NCBI Conserved Domain Search

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.

Pssm-ID: 277181 Cd Length: 118 Bit Score: 236.52 E-value: 7.64e-78

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707401627 255 CGFCHAGEDENETRGVLHSDNAKKVAAHYKCMLFSSGTVQLTTSSRAEFGNFEIKTVIQEIKRGKRMKCTLCGQLGATIG 334
Cdd:cd15711     1 CGFCHAGEEENETRGKLHIFNAKKAAAHYKCMLFSSGTVQLTTTSRAEFGDFDIKTVIQEIKRGKRMKCTLCSQLGATIG 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1707401627 335 CEIKACVKTYHYHCGLEDKAKYIENMARGIYKLYCKNH 372
Cdd:cd15711    81 CEIKACVKTYHYHCGVQDKAKYIENMSRGIYKLYCKNH 118

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.

Pssm-ID: 277143 Cd Length: 116 Bit Score: 177.97 E-value: 3.44e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707401627 255 CGFCHAGEDENETRGVLHSDnaKKVAAHYKCMLFSSGTVQLTTSSRAEFGNFEIKTVIQEIKRGKRMKCTLCGQLGATIG 334
Cdd:cd15673     1 CGFCKSGEENKETGGKLASG--EKIAAHHNCMLFSSGLVQYVSPNENDFGGFDIEDVKKEIKRGRKLKCNLCKKTGATIG 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1707401627 335 CEIKACVKTYHYHCGLEDKAKYIENMARGIYKLYCKNH 372
Cdd:cd15673    79 CDVKQCKKTYHYHCAKKDDAKIIERNSQGIYRVYCKNH 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. .

Pssm-ID: 277180 Cd Length: 115 Bit Score: 172.45 E-value: 5.08e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707401627  90 LFSSALVTSHCDSENIGGFSIEDVKKEIKRGNKLMCTSCHRPGATIGCDVKTCRRTYHYYCALWDKAQTKENPSQGIYLV 169
Cdd:cd15710    31 LFSSALVSSHSDSENLGGFSIEDVQKEIKRGTKLMCSLCHCPGATIGCDVKTCHRTYHYYCALHDKAQIRENPSQGIYMI 110


                  ....*
gi 1707401627 170 YCRKH 174
Cdd:cd15710   111 YCRKH 115

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.

Pssm-ID: 277143 Cd Length: 116 Bit Score: 131.75 E-value: 2.18e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707401627  90 LFSSALVTSHCDSEN-IGGFSIEDVKKEIKRGNKLMCTSCHRPGATIGCDVKTCRRTYHYYCALWDKAQTKENPSQGIYL 168
Cdd:cd15673    31 LFSSGLVQYVSPNENdFGGFDIEDVKKEIKRGRKLKCNLCKKTGATIGCDVKQCKKTYHYHCAKKDDAKIIERNSQGIYR 110


                  ....*.
gi 1707401627 169 VYCRKH 174
Cdd:cd15673   111 VYCKNH 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. .

Pssm-ID: 277180 Cd Length: 115 Bit Score: 120.07 E-value: 4.81e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707401627 255 CGFCHAGEDEnETRGVLHSDNaKKVAAHYKCMLFSSGTVQlTTSSRAEFGNFEIKTVIQEIKRGKRMKCTLCGQLGATIG 334
Cdd:cd15710     1 CGFCRSNREK-ECGQLLISEN-QKVAAHHKCMLFSSALVS-SHSDSENLGGFSIEDVQKEIKRGTKLMCSLCHCPGATIG 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1707401627 335 CEIKACVKTYHYHCGLEDKAKYIENMARGIYKLYCKNH 372
Cdd:cd15710    78 CDVKTCHRTYHYYCALHDKAQIRENPSQGIYMIYCRKH 115

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.

Pssm-ID: 277182 [Multi-domain] Cd Length: 115 Bit Score: 97.66 E-value: 1.03e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707401627 255 CGFCHAGEDENetrgVLHSDNAKKVAAHYKCMLFSSGTVQLTTSSRAEFG-NFEIKTVIQEIKRGKRMKCTLCGQLGATI 333
Cdd:cd15712     1 CAFCPKGEEYS----IMYFAQEQNIAAHQNCLLYSSGFVESEEYNPLNLDrRFDVESVLNEIKRGKRLKCNFCRKKGATV 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1707401627 334 GCEIKACVKTYHYHCGLEDKAKYIENMARGIYKLYCKNH 372
Cdd:cd15712    77 GCEERACRRSYHYFCALCDDAAIETDEVRGIYRVFCQKH 115

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.

Pssm-ID: 277182 [Multi-domain] Cd Length: 115 Bit Score: 91.88 E-value: 1.59e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707401627  90 LFSSALVTSH-CDSENIG-GFSIEDVKKEIKRGNKLMCTSCHRPGATIGCDVKTCRRTYHYYCALWDKAQTKENPSQGIY 167
Cdd:cd15712    29 LYSSGFVESEeYNPLNLDrRFDVESVLNEIKRGKRLKCNFCRKKGATVGCEERACRRSYHYFCALCDDAAIETDEVRGIY 108


                  ....*..
gi 1707401627 168 LVYCRKH 174
Cdd:cd15712   109 RVFCQKH 115

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.

Pssm-ID: 463977 [Multi-domain] Cd Length: 88 Bit Score: 89.70 E-value: 4.61e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707401627 282 HYKCMLFSSGTVQLTTssraEFGNFEIKTVIQEIKRGKRMKCTLCGQ-LGATIGCEIKACVKTYHYHCGLEDKAKYIENM 360
Cdd:pfam13771   1 HVVCALWSPELVQRGN----DSMGFPIEDIEKIPKRRWKLKCYLCKKkGGACIQCSKKNCRRAFHVTCALEAGLLMQFDE 76

                          90
                  ....*....|..
gi 1707401627 361 ARGIYKLYCKNH 372
Cdd:pfam13771  77 DNGTFKSYCKKH 88

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.

Pssm-ID: 277181 Cd Length: 118 Bit Score: 88.99 E-value: 1.66e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707401627  90 LFSSALVTSHCDSE-NIGGFSIEDVKKEIKRGNKLMCTSCHRPGATIGCDVKTCRRTYHYYCALWDKAQTKENPSQGIYL 168
Cdd:cd15711    33 LFSSGTVQLTTTSRaEFGDFDIKTVIQEIKRGKRMKCTLCSQLGATIGCEIKACVKTYHYHCGVQDKAKYIENMSRGIYK 112


                  ....*.
gi 1707401627 169 VYCRKH 174
Cdd:cd15711   113 LYCKNH 118

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.

Pssm-ID: 463977 [Multi-domain] Cd Length: 88 Bit Score: 87.38 E-value: 2.72e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707401627  90 LFSSALVTSHCDSeniGGFSIEDVKKEIKRGNKLMCTSCHRP-GATIGCDVKTCRRTYHYYCALWDKAQTKENPSQGIYL 168
Cdd:pfam13771   6 LWSPELVQRGNDS---MGFPIEDIEKIPKRRWKLKCYLCKKKgGACIQCSKKNCRRAFHVTCALEAGLLMQFDEDNGTFK 82


                  ....*.
gi 1707401627 169 VYCRKH 174
Cdd:pfam13771  83 SYCKKH 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.

Pssm-ID: 277139 [Multi-domain] Cd Length: 112 Bit Score: 86.15 E-value: 1.45e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707401627 255 CGFCHAGEDENETRGVLHSDNakKVAAHYKCMLFSSGTVQlTTSSRAEFGNFEIKTVIQEIKRGKRMKCTLCGQLGATIG 334
Cdd:cd15669     1 CVLCGRSDDDPDKYGEKLQKD--GICAHYFCLLFSSGLPQ-RGEDNEGIYGFLPEDIRKEVRRASRLRCFYCKKKGASIG 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1707401627 335 CEIKACVKTYHYHCGLEDKAKyieNMARGIYKLYCKNH 372
Cdd:cd15669    78 CAVKGCRRSFHFPCGLENGCV---TQFFGEYRSFCWEH 112

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.

Pssm-ID: 277046 [Multi-domain] Cd Length: 112 Bit Score: 79.94 E-value: 2.35e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707401627 255 CGFCHaGEDENETRGVLHSDNAKKVAAHYKCMLFSSGTVQLTTSSRaefgnfEIKTVIQEIKRGKRMKCTLCGQ-LGATI 333
Cdd:cd15571     1 CALCP-RSGGALKGGGALKTTSDGLWVHVVCALWSPEVYFDDGTLL------EVEGVSKIPKRRKKLKCSICGKrGGACI 73

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1707401627 334 GCEIKACVKTYHYHCGLEDKAKYIENMARGIYKLYCKNH 372
Cdd:cd15571    74 QCSYPGCPRSFHVSCAIRAGCLFEFEDGPGNFVVYCPKH 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.

Pssm-ID: 277139 [Multi-domain] Cd Length: 112 Bit Score: 79.60 E-value: 3.69e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707401627  90 LFSSALVTSHCDSENIGGFSIEDVKKEIKRGNKLMCTSCHRPGATIGCDVKTCRRTYHYYCALWDKAQTkenpsQ--GIY 167
Cdd:cd15669    31 LFSSGLPQRGEDNEGIYGFLPEDIRKEVRRASRLRCFYCKKKGASIGCAVKGCRRSFHFPCGLENGCVT-----QffGEY 105


                  ....*..
gi 1707401627 168 LVYCRKH 174
Cdd:cd15669   106 RSFCWEH 112

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.

Pssm-ID: 277046 [Multi-domain] Cd Length: 112 Bit Score: 64.14 E-value: 1.13e-12

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1707401627 110 IEDVKKEIKRGNKLMCTSCHRP-GATIGCDVKTCRRTYHYYCALWDKAQTKENPSQGIYLVYCRKH 174
Cdd:cd15571    47 VEGVSKIPKRRKKLKCSICGKRgGACIQCSYPGCPRSFHVSCAIRAGCLFEFEDGPGNFVVYCPKH 112

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.

Pssm-ID: 277134 Cd Length: 105 Bit Score: 62.04 E-value: 5.34e-12

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1707401627 308 IKTVIQEIKRGKRMKCTLCGQLGATIGCEIKACVKTYHYHCGLEDKAKYIENMargiyKLYCKNH 372
Cdd:cd15664    46 LQNVHSAVSRGRMMKCELCGKPGATVGCCLKSCPANYHFMCARKAECVFQDDK-----KVFCPAH 105

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.

Pssm-ID: 277134 Cd Length: 105 Bit Score: 59.73 E-value: 3.65e-11

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1707401627 103 ENIGGfSIEDVKKEIKRGNKLMCTSCHRPGATIGCDVKTCRRTYHYYCALWDKAQTKENPSqgiylVYCRKH 174
Cdd:cd15664    40 EEDDG-SLQNVHSAVSRGRMMKCELCGKPGATVGCCLKSCPANYHFMCARKAECVFQDDKK-----VFCPAH 105

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.

Pssm-ID: 277163 Cd Length: 113 Bit Score: 57.70 E-value: 2.40e-10

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1707401627 109 SIEDVKKEIKRGNKLMCTSCHRPGATIGCDVKTCRRTYHYYCALWDKAQTKENPSqgiylVYCRKHRD 176
Cdd:cd15693    47 SLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSCTSNYHFMCSRAKNCVFLEDKK-----VYCQRHKD 109

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.

Pssm-ID: 277163 Cd Length: 113 Bit Score: 55.78 E-value: 1.11e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707401627 281 AHYKCMLFSSGTVQLTTSSraefgnfeIKTVIQEIKRGKRMKCTLCGQLGATIGCEIKACVKTYHYHCGLEDKAKYIENM 360
Cdd:cd15693    29 THVNCALWSAEVFEDDDGS--------LKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSCTSNYHFMCSRAKNCVFLEDK 100

                          90
                  ....*....|..
gi 1707401627 361 argiyKLYCKNH 372
Cdd:cd15693   101 -----KVYCQRH 107

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.

Pssm-ID: 277136 Cd Length: 105 Bit Score: 54.23 E-value: 2.88e-09

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1707401627 102 SENIGGfSIEDVKKEIKRGNKLMCTSCHRPGATIGCDVKTCRRTYHYYCALWDKAQTKENPSqgiylVYCRKH 174
Cdd:cd15666    39 YETQNG-ALMNVEEALRRALTTTCSHCGRTGATVPCFKPRCANVYHLPCAIKDGCMFFKDKT-----MLCPSH 105

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.

Pssm-ID: 277138 Cd Length: 103 Bit Score: 53.47 E-value: 5.62e-09

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1707401627 315 IKRGKRMKCTLCGQLGATIGCEIKACVKTYHYHCGLEDKAKYIENMargiYKLYCKNH 372
Cdd:cd15668    50 VWVAKQSVCSSCQQTGATIGCLHKGCKAKYHYPCAVESGCQLDEEN----FSLLCPKH 103

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.

Pssm-ID: 277136 Cd Length: 105 Bit Score: 52.69 E-value: 1.07e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707401627 255 CGFCHAGEDENETR--GVLHSDNAKKVaaHYKCMLFSSGTVQltTSSRAeFGNFEiktviQEIKRGKRMKCTLCGQLGAT 332
Cdd:cd15666     1 CVLCGGEGDGDTDGpgRLLNLDVDKWV--HLNCALWSYEVYE--TQNGA-LMNVE-----EALRRALTTTCSHCGRTGAT 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1707401627 333 IGCEIKACVKTYHYHCGLEDKAKYIENmaRGIyklYCKNH 372
Cdd:cd15666    71 VPCFKPRCANVYHLPCAIKDGCMFFKD--KTM---LCPSH 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.

Pssm-ID: 277164 Cd Length: 105 Bit Score: 50.42 E-value: 5.95e-08

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1707401627 103 ENIGgfSIEDVKKEIKRGNKLMCTSCHRPGATIGCDVKTCRRTYHYYCALWDKAQTKENPSqgiylVYCRKH 174
Cdd:cd15694    41 ENDG--SLKNVHAAVARGRQMRCEHCQKIGATVGCCLSACLSNFHFMCARASRCCFQDDKK-----VFCQKH 105

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.

Pssm-ID: 277138 Cd Length: 103 Bit Score: 49.23 E-value: 1.73e-07

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1707401627 117 IKRGNKLMCTSCHRPGATIGCDVKTCRRTYHYYCALWDKAQTKENPsqgiYLVYCRKH 174
Cdd:cd15668    50 VWVAKQSVCSSCQQTGATIGCLHKGCKAKYHYPCAVESGCQLDEEN----FSLLCPKH 103

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.

Pssm-ID: 277164 Cd Length: 105 Bit Score: 47.73 E-value: 5.75e-07

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1707401627 308 IKTVIQEIKRGKRMKCTLCGQLGATIGCEIKACVKTYHYHCGLEDKAKYIENMargiyKLYCKNH 372
Cdd:cd15694    46 LKNVHAAVARGRQMRCEHCQKIGATVGCCLSACLSNFHFMCARASRCCFQDDK-----KVFCQKH 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.

Pssm-ID: 277135 Cd Length: 90 Bit Score: 46.93 E-value: 6.88e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707401627 255 CGFCHAGEdenetrgvlhsdnakkVAAHYKCMLFSSGTVQLTTssrAEFGNFEiKTVIQEIKRgkrmKCTLCGQLGATIG 334
Cdd:cd15665     1 CALCNLGE----------------VYAHHCCAAWSEGVCQTED---GALENVD-KAVAKALSQ----KCSFCLRYGASIS 56

                          90
                  ....*....|....
gi 1707401627 335 CEIKACVKTYHYHC 348
Cdd:cd15665    57 CRMPSCSKSFHFPC 70

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.

Pssm-ID: 277170 Cd Length: 104 Bit Score: 47.18 E-value: 8.59e-07

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1707401627 113 VKKEIKRGNKLMCTSCHRPGATIGCDVKTCRRTYHYYCA 151
Cdd:cd15700    47 LQEAVQKAADAKCSSCQGAGATVGCCHKGCTQSYHYICA 85

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.

Pssm-ID: 277170 Cd Length: 104 Bit Score: 43.33 E-value: 1.62e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1707401627 312 IQE-IKRGKRMKCTLCGQLGATIGCEIKACVKTYHYHCGLEDKAKYIENMargiYKLYCKNH 372
Cdd:cd15700    47 LQEaVQKAADAKCSSCQGAGATVGCCHKGCTQSYHYICAVEAGCLFEEEN----FSLRCPKH 104

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.

Pssm-ID: 277167 Cd Length: 105 Bit Score: 41.96 E-value: 5.70e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707401627 255 CGFCHAgEDENETRGVLHSDNAK-KVAAHYKCMLFSSgtvQLTTSSRAEFGNFEIKtviqeIKRGKRMKCTLCGQLGATI 333
Cdd:cd15697     1 CCFCHE-EGDGLTDGPARLLNLDlDLWVHLNCALWST---EVYETQAGALINVELA-----LRRGLQMKCVFCHKTGATS 71

                          90       100
                  ....*....|....*....|....*.
gi 1707401627 334 GCEIKACVKTYHYHCGLEDKAKYIEN 359
Cdd:cd15697    72 GCHRLRCTNVYHFTCAIKAQCMFFKD 97

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.

Pssm-ID: 277177 [Multi-domain] Cd Length: 113 Bit Score: 41.81 E-value: 7.08e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1707401627 123 LMCTSC-HRPGATIGCDVKTCRRTYHYYCA----LWDKAQTKENPSQGIYL-VYCRKH 174
Cdd:cd15707    56 LICVLCrERTGACIQCSVKTCKTAYHVTCGfqhgLEMKTILDEESEDGVKLrSYCQKH 113

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.

Pssm-ID: 277169 Cd Length: 103 Bit Score: 40.67 E-value: 1.55e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707401627 282 HYKCMLFSSGTVqlttssraeFGNFEIKTVIQEIKRGKRMKCTLCGQLGATIGCEIKACVKTYHYHCGLE 351
Cdd:cd15699    26 HEGCILWANGIY---------LVCGRLYGLQEALDIAREMKCSHCQEAGATLGCYNKGCSFRYHYPCAID 86

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.

Pssm-ID: 277168 Cd Length: 107 Bit Score: 40.81 E-value: 1.77e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707401627 255 CGFCHAgEDENETRGVLHSDNAK-KVAAHYKCMLFSSgtvQLTTSSRAEFGNFEIKtviqeIKRGKRMKCTLCGQLGATI 333
Cdd:cd15698     1 CCFCHE-EGDGATDGPARLLNLDlDLWVHLNCALWST---EVYETQGGALMNVEVA-----LHRGLLTKCSLCQKTGATN 71

                          90       100
                  ....*....|....*....|....*.
gi 1707401627 334 GCEIKACVKTYHYHCGLEDKAKYIEN 359
Cdd:cd15698    72 SCNRLRCPNVYHFACAIRAKCMFFKD 97

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.

Pssm-ID: 277167 Cd Length: 105 Bit Score: 40.42 E-value: 2.04e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1707401627 112 DVKKEIKRGNKLMCTSCHRPGATIGCDVKTCRRTYHYYCALwdKAQ 157
Cdd:cd15697    48 NVELALRRGLQMKCVFCHKTGATSGCHRLRCTNVYHFTCAI--KAQ 91

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.

Pssm-ID: 277165 Cd Length: 90 Bit Score: 39.13 E-value: 4.41e-04

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1707401627 281 AHYKCMLFSSGTVQLTtssraefgNFEIKTVIQEIKRGKRMKCTLCGQLGATIGCEIKACVKTYHYHC 348
Cdd:cd15695    11 VHHWCAAWSAGVKQHE--------GDGLIGVDKAVFSGISQKCEHCKRLGATIQCHAEGCPRFYHFPC 70

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.

Pssm-ID: 277166 Cd Length: 90 Bit Score: 38.77 E-value: 5.36e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707401627 255 CGFCHAGEdenetrgvlhsdnakkVAAHYKCMLFSSGTVQLTTSSraefgnfeIKTVIQEIKRGKRMKCTLCGQLGATIG 334
Cdd:cd15696     1 CAFCYCGE----------------CWAHLRCAEWSLGVCQGEEQL--------LVNVDKAVVSGSTERCAFCKHLGATIK 56

                          90
                  ....*....|....
gi 1707401627 335 CEIKACVKTYHYHC 348
Cdd:cd15696    57 CCEEKCTQMYHYPC 70

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.

Pssm-ID: 277141 Cd Length: 112 Bit Score: 38.96 E-value: 6.50e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1707401627 123 LMCTSCH-RPGATIGCDVKTCRRTYHYYCALWDKAQTK---ENPSQGIYLV-YCRKH 174
Cdd:cd15671    56 LVCVLCKeKTGACIQCSVKSCKTAFHVTCAFQHGLEMKtilEDEDDEVKFKsYCPKH 112

Extended PHD finger found in Arabidopsis thaliana ATX1, -2, and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of A. thaliana histone-lysine N-methyltransferase arabidopsis trithorax-like proteins ATX1, -2, and similar proteins. ATX1 and -2 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 known as 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 known as protein SET domain group 30, or trithorax-homolog protein 2/TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). ATX1 and ATX2 are multi-domain proteins that consist of an N-terminal PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical PHD finger, this non-canonical ePHD finger, and a C-terminal SET domain.

Pssm-ID: 277132 Cd Length: 115 Bit Score: 38.22 E-value: 1.61e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1707401627 110 IEDVKKEIKRGNKLMCTSCHRP-GATIGCDVKTCRRTYHYYCA--------LWDkAQTKENPSQGIYLV-YCRKH 174
Cdd:cd15662    42 VDGINAISKERWELSCTICKQRyGACIQCSNNSCRVAYHPLCAraaglcmeVAD-EGGEDPGDQGLRLLsYCPRH 115

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.

Pssm-ID: 277169 Cd Length: 103 Bit Score: 37.20 E-value: 2.58e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1707401627 125 CTSCHRPGATIGCDVKTCRRTYHYYCAL-WDKAQTKENPSqgiylVYCRKH 174
Cdd:cd15699    58 CSHCQEAGATLGCYNKGCSFRYHYPCAIdADCLLNEENFS-----VRCPKH 103

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.

Pssm-ID: 277168 Cd Length: 107 Bit Score: 36.95 E-value: 3.40e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1707401627 107 GFSIEDVKKEIKRGNKLMCTSCHRPGATIGCDVKTCRRTYHYYCAL 152
Cdd:cd15698    43 GGALMNVEVALHRGLLTKCSLCQKTGATNSCNRLRCPNVYHFACAI 88

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.

Pssm-ID: 277135 Cd Length: 90 Bit Score: 36.53 E-value: 3.59e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1707401627 111 EDVKKEIKRGNKLMCTSCHRPGATIGCDVKTCRRTYHYYCA 151
Cdd:cd15665    31 ENVDKAVAKALSQKCSFCLRYGASISCRMPSCSKSFHFPCA 71

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.

Pssm-ID: 277166 Cd Length: 90 Bit Score: 36.46 E-value: 3.75e-03

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1707401627 113 VKKEIKRGNKLMCTSCHRPGATIGCDVKTCRRTYHYYCA 151
Cdd:cd15696    33 VDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCA 71

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.

Pssm-ID: 277165 Cd Length: 90 Bit Score: 36.43 E-value: 4.10e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1707401627 107 GFSIEDVKKEIKRGNKLMCTSCHRPGATIGCDVKTCRRTYHYYCA 151
Cdd:cd15695    27 GDGLIGVDKAVFSGISQKCEHCKRLGATIQCHAEGCPRFYHFPCA 71