQKEIKRGTKLMCSLCHCPGATIGCDVKTCHRTYHYYCAL 93

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the second ePHD finger of KMT2C, and KMT2D. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named MLL4, a fourth human homolog of Drosophila trithorax, located on chromosome 12. It enzymatically generates trimethylated histone H3 Lysine 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. KMT2D is also a part of ASCOM. Both KMT2C and KMT2D contain the catalytic domain SET, five PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobilitygroup)-binding motif, and two FY-rich regions.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 809279653  29 RASKLKCCVCKKNGASIGCVAPRCKRSYHFPCGLQRECIF 68
Cdd:cd15666   55 RALTTTCSHCGRTGATVPCFKPRCANVYHLPCAIKDGCMF 94

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the first ePHD finger of KMTC2C and KMTC2D. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named MLL4, a fourth human homolog of Drosophila trithorax, located on chromosome 12. It enzymatically generates trimethylated histone H3 Lysine 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. KMT2D is also a part of ASCOM. Both KMT2C and KMT2D contain the catalytic domain SET, five plant PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobilitygroup)-binding motif, and two FY-rich regions.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 809279653  21 EDIRKEVNRASKLKCCVCKKNGASIGCVAPRCKRSYHFPCGLQRECiFQFTGNFASFCWDH 81
Cdd:cd15665   31 ENVDKAVAKALSQKCSFCLRYGASISCRMPSCSKSFHFPCAAAAGC-FQDIKTLTLFCPEH 90

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809279653   365 EFLSLLMQHLENSS--LFEGSLSKNL----SLNSQALKENL--YYEAGKMLAISLVHGGPSPGFFSKTLFNCLVygpeNT 436
Cdd:smart00119  25 EFFFLLSKELFNPDygLFRYSPNDYLlypnPRSGFANEEHLsyFRFIGRVLGKALYDNRLLDLFFARPFYKKLL----GK 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809279653   437 QPILDDVSDFDVA-----QIIIRINTATTVADLKSIINEC-----YNYLELI--GCLRLITTlSDKYMLVKDILGYHVIQ 504
Cdd:smart00119 101 PVTLHDLESLDPElykslKWLLLNNDTSEELDLTFSIVLTsefgqVKVVELKpgGSNIPVTE-ENKKEYVHLVIEYRLNK 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809279653   505 RVHTPFESFKQGLKTLGVLEKIQAY-PEAFCSILCHKPEsLSAKILSElFTV------HTLPDVKAlgFWnsylQAVEdg 577
Cdd:smart00119 180 GIEKQLEAFREGFSEVIPENLLKLFdPEELELLICGSPE-IDVDDLKS-NTEykggysANSQTIKW--FW----EVVE-- 249

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 809279653   578 kSTTTME--DILIFATGCSSIPPAGFKPT-PSIeCLHVD------FPVGNKCNNCLAIPITNTYKEFQENMDFTIRNT 646
Cdd:smart00119 250 -SFTNEErrKLLQFVTGSSRLPVGGFAALsPKF-TIRKAgsdderLPTAHTCFNRLKLPPYSSKEILREKLLLAINEG 325

Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. PHF6 contains two non-canonical ePHD fingers, this model corresponds to the second ePHD finger. PHF6, also termed the X-linked mental retardation disorder Borjeson-Forssman-Lehmann syndrome-associated protein, is a nucleolus, ribosomal RNA promoter-associated protein that regulates cell cycle progression by suppressing ribosomal RNA synthesis. It has been implicated in cell cycle control, genomic maintenance, and tumor suppression. PHF6 shows transcriptional repression activity through directly interacting with the nucleosome remodeling and deacetylation complex component RBBP4.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 809279653   2 SSGIWQRGKEEEGVYG-FLIEDIRKEVNRASKLKCCVCKKNGASIGCVAPRCKRSYHFPCGLQ 63
Cdd:cd15711   35 SSGTVQLTTTSRAEFGdFDIKTVIQEIKRGKRMKCTLCSQLGATIGCEIKACVKTYHYHCGVQ 97

Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of KMT2B. KMT2B is also called trithorax homolog 2 or WW domain-binding protein 7 (WBP-7). KMT2B is encoded by the gene that was first named myeloid/lymphoid or mixed-lineage leukemia 2 (MLL2), a second human homolog of Drosophila trithorax, located on chromosome 19. It belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2) and is vital for normal mammalian embryonic development. KMT2B functions as the catalytic subunit in the MLL2 complex, which contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL2 complex is highly active and specific for histone 3 lysine 4 (H3K4) methylation, which stimulates chromatin transcription in a SAM- and H3K4-dependent manner. Moreover, KMT2B plays a critical role in memory formation by mediating hippocampal H3K4 di- and trimethylation. It is also required for RNA polymerase II association and protection from DNA methylation at the MagohB CpG island promoter. KMT2B contains a CxxC (x for any residue) zinc finger domain, three PHD fingers, this ePHD finger, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 809279653  20 IEDIRKEVNRASKLKCCVCKKNGASIGCVAPRCKRSYHFPCGLQRECIFQftGNFASFCWDH 81
Cdd:cd15694   46 LKNVHAAVARGRQMRCEHCQKIGATVGCCLSACLSNFHFMCARASRCCFQ--DDKKVFCQKH 105

Extended PHD finger (ePHD) found in transcription factor 20 (TCF-20); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the C-terminal ePHD/ADD (ATRX-DNMT3-DNMT3L) domain of TCF-20. TCF-20, also termed nuclear factor SPBP, or protein AR1, or stromelysin-1 PDGF (platelet-derived growth factor)-responsive element-binding protein (SPRE-binding protein), is involved in transcriptional activation of the MMP3 (matrix metalloprotease 3) promoter. It is strongly enriched on chromatin in interphase HeLa cells, and displays low nuclear mobility, and has been implicated in Smith-Magenis syndrome and Potocki-Lupski syndrome. As a chromatin-binding protein, TCF-20 plays a role in the regulation of gene expression. It also functions as a transcriptional co-regulator that enhances or represses the transcriptional activity of certain transcription factors/cofactors, such as specificity protein 1 (Sp1), E twenty-six 1 (Ets1), paired box protein 6 (Pax6), small nuclear RING-finger (SNURF)/RNF4, c-Jun, androgen receptor (AR) and estrogen receptor alpha (ERalpha). TCF-20 contains an N-terminal transactivation domain, a novel DNA-binding domain with an AT-hook motif, three nuclear localization signals (NLSs) and a C-terminal ePHD/ADD domain.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 809279653  23 IRKEVNRASKLKCCVCKKNGASIGCVAPRCKRSYHFPCGLQRECIFQfTGNFASFCWDH 81
Cdd:cd15699   46 LQEALDIAREMKCSHCQEAGATLGCYNKGCSFRYHYPCAIDADCLLN-EENFSVRCPKH 103

Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the C-terminal ePHD/ADD (ATRX-DNMT3-DNMT3L) domain of RAI1. RAI1, a homolog of stromelysin-1 PDGF (platelet-derived growth factor)-responsive element-binding protein (SPBP, also termed TCF-20), is a chromatin-binding protein implicated in the regulation of gene expression. It is strongly enriched on chromatin in interphase HeLa cells, and displays low nuclear mobility, and has been implicated in Smith-Magenis syndrome, Potocki-Lupski syndrome, and non-syndromic autism. RAI1 contains a region with homology to the novel nucleosome-binding region SPBP and an ePHD/ADD domain with ability to bind nucleosomes.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 809279653  23 IRKEVNRASKLKCCVCKKNGASIGCVAPRCKRSYHFPCGLQRECIFQfTGNFASFCWDH 81
Cdd:cd15700   47 LQEAVQKAADAKCSSCQGAGATVGCCHKGCTQSYHYICAVEAGCLFE-EENFSLRCPKH 104

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the first ePHD finger of KMT2C. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2C contains several PHD fingers, two ePHD fingers, an ATPase alpha beta signature, a high mobility group (HMG)-1 box, a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain and two FY (phenylalanine tyrosine)-rich domains.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 809279653  19 LIEDIRKEVNRASKLKCCVCKKNGASIGCVAPRCKRSYHFPCGlQRECIFQFTGNFASFCWDH 81
Cdd:cd15696   29 LLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCA-AGAGTFQDFSRRLLLCPTH 90

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the first ePHD finger of KMT2D. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named myeloid/lymphoid or mixed-lineage leukemia 4 (MLL4), a fourth human homolog of Drosophila trithorax, located on chromosome 12. KMT2D enzymatically generates trimethylated histone H3 at Lys 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. It is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and KMT2D. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D contains the catalytic domain SET, five PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 809279653   2 SSGIWQRGKEEegvygflIEDIRKEVNRASKLKCCVCKKNGASIGCVAPRCKRSYHFPC 60
Cdd:cd15695   19 SAGVKQHEGDG-------LIGVDKAVFSGISQKCEHCKRLGATIQCHAEGCPRFYHFPC 70

Extended PHD finger found in BRPF proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the ePHD finger of the family of BRPF proteins, which includes BRPF1, BRD1/BRPF2, and BRPF3. These 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 ePHD finger, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. This 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.

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gi 809279653  32 KLKCCVCK-KNGASIGCVAPRCKRSYHFPCGLQ 63
Cdd:cd15670   54 KLTCYICKkRMGACIQCHKKNCYTAFHVTCAQQ 86

Extended PHD finger found in Drosophila melanogaster PHD finger protein rhinoceros (RNO) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Drosophila melanogaster RNO. RNO is a novel plant homeodomain (PHD)-containing nuclear protein that may function as a transcription factor that antagonizes Ras signaling by regulating the transcription of key EGFR/Ras pathway regulators in the Drosophila eye. RNO contains a canonical PHD domain followed by this non-canonical ePHD domain, both of which are zinc-binding motifs.

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gi 809279653  33 LKCCVCK-KNGASIGCVAPRCKRSYHFPCGLQ 63
Cdd:cd15707   56 LICVLCReRTGACIQCSVKTCKTAYHVTCGFQ 87