Extended PHD finger found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Snt2p. Sntp2 is a yeast protein that may function in multiple stress pathways. It coordinates the transcriptional response to hydrogen peroxide-mediated oxidative stress through interaction with Ecm5 and the Rpd3 deacetylase. Snt2p contains a bromo adjacent homology (BAH) domain, two canonical PHD fingers, a non-canonical ePHD finger, and a SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321307  1108 CSMCPTKDYDYDRYRSQSFKICPDALKCTSLGTWVHLVCSLFNEDIKYGNGQSMQPALNTTAVLIKHSRFTCGVCRINGG 1187
Cdd:cd15667    1 CSLCNAKESNYELAKKQSPRTRPDALKCTSNGTWCHVLCALFNEDIKFGNSKSLQPILNTESVLLKGSRQKCEICKVSGG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321307  1188 GLVKCNKCQYRYHITCAQNSSNFKLMFEKKNMSVDTTLPCIKDVKLNDTYTLRPILICDRH 1248
Cdd:cd15667   81 GLVKCEVCDDRFHVSCAQDTPGFKLGFKKEYLSDDTENPFITDKVDNESYTLKPIIVCPKH 141

PHD finger 2 found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and similar proteins; This group corresponds to Snt2p and similar proteins. Snt2p is a yeast protein that may function in multiple stress pathways. It coordinates the transcriptional response to hydrogen peroxide-mediated oxidative stress through interaction with Ecm5 and the Rpd3 deacetylase. Snt2p contains a bromo adjacent homology (BAH) domain, two canonical Cys4HisCys3 plant homeodomain (PHD) fingers, a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, and a SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domain; this model corresponds to the second canonical Cys4HisCys3 PHD finger.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6321307  1040 FCSVCKEKFNDNDNYEVVCGNCGLTVHYFCYAIKLPKDMKKNTNLKTFKWLCDPC 1094
Cdd:cd15498    1 KCSVCSEQFASNFNTSLSCYNCGLNVHASCYGITVPGKMNKVKNLKSYKWLCDPC 55

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 6321307     559 SFTAVEIRKFEEAVEKFGSELRPVCEYVGTQPMSMIVRFYYNWK 602
Cdd:pfam00249    3 PWTPEEDELLLEAVEKLGNRWKKIAKLLPGRTDNQCKNRWQNYL 46

Extended PHD finger found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Snt2p. Sntp2 is a yeast protein that may function in multiple stress pathways. It coordinates the transcriptional response to hydrogen peroxide-mediated oxidative stress through interaction with Ecm5 and the Rpd3 deacetylase. Snt2p contains a bromo adjacent homology (BAH) domain, two canonical PHD fingers, a non-canonical ePHD finger, and a SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321307  1108 CSMCPTKDYDYDRYRSQSFKICPDALKCTSLGTWVHLVCSLFNEDIKYGNGQSMQPALNTTAVLIKHSRFTCGVCRINGG 1187
Cdd:cd15667    1 CSLCNAKESNYELAKKQSPRTRPDALKCTSNGTWCHVLCALFNEDIKFGNSKSLQPILNTESVLLKGSRQKCEICKVSGG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321307  1188 GLVKCNKCQYRYHITCAQNSSNFKLMFEKKNMSVDTTLPCIKDVKLNDTYTLRPILICDRH 1248
Cdd:cd15667   81 GLVKCEVCDDRFHVSCAQDTPGFKLGFKKEYLSDDTENPFITDKVDNESYTLKPIIVCPKH 141

BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321307     121 VLLSANDTIYMISEPAGEPYYVGRVvnfvskpefsntihEAIKTTSvfPAKFFQVRMNWFYRPRDIQE-HVNTFNPRLVY 199
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARI--------------EELFEDT--KNGKKMVRVQWFYRPEETVHrAGKAFNKDELF 64

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321307     200 ASLHQDICPISSYRGKCSIFHKDEVFDVLPNEkecIIRPNIFYFDELFDRYTlKYYKVYS 259
Cdd:pfam01426   65 LSDEEDDVPLSAIIGKCSVLHKSDLESLDPYK---IKEPDDFFCELLYDPKT-KSFKKLP 120

PHD finger 1 found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and similar proteins; Snt2p is a yeast protein that may function in multiple stress pathways. It coordinates the transcriptional response to hydrogen peroxide-mediated oxidative stress through interaction with Ecm5 and the Rpd3 deacetylase. Snt2p contains a bromo adjacent homology (BAH) domain, two canonical Cys4HisCys3 plant homeodomain (PHD) fingers, a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, and a SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domain; this model corresponds to the first canonical Cys4HisCys3 PHD finger.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 6321307   319 RCQFCKEWCIQKESLSCDECGVCAHLYCMDPPLDRKPNKDVVWTCFSC 366
Cdd:cd15497    1 SCKVCKEWCASDDSVRCDECKVSYHLLCVDPPLTKKPNRGFVWSCAPC 48

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321307  1012 LEKDMILKHTKnkPKNPDtawanNSARTFCSVCKEKFNDNDNYEVVCGNCGLTVHYFCYAIKLpkdmkkntnLKTFKWLC 1091
Cdd:COG5141  174 FEHGLPDKHVE--PIEPS-----DEFDDICTKCTSTHNENSNAIVFCDGCEICVHQSCYGIQF---------LPEGFWLC 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321307  1092 DPCSNDLNPIISttyqCSMCPTKDydydryrsqsfkicpDALKCTSLGTWVHLVCSLFNEDIKYGNGQSMQPALNTTAVL 1171
Cdd:COG5141  238 RKCIYGEYQIRC----CSFCPSSD---------------GAFKQTSDGRWGHVICAMFNPELSFGHLLSKDPIDNIASVS 298

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6321307  1172 IKHSRFTCGVCRINGGGLVKCNK--CQYRYHITCAQNSSNFKLMFEKKNMSVD 1222
Cdd:COG5141  299 SSRWKLGCLICKEFGGTCIQCSYfnCTRAYHVTCARRAGYFDLNIYSHNGISY 351

PHD-zinc-finger like domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321307    1128 ICP---DALKCTSLGTWVHLVCSLFNEDIKYGNGQSMQPAlNTTAVLIKHSRFTCGVCRINGGGLVKCNK--CQYRYHIT 1202
Cdd:pfam13832    5 LCPlrgGALKQTSDGRWVHVLCAIFVPEVRFGNVATMEPI-DVSRIPPERWKLKCVFCKKRSGACIQCSKgrCTTAFHVT 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 6321307    1203 CAQNSsnfKLMFEkknmsvdttlpcikdvkLNDTYTLRPILICDRH 1248
Cdd:pfam13832   84 CAQAA---GVYME-----------------PEDWPNVVVIAYCQKH 109

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains. Several PHD fingers have been identified as binding modules of methylated histone H3.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 6321307    1040 FCSVCKEkfNDNDNYEVVCGNCGLTVHYFCYAIKLPKDMKKNTnlktfKWLCDPCSND 1097
Cdd:pfam00628    1 YCAVCGK--SDDGGELVQCDGCDDWFHLACLGPPLDPAEIPSG-----EWLCPECKPK 51

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 6321307     559 SFTAVEIRKFEEAVEKFGSELRPVCEYVGTQPMSMIVRFYYNWK 602
Cdd:pfam00249    3 PWTPEEDELLLEAVEKLGNRWKKIAKLLPGRTDNQCKNRWQNYL 46

Myb-Like Dna-Binding Domain of MTA3 and related proteins; Members in this SANT/myb family include domains found in mouse metastasis-associated protein 3 (MTA3) proteins and arginine-glutamic dipeptide (RERE) repeats proteins. SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domains are a diverse set of proteins that share a common 3 alpha-helix bundle. MTA3 has been shown to interact with nucleosome remodeling and deacetylase (NuRD) proteins CHD4 and HDAC1, and the core cohesin complex protein RAD21 in the ovary, and regulate G2/M progression in proliferating granulosa cells. RERE belongs to the atrophin family and has been identified as a nuclear receptor corepressor; altered expression levels of RERE are associated with cancer in humans while mutations of Rere in mice cause failure in closing the anterior neural tube and fusion of the telencephalic and optic vesicles during embryogenesis.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 6321307   559 SFTAVEIRKFEEAVEKFGSELRPV-CEYVGTQPMSMIVRFYYNWKK 603
Cdd:cd11661    1 EWSESEAKLFEEGLRKYGKDFHDIrQDFLPWKSVGELVEFYYMWKK 46

Extended PHD finger found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Snt2p. Sntp2 is a yeast protein that may function in multiple stress pathways. It coordinates the transcriptional response to hydrogen peroxide-mediated oxidative stress through interaction with Ecm5 and the Rpd3 deacetylase. Snt2p contains a bromo adjacent homology (BAH) domain, two canonical PHD fingers, a non-canonical ePHD finger, and a SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321307  1108 CSMCPTKDYDYDRYRSQSFKICPDALKCTSLGTWVHLVCSLFNEDIKYGNGQSMQPALNTTAVLIKHSRFTCGVCRINGG 1187
Cdd:cd15667    1 CSLCNAKESNYELAKKQSPRTRPDALKCTSNGTWCHVLCALFNEDIKFGNSKSLQPILNTESVLLKGSRQKCEICKVSGG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321307  1188 GLVKCNKCQYRYHITCAQNSSNFKLMFEKKNMSVDTTLPCIKDVKLNDTYTLRPILICDRH 1248
Cdd:cd15667   81 GLVKCEVCDDRFHVSCAQDTPGFKLGFKKEYLSDDTENPFITDKVDNESYTLKPIIVCPKH 141

BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321307     121 VLLSANDTIYMISEPAGEPYYVGRVvnfvskpefsntihEAIKTTSvfPAKFFQVRMNWFYRPRDIQE-HVNTFNPRLVY 199
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARI--------------EELFEDT--KNGKKMVRVQWFYRPEETVHrAGKAFNKDELF 64

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321307     200 ASLHQDICPISSYRGKCSIFHKDEVFDVLPNEkecIIRPNIFYFDELFDRYTlKYYKVYS 259
Cdd:pfam01426   65 LSDEEDDVPLSAIIGKCSVLHKSDLESLDPYK---IKEPDDFFCELLYDPKT-KSFKKLP 120

PHD finger 1 found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and similar proteins; Snt2p is a yeast protein that may function in multiple stress pathways. It coordinates the transcriptional response to hydrogen peroxide-mediated oxidative stress through interaction with Ecm5 and the Rpd3 deacetylase. Snt2p contains a bromo adjacent homology (BAH) domain, two canonical Cys4HisCys3 plant homeodomain (PHD) fingers, a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, and a SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domain; this model corresponds to the first canonical Cys4HisCys3 PHD finger.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 6321307   319 RCQFCKEWCIQKESLSCDECGVCAHLYCMDPPLDRKPNKDVVWTCFSC 366
Cdd:cd15497    1 SCKVCKEWCASDDSVRCDECKVSYHLLCVDPPLTKKPNRGFVWSCAPC 48

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321307  1012 LEKDMILKHTKnkPKNPDtawanNSARTFCSVCKEKFNDNDNYEVVCGNCGLTVHYFCYAIKLpkdmkkntnLKTFKWLC 1091
Cdd:COG5141  174 FEHGLPDKHVE--PIEPS-----DEFDDICTKCTSTHNENSNAIVFCDGCEICVHQSCYGIQF---------LPEGFWLC 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321307  1092 DPCSNDLNPIISttyqCSMCPTKDydydryrsqsfkicpDALKCTSLGTWVHLVCSLFNEDIKYGNGQSMQPALNTTAVL 1171
Cdd:COG5141  238 RKCIYGEYQIRC----CSFCPSSD---------------GAFKQTSDGRWGHVICAMFNPELSFGHLLSKDPIDNIASVS 298

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6321307  1172 IKHSRFTCGVCRINGGGLVKCNK--CQYRYHITCAQNSSNFKLMFEKKNMSVD 1222
Cdd:COG5141  299 SSRWKLGCLICKEFGGTCIQCSYfnCTRAYHVTCARRAGYFDLNIYSHNGISY 351

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains. Several PHD fingers have been identified as binding modules of methylated histone H3.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 6321307     319 RCQFCKEWCIQKESLSCDECGVCAHLYCMDPPLDRKPNKDVVWTCFSCLQK 369
Cdd:pfam00628    1 YCAVCGKSDDGGELVQCDGCDDWFHLACLGPPLDPAEIPSGEWLCPECKPK 51

PHD-zinc-finger like domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321307    1128 ICP---DALKCTSLGTWVHLVCSLFNEDIKYGNGQSMQPAlNTTAVLIKHSRFTCGVCRINGGGLVKCNK--CQYRYHIT 1202
Cdd:pfam13832    5 LCPlrgGALKQTSDGRWVHVLCAIFVPEVRFGNVATMEPI-DVSRIPPERWKLKCVFCKKRSGACIQCSKgrCTTAFHVT 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 6321307    1203 CAQNSsnfKLMFEkknmsvdttlpcikdvkLNDTYTLRPILICDRH 1248
Cdd:pfam13832   84 CAQAA---GVYME-----------------PEDWPNVVVIAYCQKH 109

Extended PHD finger found in protein AF-10 and AF-17; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of AF-10 and AF-17. AF-10, also termed ALL1 (acute lymphoblastic leukaemia)-fused gene from chromosome 10 protein, is a transcription factor encoded by gene AF10, a translocation partner of the MLL (mixed-lineage leukaemia) oncogene in leukaemia. AF-10 has been implicated in the development of leukemia following chromosomal rearrangements between the AF10 gene and one of at least two other genes, MLL and CALM. It plays a key role in the survival of uncommitted hematopoietic cells. Moreover, AF-10 functions as a follistatin-related gene (FLRG)-interacting protein. The interaction with FLRG enhances AF10-dependent transcription. It interacts with the human counterpart of yeast Dot1, hDOT1L, and may act as a bridge for the recruitment of hDOT1L to the genes targeted by MLL-AF10. It also interacts with the synovial sarcoma associated protein SYT protein and may play a role in synovial sarcomas and acute leukemias. AF-17, also termed ALL1-fused gene from chromosome 17 protein, is encoded by gene AF17 that has been identified in hematological malignancies as translocation partners of the mixed lineage leukemia gene MLL. It is a putative transcription factor that may play a role in multiple signaling pathways. It is involved in chromatin-mediated gene regulation mechanisms. It functions as a component of the multi-subunit Dot1 complex (Dotcom) and plays a role in the Wnt/Wingless signaling pathway. It also seems to be a downstream target of the beta-catenin/T-cell factor pathway, and participates in G2-M progression. Moreover, it may function as an important regulator of ENaC-mediated Na+ transport and thus blood pressure. Both AF-10 and AF-17 contain an N-terminal plant homeodomain (PHD) finger followed by this non-canonical ePHD finger. The PHD finger is involved in their homo-oligomerization. In the C-terminal region, they possess a leucine zipper domain and a glutamine-rich region. This family also includes ZFP-1, the Caenorhabditis elegans AF10 homolog. It was originally identified as a factor promoting RNAi interference in C. elegans. It also acts as Dot1-interacting protein that opposes H2B ubiquitination to reduce polymerase II (Pol II) transcription.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321307  1108 CSMCPTKDydydryrsqsfkicpDALKCTSLGTWVHLVCSLFNEDIKYGNGQSMQP-ALNttavLIKHSRF--TCGVCRI 1184
Cdd:cd15672    1 CELCPHKD---------------GALKRTDNGGWAHVVCALYIPEVRFGNVATMEPiILQ----DVPQDRFnkTCYICEE 61

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6321307  1185 NG-------GGLVKCNK--CQYRYHITCAQNSSnfkLMFEKKNMSVDTTLPC 1227
Cdd:cd15672   62 QGreskastGACMQCNKsgCKQSFHVTCAQMAG---LLCEEAGNYSDNVKYC 110

Extended PHD finger found in protein AF-10 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of AF-10. AF-10, also termed ALL1 (acute lymphoblastic leukaemia)-fused gene from chromosome 10 protein, is a transcription factor encoded by gene AF10, a translocation partner of the MLL (mixed-lineage leukaemia) oncogene in leukaemia. AF-10 has been implicated in the development of leukemia following chromosomal rearrangements between the AF10 gene and one of at least two other genes, MLL and CALM. It plays a key role in the survival of uncommitted hematopoietic cells. Moreover, AF-10 functions as a follistatin-related gene (FLRG)-interacting protein. The interaction with FLRG enhances AF10-dependent transcription. It interacts with human counterpart of the yeast Dot1, hDOT1L, and may act as a bridge for the recruitment of hDOT1L to the genes targeted by MLL-AF10. It also interacts with the synovial sarcoma associated protein SYT protein and may play a role in synovial sarcomas and acute leukemias. AF-10 contains an N-terminal plant homeodomain (PHD) finger followed by this non-canonical ePHD finger.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321307  1107 QCSMCPTKDydydryrsqsfkicpDALKCTSLGTWVHLVCSLFNEDIKYGNGQSMQPALNTTavlIKHSRF--TCGVCRI 1184
Cdd:cd15708    4 RCELCPHKD---------------GALKRTDNGGWAHVVCALYIPEVQFANVSTMEPIVLQS---VPHERYnkTCYICDE 65

                         90       100       110
                 ....*....|....*....|....*....|
gi 6321307  1185 NG-------GGLVKCNK--CQYRYHITCAQ 1205
Cdd:cd15708   66 QGreskaatGACMTCNKhgCRQAFHVTCAQ 95

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321307  1108 CSMCPTKDydydryrsqsfkicpDALKCTSLGTWVHLVCSLFNEDIKYGNGQSMQPALNTTAVLIKHSRFTCGVCRINGG 1187
Cdd:cd15670    1 CVLCPNKG---------------GAFKQTDDGRWAHVVCALWIPEVSFANTVFLEPIDGIQNIPKARWKLTCYICKKRMG 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321307  1188 GLVKCNK--CQYRYHITCAQNSSnfklMFEKKNMSVDTTLPCIKDVKlNDTYtlrpiliCDRH 1248
Cdd:cd15670   66 ACIQCHKknCYTAFHVTCAQQAG----LYMKIEPVKDPGNGTSDSVR-KEAY-------CDKH 116

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in epigenetics and chromatin-mediated transcriptional regulation. The PHD finger binds two zinc ions using the so-called 'cross-brace' motif and is thus structurally related to the RING finger and the FYVE finger. It is not yet known if PHD fingers have a common molecular function. Several reports suggest that it can function as a protein-protein interacton domain and it was recently demonstrated that the PHD finger of p300 can cooperate with the adjacent BROMO domain in nucleosome binding in vitro. Other reports suggesting that the PHD finger is a ubiquitin ligase have been refuted as these domains were RING fingers misidentified as PHD fingers.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 6321307      319 RCQFCKEWCIQKESLSCDECGVCAHLYCMDPPLDrKPNKDVVWTCFSC 366
Cdd:smart00249    1 YCSVCGKPDDGGELLQCDGCDRWYHQTCLGPPLL-EEEPDGKWYCPKC 47

Extended PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of BRPF2. BRPF2 also termed bromodomain-containing protein 1 (BRD1), or BR140-likeprotein, is encoded by BRL (BR140 Like gene). It is responsible for the bulk of the acetylation of H3K14 and forms a novel monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complex with HBO1 and ING4. The complex is required for full transcriptional activation of the erythroid-specific regulator genes essential for terminal differentiation and survival of erythroblasts in fetal liver. BRPF2 shows widespread expression and localizes to the nucleus within spermatocytes. It contains a cysteine rich region harboring a plant homeodomain (PHD) finger followed by a non-canonical ePHD finger, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321307  1128 ICPD---ALKCTSLGTWVHLVCSLFNEDIKYGNGQSMQPALNTTAVLIKHSRFTCGVCRING-GGLVKCNK--CQYRYHI 1201
Cdd:cd15702    3 LCPNkggAFKKTDDDRWGHVVCALWIPEVGFANTVFIEPIDGVRNIPPARWKLTCYLCKQKGvGACIQCHKanCYTAFHV 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 6321307  1202 TCAQNSSNFKLMFEKKNMSVDTTlpcikdvklndTYTLRPILICDRH 1248
Cdd:cd15702   83 TCAQKAGLYMKMEPVKEVTGGGT-----------TFSVRKTAYCDAH 118

Extended PHD finger found in protein Jade-2 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-2. Jade-2, also termed PHD finger protein 15 (PHF15), is a plant homeodomain (PHD) zinc finger protein that is closely related to Jade-1, which functions as an essential regulator of multiple cell signaling pathways. Like Jade-1, Jade-2 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, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. Jade-2 contains a canonical PHD finger followed by this non-canonical ePHD finger, both of which are zinc-binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321307  1128 ICPD---ALKCTSLGT-WVHLVCSLFNEDIKYGNGQSMQPALNTTAVLIKHSRFTCGVCRINGGGLVKCN--KCQYRYHI 1201
Cdd:cd15705    3 LCPKrggALKPTRSGTkWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKECTGTCIQCSmpSCITAFHV 82

                 ...
gi 6321307  1202 TCA 1204
Cdd:cd15705   83 TCA 85

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321307  1128 ICPD---ALKCTSLGT-WVHLVCSLFNEDIKYGNGQSMQPAlnTTAVLIKHSRFT--CGVCRINGGGLVKCN--KCQYRY 1199
Cdd:cd15707    3 LCPNkggAMKSTRSGTkWAHVSCALWIPEVSIGCVEKMEPI--TKISSIPASRWAliCVLCRERTGACIQCSvkTCKTAY 80

                         90
                 ....*....|....*..
gi 6321307  1200 HITCA-QNSSNFKLMFE 1215
Cdd:cd15707   81 HVTCGfQHGLEMKTILD 97

PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein 2 (UHRF2); UHRF2 (also termed Np95/ICBP90-like RING finger protein (NIRF), Np95-like RING finger protein, nuclear protein 97, nuclear zinc finger protein Np97, RING finger protein 107, or E3 ubiquitin-protein ligase UHRF2) was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131 (ZNF131) SUMOylation but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs,p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) by interacting with the HBV core protein and promoting its degradation. UHRF2 contains an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a SET- and RING-associated (SRA) domain, and a C-terminal RING finger.

                         10        20        30
                 ....*....|....*....|....*....|....
gi 6321307   333 LSCDECGVCAHLYCMDPPLDRKPnKDVVWTCFSC 366
Cdd:cd15617   15 LLCDECNMAYHIYCLNPPLDKIP-EDEDWYCPSC 47

PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein UHRF1 and UHRF2; UHRF1 is a unique chromatin effector protein that integrates the recognition of both histone PTMs and DNA methylation. It is essential for cell proliferation and plays a critical role in the development and progression of many human carcinomas, such as laryngeal squamous cell carcinoma (LSCC), gastric cancer (GC), esophageal squamous cell carcinoma (ESCC), colorectal cancer, prostate cancer, and breast cancer. UHRF1 acts as a transcriptional repressor through its binding to histone H3 when it is unmodified at Arg2. Its overexpression in human lung fibroblasts results in downregulation of expression of the tumour suppressor pRB. It also plays a role in transcriptional repression of the cell cycle regulator p21. Moreover, UHRF1-dependent repression of transcription factors can facilitate the G1-S transition. It interacts with Tat-interacting protein of 60 kDa (TIP60) and induces degradation-independent ubiquitination of TIP60. It is also an N-methylpurine DNA glycosylase (MPG)-interacting protein that binds MPG in a p53 status-independent manner in the DNA base excision repair (BER) pathway. In addition, UHRF1 functions as an epigenetic regulator that is important for multiple aspects of epigenetic regulation, including maintenance of DNA methylation patterns and recognition of various histone modifications. UHRF2 was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131 (ZNF131) SUMOylation but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs, p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) by interacting with the HBV core protein and promoting its degradation. Both UHRF1 and UHRF2 contain an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a SET- and RING-associated (SRA) domain, and a C-terminal RING finger.

                         10        20        30
                 ....*....|....*....|....*....|....
gi 6321307   333 LSCDECGVCAHLYCMDPPLDRKPNKDvVWTCFSC 366
Cdd:cd15525   15 LLCDECDMAYHLYCLDPPLTSLPDDD-EWYCPDC 47

PHD finger 1 found in Schizosaccharomyces pombe Lid2 complex component Lid2p and similar proteins; Lid2p is a trimethyl H3K4 (H3K4me3) demethylase responsible for H3K4 hypomethylation in heterochromatin. It interacts with the histone lysine-9 methyltransferase, Clr4, through the Dos1/Clr8-Rik1 complex, and mediates H3K9 methylation and small RNA production. It also acts cooperatively with the histone modification enzymes Set1 and Lsd1 and plays an essential role in cross-talk between H3K4 and H3K9 methylation in euchromatin. Lid2p contains a JmjC domain, three PHD fingers and a JmjN domain. This model corresponds to the first PHD finger.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 6321307   320 CQFCKEWCIQKESLSCDECGVCAHLYCMDPPLDRKPNKDvvWTCFSC 366
Cdd:cd15519    2 CEVCGLDDNEGEVLLCDGCDAEYHTSCLDPPLGEIPPGT--WFCPSC 46

PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein 1 (UHRF1); UHRF1 (also termed inverted CCAAT box-binding protein of 90 kDa, nuclear protein 95, nuclear zinc finger protein Np95 (Np95), RING finger protein 106, transcription factor ICBP90, or E3 ubiquitin-protein ligase UHRF1) is a unique chromatin effector protein that integrates the recognition of both histone PTMs and DNA methylation. It is essential for cell proliferation and plays a critical role in the development and progression of many human carcinomas, such as laryngeal squamous cell carcinoma (LSCC), gastric cancer (GC), esophageal squamous cell carcinoma (ESCC), colorectal cancer, prostate cancer, and breast cancer. UHRF1 acts as a transcriptional repressor through its binding to histone H3 when it is unmodified at Arg2. Its overexpression in human lung fibroblasts results in downregulation of expression of the tumour suppressor pRB. It also plays a role in transcriptional repression of the cell cycle regulator p21. Moreover, UHRF1-dependent repression of transcription factors can facilitate the G1-S transition. It interacts with Tat-interacting protein of 60 kDa (TIP60) and induces degradation-independent ubiquitination of TIP60. It is also an N-methylpurine DNA glycosylase (MPG)-interacting protein that binds MPG in a p53 status-independent manner in the DNA base excision repair (BER) pathway. In addition, UHRF1 functions as an epigenetic regulator that is important for multiple aspects of epigenetic regulation, including maintenance of DNA methylation patterns and recognition of various histone modifications. UHRF1 contains an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a SET and RING finger associated (SRA) domain, and a C-terminal RING-finger domain. It specifically binds to hemimethylated DNA, double-stranded CpG dinucleotides, and recruits the maintenance methyltransferase DNMT1 to its hemimethylated DNA substrate through its SRA domain. UHRF1-dependent H3K23 ubiquitylation has an essential role in maintaining DNA methylation and replication. The tandem Tudor domain directs UHRF1 binding to the heterochromatin mark histone H3K9me3 and the PHD finger targets UHRF1 to unmodified histone H3 in euchromatic regions. The RING-finger domain exhibit both autocatalytic E3 ubiquitin (Ub) ligase activity and activity against histone H3 and DNMT1.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 6321307   320 CQFCKEWCIQKESLSCDECGVCAHLYCMDPPLDRKPNKDvVWTCFSC 366
Cdd:cd15616    2 CHVCGGKQDPDKQLMCDECDMAFHIYCLNPPLSSIPDDE-DWYCPEC 47

PHD finger 1 found in PHD finger protein 12 (PHF12); PHF12, also termed PHD factor 1 (Pf1), is a plant homeodomain (PHD) zinc finger-containing protein that bridges the transducin-like enhancer of split (TLE) corepressor to the mSin3A-histone deacetylase (HDAC)-complex, and further represses transcription at targeted genes. PHF12 also interacts with MRG15 (mortality factor-related genes on chromosome 15), a member of the mortality factor (MORF) family of proteins implicated in regulating cellular senescence. PHF12 contains two plant-homeodomain (PHD) zinc fingers followed by a polybasic region. The PHD fingers function downstream of phosphoinositide signaling triggered by the interaction between polybasic regions and phosphoinositides. This model corresponds to the first PHD finger.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 6321307   320 CQFCKEwciQKESLSCDECGVCAHLYCMDPPLDRKPNKDVVWTCFSC 366
Cdd:cd15533    2 CDSCGE---GGDLLCCDRCPASFHLQCCNPPLDEEDLPPGEWLCHRC 45

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
                 ....*....|....*....|....*....|....*....|....*....
gi 6321307   319 RCQFCKEWCIQKES-LSCDECGVCAHLYCMDPPLdRKPNKDVVWTCFSC 366
Cdd:cd15489    1 SCIVCGKGGDLGGElLQCDGCGKWFHADCLGPPL-SSFVPNGKWICPVC 48

PHD finger 5 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 4 found in 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, several plant homeodomain (PHD) fingers, extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions. This model corresponds to the fifth PHD finger of KMT2C and the fourth PHD finger of KMT2D.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 6321307   320 CQFCKEWCIQKESLSCDECGVCAHLYCMDPPLDRKPNKDvvWTCFSC 366
Cdd:cd15513    2 CEGCGKASDESRLLLCDDCDISYHTYCLDPPLQTVPKGG--WKCKWC 46

Extended PHD finger found in Jumonji domain-containing protein 2C (JMJD2C); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of JMJD2C. JMJD2C, also termed lysine-specific demethylase 4C (KDM4C), or gene amplified in squamous cell carcinoma 1 protein (GASC-1 protein), or JmjC domain-containing histone demethylation protein 3C (JHDM3C), is an epigenetic factor that catalyzes the demethylation of di- and trimethylated H3K9 and H3K36, and may be involved in the development and/or progression of various types of cancer including esophageal squamous cell carcinoma (ESC) and breast cancer. It selectively interacts with hypoxia-inducible factor 1alpha (HIF1alpha) and plays a role in breast cancer progression. Moreover, JMJD2C may play an important role in the treatment of obesity and its complications by modulating the regulation of adipogenesis by nuclear receptor peroxisome proliferator-activated receptor gamma (PPARgamma). JMJD2C contains jmjN and jmjC domains in the N-terminal region, followed by a canonical plant homeodomain (PHD) finger, this non-canonical ePHD finger, and a Tudor domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321307  1132 ALKCTSLGTWVHLVCSLFNEDIKYGNGQSMQPaLNTTAVLIKHSRFTCGVCRIN----GGGLVKCN--KCQYRYHITCAQ 1205
Cdd:cd15715   10 ALKQTSDDKWAHVMCAVALPEVRFINVVERTP-IDISRIPLQRLKLKCIFCRNRikrvSGACIQCSygRCPASFHVTCAH 88

PHD finger 3 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel nuclear transcription factor that controls the proliferation of mesenchymal cells by directly repressing platelet-derived growth factor receptor-alpha (PDGFRalpha) expression. It also acts as an epigenetic regulator and plays an important role in the development of multiple organs in mammals. PHF14 contains three canonical plant homeodomain (PHD) fingers and a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His. It can interact with histones through its PHD fingers. The model corresponds to the third PHD finger.

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                 ....*....|....*....|....*....|....*....|....*...
gi 6321307   320 CQFCKEWCIQKESLSCDECGVCAHLYCMDPPLDRKPN-KDVVWTCFSC 366
Cdd:cd15563    2 CCVCKQTGDNSQLVRCDECKLCYHFGCLDPPLKKSPKqRGYGWVCEEC 49

PHD finger found in bromodomain adjacent to zinc finger domain protein 1A (BAZ1A); BAZ1A, also termed ATP-dependent chromatin-remodeling protein, or ATP-utilizing chromatin assembly and remodeling factor 1 (ACF1), or CHRAC subunit ACF1, or Williams syndrome transcription factor-related chromatin-remodeling factor 180 (WCRF180), or WALp1, is a subunit of the conserved imitation switch (ISWI)-family ATP-dependent chromatin assembly and remodeling factor (ACF)/chromatin accessibility complex (CHRAC) chromatin remodeling complex, which is required for DNA replication through heterochromatin. It alters the remodeling properties of the ATPase motor protein sucrose nonfermenting-2 homolog (SNF2H). Moreover, BAZ1A and its complexes play important roles in DNA double-strand break (DSB) repair. It is essential for averting improper gene expression during spermatogenesis. It also regulates transcriptional repression of vitamin D3 receptor-regulated genes. BAZ1A contains a WAC motif, a DDT domain, BAZ 1 and BAZ 2 motifs, a WAKZ (WSTF/Acf1/KIAA0314/ZK783.4) motif, a plant homeodomain (PHD) finger, and a bromodomain.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 6321307   319 RCQFCKEWCIQKESLSCDECGVCAHLYCMDPPLDRKPNKDvvWTCFSC 366
Cdd:cd15627    1 RCRICRRKGDAEKMLLCDGCDRGHHMYCLRPPLKKVPEGD--WFCPDC 46

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
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6321307  1040 FCSVCKEKFNDNDNyEVVCGNCGLTVHYFCYAIKLPKDMKKNtnlktfKWLCDPC 1094
Cdd:cd15489    1 SCIVCGKGGDLGGE-LLQCDGCGKWFHADCLGPPLSSFVPNG------KWICPVC 48