PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) finger typically characterized as Cys4HisCys3, and a non-canonical extended PHD finger, characterized as Cys2HisCys5HisCys2His. Variations include the RAG2 PHD finger characterized by Cys3His2Cys2His and the PHD finger 5 found in nuclear receptor-binding SET domain-containing proteins characterized by Cys4HisCys2His. The PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. Single or multiple copies of PHD fingers have 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. The PHD finger domain SF is structurally similar to the RING and FYVE_like superfamilies.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619784 1068 CVFCKRGPHKLGLGDLFGPYlvtsdcdeyraavqtpgaqdidgmfvnkrrredmvkgqernlpavpatlanimqapkism 1147
Cdd:cd15668     1 CVFCKRGPHYKGLGDLFGPY------------------------------------------------------------ 20

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619784 1148 hkrkrkqthdssisysddpnesrsqcssvdlldcsteskfvetfrgmgktsengFEVWLHEDCAVWSNDIHLIGAHVNGL 1227
Cdd:cd15668    21 ------------------------------------------------------YEVWVHEDCAVWAPGVYLVGGKLYGL 46

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 939619784 1228 DAAVWDSTRYQCVLCQQTGASICCFQRCCKAAAHVPCGRSANWSLSEEDRKVYCHLH 1284
Cdd:cd15668    47 EEAVWVAKQSVCSSCQQTGATIGCLHKGCKAKYHYPCAVESGCQLDEENFSLLCPKH 103

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        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619784 1068 CVFCKRGPHKLGLGDLFGPYlvtsdcdeyraavqtpgaqdidgmfvnkrrredmvkgqernlpavpatlanimqapkism 1147
Cdd:cd15668     1 CVFCKRGPHYKGLGDLFGPY------------------------------------------------------------ 20

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619784 1148 hkrkrkqthdssisysddpnesrsqcssvdlldcsteskfvetfrgmgktsengFEVWLHEDCAVWSNDIHLIGAHVNGL 1227
Cdd:cd15668    21 ------------------------------------------------------YEVWVHEDCAVWAPGVYLVGGKLYGL 46

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 939619784 1228 DAAVWDSTRYQCVLCQQTGASICCFQRCCKAAAHVPCGRSANWSLSEEDRKVYCHLH 1284
Cdd:cd15668    47 EEAVWVAKQSVCSSCQQTGATIGCLHKGCKAKYHYPCAVESGCQLDEENFSLLCPKH 103

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619784 1193 GMGKTSENGfeVWLHEDCAVWSNDIHLIGAH-------VNGLDAAVWDSTryqCVLCQQT-GASICCFQRCCKAAAHVPC 1264
Cdd:COG5141   258 GAFKQTSDG--RWGHVICAMFNPELSFGHLLskdpidnIASVSSSRWKLG---CLICKEFgGTCIQCSYFNCTRAYHVTC 332

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 939619784 1265 GRSANWSLSEE----------DRKVYCHLHrHEPG 1289
Cdd:COG5141   333 ARRAGYFDLNIyshngisyciDHEPLCRKH-YPLG 366

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        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619784 1068 CVFCKRGPHKLGLGDLFGPYlvtsdcdeyraavqtpgaqdidgmfvnkrrredmvkgqernlpavpatlanimqapkism 1147
Cdd:cd15668     1 CVFCKRGPHYKGLGDLFGPY------------------------------------------------------------ 20

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619784 1148 hkrkrkqthdssisysddpnesrsqcssvdlldcsteskfvetfrgmgktsengFEVWLHEDCAVWSNDIHLIGAHVNGL 1227
Cdd:cd15668    21 ------------------------------------------------------YEVWVHEDCAVWAPGVYLVGGKLYGL 46

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 939619784 1228 DAAVWDSTRYQCVLCQQTGASICCFQRCCKAAAHVPCGRSANWSLSEEDRKVYCHLH 1284
Cdd:cd15668    47 EEAVWVAKQSVCSSCQQTGATIGCLHKGCKAKYHYPCAVESGCQLDEENFSLLCPKH 103

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 939619784 1181 CSTESKFVETFRGMGKTSENGfevWLHEDCAVWSNDI---HLIGAHVNGLDAAVWDSTRYQCVLCQQT-GASICCFQRCC 1256
Cdd:cd15571     4 CPRSGGALKGGGALKTTSDGL---WVHVVCALWSPEVyfdDGTLLEVEGVSKIPKRRKKLKCSICGKRgGACIQCSYPGC 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 939619784 1257 KAAAHVPCGRSANWSLSEED----RKVYCHLH 1284
Cdd:cd15571    81 PRSFHVSCAIRAGCLFEFEDgpgnFVVYCPKH 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 939619784  1207 HEDCAVWSNDIHLIGAH-----VNGLDAAVWDSTRYQCVLC-QQTGASICCFQRCCKAAAHVPCGRSANWSL----SEED 1276
Cdd:pfam13771    1 HVVCALWSPELVQRGNDsmgfpIEDIEKIPKRRWKLKCYLCkKKGGACIQCSKKNCRRAFHVTCALEAGLLMqfdeDNGT 80

                   ....*...
gi 939619784  1277 RKVYCHLH 1284
Cdd:pfam13771   81 FKSYCKKH 88

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        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619784 1204 VWLHEDCAVWSNDIH--LIGAHVNgLDAAVWDSTRYQCVLCQQTGASICCFQRCCKAAAHVPCGRSANWSLSeEDRKVYC 1281
Cdd:cd15666    25 KWVHLNCALWSYEVYetQNGALMN-VEEALRRALTTTCSHCGRTGATVPCFKPRCANVYHLPCAIKDGCMFF-KDKTMLC 102

                  ...
gi 939619784 1282 HLH 1284
Cdd:cd15666   103 PSH 105

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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619784 1205 WLHEDCAVWS------NDIHLIGAHvngldAAVWDSTRYQCVLCQQTGASICCFQRCCKAAAHVPCGRsANWSLSEEDRK 1278
Cdd:cd15694    26 WTHVNCAIWSaevfeeNDGSLKNVH-----AAVARGRQMRCEHCQKIGATVGCCLSACLSNFHFMCAR-ASRCCFQDDKK 99

                  ....*.
gi 939619784 1279 VYCHLH 1284
Cdd:cd15694   100 VFCQKH 105

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the second 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 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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619784 1202 FEVWLHEDCAVWSNDIH--LIGAHVNgLDAAVWDSTRYQCVLCQQTGASICCFQRCCKAAAHVPCGRSANWSLSeEDRKV 1279
Cdd:cd15697    23 LDLWVHLNCALWSTEVYetQAGALIN-VELALRRGLQMKCVFCHKTGATSGCHRLRCTNVYHFTCAIKAQCMFF-KDKTM 100

                  ....*
gi 939619784 1280 YCHLH 1284
Cdd:cd15697   101 LCPMH 105

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the second 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 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        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619784 1203 EVWLHEDCAVWSNDIHLI--GAHVNgLDAAVWDSTRYQCVLCQQTGASICCFQRCCKAAAHVPCGRSANwSLSEEDRKVY 1280
Cdd:cd15698    24 DLWVHLNCALWSTEVYETqgGALMN-VEVALHRGLLTKCSLCQKTGATNSCNRLRCPNVYHFACAIRAK-CMFFKDKTML 101

                  ....*
gi 939619784 1281 CHLHR 1285
Cdd:cd15698   102 CPMHK 106

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619784 1203 EVWLHEDCAVWS-NDIHLIGAHVNGLDAAVWDSTRYQCVLCQQTGASI-CCFQRCCKaAAHVPCGRSANWSLSEEDRKVY 1280
Cdd:cd15665     8 EVYAHHCCAAWSeGVCQTEDGALENVDKAVAKALSQKCSFCLRYGASIsCRMPSCSK-SFHFPCAAAAGCFQDIKTLTLF 86

                  ....
gi 939619784 1281 CHLH 1284
Cdd:cd15665    87 CPEH 90

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619784 1205 WLHEDCAVWSNDIHlIG--------AHVNGLDAAVWDSTryqCVLCQQ-TGASICCFQRCCKAAAHVPCG 1265
Cdd:cd15707    20 WAHVSCALWIPEVS-IGcvekmepiTKISSIPASRWALI---CVLCRErTGACIQCSVKTCKTAYHVTCG 85

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619784 1193 GMGKTSENGfeVWLHEDCAVWSNDIHLIGAH-------VNGLDAAVWDSTryqCVLCQQT-GASICCFQRCCKAAAHVPC 1264
Cdd:COG5141   258 GAFKQTSDG--RWGHVICAMFNPELSFGHLLskdpidnIASVSSSRWKLG---CLICKEFgGTCIQCSYFNCTRAYHVTC 332

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 939619784 1265 GRSANWSLSEE----------DRKVYCHLHrHEPG 1289
Cdd:COG5141   333 ARRAGYFDLNIyshngisyciDHEPLCRKH-YPLG 366

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
                  ....*....|....*....|....*....|....*....|....*....|.
gi 939619784 1236 RYQCVLCQQTGASICCFQRCCKAAAHVPCGRSaNWSLSE--EDRKVYCHLH 1284
Cdd:cd15669    63 RLRCFYCKKKGASIGCAVKGCRRSFHFPCGLE-NGCVTQffGEYRSFCWEH 112