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Conserved domains on  [gi|2217355360|ref|XP_047272995|]
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E3 ubiquitin-protein ligase Jade-2 isoform X13 [Homo sapiens]

Protein Classification

protein Jade-1; PHD finger domain-containing protein( domain architecture ID 13419466)

protein Jade-1 is a scaffold subunit of some HBO1 complexes, which have a histone H4 acetyltransferase activity; contains an extended plant homeodomain (ePHD) zinc finger; PHD (plant homeodomain) finger domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ePHD_JADE2 cd15705
Extended PHD finger found in protein Jade-2 and similar proteins; The extended plant ...
254-364 2.39e-80

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.


:

Pssm-ID: 277175  Cd Length: 111  Bit Score: 252.71  E-value: 2.39e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 254 CLLCPKRGGALKPTRSGTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKECTGTCIQCSMPSCVTAF 333
Cdd:cd15705     1 CLLCPKRGGALKPTRSGTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKECTGTCIQCSMPSCITAF 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2217355360 334 HVTCAFDHGLEMRTILADNDEVKFKSFCQEH 364
Cdd:cd15705    81 HVTCAFDHGLEMRTTLADNDEVKFKSFCLEH 111
COG5141 super family cl34917
PHD zinc finger-containing protein [General function prediction only];
137-530 1.82e-63

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


The actual alignment was detected with superfamily member COG5141:

Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 225.25  E-value: 1.82e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 137 YDLDEIDAYWLELIN-SELKEMERPELDELTLERVLEELETLCHQNMARAIETqegLGIEYDEDVVCDVCRSPEGEDGNE 215
Cdd:COG5141   133 YDLDEYDTMWLRYLNeSAIDENVSEEAFEIIVTRLEKEWFFFEHGLPDKHVEP---IEPSDEFDDICTKCTSTHNENSNA 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 216 MVFCDKCNVCVHQACYGILKVPTGSWLCRTCALGVQP--KCLLCPKRGGALKPTRSGtKWVHVSCALWIPEVSIGCPEKM 293
Cdd:COG5141   210 IVFCDGCEICVHQSCYGIQFLPEGFWLCRKCIYGEYQirCCSFCPSSDGAFKQTSDG-RWGHVICAMFNPELSFGHLLSK 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 294 EPITKISHIPASRWALSCSLCKECTGTCIQCSMPSCVTAFHVTCAFDHGLEMRTILADN---DEVKFKSFCQEHSDGG-- 368
Cdd:COG5141   289 DPIDNIASVSSSRWKLGCLICKEFGGTCIQCSYFNCTRAYHVTCARRAGYFDLNIYSHNgisYCIDHEPLCRKHYPLGyg 368
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 369 --------------PRNEPTSEP--TEPSQAGEDLEKVTLRKQ---------RLQQLEEDFYELVEPAevaerldlaeAL 423
Cdd:COG5141   369 rmnglryfgyeklrYKNPPTAIPrkVRAARPRATLFMKLCWKQppatpsvlsRVEACDLKEKDRQDLP----------VN 438
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 424 VDFIYQYWKLKRKANANQPlLTPKTDEVDNLAQQEQDVLYRRLKLFTHLRQDLERVRNLCYMVTRRERTKHAICKLQEQI 503
Cdd:COG5141   439 IFDICKYWEMKRKSEIGGP-LVILPDIVYSLKTLEDWMSKRRMREVAKALQDQYQLLTLVESTAKRQLLKCQLSNLRKKF 517
                         410       420
                  ....*....|....*....|....*..
gi 2217355360 504 FHLqMKLIEQDLCRGLSTSFPIDGTFF 530
Cdd:COG5141   518 LNL-NYFPAQRLLQVKIIDLDVDGLFN 543
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
581-785 3.50e-06

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 50.75  E-value: 3.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 581 RDPSLRPGDPARKARGRTRLPAKKKPPPPPPQDGPGSRTTPDKAPKKTWGQDAGsgkGGQGPPTRKPPRRTSSHLPSSPA 660
Cdd:PRK07764  634 AAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAP---AAPAAPAGAAPAQPAPAPAATPP 710
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 661 AgdcpilATPESPPPLAPETPDEAASVAADSDVQVPGPAASPKPLGRLRPPRESKVTRRLPGARPDAGMGPPSAVAERPk 740
Cdd:PRK07764  711 A------GQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEE- 783
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2217355360 741 vslhfdtetdgyfsdgEMSDSDVEAEDGGVQRGPREAGAEEVVRM 785
Cdd:PRK07764  784 ----------------EMAEDDAPSMDDEDRRDAEEVAMELLEEE 812
EPL1 super family cl38323
Enhancer of polycomb-like; This is a family of EPL1 (Enhancer of polycomb-like) proteins. The ...
10-175 9.76e-03

Enhancer of polycomb-like; This is a family of EPL1 (Enhancer of polycomb-like) proteins. The EPL1 protein is a member of a histone acetyltransferase complex which is involved in transcriptional activation of selected genes.


The actual alignment was detected with superfamily member pfam10513:

Pssm-ID: 463128  Cd Length: 168  Bit Score: 37.85  E-value: 9.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360  10 ISSDNSDTTDSHATSTSASRCSKLPSSTKSGWPRQNEKKPSEVFRTDLITAMKIPDSYQLSPDDyyiladpwrqEWEKGV 89
Cdd:pfam10513  14 ISEDEVDGLDTSPDEDEPSECNSNKENSLHAVETGVDKEEEDEVHLKVINAAKKALSSSKKSQN----------TSESSV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360  90 QVPAGAEA-IPEPVVRILPPLEGPPA---QASpsstmlgEGSQPDWPGGSRYDLDEIDAYWLELINSELKEMERPELDEL 165
Cdd:pfam10513  84 PAPNKERLyLPTPDAGKFREFERPPAsyiRFS-------ETVEEELDEGVEYDMDEEDEAWLEELNEKRKSEGVEKISED 156
                         170
                  ....*....|
gi 2217355360 166 TLERVLEELE 175
Cdd:pfam10513 157 EFEILMDRFE 166
 
Name Accession Description Interval E-value
ePHD_JADE2 cd15705
Extended PHD finger found in protein Jade-2 and similar proteins; The extended plant ...
254-364 2.39e-80

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.


Pssm-ID: 277175  Cd Length: 111  Bit Score: 252.71  E-value: 2.39e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 254 CLLCPKRGGALKPTRSGTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKECTGTCIQCSMPSCVTAF 333
Cdd:cd15705     1 CLLCPKRGGALKPTRSGTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKECTGTCIQCSMPSCITAF 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2217355360 334 HVTCAFDHGLEMRTILADNDEVKFKSFCQEH 364
Cdd:cd15705    81 HVTCAFDHGLEMRTTLADNDEVKFKSFCLEH 111
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
137-530 1.82e-63

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


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 225.25  E-value: 1.82e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 137 YDLDEIDAYWLELIN-SELKEMERPELDELTLERVLEELETLCHQNMARAIETqegLGIEYDEDVVCDVCRSPEGEDGNE 215
Cdd:COG5141   133 YDLDEYDTMWLRYLNeSAIDENVSEEAFEIIVTRLEKEWFFFEHGLPDKHVEP---IEPSDEFDDICTKCTSTHNENSNA 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 216 MVFCDKCNVCVHQACYGILKVPTGSWLCRTCALGVQP--KCLLCPKRGGALKPTRSGtKWVHVSCALWIPEVSIGCPEKM 293
Cdd:COG5141   210 IVFCDGCEICVHQSCYGIQFLPEGFWLCRKCIYGEYQirCCSFCPSSDGAFKQTSDG-RWGHVICAMFNPELSFGHLLSK 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 294 EPITKISHIPASRWALSCSLCKECTGTCIQCSMPSCVTAFHVTCAFDHGLEMRTILADN---DEVKFKSFCQEHSDGG-- 368
Cdd:COG5141   289 DPIDNIASVSSSRWKLGCLICKEFGGTCIQCSYFNCTRAYHVTCARRAGYFDLNIYSHNgisYCIDHEPLCRKHYPLGyg 368
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 369 --------------PRNEPTSEP--TEPSQAGEDLEKVTLRKQ---------RLQQLEEDFYELVEPAevaerldlaeAL 423
Cdd:COG5141   369 rmnglryfgyeklrYKNPPTAIPrkVRAARPRATLFMKLCWKQppatpsvlsRVEACDLKEKDRQDLP----------VN 438
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 424 VDFIYQYWKLKRKANANQPlLTPKTDEVDNLAQQEQDVLYRRLKLFTHLRQDLERVRNLCYMVTRRERTKHAICKLQEQI 503
Cdd:COG5141   439 IFDICKYWEMKRKSEIGGP-LVILPDIVYSLKTLEDWMSKRRMREVAKALQDQYQLLTLVESTAKRQLLKCQLSNLRKKF 517
                         410       420
                  ....*....|....*....|....*..
gi 2217355360 504 FHLqMKLIEQDLCRGLSTSFPIDGTFF 530
Cdd:COG5141   518 LNL-NYFPAQRLLQVKIIDLDVDGLFN 543
zf-HC5HC2H_2 pfam13832
PHD-zinc-finger like domain;
252-364 1.57e-43

PHD-zinc-finger like domain;


Pssm-ID: 463991 [Multi-domain]  Cd Length: 109  Bit Score: 152.88  E-value: 1.57e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 252 PKCLLCPKRGGALKPTrSGTKWVHVSCALWIPEVSIGCPEKMEPITkISHIPASRWALSCSLCKECTGTCIQCSMPSCVT 331
Cdd:pfam13832   1 VRCCLCPLRGGALKQT-SDGRWVHVLCAIFVPEVRFGNVATMEPID-VSRIPPERWKLKCVFCKKRSGACIQCSKGRCTT 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2217355360 332 AFHVTCAFDHGLEMRtiLADNDEVKFKSFCQEH 364
Cdd:pfam13832  79 AFHVTCAQAAGVYME--PEDWPNVVVIAYCQKH 109
PHD_JADE2 cd15680
PHD finger found in protein Jade-2 and similar proteins; Jade-2, also termed PHD finger ...
201-246 2.36e-29

PHD finger found in protein Jade-2 and similar proteins; 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 Cys4HisCys3 PHD finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, both of which are zinc-binding motifs. This model corresponds to the canonical Cys4HisCys3 PHD finger.


Pssm-ID: 277150 [Multi-domain]  Cd Length: 46  Bit Score: 110.48  E-value: 2.36e-29
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2217355360 201 VCDVCRSPEGEDGNEMVFCDKCNVCVHQACYGILKVPTGSWLCRTC 246
Cdd:cd15680     1 VCDVCRSPEGEDGNEMVFCDKCNVCVHQACYGILKVPTGSWLCRTC 46
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
201-246 5.95e-12

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.


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 60.97  E-value: 5.95e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217355360 201 VCDVCRSPEgeDGNEMVFCDKCNVCVHQACYGI----LKVPTGSWLCRTC 246
Cdd:pfam00628   1 YCAVCGKSD--DGGELVQCDGCDDWFHLACLGPpldpAEIPSGEWLCPEC 48
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
201-246 3.43e-10

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.


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 56.07  E-value: 3.43e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2217355360  201 VCDVCRSPEgeDGNEMVFCDKCNVCVHQACYGI---LKVPTGSWLCRTC 246
Cdd:smart00249   1 YCSVCGKPD--DGGELLQCDGCDRWYHQTCLGPpllEEEPDGKWYCPKC 47
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
581-785 3.50e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 50.75  E-value: 3.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 581 RDPSLRPGDPARKARGRTRLPAKKKPPPPPPQDGPGSRTTPDKAPKKTWGQDAGsgkGGQGPPTRKPPRRTSSHLPSSPA 660
Cdd:PRK07764  634 AAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAP---AAPAAPAGAAPAQPAPAPAATPP 710
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 661 AgdcpilATPESPPPLAPETPDEAASVAADSDVQVPGPAASPKPLGRLRPPRESKVTRRLPGARPDAGMGPPSAVAERPk 740
Cdd:PRK07764  711 A------GQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEE- 783
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2217355360 741 vslhfdtetdgyfsdgEMSDSDVEAEDGGVQRGPREAGAEEVVRM 785
Cdd:PRK07764  784 ----------------EMAEDDAPSMDDEDRRDAEEVAMELLEEE 812
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
612-720 9.09e-04

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 42.68  E-value: 9.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 612 QDGPGSRTTPDKAPKKTwgqdAGSGKGGQGPPTRKPPRRTSSHLPSSPAAGDCPiLATPESPPPLAPETPD-EAASVAAD 690
Cdd:NF041121   14 QMGRAAAPPSPEGPAPT----AASQPATPPPPAAPPSPPGDPPEPPAPEPAPLP-APYPGSLAPPPPPPPGpAGAAPGAA 88
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2217355360 691 SDVQVPGPAASPKP--LGR-LRP---PRESKVTRRL 720
Cdd:NF041121   89 LPVRVPAPPALPNPleLARaLRPlkrRVPSPRRVEL 124
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
311-364 7.31e-03

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.


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 35.27  E-value: 7.31e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217355360  311 CSLCKEC--TGTCIQCSMpsCVTAFHVTCAFDHGLEmrtiladnDEVKFKSFCQEH 364
Cdd:smart00249   2 CSVCGKPddGGELLQCDG--CDRWYHQTCLGPPLLE--------EEPDGKWYCPKC 47
EPL1 pfam10513
Enhancer of polycomb-like; This is a family of EPL1 (Enhancer of polycomb-like) proteins. The ...
10-175 9.76e-03

Enhancer of polycomb-like; This is a family of EPL1 (Enhancer of polycomb-like) proteins. The EPL1 protein is a member of a histone acetyltransferase complex which is involved in transcriptional activation of selected genes.


Pssm-ID: 463128  Cd Length: 168  Bit Score: 37.85  E-value: 9.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360  10 ISSDNSDTTDSHATSTSASRCSKLPSSTKSGWPRQNEKKPSEVFRTDLITAMKIPDSYQLSPDDyyiladpwrqEWEKGV 89
Cdd:pfam10513  14 ISEDEVDGLDTSPDEDEPSECNSNKENSLHAVETGVDKEEEDEVHLKVINAAKKALSSSKKSQN----------TSESSV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360  90 QVPAGAEA-IPEPVVRILPPLEGPPA---QASpsstmlgEGSQPDWPGGSRYDLDEIDAYWLELINSELKEMERPELDEL 165
Cdd:pfam10513  84 PAPNKERLyLPTPDAGKFREFERPPAsyiRFS-------ETVEEELDEGVEYDMDEEDEAWLEELNEKRKSEGVEKISED 156
                         170
                  ....*....|
gi 2217355360 166 TLERVLEELE 175
Cdd:pfam10513 157 EFEILMDRFE 166
 
Name Accession Description Interval E-value
ePHD_JADE2 cd15705
Extended PHD finger found in protein Jade-2 and similar proteins; The extended plant ...
254-364 2.39e-80

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.


Pssm-ID: 277175  Cd Length: 111  Bit Score: 252.71  E-value: 2.39e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 254 CLLCPKRGGALKPTRSGTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKECTGTCIQCSMPSCVTAF 333
Cdd:cd15705     1 CLLCPKRGGALKPTRSGTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKECTGTCIQCSMPSCITAF 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2217355360 334 HVTCAFDHGLEMRTILADNDEVKFKSFCQEH 364
Cdd:cd15705    81 HVTCAFDHGLEMRTTLADNDEVKFKSFCLEH 111
ePHD_JADE cd15671
Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended ...
254-364 1.22e-77

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: 245.43  E-value: 1.22e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 254 CLLCPKRGGALKPTRSGTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKECTGTCIQCSMPSCVTAF 333
Cdd:cd15671     1 CVLCPKKGGAMKSTKSGTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPMSRWALVCVLCKEKTGACIQCSVKSCKTAF 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2217355360 334 HVTCAFDHGLEMRTIL-ADNDEVKFKSFCQEH 364
Cdd:cd15671    81 HVTCAFQHGLEMKTILeDEDDEVKFKSYCPKH 112
ePHD_JADE3 cd15706
Extended PHD finger found in protein Jade-3 and similar proteins; The extended plant ...
254-364 1.09e-63

Extended PHD finger found in protein Jade-3 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-3. Jade-3, also termed PHD finger protein 16 (PHF16), is a plant homeodomain (PHD) zinc finger protein that is close related to Jade-1, which functions as an essential regulator of multiple cell signaling pathways. Like Jade-1, Jade-3 is required for ING4 and ING5 to associate with histone acetyl transferase (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-3 contains a canonical PHD domain followed by this non-canonical ePHD domain, both of which are zinc-binding motifs.


Pssm-ID: 277176  Cd Length: 111  Bit Score: 208.42  E-value: 1.09e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 254 CLLCPKRGGALKPTRSGTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKECTGTCIQCSMPSCVTAF 333
Cdd:cd15706     1 CLLCPKTGGAMKATRTGTKWAHVSCALWIPEVSIACPERMEPITKVSHIPPSRWALVCSLCKLKTGACIQCSVKSCITAF 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2217355360 334 HVTCAFDHGLEMRTILADNDEVKFKSFCQEH 364
Cdd:cd15706    81 HVTCAFEHSLEMKTILDEGDEVKFKSYCLKH 111
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
137-530 1.82e-63

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


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 225.25  E-value: 1.82e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 137 YDLDEIDAYWLELIN-SELKEMERPELDELTLERVLEELETLCHQNMARAIETqegLGIEYDEDVVCDVCRSPEGEDGNE 215
Cdd:COG5141   133 YDLDEYDTMWLRYLNeSAIDENVSEEAFEIIVTRLEKEWFFFEHGLPDKHVEP---IEPSDEFDDICTKCTSTHNENSNA 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 216 MVFCDKCNVCVHQACYGILKVPTGSWLCRTCALGVQP--KCLLCPKRGGALKPTRSGtKWVHVSCALWIPEVSIGCPEKM 293
Cdd:COG5141   210 IVFCDGCEICVHQSCYGIQFLPEGFWLCRKCIYGEYQirCCSFCPSSDGAFKQTSDG-RWGHVICAMFNPELSFGHLLSK 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 294 EPITKISHIPASRWALSCSLCKECTGTCIQCSMPSCVTAFHVTCAFDHGLEMRTILADN---DEVKFKSFCQEHSDGG-- 368
Cdd:COG5141   289 DPIDNIASVSSSRWKLGCLICKEFGGTCIQCSYFNCTRAYHVTCARRAGYFDLNIYSHNgisYCIDHEPLCRKHYPLGyg 368
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 369 --------------PRNEPTSEP--TEPSQAGEDLEKVTLRKQ---------RLQQLEEDFYELVEPAevaerldlaeAL 423
Cdd:COG5141   369 rmnglryfgyeklrYKNPPTAIPrkVRAARPRATLFMKLCWKQppatpsvlsRVEACDLKEKDRQDLP----------VN 438
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 424 VDFIYQYWKLKRKANANQPlLTPKTDEVDNLAQQEQDVLYRRLKLFTHLRQDLERVRNLCYMVTRRERTKHAICKLQEQI 503
Cdd:COG5141   439 IFDICKYWEMKRKSEIGGP-LVILPDIVYSLKTLEDWMSKRRMREVAKALQDQYQLLTLVESTAKRQLLKCQLSNLRKKF 517
                         410       420
                  ....*....|....*....|....*..
gi 2217355360 504 FHLqMKLIEQDLCRGLSTSFPIDGTFF 530
Cdd:COG5141   518 LNL-NYFPAQRLLQVKIIDLDVDGLFN 543
ePHD_JADE1 cd15704
Extended PHD finger found in protein Jade-1 and similar proteins; The extended plant ...
251-365 3.98e-63

Extended PHD finger found in protein Jade-1 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-1. Jade-1, also termed PHD finger protein 17 (PHF17), is a novel binding partner of von Hippel-Lindau (VHL) tumor suppressor Pvhl, a key regulator of cellular oxygen sensing pathway. It is highly expressed in renal proximal tubules. Jade-1 functions as an essential regulator of multiple cell signaling pathways. It may be involved in the Serine/threonine kinase AKT/AKT1 pathway during renal cancer pathogenesis and normally prevents renal epithelial cell proliferation and transformation. It also acts as a pro-apoptotic and growth suppressive ubiquitin ligase to inhibit canonical Wnt downstream effector beta-catenin for proteasomal degradation and ASA transcription factor associated with histone acetyltransferase activity and with increased abundance of cyclin-dependent kinase inhibitor p21. Moreover, Jade-1 is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and Eaf6 to form a HBO1 complex, and plays a role in epithelial cell regeneration. It has also been identified as a novel component of the nephrocystin protein (NPHP) complex and interacts with the ciliary protein nephrocystin-4 (NPHP4). Jade-1 contains a canonical plant homeodomain (PHD) finger followed by this non-canonical ePHD finger, both of which are zinc-binding motifs.


Pssm-ID: 277174  Cd Length: 118  Bit Score: 206.85  E-value: 3.98e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 251 QPKCLLCPKRGGALKPTRSGTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKECTGTCIQCSMPSCV 330
Cdd:cd15704     1 QPKCLLCPKKGGAMKPTRSGTKWVHVSCALWIPEVSIGSPEKMEPITKVSHIPSSRWALVCSLCNEKVGASIQCSVKNCR 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2217355360 331 TAFHVTCAFDHGLEMRTILADNDEVKFKSFCQEHS 365
Cdd:cd15704    81 TAFHVTCAFDRGLEMKTILAENDEVKFKSYCPKHS 115
ePHD_RNO cd15707
Extended PHD finger found in Drosophila melanogaster PHD finger protein rhinoceros (RNO) and ...
254-364 6.16e-63

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: 206.29  E-value: 6.16e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 254 CLLCPKRGGALKPTRSGTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKECTGTCIQCSMPSCVTAF 333
Cdd:cd15707     1 CILCPNKGGAMKSTRSGTKWAHVSCALWIPEVSIGCVEKMEPITKISSIPASRWALICVLCRERTGACIQCSVKTCKTAY 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2217355360 334 HVTCAFDHGLEMRTILADN--DEVKFKSFCQEH 364
Cdd:cd15707    81 HVTCGFQHGLEMKTILDEEseDGVKLRSYCQKH 113
zf-HC5HC2H_2 pfam13832
PHD-zinc-finger like domain;
252-364 1.57e-43

PHD-zinc-finger like domain;


Pssm-ID: 463991 [Multi-domain]  Cd Length: 109  Bit Score: 152.88  E-value: 1.57e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 252 PKCLLCPKRGGALKPTrSGTKWVHVSCALWIPEVSIGCPEKMEPITkISHIPASRWALSCSLCKECTGTCIQCSMPSCVT 331
Cdd:pfam13832   1 VRCCLCPLRGGALKQT-SDGRWVHVLCAIFVPEVRFGNVATMEPID-VSRIPPERWKLKCVFCKKRSGACIQCSKGRCTT 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2217355360 332 AFHVTCAFDHGLEMRtiLADNDEVKFKSFCQEH 364
Cdd:pfam13832  79 AFHVTCAQAAGVYME--PEDWPNVVVIAYCQKH 109
ePHD_BRPF cd15670
Extended PHD finger found in BRPF proteins; The extended plant homeodomain (ePHD) zinc finger ...
254-364 5.65e-41

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.


Pssm-ID: 277140  Cd Length: 116  Bit Score: 145.94  E-value: 5.65e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 254 CLLCPKRGGALKPTRSGtKWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKECTGTCIQCSMPSCVTAF 333
Cdd:cd15670     1 CVLCPNKGGAFKQTDDG-RWAHVVCALWIPEVSFANTVFLEPIDGIQNIPKARWKLTCYICKKRMGACIQCHKKNCYTAF 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2217355360 334 HVTCAFDHGLEMR------TILADNDEVKFKSFCQEH 364
Cdd:cd15670    80 HVTCAQQAGLYMKiepvkdPGNGTSDSVRKEAYCDKH 116
ePHD cd15571
Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is ...
254-364 1.02e-37

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: 136.56  E-value: 1.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 254 CLLCPKRGGALKP-----TRSGTKWVHVSCALWIPEVSIGCPEKMEPItKISHIPASRWALSCSLCKECTGTCIQCSMPS 328
Cdd:cd15571     1 CALCPRSGGALKGggalkTTSDGLWVHVVCALWSPEVYFDDGTLLEVE-GVSKIPKRRKKLKCSICGKRGGACIQCSYPG 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2217355360 329 CVTAFHVTCAFDHGLEMRTIladNDEVKFKSFCQEH 364
Cdd:cd15571    80 CPRSFHVSCAIRAGCLFEFE---DGPGNFVVYCPKH 112
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
275-364 9.22e-34

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: 124.36  E-value: 9.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 275 HVSCALWIPEVSI-GCPEKMEPITKISHIPASRWALSCSLCKECTGTCIQCSMPSCVTAFHVTCAFDHGLEMRTilaDND 353
Cdd:pfam13771   1 HVVCALWSPELVQrGNDSMGFPIEDIEKIPKRRWKLKCYLCKKKGGACIQCSKKNCRRAFHVTCALEAGLLMQF---DED 77
                          90
                  ....*....|.
gi 2217355360 354 EVKFKSFCQEH 364
Cdd:pfam13771  78 NGTFKSYCKKH 88
ePHD_ATX1_2_like cd15662
Extended PHD finger found in Arabidopsis thaliana ATX1, -2, and similar proteins; The extended ...
254-364 3.10e-31

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: 117.96  E-value: 3.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 254 CLLCPKRGGALKPTRSGTkWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKECTGTCIQCSMPSCVTAF 333
Cdd:cd15662     1 CCLCPVVGGALKPTTDGR-WAHLACAIWIPETCLLDVKTMEPVDGINAISKERWELSCTICKQRYGACIQCSNNSCRVAY 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2217355360 334 HVTCAFDHGLEMRTILADNDE-----VKFKSFCQEH 364
Cdd:cd15662    80 HPLCARAAGLCMEVADEGGEDpgdqgLRLLSYCPRH 115
ePHD_BRPF1 cd15701
Extended PHD finger found in bromodomain and PHD finger-containing protein 1 (BRPF1) and ...
254-346 1.57e-30

Extended PHD finger found in bromodomain and PHD finger-containing protein 1 (BRPF1) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of BRPF1. BRPF1, also termed peregrin, or protein Br140, is a multi-domain protein that binds histones, mediates monocytic leukemic zinc-finger protein (MOZ) -dependent histone acetylation, and is required for Hox gene expression and segmental identity. It is a close partner of the MOZ histone acetyltransferase (HAT) complex and a novel Trithorax group (TrxG) member with a central role during development. BRPF1 is primarily a nuclear protein that has a broad tissue distribution and is abundant in testes and spermatogonia. It contains 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 methylated lysine 4 of histone H3 (H3K4me), 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. BRPF1 may be involved in chromatin remodeling.


Pssm-ID: 277171 [Multi-domain]  Cd Length: 121  Bit Score: 116.33  E-value: 1.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 254 CLLCPKRGGALKPTRSGtKWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKE-CTGTCIQCSMPSCVTA 332
Cdd:cd15701     1 CALCPNKGGAFKQTDDG-RWAHVVCALWIPEVCFANTVFLEPIDSIEHIPPARWKLTCYICKQrGSGACIQCHKANCYTA 79
                          90
                  ....*....|....
gi 2217355360 333 FHVTCAFDHGLEMR 346
Cdd:cd15701    80 FHVTCAQQAGLYMK 93
ePHD_JMJD2 cd15675
Extended PHD finger found in Jumonji domain-containing protein 2 (JMJD2) family of histone ...
254-347 3.72e-30

Extended PHD finger found in Jumonji domain-containing protein 2 (JMJD2) family of histone demethylases; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of JMJD2 proteins. JMJD2 proteins, also termed lysine-specific demethylase 4 histone demethylases (KDM4), have been implicated in various cellular processes including DNA damage response, transcription, cell cycle regulation, cellular differentiation, senescence, and carcinogenesis. They selectively catalyze the demethylation of di- and trimethylated H3K9 and H3K36. This model contains three JMJD2 proteins, JMJD2A-C, which all contain jmjN and jmjC domains in the N-terminal region, followed by a canonical PHD finger, this non-canonical ePHD finger, and a Tudor domain. JMJD2D is not included in this family, since it lacks both PHD and Tudor domains and has a different substrate specificity. JMJD2A-C are required for efficient cancer cell growth.


Pssm-ID: 277145 [Multi-domain]  Cd Length: 112  Bit Score: 114.76  E-value: 3.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 254 CLLCPKRGGALKPTRSGtKWVHVSCALWIPEVSIGCPEKMEPITkISHIPASRWALSCSLCKECT------GTCIQCSMP 327
Cdd:cd15675     1 CCLCCLRGGALKPTTDG-RWAHVVCAIAIPEVRFSNVPERGPID-ISKIPPARLKLKCIYCSKITksmshmGACIQCSTG 78
                          90       100
                  ....*....|....*....|
gi 2217355360 328 SCVTAFHVTCAFDHGLEMRT 347
Cdd:cd15675    79 KCTTSFHVTCAHAAGVQMEP 98
PHD_JADE2 cd15680
PHD finger found in protein Jade-2 and similar proteins; Jade-2, also termed PHD finger ...
201-246 2.36e-29

PHD finger found in protein Jade-2 and similar proteins; 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 Cys4HisCys3 PHD finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, both of which are zinc-binding motifs. This model corresponds to the canonical Cys4HisCys3 PHD finger.


Pssm-ID: 277150 [Multi-domain]  Cd Length: 46  Bit Score: 110.48  E-value: 2.36e-29
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2217355360 201 VCDVCRSPEGEDGNEMVFCDKCNVCVHQACYGILKVPTGSWLCRTC 246
Cdd:cd15680     1 VCDVCRSPEGEDGNEMVFCDKCNVCVHQACYGILKVPTGSWLCRTC 46
ePHD_BRPF3 cd15703
Extended PHD finger found in bromodomain and PHD finger-containing protein 3 (BRPF3) and ...
254-346 1.07e-28

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


Pssm-ID: 277173 [Multi-domain]  Cd Length: 118  Bit Score: 110.92  E-value: 1.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 254 CLLCPKRGGALKPTRSGtKWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKE-CTGTCIQCSMPSCVTA 332
Cdd:cd15703     1 CVLCPNKGGAFKQTSDG-RWAHVVCAIWIPEVCFANTVFLEPVEGVNNIPPARWKLTCYLCKQkGRGAAIQCHKVNCYTA 79
                          90
                  ....*....|....
gi 2217355360 333 FHVTCAFDHGLEMR 346
Cdd:cd15703    80 FHVTCAQRAGLFMK 93
PHD_JADE cd15573
PHD finger found in proteins Jade-1, Jade-2, Jade-3, and similar proteins; This family ...
201-246 3.84e-28

PHD finger found in proteins Jade-1, Jade-2, Jade-3, and similar proteins; This family includes proteins Jade-1 (PHF17), Jade-2 (PHF15), and Jade-3 (PHF16), each of which 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. 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 Cys4HisCys3 PHD finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, both of which are zinc-binding motifs. This model corresponds to the canonical Cys4HisCys3 PHD finger.


Pssm-ID: 277048 [Multi-domain]  Cd Length: 46  Bit Score: 106.72  E-value: 3.84e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2217355360 201 VCDVCRSPEGEDGNEMVFCDKCNVCVHQACYGILKVPTGSWLCRTC 246
Cdd:cd15573     1 VCDVCRSPDSEEGNEMVFCDKCNICVHQACYGIQKIPEGSWLCRTC 46
ePHD_BRPF2 cd15702
Extended PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and ...
254-346 4.31e-28

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.


Pssm-ID: 277172  Cd Length: 118  Bit Score: 109.36  E-value: 4.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 254 CLLCPKRGGALKPTRSgTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKE-CTGTCIQCSMPSCVTA 332
Cdd:cd15702     1 CVLCPNKGGAFKKTDD-DRWGHVVCALWIPEVGFANTVFIEPIDGVRNIPPARWKLTCYLCKQkGVGACIQCHKANCYTA 79
                          90
                  ....*....|....
gi 2217355360 333 FHVTCAFDHGLEMR 346
Cdd:cd15702    80 FHVTCAQKAGLYMK 93
PHD_JADE1 cd15679
PHD finger found in protein Jade-1 and similar proteins; Jade-1, also termed PHD finger ...
201-246 8.41e-28

PHD finger found in protein Jade-1 and similar proteins; Jade-1, also termed PHD finger protein 17 (PHF17), is a novel binding partner of von Hippel-Lindau (VHL) tumor suppressor Pvhl, a key regulator of the cellular oxygen sensing pathway. It is highly expressed in renal proximal tubules. Jade-1 functions as an essential regulator of multiple cell signaling pathways. It may be involved in the serine/threonine kinase AKT/AKT1 pathway during renal cancer pathogenesis and normally prevents renal epithelial cell proliferation and transformation. It also acts as a pro-apoptotic and growth suppressive ubiquitin ligase to inhibit canonical Wnt downstream effector beta-catenin for proteasomal degradation, and as a transcription factor associated with histone acetyltransferase activity and with increased abundance of cyclin-dependent kinase inhibitor p21. Moreover, Jade-1 is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and Eaf6 to form a HBO1 complex, and plays a role in epithelial cell regeneration. It has also been identified as a novel component of the nephrocystin protein (NPHP) complex and interacts with the ciliary protein nephrocystin-4 (NPHP4). Jade-1 contains a canonical Cys4HisCys3 plant homeodomain (PHD) finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, both of which are zinc-binding motifs. This model corresponds to the canonical Cys4HisCys3 PHD finger.


Pssm-ID: 277149 [Multi-domain]  Cd Length: 46  Bit Score: 105.93  E-value: 8.41e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2217355360 201 VCDVCRSPEGEDGNEMVFCDKCNVCVHQACYGILKVPTGSWLCRTC 246
Cdd:cd15679     1 VCDVCQSPDGEDGNEMVFCDKCNICVHQACYGILKVPEGSWLCRTC 46
PHD_JADE3 cd15681
PHD finger found in protein Jade-3 and similar proteins; Jade-3, also termed PHD finger ...
201-250 3.34e-27

PHD finger found in protein Jade-3 and similar proteins; Jade-3, also termed PHD finger protein 16 (PHF16), 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-3 is required for ING4 and ING5 to associate with histone acetyl transferase (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-3 contains a canonical Cys4HisCys3 PHD domain followed by a non-canonical extended PHD (ePHD) domain, Cys2HisCys5HisCys2His, both of which are zinc-binding motifs. This model corresponds to the canonical Cys4HisCys3 PHD finger.


Pssm-ID: 277151 [Multi-domain]  Cd Length: 50  Bit Score: 104.28  E-value: 3.34e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217355360 201 VCDVCRSPEGEDGNEMVFCDKCNVCVHQACYGILKVPTGSWLCRTCALGV 250
Cdd:cd15681     1 ICDVCRSPDSEEGNDMVFCDKCNICVHQACYGILKVPEGSWLCRTCVLGI 50
PHD_BRPF_JADE_like cd15492
PHD finger found in BRPF proteins, Jade proteins, protein AF-10, AF-17, and similar proteins; ...
201-246 4.31e-26

PHD finger found in BRPF proteins, Jade proteins, protein AF-10, AF-17, and similar proteins; The family includes BRPF proteins, Jade proteins, protein AF-10 and AF-17. BRPF proteins 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 canonical Cys4HisCys3 plant homeodomain (PHD) zinc finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. PHD and ePHD fingers both bind to lysine 4 of histone H3 (K4H3), bromodomains interact with acetylated lysines on N-terminal tails of histones and other proteins, and PWWP domains show histone-binding and chromatin association properties. Jade proteins are 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. AF-10, also termed ALL1 (acute lymphoblastic leukemia)-fused gene from chromosome 10 protein, is a transcription factor that 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. AF-17, also termed ALL1-fused gene from chromosome 17 protein, is a putative transcription factor that may play a role in multiple signaling pathways. All Jade proteins, AF-10, and AF-17 contain a canonical PHD finger followed by a non-canonical ePHD finger. This model corresponds to the canonical PHD finger.


Pssm-ID: 276967 [Multi-domain]  Cd Length: 46  Bit Score: 101.16  E-value: 4.31e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2217355360 201 VCDVCRSPEGEDGNEMVFCDKCNVCVHQACYGILKVPTGSWLCRTC 246
Cdd:cd15492     1 VCDVCLDGESEDDNEIVFCDGCNVAVHQSCYGIPLIPEGDWFCRKC 46
ePHD_ATX3_4_5_like cd15663
Extended PHD finger found in Arabidopsis thaliana ATX3, -4, -5, and similar proteins; The ...
254-364 5.90e-26

Extended PHD finger found in Arabidopsis thaliana ATX3, -4, -5, 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 ATX3 (also termed protein SET domain group 14, or trithorax-homolog protein 3), ATX4 (also termed protein SET domain group 16, or trithorax-homolog protein 4) and ATX5 (also termed protein SET domain group 29, or trithorax-homolog protein 5), which belong to the histone-lysine methyltransferase family. These proteins show distinct phylogenetic origins from the family of ATX1 and ATX2. They are multi-domain proteins that consist of an N-terminal PWWP domain, a canonical PHD finger, this non-canonical extended PHD finger, and a C-terminal SET domain.


Pssm-ID: 277133  Cd Length: 112  Bit Score: 102.98  E-value: 5.90e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 254 CLLCPKRGGALKPTRSGTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKECTGTCIQCSmpSCVTAF 333
Cdd:cd15663     1 CCLCPVKGGALKPTDVEGLWVHVTCAWFRPEVCFKNEEKMEPAVGLLRIPLSTFLKACVICKQIHGSCTQCC--KCATYF 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2217355360 334 HVTCAFDHGLEMRT-ILADN--DEVKFKSFCQEH 364
Cdd:cd15663    79 HAMCASRAGYHMELhCLEKNgvQITRMVSYCSFH 112
ePHD_PHF14 cd15674
Extended PHD finger found in PHD finger protein 14 (PHF14) and similar proteins; The extended ...
254-364 7.46e-24

Extended PHD finger found in PHD finger protein 14 (PHF14) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of PHF14. 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 this non-canonical ePHD finger. It can interact with histones through its PHD fingers.


Pssm-ID: 277144  Cd Length: 114  Bit Score: 97.07  E-value: 7.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 254 CLLCPKRGGALKPTRSGtKWVHVSCALWIPEVSIGCPEKMEPITkISHIPASRW-ALSCSLCKEC----TGTCIQCSMPS 328
Cdd:cd15674     1 CELCPNRGGIFKETDTG-RWVHLVCALYTPGVAFGDVDKLSPVT-LTEMNYSKWgARECSLCEDPrfarTGVCISCDAGM 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2217355360 329 CVTAFHVTCAFDHGLEMRTILADNDEVKFKSFCQEH 364
Cdd:cd15674    79 CKSYFHVTCAQREGLLSEATDEEDIADPFYAYCKQH 114
ePHD_AF10_like cd15672
Extended PHD finger found in protein AF-10 and AF-17; The extended plant homeodomain (ePHD) ...
254-364 2.45e-23

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.


Pssm-ID: 277142  Cd Length: 116  Bit Score: 95.61  E-value: 2.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 254 CLLCPKRGGALKPTRSGTkWVHVSCALWIPEVSIGCPEKMEPITkISHIPASRWALSCSLCKE-------CTGTCIQCSM 326
Cdd:cd15672     1 CELCPHKDGALKRTDNGG-WAHVVCALYIPEVRFGNVATMEPII-LQDVPQDRFNKTCYICEEqgreskaSTGACMQCNK 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217355360 327 PSCVTAFHVTCAFDHGL--EMRTILADNdeVKFKSFCQEH 364
Cdd:cd15672    79 SGCKQSFHVTCAQMAGLlcEEAGNYSDN--VKYCGYCSYH 116
ePHD_JMJD2B cd15714
Extended PHD finger found in Jumonji domain-containing protein 2B (JMJD2B); The extended plant ...
254-346 1.83e-22

Extended PHD finger found in Jumonji domain-containing protein 2B (JMJD2B); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of JMJD2B. JMJD2B, also termed lysine-specific demethylase 4B (KDM4B), or JmjC domain-containing histone demethylation protein 3B (JHDM3B), specifically antagonizes the trimethyl group from H3K9 in pericentric heterochromatin and reduces H3K36 methylation in mammalian cells. It plays an essential role in the growth regulation of cancer cells by modulating the G1-S transition and promotes cell-cycle progression through the regulation of cyclin-dependent kinase 6 (CDK6). It interacts with heat shock protein 90 (Hsp90) and its stability can be regulated by Hsp90. JMJD2B also functions as a direct transcriptional target of p53, which induces its expression through promoter binding. Moreover, JMJD2B expression can be controlled by hypoxia-inducible factor 1alpha (HIF1alpha) in colorectal cancer and estrogen receptor alpha (ERalpha) in breast cancer. It is also involved in bladder, lung, and gastric cancer. JMJD2B contains jmjN and jmjC domains in the N-terminal region, followed by a canonical PHD finger, this non-canonical ePHD finger, and a Tudor domain.


Pssm-ID: 277184  Cd Length: 110  Bit Score: 93.08  E-value: 1.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 254 CLLCPKRGGALKPTrSGTKWVHVSCALWIPEVSIGCPEKMEPItKISHIPASRWALSCSLC----KECTGTCIQCSMPSC 329
Cdd:cd15714     1 CCLCNLRGGALQMT-TDERWVHVICAIAVPEARFLNVIERHPV-DVSAIPEQRWKLKCVYCrkrmKKVSGACIQCSYDHC 78
                          90
                  ....*....|....*..
gi 2217355360 330 VTAFHVTCAFDHGLEMR 346
Cdd:cd15714    79 STSFHVTCAHAAGVVME 95
ePHD_JMJD2C cd15715
Extended PHD finger found in Jumonji domain-containing protein 2C (JMJD2C); The extended plant ...
254-345 2.51e-21

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.


Pssm-ID: 277185  Cd Length: 110  Bit Score: 89.63  E-value: 2.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 254 CLLCPKRGGALKPTrSGTKWVHVSCALWIPEVSIGCPEKMEPItKISHIPASRWALSCSLC----KECTGTCIQCSMPSC 329
Cdd:cd15715     1 CCLCNLRGGALKQT-SDDKWAHVMCAVALPEVRFINVVERTPI-DISRIPLQRLKLKCIFCrnriKRVSGACIQCSYGRC 78
                          90
                  ....*....|....*.
gi 2217355360 330 VTAFHVTCAFDHGLEM 345
Cdd:cd15715    79 PASFHVTCAHAAGVLM 94
ePHD_AF10 cd15708
Extended PHD finger found in protein AF-10 and similar proteins; The extended plant ...
253-364 2.79e-21

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.


Pssm-ID: 277178  Cd Length: 129  Bit Score: 90.14  E-value: 2.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 253 KCLLCPKRGGALKPTRSGtKWVHVSCALWIPEVSIGCPEKMEPITkISHIPASRWALSCSLCKE-------CTGTCIQCS 325
Cdd:cd15708     4 RCELCPHKDGALKRTDNG-GWAHVVCALYIPEVQFANVSTMEPIV-LQSVPHERYNKTCYICDEqgreskaATGACMTCN 81
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2217355360 326 MPSCVTAFHVTCAFDHGLEMRTILADNDEVKFKSFCQEH 364
Cdd:cd15708    82 KHGCRQAFHVTCAQLAGLLCEEEGNGADNVQYCGYCKYH 120
ePHD_AF17 cd15709
Extended PHD finger found in protein AF-17 and similar proteins; The extended plant ...
253-364 2.86e-18

Extended PHD finger found in protein AF-17 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of AF-17. AF-17, also termed ALL1-fused gene from chromosome 17 protein, is encoded by gene AF17 that has been identified in hematological malignancies as a translocation partner 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. AF-17 contains an N-terminal plant homeodomain (PHD) finger followed by a non-canonical ePHD finger.


Pssm-ID: 277179  Cd Length: 125  Bit Score: 81.65  E-value: 2.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 253 KCLLCPKRGGALKPTRSGtKWVHVSCALWIPEVSIGCPEKMEPITkISHIPASRWALSCSLCKE-------CTGTCIQCS 325
Cdd:cd15709     4 RCELCPHKDGALKRTDNG-GWAHVVCALYIPEVQFANVLTMEPIV-LQYVPHDRFNKTCYICEEqgreskaASGACMTCN 81
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2217355360 326 MPSCVTAFHVTCAFDHGLEMRTILADNDEVKFKSFCQEH 364
Cdd:cd15709    82 RHGCRQAFHVTCAQMAGLLCEEEVLEVDNVKYCGYCKYH 120
ePHD_JMJD2A cd15713
Extended PHD finger (ePHD) found in Jumonji domain-containing protein 2A (JMJD2A); The ...
254-346 7.82e-17

Extended PHD finger (ePHD) found in Jumonji domain-containing protein 2A (JMJD2A); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of JMJD2A. JMJD2A, also termed lysine-specific demethylase 4A (KDM4A), or JmjC domain-containing histone demethylation protein 3A (JHDM3A), catalyzes the demethylation of di- and trimethylated H3K9 and H3K36. It is involved in carcinogenesis and functions as a transcription regulator that may either stimulate or repress gene transcription. It associates with nuclear receptor co-repressor complex or histone deacetylases. Moreover, JMJD2A forms complexes with both the androgen and estrogen receptor (ER) and plays an essential role in growth of both ER-positive and -negative breast tumors. It is also involved in prostate, colon, and lung cancer progression. JMJD2A contains jmjN and jmjC domains in the N-terminal region, followed by a canonical PHD finger, this non-canonical ePHD finger, and a Tudor domain.


Pssm-ID: 277183  Cd Length: 110  Bit Score: 76.94  E-value: 7.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 254 CLLCPKRGGALKPTRSgTKWVHVSCALWIPEVSIGCPEKMEPItKISHIPASRWALSCSLCKE----CTGTCIQCSMPSC 329
Cdd:cd15713     1 CCLCSLRGGALQRAND-DKWVHVMCAVAVLEARFVNIAERSPV-DVSKIPLQRFKLKCIFCKKrrkrTAGCCVQCSHGRC 78
                          90
                  ....*....|....*..
gi 2217355360 330 VTAFHVTCAFDHGLEMR 346
Cdd:cd15713    79 PTSFHASCAQAAGVMMQ 95
PHD_BRPF2 cd15677
PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and similar ...
199-246 2.84e-14

PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and similar proteins; BRPF2, also termed bromodomain-containing protein 1 (BRD1), or BR140-like protein, 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 canonical Cys4HisCys3 plant homeodomain (PHD) finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. This model corresponds to the canonical Cys4HisCys3 PHD finger.


Pssm-ID: 277147 [Multi-domain]  Cd Length: 54  Bit Score: 67.73  E-value: 2.84e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217355360 199 DVVCDVCRSPEGEDGNEMVFCDKCNVCVHQACYGILKVPTGSWLCRTC 246
Cdd:cd15677     1 DAVCCICMDGECQNSNVILFCDMCNLAVHQECYGVPYIPEGQWLCRHC 48
PHD_BRPF cd15572
PHD finger found in bromodomain and PHD finger-containing (BRPF) proteins; The family of BRPF ...
199-246 6.59e-14

PHD finger found in bromodomain and PHD finger-containing (BRPF) proteins; The family of BRPF proteins includes BRPF1, BRD1/BRPF2, and BRPF3. They 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 canonical Cys4HisCys3 plant homeodomain (PHD) zinc finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. PHD and ePHD fingers both bind to lysine 4 of histone H3 (K4H3), bromodomains interact with acetylated lysines on N-terminal tails of histones and other proteins, and PWWP domains show histone-binding and chromatin association properties. This model corresponds to the canonical Cys4HisCys3 PHD finger.


Pssm-ID: 277047 [Multi-domain]  Cd Length: 54  Bit Score: 66.49  E-value: 6.59e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217355360 199 DVVCDVCRSPEGEDGNEMVFCDKCNVCVHQACYGILKVPTGSWLCRTC 246
Cdd:cd15572     1 DAVCCICLDGECQNSNVILFCDMCNLAVHQECYGVPYIPEGQWLCRRC 48
PHD_ATX3_4_5_like cd15495
PHD finger found in Arabidopsis thaliana histone-lysine N-methyltransferase arabidopsis ...
202-246 7.60e-14

PHD finger found in Arabidopsis thaliana histone-lysine N-methyltransferase arabidopsis trithorax-like protein ATX3, ATX4, ATX5, and similar proteins; The family includes A. thaliana ATX3 (also termed protein SET domain group 14, or trithorax-homolog protein 3), ATX4 (also termed protein SET domain group 16, or trithorax-homolog protein 4) and ATX5 (also termed protein SET domain group 29, or trithorax-homolog protein 5), which belong to the histone-lysine methyltransferase family. They show distinct phylogenetic origins from the ATX1 and ATX2 family. They are multi-domain containing proteins that consist of an N-terminal PWWP domain, a canonical Cys4HisCys3 plant homeodomain (PHD) finger, a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, and a C-terminal SET domain; this model corresponds to the Cys4HisCys3 canonical PHD finger.


Pssm-ID: 276970 [Multi-domain]  Cd Length: 47  Bit Score: 66.24  E-value: 7.60e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2217355360 202 CDVCRSPEGEDGNEMVFCDKCNVCVHQACYGILKV-PTGSWLCRTC 246
Cdd:cd15495     2 CAVCNEGEDDDNNPLITCNRCQISVHQKCYGIREVdPDGSWVCRAC 47
PHD_BRPF1 cd15676
PHD finger found in bromodomain and PHD finger-containing protein 1 (BRPF1) and similar ...
197-246 1.60e-13

PHD finger found in bromodomain and PHD finger-containing protein 1 (BRPF1) and similar proteins; BRPF1, also termed peregrin or protein Br140, is a multi-domain protein that binds histones, mediates monocytic leukemic zinc-finger protein (MOZ)-dependent histone acetylation, and is required for Hox gene expression and segmental identity. It is a close partner of the MOZ histone acetyltransferase (HAT) complex and a novel Trithorax group (TrxG) member with a central role during development. BRPF1 is primarily a nuclear protein that has a broad tissue distribution and is abundant in testes and spermatogonia. It contains a canonical Cys4HisCys3 plant homeodomain (PHD) zinc finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. PHD and ePHD fingers both bind to lysine 4 of histone H3 (K4H3), bromodomains interact with acetylated lysines on N-terminal tails of histones and other proteins, and PWWP domains show histone-binding and chromatin association properties. BRPF1 may be involved in chromatin remodeling. This model corresponds to the canonical Cys4HisCys3 PHD finger.


Pssm-ID: 277146 [Multi-domain]  Cd Length: 62  Bit Score: 65.85  E-value: 1.60e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217355360 197 DEDVVCDVCRSPEGEDGNEMVFCDKCNVCVHQACYGILKVPTGSWLCRTC 246
Cdd:cd15676     5 DEDAVCCICNDGECQNSNVILFCDMCNLAVHQECYGVPYIPEGQWLCRRC 54
PHD_AF10_AF17 cd15574
PHD finger found in protein AF-10 and AF-17; This family includes protein AF-10 and AF-17. ...
202-246 1.91e-13

PHD finger found in protein AF-10 and AF-17; This family includes protein AF-10 and AF-17. AF-10, also termed ALL1 (acute lymphoblastic leukemia)-fused gene from chromosome 10 protein, is a transcription factor encoded by gene AF10, a translocation partner of the MLL (mixed-lineage leukemia) oncogene in leukemia. 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 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 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 canonical Cys4HisCys3 plant homeodomain (PHD) finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His. 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 a Dot1-interacting protein that opposes H2B ubiquitination to reduce polymerase II (Pol II) transcription. This model corresponds to the canonical Cys4HisCys3 PHD finger.


Pssm-ID: 277049 [Multi-domain]  Cd Length: 48  Bit Score: 65.23  E-value: 1.91e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2217355360 202 CDVCRSPEGEDGNEMVFCD--KCNVCVHQACYGILKVPTGSWLCRTC 246
Cdd:cd15574     2 CCVCSDERGWAENPLVYCDghGCNVAVHQACYGIVQVPTGPWFCRKC 48
ePHD_Snt2p_like cd15667
Extended PHD finger found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) ...
263-340 3.41e-13

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.


Pssm-ID: 277137  Cd Length: 141  Bit Score: 67.41  E-value: 3.41e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217355360 263 ALKPTRSGTkWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKECTGTCIQCSmpSCVTAFHVTCAFD 340
Cdd:cd15667    25 ALKCTSNGT-WCHVLCALFNEDIKFGNSKSLQPILNTESVLLKGSRQKCEICKVSGGGLVKCE--VCDDRFHVSCAQD 99
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
201-246 5.95e-12

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.


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 60.97  E-value: 5.95e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217355360 201 VCDVCRSPEgeDGNEMVFCDKCNVCVHQACYGI----LKVPTGSWLCRTC 246
Cdd:pfam00628   1 YCAVCGKSD--DGGELVQCDGCDDWFHLACLGPpldpAEIPSGEWLCPEC 48
PHD_BRPF3 cd15678
PHD finger found in bromodomain and PHD finger-containing protein 3 (BRPF3) and similar ...
199-246 5.00e-11

PHD finger found in bromodomain and PHD finger-containing protein 3 (BRPF3) and similar proteins; BRPF3 is a homolog of BRPF1 and BRPF2. It is a scaffold protein that forms a novel monocytic leukemic zinc finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complex with other regulatory subunits. BRPF3 contains a canonical Cys4HisCys3 plant homeodomain (PHD) finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. This model corresponds to the canonical Cys4HisCys3 PHD finger.


Pssm-ID: 277148 [Multi-domain]  Cd Length: 55  Bit Score: 58.49  E-value: 5.00e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217355360 199 DVVCDVCRSPEGEDGNEMVFCDKCNVCVHQACYGILKVPTGSWLCRTC 246
Cdd:cd15678     1 DAFCCVCLDDECHNSNVILFCDICNLAVHQECYGVPYIPEGQWLCRCC 48
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
201-246 3.43e-10

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.


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 56.07  E-value: 3.43e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2217355360  201 VCDVCRSPEgeDGNEMVFCDKCNVCVHQACYGI---LKVPTGSWLCRTC 246
Cdd:smart00249   1 YCSVCGKPD--DGGELLQCDGCDRWYHQTCLGPpllEEEPDGKWYCPKC 47
PHD_2 pfam13831
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
214-246 2.62e-09

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.


Pssm-ID: 463990 [Multi-domain]  Cd Length: 35  Bit Score: 53.11  E-value: 2.62e-09
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2217355360 214 NEMVFCDKCNVCVHQACYGILKVPTG-SWLCRTC 246
Cdd:pfam13831   2 SPLVYCSKCSVQVHASCYGVPPIPDGdGWKCRRC 35
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
201-246 4.16e-09

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.


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 52.70  E-value: 4.16e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2217355360 201 VCDVCRSPeGEDGNEMVFCDKCNVCVHQACYGI---LKVPTGSWLCRTC 246
Cdd:cd15489     1 SCIVCGKG-GDLGGELLQCDGCGKWFHADCLGPplsSFVPNGKWICPVC 48
PHD2_PHF10 cd15529
PHD finger 2 found in PHD finger protein 10 (PHF10) and similar proteins; PHF10, also termed ...
201-246 5.83e-09

PHD finger 2 found in PHD finger protein 10 (PHF10) and similar proteins; PHF10, also termed BRG1-associated factor 45a (BAF45a), or XAP135, is a ubiquitously expressed transcriptional regulator that is required for maintaining the undifferentiated status of neuroblasts. It contains a SAY (supporter of activation of yellow) domain and two adjacent plant homeodomain (PHD) fingers. This model corresponds to the second PHD finger.


Pssm-ID: 277004  Cd Length: 44  Bit Score: 52.31  E-value: 5.83e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2217355360 201 VCDVCRSPEGEDgnEMVFCDKCNVCVHQACYGILKVPTGSWLCRTC 246
Cdd:cd15529     1 TCTKCGDPHDED--KMMFCDQCDRGYHTFCVGLRSIPDGRWICPLC 44
PHD1_MTF2_PHF19_like cd15499
PHD finger 1 found in polycomb repressive complex 2 (PRC2)-associated polycomb-like (PCL) ...
201-246 2.54e-08

PHD finger 1 found in polycomb repressive complex 2 (PRC2)-associated polycomb-like (PCL) family proteins MTF2, PHF19, and similar proteins; The family includes two PCL family proteins, metal-response element-binding transcription factor 2 (MTF2/PCL2) and PHF19/PCL3, which are homologs of PHD finger protein1 (PHF1). PCL family proteins are accessory components of the polycomb repressive complex 2 (PRC2) core complex and all contain an N-terminal Tudor domain followed by two PHD fingers, and a C-terminal MTF2 domain. They specifically recognize tri-methylated H3K36 (H3K36me3) through their N-terminal Tudor domains. The interaction between their Tudor domains and H3K36me3 is critical for both the targeting and spreading of PRC2 into active chromatin regions and for the maintenance of optimal repression of poised developmental genes where PCL proteins, H3K36me3, and H3K27me3 coexist. Moreover, unlike other PHD finger-containing proteins, the first PHD fingers of PCL proteins do not display histone H3K4 binding affinity and they do not affect the Tudor domain binding to histones. This model corresponds to the first PHD finger.


Pssm-ID: 276974  Cd Length: 53  Bit Score: 50.58  E-value: 2.54e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217355360 201 VCDVCRSPEGEDGNEMVFCDKCNVCVHQACY-----GILKVPTGSWLCRTC 246
Cdd:cd15499     1 TCSICGGAEARDGNEILICDKCDKGYHQLCHspkvrTSPLEGDEKWFCSRC 51
ePHD_KMT2B cd15694
Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant ...
254-364 7.48e-08

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: 51.19  E-value: 7.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 254 CLLCPKRGGAlKPTRSG-------TKWVHVSCALWIPEVSigcpEKMEPITKISHIPASRW-ALSCSLCKEcTGTCIQCS 325
Cdd:cd15694     1 CALCLKYGDA-DSKDAGrllyigqNEWTHVNCAIWSAEVF----EENDGSLKNVHAAVARGrQMRCEHCQK-IGATVGCC 74
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2217355360 326 MPSCVTAFHVTCAfdhgLEMRTILADNDEVkfksFCQEH 364
Cdd:cd15694    75 LSACLSNFHFMCA----RASRCCFQDDKKV----FCQKH 105
ePHD_KMT2A_like cd15664
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The ...
254-364 7.81e-08

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: 50.87  E-value: 7.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 254 CLLCPKRGGALkPTRSG-------TKWVHVSCALWIPEVSigcpEKMEPITKISHIPASRW-ALSCSLCKEcTGTCIQCS 325
Cdd:cd15664     1 CALCGVYGDDE-PNDAGrllycgqDEWVHINCALWSAEVF----EEDDGSLQNVHSAVSRGrMMKCELCGK-PGATVGCC 74
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2217355360 326 MPSCVTAFHVTCAfdhglemRTILADNDEVKfKSFCQEH 364
Cdd:cd15664    75 LKSCPANYHFMCA-------RKAECVFQDDK-KVFCPAH 105
ePHD_KMT2A cd15693
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant ...
272-366 1.09e-07

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: 50.77  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 272 KWVHVSCALWIPEVSigcpEKMEPITKISHIPASRWA-LSCSLCKEcTGTCIQCSMPSCVTAFHVTCAfdhgLEMRTILA 350
Cdd:cd15693    27 EWTHVNCALWSAEVF----EDDDGSLKNVHMAVIRGKqLRCEFCQK-PGATVGCCLTSCTSNYHFMCS----RAKNCVFL 97
                          90
                  ....*....|....*.
gi 2217355360 351 DNDEVkfksFCQEHSD 366
Cdd:cd15693    98 EDKKV----YCQRHKD 109
PHD1_MTF2 cd15578
PHD finger 1 found in metal-response element-binding transcription factor 2 (MTF2); MTF2, also ...
201-246 1.85e-07

PHD finger 1 found in metal-response element-binding transcription factor 2 (MTF2); MTF2, also termed metal regulatory transcription factor 2, or metal-response element DNA-binding protein M96, or polycomb-like protein 2 (PCL2), complexes with the polycomb repressive complex-2 (PRC2) in embryonic stem cells and regulates the transcriptional networks during embryonic stem cell self-renewal and differentiation. It recruits the PRC2 complex to the inactive X chromosome and target loci in embryonic stem cells. Moreover, MTF2 is required for PRC2-mediated Hox cluster repression. It activates the Cdkn2a gene and promotes cellular senescence, thus suppressing the catalytic activity of PRC2 locally. MTF2 consists of an N-terminal Tudor domain followed by two PHD fingers, and a C-terminal MTF2 domain. This model corresponds to the first PHD finger.


Pssm-ID: 277053  Cd Length: 53  Bit Score: 48.16  E-value: 1.85e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217355360 201 VCDVCRSPEGEDGNEMVFCDKCNVCVHQACY-----GILKVPTGSWLCRTC 246
Cdd:cd15578     1 VCTVCQDGSSESPNEIVLCDKCGQGYHQLCHnpkidSSVLDPDVPWLCRQC 51
PHD_ATX1_2_like cd15494
PHD finger found in Arabidopsis thaliana histone-lysine N-methyltransferase arabidopsis ...
201-246 2.25e-07

PHD finger found in Arabidopsis thaliana histone-lysine N-methyltransferase arabidopsis trithorax-like protein ATX1, ATX2, and similar proteins; The family includes A. thaliana ATX1 and ATX2, both of which 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 termed 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. ATX1regulates 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 termed protein SET domain group 30, or trithorax-homolog protein 2 (TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). Both ATX1 and ATX2 are multi-domain containing proteins that consist of an N-terminal PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical Cys4HisCys3 plant homeodomain (PHD) finger, a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, and a C-terminal SET domain; this model corresponds to the Cys4HisCys3 canonical PHD finger.


Pssm-ID: 276969  Cd Length: 47  Bit Score: 47.83  E-value: 2.25e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2217355360 201 VCDVCRSPEGEDGNEMVFCDKCNVCVHQACYGILKVPTG-SWLCRTC 246
Cdd:cd15494     1 KCSVCGEDEEYEDNLLLQCDKCRMMVHMRCYGVLEPPPGaLWLCNLC 47
PHD_Phf1p_Phf2p_like cd15502
PHD finger found in Schizosaccharomyces pombe SWM histone demethylase complex subunits Phf1 ...
201-246 3.55e-07

PHD finger found in Schizosaccharomyces pombe SWM histone demethylase complex subunits Phf1 (Phf1p) and Phf2 (Phf2p); Phf1p and Phf2p are components of the SWM histone demethylase complex that specifically demethylates histone H3 at lysine 9 (H3K9me2), a specific tag for epigenetic transcriptional activation. They function as corepressors and play roles in regulating heterochromatin propagation and euchromatic transcription. Both Phf1p and Phf2p contain a plant homeodomain (PHD) finger.


Pssm-ID: 276977  Cd Length: 52  Bit Score: 47.43  E-value: 3.55e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217355360 201 VCDVCRSPEGEDGNEMVFCDKCNVCVHQACY------GILKVPTGSWLCRTC 246
Cdd:cd15502     1 VCIVCQRGHSPKSNRIVFCDGCNTPYHQLCHdpsiddEVVEDPDAEWFCKKC 52
PHD1_PHF14 cd15561
PHD finger 1 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...
201-246 5.75e-07

PHD finger 1 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 first PHD finger.


Pssm-ID: 277036  Cd Length: 56  Bit Score: 47.05  E-value: 5.75e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217355360 201 VCDVCRSPEGEDGNEMVFCDKCNVCVHQACYGILKVP----------TGSWLCRTC 246
Cdd:cd15561     1 ICCVCLGDRSNDADEIIECDKCGISVHEGCYGVIDESdssssassssTEPWFCEPC 56
ePHD_RAI1_like cd15668
Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 ...
273-364 8.72e-07

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: 48.07  E-value: 8.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 273 WVHVSCALWIPEVSIGCPekmepitKISHIPASRWALS---CSLCKEcTGTCIQCSMPSCVTAFHVTCAFDHGLEMrtil 349
Cdd:cd15668    24 WVHEDCAVWAPGVYLVGG-------KLYGLEEAVWVAKqsvCSSCQQ-TGATIGCLHKGCKAKYHYPCAVESGCQL---- 91
                          90
                  ....*....|....*
gi 2217355360 350 adnDEVKFKSFCQEH 364
Cdd:cd15668    92 ---DEENFSLLCPKH 103
ePHD2_KMT2C_like cd15666
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
254-338 1.54e-06

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: 47.30  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 254 CLLCpKRGGALKPTRSG-------TKWVHVSCALWIPEV---SIGCPEKMEpitkishiPASRWALS--CSLCKEcTGTC 321
Cdd:cd15666     1 CVLC-GGEGDGDTDGPGrllnldvDKWVHLNCALWSYEVyetQNGALMNVE--------EALRRALTttCSHCGR-TGAT 70
                          90
                  ....*....|....*..
gi 2217355360 322 IQCSMPSCVTAFHVTCA 338
Cdd:cd15666    71 VPCFKPRCANVYHLPCA 87
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
581-785 3.50e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 50.75  E-value: 3.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 581 RDPSLRPGDPARKARGRTRLPAKKKPPPPPPQDGPGSRTTPDKAPKKTWGQDAGsgkGGQGPPTRKPPRRTSSHLPSSPA 660
Cdd:PRK07764  634 AAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAP---AAPAAPAGAAPAQPAPAPAATPP 710
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 661 AgdcpilATPESPPPLAPETPDEAASVAADSDVQVPGPAASPKPLGRLRPPRESKVTRRLPGARPDAGMGPPSAVAERPk 740
Cdd:PRK07764  711 A------GQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEE- 783
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2217355360 741 vslhfdtetdgyfsdgEMSDSDVEAEDGGVQRGPREAGAEEVVRM 785
Cdd:PRK07764  784 ----------------EMAEDDAPSMDDEDRRDAEEVAMELLEEE 812
PHD2_Snt2p_like cd15498
PHD finger 2 found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and ...
201-246 4.25e-06

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.


Pssm-ID: 276973  Cd Length: 55  Bit Score: 44.39  E-value: 4.25e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217355360 201 VCDVCRSPEGEDGNEMVFCDKCNVCVHQACYGIlKVP----------TGSWLCRTC 246
Cdd:cd15498     1 KCSVCSEQFASNFNTSLSCYNCGLNVHASCYGI-TVPgkmnkvknlkSYKWLCDPC 55
PHD_BAZ2A_like cd15545
PHD finger found in bromodomain adjacent to zinc finger domain protein 2A (BAZ2A) and 2B ...
202-246 1.91e-05

PHD finger found in bromodomain adjacent to zinc finger domain protein 2A (BAZ2A) and 2B (BAZ2B); BAZ2A, also termed transcription termination factor I-interacting protein 5 (TTF-I-interacting protein 5, or Tip5), or WALp3, is an epigenetic regulator. It has been implicated in epigenetic rRNA gene silencing, as the large subunit of the SNF2h-containing chromatin-remodeling complex NoRC that induces nucleosome sliding in an ATP- and histone H4 tail-dependent fashion. BAZ2A has also been shown to be broadly overexpressed in prostate cancer, to regulate numerous protein-coding genes and to cooperate with EZH2 (enhancer of zeste homolog 2) to maintain epigenetic silencing at genes repressed in prostate cancer metastasis. Its overexpression is tightly associated with a prostate cancer subtype displaying CpG island methylator phenotype (CIMP) in tumors and with prostate cancer recurrence in patients. BAZ2B, also termed WALp4, is a bromodomain-containing protein whose biological role is still elusive. It shows high sequence similarly with BAZ2A. Both BAZ2A and BAZ2B contain a TAM (TIP5/ARBP/MBD) domain, a DDT domain, four AT-hooks, BAZ 1 and BAZ 2 motifs, a WAKZ (WSTF/Acf1/KIAA0314/ZK783.4) motif, a plant homeodomain (PHD) finger, and a bromodomain. BAZ2B also harbors an extra Apolipophorin-III like domain in its N-terminal region.


Pssm-ID: 277020 [Multi-domain]  Cd Length: 46  Bit Score: 42.30  E-value: 1.91e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2217355360 202 CDVCRSPEGEDgnEMVFCDKCNVCVHQACYG--ILKVPTGSWLCRTC 246
Cdd:cd15545     2 CQICRSGDNED--QLLLCDGCDRGYHTYCFKpkMTNVPEGDWFCPEC 46
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
634-741 2.73e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 47.56  E-value: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 634 GSGKGGQGPPTRKPPRRtsshlPSSPAAGDCPILATPesPPPLAPETPDEAASVAADSDVQVPGPAASPKPLGRLRPPRE 713
Cdd:PRK12323  366 GQSGGGAGPATAAAAPV-----AQPAPAAAAPAAAAP--APAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQ 438
                          90       100
                  ....*....|....*....|....*...
gi 2217355360 714 SKVTRRLPGARPDAGMGPPSAVAERPKV 741
Cdd:PRK12323  439 ASARGPGGAPAPAPAPAAAPAAAARPAA 466
ePHD_PHF6_like cd15673
Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11); ...
309-364 3.58e-05

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: 43.53  E-value: 3.58e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217355360 309 LSCSLCKeCTGTCIQCSMPSCVTAFHVTCAFDHGLEmrtILADNDEVKFKSFCQEH 364
Cdd:cd15673    65 LKCNLCK-KTGATIGCDVKQCKKTYHYHCAKKDDAK---IIERNSQGIYRVYCKNH 116
ePHD1_KMT2C_like cd15665
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
273-364 3.76e-05

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: 43.08  E-value: 3.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 273 WVHVSCALWIPEVSIGCPEKMEPITKISHIPASRwalSCSLCKEcTGTCIQCSMPSCVTAFHVTCAFDHG--LEMRTILA 350
Cdd:cd15665    10 YAHHCCAAWSEGVCQTEDGALENVDKAVAKALSQ---KCSFCLR-YGASISCRMPSCSKSFHFPCAAAAGcfQDIKTLTL 85
                          90
                  ....*....|....
gi 2217355360 351 dndevkfksFCQEH 364
Cdd:cd15665    86 ---------FCPEH 90
PHD_TAF3 cd15522
PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3); TAF3 (also termed ...
201-246 3.98e-05

PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3); TAF3 (also termed 140 kDa TATA box-binding protein-associated factor, TBP-associated factor 3, transcription initiation factor TFIID 140 kDa subunit (TAF140), or TAFII-140, is an integral component of TFIID) is a general initiation factor (GTF) that plays a key role in preinitiation complex (PIC) assembly through core promoter recognition. The interaction of H3K4me3 with TAF3 directs global TFIID recruitment to active genes, which regulates gene-selective functions of p53 in response to genotoxic stress. TAF3 is highly enriched in embryonic stem cells and is required for endoderm lineage differentiation and prevents premature specification of neuroectoderm and mesoderm. Moreover, TAF3, along with TRF3, forms a complex that is essential for myogenic differentiation. TAF3 contains a plant homeodomain (PHD) finger. This family also includes Drosophila melanogaster BIP2 (Bric-a-brac interacting protein 2) protein, which functions as an interacting partner of D. melanogaster p53 (Dmp53).


Pssm-ID: 276997 [Multi-domain]  Cd Length: 46  Bit Score: 41.50  E-value: 3.98e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217355360 201 VCDVCRSPEgeDGNEMVFCDKCNVCVHQACYGILKVP--TGSWLCRTC 246
Cdd:cd15522     1 ICPICKKPD--DGSPMIGCDECDDWYHWECVGITDEPpeEDDWFCPKC 46
PHD_BAZ1A_like cd15544
PHD finger found in bromodomain adjacent to zinc finger domain protein BAZ1A and BAZ1B; BAZ1A, ...
202-246 5.46e-05

PHD finger found in bromodomain adjacent to zinc finger domain protein BAZ1A and BAZ1B; 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. BAZ1B, also termed Tyrosine-protein kinase BAZ1B, or Williams syndrome transcription factor (WSTF), or Williams-Beuren syndrome chromosomal region 10 protein, Williams-Beuren syndrome chromosomal region 9 protein, or WALp2, is a multifunctional protein implicated in several nuclear processes, including replication, transcription, and the DNA damage response. BAZ1B/WSTF, together with the imitation switch (ISWI) ATPase, forms a WSTF-ISWI chromatin remodeling complex (WICH), which transiently associates with the human inactive X chromosome (Xi) during late S-phase prior to BRCA1 and gamma-H2AX. Moreover, BAZ1B/WSTF, SNF2h, and nuclear myosin 1 (NM1) forms the chromatin remodeling complex B-WICH that is involved in regulating rDNA transcription. Both BAZ1A and BAZ1B contain 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.


Pssm-ID: 277019  Cd Length: 46  Bit Score: 41.24  E-value: 5.46e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2217355360 202 CDVCRspEGEDGNEMVFCDKCNVCVHQACY--GILKVPTGSWLCRTC 246
Cdd:cd15544     2 CKVCR--KKGDPDNMILCDGCDKAFHLYCLrpALREVPSGDWFCPAC 46
PHD2_KMT2C cd15594
PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...
201-246 5.71e-05

PHD finger 2 found in Histone-lysine N-methyltransferase 2C (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 plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, 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. This model corresponds to the second PHD finger.


Pssm-ID: 277069  Cd Length: 46  Bit Score: 41.08  E-value: 5.71e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217355360 201 VCDVCRSPeGEDgNEMVFCDKCNVCVHQACYG--ILKVPTGSWLCRTC 246
Cdd:cd15594     1 VCQTCRQP-GDD-NKMLVCDTCDKGYHTFCLQpvMTTIPKNGWKCKNC 46
PHD2_KMT2D cd15595
PHD finger 2 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...
201-246 1.50e-04

PHD finger 2 found in Histone-lysine N-methyltransferase 2D (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 asHOXA1-3 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 plant homeodomain (PHD) fingers, two 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 second PHD finger.


Pssm-ID: 277070  Cd Length: 46  Bit Score: 39.98  E-value: 1.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217355360 201 VCDVCRSPeGEDgNEMVFCDKCNVCVHQACY--GILKVPTGSWLCRTC 246
Cdd:cd15595     1 VCQTCRKP-GED-SKMLVCEACDKGYHTFCLkpAMESLPTDSWKCKAC 46
PHD_BAZ1A cd15627
PHD finger found in bromodomain adjacent to zinc finger domain protein 1A (BAZ1A); BAZ1A, also ...
202-246 1.82e-04

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.


Pssm-ID: 277097 [Multi-domain]  Cd Length: 46  Bit Score: 39.68  E-value: 1.82e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2217355360 202 CDVCRspEGEDGNEMVFCDKCNVCVHQACY--GILKVPTGSWLCRTC 246
Cdd:cd15627     2 CRICR--RKGDAEKMLLCDGCDRGHHMYCLrpPLKKVPEGDWFCPDC 46
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
588-785 2.07e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 588 GDPARKARGRTRLPAKKKPPPPPPQDGPGSRTTPDKAPKKTWGQDAGSGKGGQGPPTRKPPRRTSSHLPS-SPAAGDCPI 666
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVpDASDGGDGW 669
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 667 LATPESPPPLAPETPDEAASVAADSDvqVPGPAASPKPLGRLRPPRESKVTRRLPGARPDAGMGPPSAVAERPKVSLHFD 746
Cdd:PRK07764  670 PAKAGGAAPAAPPPAPAPAAPAAPAG--AAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDD 747
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2217355360 747 TETDGYFSDGEMSDSDVEAEDGGVQRGPREAGAEEVVRM 785
Cdd:PRK07764  748 PPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMA 786
PHD1_AIRE cd15539
PHD finger 1 found in autoimmune regulator (AIRE); AIRE, also termed autoimmune ...
202-246 2.14e-04

PHD finger 1 found in autoimmune regulator (AIRE); AIRE, also termed autoimmune polyendocrinopathy candidiasis ectodermal dystrophy (APECED) protein, functions as a regulator of gene transcription in the thymus. It is essential for prevention of autoimmunity. AIRE plays a critical role in the induction of central tolerance. It promotes self-tolerance through tissue-specific antigen (TSA) expression. It also acts as an active regulator of chondrocyte differentiation. AIRE contains a homogeneously-staining region (HSR) or caspase-recruitment domain (CARD), a nuclear localization signal (NLS), a SAND (for Sp100, AIRE, nuclear phosphoprotein 41/75 or NucP41/75, and deformed epidermal auto regulatory factor 1 or Deaf1) domain, two plant homeodomain (PHD) fingers, and four LXXLL (where L stands for leucine) motifs. This model corresponds to the first PHD finger that recognizes the unmethylated tail of histone H3 and targets AIRE-dependent genes.


Pssm-ID: 277014 [Multi-domain]  Cd Length: 43  Bit Score: 39.36  E-value: 2.14e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2217355360 202 CDVCRspegeDGNEMVFCDKCNVCVHQACYG--ILKVPTGSWLCRTC 246
Cdd:cd15539     2 CAVCG-----DGGELLCCDGCPRAFHLACLVppLTLIPSGTWRCSSC 43
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
582-766 2.98e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 2.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360  582 DPSLRPGDPARKARGRTRLPAKKKPPPPPPQDGPGSRTTPDKAPKKTWGQDAGSGKGGQGPPTRKPPRRTSSHLPSSPAA 661
Cdd:PHA03307    70 GPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPA 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360  662 GDCPILATPESPPPLAPETPDEAASVAA--DSDVQVPGPAASPKPLGRLRPPRESKVTRRLPGARPDAgMGPPSAVAERP 739
Cdd:PHA03307   150 ASPPAAGASPAAVASDAASSRQAALPLSspEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASA-SSPAPAPGRSA 228
                          170       180
                   ....*....|....*....|....*..
gi 2217355360  740 KVSLHFDTEtDGYFSDGEMSDSDVEAE 766
Cdd:PHA03307   229 ADDAGASSS-DSSSSESSGCGWGPENE 254
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
583-723 3.01e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 44.46  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 583 PSLRPGDPARKARGRTRLPAKKKPPPPPPQDGPGSRTTPDKAPKKTWGQDAGSGKGGQGPPTRKPPrrtSSHLPSSPAAG 662
Cdd:PRK07003  406 AGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPP---ADSGSASAPAS 482
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217355360 663 DCPILATPESPPPLAPETP------DEAASVAADSDVQVPGPAASPKPLGRLRPPRESKVTRRLPGA 723
Cdd:PRK07003  483 DAPPDAAFEPAPRAAAPSAatpaavPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARAGGA 549
PHA03247 PHA03247
large tegument protein UL36; Provisional
587-740 4.54e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 4.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360  587 PGDPARKARGRTRLPAKKKPPPPPPQDGPGSRTT-PDKAPKKTWGQDAGSGKGGQGPPTRKPPRRTSSHLPSSPAAGDCP 665
Cdd:PHA03247  2751 PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTrPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP 2830
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360  666 ILATPESPPPLAPETPDEA----ASVAADSDVQVPGPAASP--KPLGRLRPPreskvTRRLPG---ARPDAGMGPPSAVA 736
Cdd:PHA03247  2831 PTSAQPTAPPPPPGPPPPSlplgGSVAPGGDVRRRPPSRSPaaKPAAPARPP-----VRRLARpavSRSTESFALPPDQP 2905

                   ....
gi 2217355360  737 ERPK 740
Cdd:PHA03247  2906 ERPP 2909
ePHD_PHF7_G2E3_like cd15669
Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ...
309-364 5.91e-04

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: 39.93  E-value: 5.91e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217355360 309 LSCSLCKEcTGTCIQCSMPSCVTAFHVTCAFDHGleMRTILADNdevkFKSFCQEH 364
Cdd:cd15669    64 LRCFYCKK-KGASIGCAVKGCRRSFHFPCGLENG--CVTQFFGE----YRSFCWEH 112
PHD_MMD1_like cd15556
PHD finger found in Arabidopsis thaliana PHD finger protein MALE MEIOCYTE DEATH 1 (MMD1), PHD ...
211-246 6.34e-04

PHD finger found in Arabidopsis thaliana PHD finger protein MALE MEIOCYTE DEATH 1 (MMD1), PHD finger protein MALE STERILITY 1 (MS1), and similar proteins; MMD1 is a plant homeodomain (PHD) finger protein expressed in male meiocytes. It is encoded by the gene DUET, which is required for male meiotic chromosome organization and progression. MMD1 has been implicated in the regulation of gene expression during meiosis. The mmd1 mutation triggers cell death in male meiocytes. MS1 is a nuclear transcriptional activator that is important for tapetal development and pollen wall biosynthesis. It contains a Leu zipper-like domain and a PHD finger motif, both of which are essential for its function.


Pssm-ID: 277031 [Multi-domain]  Cd Length: 46  Bit Score: 38.13  E-value: 6.34e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2217355360 211 EDGNEMVFCDKCNVCVHQACYGI--LKVPTGSWLCRTC 246
Cdd:cd15556     9 DDGERMIACDVCEVWQHTRCVGIadNEEPPDHFLCRRC 46
PHA03247 PHA03247
large tegument protein UL36; Provisional
582-742 6.54e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 6.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360  582 DPSLRPGDPARKARGRTRLPAKKKPPPPPPQD----GPGSRTTPDKAPKKTWGQDAGSGKGGQGPPTRKPPRRTSSHLPS 657
Cdd:PHA03247  2621 THAPDPPPPSPSPAANEPDPHPPPTVPPPERPrddpAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLAD 2700
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360  658 SPAAGDCP----ILATPESPPPLAPETPDEAASVAADSDVQVPGPAASPKPLGRLRPPRESKVTRRLPGARPDAGMGPPS 733
Cdd:PHA03247  2701 PPPPPPTPepapHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPP 2780

                   ....*....
gi 2217355360  734 AVAERPKVS 742
Cdd:PHA03247  2781 RRLTRPAVA 2789
PHD1_PHF1 cd15500
PHD finger 1 found in PHD finger protein1 (PHF1); PHF1, also termed polycomb-like protein 1 ...
201-246 6.54e-04

PHD finger 1 found in PHD finger protein1 (PHF1); PHF1, also termed polycomb-like protein 1 (PCL1), together with JARID2 and AEBP2, associates with the polycomb repressive complex 2 (PRC2), which is the major H3K27 methyltransferase that regulates pluripotency, differentiation, and tumorigenesis through catalysis of histone H3 lysine 27 trimethylation (H3K27me3) on chromatin. PHF1 is essential in epigenetic regulation and genome maintenance. It acts as a dual reader of Lysine trimethylation at Lysine 36 of Histone H3 and Lysine 27 of Histone variant H3t. PHF1 consists of an N-terminal Tudor domain followed by two PHD fingers, and a C-terminal MTF2 domain. Its Tudor domain selectively binds to histone H3K36me3. Moreover, PHF1 is required for efficient H3K27me3 and Hox gene silencing. It can mediate deposition of the repressive H3K27me3 mark and acts as a cofactor in early DNA-damage response. This model corresponds to the first PHD finger.


Pssm-ID: 276975  Cd Length: 51  Bit Score: 38.27  E-value: 6.54e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217355360 201 VCDVCRSPEGEDGNEMVFCDKCNVCVHQACYgilkVPT---------GSWLCRTC 246
Cdd:cd15500     1 ICCVCDSETVSPKNPLVNCEKCHHAYHQECH----VPRvplesagdgDSWMCRQC 51
PHD_JMJD2 cd15493
PHD finger found in Jumonji domain-containing protein 2 (JMJD2) family of histone demethylases; ...
219-246 7.65e-04

PHD finger found in Jumonji domain-containing protein 2 (JMJD2) family of histone demethylases; JMJD2 proteins, also termed lysine-specific demethylase 4 histone demethylases (KDM4), have been implicated in various cellular processes including DNA damage response, transcription, cell cycle regulation, cellular differentiation, senescence, and carcinogenesis. They selectively catalyze the demethylation of di- and trimethylated H3K9 and H3K36. This model contains only three JMJD2 proteins, JMJD2A-C, which all contain jmjN and jmjC domains in the N-terminal region, followed by a Cys4HisCys3 canonical PHD finger, a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, and a Tudor domain. JMJD2D is not included in this family, since it lacks both PHD and Tudor domains and has a different substrate specificity. JMJD2A-C are required for efficient cancer cell growth. This model corresponds to the Cys4HisCys3 canonical PHD finger.


Pssm-ID: 276968  Cd Length: 42  Bit Score: 37.68  E-value: 7.65e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2217355360 219 CDKCNVCVHQACYGILKVP--TGSWLCRTC 246
Cdd:cd15493    13 CSRCCVCVHASCYGVPDIPgdGEGWKCDRC 42
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
612-720 9.09e-04

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 42.68  E-value: 9.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 612 QDGPGSRTTPDKAPKKTwgqdAGSGKGGQGPPTRKPPRRTSSHLPSSPAAGDCPiLATPESPPPLAPETPD-EAASVAAD 690
Cdd:NF041121   14 QMGRAAAPPSPEGPAPT----AASQPATPPPPAAPPSPPGDPPEPPAPEPAPLP-APYPGSLAPPPPPPPGpAGAAPGAA 88
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2217355360 691 SDVQVPGPAASPKP--LGR-LRP---PRESKVTRRL 720
Cdd:NF041121   89 LPVRVPAPPALPNPleLARaLRPlkrRVPSPRRVEL 124
PHD_JMJD2A cd15575
PHD finger found in Jumonji domain-containing protein 2A (JMJD2A); JMJD2A, also termed ...
211-246 9.79e-04

PHD finger found in Jumonji domain-containing protein 2A (JMJD2A); JMJD2A, also termed lysine-specific demethylase 4A (KDM4A), or JmjC domain-containing histone demethylation protein 3A (JHDM3A), catalyzes the demethylation of di- and trimethylated H3K9 and H3K36. It is involved in carcinogenesis and functions as a transcription regulator that may either stimulate or repress gene transcription. It associates with nuclear receptor co-repressor complex or histone deacetylases. Moreover, JMJD2A forms complexes with both the androgen and estrogen receptor (ER) and plays an essential role in growth of both ER-positive and -negative breast tumors. It is also involved in prostate, colon, and lung cancer progression. JMJD2A contains jmjN and jmjC domains in the N-terminal region, followed by a canonical Cys4HisCys3 PHD finger, a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, and a Tudor domain. This model corresponds to the canonical Cys4HisCys3 PHD finger.


Pssm-ID: 277050  Cd Length: 100  Bit Score: 39.12  E-value: 9.79e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2217355360 211 EDGNE-MVFCDKCNVCVHQACYGILKVP-TGSWLCRTC 246
Cdd:cd15575    63 EDGTSiLVTCKKCCVCVHASCYGVSPEKaAEDWMCSRC 100
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
584-725 1.01e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360  584 SLRPGDPARKARGRTRLPAKKKPPPPPPQDGPGSRTTPDKAPkktwGQDAGSGKGGQGPPTrkPPRRTSSHLPSSPAAGD 663
Cdd:PHA03307   253 NECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRER----SPSPSPSSPGSGPAP--SSPRASSSSSSSRESSS 326
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217355360  664 CPILATPESPPPLAPETPDEAASVAADSDvqvPGPAASPKPLGRLRPPRESKVTRRLPGARP 725
Cdd:PHA03307   327 SSTSSSSESSRGAAVSPGPSPSRSPSPSR---PPPPADPSSPRKRPRPSRAPSSPAASAGRP 385
PHD_BAZ1B cd15628
PHD finger found in bromodomain adjacent to zinc finger domain protein 1B (BAZ1B); BAZ1B, also ...
202-246 1.10e-03

PHD finger found in bromodomain adjacent to zinc finger domain protein 1B (BAZ1B); BAZ1B, also termed Tyrosine-protein kinase BAZ1B, or Williams syndrome transcription factor (WSTF), or Williams-Beuren syndrome chromosomal region 10 protein, Williams-Beuren syndrome chromosomal region 9 protein, or WALp2, is a multifunctional protein implicated in several nuclear processes, including replication, transcription, and the DNA damage response. BAZ1B/WSTF, together with the imitation switch (ISWI) ATPase, forms a WSTF-ISWI chromatin remodeling complex (WICH), which transiently associates with the human inactive X chromosome (Xi) during late S-phase prior to BRCA1 and gamma-H2AX. Moreover, BAZ1B/WSTF, SNF2h, and nuclear myosin 1 (NM1) forms the chromatin remodeling complex B-WICH that is involved in regulating rDNA transcription. BAZ1B 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.


Pssm-ID: 277098  Cd Length: 46  Bit Score: 37.42  E-value: 1.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2217355360 202 CDVCRSpEGEDgNEMVFCDKCNVCVHQACY--GILKVPTGSWLCRTC 246
Cdd:cd15628     2 CKVCRK-KGED-DKLILCDECNQAFHLFCLrpALYEVPDGEWMCPAC 46
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
586-734 1.48e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.17  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 586 RPGDPARKARGRTRLPAKKKPPPPPPQDGPGSRTTPDKAPKKTWGQDAGSGKGGQGPPTRKPPrrtsshlpSSPAAGDCP 665
Cdd:PRK12323  393 AAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPA--------AAPAAAARP 464
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217355360 666 ILATPESPPPLAPETPDEAAsvaadsdvqvpgPAASPKPLGRLRPPRESkvtrrLPGARPDAGMGPPSA 734
Cdd:PRK12323  465 AAAGPRPVAAAAAAAPARAA------------PAAAPAPADDDPPPWEE-----LPPEFASPAPAQPDA 516
PHD5_NSD cd15568
PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
201-244 1.57e-03

PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein is a family of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1, that are critical in maintaining chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play non-redundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). This model corresponds to the fifth PHD finger.


Pssm-ID: 277043 [Multi-domain]  Cd Length: 43  Bit Score: 36.92  E-value: 1.57e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2217355360 201 VCDVCRspegeDGNEMVFCDK--CNVCVHQACYGILKVPTGSWLCR 244
Cdd:cd15568     1 ECFRCG-----DGGDLVLCDFkgCPKVYHLSCLGLEKPPGGKWICP 41
PHD_BAZ2A cd15629
PHD finger found in bromodomain adjacent to zinc finger domain protein 2A (BAZ2A); BAZ2A, also ...
202-246 1.60e-03

PHD finger found in bromodomain adjacent to zinc finger domain protein 2A (BAZ2A); BAZ2A, also termed transcription termination factor I-interacting protein 5 (TTF-I-interacting protein 5, or Tip5), or WALp3, is an epigenetic regulator. It has been implicated in epigenetic rRNA gene silencing, as the large subunit of the SNF2h-containing chromatin-remodeling complex NoRC that induces nucleosome sliding in an ATP- and histone H4 tail-dependent fashion. BAZ2A has also been shown to be broadly overexpressed in prostate cancer, to regulate numerous protein-coding genes and to cooperate with EZH2 (enhancer of zeste homolog 2) to maintain epigenetic silencing at genes repressed in prostate cancer metastasis. Its overexpression is tightly associated with a prostate cancer subtype displaying CpG island methylator phenotype (CIMP) in tumors and with prostate cancer recurrence in patients. It contains a TAM (TIP5/ARBP/MBD) domain, a DDT domain, four AT-hooks, BAZ 1 and BAZ 2 motifs, a WAKZ (WSTF/Acf1/KIAA0314/ZK783.4) motif, a plant homeodomain (PHD) finger, and a bromodomain.


Pssm-ID: 277099  Cd Length: 47  Bit Score: 37.14  E-value: 1.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2217355360 202 CDVCRspEGEDGNEMVFCDKCNVCVHQACY--GILKVPTGSWLCRTC 246
Cdd:cd15629     2 CLVCR--KGDNDEYLLLCDGCDRGCHMYCHrpKMLQVPEGDWFCPNC 46
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
558-734 2.21e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 2.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360  558 EDPAPGLLSEELLQDEETLlSFMRDPSLRPGDPARKARGRTRLPAKKKPPPPPPQ-DGPGSRTTPDKAPKKTWGQDAGSG 636
Cdd:PHA03307    69 TGPPPGPGTEAPANESRST-PTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPpASPPPSPAPDLSEMLRPVGSPGPP 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360  637 KGGQGPPTRKPPRRTSSHLPSSPAAGDcPILATPE------SP----PPLAPETPDEAASVAADSDVQVPGPAASPKPLG 706
Cdd:PHA03307   148 PAASPPAAGASPAAVASDAASSRQAAL-PLSSPEEtarapsSPpaepPPSTPPAAASPRPPRRSSPISASASSPAPAPGR 226
                          170       180
                   ....*....|....*....|....*...
gi 2217355360  707 RLRPPRESKVTRRLPGARPDAGMGPPSA 734
Cdd:PHA03307   227 SAADDAGASSSDSSSSESSGCGWGPENE 254
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
581-739 2.33e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360  581 RDPSLRPGDPARKARGRTRLPAKKKPPPPPPQDG----PGSRTTPDKAPKKTWGQDAGSGKGGQGPPTRKPPRRTSSHLP 656
Cdd:PHA03307   218 SSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPenecPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPS 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360  657 SSPAAGDCPilATPESPPPLAPETPDEAASVAADSDVQVP------GPAASPKPLGRLRPPRESKVTRRLP-GARPDAGM 729
Cdd:PHA03307   298 PSPSSPGSG--PAPSSPRASSSSSSSRESSSSSTSSSSESsrgaavSPGPSPSRSPSPSRPPPPADPSSPRkRPRPSRAP 375
                          170
                   ....*....|
gi 2217355360  730 GPPSAVAERP 739
Cdd:PHA03307   376 SSPAASAGRP 385
ePHD_RAI1 cd15700
Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant ...
273-342 3.23e-03

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: 37.93  E-value: 3.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 273 WVHVSCALWIPEVSIgCPEKMEPITKISHIPAsrwALSCSLCKEcTGTCIQCSMPSCVTAFHVTCAFDHG 342
Cdd:cd15700    25 WVHEACAVWTTGVYL-VAGKLFGLQEAVQKAA---DAKCSSCQG-AGATVGCCHKGCTQSYHYICAVEAG 89
PHA03247 PHA03247
large tegument protein UL36; Provisional
584-733 3.61e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 3.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360  584 SLRPGDPARKaRGRTRLPAKKKPPPPPpqdgPGSRTTPDKAPKKTWGQDAGSGKGGQGPPTRKPPRRTSSHLPSSPAAGD 663
Cdd:PHA03247  2855 SVAPGGDVRR-RPPSRSPAAKPAAPAR----PPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQP 2929
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360  664 CPILATPESPPPLAPETPDEAAsvaadsdVQVPGPAASPKPLGRLRPPRESKVTRRLPGARPDAGMGPPS 733
Cdd:PHA03247  2930 QPPPPPPPRPQPPLAPTTDPAG-------AGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASS 2992
PHD_RSF1 cd15543
PHD finger found in Remodeling and spacing factor 1 (Rsf-1); Rsf-1, also termed HBV ...
202-246 3.91e-03

PHD finger found in Remodeling and spacing factor 1 (Rsf-1); Rsf-1, also termed HBV pX-associated protein 8, or Hepatitis B virus X-associated protein alpha (HBxAPalpha), or p325 subunit of RSF chromatin-remodeling complex, is a novel nuclear protein with histone chaperon function. It is a subunit of an ISWI chromatin remodeling complex, remodeling and spacing factor (RSF), and plays a role in mediating ATPase-dependent chromatin remodeling and conferring tumor aggressiveness in common carcinomas. As an ataxia-telangiectasia mutated (ATM)-dependent chromatin remodeler, Rsf-1 facilitates DNA damage checkpoints and homologous recombination repair. It regulates the mitotic spindle checkpoint and chromosome instability through the association with serine/threonine kinase BubR1 (BubR1) and Hepatitis B virus (HBV) X protein (HBx) in the chromatin fraction during mitosis. It also interacts with cyclin E1 and promotes tumor development. Rsf-1 contains a plant homeodomain (PHD) finger.


Pssm-ID: 277018 [Multi-domain]  Cd Length: 46  Bit Score: 35.71  E-value: 3.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217355360 202 CDVCRSpeGEDGNEMVFCDKCNVCVHQACygiLK-----VPTGSWLCRTC 246
Cdd:cd15543     2 CRKCGL--SDHPEWILLCDRCDAGYHTAC---LRpplmiIPDGNWFCPPC 46
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
539-728 4.14e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 4.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360  539 QITAENMAMSEWPLNNGHREDPAPGLLSEELLQDEEtllSFMRDPSLRPGDPARKARGRTrlpAKKKPPPPPPQDGPGSR 618
Cdd:PHA03307   759 SNPSLVPAKLAEALALLEPAEPQRGAGSSPPVRAEA---AFRRPGRLRRSGPAADAASRT---ASKRKSRSHTPDGGSES 832
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360  619 TTPDKAPkktwgqdagsGKGGQGPPTRKPPRRTSSHLPSSPAAGDCPILATPESPPPLAPETPDEAASVAAdsdvqVPGP 698
Cdd:PHA03307   833 SGPARPP----------GAAARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAA-----AAPP 897
                          170       180       190
                   ....*....|....*....|....*....|
gi 2217355360  699 AASPKPLGRLRPPResKVTRRLPGARPDAG 728
Cdd:PHA03307   898 AGAPAPRPRPAPRV--KLGPMPPGGPDPRG 925
PHD1_PHF19 cd15579
PHD finger 1 found in PHD finger protein 19 (PHF19); PHF19, also termed Polycomb-like protein ...
202-246 4.20e-03

PHD finger 1 found in PHD finger protein 19 (PHF19); PHF19, also termed Polycomb-like protein 3 (PCL3), is a component of the polycomb repressive complex 2 (PRC2), which is the major H3K27 methyltransferase that regulates pluripotency, differentiation, and tumorigenesis through catalysis of histone H3 lysine 27 trimethylation (H3K27me3) on chromatin. PHF19 consists of an N-terminal Tudor domain followed by two PHD fingers, and a C-terminal MTF2 domain. It binds trimethylated histone H3 Lys36 (H3K36me3) through its Tudor domain and recruits the PRC2 complex and the H3K36me3 demethylase NO66 to embryonic stem cell genes during differentiation. Moreover, PHF19 and its upstream regulator, Akt, play roles in the phenotype switch of melanoma cells from proliferative to invasive states. This model corresponds to the first PHD finger.


Pssm-ID: 277054  Cd Length: 53  Bit Score: 36.01  E-value: 4.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217355360 202 CDVCRSPEGEDGNEMVFCDKCNVCVHQACYgILKVPTGS------WLCRTC 246
Cdd:cd15579     2 CNVCLGKSSGPLNEILICGKCGLGYHQQCH-IPVVDSSDdppltpWFCRRC 51
PHD5_KMT2C_like cd15513
PHD finger 5 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 4 found in ...
201-247 4.44e-03

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.


Pssm-ID: 276988  Cd Length: 47  Bit Score: 35.91  E-value: 4.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2217355360 201 VCDVCRSPEgeDGNEMVFCDKCNVCVHQACYG--ILKVPTGSWLCRTCA 247
Cdd:cd15513     1 VCEGCGKAS--DESRLLLCDDCDISYHTYCLDppLQTVPKGGWKCKWCV 47
PHD2_KAT6A_6B cd15527
PHD finger 2 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ, ...
202-246 5.49e-03

PHD finger 2 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ, also termed histone acetyltransferase KAT6A, YBF2/SAS3, SAS2 and TIP60 protein 3 (MYST-3), or runt-related transcription factor-binding protein 2, or zinc finger protein 220, is a MYST-type histone acetyltransferase (HAT) that functions as a coactivator for acute myeloid leukemia 1 protein (AML1)- and p53-dependent transcription. It possesses intrinsic HAT activity to acetylate both itself and lysine (K) residues on histone H2B, histone H3 (K14) and histone H4 (K5, K8, K12 and K16) in vitro and H3K9 in vivo. MOZ-related factor (MORF), also termed MOZ2, or histone acetyltransferase KAT6B, or MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4 (MYST4), is a ubiquitously expressed transcriptional regulator with intrinsic HAT activity. It can interact with the Runt-domain transcription factor Runx2 and form a tetrameric complex with BRPFs, ING5, and EAF6. Both MOZ and MORF are catalytic subunits of HAT complexes that are required for normal developmental programs, such as hematopoiesis, neurogenesis, and skeletogenesis, and are also implicated in human leukemias. MOZ is also the catalytic subunit of a tetrameric inhibitor of growth 5 (ING5) complex, which specifically acetylates nucleosomal histone H3K14. Moreover, MOZ and MORF are involved in regulating transcriptional activation mediated by Runx2 (or Cbfa1), a Runt-domain transcription factor known to play important roles in T cell lymphomagenesis and bone development, and its homologs. MOZ contains a linker histone 1 and histone 5 domains and two plant homeodomain (PHD) fingers. In contrast, MORF contains an N-terminal region containing two PHD fingers, a putative HAT domain, an acidic region, and a C-terminal Ser/Met-rich domain. The family corresponds to the first PHD finger.


Pssm-ID: 277002  Cd Length: 46  Bit Score: 35.43  E-value: 5.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2217355360 202 CDVCRspEGEDGNEMVFCDKCNVCVHQACYG--ILKVPTGSWLCRTC 246
Cdd:cd15527     2 CSVCQ--DSGNADNLLFCDACDKGFHMECHDppLTRMPKGKWVCQIC 46
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
581-742 5.89e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.22  E-value: 5.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 581 RDPSLRPGDPARKARGRTRLPAKKKPPPPPPQDGPGS-RTTPDKAPKKTWGQDAGSGKGGQGPPTRKPPRRTSSHLPSSP 659
Cdd:PRK07003  418 AAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANaRASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAA 497
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 660 AAGDCPILATPESPPPLAPETPDEAASVAA-DSDVQVPGPAASPKP---------LGRLRPP--RESKVTRRLPGARPDA 727
Cdd:PRK07003  498 APSAATPAAVPDARAPAAASREDAPAAAAPpAPEARPPTPAAAAPAaraggaaaaLDVLRNAgmRVSSDRGARAAAAAKP 577
                         170
                  ....*....|....*...
gi 2217355360 728 GMGPPSA---VAERPKVS 742
Cdd:PRK07003  578 AAAPAAApkpAAPRVAVQ 595
PHD4_NSD cd15567
PHD finger 4 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
212-246 6.39e-03

PHD finger 4 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein is a family of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1, that are critical in maintaining chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play non-redundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). This model corresponds to the fourth PHD finger.


Pssm-ID: 277042 [Multi-domain]  Cd Length: 41  Bit Score: 35.30  E-value: 6.39e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2217355360 212 DGNEMVFCDKCNVCVHQACYGILKVPTGSWLCRTC 246
Cdd:cd15567     7 EGGSLICCESCPASFHPECLGLEPPPEGKFYCEDC 41
PHD5_NSD2 cd15660
PHD finger 5 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed ...
212-243 7.04e-03

PHD finger 5 found in nuclear SET domain-containing protein 2 (NSD2); NSD2, also termed histone-lysine N-methyltransferase NSD2, or multiple myeloma SET domain-containing protein (MMSET), or protein trithorax-5 Wolf-Hirschhorn syndrome candidate 1 protein (WHSC1), is overexpressed frequently in the t(4;14) translocation in 15% to 20% of multiple myeloma. It plays important roles in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. It also enhances androgen receptor (AR)-mediated transcription. The principal chromatin-regulatory activity of NSD2 is dimethylation of histone H3 at lysine 36 (H3K36me2). NSD2 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, a high mobility group (HMG) box, five PHD (plant-homeodomain) zinc fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD fingers mediate chromatin interaction and recognition of histone marks. This model corresponds to the fifth PHD finger.


Pssm-ID: 277130  Cd Length: 43  Bit Score: 35.30  E-value: 7.04e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2217355360 212 DGNEMVFCDK--CNVCVHQACYGILKVPTGSWLC 243
Cdd:cd15660     7 DGGQLVLCDRksCTKAYHLSCLGLTKRPFGKWEC 40
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
311-364 7.31e-03

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.


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 35.27  E-value: 7.31e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217355360  311 CSLCKEC--TGTCIQCSMpsCVTAFHVTCAFDHGLEmrtiladnDEVKFKSFCQEH 364
Cdd:smart00249   2 CSVCGKPddGGELLQCDG--CDRWYHQTCLGPPLLE--------EEPDGKWYCPKC 47
PHD_TIF1delta cd15625
PHD finger found in transcriptional intermediary factor 1 delta (TIF1delta); TIF1delta, also ...
202-246 7.47e-03

PHD finger found in transcriptional intermediary factor 1 delta (TIF1delta); TIF1delta, also termed tripartite motif-containing protein 66 (TRIM66), is a novel heterochromatin protein 1 (HP1)-interacting member of the transcriptional intermediary factor1 (TIF1) family expressed by elongating spermatids. Like other TIF1 proteins, TIF1delta displays a potent trichostatin A (TSA)-sensitive repression function; TSA is a specific inhibitor of histone deacetylases. Moreover, TIF1delta plays an important role in heterochromatin-mediated gene silencing during postmeiotic phases of spermatogenesis. It functions as a negative regulator of postmeiotic genes acting through HP1 isotype gamma (HP1gamma) complex formation and centromere association. TIF1delta contains an N-terminal RBCC (RING finger, B-box zinc-fingers, coiled-coil), a plant homeodomain (PHD) finger, followed by a bromodomain in the C-terminal region.


Pssm-ID: 277095 [Multi-domain]  Cd Length: 49  Bit Score: 35.32  E-value: 7.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2217355360 202 CDVCRspegeDGNEMVFCDKCNVCVHQACY--GILKVPTGSWLCRTC 246
Cdd:cd15625     5 CAVCL-----NGGELLCCDRCPKVFHLSCHvpALLSFPVGEWVCTLC 46
PHD_PRHA_like cd15504
PHD finger found in Arabidopsis thaliana pathogenesis-related homeodomain protein (PRHA) and ...
201-246 8.26e-03

PHD finger found in Arabidopsis thaliana pathogenesis-related homeodomain protein (PRHA) and similar proteins; PRHA is a homeodomain protein encoded by a single-copy Arabidopsis thaliana homeobox gene, prha. It shows the capacity to bind to TAATTG core sequence elements but requires additional adjacent bases for high-affinity binding. PRHA contains a plant homeodomain (PHD) finger, a homeodomain, peptide repeats and a putative leucine zipper dimerization domain.


Pssm-ID: 276979  Cd Length: 53  Bit Score: 35.10  E-value: 8.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217355360 201 VCDVCRSPEGEDGNEMVFCD-KCNVCVHQAC------YGILKVPTGSWLCRTC 246
Cdd:cd15504     1 FCAKCQSGEASPDNDILLCDgGCNRAYHQKCleppllTEDIPPEDEGWLCPLC 53
EPL1 pfam10513
Enhancer of polycomb-like; This is a family of EPL1 (Enhancer of polycomb-like) proteins. The ...
10-175 9.76e-03

Enhancer of polycomb-like; This is a family of EPL1 (Enhancer of polycomb-like) proteins. The EPL1 protein is a member of a histone acetyltransferase complex which is involved in transcriptional activation of selected genes.


Pssm-ID: 463128  Cd Length: 168  Bit Score: 37.85  E-value: 9.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360  10 ISSDNSDTTDSHATSTSASRCSKLPSSTKSGWPRQNEKKPSEVFRTDLITAMKIPDSYQLSPDDyyiladpwrqEWEKGV 89
Cdd:pfam10513  14 ISEDEVDGLDTSPDEDEPSECNSNKENSLHAVETGVDKEEEDEVHLKVINAAKKALSSSKKSQN----------TSESSV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360  90 QVPAGAEA-IPEPVVRILPPLEGPPA---QASpsstmlgEGSQPDWPGGSRYDLDEIDAYWLELINSELKEMERPELDEL 165
Cdd:pfam10513  84 PAPNKERLyLPTPDAGKFREFERPPAsyiRFS-------ETVEEELDEGVEYDMDEEDEAWLEELNEKRKSEGVEKISED 156
                         170
                  ....*....|
gi 2217355360 166 TLERVLEELE 175
Cdd:pfam10513 157 EFEILMDRFE 166
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
582-790 9.82e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.58  E-value: 9.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 582 DPSLRPGDPARKARGRTRLPAKKKPPPPPPQDGPGSRTTPDKAPkkTWGQDAGSGKGGQGPPTRKPPRRTSSHLPSSPAA 661
Cdd:PRK07764  591 APGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAA--APAEASAAPAPGVAAPEHHPKHVAVPDASDGGDG 668
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355360 662 GDCPI-LATPESPPPLAPETPDEAASVAADSDVQVPGPAASPK-------------PLGRLRPPRESKVTRRLPGARPDA 727
Cdd:PRK07764  669 WPAKAgGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAgqaddpaaqppqaAQGASAPSPAADDPVPLPPEPDDP 748
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217355360 728 GMGPPSAVAERPKVSLHFDTETDGYFSDGEMSDSDVEAEDGGVQRGPREAGAEEVVRMGVLAS 790
Cdd:PRK07764  749 PDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEEVAMELLEE 811
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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