Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ubiquitin-protein ligase (G2E3); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of PHF7 and G2E3. PHF7, also termed testis development protein NYD-SP6, is a testis-specific 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 PHD finger and a non-canonical ePHD finger, 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548920  33 CLLCLQEPGDPEKLGEFLQKDNLCVHYFCLILSSRLPQKGQPNRGLHGFMPEDIKREAVRASKKICFVCKKKGAAIRCQN 112
Cdd:cd15669    1 CVLCGRSDDDPDKYGEKLQKDGICAHYFCLLFSSGLPQRGEDNEGIYGFLPEDIRKEVRRASRLRCFYCKKKGASIGCAV 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 755548920 113 DQCVQNFHLPCGQERGCLSQFFGEYKSYCRKH 144
Cdd:cd15669   81 KGCRRSFHFPCGLENGCVTQFFGEYRSFCWEH 112

Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ubiquitin-protein ligase (G2E3); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of PHF7 and G2E3. PHF7, also termed testis development protein NYD-SP6, is a testis-specific 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 PHD finger and a non-canonical ePHD finger, 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548920  33 CLLCLQEPGDPEKLGEFLQKDNLCVHYFCLILSSRLPQKGQPNRGLHGFMPEDIKREAVRASKKICFVCKKKGAAIRCQN 112
Cdd:cd15669    1 CVLCGRSDDDPDKYGEKLQKDGICAHYFCLLFSSGLPQRGEDNEGIYGFLPEDIRKEVRRASRLRCFYCKKKGASIGCAV 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 755548920 113 DQCVQNFHLPCGQERGCLSQFFGEYKSYCRKH 144
Cdd:cd15669   81 KGCRRSFHFPCGLENGCVTQFFGEYRSFCWEH 112

PHD zinc finger-containing protein [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548920  33 CLLClqepgdPEKLGEFLQK-DNLCVHYFCLILssrLPQKGQPNrgLHGFMP-EDIKREAVRASKKICFVCKKK-GAAIR 109
Cdd:COG5141  250 CSFC------PSSDGAFKQTsDGRWGHVICAMF---NPELSFGH--LLSKDPiDNIASVSSSRWKLGCLICKEFgGTCIQ 318

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 755548920 110 CQNDQCVQNFHLPCGQERG-------CLSQFFGEY--KSYCRKHRP 146
Cdd:COG5141  319 CSYFNCTRAYHVTCARRAGyfdlniySHNGISYCIdhEPLCRKHYP 364

Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ubiquitin-protein ligase (G2E3); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of PHF7 and G2E3. PHF7, also termed testis development protein NYD-SP6, is a testis-specific 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 PHD finger and a non-canonical ePHD finger, 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548920  33 CLLCLQEPGDPEKLGEFLQKDNLCVHYFCLILSSRLPQKGQPNRGLHGFMPEDIKREAVRASKKICFVCKKKGAAIRCQN 112
Cdd:cd15669    1 CVLCGRSDDDPDKYGEKLQKDGICAHYFCLLFSSGLPQRGEDNEGIYGFLPEDIRKEVRRASRLRCFYCKKKGASIGCAV 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 755548920 113 DQCVQNFHLPCGQERGCLSQFFGEYKSYCRKH 144
Cdd:cd15669   81 KGCRRSFHFPCGLENGCVTQFFGEYRSFCWEH 112

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 755548920  47 GEFLQKDNLCVHYFCLILSSRLPQKGQPNRG-LHGFMPEDIKREAVRASKKICFVCKKKGAAIRCQNDQCVQNFHLPCGQ 125
Cdd:cd15673   15 GKLASGEKIAAHHNCMLFSSGLVQYVSPNENdFGGFDIEDVKKEIKRGRKLKCNLCKKTGATIGCDVKQCKKTYHYHCAK 94

                         90       100
                 ....*....|....*....|..
gi 755548920 126 ERGCLSQFF---GEYKSYCRKH 144
Cdd:cd15673   95 KDDAKIIERnsqGIYRVYCKNH 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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548920  58 HYFCLILSSRLPQKGQPNRGLHGFMPEDIKREAVRASKKICFVCKKKGAAIRCQNDQCVQNFHLPC-----GQERGCLSQ 132
Cdd:cd15710   26 HHKCMLFSSALVSSHSDSENLGGFSIEDVQKEIKRGTKLMCSLCHCPGATIGCDVKTCHRTYHYYCalhdkAQIRENPSQ 105

                         90
                 ....*....|..
gi 755548920 133 ffGEYKSYCRKH 144
Cdd:cd15710  106 --GIYMIYCRKH 115

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        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755548920  92 RASKKICFVCKKKGAAIRCQNDQCVQNFHLPCGQERGCLsqFFGEYKSYCRKH 144
Cdd:cd15666   55 RALTTTCSHCGRTGATVPCFKPRCANVYHLPCAIKDGCM--FFKDKTMLCPSH 105

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548920  58 HYFCLILSSRLPQKGQPNRGLHG-FMPEDIKREAVRASKKICFVCKKKGAAIRCQNDQCVQNFHLPCGQE---RGCLSQF 133
Cdd:cd15711   28 HYKCMLFSSGTVQLTTTSRAEFGdFDIKTVIQEIKRGKRMKCTLCSQLGATIGCEIKACVKTYHYHCGVQdkaKYIENMS 107

                         90
                 ....*....|.
gi 755548920 134 FGEYKSYCRKH 144
Cdd:cd15711  108 RGIYKLYCKNH 118

Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of histone-lysine N-methyltransferase trithorax (Trx) like proteins, KMT2A/MLL1 and KMT2B/MLL2. KMT2A and KMT2B comprise the mammalian Trx branch of COMPASS family, and are both essential for mammalian embryonic development. KMT2A regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in the MLL1 complex. KMT2B is a second human homolog of Drosophila trithorax, located on chromosome 19 and functions as the catalytic subunit in the MLL2 complex. It 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. Both KMT2A and KMT2B contain a CxxC (x for any residue) zinc finger domain, three PHD fingers, this extended PHD (ePHD) finger, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755548920  89 EAVRASKKI-CFVCKKKGAAIRCQNDQCVQNFHLPCGQERGCLsqFFGEYKSYCRKH 144
Cdd:cd15664   51 SAVSRGRMMkCELCGKPGATVGCCLKSCPANYHFMCARKAECV--FQDDKKVFCPAH 105

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        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755548920  57 VHYFCLILSSRLPQKGQPNRglhgfmpEDIKREAVRASKKICFVCKKKGAAIRCQNDQCVQNFHLPCGQERGCL 130
Cdd:cd15665   11 AHHCCAAWSEGVCQTEDGAL-------ENVDKAVAKALSQKCSFCLRYGASISCRMPSCSKSFHFPCAAAAGCF 77

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755548920  95 KKICFVCKKK-GAAIRCQNDQCVQNFHLPCGQERG-------CLSQFFGEY-----KSYCRKH 144
Cdd:cd15670   54 KLTCYICKKRmGACIQCHKKNCYTAFHVTCAQQAGlymkiepVKDPGNGTSdsvrkEAYCDKH 116

PHD zinc finger-containing protein [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548920  33 CLLClqepgdPEKLGEFLQK-DNLCVHYFCLILssrLPQKGQPNrgLHGFMP-EDIKREAVRASKKICFVCKKK-GAAIR 109
Cdd:COG5141  250 CSFC------PSSDGAFKQTsDGRWGHVICAMF---NPELSFGH--LLSKDPiDNIASVSSSRWKLGCLICKEFgGTCIQ 318

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 755548920 110 CQNDQCVQNFHLPCGQERG-------CLSQFFGEY--KSYCRKHRP 146
Cdd:COG5141  319 CSYFNCTRAYHVTCARRAGyfdlniySHNGISYCIdhEPLCRKHYP 364