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 21313646  33 CLLCLQEPGDPEKLGEFLQKDNLCVHYFCLILSSRLPQKGQPNRGLHGFMPEDIKREAVRASKKICFVCKKKGAAIRCQN 112
Cdd:cd15669   1 CVLCGRSDDDPDKYGEKLQKDGICAHYFCLLFSSGLPQRGEDNEGIYGFLPEDIRKEVRRASRLRCFYCKKKGASIGCAV 80

                        90       100       110
                ....*....|....*....|....*....|..
gi 21313646 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 21313646  33 CLLCLQEPGDPEKLGEFLQKDNLCVHYFCLILSSRLPQKGQPNRGLHGFMPEDIKREAVRASKKICFVCKKKGAAIRCQN 112
Cdd:cd15669   1 CVLCGRSDDDPDKYGEKLQKDGICAHYFCLLFSSGLPQRGEDNEGIYGFLPEDIRKEVRRASRLRCFYCKKKGASIGCAV 80

                        90       100       110
                ....*....|....*....|....*....|..
gi 21313646 113 DQCVQNFHLPCGQERGCLSQFFGEYKSYCRKH 144
Cdd:cd15669  81 KGCRRSFHFPCGLENGCVTQFFGEYRSFCWEH 112

PHD-like zinc-binding domain; The members of this family are annotated as containing PHD domain, but the zinc-binding region here is not typical of PHD domains. The conformation here is a well-conserved cysteine-histidine rich region spanning 90 residues, where the Cys and His are arranged as HxxC(31)CxxC(6)CxxCxxxxCxxxxHxxC (21)CxxH.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313646    58 HYFCLILSSRLPQKGQPNRGlhgFMPEDIKREAVRASKKICFVCKKK-GAAIRCQNDQCVQNFHLPCGQERGCLSQFF-- 134
Cdd:pfam13771   1 HVVCALWSPELVQRGNDSMG---FPIEDIEKIPKRRWKLKCYLCKKKgGACIQCSKKNCRRAFHVTCALEAGLLMQFDed 77

                          90
                  ....*....|.
gi 21313646   135 -GEYKSYCRKH 144
Cdd:pfam13771  78 nGTFKSYCKKH 88

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 21313646  33 CLLCLQEPGDPEKLGEFLQKDNLCVHYFCLILSSRLPQKGQPNRGLHGFMPEDIKREAVRASKKICFVCKKKGAAIRCQN 112
Cdd:cd15669   1 CVLCGRSDDDPDKYGEKLQKDGICAHYFCLLFSSGLPQRGEDNEGIYGFLPEDIRKEVRRASRLRCFYCKKKGASIGCAV 80

                        90       100       110
                ....*....|....*....|....*....|..
gi 21313646 113 DQCVQNFHLPCGQERGCLSQFFGEYKSYCRKH 144
Cdd:cd15669  81 KGCRRSFHFPCGLENGCVTQFFGEYRSFCWEH 112

PHD-like zinc-binding domain; The members of this family are annotated as containing PHD domain, but the zinc-binding region here is not typical of PHD domains. The conformation here is a well-conserved cysteine-histidine rich region spanning 90 residues, where the Cys and His are arranged as HxxC(31)CxxC(6)CxxCxxxxCxxxxHxxC (21)CxxH.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313646    58 HYFCLILSSRLPQKGQPNRGlhgFMPEDIKREAVRASKKICFVCKKK-GAAIRCQNDQCVQNFHLPCGQERGCLSQFF-- 134
Cdd:pfam13771   1 HVVCALWSPELVQRGNDSMG---FPIEDIEKIPKRRWKLKCYLCKKKgGACIQCSKKNCRRAFHVTCALEAGLLMQFDed 77

                          90
                  ....*....|.
gi 21313646   135 -GEYKSYCRKH 144
Cdd:pfam13771  78 nGTFKSYCKKH 88

Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. The extended PHD finger is characterized as Cys2HisCys5HisCys2His, which has been found in a variety of eukaryotic proteins involved in the control of gene transcription and chromatin dynamics. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. They also function as epigenome readers controlling gene expression through molecular recruitment of multi-protein complexes of chromatin regulators and transcription factors.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313646  33 CLLCLQEPGDPEKLGEFLQKDNLC-VHYFCLILSSRLPQKGQPNRGLHGfmpedIKREAVRASKKICFVCKKK-GAAIRC 110
Cdd:cd15571   1 CALCPRSGGALKGGGALKTTSDGLwVHVVCALWSPEVYFDDGTLLEVEG-----VSKIPKRRKKLKCSICGKRgGACIQC 75

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 21313646 111 QNDQCVQNFHLPCGQERGCLSQFFGE---YKSYCRKH 144
Cdd:cd15571  76 SYPGCPRSFHVSCAIRAGCLFEFEDGpgnFVVYCPKH 112

Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 (TCF-20) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the C-terminal ePHD/ADD (ATRX-DNMT3-DNMT3L) domain of RAI1 and TCF-20. 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. TCF-20 is involved in transcriptional activation of the MMP3 (matrix metalloprotease 3) promoter. 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). Both RAI1 and TCF-20 are strongly enriched in chromatin in interphase HeLa cells, and display low nuclear mobility, and have been implicated in Smith-Magenis syndrome and Potocki-Lupski syndrome.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21313646  89 EAVRASKK-ICFVCKKKGAAIRCQNDQCVQNFHLPCGQERGCLSQfFGEYKSYCRKH 144
Cdd:cd15668  48 EAVWVAKQsVCSSCQQTGATIGCLHKGCKAKYHYPCAVESGCQLD-EENFSLLCPKH 103

Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of PHF11. 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 21313646  49 FLQKDNLCVHYFCLILSSRL--PQKGQPNRGLHGFMPEDIKREAVRASKKICFVCKKKGAAIRCQNDQCVQNFHLPCGQE 126
Cdd:cd15712  15 FAQEQNIAAHQNCLLYSSGFveSEEYNPLNLDRRFDVESVLNEIKRGKRLKCNFCRKKGATVGCEERACRRSYHYFCALC 94

                        90       100
                ....*....|....*....|.
gi 21313646 127 RGCLSQ---FFGEYKSYCRKH 144
Cdd:cd15712  95 DDAAIEtdeVRGIYRVFCQKH 115

Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of KMT2A. KMT2A also termed ALL-1, or CXXC-type zinc finger protein 7, or myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), or trithorax-like protein (Htrx), or zinc finger protein HRX, is a histone methyltransferase that belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2). It 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, which also contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL1 complex is highly active and specific for H3K4methylation. KMT2A contains a CxxC (x for any residue) zinc finger domain, three PHD fingers, a Bromodomain domain, this extended PHD 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 21313646  84 EDIKREAVRASKKICFVCKKKGAAIRCQNDQCVQNFHLPCGQERGCLsqFFGEYKSYCRKHR 145
Cdd:cd15693  49 KNVHMAVIRGKQLRCEFCQKPGATVGCCLTSCTSNYHFMCSRAKNCV--FLEDKKVYCQRHK 108

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 21313646  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 21313646  95 KKICFVCKKK-GAAIRCQNDQCVQNFHLPCGQERG-------CLSQFFGEY-----KSYCRKH 144
Cdd:cd15670  54 KLTCYICKKRmGACIQCHKKNCYTAFHVTCAQQAGlymkiepVKDPGNGTSdsvrkEAYCDKH 116

Extended PHD finger found in bromodomain and PHD finger-containing protein 3 (BRPF3) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of BRPF3. BRF3 is a homolog of BRPF1 and BRPF2. It is a scaffold protein that forms a novel monocytic leukemic zinc finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complex with other regulatory subunits. BRPF3 contains a plant homeodomain (PHD) finger followed by this non-canonical ePHD finger, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain.

                        10        20        30
                ....*....|....*....|....*....|....*.
gi 21313646  95 KKICFVCKKKG--AAIRCQNDQCVQNFHLPCGQERG 128
Cdd:cd15703  54 KLTCYLCKQKGrgAAIQCHKVNCYTAFHVTCAQRAG 89

Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-1 (PHF17), Jade-2 (PHF15), and Jade-3 (PHF16); each of these proteins is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and EAF6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, has reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. This family also contains Drosophila melanogaster PHD finger protein rhinoceros (RNO). It is a novel plant homeodomain (PHD)-containing nuclear protein that may function as a transcription factor that antagonizes Ras signaling by regulating transcription of key EGFR/Ras pathway regulators in the Drosophila eye. All Jade proteins contain a canonical PHD finger followed by this non-canonical ePHD finger, both of which are zinc-binding motifs.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21313646  97 ICFVCK-KKGAAIRCQNDQCVQNFHLPCGQERGC-LSQFFGE------YKSYCRKH 144
Cdd:cd15671  57 VCVLCKeKTGACIQCSVKSCKTAFHVTCAFQHGLeMKTILEDeddevkFKSYCPKH 112