NCBI Conserved Domain Search

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...

4798-4904

9.32e-77

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the second ePHD finger of KMT2D. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named myeloid/lymphoid or mixed-lineage leukemia 4 (MLL4), a fourth human homolog of Drosophila trithorax, located on chromosome 12. KMT2D enzymatically generates trimethylated histone H3 Lys 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. It is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and KMT2D. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D contains the catalytic domain SET, five PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions.

Pssm-ID: 277168 Cd Length: 107 Bit Score: 250.35 E-value: 9.32e-77

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4798 CCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQRTGATSSCNRMRCPN 4877
Cdd:cd15698     1 CCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQKTGATNSCNRLRCPN 80

                          90       100
                  ....*....|....*....|....*..
gi 558137628 4878 VYHFACAIRAKCMFFKDKTMLCPMHKI 4904
Cdd:cd15698    81 VYHFACAIRAKCMFFKDKTMLCPMHKL 107

HMG-box_KMT2D

cd22027

high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2D (KMT2D) and ...

1722-1805

1.38e-59

high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2D (KMT2D) and similar proteins; KMT2D, also called ALL1-related protein (ALR), is encoded by the gene that was named myeloid/lymphoid or mixed-lineage leukemia 4 (MLL4), a fourth human homolog of Drosophila trithorax, located on chromosome 12. KMT2D enzymatically generates trimethylated histone H3 Lys 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. It is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and KMT2D. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis.

Pssm-ID: 438836 Cd Length: 84 Bit Score: 200.31 E-value: 1.38e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1722 GLSYNQRSLQRWEKDEELGQLSTISPVLYANINFPNLKQDYPDWSSRCKQIMKLWRKVPAADKAPYLQKAKDNRAAHRIN 1801
Cdd:cd22027     1 GLSYNQRSLQRWEKDEELGELSTISPVLYANINFPNLKQDYPDWSSRCKQIMKLWRKVPAADKAPYLQKAKDNRAAHRIN 80


                  ....
gi 558137628 1802 KVQK 1805
Cdd:cd22027    81 KVQK 84

ePHD1_KMT2D

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...

134-217

1.18e-51

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the first ePHD finger of KMT2D. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named myeloid/lymphoid or mixed-lineage leukemia 4 (MLL4), a fourth human homolog of Drosophila trithorax, located on chromosome 12. KMT2D enzymatically generates trimethylated histone H3 at Lys 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. It is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and KMT2D. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D contains the catalytic domain SET, five PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions.

Pssm-ID: 277165 Cd Length: 90 Bit Score: 177.80 E-value: 1.18e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  134 GSCWAHHWCAVWSAGVWGKGGPELCGVDKAIFSGISQRCSHCTRLGASIPCRSPGCPRLYHFPCATASGSFLSMKTLQLL 213
Cdd:cd15695     7 GECWVHHWCAAWSAGVKQHEGDGLIGVDKAVFSGISQKCEHCKRLGATIQCHAEGCPRFYHFPCAAASGSFQSMKTLLLL 86


                  ....
gi 558137628  214 CPEH 217
Cdd:cd15695    87 CPEH 90

PHD5_KMT2D

cd15601

PHD finger 5 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...

1233-1283

4.09e-33

PHD finger 5 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 downregulated 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 fifth PHD finger.

Pssm-ID: 277074 Cd Length: 51 Bit Score: 123.48 E-value: 4.09e-33

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 558137628 1233 TCPICHAPYVEEDLLIQCRHCERWMHAGCESLFTEDDVEQAADEGFDCVSC 1283
Cdd:cd15601     1 TCPVCRAKYVEEDLLIQCRHCDRWVHAVCESLFTEDEVEQAADEGFDCSSC 51

PHD3_KMT2D

PHD finger 3 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...

1105-1155

7.91e-33

PHD finger 3 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 as HOXA1-3 and NESTIN. It is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and KMT2D. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D contains the catalytic domain SET, five 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 third PHD finger.

Pssm-ID: 277072 Cd Length: 51 Bit Score: 122.84 E-value: 7.91e-33

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 558137628 1105 DMCVVCGSFGRGAEGHLLACSQCSQCYHPYCVNSKITKVMLLKGWRCVECI 1155
Cdd:cd15597     1 DMCVVCGSFGRGSEGHLLACSQCSQCYHPYCVNSKITKVMLLKGWRCVECI 51

FYRC

smart00542

FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...

5006-5093

1.13e-31

FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region (FYRN), but sometimes is far distant. Unknown function, but occurs frequently in chromatin-associated proteins.

Pssm-ID: 197781 Cd Length: 86 Bit Score: 120.48 E-value: 1.13e-31

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628   5006 EFIIKVMEQGleDLVFTDASPQAVWNRIIEPVAAMRKEADMLRLFPEYLKGEELFGLTVHAVLRIAESLPGVESCQNYLF 5085
Cdd:smart00542    1 LFRVEIESDP--GEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNYWF 78


                    ....*...
gi 558137628   5086 RYGRHPLM 5093
Cdd:smart00542   79 RYHRSPLL 86

PHD5_KMT2C_like

PHD finger 5 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 4 found in ...

1156-1202

3.57e-29

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: 112.18 E-value: 3.57e-29

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 558137628 1156 VCEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWCV 1202
Cdd:cd15513     1 VCEGCGKASDESRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWCV 47

PHD2_KMT2D

PHD finger 2 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...

275-320

8.29e-28

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: 108.16 E-value: 8.29e-28

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  275 VCQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15595     1 VCQTCRKPGEDSKMLVCEACDKGYHTFCLKPAMESLPTDSWKCKAC 46

PHD1_KMT2C_like

PHD finger 1 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...

228-273

8.55e-22

PHD finger 1 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (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, 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 first PHD finger.

Pssm-ID: 276984 Cd Length: 48 Bit Score: 91.22 E-value: 8.55e-22

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 558137628  228 RCAVCEGPGELCDLFFCTSCGHHYHGACLDTAL--TARKRAGWQCPEC 273
Cdd:cd15509     1 NCAVCDSPGDLSDLLFCTSCGQHYHGSCLDPAVrpTPLVRAGWQCPEC 48

FYRN

pfam05964

F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...

4947-4998

3.47e-18

F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It is similar to SMART:SM00541.

Pssm-ID: 461787 Cd Length: 51 Bit Score: 81.01 E-value: 3.47e-18

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 558137628  4947 GGLVFHAIGQLLPHQMAdFHSATALYPVGYEATRIYWSLRTNNRRCCYRCSI 4998
Cdd:pfam05964    1 GSLTVLSLGEIVPDRPA-FHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51

PHA03247 super family

cl33720

large tegument protein UL36; Provisional

1834-2403

4.21e-16

large tegument protein UL36; Provisional

The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 86.92 E-value: 4.21e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1834 PPQPGALGSPPPAAAPTIFIGSPTTP---------AGLSTSADGFLKPPAGTVPGPDSPGElflKLPPQVPAQVPSQdpf 1904
Cdd:PHA03247 2506 PDAPPAPSRLAPAILPDEPVGEPVHPrmltwirglEELASDDAGDPPPPLPPAAPPAAPDR---SVPPPRPAPRPSE--- 2579

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1905 glaPAYALEPRFPtapstyppypspaGAPVQPptlgtsSRPGTgqPGEFHTTPPGTPRHQPSTPDPFlKPRCPSLDNLAV 1984
Cdd:PHA03247 2580 ---PAVTSRARRP-------------DAPPQS------ARPRA--PVDDRGDPRGPAPPSPLPPDTH-APDPPPPSPSPA 2634

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1985 PESPGVGGGKASEPLLSP-----PPFGESRKALEVKKEELGASSPSYGPPNLGFvdSPSSGPHLGSLELKAPDVFKAPLT 2059
Cdd:PHA03247 2635 ANEPDPHPPPTVPPPERPrddpaPGRVSRPRRARRLGRAAQASSPPQRPRRRAA--RPTVGSLTSLADPPPPPPTPEPAP 2712

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2060 PRASQVEPQSPGLGLRPQEPSPAQALAPSPPSHSDIFRPGPYPDPYAQPPLTPRPQPPAPESCCALPPRSLPSDPFSRVP 2139
Cdd:PHA03247 2713 HALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLS 2792

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2140 ASPQSQSSSQSpltPRPLSAEAFCPSPVTPRFQSPDPYSRPPSRPQSRDPFAPLHKPPRPQPPEVAFK-SGPLAH--TPL 2216
Cdd:PHA03247 2793 ESRESLPSPWD---PADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVApGGDVRRrpPSR 2869

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2217 GAGGFPAALPSGPAGELHAKVPSGQPPNFARSPgtgafvgtPSPMRFTFPQAVGEPSSLKPPVPQPGLPPPHginshfgP 2296
Cdd:PHA03247 2870 SPAAKPAAPARPPVRRLARPAVSRSTESFALPP--------DQPERPPQPQAPPPPQPQPQPPPPPQPQPPP-------P 2934

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2297 GPTLGKPQSTNYSVATGNFHPSGSPLGPSSGSTGEGYGLSPLRPQSVLPPPVPDGSLPYPPHGASQRAGITSpvdkredp 2376
Cdd:PHA03247 2935 PPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSS-------- 3006

                         570       580
                  ....*....|....*....|....*..
gi 558137628 2377 gagMAGSLAAPELPgtqDPGISSLSQT 2403
Cdd:PHA03247 3007 ---WASSLALHEET---DPPPVSLKQT 3027

PHA03247 super family

cl33720

large tegument protein UL36; Provisional

3928-4214

5.65e-07

large tegument protein UL36; Provisional

The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.87 E-value: 5.65e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 3928 RPLQNNAGPQPAKPGSVPQSGQglPGAGVMPTvGQFRAQLQGvlAKNPQLRHLSPQQQQQLQALLMQRQLQQSQAirqAP 4007
Cdd:PHA03247 2576 RPSEPAVTSRARRPDAPPQSAR--PRAPVDDR-GDPRGPAPP--SPLPPDTHAPDPPPPSPSPAANEPDPHPPPT---VP 2647

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4008 SYQEPGTQPSPLQGLLGRQPQVGGFPGSQTGPLQ------------ELGAGLRPQGPPRLPAPQ-GALSTGPVPGPVHPT 4074
Cdd:PHA03247 2648 PPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQrprrraarptvgSLTSLADPPPPPPTPEPApHALVSATPLPPGPAA 2727

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4075 PPPSSPQEPKRPSQLPSPSSQLPSEAQLPPTQPGT------PKPQALPLELPPGKISPAAAQLADTLFGKGLGPWDPPDN 4148
Cdd:PHA03247 2728 ARQASPALPAAPAPPAVPAGPATPGGPARPARPPTtagppaPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADP 2807

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 558137628 4149 PAEAQKP---EQSSLVPGHPEQVNGQAVPEPSylSIKQEPREEPCALGAQVV------KREANGEPIGTPGTSNH 4214
Cdd:PHA03247 2808 PAAVLAPaaaLPPAASPAGPLPPPTSAQPTAP--PPPPGPPPPSLPLGGSVApggdvrRRPPSRSPAAKPAAPAR 2880

PRK12323 super family

cl46901

DNA polymerase III subunit gamma/tau;

687-892

1.02e-04

DNA polymerase III subunit gamma/tau;

The actual alignment was detected with superfamily member PRK12323:

Pssm-ID: 481241 [Multi-domain] Cd Length: 700 Bit Score: 48.72 E-value: 1.02e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  687 PFGAKGDSDPESPLAAPILETPISPPPEANCTDPEPVPPMILPPSPGSPMGLASPILME-PLPPRCSPLLQHSLPPQNSP 765
Cdd:PRK12323  365 PGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPaRRSPAPEALAAARQASARGP 444

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  766 PSQCSPPALPLSIPSPLSPIEKAmevshEAEPPEMEIEKAPEPECPALEPSPTSPLPSPMGNLSCPAPSPAPALEDFSGM 845
Cdd:PRK12323  445 GGAPAPAPAPAAAPAAAARPAAA-----GPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPA 519

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 558137628  846 GEDTAPL-DGTDTPDSQPEAGQTPGSLASELkgSPVLLDPEELAPVTP 892
Cdd:PRK12323  520 GWVAESIpDPATADPDDAFETLAPAPAAAPA--PRAAAATEPVVAPRP 565

Name

Accession

Description

Interval

E-value

SET_KMT2D

cd19209

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...

5148-5302

1.44e-109

Pssm-ID: 380986 [Multi-domain] Cd Length: 155 Bit Score: 346.30 E-value: 1.44e-109

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5148 HSKSSQYRRLRTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVI 5227
Cdd:cd19209     1 HSKSSQYRRLKTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 558137628 5228 DATLTGGPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIPCHCGAWNCRKWM 5302
Cdd:cd19209    81 DATLTGGPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIPCHCGAWNCRKWM 155

ePHD2_KMT2D

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...

4798-4904

9.32e-77

Pssm-ID: 277168 Cd Length: 107 Bit Score: 250.35 E-value: 9.32e-77

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4798 CCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQRTGATSSCNRMRCPN 4877
Cdd:cd15698     1 CCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQKTGATNSCNRLRCPN 80

                          90       100
                  ....*....|....*....|....*..
gi 558137628 4878 VYHFACAIRAKCMFFKDKTMLCPMHKI 4904
Cdd:cd15698    81 VYHFACAIRAKCMFFKDKTMLCPMHKL 107

HMG-box_KMT2D

cd22027

high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2D (KMT2D) and ...

1722-1805

1.38e-59

Pssm-ID: 438836 Cd Length: 84 Bit Score: 200.31 E-value: 1.38e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1722 GLSYNQRSLQRWEKDEELGQLSTISPVLYANINFPNLKQDYPDWSSRCKQIMKLWRKVPAADKAPYLQKAKDNRAAHRIN 1801
Cdd:cd22027     1 GLSYNQRSLQRWEKDEELGELSTISPVLYANINFPNLKQDYPDWSSRCKQIMKLWRKVPAADKAPYLQKAKDNRAAHRIN 80


                  ....
gi 558137628 1802 KVQK 1805
Cdd:cd22027    81 KVQK 84

ePHD1_KMT2D

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...

134-217

1.18e-51

Pssm-ID: 277165 Cd Length: 90 Bit Score: 177.80 E-value: 1.18e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  134 GSCWAHHWCAVWSAGVWGKGGPELCGVDKAIFSGISQRCSHCTRLGASIPCRSPGCPRLYHFPCATASGSFLSMKTLQLL 213
Cdd:cd15695     7 GECWVHHWCAAWSAGVKQHEGDGLIGVDKAVFSGISQKCEHCKRLGATIQCHAEGCPRFYHFPCAAASGSFQSMKTLLLL 86


                  ....
gi 558137628  214 CPEH 217
Cdd:cd15695    87 CPEH 90

PHD5_KMT2D

cd15601

PHD finger 5 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...

1233-1283

4.09e-33

Pssm-ID: 277074 Cd Length: 51 Bit Score: 123.48 E-value: 4.09e-33

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 558137628 1233 TCPICHAPYVEEDLLIQCRHCERWMHAGCESLFTEDDVEQAADEGFDCVSC 1283
Cdd:cd15601     1 TCPVCRAKYVEEDLLIQCRHCDRWVHAVCESLFTEDEVEQAADEGFDCSSC 51

PHD3_KMT2D

PHD finger 3 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...

1105-1155

7.91e-33

Pssm-ID: 277072 Cd Length: 51 Bit Score: 122.84 E-value: 7.91e-33

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 558137628 1105 DMCVVCGSFGRGAEGHLLACSQCSQCYHPYCVNSKITKVMLLKGWRCVECI 1155
Cdd:cd15597     1 DMCVVCGSFGRGSEGHLLACSQCSQCYHPYCVNSKITKVMLLKGWRCVECI 51

SET

COG2940

SET domain-containing protein (function unknown) [General function prediction only];

5164-5301

9.04e-32

SET domain-containing protein (function unknown) [General function prediction only];

Pssm-ID: 442183 [Multi-domain] Cd Length: 134 Bit Score: 122.76 E-value: 9.04e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5164 NVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRgiYMFRINNEHVIDATLTGGPARYINHSC 5243
Cdd:COG2940     7 RIEVRPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKEPLHT--YLFELDDDGVIDGALGGNPARFINHSC 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 558137628 5244 APNCVAEVVTFD-----KEDkiiiissrrIPKGEELTYDYQFDFEDDQHkiPCHCGawNCRKW 5301
Cdd:COG2940    85 DPNCEADEEDGRifivaLRD---------IAAGEELTYDYGLDYDEEEY--PCRCP--NCRGT 134

FYRC

smart00542

FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...

5006-5093

1.13e-31

Pssm-ID: 197781 Cd Length: 86 Bit Score: 120.48 E-value: 1.13e-31

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628   5006 EFIIKVMEQGleDLVFTDASPQAVWNRIIEPVAAMRKEADMLRLFPEYLKGEELFGLTVHAVLRIAESLPGVESCQNYLF 5085
Cdd:smart00542    1 LFRVEIESDP--GEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNYWF 78


                    ....*...
gi 558137628   5086 RYGRHPLM 5093
Cdd:smart00542   79 RYHRSPLL 86

SET

smart00317

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...

5163-5285

3.95e-31

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on outlier plant homologues

Pssm-ID: 214614 [Multi-domain] Cd Length: 124 Bit Score: 120.52 E-value: 3.95e-31

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628   5163 NNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYE-EQNRGIYMFRINNEHVIDATLTGGPARYINH 5241
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDtDGAKAFYLFDIDSDLCIDARRKGNLARFINH 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 558137628   5242 SCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDD 5285
Cdd:smart00317   81 SCEPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124

PHD5_KMT2C_like

PHD finger 5 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 4 found in ...

1156-1202

3.57e-29

Pssm-ID: 276988 Cd Length: 47 Bit Score: 112.18 E-value: 3.57e-29

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 558137628 1156 VCEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWCV 1202
Cdd:cd15513     1 VCEGCGKASDESRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWCV 47

PHD2_KMT2D

PHD finger 2 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...

275-320

8.29e-28

Pssm-ID: 277070 Cd Length: 46 Bit Score: 108.16 E-value: 8.29e-28

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  275 VCQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15595     1 VCQTCRKPGEDSKMLVCEACDKGYHTFCLKPAMESLPTDSWKCKAC 46

FYRC

pfam05965

F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...

5004-5088

1.20e-25

F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It is similar to SMART:SM00542.

Pssm-ID: 461788 Cd Length: 83 Bit Score: 103.46 E-value: 1.20e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  5004 RPEFIIKVMEQglEDLVFTDASPQAVWNRIIEPVAAMRKEADMLRLFPEYLKGEELFGLTVHAVLRIAESLPGVESCQNY 5083
Cdd:pfam05965    1 GPLFRVTVEED--PDESFEGSSPTKCWSMVLERVQELRREAGLKLKLPESISGEDMFGLTHPAVVRLIESLPGAEKCTNY 78


                   ....*
gi 558137628  5084 LFRYG 5088
Cdd:pfam05965   79 KFRYG 83

PHD1_KMT2C_like

PHD finger 1 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...

228-273

8.55e-22

Pssm-ID: 276984 Cd Length: 48 Bit Score: 91.22 E-value: 8.55e-22

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 558137628  228 RCAVCEGPGELCDLFFCTSCGHHYHGACLDTAL--TARKRAGWQCPEC 273
Cdd:cd15509     1 NCAVCDSPGDLSDLLFCTSCGQHYHGSCLDPAVrpTPLVRAGWQCPEC 48

SET

pfam00856

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...

5174-5278

5.43e-21

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure.

Pssm-ID: 459965 [Multi-domain] Cd Length: 115 Bit Score: 91.43 E-value: 5.43e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  5174 GLGLYAAKDLEKHTMVIEYIGT-IIRNEVANRREKIYEEQNR----GIYMFRIN--NEHVIDATLT--GGPARYINHSCA 5244
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLElrlwGPYLFTLDedSEYCIDARALyyGNWARFINHSCD 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 558137628  5245 PNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDY 5278
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDY 114

FYRN

pfam05964

F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...

4947-4998

3.47e-18

F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It is similar to SMART:SM00541.

Pssm-ID: 461787 Cd Length: 51 Bit Score: 81.01 E-value: 3.47e-18

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 558137628  4947 GGLVFHAIGQLLPHQMAdFHSATALYPVGYEATRIYWSLRTNNRRCCYRCSI 4998
Cdd:pfam05964    1 GSLTVLSLGEIVPDRPA-FHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51

FYRN

smart00541

FY-rich domain, N-terminal region; is sometimes closely juxtaposed with the C-terminal region ...

4957-5000

2.23e-16

FY-rich domain, N-terminal region; is sometimes closely juxtaposed with the C-terminal region (FYRC), but sometimes is far distant. Unknown function, but occurs frequently in chromatin-associated proteins.

Pssm-ID: 128814 Cd Length: 44 Bit Score: 75.78 E-value: 2.23e-16

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 558137628   4957 LLPHQMADFHSATALYPVGYEATRIYWSLRTNNRRCCYRCSIGE 5000
Cdd:smart00541    1 LLPIQGKLFHSESAIFPVGYKSTRKYWSVKDPNRRCLYSCVIDE 44

PHA03247

large tegument protein UL36; Provisional

1834-2403

4.21e-16

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 86.92 E-value: 4.21e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1834 PPQPGALGSPPPAAAPTIFIGSPTTP---------AGLSTSADGFLKPPAGTVPGPDSPGElflKLPPQVPAQVPSQdpf 1904
Cdd:PHA03247 2506 PDAPPAPSRLAPAILPDEPVGEPVHPrmltwirglEELASDDAGDPPPPLPPAAPPAAPDR---SVPPPRPAPRPSE--- 2579

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1905 glaPAYALEPRFPtapstyppypspaGAPVQPptlgtsSRPGTgqPGEFHTTPPGTPRHQPSTPDPFlKPRCPSLDNLAV 1984
Cdd:PHA03247 2580 ---PAVTSRARRP-------------DAPPQS------ARPRA--PVDDRGDPRGPAPPSPLPPDTH-APDPPPPSPSPA 2634

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1985 PESPGVGGGKASEPLLSP-----PPFGESRKALEVKKEELGASSPSYGPPNLGFvdSPSSGPHLGSLELKAPDVFKAPLT 2059
Cdd:PHA03247 2635 ANEPDPHPPPTVPPPERPrddpaPGRVSRPRRARRLGRAAQASSPPQRPRRRAA--RPTVGSLTSLADPPPPPPTPEPAP 2712

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2060 PRASQVEPQSPGLGLRPQEPSPAQALAPSPPSHSDIFRPGPYPDPYAQPPLTPRPQPPAPESCCALPPRSLPSDPFSRVP 2139
Cdd:PHA03247 2713 HALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLS 2792

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2140 ASPQSQSSSQSpltPRPLSAEAFCPSPVTPRFQSPDPYSRPPSRPQSRDPFAPLHKPPRPQPPEVAFK-SGPLAH--TPL 2216
Cdd:PHA03247 2793 ESRESLPSPWD---PADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVApGGDVRRrpPSR 2869

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2217 GAGGFPAALPSGPAGELHAKVPSGQPPNFARSPgtgafvgtPSPMRFTFPQAVGEPSSLKPPVPQPGLPPPHginshfgP 2296
Cdd:PHA03247 2870 SPAAKPAAPARPPVRRLARPAVSRSTESFALPP--------DQPERPPQPQAPPPPQPQPQPPPPPQPQPPP-------P 2934

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2297 GPTLGKPQSTNYSVATGNFHPSGSPLGPSSGSTGEGYGLSPLRPQSVLPPPVPDGSLPYPPHGASQRAGITSpvdkredp 2376
Cdd:PHA03247 2935 PPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSS-------- 3006

                         570       580
                  ....*....|....*....|....*..
gi 558137628 2377 gagMAGSLAAPELPgtqDPGISSLSQT 2403
Cdd:PHA03247 3007 ---WASSLALHEET---DPPPVSLKQT 3027

PHD

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...

1156-1204

1.90e-13

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: 67.52 E-value: 1.90e-13

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 558137628  1156 VCEVCGQASDPSRLLLCDDCDISYHTYCLDPPL--LTVPKGGWKCKWCVSC 1204
Cdd:pfam00628    1 YCAVCGKSDDGGELVQCDGCDDWFHLACLGPPLdpAEIPSGEWLCPECKPK 51

PHD

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...

275-323

2.07e-13

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 67.52 E-value: 2.07e-13

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 558137628   275 VCQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHS--WKCKACRVC 323
Cdd:pfam00628    1 YCAVCGKSDDGGELVQCDGCDDWFHLACLGPPLDPAEIPSgeWLCPECKPK 51

zf-HC5HC2H

PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...

4825-4902

3.68e-13

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: 68.12 E-value: 3.68e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  4825 HLNCALWSTEVY----ETQGGALMNVEVALHRGLLTKCSLC-QRTGATSSCNRMRCPNVYHFACAIRAKCMF-FKDKT-- 4896
Cdd:pfam13771    1 HVVCALWSPELVqrgnDSMGFPIEDIEKIPKRRWKLKCYLCkKKGGACIQCSKKNCRRAFHVTCALEAGLLMqFDEDNgt 80


                   ....*...
gi 558137628  4897 --MLCPMH 4902
Cdd:pfam13771   81 fkSYCKKH 88

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

1156-1201

1.85e-12

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: 64.54 E-value: 1.85e-12

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 558137628   1156 VCEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLT-VPKGGWKCKWC 1201
Cdd:smart00249    1 YCSVCGKPDDGGELLQCDGCDRWYHQTCLGPPLLEeEPDGKWYCPKC 47

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

275-320

4.55e-12

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 63.38 E-value: 4.55e-12

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 558137628    275 VCQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEE-LPAHSWKCKAC 320
Cdd:smart00249    1 YCSVCGKPDDGGELLQCDGCDRWYHQTCLGPPLLEeEPDGKWYCPKC 47

zf-HC5HC2H

PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...

139-217

1.00e-11

Pssm-ID: 463977 [Multi-domain] Cd Length: 88 Bit Score: 63.89 E-value: 1.00e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628   139 HHWCAVWSAGVWGKGGPE----LCGVDKAIFSGISQRCSHC-TRLGASIPCRSPGCPRLYHFPCATASGSFLSMK----T 209
Cdd:pfam13771    1 HVVCALWSPELVQRGNDSmgfpIEDIEKIPKRRWKLKCYLCkKKGGACIQCSKKNCRRAFHVTCALEAGLLMQFDedngT 80


                   ....*...
gi 558137628   210 LQLLCPEH 217
Cdd:pfam13771   81 FKSYCKKH 88

PHD

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...

228-276

2.74e-11

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 61.35 E-value: 2.74e-11

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 558137628   228 RCAVCEGPGELCDLFFCTSCGHHYHGACLDTALTARKRA--GWQCPECKVC 276
Cdd:pfam00628    1 YCAVCGKSDDGGELVQCDGCDDWFHLACLGPPLDPAEIPsgEWLCPECKPK 51

PHD

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...

1107-1157

3.38e-10

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 58.27 E-value: 3.38e-10

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 558137628  1107 CVVCGsfGRGAEGHLLACSQCSQCYHPYCVNSKITKVMLLKG-WRCVECIVC 1157
Cdd:pfam00628    2 CAVCG--KSDDGGELVQCDGCDDWFHLACLGPPLDPAEIPSGeWLCPECKPK 51

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

1106-1154

7.49e-10

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 57.22 E-value: 7.49e-10

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 558137628   1106 MCVVCGsfGRGAEGHLLACSQCSQCYHPYCVNSKITKVMLLKGWRCVEC 1154
Cdd:smart00249    1 YCSVCG--KPDDGGELLQCDGCDRWYHQTCLGPPLLEEEPDGKWYCPKC 47

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

228-273

6.32e-09

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 54.53 E-value: 6.32e-09

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 558137628    228 RCAVCEGPGELCDLFFCTSCGHHYHGACLDTALT-ARKRAGWQCPEC 273
Cdd:smart00249    1 YCSVCGKPDDGGELLQCDGCDRWYHQTCLGPPLLeEEPDGKWYCPKC 47

HMG

smart00398

high mobility group;

1748-1799

5.08e-07

high mobility group;

Pssm-ID: 197700 [Multi-domain] Cd Length: 70 Bit Score: 50.01 E-value: 5.08e-07

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 558137628   1748 VLYANINFPNLKQDYPDWSS--RCKQIMKLWRKVPAADKAPYLQKAKDNRAAHR 1799
Cdd:smart00398   10 MLFSQENRAKIKAENPDLSNaeISKKLGERWKLLSEEEKAPYEEKAKKDKERYE 63

PHA03247

large tegument protein UL36; Provisional

3928-4214

5.65e-07

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.87 E-value: 5.65e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 3928 RPLQNNAGPQPAKPGSVPQSGQglPGAGVMPTvGQFRAQLQGvlAKNPQLRHLSPQQQQQLQALLMQRQLQQSQAirqAP 4007
Cdd:PHA03247 2576 RPSEPAVTSRARRPDAPPQSAR--PRAPVDDR-GDPRGPAPP--SPLPPDTHAPDPPPPSPSPAANEPDPHPPPT---VP 2647

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4008 SYQEPGTQPSPLQGLLGRQPQVGGFPGSQTGPLQ------------ELGAGLRPQGPPRLPAPQ-GALSTGPVPGPVHPT 4074
Cdd:PHA03247 2648 PPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQrprrraarptvgSLTSLADPPPPPPTPEPApHALVSATPLPPGPAA 2727

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4075 PPPSSPQEPKRPSQLPSPSSQLPSEAQLPPTQPGT------PKPQALPLELPPGKISPAAAQLADTLFGKGLGPWDPPDN 4148
Cdd:PHA03247 2728 ARQASPALPAAPAPPAVPAGPATPGGPARPARPPTtagppaPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADP 2807

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 558137628 4149 PAEAQKP---EQSSLVPGHPEQVNGQAVPEPSylSIKQEPREEPCALGAQVV------KREANGEPIGTPGTSNH 4214
Cdd:PHA03247 2808 PAAVLAPaaaLPPAASPAGPLPPPTSAQPTAP--PPPPGPPPPSLPLGGSVApggdvrRRPPSRSPAAKPAAPAR 2880

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

1233-1283

6.07e-07

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 49.13 E-value: 6.07e-07

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 558137628   1233 TCPICHAPYvEEDLLIQCRHCERWMHAGCESLFTEDDVEqaaDEGFDCVSC 1283
Cdd:smart00249    1 YCSVCGKPD-DGGELLQCDGCDRWYHQTCLGPPLLEEEP---DGKWYCPKC 47

Atrophin-1

pfam03154

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...

1937-2372

8.18e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.

Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 52.46 E-value: 8.18e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  1937 PTLGTSSRPGTGQPGEFHTTPPGTPRHQPSTPDPFLKPRCPSLDNLAVPESPGVGGGKASEPLLSPPPfgeSRKALEVKK 2016
Cdd:pfam03154  151 PQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPP---NQTQSTAAP 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  2017 EELGASSPSYGPPNLgfvdsPSsgPHlgslelkaPDVFKAPLTPRASQVEPQS-PGLGLRPQEPSPAQALAPSPPSHSDI 2095
Cdd:pfam03154  228 HTLIQQTPTLHPQRL-----PS--PH--------PPLQPMTQPPPPSQVSPQPlPQPSLHGQMPPMPHSLQTGPSHMQHP 292

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  2096 FRPGPYPDPyaqPPLTPRPQPPAPESCCALPPRSLPSDPFSRvPASPQSQSSSQSPLTPRPLSAEAFCPSPVTPRFQSPD 2175
Cdd:pfam03154  293 VPPQPFPLT---PQSSQSQVPPGPSPAAPGQSQQRIHTPPSQ-SQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPN 368

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  2176 PYS-RPPSRPQSRDPFA-PLHKPPrpqPPEVAFKSGPLAHTPLGAggFPAALPSGPAGElHAKVPSGQPPNFARS---PG 2250
Cdd:pfam03154  369 PQShKHPPHLSGPSPFQmNSNLPP---PPALKPLSSLSTHHPPSA--HPPPLQLMPQSQ-QLPPPPAQPPVLTQSqslPP 442

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  2251 TGAFVGTPSPMRFTFPQAVGEPSSLKPPVPQPGLPPPHGINSHFGPGPTLGKPQSTNYSVATGNFHPSGSPLGPSsgSTG 2330
Cdd:pfam03154  443 PAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPV--QIK 520

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 558137628  2331 EGYGLSPLRPQSVLPP---PVPDGSLPYPPHGASQRAGITSPVDK 2372
Cdd:pfam03154  521 EEALDEAEEPESPPPPprsPSPEPTVVNTPSHASQSARFYKHLDR 565

HMG_box

pfam00505

HMG (high mobility group) box;

1748-1799

1.61e-05

HMG (high mobility group) box;

Pssm-ID: 459837 [Multi-domain] Cd Length: 68 Bit Score: 45.68 E-value: 1.61e-05

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 558137628  1748 VLYANINFPNLKQDYPDWSSR--CKQIMKLWRKVPAADKAPYLQKAKDNRAAHR 1799
Cdd:pfam00505    9 FLFSKEQRAKLKAENPGLKNAeiSKILGEKWKALSEEEKKPYEEKAEKEKARYE 62

PHD

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...

1234-1285

7.49e-05

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 43.25 E-value: 7.49e-05

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 558137628  1234 CPICHAPyVEEDLLIQCRHCERWMHAGCESLftEDDVEQAADEGFDCVSCQP 1285
Cdd:pfam00628    2 CAVCGKS-DDGGELVQCDGCDDWFHLACLGP--PLDPAEIPSGEWLCPECKP 50

PRK12323

DNA polymerase III subunit gamma/tau;

687-892

1.02e-04

DNA polymerase III subunit gamma/tau;

Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 48.72 E-value: 1.02e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  687 PFGAKGDSDPESPLAAPILETPISPPPEANCTDPEPVPPMILPPSPGSPMGLASPILME-PLPPRCSPLLQHSLPPQNSP 765
Cdd:PRK12323  365 PGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPaRRSPAPEALAAARQASARGP 444

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  766 PSQCSPPALPLSIPSPLSPIEKAmevshEAEPPEMEIEKAPEPECPALEPSPTSPLPSPMGNLSCPAPSPAPALEDFSGM 845
Cdd:PRK12323  445 GGAPAPAPAPAAAPAAAARPAAA-----GPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPA 519

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 558137628  846 GEDTAPL-DGTDTPDSQPEAGQTPGSLASELkgSPVLLDPEELAPVTP 892
Cdd:PRK12323  520 GWVAESIpDPATADPDDAFETLAPAPAAAPA--PRAAAATEPVVAPRP 565

PABP-1234

TIGR01628

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...

4004-4132

1.88e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.

Pssm-ID: 130689 [Multi-domain] Cd Length: 562 Bit Score: 47.88 E-value: 1.88e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  4004 RQAPSYQEPgtQPSPLQGLLGRQPQVGGFPGSQTGPLQELGAGLRPQGPPRLPapqGALSTGPVPGPVHPTPPPSSPQEP 4083
Cdd:TIGR01628  378 LQPRMRQLP--MGSPMGGAMGQPPYYGQGPQQQFNGQPLGWPRMSMMPTPMGP---GGPLRPNGLAPMNAVRAPSRNAQN 452

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 558137628  4084 kRPSQLPSPSSQLPSEAQLPPTQPGTPKPQALPLELppGKISPAAAQLA 4132
Cdd:TIGR01628  453 -AAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTASQG--GQNKKLAQVLA 498

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

4858-4902

3.73e-04

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 41.04 E-value: 3.73e-04

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 558137628   4858 CSLCQRTGATS---SCNRmrCPNVYHFACAIRAKCMFFKDKTMLCPMH 4902
Cdd:smart00249    2 CSVCGKPDDGGellQCDG--CDRWYHQTCLGPPLLEEEPDGKWYCPKC 47

Med15

pfam09606

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...

3761-4110

3.91e-03

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.

Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 43.84 E-value: 3.91e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  3761 LGPGmPAKPLQQHFSSPGALGPTLLLSGKEQSIVETTLPPE-----ATEGPSTHQGGVAIGTVPEAVPTEPGEVKPSlSG 3835
Cdd:pfam09606  102 MGPG-PGGPMGQQMGGPGTASNLLASLGRPQMPMGGAGFPSqmsrvGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPN-GG 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  3836 DSQLLLVQPQAQpQPNSVPLQPPLRLQGQqqqqqvNLLHTAGVGSHGQSNSGSSSEASsvPHLLTQSSVSLGEQPGPITQ 3915
Cdd:pfam09606  180 PGQGQAGGMNGG-QQGPMGGQMPPQMGVP------GMPGPADAGAQMGQQAQANGGMN--PQQMGGAPNQVAMQQQQPQQ 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  3916 NPLGSQQHHGLERPLQNNAGPQPAKPGSVPQSGQGLPGAGVMPTVGQFRAQLQGVLAKNPQlrhlSPQQQQQLQALLMQR 3995
Cdd:pfam09606  251 QGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQT----RQQQQQQGGNHPAAH 326

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  3996 QLQQSQAIRQA------PSYQEPGTQPSPLQGLLGRQPQVGGFPGSQTGPLQELGAGLRPQGPPRLPAPQGALSTGPVPG 4069
Cdd:pfam09606  327 QQQMNQSVGQGgqvvalGGLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQG 406

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 558137628  4070 PVHPTPPPSSPQEPKRPSQLPSPS---SQLPSEAQLPPTQ-PGTP 4110
Cdd:pfam09606  407 PGSQPPQSHPGGMIPSPALIPSPSpqmSQQPAQQRTIGQDsPGGS 451

Name

Accession

Description

Interval

E-value

SET_KMT2D

cd19209

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...

5148-5302

1.44e-109

Pssm-ID: 380986 [Multi-domain] Cd Length: 155 Bit Score: 346.30 E-value: 1.44e-109

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5148 HSKSSQYRRLRTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVI 5227
Cdd:cd19209     1 HSKSSQYRRLKTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 558137628 5228 DATLTGGPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIPCHCGAWNCRKWM 5302
Cdd:cd19209    81 DATLTGGPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIPCHCGAWNCRKWM 155

SET_KMT2C_2D

cd19171

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...

5150-5302

1.98e-109

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), 2D (KMT2D) and similar proteins; This family includes KMT2C and KMT2D. Both, KMT2C (also termed HALR or MLL3) and KMT2D (also termed ALR or MLL2), act as histone methyltransferases that methylate 'Lys-4' of histone H3 (H3K4me). They are subunits of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation.

Pssm-ID: 380948 [Multi-domain] Cd Length: 153 Bit Score: 345.95 E-value: 1.98e-109

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5150 KSSQYRRLRTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVIDA 5229
Cdd:cd19171     1 KSSQYRKLKTEWRSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNRGIYMFRIDNDWVIDA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 558137628 5230 TLTGGPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIPCHCGAWNCRKWM 5302
Cdd:cd19171    81 TMTGGPARYINHSCNPNCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQHKIPCLCGAPNCRKWM 153

SET_KMT2C

cd19208

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...

5149-5302

5.93e-90

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) and similar proteins; KMT2C (EC2.1.1.43; also termed lysine N-methyltransferase 2C, homologous to ALR protein (HALR) myeloid/lymphoid, or mixed-lineage leukemia protein 3 (MLL3)), acts as a histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me) and may be involved in leukemogenesis and developmental disorder. KMT2C is a catalytic subunit of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation. Overexpression of KMT2C is associated with estrogen receptor-positive breast cancer; KMT2C mediates the estrogen dependence of breast cancer through regulation of estrogen receptor alpha (ERalpha) enhancer function. KMT2C is frequently mutated in certain populations with diffuse-type gastric adenocarcinomas (DGA); its loss promotes epithelial-to-mesenchymal transition (EMT) and is associated with worse overall survival.

Pssm-ID: 380985 [Multi-domain] Cd Length: 154 Bit Score: 289.99 E-value: 5.93e-90

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5149 SKSSQYRRLRTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVID 5228
Cdd:cd19208     1 SKSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRIDNDHVID 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 558137628 5229 ATLTGGPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIPCHCGAWNCRKWM 5302
Cdd:cd19208    81 ATLTGGPARYINHSCAPNCVAEVVTFEKGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWM 154

ePHD2_KMT2D

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...

4798-4904

9.32e-77

Pssm-ID: 277168 Cd Length: 107 Bit Score: 250.35 E-value: 9.32e-77

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4798 CCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQRTGATSSCNRMRCPN 4877
Cdd:cd15698     1 CCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQKTGATNSCNRLRCPN 80

                          90       100
                  ....*....|....*....|....*..
gi 558137628 4878 VYHFACAIRAKCMFFKDKTMLCPMHKI 4904
Cdd:cd15698    81 VYHFACAIRAKCMFFKDKTMLCPMHKL 107

ePHD2_KMT2C_like

cd15666

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...

4798-4902

6.10e-71

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: 233.73 E-value: 6.10e-71

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4798 CCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQRTGATSSCNRMRCPN 4877
Cdd:cd15666     1 CVLCGGEGDGDTDGPGRLLNLDVDKWVHLNCALWSYEVYETQNGALMNVEEALRRALTTTCSHCGRTGATVPCFKPRCAN 80

                          90       100
                  ....*....|....*....|....*
gi 558137628 4878 VYHFACAIRAKCMFFKDKTMLCPMH 4902
Cdd:cd15666    81 VYHLPCAIKDGCMFFKDKTMLCPSH 105

SET_SETD1-like

cd10518

SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...

5151-5299

5.00e-70

SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), histone-lysine N-methyltransferases (KMT2A/KMT2B/KMT2C/KMT2D) and similar proteins; This family includes SET domain-containing protein 1A (SETD1A), 1B (SETD1B), as well as histone-lysine N-methyltransferase 2A (KMT2A), 2B (KMT2B), 2C (KMT2C), 2D (KMT2D). These proteins are histone-lysine N-methyltransferases (EC 2.1.1.43) that specifically methylate 'Lys-4' of histone H3 (H3K4me).

Pssm-ID: 380916 Cd Length: 150 Bit Score: 232.87 E-value: 5.00e-70

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5151 SSQYRRLRTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQN-RGIYMFRINNEHVIDA 5229
Cdd:cd10518     2 SKRFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKRYDEEGgGGTYMFRIDEDLVIDA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5230 TLTGGPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQhKIPCHCGAWNCR 5299
Cdd:cd10518    82 TKKGNIARFINHSCDPNCYAKIITVDGEKHIVIFAKRDIAPGEELTYDYKFPIEDEE-KIPCLCGAPNCR 150

ePHD2_KMT2C

cd15697

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...

4798-4902

2.22e-62

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the second ePHD finger of KMT2C. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2C contains PHD fingers, two ePHD fingers, an ATPase alpha beta signature, a high mobility group (HMG)-1 box, a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain and two FY (phenylalanine tyrosine)-rich domains.

Pssm-ID: 277167 Cd Length: 105 Bit Score: 209.13 E-value: 2.22e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4798 CCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQRTGATSSCNRMRCPN 4877
Cdd:cd15697     1 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRLRCTN 80

                          90       100
                  ....*....|....*....|....*
gi 558137628 4878 VYHFACAIRAKCMFFKDKTMLCPMH 4902
Cdd:cd15697    81 VYHFTCAIKAQCMFFKDKTMLCPMH 105

HMG-box_KMT2D

cd22027

high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2D (KMT2D) and ...

1722-1805

1.38e-59

Pssm-ID: 438836 Cd Length: 84 Bit Score: 200.31 E-value: 1.38e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1722 GLSYNQRSLQRWEKDEELGQLSTISPVLYANINFPNLKQDYPDWSSRCKQIMKLWRKVPAADKAPYLQKAKDNRAAHRIN 1801
Cdd:cd22027     1 GLSYNQRSLQRWEKDEELGELSTISPVLYANINFPNLKQDYPDWSSRCKQIMKLWRKVPAADKAPYLQKAKDNRAAHRIN 80


                  ....
gi 558137628 1802 KVQK 1805
Cdd:cd22027    81 KVQK 84

ePHD1_KMT2D

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...

134-217

1.18e-51

Pssm-ID: 277165 Cd Length: 90 Bit Score: 177.80 E-value: 1.18e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  134 GSCWAHHWCAVWSAGVWGKGGPELCGVDKAIFSGISQRCSHCTRLGASIPCRSPGCPRLYHFPCATASGSFLSMKTLQLL 213
Cdd:cd15695     7 GECWVHHWCAAWSAGVKQHEGDGLIGVDKAVFSGISQKCEHCKRLGATIQCHAEGCPRFYHFPCAAASGSFQSMKTLLLL 86


                  ....
gi 558137628  214 CPEH 217
Cdd:cd15695    87 CPEH 90

SET_KMT2A_2B

cd19170

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...

5151-5303

1.42e-51

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), 2B (KMT2B) and similar proteins; This family includes KMT2A and KMT2B. Both KMT2A (also termed ALL-1 or CXXC7 or MLL or MLL1 or TRX1 or HRX) and KMT2B (also termed MLL4 or TRX2) act as histone methyltransferases that methylate 'Lys-4' of histone H3 (H3K4me).

Pssm-ID: 380947 [Multi-domain] Cd Length: 152 Bit Score: 180.28 E-value: 1.42e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5151 SSQYRRLRTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVIDAT 5230
Cdd:cd19170     2 AMRFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKYYESKGIGCYMFRIDDDEVVDAT 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 558137628 5231 LTGGPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDqhKIPCHCGAWNCRKWMN 5303
Cdd:cd19170    82 MHGNAARFINHSCEPNCYSRVVNIDGKKHIVIFALRRILRGEELTYDYKFPIEDV--KIPCTCGSKKCRKYLN 152

SET_SETD1

cd19169

SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...

5162-5299

1.12e-47

SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and similar proteins; This family includes SET domain-containing protein 1A (SETD1A) and SET domain-containing protein 1B (SETD1B). These proteins are histone-lysine N-methyltransferases that specifically methylate 'Lys-4' of histone H3 (H3K4me) when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated.

Pssm-ID: 380946 Cd Length: 148 Bit Score: 168.67 E-value: 1.12e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5162 KNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEqnRGI---YMFRINNEHVIDATLTGGPARY 5238
Cdd:cd19169    12 KKQLKFAKSRIHDWGLFALEPIAADEMVIEYVGQVIRQSVADEREKRYEA--IGIgssYLFRVDDDTIIDATKCGNLARF 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 558137628 5239 INHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDqhKIPCHCGAWNCR 5299
Cdd:cd19169    90 INHSCNPNCYAKIITVESQKKIVIYSKRPIAVNEEITYDYKFPIEDE--KIPCLCGAPQCR 148

ePHD1_KMT2C_like

cd15665

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...

134-217

1.26e-44

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: 157.87 E-value: 1.26e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  134 GSCWAHHWCAVWSAGVWGKGGPELCGVDKAIFSGISQRCSHCTRLGASIPCRSPGCPRLYHFPCATASGSFLSMKTLQLL 213
Cdd:cd15665     7 GEVYAHHCCAAWSEGVCQTEDGALENVDKAVAKALSQKCSFCLRYGASISCRMPSCSKSFHFPCAAAAGCFQDIKTLTLF 86


                  ....
gi 558137628  214 CPEH 217
Cdd:cd15665    87 CPEH 90

SET_KMT2A

cd19206

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...

5153-5303

1.18e-42

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) and similar proteins; KMT2A (EC2.1.1.43; also termed lysine N-methyltransferase 2A, ALL-1, CXXC-type zinc finger protein 7 (CXXC7), myeloid/lymphoid or mixed-lineage leukemia (MLL), myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), trithorax-like protein (TRX1), or zinc finger protein HRX) acts as a histone methyltransferase that plays an essential role in early development and hematopoiesis. It is a catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac).

Pssm-ID: 380983 [Multi-domain] Cd Length: 154 Bit Score: 154.79 E-value: 1.18e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5153 QYRRLRTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVIDATLT 5232
Cdd:cd19206     4 RFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREKYYDSKGIGCYMFRIDDSEVVDATMH 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 558137628 5233 GGPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIPCHCGAWNCRKWMN 5303
Cdd:cd19206    84 GNAARFINHSCEPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDASNKLPCNCGAKKCRKFLN 154

SET_SET1

cd20072

SET domain (including post-SET domain) found in catalytic component of the Saccharomyces ...

5162-5299

1.53e-42

SET domain (including post-SET domain) found in catalytic component of the Saccharomyces cerevisiae COMPASS complex and similar proteins; The family contains mostly fungal SET domains, including SET1 found in the catalytic component of the Saccharomyces cerevisiae COMPASS (complex of proteins associated with Set1). SET1 is a histone-lysine N-methyltransferase that specifically methylates 'Lys-4' of histone H3 (H3K4me), when part of the SET1 histone methyltransferase (HMT) complex. The activity of this catalytic domain is established through forming a complex with a set of core proteins; it is extensively contacted by Cps60 (Bre2), Cps50 (Swd1), and Cps30 (Swd3).

Pssm-ID: 380998 Cd Length: 148 Bit Score: 154.12 E-value: 1.53e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5162 KNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRG-IYMFRINNEHVIDATLTGGPARYIN 5240
Cdd:cd20072    12 KKQLKFARSAIHNWGLYAMENISAKDMVIEYVGEVIRQQVADEREKRYLRQGIGsSYLFRIDDDTVVDATKKGNIARFIN 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 558137628 5241 HSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDqhKIPCHCGAWNCR 5299
Cdd:cd20072    92 HCCDPNCTAKIIKVEGEKRIVIYAKRDIAAGEELTYDYKFPREED--KIPCLCGAPNCR 148

HMG_KMT2C-like

cd21997

high mobility group (HMG)-box found in histone-lysine N-methyltransferases KMT2C, KMT2D and ...

1732-1798

7.03e-42

high mobility group (HMG)-box found in histone-lysine N-methyltransferases KMT2C, KMT2D and similar proteins; This subfamily includes KMT2C and KMT2D. KMT2C, also called myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3) or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) 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, and 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 called 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. All subfamily members contain one HMG-box domain.

Pssm-ID: 438813 Cd Length: 67 Bit Score: 149.04 E-value: 7.03e-42

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 558137628 1732 RWEKDEELGQLSTISPVLYANINFPNLKQDYPDWSSRCKQIMKLWRKVPAADKAPYLQKAKDNRAAH 1798
Cdd:cd21997     1 KWEKDEPLGDMATISPVLYANINHPNLKQEYPDWTDRAKQIAKLWRKLSAEERAPYLQKARENRAAL 67

HMG-box_KMT2C

cd22026

high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2C (KMT2C) and ...

1727-1804

6.65e-38

high mobility group (HMG)-box found in histone-lysine N-methyltransferase 2C (KMT2C) and similar proteins; KMT2C, also called 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.

Pssm-ID: 438835 Cd Length: 81 Bit Score: 138.38 E-value: 6.65e-38

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 558137628 1727 QRSLQRWEKDEELGQLSTISPVLYANINFPNLKQDYPDWSSRCKQIMKLWRKVPAADKAPYLQKAKDNRAAHRINKVQ 1804
Cdd:cd22026     1 QRSTLKWEKEEALGEMATVAPVLYTNINFPNLKEEFPDWTTRVKQIAKLWRKASSQERAPYVQKARDNRAALRINKVQ 78

SET_KMT2B

cd19207

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...

5153-5303

1.72e-37

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) and similar proteins; KMT2B (EC2.1.1.43; also termed lysine N-methyltransferase 2B, myeloid/lymphoid or mixed-lineage leukemia protein 4 (MLL2/MLL4), trithorax homolog 2 (TRX2), or WW domain-binding protein 7 (WBP-7)), acts as a histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me). It is required during the transcriptionally active period of oocyte growth for the establishment and/or maintenance of bulk H3K4 trimethylation (H3K4me3), global transcriptional silencing that precedes resumption of meiosis, oocyte survival and normal zygotic genome activation.

Pssm-ID: 380984 [Multi-domain] Cd Length: 154 Bit Score: 140.16 E-value: 1.72e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5153 QYRRLRTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVIDATLT 5232
Cdd:cd19207     4 RFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDSKGIGCYMFRIDDFDVVDATMH 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 558137628 5233 GGPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIPCHCGAWNCRKWMN 5303
Cdd:cd19207    84 GNAARFINHSCEPNCYSRVIHVEGQKHIVIFALRKIYRGEELTYDYKFPIEDASNKLPCNCGAKRCRRFLN 154

ePHD_KMT2A_like

cd15664

Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The ...

4798-4902

3.86e-35

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: 131.37 E-value: 3.86e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4798 CCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQRTGATSSCNRMRCPN 4877
Cdd:cd15664     1 CALCGVYGDDEPNDAGRLLYCGQDEWVHINCALWSAEVFEEDDGSLQNVHSAVSRGRMMKCELCGKPGATVGCCLKSCPA 80

                          90       100
                  ....*....|....*....|....*
gi 558137628 4878 VYHFACAIRAKCMFFKDKTMLCPMH 4902
Cdd:cd15664    81 NYHFMCARKAECVFQDDKKVFCPAH 105

SET_SETD1A

cd19204

SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...

5162-5303

1.22e-34

SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and similar proteins; SETD1A (EC2.1.1.43), also termed lysine N-methyltransferase 2F, or Set1/Ash2 histone methyltransferase complex subunit SET1, is a histone-lysine N-methyltransferase that specifically methylates 'Lys-4' of histone H3 (H3K4me), when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. Human SET domain containing protein 1A (hSETD1A) expression occurs at a high rate in hepatocellular carcinoma patients and controls tumor metastasis in breast cancer by activating MMP expression.

Pssm-ID: 380981 [Multi-domain] Cd Length: 153 Bit Score: 131.69 E-value: 1.22e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5162 KNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGI-YMFRINNEHVIDATLTGGPARYIN 5240
Cdd:cd19204    13 KKKLRFGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQVVADMREKRYVQEGIGSsYLFRVDHDTIIDATKCGNLARFIN 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 558137628 5241 HSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDqhKIPCHCGAWNCRKWMN 5303
Cdd:cd19204    93 HCCTPNCYAKVITIESQKKIVIYSKQPIGVNEEITYDYKFPIEDN--KIPCLCGTENCRGTLN 153

SET_SETD1B

cd19205

SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...

5162-5303

5.01e-34

SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and similar proteins; SETD1B (EC2.1.1.43), also termed lysine N-methyltransferase 2G, is a histone-lysine N-methyltransferase that specifically methylates 'Lys-4' of histone H3 (H3K4me) when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. Loss of SETD1B occurs in up to half the gastric and colorectal cancers, most commonly via SETD1B mutations, while de novo variants in SETD1B are associated with intellectual disability, epilepsy and autism.

Pssm-ID: 380982 [Multi-domain] Cd Length: 153 Bit Score: 130.18 E-value: 5.01e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5162 KNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGI-YMFRINNEHVIDATLTGGPARYIN 5240
Cdd:cd19205    13 KKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKRYEDEGIGSsYMFRVDHDTIIDATKCGNFARFIN 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 558137628 5241 HSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDqhKIPCHCGAWNCRKWMN 5303
Cdd:cd19205    93 HSCNPNCYAKVITVESQKKIVIYSKQHINVNEEITYDYKFPIEDV--KIPCLCGSENCRGTLN 153

PHD5_KMT2D

cd15601

PHD finger 5 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...

1233-1283

4.09e-33

Pssm-ID: 277074 Cd Length: 51 Bit Score: 123.48 E-value: 4.09e-33

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 558137628 1233 TCPICHAPYVEEDLLIQCRHCERWMHAGCESLFTEDDVEQAADEGFDCVSC 1283
Cdd:cd15601     1 TCPVCRAKYVEEDLLIQCRHCDRWVHAVCESLFTEDEVEQAADEGFDCSSC 51

PHD3_KMT2D

PHD finger 3 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...

1105-1155

7.91e-33

Pssm-ID: 277072 Cd Length: 51 Bit Score: 122.84 E-value: 7.91e-33

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 558137628 1105 DMCVVCGSFGRGAEGHLLACSQCSQCYHPYCVNSKITKVMLLKGWRCVECI 1155
Cdd:cd15597     1 DMCVVCGSFGRGSEGHLLACSQCSQCYHPYCVNSKITKVMLLKGWRCVECI 51

SET_SETD2

cd19172

SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...

5158-5302

4.67e-32

SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and similar proteins; SETD2 (also termed HIF-1, huntingtin yeast partner B, huntingtin-interacting protein 1 (HIP-1), huntingtin-interacting protein B, lysine N-methyltransferase 3A or protein-lysine N-methyltransferase SETD2) acts as histone-lysine N-methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using demethylated 'Lys-36' (H3K36me2) as substrate. It has been shown that methylation is a posttranslational modification of dynamic microtubules and that SETD2 methylates alpha-tubulin at lysine 40, the same lysine that is marked by acetylation on microtubules. Methylation of microtubules occurs during mitosis and cytokinesis and can be ablated by SETD2 deletion, which causes mitotic spindle and cytokinesis defects, micronuclei, and polyploidy.

Pssm-ID: 380949 [Multi-domain] Cd Length: 142 Bit Score: 123.85 E-value: 4.67e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5158 RTEWKnnvylarsriqGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYE-EQNRGIYMFRINNEHVIDATLTGGPA 5236
Cdd:cd19172     8 RTEKK-----------GWGLRAAEDLPKGTFVIEYVGEVLDEKEFKRRMKEYArEGNRHYYFMALKSDEIIDATKKGNLS 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 558137628 5237 RYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFD--FEDDQhkiPCHCGAWNCRKWM 5302
Cdd:cd19172    77 RFINHSCEPNCETQKWTVNGELRVGFFAKRDIPAGEELTFDYQFEryGKEAQ---KCYCGSPNCRGYI 141

SET

COG2940

SET domain-containing protein (function unknown) [General function prediction only];

5164-5301

9.04e-32

SET domain-containing protein (function unknown) [General function prediction only];

Pssm-ID: 442183 [Multi-domain] Cd Length: 134 Bit Score: 122.76 E-value: 9.04e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5164 NVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRgiYMFRINNEHVIDATLTGGPARYINHSC 5243
Cdd:COG2940     7 RIEVRPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKEPLHT--YLFELDDDGVIDGALGGNPARFINHSC 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 558137628 5244 APNCVAEVVTFD-----KEDkiiiissrrIPKGEELTYDYQFDFEDDQHkiPCHCGawNCRKW 5301
Cdd:COG2940    85 DPNCEADEEDGRifivaLRD---------IAAGEELTYDYGLDYDEEEY--PCRCP--NCRGT 134

FYRC

smart00542

FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...

5006-5093

1.13e-31

Pssm-ID: 197781 Cd Length: 86 Bit Score: 120.48 E-value: 1.13e-31

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628   5006 EFIIKVMEQGleDLVFTDASPQAVWNRIIEPVAAMRKEADMLRLFPEYLKGEELFGLTVHAVLRIAESLPGVESCQNYLF 5085
Cdd:smart00542    1 LFRVEIESDP--GEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNYWF 78


                    ....*...
gi 558137628   5086 RYGRHPLM 5093
Cdd:smart00542   79 RYHRSPLL 86

SET

smart00317

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...

5163-5285

3.95e-31

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on outlier plant homologues

Pssm-ID: 214614 [Multi-domain] Cd Length: 124 Bit Score: 120.52 E-value: 3.95e-31

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628   5163 NNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYE-EQNRGIYMFRINNEHVIDATLTGGPARYINH 5241
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDtDGAKAFYLFDIDSDLCIDARRKGNLARFINH 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 558137628   5242 SCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDD 5285
Cdd:smart00317   81 SCEPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124

ePHD_KMT2A

cd15693

Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant ...

4796-4906

1.87e-30

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: 118.18 E-value: 1.87e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4796 RRCCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQRTGATSSCNRMRC 4875
Cdd:cd15693     1 RQCALCLKYGDDSANDAGRLLYIGQNEWTHVNCALWSAEVFEDDDGSLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSC 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 558137628 4876 PNVYHFACAIRAKCMFFKDKTMLCPMHK--IKG 4906
Cdd:cd15693    81 TSNYHFMCSRAKNCVFLEDKKVYCQRHKdlIKG 113

SET_SETD2-like

cd10531

SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...

5164-5299

2.12e-30

SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), nuclear SETD2 (NSD2), ASH1-like protein (ASH1L) and similar proteins; This family includes SET domain-containing protein 2 (SETD2), nuclear SETD2 (NSD2) and ASH1-like protein (ASH1L), which function as histone-lysine N-methyltransferases. SETD2 specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using demethylated 'Lys-36' (H3K36me2) as substrate. NSD2 shows histone H3 'Lys-27' (H3K27me) methyltransferase activity. ASH1L specifically methylates 'Lys-36' of histone H3 (H3K36me). The family also includes Arabidopsis thaliana ASH1-related protein 3 (ASHR3) and similar proteins.

Pssm-ID: 380929 Cd Length: 136 Bit Score: 118.90 E-value: 2.12e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5164 NVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRR-EKIYEEQNRGIYMFRINNEHVIDATLTGGPARYINHS 5242
Cdd:cd10531     1 KLELFRTEKKGWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERlDEYEELGKSNFYILSLSDDVVIDATRKGNLSRFINHS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 558137628 5243 CAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQhKIPCHCGAWNCR 5299
Cdd:cd10531    81 CEPNCETQKWIVNGEYRIGIFALRDIPAGEELTFDYNFVNYNEA-KQVCLCGAQNCR 136

PHD4_KMT2C

cd15596

PHD finger 4 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...

1099-1154

2.12e-30

PHD finger 4 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 fourth PHD finger.

Pssm-ID: 277071 Cd Length: 57 Bit Score: 115.88 E-value: 2.12e-30

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 558137628 1099 KFVLMQDMCVVCGSFGRGAEGHLLACSQCSQCYHPYCVNSKITKVMLLKGWRCVEC 1154
Cdd:cd15596     1 KFTLNQDMCVVCGSFGQGAEGRLLACSQCGQCYHPYCVSIKITKVVLSKGWRCLEC 56

PHD5_KMT2C_like

PHD finger 5 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 4 found in ...

1156-1202

3.57e-29

Pssm-ID: 276988 Cd Length: 47 Bit Score: 112.18 E-value: 3.57e-29

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 558137628 1156 VCEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWCV 1202
Cdd:cd15513     1 VCEGCGKASDESRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWCV 47

SET_ASHR3-like

cd19175

SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...

5174-5302

4.40e-29

SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 (ASHR3) and similar proteins; This family includes Arabidopsis thaliana ASH1-related protein 3 (ASHR3, also termed protein SET DOMAIN GROUP 4 or protein stamen loss), ASH1 homolog 3 (ASHH3, also termed protein SET DOMAIN GROUP 7) and homolog 4 (ASHH4, also termed protein SET DOMAIN GROUP 24). They all function as histone-lysine N-methyltransferases (EC 2.1.1.43).

Pssm-ID: 380952 [Multi-domain] Cd Length: 139 Bit Score: 115.21 E-value: 4.40e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5174 GLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQ-NRGIYMFRINNEHVIDATLTGGPARYINHSCAPNCVAEVV 5252
Cdd:cd19175    11 GWGLVADEDINAGEFIIEYVGEVIDDKTCEERLWDMKHKgEKNFYMCEIDKDMVIDATFKGNLSRFINHSCDPNCELQKW 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 558137628 5253 TFDKEDKIIIISSRRIPKGEELTYDYQF-DFEDDQHkipCHCGAWNCRKWM 5302
Cdd:cd19175    91 QVDGETRIGVFAIRDIKKGEELTYDYQFvQFGADQD---CHCGSKNCRGKL 138

ePHD

cd15571

Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is ...

4798-4902

8.44e-29

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: 113.45 E-value: 8.44e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4798 CCFCHEEGdGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALM--NVEVALHRGLLTKCSLCQRT-GATSSCNRMR 4874
Cdd:cd15571     1 CALCPRSG-GALKGGGALKTTSDGLWVHVVCALWSPEVYFDDGTLLEveGVSKIPKRRKKLKCSICGKRgGACIQCSYPG 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 558137628 4875 CPNVYHFACAIRAKCMF-----FKDKTMLCPMH 4902
Cdd:cd15571    80 CPRSFHVSCAIRAGCLFefedgPGNFVVYCPKH 112

ePHD1_KMT2C

cd15696

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...

134-217

1.63e-28

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the first ePHD finger of KMT2C. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2C contains several PHD fingers, two ePHD fingers, an ATPase alpha beta signature, a high mobility group (HMG)-1 box, a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain and two FY (phenylalanine tyrosine)-rich domains.

Pssm-ID: 277166 Cd Length: 90 Bit Score: 111.96 E-value: 1.63e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  134 GSCWAHHWCAVWSAGVWGKGGPELCGVDKAIFSGISQRCSHCTRLGASIPCRSPGCPRLYHFPCATASGSFLSMKTLQLL 213
Cdd:cd15696     7 GECWAHLRCAEWSLGVCQGEEQLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQDFSRRLLL 86


                  ....
gi 558137628  214 CPEH 217
Cdd:cd15696    87 CPTH 90

PHD4_KMT2C_like

cd15512

PHD finger 4 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD domain 3 found in ...

1106-1154

2.70e-28

PHD finger 4 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD domain 3 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, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, two extended PHD (ePHD) fingers, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions. This model corresponds to the fourth PHD finger of KMT2C and the third domain of KMT2D.

Pssm-ID: 276987 Cd Length: 49 Bit Score: 109.86 E-value: 2.70e-28

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 558137628 1106 MCVVCGSFGRGAEGHLLACSQCSQCYHPYCVNSKITKVMLLKGWRCVEC 1154
Cdd:cd15512     1 MCVSCGSFGRGAEGRLIACSQCGQCYHPYCVNVKVTKVILSKGWRCLDC 49

SET_EZH

cd10519

SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...

5165-5280

7.52e-28

SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar proteins; The family includes EZH1 and EZH2. EZH1 (EC 2.1.1.43; also termed ENX-2, or histone-lysine N-methyltransferase EZH1) is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. EZH2 (EC 2.1.1.43; also termed lysine N-methyltransferase 6, ENX-1, or histone-lysine N-methyltransferase EZH2) is a catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Both, EZH1 and EZH2, can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively.

Pssm-ID: 380917 Cd Length: 117 Bit Score: 110.80 E-value: 7.52e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5165 VYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGiYMFRINNEHVIDATLTGGPARYINHSCA 5244
Cdd:cd10519     3 LLLGKSDVAGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGKIYDKYNSS-YLFNLNDQFVVDATRKGNKIRFANHSSN 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 558137628 5245 PNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQF 5280
Cdd:cd10519    82 PNCYAKVMMVNGDHRIGIFAKRDIEAGEELFFDYGY 117

PHD2_KMT2D

PHD finger 2 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...

275-320

8.29e-28

Pssm-ID: 277070 Cd Length: 46 Bit Score: 108.16 E-value: 8.29e-28

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  275 VCQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15595     1 VCQTCRKPGEDSKMLVCEACDKGYHTFCLKPAMESLPTDSWKCKAC 46

SET_NSD

cd19173

SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...

5174-5298

7.68e-27

SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, NSD2, NSD3 and similar proteins; The nuclear receptor-binding SET Domain (NSD) family of histone H3 lysine 36 methyltransferases is comprised of NSD1, NSD2, and NSD3, which are primarily known to be involved in chromatin integrity and gene expression through mono-, di-, or tri-methylating lysine 36 of histone H3 (H3K36), respectively. NSD1 (EC 2.1.1.43; also termed histone-lysine N-methyltransferase H3 lysine-36 and H4 lysine-20 specific, androgen receptor coactivator 267 kDa protein (ARA267), androgen receptor-associated protein of 267 kDa, H3-K36-HMTase, H4-K20-HMTase, lysine N-methyltransferase 3B (KMT3B) or NR-binding SET domain-containing protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4. NSD2 (EC 2.1.1.43; also termed multiple myeloma SET domain-containing protein (MMSET), protein trithorax-5 (TRX5), or wolf-Hirschhorn syndrome candidate 1 protein (WHSC1)) acts as histone-lysine N-methyltransferase with histone H3 'Lys-27' (H3K27me) methyltransferase activity. NSD3 (EC 2.1.1.43; also termed protein whistle, WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1L1), or WHSC1-like protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-4' and 'Lys-27' of histone H3.

Pssm-ID: 380950 [Multi-domain] Cd Length: 142 Bit Score: 108.94 E-value: 7.68e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5174 GLGLYAAKDLEKHTMVIEYIGTIIRNEVANRR-EKIYEEQNRGIYMFRINNEHVIDATLTGGPARYINHSCAPNCVAEVV 5252
Cdd:cd19173    13 GWGLRTKRDIKKGDFVIEYVGELIDEEECRRRlKKAHENNITNFYMLTLDKDRIIDAGPKGNLSRFMNHSCQPNCETQKW 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628 5253 TFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQhKIPCHCGAWNC 5298
Cdd:cd19173    93 TVNGDTRVGLFAVRDIPAGEELTFNYNLDCLGNE-KKVCRCGAPNC 137

PHD6_KMT2C_like

cd15514

PHD finger 6 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 5 found in ...

1233-1283

2.06e-26

PHD finger 6 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 5 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, 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 sixth PHD finger of KMT2C and the fifth PHD finger of KMT2D.

Pssm-ID: 276989 Cd Length: 51 Bit Score: 104.29 E-value: 2.06e-26

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 558137628 1233 TCPICHAPYVEEDLLIQCRHCERWMHAGCESLFTEDDVEQAADEGFDCVSC 1283
Cdd:cd15514     1 KCPVCSRSYNEGELIIQCSQCERWLHGACDSLRTEEEAERAADNGYRCLLC 51

PHD2_KMT2C_like

cd15510

PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...

275-320

3.38e-26

PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (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 plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, a RING finger, an HMG (high-mobilitygroup)-binding motif, and two FY-rich regions. This model corresponds to the second PHD finger.

Pssm-ID: 276985 Cd Length: 46 Bit Score: 103.67 E-value: 3.38e-26

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  275 VCQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15510     1 VCQACRQPGDDTKMLVCETCDKGYHTSCLRPVMSSIPKYGWKCKNC 46

ePHD_KMT2B

cd15694

Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant ...

4798-4902

4.11e-26

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: 105.51 E-value: 4.11e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4798 CCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQRTGATSSCNRMRCPN 4877
Cdd:cd15694     1 CALCLKYGDADSKDAGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCEHCQKIGATVGCCLSACLS 80

                          90       100
                  ....*....|....*....|....*
gi 558137628 4878 VYHFACAIRAKCMFFKDKTMLCPMH 4902
Cdd:cd15694    81 NFHFMCARASRCCFQDDKKVFCQKH 105

FYRC

pfam05965

F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...

5004-5088

1.20e-25

F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It is similar to SMART:SM00542.

Pssm-ID: 461788 Cd Length: 83 Bit Score: 103.46 E-value: 1.20e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  5004 RPEFIIKVMEQglEDLVFTDASPQAVWNRIIEPVAAMRKEADMLRLFPEYLKGEELFGLTVHAVLRIAESLPGVESCQNY 5083
Cdd:pfam05965    1 GPLFRVTVEED--PDESFEGSSPTKCWSMVLERVQELRREAGLKLKLPESISGEDMFGLTHPAVVRLIESLPGAEKCTNY 78


                   ....*
gi 558137628  5084 LFRYG 5088
Cdd:pfam05965   79 KFRYG 83

SET_SUV39H

cd10542

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...

5174-5302

8.27e-24

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 homologs, SUV39H1, SUV39H2 and similar proteins; This family includes SUV39H1 (also termed histone H3-K9 methyltransferase 1, H3-K9-HMTase 1, lysine N-methyltransferase 1A, KMT1A, position-effect variegation 3-9 homolog, SUV39H, or Su(var)3-9 homolog 1) and SUV39H2 (also termed histone H3-K9 methyltransferase 2, H3-K9-HMTase 2, lysine N-methyltransferase 1B, KMT1B, or Su(var)3-9 homolog 2), both act as histone-lysine N-methyltransferases that specifically trimethylate 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. They mainly function in heterochromatin regions, thereby playing central roles in the establishment of constitutive heterochromatin at pericentric and telomere regions. Also included are Schizosaccharomyces pombe H3K9 methyltransferase Clr4 (SUV39H homolog) and Neurospora crassa DIM-5, both of which also methylate 'Lys-9' of histone H3.

Pssm-ID: 380940 [Multi-domain] Cd Length: 245 Bit Score: 103.91 E-value: 8.27e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5174 GLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRgIYMFRIN-----NEHVIDATLTGGPARYINHSCAPN-- 5246
Cdd:cd10542    99 GWGVKTLEDIKKGTFVMEYVGEIITSEEAERRGKIYDANGR-TYLFDLDyndddCEYTVDAAYYGNISHFINHSCDPNla 177

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 558137628 5247 ---CVAE--------VVTFDKEDkiiiissrrIPKGEELTYDYQFDFEDDQH----------KIPCHCGAWNCRKWM 5302
Cdd:cd10542   178 vyaVWINhldprlprIAFFAKRD---------IKAGEELTFDYLMTGTGGSSestipkpkdvRVPCLCGSKNCRKYL 245

PHD2_KMT2C

cd15594

PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...

275-320

3.61e-23

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: 95.01 E-value: 3.61e-23

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  275 VCQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15594     1 VCQTCRQPGDDNKMLVCDTCDKGYHTFCLQPVMTTIPKNGWKCKNC 46

SET_ASH1L

cd19174

SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...

5174-5303

4.30e-22

SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ASH1L (EC 2.1.1.43; also termed absent small and homeotic disks protein 1 homolog, KMT2H, or lysine N-methyltransferase 2H) acts as histone-lysine N-methyltransferase that specifically methylates 'Lys-36' of histone H3 (H3K36me). It plays important roles in development; heterozygous mutation of ASH1L is associated with severe intellectual disability (ID) and multiple congenital anomaly (MCA).

Pssm-ID: 380951 [Multi-domain] Cd Length: 141 Bit Score: 95.44 E-value: 4.30e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5174 GLGLYAAKDLEKHTMVIEYIGTII-RNEVANRREKIYEeQNRGIYMFRINNEHVIDATLTGGPARYINHSCAPNC----- 5247
Cdd:cd19174    11 GWGVRTKEPIKAGQFIIEYVGEVVsEQEFRRRMIEQYH-NHSHHYCLNLDSGMVIDGYRMGNEARFVNHSCDPNCemqkw 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5248 ----VAEVVTFDKEDkiiiissrrIPKGEELTYDYQFDFEDDQHKIPCHCGAWNCRKWMN 5303
Cdd:cd19174    90 svngVYRIGLFALKD---------IPAGEELTYDYNFHSFNVEKQQPCKCGSPNCRGVIG 140

PHD6_KMT2C

cd15600

PHD finger 6 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...

1233-1283

5.87e-22

PHD finger 6 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 sixth PHD finger.

Pssm-ID: 277073 Cd Length: 51 Bit Score: 91.91 E-value: 5.87e-22

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 558137628 1233 TCPICHAPYVEEDLLIQCRHCERWMHAGCESLFTEDDVEQAADEGFDCVSC 1283
Cdd:cd15600     1 TCPICYRNYREEELILQCRQCDRWMHASCQNLNTEEEVENAADNGFDCTMC 51

PHD1_KMT2C_like

PHD finger 1 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...

228-273

8.55e-22

Pssm-ID: 276984 Cd Length: 48 Bit Score: 91.22 E-value: 8.55e-22

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 558137628  228 RCAVCEGPGELCDLFFCTSCGHHYHGACLDTAL--TARKRAGWQCPEC 273
Cdd:cd15509     1 NCAVCDSPGDLSDLLFCTSCGQHYHGSCLDPAVrpTPLVRAGWQCPEC 48

ePHD

cd15571

Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is ...

129-217

2.79e-21

Pssm-ID: 277046 [Multi-domain] Cd Length: 112 Bit Score: 91.88 E-value: 2.79e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  129 LGEPGGSCWAHHWCAVWSAGVW--GKGGPELCGVDKAIFSGISQRCSHC-TRLGASIPCRSPGCPRLYHFPCATASGSFL 205
Cdd:cd15571    17 LKTTSDGLWVHVVCALWSPEVYfdDGTLLEVEGVSKIPKRRKKLKCSICgKRGGACIQCSYPGCPRSFHVSCAIRAGCLF 96

                          90
                  ....*....|....*.
gi 558137628  206 SMKT----LQLLCPEH 217
Cdd:cd15571    97 EFEDgpgnFVVYCPKH 112

SET

pfam00856

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...

5174-5278

5.43e-21

Pssm-ID: 459965 [Multi-domain] Cd Length: 115 Bit Score: 91.43 E-value: 5.43e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  5174 GLGLYAAKDLEKHTMVIEYIGT-IIRNEVANRREKIYEEQNR----GIYMFRIN--NEHVIDATLT--GGPARYINHSCA 5244
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLElrlwGPYLFTLDedSEYCIDARALyyGNWARFINHSCD 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 558137628  5245 PNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDY 5278
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDY 114

ePHD1_KMT2C_like

cd15665

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...

4798-4902

5.70e-20

Pssm-ID: 277135 Cd Length: 90 Bit Score: 87.38 E-value: 5.70e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4798 CCFCheegdgatdgparllNLDlDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQRTGATSSCNRMRCPN 4877
Cdd:cd15665     1 CALC---------------NLG-EVYAHHCCAAWSEGVCQTEDGALENVDKAVAKALSQKCSFCLRYGASISCRMPSCSK 64

                          90       100
                  ....*....|....*....|....*..
gi 558137628 4878 VYHFACAIRAKCmF--FKDKTMLCPMH 4902
Cdd:cd15665    65 SFHFPCAAAAGC-FqdIKTLTLFCPEH 90

ePHD2_KMT2C_like

cd15666

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...

137-217

2.98e-19

Pssm-ID: 277136 Cd Length: 105 Bit Score: 85.82 E-value: 2.98e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  137 WAHHWCAVWSAGVWGKGGPELCGVDKAIFSGISQRCSHCTRLGASIPCRSPGCPRLYHFPCATASG-SFLSMKTlqLLCP 215
Cdd:cd15666    26 WVHLNCALWSYEVYETQNGALMNVEEALRRALTTTCSHCGRTGATVPCFKPRCANVYHLPCAIKDGcMFFKDKT--MLCP 103


                  ..
gi 558137628  216 EH 217
Cdd:cd15666   104 SH 105

SET_NSD2

cd19211

SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...

5167-5298

3.93e-19

SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) and similar proteins; NSD2 (EC 2.1.1.43; also termed multiple myeloma SET domain-containing protein (MMSET), protein trithorax-5 (TRX5), or wolf-Hirschhorn syndrome candidate 1 protein (WHSC1)) acts as histone-lysine N-methyltransferase with histone H3 'Lys-36' (H3K36me) methyltransferase activity. NSD2 has been shown to mediate di- and trimethylation of H3K36 and dimethylation of H4K20 in different systems, and has been characterized as a transcriptional repressor interacting with histone deacetylase HDAC1 and histone demethylase LSD1. NSD2 mediates constitutive NF-kappaB signaling for cancer cell proliferation, survival and tumor growth. It is highly overexpressed in several types of human cancers, including small-cell lung cancers, neuroblastoma, carcinomas of stomach and colon, and bladder cancers, and its overexpression tends to be associated with tumor aggressiveness. WHSC1 is frequently deleted in Wolf-Hirschhorn syndrome (WHS).

Pssm-ID: 380988 [Multi-domain] Cd Length: 142 Bit Score: 86.97 E-value: 3.93e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5167 LARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQN-RGIYMFRINNEHVIDATLTGGPARYINHSCAP 5245
Cdd:cd19211     6 IIKTEGKGWGLIAKRDIKKGEFVNEYVGELIDEEECMARIKHAHENDiTHFYMLTIDKDRIIDAGPKGNYSRFMNHSCQP 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 558137628 5246 NCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIpCHCGAWNC 5298
Cdd:cd19211    86 NCETQKWTVNGDTRVGLFAVCDIPAGTELTFNYNLDCLGNEKTV-CRCGAPNC 137

SET_EZH2

cd19218

SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...

5161-5280

7.56e-19

SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43), also termed lysine N-methyltransferase 6, or ENX-1, or histone-lysine N-methyltransferase EZH2, is a catalytic subunit of the polycomb repressive complex 2 (PRC2)/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. It can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. PRC2 is involved in several cancers; EZH2 is overexpressed in breast, liver and prostate cancer, while point mutations in EZH2 alter the substrate preference and product specificity of PRC2 in Non-Hodgkin lymphomas (NHLs). Thus, PRC2 is a popular target for cancer therapeutics.

Pssm-ID: 380995 Cd Length: 120 Bit Score: 85.35 E-value: 7.56e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5161 WKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEqnrgiYM----FRINNEHVIDATLTGGPA 5236
Cdd:cd19218     2 SKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDK-----YMcsflFNLNNDFVVDATRKGNKI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 558137628 5237 RYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQF 5280
Cdd:cd19218    77 RFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRY 120

FYRN

pfam05964

F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...

4947-4998

3.47e-18

F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It is similar to SMART:SM00541.

Pssm-ID: 461787 Cd Length: 51 Bit Score: 81.01 E-value: 3.47e-18

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 558137628  4947 GGLVFHAIGQLLPHQMAdFHSATALYPVGYEATRIYWSLRTNNRRCCYRCSI 4998
Cdd:pfam05964    1 GSLTVLSLGEIVPDRPA-FHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51

SET_EZH1

cd19217

SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...

5162-5284

6.98e-18

SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43), also termed ENX-2, or histone-lysine N-methyltransferase EZH1, is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. It can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively.

Pssm-ID: 380994 Cd Length: 136 Bit Score: 83.19 E-value: 6.98e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5162 KNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGiYMFRINNEHVIDATLTGGPARYINH 5241
Cdd:cd19217     5 KKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYDKYMSS-FLFNLNNDFVVDATRKGNKIRFANH 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 558137628 5242 SCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFED 5284
Cdd:cd19217    84 SVNPNCYAKVVMVNGDHRIGIFAKRAIQQGEELFFDYRYSQAD 126

ePHD_RAI1_like

cd15668

Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 ...

4798-4902

9.64e-18

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: 81.58 E-value: 9.64e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4798 CCFC----HEEGDGATDGPArllnldLDLWVHLNCALWSTEVYETqGGALMNVEVALHRGLLTKCSLCQRTGATSSCNRM 4873
Cdd:cd15668     1 CVFCkrgpHYKGLGDLFGPY------YEVWVHEDCAVWAPGVYLV-GGKLYGLEEAVWVAKQSVCSSCQQTGATIGCLHK 73

                          90       100       110
                  ....*....|....*....|....*....|
gi 558137628 4874 RCPNVYHFACAIRAKCMFFKDK-TMLCPMH 4902
Cdd:cd15668    74 GCKAKYHYPCAVESGCQLDEENfSLLCPKH 103

SET_NSD3

cd19212

SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...

5173-5298

2.67e-17

SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing protein 3 (NSD3) and similar proteins; NSD3 (EC 2.1.1.43; also termed protein whistle, WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1L1), or WHSC1-like protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-4' and 'Lys-27' of histone H3. NSD3 is amplified and overexpressed in multiple cancer types, including acute myeloid leukemia (AML), breast, lung, pancreatic and bladder cancers, as well as squamous cell carcinoma of the head and neck (SCCHN). NSD3 contributes to tumorigenesis by interacting with bromodomain-containing protein 4 (BRD4), the bromodomain and extraterminal (BET) protein, which is a potential therapeutic target in acute myeloid leukemia (AML). NSD3 is amplified in primary tumors and cell lines from breast carcinoma, and can promote the cell viability of small-cell lung cancer and pancreatic ductal adenocarcinoma. High NSD3 expression is implicated in poor grade and heavy smoking history in SCCHN. Thus, NSD3 may serve as a potential druggable target for selective cancer therapy.

Pssm-ID: 380989 [Multi-domain] Cd Length: 142 Bit Score: 81.90 E-value: 2.67e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5173 QGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQN-RGIYMFRINNEHVIDATLTGGPARYINHSCAPNCVAEV 5251
Cdd:cd19212    12 RGWGLRTKRSIKKGEFVNEYVGELIDEEECRLRIKRAHENSvTNFYMLTVTKDRIIDAGPKGNYSRFMNHSCNPNCETQK 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 558137628 5252 VTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIpCHCGAWNC 5298
Cdd:cd19212    92 WTVNGDVRVGLFALCDIPAGMELTFNYNLDCLGNGRTE-CHCGADNC 137

SET_SETDB-like

cd10538

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...

5169-5279

4.51e-17

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) and 2 (SETDB2), suppressor of variegation 3-9 homologs, SUV39H1 and SUV39H2, euchromatic histone-lysine N-methyltransferase EHMT1 and EHMT2, and similar proteins; The family includes SET domain bifurcated 1 (SETDB1) and 2 (SETDB2), suppressor of variegation 3-9 homologs, SUV39H1 and SUV39H2, euchromatic histone-lysine N-methyltransferase EHMT1 and EHMT2. SETDB1 (EC 2.1.1.43; also termed ERG-associated protein with SET domain (ESET), histone H3-K9 methyltransferase 4, H3-K9-HMTase 4, or lysine N-methyltransferase 1E (KMT1E)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. SETDB2 (EC 2.1.1.43; also termed chronic lymphocytic leukemia deletion region gene 8 protein (CLLD8), or lysine N-methyltransferase 1F (KMT1F)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It is involved in left-right axis specification in early development and mitosis. SUV39H1 (also termed histone H3-K9 methyltransferase 1, H3-K9-HMTase 1, lysine N-methyltransferase 1A, KMT1A, position-effect variegation 3-9 homolog, SUV39H, or Su(var)3-9 homolog 1) and SUV39H2 (also termed histone H3-K9 methyltransferase 2, H3-K9-HMTase 2, lysine N-methyltransferase 1B, KMT1B, or Su(var)3-9 homolog 2), both act as histone-lysine N-methyltransferases that specifically trimethylate 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. They mainly function in heterochromatin regions, thereby playing central roles in the establishment of constitutive heterochromatin at pericentric and telomere regions. EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, lysine N-methyltransferase 1D, or KMT1D) and EHMT2 (also termed Eu-HMTase2, HLA-B-associated transcript 8, histone H3-K9 methyltransferase 3, H3-K9-HMTase 3, lysine N-methyltransferase 1C, KMT1C, or protein G9a), both act as histone-lysine N-methyltransferases that specifically mono- and dimethylate 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. This family also includes the pre-SET domain, which is found in a number of histone methyltransferases (HMTase), N-terminal to the SET domain. Pre-SET domain is a zinc binding motif which contains 9 conserved cysteines that coordinate three zinc ions. It is thought that this region plays a structural role in stabilizing SET domains. Most family members, except for Arabidopsis thaliana SUVH9, contain a post-SET domain which harbors a zinc-binding site.

Pssm-ID: 380936 [Multi-domain] Cd Length: 217 Bit Score: 83.57 E-value: 4.51e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5169 RSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEeQNRGIYMFRINN---------EHVIDATLTGGPARYI 5239
Cdd:cd10538    95 RTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRGKIYD-KSGGSYLFDLDEfsdsdgdgeELCVDATFCGNVSRFI 173

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 558137628 5240 NHSCAPNCVAEVVTFDKEDKIIII----SSRRIPKGEELTYDYQ 5279
Cdd:cd10538   174 NHSCDPNLFPFNVVIDHDDLRYPRialfATRDILPGEELTFDYG 217

ePHD_RAI1_like

cd15668

Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 ...

137-217

1.12e-16

Pssm-ID: 277138 Cd Length: 103 Bit Score: 78.50 E-value: 1.12e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  137 WAHHWCAVWSAGVWGKGGpELCGVDKAIFSGISQRCSHCTRLGASIPCRSPGCPRLYHFPCATASGSFLSMKTLQLLCPE 216
Cdd:cd15668    24 WVHEDCAVWAPGVYLVGG-KLYGLEEAVWVAKQSVCSSCQQTGATIGCLHKGCKAKYHYPCAVESGCQLDEENFSLLCPK 102


                  .
gi 558137628  217 H 217
Cdd:cd15668   103 H 103

FYRN

smart00541

FY-rich domain, N-terminal region; is sometimes closely juxtaposed with the C-terminal region ...

4957-5000

2.23e-16

Pssm-ID: 128814 Cd Length: 44 Bit Score: 75.78 E-value: 2.23e-16

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 558137628   4957 LLPHQMADFHSATALYPVGYEATRIYWSLRTNNRRCCYRCSIGE 5000
Cdd:smart00541    1 LLPIQGKLFHSESAIFPVGYKSTRKYWSVKDPNRRCLYSCVIDE 44

SET_NSD1

cd19210

SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...

5165-5298

2.77e-16

SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and similar proteins; NSD1 (EC 2.1.1.43; also termed Histone-lysine N-methyltransferase H3 lysine-36 and H4 lysine-20 specific, androgen receptor coactivator 267 kDa protein (ARA267), androgen receptor-associated protein of 267 kDa, H3-K36-HMTase, H4-K20-HMTase, lysine N-methyltransferase 3B (KMT3B), or NR-binding SET domain-containing protein 1) functions as a histone-lysine N-methyltransferase that preferentially methylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4. NSD1 is altered in approximately 10% of head and neck cancer patients with 55% decrease in risk of death in NSD1-mutated versus non-mutated patients; its disruption promotes favorable chemotherapeutic responses linked to hypomethylation.

Pssm-ID: 380987 [Multi-domain] Cd Length: 142 Bit Score: 78.82 E-value: 2.77e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5165 VYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQN-RGIYMFRINNEHVIDATLTGGPARYINHSC 5243
Cdd:cd19210     4 VEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDiTNFYMLTLDKDRIIDAGPKGNYARFMNHCC 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 558137628 5244 APNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQhKIPCHCGAWNC 5298
Cdd:cd19210    84 QPNCETQKWTVNGDTRVGLFALCDIKAGTELTFNYNLECLGNG-KTVCKCGAPNC 137

PHA03247

large tegument protein UL36; Provisional

1834-2403

4.21e-16

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 86.92 E-value: 4.21e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1834 PPQPGALGSPPPAAAPTIFIGSPTTP---------AGLSTSADGFLKPPAGTVPGPDSPGElflKLPPQVPAQVPSQdpf 1904
Cdd:PHA03247 2506 PDAPPAPSRLAPAILPDEPVGEPVHPrmltwirglEELASDDAGDPPPPLPPAAPPAAPDR---SVPPPRPAPRPSE--- 2579

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1905 glaPAYALEPRFPtapstyppypspaGAPVQPptlgtsSRPGTgqPGEFHTTPPGTPRHQPSTPDPFlKPRCPSLDNLAV 1984
Cdd:PHA03247 2580 ---PAVTSRARRP-------------DAPPQS------ARPRA--PVDDRGDPRGPAPPSPLPPDTH-APDPPPPSPSPA 2634

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1985 PESPGVGGGKASEPLLSP-----PPFGESRKALEVKKEELGASSPSYGPPNLGFvdSPSSGPHLGSLELKAPDVFKAPLT 2059
Cdd:PHA03247 2635 ANEPDPHPPPTVPPPERPrddpaPGRVSRPRRARRLGRAAQASSPPQRPRRRAA--RPTVGSLTSLADPPPPPPTPEPAP 2712

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2060 PRASQVEPQSPGLGLRPQEPSPAQALAPSPPSHSDIFRPGPYPDPYAQPPLTPRPQPPAPESCCALPPRSLPSDPFSRVP 2139
Cdd:PHA03247 2713 HALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLS 2792

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2140 ASPQSQSSSQSpltPRPLSAEAFCPSPVTPRFQSPDPYSRPPSRPQSRDPFAPLHKPPRPQPPEVAFK-SGPLAH--TPL 2216
Cdd:PHA03247 2793 ESRESLPSPWD---PADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVApGGDVRRrpPSR 2869

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2217 GAGGFPAALPSGPAGELHAKVPSGQPPNFARSPgtgafvgtPSPMRFTFPQAVGEPSSLKPPVPQPGLPPPHginshfgP 2296
Cdd:PHA03247 2870 SPAAKPAAPARPPVRRLARPAVSRSTESFALPP--------DQPERPPQPQAPPPPQPQPQPPPPPQPQPPP-------P 2934

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2297 GPTLGKPQSTNYSVATGNFHPSGSPLGPSSGSTGEGYGLSPLRPQSVLPPPVPDGSLPYPPHGASQRAGITSpvdkredp 2376
Cdd:PHA03247 2935 PPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSS-------- 3006

                         570       580
                  ....*....|....*....|....*..
gi 558137628 2377 gagMAGSLAAPELPgtqDPGISSLSQT 2403
Cdd:PHA03247 3007 ---WASSLALHEET---DPPPVSLKQT 3027

ePHD_RAI1

cd15700

Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant ...

126-217

4.59e-16

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: 76.84 E-value: 4.59e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  126 PAHLGEPGGSC-------WAHHWCAVWSAGVWGKGGpELCGVDKAIFSGISQRCSHCTRLGASIPCRSPGCPRLYHFPCA 198
Cdd:cd15700     7 PANYKDLGDLCgpyypehWVHEACAVWTTGVYLVAG-KLFGLQEAVQKAADAKCSSCQGAGATVGCCHKGCTQSYHYICA 85

                          90
                  ....*....|....*....
gi 558137628  199 TASGSFLSMKTLQLLCPEH 217
Cdd:cd15700    86 VEAGCLFEEENFSLRCPKH 104

PHD2_KMT2C

cd15594

PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...

1156-1201

1.71e-15

Pssm-ID: 277069 Cd Length: 46 Bit Score: 73.43 E-value: 1.71e-15

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628 1156 VCEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15594     1 VCQTCRQPGDDNKMLVCDTCDKGYHTFCLQPVMTTIPKNGWKCKNC 46

SET_SUV39H_Clr4-like

cd20073

SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 ...

5173-5302

5.89e-15

SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 methyltransferase Clr4, and similar proteins; This subfamily contains fission yeast Schizosaccharomyces pombe H3K9 methyltransferase Clr4 (also known as Suv39h), the sole homolog of the mammalian SUV39H1 and SUV39H2 enzymes, that has a critical role in preventing aberrant heterochromatin formation. It is known to di- and tri-methylate Lys-9 of histone H3, a central heterochromatic histone modification, with its specificity profile most similar to that of the human SUV39H2 homolog.

Pssm-ID: 380999 [Multi-domain] Cd Length: 259 Bit Score: 78.38 E-value: 5.89e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5173 QGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEeqNRGI-YMF-------RINNEHVIDATLTGGPARYINHSCA 5244
Cdd:cd20073   103 KGWGLRCPRFIKAGTFIGVYLGEVITQSEAEIRGKKYD--NVGVtYLFdldlfedQVDEYYTVDAQYCGDVTRFINHSCD 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 558137628 5245 PNCVAEVVTFDKEDKIIIISS----RRIPKGEELTYDYQFDFEDDQ----------------HKIPCHCGAWNCRKWM 5302
Cdd:cd20073   181 PNLAIYSVLRDKSDSKIYDLAffaiKDIPALEELTFDYSGRNNFDQlgfignrsnskyinlkNKRPCYCGSANCRGWL 258

SET_SETD8

cd10528

SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2. ...

5171-5278

7.00e-15

SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2.1.1.43; also termed N-lysine methyltransferase KMT5A, H4-K20-HMTase KMT5A, lysine N-methyltransferase 5A, lysine-specific methylase 5A, PR/SET domain-containing protein 07, PR-Set7 or PR/SET07) is a nucleosomal histone-lysine N-methyltransferase that specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). It plays a central role in the silencing of euchromatic genes.

Pssm-ID: 380926 [Multi-domain] Cd Length: 141 Bit Score: 74.54 E-value: 7.00e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5171 RIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEE-QNRGIYM--FRINNE-HVIDATL-TGGPARYINHSC-A 5244
Cdd:cd10528    25 DGKGRGVIATRPFEKGDFVVEYHGDLITITEAKKREALYAKdPSTGCYMyyFQYKGKtYCVDATKeSGRLGRLINHSKkK 104

                          90       100       110
                  ....*....|....*....|....*....|....
gi 558137628 5245 PNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDY 5278
Cdd:cd10528   105 PNLKTKLLVIDGVPHLILVAKRDIKPGEELLYDY 138

PHA03247

large tegument protein UL36; Provisional

1844-2510

7.15e-15

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 82.68 E-value: 7.15e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1844 PPAAAPTIFIGSPTTP------------AGLSTSADGFLkppAGTVPG-PDSPGELFLKLPPQVPA-QVPSQDPFGLAPA 1909
Cdd:PHA03247 2417 PPGPPDVRFVGSEEIEelpfvspggdvlAGLAADGDPFF---ARTILGaPFSLSLLLGELFPGAPVyRRPAEARFPFAAG 2493

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1910 YALEPrfptapstyppYPSPAGAPVQPPTlgtssrPGTGQPGEFHTTPPGTPRHqpstpdPFLKPRCPSLDNLAvpeSPG 1989
Cdd:PHA03247 2494 AAPDP-----------GGGGPPDPDAPPA------PSRLAPAILPDEPVGEPVH------PRMLTWIRGLEELA---SDD 2547

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1990 VGGGKASEPLLSPPPfgesrkalevkkeelgASSPSYGPPNLGfvdSPSSGPHLGSLELKaPDVFKAPLTPRASqVEPQS 2069
Cdd:PHA03247 2548 AGDPPPPLPPAAPPA----------------APDRSVPPPRPA---PRPSEPAVTSRARR-PDAPPQSARPRAP-VDDRG 2606

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2070 PGLGLRPQEPSPAQALAPSPPSHSDIFRPGPYPDPYAQPPLTPRPQPPAPESCCALPPRslpsdpfsRVPASPQSQSSSQ 2149
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPR--------RARRLGRAAQASS 2678

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2150 SPLTPRPLSAEAFCpSPVTPRFQSPDPYSRPPSRPQSRDPFAPLhkPPRPQPPEVAFKSGPLAHTPLGaggfPAALPSGP 2229
Cdd:PHA03247 2679 PPQRPRRRAARPTV-GSLTSLADPPPPPPTPEPAPHALVSATPL--PPGPAAARQASPALPAAPAPPA----VPAGPATP 2751

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2230 AGElhAKVPSGQPPNFARSPGTGAFVGTPSPMRFTFPQAVGEPSSLKPPvpqpglppphginshfgPGPTLGKPQSTNYS 2309
Cdd:PHA03247 2752 GGP--ARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESL-----------------PSPWDPADPPAAVL 2812

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2310 VATGNFHPSGSPLGPSSGSTgEGYGLSPLRPQSVLPPPVPDGSLPYPPHGASQRAGITSPVDKREDPGAGMAGSLAAPEL 2389
Cdd:PHA03247 2813 APAAALPPAASPAGPLPPPT-SAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAV 2891

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2390 PgtqdPGISSLSQTELEKQRQRQrlrellirQQIQRNTLRQEKETAAAAAGavgppgnwgtepsnPAFEQLSRGQTPFAG 2469
Cdd:PHA03247 2892 S----RSTESFALPPDQPERPPQ--------PQAPPPPQPQPQPPPPPQPQ--------------PPPPPPPRPQPPLAP 2945

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....
gi 558137628 2470 TQDKSSLGLPSNKLGGPILG---PGAFPSDDRLSRPPPPATPSS 2510
Cdd:PHA03247 2946 TTDPAGAGEPSGAVPQPWLGalvPGRVAVPRFRVPQPAPSREAP 2989

PHD_BAZ1A

cd15627

PHD finger found in bromodomain adjacent to zinc finger domain protein 1A (BAZ1A); BAZ1A, also ...

276-320

7.54e-15

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: 71.27 E-value: 7.54e-15

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628  276 CQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15627     2 CRICRRKGDAEKMLLCDGCDRGHHMYCLRPPLKKVPEGDWFCPDC 46

PHD_BAZ2A_like

cd15545

PHD finger found in bromodomain adjacent to zinc finger domain protein 2A (BAZ2A) and 2B ...

276-320

7.90e-15

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: 71.19 E-value: 7.90e-15

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628  276 CQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15545     2 CQICRSGDNEDQLLLCDGCDRGYHTYCFKPKMTNVPEGDWFCPEC 46

PHD1_KDM5B

cd15603

PHD finger 1 found in lysine-specific demethylase 5B (KDM5B); KDM5B (also termed Cancer/testis ...

1156-1201

1.29e-14

PHD finger 1 found in lysine-specific demethylase 5B (KDM5B); KDM5B (also termed Cancer/testis antigen 31 (CT31), Histone demethylase JARID1B, Jumonji/ARID domain-containing protein 1B (JARID1B), PLU-1, or retinoblastoma-binding protein 2 homolog 1 (RBP2-H1 or RBBP2H1A)) is a member of the JARID subfamily within the JmjC proteins. It has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of pregnant females and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. KDM5B acts as a histone demethylase that catalyzes the removal of trimethylation of lysine 4 on histone H3 (H3K4me3), induced by polychlorinated biphenyls (PCBs). It also mediates demethylation of H3K4me2 and H3K4me1. Moreover, KDM5B functions as a negative regulator of hematopoietic stem cell (HSC) self-renewal and progenitor cell activity. KDM5B has also been shown to interact with the DNA binding transcription factors BF-1 and PAX9, as well as TIEG1/KLF10 (transforming growth factor-beta inducible early gene-1/Kruppel-like transcription factor 10), and possibly function as a transcriptional corepressor. KDM5B contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger.

Pssm-ID: 277076 Cd Length: 46 Bit Score: 70.75 E-value: 1.29e-14

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628 1156 VCEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15603     1 VCLVCGSGNDEDRLLLCDGCDDSYHTFCLIPPLHDVPKGDWRCPKC 46

PHD2_KMT2C_like

cd15510

PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...

1156-1201

1.70e-14

Pssm-ID: 276985 Cd Length: 46 Bit Score: 70.54 E-value: 1.70e-14

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628 1156 VCEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15510     1 VCQACRQPGDDTKMLVCETCDKGYHTSCLRPVMSSIPKYGWKCKNC 46

PHD_RSF1

cd15543

PHD finger found in Remodeling and spacing factor 1 (Rsf-1); Rsf-1, also termed HBV ...

1157-1201

1.77e-14

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: 70.38 E-value: 1.77e-14

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628 1157 CEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15543     2 CRKCGLSDHPEWILLCDRCDAGYHTACLRPPLMIIPDGNWFCPPC 46

SET_SETMAR

cd10544

SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...

5174-5302

2.03e-14

SET domain (including pre-SET and post-SET domains) found in SET domain and mariner transposase fusion protein (SETMAR) and similar proteins; SETMAR (also termed metnase) is a DNA-binding protein that is indirectly recruited to sites of DNA damage through protein-protein interactions. It has a sequence-specific DNA-binding activity recognizing the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element and displays a DNA nicking and end joining activity. SETMAR also acts as a histone-lysine N-methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3. It specifically mediates dimethylation of H3 'Lys-36' at sites of DNA double-strand break and may recruit proteins required for efficient DSB repair through non-homologous end-joining.

Pssm-ID: 380942 [Multi-domain] Cd Length: 254 Bit Score: 76.57 E-value: 2.03e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5174 GLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKiyeEQNRGI--YMFRINnEHV---------IDATLTGGPARYINHS 5242
Cdd:cd10544   101 GWGLRTLEFIPKGRFVCEYAGEVIGFEEARRRTK---SQTKGDmnYIIVLR-EHLssgkvletfVDPTYIGNIGRFLNHS 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5243 CAPNC----------VAEVVTFDKEDkiiiissrrIPKGEELTYDY------------QFDFEDDQHKIPCHCGAWNCRK 5300
Cdd:cd10544   177 CEPNLfmvpvrvdsmVPKLALFAARD---------IVAGEELSFDYsgefsnsvesvtLARQDESKSRKPCLCGAENCRG 247


                  ..
gi 558137628 5301 WM 5302
Cdd:cd10544   248 FL 249

PHD_BAZ1A_like

cd15544

PHD finger found in bromodomain adjacent to zinc finger domain protein BAZ1A and BAZ1B; BAZ1A, ...

276-320

2.98e-14

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: 69.75 E-value: 2.98e-14

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628  276 CQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15544     2 CKVCRKKGDPDNMILCDGCDKAFHLYCLRPALREVPSGDWFCPAC 46

PHD1_KDM5A_like

cd15515

PHD finger 1 found in Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and similar ...

1156-1201

3.26e-14

PHD finger 1 found in Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and similar proteins; The JARID subfamily within the JmjC proteins includes Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and a Drosophila homolog, protein little imaginal discs (Lid). KDM5A was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5B has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. Both KDM5A and KDM5B function as trimethylated histone H3 lysine 4 (H3K4me3) demethylases. KDM5C is a H3K4 trimethyl-histone demethylase that catalyzes demethylation of H3K4me3 and H3K4me2 to H3K4me1. It plays a role in neuronal survival and dendrite development. KDM5C defects are associated with X-linked mental retardation (XLMR). KDM5D is a male-specific antigen that shows a demethylase activity specific for di- and tri-methylated histone H3K4 (H3K4me2 and H3K4me3), and has a male-specific function as a histone H3K4 demethylase by recruiting a meiosis-regulatory protein, MSH5, to condensed DNA. KDM5D directly interacts with a polycomb-like protein Ring6a/MBLR, and plays a role in regulation of transcriptional initiation through H3K4 demethylation. This family also includes Drosophila melanogaster protein little imaginal discs (Lid) that functions as a JmjC-dependent H3K4me3 demethylase, which is required for dMyc-induced cell growth. It positively regulates Hox gene expression in S2 cells. Members in this family contain the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as two or three plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger.

Pssm-ID: 276990 Cd Length: 46 Bit Score: 69.73 E-value: 3.26e-14

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628 1156 VCEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15515     1 ICQVCGRGDDEDKLLLCDGCDDSYHTFCLIPPLPDIPPGDWRCPKC 46

PHD1_Lid2p_like

cd15519

PHD finger 1 found in Schizosaccharomyces pombe Lid2 complex component Lid2p and similar ...

1156-1201

4.32e-14

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

Pssm-ID: 276994 [Multi-domain] Cd Length: 46 Bit Score: 69.42 E-value: 4.32e-14

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628 1156 VCEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15519     1 GCEVCGLDDNEGEVLLCDGCDAEYHTSCLDPPLGEIPPGTWFCPSC 46

ePHD1_KMT2D

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...

4821-4902

5.84e-14

Pssm-ID: 277165 Cd Length: 90 Bit Score: 70.33 E-value: 5.84e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4821 DLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQRTGATSSCNRMRCPNVYHFACAIrAKCMFFKDKT--ML 4898
Cdd:cd15695     8 ECWVHHWCAAWSAGVKQHEGDGLIGVDKAVFSGISQKCEHCKRLGATIQCHAEGCPRFYHFPCAA-ASGSFQSMKTllLL 86


                  ....
gi 558137628 4899 CPMH 4902
Cdd:cd15695    87 CPEH 90

PHD_BAZ1A

cd15627

PHD finger found in bromodomain adjacent to zinc finger domain protein 1A (BAZ1A); BAZ1A, also ...

1157-1201

6.64e-14

Pssm-ID: 277097 [Multi-domain] Cd Length: 46 Bit Score: 68.57 E-value: 6.64e-14

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628 1157 CEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15627     2 CRICRRKGDAEKMLLCDGCDRGHHMYCLRPPLKKVPEGDWFCPDC 46

SET_SUV39H_DIM5-like

cd19473

SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...

5174-5302

8.00e-14

SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; This subfamily contains Neurospora crassa DIM-5 (also termed H3-K9-HMTase dim-5, or HKMT) which functions as histone-lysine N-methyltransferase that specifically trimethylates histone H3 to form H3K9me3.

Pssm-ID: 380996 [Multi-domain] Cd Length: 274 Bit Score: 75.43 E-value: 8.00e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5174 GLGLYAAKDLEKHTMVIEYIGTIIRNEVAN-RREKIYEEQNRGIYMF-------------RINNE-HVIDATLTGGPARY 5238
Cdd:cd19473   117 GWGVRSTVDIKRGQFVDCYVGEIITPEEAQrRRDAATIAQRKDVYLFaldkfsdpdsldpRLRGDpYEIDGEFMSGPTRF 196

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 558137628 5239 INHSCAPNC-VAEVVTfDKEDKIIII----SSRRIPKGEELTYDY----------QFDFEDDQHKIPCHCGAWNCRKWM 5302
Cdd:cd19473   197 INHSCDPNLrIFARVG-DHADKHIHDlaffAIKDIPRGTELTFDYvdgvtgldddAGDEEKEKEMTKCLCGSPKCRGYL 274

ePHD_TCF20

cd15699

Extended PHD finger (ePHD) found in transcription factor 20 (TCF-20); The extended plant ...

128-217

8.55e-14

Extended PHD finger (ePHD) found in transcription factor 20 (TCF-20); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the C-terminal ePHD/ADD (ATRX-DNMT3-DNMT3L) domain of TCF-20. TCF-20, also termed nuclear factor SPBP, or protein AR1, or stromelysin-1 PDGF (platelet-derived growth factor)-responsive element-binding protein (SPRE-binding protein), is involved in transcriptional activation of the MMP3 (matrix metalloprotease 3) promoter. It is strongly enriched on chromatin in interphase HeLa cells, and displays low nuclear mobility, and has been implicated in Smith-Magenis syndrome and Potocki-Lupski syndrome. As a chromatin-binding protein, TCF-20 plays a role in the regulation of gene expression. It also functions as a transcriptional co-regulator that enhances or represses the transcriptional activity of certain transcription factors/cofactors, such as specificity protein 1 (Sp1), E twenty-six 1 (Ets1), paired box protein 6 (Pax6), small nuclear RING-finger (SNURF)/RNF4, c-Jun, androgen receptor (AR) and estrogen receptor alpha (ERalpha). TCF-20 contains an N-terminal transactivation domain, a novel DNA-binding domain with an AT-hook motif, three nuclear localization signals (NLSs) and a C-terminal ePHD/ADD domain.

Pssm-ID: 277169 Cd Length: 103 Bit Score: 70.33 E-value: 8.55e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  128 HLGE---PGGSCWAHHWCAVWSAGVWGKGGpELCGVDKAIFSGISQRCSHCTRLGASIPCRSPGCPRLYHFPCATASGSF 204
Cdd:cd15699    12 NLGDlfgPFYEFWVHEGCILWANGIYLVCG-RLYGLQEALDIAREMKCSHCQEAGATLGCYNKGCSFRYHYPCAIDADCL 90

                          90
                  ....*....|...
gi 558137628  205 LSMKTLQLLCPEH 217
Cdd:cd15699    91 LNEENFSVRCPKH 103

ePHD1_KMT2C

cd15696

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...

4821-4902

1.18e-13

Pssm-ID: 277166 Cd Length: 90 Bit Score: 69.59 E-value: 1.18e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4821 DLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQRTGATSSCNRMRCPNVYHFACAIRAKCMF-FKDKTMLC 4899
Cdd:cd15696     8 ECWAHLRCAEWSLGVCQGEEQLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCAAGAGTFQdFSRRLLLC 87


                  ...
gi 558137628 4900 PMH 4902
Cdd:cd15696    88 PTH 90

PHD

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...

1156-1204

1.90e-13

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 67.52 E-value: 1.90e-13

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 558137628  1156 VCEVCGQASDPSRLLLCDDCDISYHTYCLDPPL--LTVPKGGWKCKWCVSC 1204
Cdd:pfam00628    1 YCAVCGKSDDGGELVQCDGCDDWFHLACLGPPLdpAEIPSGEWLCPECKPK 51

PHD

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...

275-323

2.07e-13

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 67.52 E-value: 2.07e-13

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 558137628   275 VCQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHS--WKCKACRVC 323
Cdd:pfam00628    1 YCAVCGKSDDGGELVQCDGCDDWFHLACLGPPLDPAEIPSgeWLCPECKPK 51

zf-HC5HC2H

PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...

4825-4902

3.68e-13

Pssm-ID: 463977 [Multi-domain] Cd Length: 88 Bit Score: 68.12 E-value: 3.68e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  4825 HLNCALWSTEVY----ETQGGALMNVEVALHRGLLTKCSLC-QRTGATSSCNRMRCPNVYHFACAIRAKCMF-FKDKT-- 4896
Cdd:pfam13771    1 HVVCALWSPELVqrgnDSMGFPIEDIEKIPKRRWKLKCYLCkKKGGACIQCSKKNCRRAFHVTCALEAGLLMqFDEDNgt 80


                   ....*...
gi 558137628  4897 --MLCPMH 4902
Cdd:pfam13771   81 fkSYCKKH 88

PHD1_KDM5A

cd15602

PHD finger 1 found in Lysine-specific demethylase 5A (KDM5A); KDM5A (also termed Histone ...

1156-1203

4.11e-13

PHD finger 1 found in Lysine-specific demethylase 5A (KDM5A); KDM5A (also termed Histone demethylase JARID1A, Jumonji/ARID domain-containing protein 1A, or Retinoblastoma-binding protein 2 (RBBP-2 or RBP2)) was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5A functions as a trimethylated histone H3 lysine 4 (H3K4me3) demethylase that belongs to the JARID subfamily within the JmjC proteins. It also displays DNA-binding activities that can recognize the specific DNA sequence CCGCCC. KDM5A contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger.

Pssm-ID: 277075 Cd Length: 49 Bit Score: 66.51 E-value: 4.11e-13

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 558137628 1156 VCEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWCVS 1203
Cdd:cd15602     1 VCLFCGRGNNEDKLLLCDGCDDSYHTFCLIPPLPDVPKGDWRCPKCVA 48

PHD_BAZ1A_like

cd15544

PHD finger found in bromodomain adjacent to zinc finger domain protein BAZ1A and BAZ1B; BAZ1A, ...

1157-1201

4.81e-13

Pssm-ID: 277019 Cd Length: 46 Bit Score: 66.28 E-value: 4.81e-13

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628 1157 CEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15544     2 CKVCRKKGDPDNMILCDGCDKAFHLYCLRPALREVPSGDWFCPAC 46

PHD5_KMT2C_like

PHD finger 5 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 4 found in ...

275-320

5.24e-13

Pssm-ID: 276988 Cd Length: 47 Bit Score: 66.35 E-value: 5.24e-13

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  275 VCQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15513     1 VCEGCGKASDESRLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 46

PHD_UHRF1_2

cd15525

PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein UHRF1 and ...

1157-1201

5.59e-13

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

Pssm-ID: 277000 Cd Length: 47 Bit Score: 66.24 E-value: 5.59e-13

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628 1157 CEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGG-WKCKWC 1201
Cdd:cd15525     2 CHVCGGKQDPEKQLLCDECDMAYHLYCLDPPLTSLPDDDeWYCPDC 47

SET_EHMT

cd10543

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...

5167-5299

6.70e-13

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine N-methyltransferase EHMT1, EHMT2 and similar proteins; This family includes EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, lysine N-methyltransferase 1D, or KMT1D) and EHMT2 (also termed Eu-HMTase2, HLA-B-associated transcript 8, histone H3-K9 methyltransferase 3, H3-K9-HMTase 3, lysine N-methyltransferase 1C, KMT1C, or protein G9a), both act as histone-lysine N-methyltransferases that specifically mono- and dimethylate 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin.

Pssm-ID: 380941 [Multi-domain] Cd Length: 231 Bit Score: 71.60 E-value: 6.70e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5167 LARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKiyeeqnrGIYMFRINNE----HVIDATLTGGPARYINHS 5242
Cdd:cd10543    95 LFRTRGMGWGVRALQDIPKGTFVCEYIGELISDSEADSRED-------DSYLFDLDNKdgetYCIDARRYGNISRFINHL 167

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 558137628 5243 CAPNCVAEVVTFDKED----KIIIISSRRIPKGEELTYDYQFDFEDDQHK-IPCHCGAWNCR 5299
Cdd:cd10543   168 CEPNLIPVRVFVEHQDlrfpRIAFFASRDIKAGEELGFDYGEKFWRIKGKyFTCRCGSPKCK 229

ePHD_TCF20

cd15699

Extended PHD finger (ePHD) found in transcription factor 20 (TCF-20); The extended plant ...

4798-4902

7.20e-13

Pssm-ID: 277169 Cd Length: 103 Bit Score: 67.63 E-value: 7.20e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4798 CCFCHEEGD----GATDGPArllnldLDLWVHLNCALWSTEVYETQGgALMNVEVALHRGLLTKCSLCQRTGATSSCNRM 4873
Cdd:cd15699     1 CCLCGKWANyrnlGDLFGPF------YEFWVHEGCILWANGIYLVCG-RLYGLQEALDIAREMKCSHCQEAGATLGCYNK 73

                          90       100       110
                  ....*....|....*....|....*....|
gi 558137628 4874 RCPNVYHFACAIRAKCMFFKDK-TMLCPMH 4902
Cdd:cd15699    74 GCSFRYHYPCAIDADCLLNEENfSVRCPKH 103

SET_SUV39H1

cd10525

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...

5173-5302

7.97e-13

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 homolog 1 (SUV39H1) and similar proteins; SUV39H1 (EC 2.1.1.43; also termed histone H3-K9 methyltransferase 1, H3-K9-HMTase 1, lysine N-methyltransferase 1A (KMT1A), position-effect variegation 3-9 homolog (SUV39H), or Su(var)3-9 homolog 1) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. It mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions.

Pssm-ID: 380923 [Multi-domain] Cd Length: 255 Bit Score: 71.85 E-value: 7.97e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5173 QGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNrGIYMFR---INNEHVIDATLTGGPARYINHSCAPNCVA 5249
Cdd:cd10525    97 RGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQG-ATYLFDldyVEDVYTVDAAYYGNISHFVNHSCDPNLQV 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 558137628 5250 EVVTFDKEDKIIIISSRRIPK----GEELTYDYQF-----DFEDDQH-----------------KIPCHCGAWNCRKWM 5302
Cdd:cd10525   176 YNVFIDNLDERLPRIALFATRtiraGEELTFDYNMqvdpvDAESTKMdsnfglaglpgspkkrvRIECKCGVRSCRKYL 254

PHD1_Lid_like

cd15605

PHD finger 1 found in Drosophila melanogaster protein little imaginal discs (Lid) and similar ...

1156-1201

8.01e-13

PHD finger 1 found in Drosophila melanogaster protein little imaginal discs (Lid) and similar proteins; Drosophila melanogaster Lid, also termed Retinoblastoma-binding protein 2 homolog, is identified genetically as a trithorax group (trxG) protein that is a Drosophila homolog of the human protein JARID1A/kdm5A, a member of the JARID subfamily within the JmjC proteins. Lid functions as a JmjC-dependent trimethyl histone H3K4 (H3K4me3) demethylase, which is required for dMyc-induced cell growth. It positively regulates Hox gene expression in S2 cells. Lid contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger of Lid.

Pssm-ID: 277078 Cd Length: 46 Bit Score: 65.55 E-value: 8.01e-13

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628 1156 VCEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15605     1 VCHTCGRGDGEESMLLCDGCDDSYHTFCLLPPLSEVPKGDWRCPKC 46

SET_EZH-like

cd19168

SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb ...

5165-5282

9.00e-13

SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb repressive complex 2 (PRC2), and similar proteins; The family includes EZH1 and EZH2. EZH1 (EC 2.1.1.43; also termed ENX-2, or histone-lysine N-methyltransferase EZH1) is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. EZH2 (EC 2.1.1.43; also termed lysine N-methyltransferase 6, ENX-1, or histone-lysine N-methyltransferase EZH2) is a catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Both EZH1 and EZH2 can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. PRC2 is involved in several cancers; EZH2 is overexpressed in breast, liver and prostate cancer, while point mutations in EZH2 alter the substrate preference and product specificity of PRC2 in Non-Hodgkin lymphomas (NHLs). Thus, PRC2 is a popular target for cancer therapeutics.

Pssm-ID: 380945 Cd Length: 124 Bit Score: 67.98 E-value: 9.00e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5165 VYLARSRIQ-GLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRgIYMFRINNEHVIDATLTGGPARYINH-- 5241
Cdd:cd19168     3 VVLGKSQLEcGLGLFAAEDIKEGEFVIEYTGELISHDEGVRREHRRGDVSY-LYLFEEQEGIWVDAAIYGNLSRYINHat 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 558137628 5242 --SCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDF 5282
Cdd:cd19168    82 dkVKTGNCMPKIMYVNHEWRIKFTAIKDIKIGEELFFNYGDNF 124

SET_SUV39H2

cd10532

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...

5173-5302

1.03e-12

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 homolog 2 (SUV39H2) and similar proteins; SUV39H2 (EC 2.1.1.43; also termed histone H3-K9 methyltransferase 2, H3-K9-HMTase 2, lysine N-methyltransferase 1B (KMT1B), or Su(var)3-9 homolog 2) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. It mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions.

Pssm-ID: 380930 [Multi-domain] Cd Length: 243 Bit Score: 71.46 E-value: 1.03e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5173 QGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEeqNRGI-YMFRIN---NEHVIDATLTGGPARYINHSCAPNCV 5248
Cdd:cd10532    95 RGWGVKTLQKIKKNSFVMEYVGEVITSEEAERRGQFYD--SKGItYLFDLDyesDEFTVDAARYGNVSHFVNHSCDPNLQ 172

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 558137628 5249 AEVVTFDKED----KIIIISSRRIPKGEELTYDYQFDFEDD-------------QHKIPCHCGAWNCRKWM 5302
Cdd:cd10532   173 VFNVFIDNLDtrlpRIALFSTRTIKAGEELTFDYQMKGSGDlssdsidnspakkRVRTVCKCGAVTCRGYL 243

ePHD2_KMT2D

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...

126-217

1.04e-12

Pssm-ID: 277168 Cd Length: 107 Bit Score: 67.38 E-value: 1.04e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  126 PAHLGEPGGSCWAHHWCAVWSAGVWGKGGPELCGVDKAIFSGISQRCSHCTRLGASIPCRSPGCPRLYHFPCAT-ASGSF 204
Cdd:cd15698    15 PARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQKTGATNSCNRLRCPNVYHFACAIrAKCMF 94

                          90
                  ....*....|...
gi 558137628  205 LSMKTlqLLCPEH 217
Cdd:cd15698    95 FKDKT--MLCPMH 105

PHD1_KDM5C_5D

cd15604

PHD finger 1 found in Lysine-specific demethylase 5C (KDM5C) and 5D (KDM5D); The family ...

1156-1201

1.41e-12

PHD finger 1 found in Lysine-specific demethylase 5C (KDM5C) and 5D (KDM5D); The family includes KDM5C and KDM5D, both of which belong to the JARID subfamily within the JmjC proteins. KDM5C (also termed Histone demethylase JARID1C, Jumonji/ARID domain-containing protein 1C, SmcX, or Xe169) is a H3K4 trimethyl-histone demethylase that catalyzes demethylation of H3K4me3 and H3K4me2 to H3K4me1. It plays a role in neuronal survival and dendrite development. KDM5C defects are associated with X-linked mental retardation (XLMR). KDM5D (also termed Histocompatibility Y antigen (H-Y), Histone demethylase JARID1D, Jumonji/ARID domain-containing protein 1D, or SmcY) is a male-specific antigen that shows a demethylase activity specific for di- and tri-methylated histone H3K4 (H3K4me3 andH3K4me2), and has a male-specific function as a histone H3K4 demethylase by recruiting a meiosis-regulatory protein, MSH5, to condensed DNA. KDM5D directly interacts with a polycomb-like protein Ring6a/MBLR, and plays a role in regulation of transcriptional initiation through H3K4 demethylation. Both KDM5C and KDM5D contain the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as two plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger.

Pssm-ID: 277077 Cd Length: 46 Bit Score: 64.86 E-value: 1.41e-12

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628 1156 VCEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15604     1 VCRMCSRGDEDDKLLLCDGCDDNYHTFCLLPPLPEPPKGIWRCPKC 46

ePHD_RAI1

cd15700

Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant ...

4798-4902

1.55e-12

Pssm-ID: 277170 Cd Length: 104 Bit Score: 66.82 E-value: 1.55e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4798 CCFCHEegdgatdgPARLLNL-DL------DLWVHLNCALWSTEVYETqGGALMNVEVALHRGLLTKCSLCQRTGATSSC 4870
Cdd:cd15700     1 CCLCRN--------PANYKDLgDLcgpyypEHWVHEACAVWTTGVYLV-AGKLFGLQEAVQKAADAKCSSCQGAGATVGC 71

                          90       100       110
                  ....*....|....*....|....*....|...
gi 558137628 4871 NRMRCPNVYHFACAIRAKCMFFKDK-TMLCPMH 4902
Cdd:cd15700    72 CHKGCTQSYHYICAVEAGCLFEEENfSLRCPKH 104

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

1156-1201

1.85e-12

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 64.54 E-value: 1.85e-12

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 558137628   1156 VCEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLT-VPKGGWKCKWC 1201
Cdd:smart00249    1 YCSVCGKPDDGGELLQCDGCDRWYHQTCLGPPLLEeEPDGKWYCPKC 47

PHD_UHRF1

cd15616

PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein 1 (UHRF1); ...

1157-1201

2.24e-12

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

Pssm-ID: 277088 Cd Length: 47 Bit Score: 64.60 E-value: 2.24e-12

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628 1157 CEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVP-KGGWKCKWC 1201
Cdd:cd15616     2 CHVCGGKQDPDKQLMCDECDMAFHIYCLNPPLSSIPdDEDWYCPEC 47

PHD2_PHF10

cd15529

PHD finger 2 found in PHD finger protein 10 (PHF10) and similar proteins; PHF10, also termed ...

275-320

3.12e-12

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: 63.86 E-value: 3.12e-12

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  275 VCQACRKPGNDSKMLVCETCDKGYHTFCLKppMEELPAHSWKCKAC 320
Cdd:cd15529     1 TCTKCGDPHDEDKMMFCDQCDRGYHTFCVG--LRSIPDGRWICPLC 44

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

275-320

4.55e-12

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 63.38 E-value: 4.55e-12

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 558137628    275 VCQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEE-LPAHSWKCKAC 320
Cdd:smart00249    1 YCSVCGKPDDGGELLQCDGCDRWYHQTCLGPPLLEeEPDGKWYCPKC 47

PHD_PHRF1

cd15536

PHD finger found in PHD and RING finger domain-containing protein 1 (PHRF1); PHRF1, also ...

1157-1201

4.58e-12

PHD finger found in PHD and RING finger domain-containing protein 1 (PHRF1); PHRF1, also termed KIAA1542, or CTD-binding SR-like protein rA9, is a ubiquitin ligase that induces the ubiquitination of TGIF (TG-interacting factor) at lysine 130. It acts as a tumor suppressor that promotes the transforming growth factor (TGF)-beta cytostatic program through selective release of TGIF-driven promyelocytic leukemia protein (PML) inactivation. PHRF1 contains a plant homeodomain (PHD) finger and a RING finger.

Pssm-ID: 277011 Cd Length: 46 Bit Score: 63.59 E-value: 4.58e-12

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628 1157 CEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15536     2 CEVCGRSDREDRLLLCDGCDAGYHMECLTPPLDEVPIEEWFCPEC 46

ePHD_KMT2A_like

cd15664

Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The ...

133-217

6.44e-12

Pssm-ID: 277134 Cd Length: 105 Bit Score: 65.12 E-value: 6.44e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  133 GGSCWAHHWCAVWSAGVWGKGGPELCGVDKAIFSGISQRCSHCTRLGASIPCRSPGCPRLYHFPCA-TASGSFLSMKtlQ 211
Cdd:cd15664    22 GQDEWVHINCALWSAEVFEEDDGSLQNVHSAVSRGRMMKCELCGKPGATVGCCLKSCPANYHFMCArKAECVFQDDK--K 99


                  ....*.
gi 558137628  212 LLCPEH 217
Cdd:cd15664   100 VFCPAH 105

SET_LegAS4-like

cd10522

SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...

5174-5284

7.91e-12

SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and similar proteins; LegAS4 is a type IV secretion system effector of Legionella pneumophila. It contains a SET domain that is involved in the modification of Lys4 of histone H3 (H3K4) in the nucleolus of the host cell, thereby enhancing heterochromatic rDNA transcription. It also contains an ankyrin repeat domain of unknown function at its C-terminal region.

Pssm-ID: 380920 [Multi-domain] Cd Length: 122 Bit Score: 65.44 E-value: 7.91e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5174 GLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNrgiYMFRINNEH-VIDATLTGGPARYINHSCAPNCVAEVV 5252
Cdd:cd10522    14 GLGLFAAETIAKGEFVGEYTGEVLDRWEEDRDSVYHYDPL---YPFDLNGDIlVIDAGKKGNLTRFINHSDQPNLELIVR 90

                          90       100       110
                  ....*....|....*....|....*....|..
gi 558137628 5253 TFDKEDKIIIISSRRIPKGEELTYDYQFDFED 5284
Cdd:cd10522    91 TLKGEQHIGFVAIRDIKPGEELFISYGPKYWK 122

ePHD2_KMT2C

cd15697

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...

120-217

8.22e-12

Pssm-ID: 277167 Cd Length: 105 Bit Score: 64.68 E-value: 8.22e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  120 FPEGLT--PAHLGEPGGSCWAHHWCAVWSAGVWGKGGPELCGVDKAIFSGISQRCSHCTRLGASIPCRSPGCPRLYHFPC 197
Cdd:cd15697     7 EGDGLTdgPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRLRCTNVYHFTC 86

                          90       100
                  ....*....|....*....|.
gi 558137628  198 A-TASGSFLSMKTlqLLCPEH 217
Cdd:cd15697    87 AiKAQCMFFKDKT--MLCPMH 105

PHD_BAZ2A_like

cd15545

PHD finger found in bromodomain adjacent to zinc finger domain protein 2A (BAZ2A) and 2B ...

1157-1201

8.75e-12

Pssm-ID: 277020 [Multi-domain] Cd Length: 46 Bit Score: 62.71 E-value: 8.75e-12

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628 1157 CEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15545     2 CQICRSGDNEDQLLLCDGCDRGYHTYCFKPKMTNVPEGDWFCPEC 46

PHD_BAZ2A

cd15629

PHD finger found in bromodomain adjacent to zinc finger domain protein 2A (BAZ2A); BAZ2A, also ...

276-320

1.00e-11

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: 62.56 E-value: 1.00e-11

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628  276 CQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15629     2 CLVCRKGDNDEYLLLCDGCDRGCHMYCHRPKMLQVPEGDWFCPNC 46

zf-HC5HC2H

PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...

139-217

1.00e-11

Pssm-ID: 463977 [Multi-domain] Cd Length: 88 Bit Score: 63.89 E-value: 1.00e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628   139 HHWCAVWSAGVWGKGGPE----LCGVDKAIFSGISQRCSHC-TRLGASIPCRSPGCPRLYHFPCATASGSFLSMK----T 209
Cdd:pfam13771    1 HVVCALWSPELVQRGNDSmgfpIEDIEKIPKRRWKLKCYLCkKKGGACIQCSKKNCRRAFHVTCALEAGLLMQFDedngT 80


                   ....*...
gi 558137628   210 LQLLCPEH 217
Cdd:pfam13771   81 FKSYCKKH 88

PHD2_KAT6A_6B

cd15527

PHD finger 2 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ, ...

1157-1201

1.07e-11

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: 62.40 E-value: 1.07e-11

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628 1157 CEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15527     2 CSVCQDSGNADNLLFCDACDKGFHMECHDPPLTRMPKGKWVCQIC 46

SET_EHMT1

cd10535

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...

5150-5299

1.09e-11

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine N-methyltransferase 1 (EHMT1) and similar proteins; EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, or lysine N-methyltransferase 1D (KMT1D)) acts as a histone-lysine N-methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin.

Pssm-ID: 380933 [Multi-domain] Cd Length: 231 Bit Score: 68.04 E-value: 1.09e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5150 KSSQYRRLRTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKiyeeqnrGIYMFRINNE----H 5225
Cdd:cd10535    78 RNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE-------DSYLFDLDNKdgevY 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 558137628 5226 VIDATLTGGPARYINHSCAPNCVAEVVTFDKED----KIIIISSRRIPKGEELTYDYQFDFEDDQHKI-PCHCGAWNCR 5299
Cdd:cd10535   151 CIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 229

PHD2_KMT2D

PHD finger 2 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...

1156-1201

1.52e-11

Pssm-ID: 277070 Cd Length: 46 Bit Score: 61.94 E-value: 1.52e-11

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628 1156 VCEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15595     1 VCQTCRKPGEDSKMLVCEACDKGYHTFCLKPAMESLPTDSWKCKAC 46

PHD1_KDM5A_like

cd15515

PHD finger 1 found in Lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and similar ...

275-320

2.35e-11

Pssm-ID: 276990 Cd Length: 46 Bit Score: 61.64 E-value: 2.35e-11

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  275 VCQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15515     1 ICQVCGRGDDEDKLLLCDGCDDSYHTFCLIPPLPDIPPGDWRCPKC 46

PHD_RSF1

cd15543

PHD finger found in Remodeling and spacing factor 1 (Rsf-1); Rsf-1, also termed HBV ...

276-320

2.59e-11

Pssm-ID: 277018 [Multi-domain] Cd Length: 46 Bit Score: 61.52 E-value: 2.59e-11

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628  276 CQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15543     2 CRKCGLSDHPEWILLCDRCDAGYHTACLRPPLMIIPDGNWFCPPC 46

PHD_BAZ1B

cd15628

PHD finger found in bromodomain adjacent to zinc finger domain protein 1B (BAZ1B); BAZ1B, also ...

276-320

2.62e-11

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: 61.30 E-value: 2.62e-11

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628  276 CQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15628     2 CKVCRKKGEDDKLILCDECNQAFHLFCLRPALYEVPDGEWMCPAC 46

PHD

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...

228-276

2.74e-11

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 61.35 E-value: 2.74e-11

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 558137628   228 RCAVCEGPGELCDLFFCTSCGHHYHGACLDTALTARKRA--GWQCPECKVC 276
Cdd:pfam00628    1 YCAVCGKSDDGGELVQCDGCDDWFHLACLGPPLDPAEIPsgEWLCPECKPK 51

PHD2_d4

cd15530

PHD finger 2 found in d4 gene family proteins; The family includes proteins coded by three ...

276-320

3.33e-11

PHD finger 2 found in d4 gene family proteins; The family includes proteins coded by three members of the d4 gene family, DPF1 (neuro-d4), DPF2 (ubi-d4/Requiem), and DPF3 (cer-d4), which function as transcription factors and are involved in transcriptional regulation of genes by changing the condensed/decondensed state of chromatin in the nucleus. DPF2 is ubiquitously expressed and it acts as a transcription factor that may participate in developmentally programmed cell death. DPF1 and DPF3 are expressed predominantly in neural tissues, and they may be involved in the transcription regulation of neuro-specific gene clusters. The d4 family proteins show distinct domain organization with domain 2/3 in the N-terminal region, a Cys2His2 (C2H2) zinc finger or Kruppel-type zinc finger in the central part and two adjacent plant homeodomain (PHD) fingers (d4-domain) in the C-terminal part of the molecule. This model corresponds to the second PHD finger.

Pssm-ID: 277005 Cd Length: 46 Bit Score: 60.86 E-value: 3.33e-11

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628  276 CQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15530     2 CSLCGTSENDDQLLFCDDCDRGYHMYCLSPPMSEPPEGSWSCHLC 46

PHD2_d4

cd15530

PHD finger 2 found in d4 gene family proteins; The family includes proteins coded by three ...

1157-1201

3.64e-11

Pssm-ID: 277005 Cd Length: 46 Bit Score: 60.86 E-value: 3.64e-11

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628 1157 CEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15530     2 CSLCGTSENDDQLLFCDDCDRGYHMYCLSPPMSEPPEGSWSCHLC 46

PHD_UHRF2

cd15617

PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein 2 (UHRF2); ...

1157-1201

7.94e-11

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

Pssm-ID: 277089 Cd Length: 47 Bit Score: 59.97 E-value: 7.94e-11

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628 1157 CEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKG-GWKCKWC 1201
Cdd:cd15617     2 CYVCGGKQDAHMQLLCDECNMAYHIYCLNPPLDKIPEDeDWYCPSC 47

PHD1_KDM5C_5D

cd15604

PHD finger 1 found in Lysine-specific demethylase 5C (KDM5C) and 5D (KDM5D); The family ...

275-320

9.42e-11

Pssm-ID: 277077 Cd Length: 46 Bit Score: 59.86 E-value: 9.42e-11

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  275 VCQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15604     1 VCRMCSRGDEDDKLLLCDGCDDNYHTFCLLPPLPEPPKGIWRCPKC 46

PHD2_KAT6A_6B

cd15527

PHD finger 2 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ, ...

276-320

9.43e-11

Pssm-ID: 277002 Cd Length: 46 Bit Score: 59.70 E-value: 9.43e-11

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628  276 CQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15527     2 CSVCQDSGNADNLLFCDACDKGFHMECHDPPLTRMPKGKWVCQIC 46

SET_SETDB1

cd10517

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...

5174-5300

9.64e-11

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) and similar proteins; SETDB1 (EC 2.1.1.43; also termed ERG-associated protein with SET domain (ESET), histone H3-K9 methyltransferase 4, H3-K9-HMTase 4, or lysine N-methyltransferase 1E (KMT1E)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes.

Pssm-ID: 380915 [Multi-domain] Cd Length: 288 Bit Score: 66.16 E-value: 9.64e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5174 GLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIY-------------EEQNRGIYMfRINNEH--VIDATLTGGPARY 5238
Cdd:cd10517   140 GWGIRCLDDIPKGSFVCIYAGQILTEDEANEEGLQYgdeyfaeldyievVEKLKEGYE-SDVEEHcyIIDAKSEGNLGRY 218

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 558137628 5239 INHSCAPNCVAEVVTFDKEDKIIII----SSRRIPKGEELTYDYQFDFEDDQHKI-PCHCGAWNCRK 5300
Cdd:cd10517   219 LNHSCSPNLFVQNVFVDTHDLRFPWvaffASRYIRAGTELTWDYNYEVGSVPGKVlYCYCGSSNCRG 285

zf-HC5HC2H_2

pfam13832

PHD-zinc-finger like domain;

4796-4891

9.86e-11

PHD-zinc-finger like domain;

Pssm-ID: 463991 [Multi-domain] Cd Length: 109 Bit Score: 61.98 E-value: 9.86e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  4796 RRCCFCHEEGdGAtdgparLLNLDLDLWVHLNCALWSTEV----YETQggALMNVEVALHRGLLTKCSLC-QRTGATSSC 4870
Cdd:pfam13832    1 VRCCLCPLRG-GA------LKQTSDGRWVHVLCAIFVPEVrfgnVATM--EPIDVSRIPPERWKLKCVFCkKRSGACIQC 71

                           90       100
                   ....*....|....*....|.
gi 558137628  4871 NRMRCPNVYHFACAIRAKCMF 4891
Cdd:pfam13832   72 SKGRCTTAFHVTCAQAAGVYM 92

PHD1_Lid2p_like

cd15519

PHD finger 1 found in Schizosaccharomyces pombe Lid2 complex component Lid2p and similar ...

275-320

1.26e-10

Pssm-ID: 276994 [Multi-domain] Cd Length: 46 Bit Score: 59.40 E-value: 1.26e-10

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  275 VCQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15519     1 GCEVCGLDDNEGEVLLCDGCDAEYHTSCLDPPLGEIPPGTWFCPSC 46

SET_EHMT2

cd10533

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...

5150-5299

1.67e-10

SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine N-methyltransferase 2 (EHMT2) and similar proteins; EHMT2 (also termed Eu-HMTase2, HLA-B-associated transcript 8, histone H3-K9 methyltransferase 3, H3-K9-HMTase 3, lysine N-methyltransferase 1C (KMT1C), or protein G9a) acts as a histone-lysine N-methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin.

Pssm-ID: 380931 [Multi-domain] Cd Length: 239 Bit Score: 64.65 E-value: 1.67e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5150 KSSQYRRLRTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKiyeeqnrGIYMFRINNE----H 5225
Cdd:cd10533    78 RNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED-------DSYLFDLDNKdgevY 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 558137628 5226 VIDATLTGGPARYINHSCAPNCVAEVVTFDKED----KIIIISSRRIPKGEELTYDYQFDFEDDQHK-IPCHCGAWNCR 5299
Cdd:cd10533   151 CIDARYYGNISRFINHLCDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWDIKSKyFTCQCGSEKCK 229

PHD1_KDM5A

cd15602

PHD finger 1 found in Lysine-specific demethylase 5A (KDM5A); KDM5A (also termed Histone ...

275-320

2.68e-10

Pssm-ID: 277075 Cd Length: 49 Bit Score: 58.42 E-value: 2.68e-10

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  275 VCQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15602     1 VCLFCGRGNNEDKLLLCDGCDDSYHTFCLIPPLPDVPKGDWRCPKC 46

PHD

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...

1107-1157

3.38e-10

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 58.27 E-value: 3.38e-10

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 558137628  1107 CVVCGsfGRGAEGHLLACSQCSQCYHPYCVNSKITKVMLLKG-WRCVECIVC 1157
Cdd:pfam00628    2 CAVCG--KSDDGGELVQCDGCDDWFHLACLGPPLDPAEIPSGeWLCPECKPK 51

PHD2_PHF10

cd15529

PHD finger 2 found in PHD finger protein 10 (PHF10) and similar proteins; PHF10, also termed ...

1156-1201

4.69e-10

Pssm-ID: 277004 Cd Length: 44 Bit Score: 57.70 E-value: 4.69e-10

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628 1156 VCEVCGQASDPSRLLLCDDCDISYHTYCLDppLLTVPKGGWKCKWC 1201
Cdd:cd15529     1 TCTKCGDPHDEDKMMFCDQCDRGYHTFCVG--LRSIPDGRWICPLC 44

PHD2_PHF14

cd15562

PHD finger 2 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...

1156-1201

5.18e-10

PHD finger 2 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 second PHD finger.

Pssm-ID: 277037 Cd Length: 50 Bit Score: 57.80 E-value: 5.18e-10

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 558137628 1156 VCEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKG----GWKCKWC 1201
Cdd:cd15562     1 SCGICKKSNDQHLLALCDTCKLYYHLGCLDPPLTRMPKKtknsGWQCSEC 50

ePHD_PHF7_G2E3_like

cd15669

Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ...

4798-4902

5.51e-10

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: 59.96 E-value: 5.51e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4798 CCFCHEEgDGATDGPARLLNLDlDLWVHLNCALWSTEV----YETQG--GALMN-VEVALHRGLLTKCSLCQRTGATSSC 4870
Cdd:cd15669     1 CVLCGRS-DDDPDKYGEKLQKD-GICAHYFCLLFSSGLpqrgEDNEGiyGFLPEdIRKEVRRASRLRCFYCKKKGASIGC 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 558137628 4871 NRMRCPNVYHFACAIRAKC--MFFKDKTMLCPMH 4902
Cdd:cd15669    79 AVKGCRRSFHFPCGLENGCvtQFFGEYRSFCWEH 112

PHD1_Lid_like

cd15605

PHD finger 1 found in Drosophila melanogaster protein little imaginal discs (Lid) and similar ...

275-320

6.40e-10

Pssm-ID: 277078 Cd Length: 46 Bit Score: 57.46 E-value: 6.40e-10

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  275 VCQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15605     1 VCHTCGRGDGEESMLLCDGCDDSYHTFCLLPPLSEVPKGDWRCPKC 46

PHD_PHRF1

cd15536

PHD finger found in PHD and RING finger domain-containing protein 1 (PHRF1); PHRF1, also ...

276-320

7.23e-10

Pssm-ID: 277011 Cd Length: 46 Bit Score: 57.42 E-value: 7.23e-10

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628  276 CQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15536     2 CEVCGRSDREDRLLLCDGCDAGYHMECLTPPLDEVPIEEWFCPEC 46

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

1106-1154

7.49e-10

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 57.22 E-value: 7.49e-10

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 558137628   1106 MCVVCGsfGRGAEGHLLACSQCSQCYHPYCVNSKITKVMLLKGWRCVEC 1154
Cdd:smart00249    1 YCSVCG--KPDDGGELLQCDGCDRWYHQTCLGPPLLEEEPDGKWYCPKC 47

ePHD_PHF7_G2E3_like

cd15669

Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ...

138-217

8.05e-10

Pssm-ID: 277139 [Multi-domain] Cd Length: 112 Bit Score: 59.19 E-value: 8.05e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  138 AHHWCAVWSAGVWGKGgPELCGVDKAIFSGIS--------QRCSHCTRLGASIPCRSPGCPRLYHFPCATASGS-FLSMK 208
Cdd:cd15669    25 AHYFCLLFSSGLPQRG-EDNEGIYGFLPEDIRkevrrasrLRCFYCKKKGASIGCAVKGCRRSFHFPCGLENGCvTQFFG 103


                  ....*....
gi 558137628  209 TLQLLCPEH 217
Cdd:cd15669   104 EYRSFCWEH 112

SET_SETD5-like

cd10529

SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...

5176-5282

8.23e-10

SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar proteins; SETD5 is a probable transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. KMT2E (also termed inactive lysine N-methyltransferase 2E or myeloid/lymphoid or mixed-lineage leukemia protein 5 (MLL5)) associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription. The family also includes Saccharomyces cerevisiae SET domain-containing proteins, SET3 and SET4, and Schizosaccharomyces pombe SET3. Most of these family members contain a post-SET domain which harbors a zinc-binding site.

Pssm-ID: 380927 Cd Length: 127 Bit Score: 59.60 E-value: 8.23e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5176 GLYAAKDLEKHTMVIEYIGTI-IRNEVanrrEKIYEEQNRGI-YMFRINNEH----VIDATLTGGPARYINHSCAPNCVA 5249
Cdd:cd10529    18 GLVATEDISPGEPILEYKGEVsLRSEF----KEDNGFFKRPSpFVFFYDGFEglplCVDARKYGNEARFIRRSCRPNAEL 93

                          90       100       110
                  ....*....|....*....|....*....|....
gi 558137628 5250 EVVTFDK-EDKIIIISSRRIPKGEELTYDYQFDF 5282
Cdd:cd10529    94 RHVVVSNgELRLFIFALKDIRKGTEITIPFDYDY 127

ePHD_KMT2B

cd15694

Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant ...

133-201

8.39e-10

Pssm-ID: 277164 Cd Length: 105 Bit Score: 58.90 E-value: 8.39e-10

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 558137628  133 GGSCWAHHWCAVWSAGVWGKGGPELCGVDKAIFSGISQRCSHCTRLGASIPCRSPGCPRLYHFPCATAS 201
Cdd:cd15694    22 GQNEWTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCEHCQKIGATVGCCLSACLSNFHFMCARAS 90

SET_SETDB2

cd10523

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...

5173-5302

8.58e-10

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) and similar proteins; SETDB2 (EC 2.1.1.43; also termed chronic lymphocytic leukemia deletion region gene 8 protein (CLLD8), or lysine N-methyltransferase 1F (KMT1F)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It is involved in left-right axis specification in early development and mitosis.

Pssm-ID: 380921 [Multi-domain] Cd Length: 266 Bit Score: 62.93 E-value: 8.58e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5173 QGLGLYAAKDLEKHTMVIEYIGTIIRNEVA--------------NRREKIYEEQNRGIYMFRINNEHVIDATLTGGPARY 5238
Cdd:cd10523   118 KGWGVRCLDDIDKGTFVCIYAGRVLSRARSpteplppklelpseNEVEVVTSWLILSKKRKLRENVCFLDASKEGNVGRF 197

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5239 INHSCAPNCVAEVVTFDKEDKIIII----SSRRIPKGEELTYDYQFDF--EDDQhKIPCHCGAWNCRKWM 5302
Cdd:cd10523   198 LNHSCCPNLFVQNVFVDTHDKNFPWvaffTNRVVKAGTELTWDYSYDAgtSPEQ-EIPCLCGVNKCQKKI 266

PHD_SF

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...

1156-1201

9.29e-10

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: 56.94 E-value: 9.29e-10

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 558137628 1156 VCEVCGQA-SDPSRLLLCDDCDISYHTYCLDPPLLT-VPKGGWKCKWC 1201
Cdd:cd15489     1 SCIVCGKGgDLGGELLQCDGCGKWFHADCLGPPLSSfVPNGKWICPVC 48

PHD_BAZ1B

cd15628

PHD finger found in bromodomain adjacent to zinc finger domain protein 1B (BAZ1B); BAZ1B, also ...

1157-1201

1.01e-09

Pssm-ID: 277098 Cd Length: 46 Bit Score: 56.68 E-value: 1.01e-09

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628 1157 CEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15628     2 CKVCRKKGEDDKLILCDECNQAFHLFCLRPALYEVPDGEWMCPAC 46

PHD2_CHD_II

cd15532

PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...

1156-1201

1.27e-09

PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD proteins includes chromodomain-helicase-DNA-binding protein CHD3, CHD4, and CHD5, which are nuclear and ubiquitously expressed chromatin remodelling ATPases generally associated with histone deacetylases (HDACs). They are involved in DNA Double Strand Break (DSB) signaling, DSB repair and/or p53-dependent pathways such as apoptosis and senescence, as well as in the maintenance of genomic stability, and/or cancer prevention. They function as subunits of the Nucleosome Remodelling and Deacetylase (NuRD) complex, which is generally associated with gene repression, heterochromatin formation, and overall chromatin compaction. In contrast to the class I CHD enzymes (CHD1 and CHD2), class II CHD proteins lack identifiable DNA-binding domains, but possess a C-terminal coiled-coil region. Moreover, in addition to the tandem chromodomains and a helicase domain, they all harbor tandem plant homeodomain (PHD) zinc fingers involved in the recognition of methylated histone tails. This model corresponds to the second PHD finger.

Pssm-ID: 277007 [Multi-domain] Cd Length: 43 Bit Score: 56.52 E-value: 1.27e-09

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628 1156 VCEVCGQASDpsrLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15532     1 FCRVCKDGGE---LLCCDGCPSSYHLHCLNPPLAEIPDGDWFCPRC 43

PHD1_KDM5B

cd15603

PHD finger 1 found in lysine-specific demethylase 5B (KDM5B); KDM5B (also termed Cancer/testis ...

275-320

2.16e-09

Pssm-ID: 277076 Cd Length: 46 Bit Score: 56.11 E-value: 2.16e-09

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  275 VCQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15603     1 VCLVCGSGNDEDRLLLCDGCDDSYHTFCLIPPLHDVPKGDWRCPKC 46

ePHD_PHF6_like

cd15673

Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11); ...

4798-4902

2.18e-09

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: 58.17 E-value: 2.18e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4798 CCFCHEEGDGATDGParLLNLDLDLWVHLNCALWSTEVYETQ-------GGALMN-VEVALHRGLLTKCSLCQRTGATSS 4869
Cdd:cd15673     1 CGFCKSGEENKETGG--KLASGEKIAAHHNCMLFSSGLVQYVspnendfGGFDIEdVKKEIKRGRKLKCNLCKKTGATIG 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 558137628 4870 CNRMRCPNVYHFACAIRAKCMFFKDK-----TMLCPMH 4902
Cdd:cd15673    79 CDVKQCKKTYHYHCAKKDDAKIIERNsqgiyRVYCKNH 116

PHD_BAZ2A

cd15629

PHD finger found in bromodomain adjacent to zinc finger domain protein 2A (BAZ2A); BAZ2A, also ...

1157-1202

3.24e-09

Pssm-ID: 277099 Cd Length: 47 Bit Score: 55.63 E-value: 3.24e-09

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628 1157 CEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWCV 1202
Cdd:cd15629     2 CLVCRKGDNDEYLLLCDGCDRGCHMYCHRPKMLQVPEGDWFCPNCV 47

SET_SETDB

cd10541

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...

5173-5300

3.82e-09

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), SET domain bifurcated 2 (SETDB2), and similar proteins; SETDB1 (EC 2.1.1.43; also termed ERG-associated protein with SET domain (ESET), histone H3-K9 methyltransferase 4, H3-K9-HMTase 4, or lysine N-methyltransferase 1E (KMT1E)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. SETDB2 (EC 2.1.1.43; also termed chronic lymphocytic leukemia deletion region gene 8 protein (CLLD8), or lysine N-methyltransferase 1F (KMT1F)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It is involved in left-right axis specification in early development and mitosis.

Pssm-ID: 380939 [Multi-domain] Cd Length: 236 Bit Score: 60.64 E-value: 3.82e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5173 QGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVIDATLTGGPARYINHSCAPNCVAEVV 5252
Cdd:cd10541   102 KGWGIRCLDDIAKGTFVCIYAGKILTDDFADKEGLEMGDEYFANLDHIEESCYIIDAKLEGNLGRYLNHSCSPNLFVQNV 181

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 558137628 5253 TFDKEDKIIIISSRRIPK----GEELTYDYQFDFED-DQHKIPCHCGAWNCRK 5300
Cdd:cd10541   182 FVDTHDLRFPWVAFFASKrikaGTELTWDYNYEVGSvEGKELLCCCGSNECRG 234

PHA03247

large tegument protein UL36; Provisional

1827-2213

3.94e-09

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 63.80 E-value: 3.94e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1827 PALHLRIPPQPGALGSPPPAAAPTIFIGSPTTPAGLSTSAdgflkppagtvpGPDSPGelflklPPQVPAQVPsQDPFGL 1906
Cdd:PHA03247 2725 PAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTA------------GPPAPA------PPAAPAAGP-PRRLTR 2785

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1907 APAYALEPRFPTAPSTYPPYPSPAGAPVQPPTLGTSSRPGTGQPgefhtTPPGTPRHQPSTPDPFLKPRCPSLDNLAvpe 1986
Cdd:PHA03247 2786 PAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP-----PPTSAQPTAPPPPPGPPPPSLPLGGSVA--- 2857

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1987 sPGvGGGKASEPLLSPPPFGESRKALEVKKeelgASSPSYGPPNLGFVDSPSSGPHLGSLELKAPDVFKAPLTPRAS-QV 2065
Cdd:PHA03247 2858 -PG-GDVRRRPPSRSPAAKPAAPARPPVRR----LARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQpQP 2931

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2066 EPQSPGLGLRPQEPSPAQALAPSPPSHSDIFR-----PGPYPDPYAQpPLTPRPQPPAPESccalPPRSLPSDPFSRVPA 2140
Cdd:PHA03247 2932 PPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWlgalvPGRVAVPRFR-VPQPAPSREAPAS----STPPLTGHSLSRVSS 3006

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2141 SPQSQSSSQSPlTPRPLSAEAFCPSP--------VTPRFQSPDPYSRPPSRPQSRDPFAPLHKPPRPQPPEVAFKSGPLA 2212
Cdd:PHA03247 3007 WASSLALHEET-DPPPVSLKQTLWPPddtedsdaDSLFDSDSERSDLEALDPLPPEPHDPFAHEPDPATPEAGARESPSS 3085


                  .
gi 558137628 2213 H 2213
Cdd:PHA03247 3086 Q 3086

PHD_SF

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...

275-320

4.81e-09

Pssm-ID: 276966 [Multi-domain] Cd Length: 48 Bit Score: 55.02 E-value: 4.81e-09

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 558137628  275 VCQACRKPGND-SKMLVCETCDKGYHTFCLKPPMEELPAH-SWKCKAC 320
Cdd:cd15489     1 SCIVCGKGGDLgGELLQCDGCGKWFHADCLGPPLSSFVPNgKWICPVC 48

PHA03247

large tegument protein UL36; Provisional

1832-2199

5.46e-09

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 63.42 E-value: 5.46e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1832 RIPPQPGALGSPPPAAAPTIFIGSPTTPAGLSTSADGFLKPPAGTVPGPDSPGelflkLPPQVPAQVPSQDPFGLAPAYA 1911
Cdd:PHA03247 2662 SRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHA-----LVSATPLPPGPAAARQASPALP 2736

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1912 LEPRFPTAPSTYPPYpspaGAPVQPPTLGTSSRPGTGQPGefhTTPPGTPrhQPSTPDPFLKPRCPSLDNLAVPESPGVG 1991
Cdd:PHA03247 2737 AAPAPPAVPAGPATP----GGPARPARPPTTAGPPAPAPP---AAPAAGP--PRRLTRPAVASLSESRESLPSPWDPADP 2807

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1992 GGKASEPLLSPPPFGESRKALEVKKEELGASSPSYGPPnlgfvdSPSSGPHLGSLELKAPDVFKAPltPRASQVEPQSPG 2071
Cdd:PHA03247 2808 PAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP------PPPSLPLGGSVAPGGDVRRRPP--SRSPAAKPAAPA 2879

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2072 LG-----LRPQEPSPAQALAPSPPShsdifrPGPYPDPYAQPPLTPRPQPPAPES-CCALPPRSLPSDPFSrvPASPQSQ 2145
Cdd:PHA03247 2880 RPpvrrlARPAVSRSTESFALPPDQ------PERPPQPQAPPPPQPQPQPPPPPQpQPPPPPPPRPQPPLA--PTTDPAG 2951

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 558137628 2146 SSSQSPLTPRPLSAEAFCPSPVTPRFQSPDPysrPPSRPQSRDPFAPLHKPPRP 2199
Cdd:PHA03247 2952 AGEPSGAVPQPWLGALVPGRVAVPRFRVPQP---APSREAPASSTPPLTGHSLS 3002

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

228-273

6.32e-09

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 54.53 E-value: 6.32e-09

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 558137628    228 RCAVCEGPGELCDLFFCTSCGHHYHGACLDTALT-ARKRAGWQCPEC 273
Cdd:smart00249    1 YCSVCGKPDDGGELLQCDGCDRWYHQTCLGPPLLeEEPDGKWYCPKC 47

PHA03247

large tegument protein UL36; Provisional

1827-2212

8.16e-09

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 62.65 E-value: 8.16e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1827 PALHLRIPPQPGALGSPPPAAAPTifigSPTTPAGLSTSADGFLKPPAGTVPGPDSPGelflklPPQVPAQVPsQDPFGL 1906
Cdd:PHA03247 2717 SATPLPPGPAAARQASPALPAAPA----PPAVPAGPATPGGPARPARPPTTAGPPAPA------PPAAPAAGP-PRRLTR 2785

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1907 APAYALEPRFPTAPSTYPPYPSPAGAPVQPPTLGTSSRPGTGQPgefhtTPPGTPRHQPSTPDPFLKPRCPSLDNLAvpe 1986
Cdd:PHA03247 2786 PAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP-----PPTSAQPTAPPPPPGPPPPSLPLGGSVA--- 2857

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1987 sPGvGGGKASEPLLSPPPFGESRKALEVKKeelgASSPSYGPPNLGFVDSPSSGPHLGSLELKAPDVFKAPLTPRAS-QV 2065
Cdd:PHA03247 2858 -PG-GDVRRRPPSRSPAAKPAAPARPPVRR----LARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQpQP 2931

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2066 EPQSPGLGLRPQEPSPAQALAPSPPSHSDIFR-----PGPYPDPYAQPPLTPRPQPpAPESccalPPRSLPSDPFSRVPA 2140
Cdd:PHA03247 2932 PPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWlgalvPGRVAVPRFRVPQPAPSRE-APAS----STPPLTGHSLSRVSS 3006

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2141 SPQSQSSSQSPlTPRPLS----------------AEAFCPSPVTPRFQSPDPYSRPPSRPQSRDPFAPLHKPPRPQPPEV 2204
Cdd:PHA03247 3007 WASSLALHEET-DPPPVSlkqtlwppddtedsdaDSLFDSDSERSDLEALDPLPPEPHDPFAHEPDPATPEAGARESPSS 3085


                  ....*...
gi 558137628 2205 AFKSGPLA 2212
Cdd:PHA03247 3086 QFGPPPLS 3093

PHD_BAZ2B

cd15630

PHD finger found in bromodomain adjacent to zinc finger domain protein 2B (BAZ2B); BAZ2B, also ...

276-320

8.75e-09

PHD finger found in bromodomain adjacent to zinc finger domain protein 2B (BAZ2B); BAZ2B, also termed WALp4, is a bromodomain-containing protein whose biological role is still elusive. It shows high sequence similarly with BAZ2A, which is the large subunit of the SNF2h-containing chromatin-remodeling complex NoRC that induces nucleosome sliding in an ATP-and histone H4 tail-dependent fashion. BAZ2B contains a TAM (TIP5/ARBP/MBD) domain, an Apolipophorin-III like 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: 277100 Cd Length: 49 Bit Score: 54.21 E-value: 8.75e-09

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628  276 CQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15630     3 CQICRKGDNEELLLLCDGCDKGCHTYCHRPKITTIPEGDWFCPAC 47

ePHD_KMT2A

cd15693

Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant ...

133-219

9.23e-09

Pssm-ID: 277163 Cd Length: 113 Bit Score: 56.55 E-value: 9.23e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  133 GGSCWAHHWCAVWSAGVWGKGGPELCGVDKAIFSGISQRCSHCTRLGASIPCRSPGCPRLYHFPCATASG-SFLSMKtlQ 211
Cdd:cd15693    24 GQNEWTHVNCALWSAEVFEDDDGSLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSCTSNYHFMCSRAKNcVFLEDK--K 101


                  ....*...
gi 558137628  212 LLCPEHSE 219
Cdd:cd15693   102 VYCQRHKD 109

PHD2_CHD_II

cd15532

PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...

275-320

1.26e-08

Pssm-ID: 277007 [Multi-domain] Cd Length: 43 Bit Score: 53.44 E-value: 1.26e-08

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  275 VCQACRKPGNdskMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15532     1 FCRVCKDGGE---LLCCDGCPSSYHLHCLNPPLAEIPDGDWFCPRC 43

PHD_UHRF1_2

cd15525

PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein UHRF1 and ...

278-320

1.27e-08

Pssm-ID: 277000 Cd Length: 47 Bit Score: 53.91 E-value: 1.27e-08

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 558137628  278 ACRKPGN---DSKMLVCETCDKGYHTFCLKPPMEELPAHS-WKCKAC 320
Cdd:cd15525     1 ACHVCGGkqdPEKQLLCDECDMAYHLYCLDPPLTSLPDDDeWYCPDC 47

PHD_PHF21A

cd15523

PHD finger found in PHD finger protein 21A (PHF21A); PHF21A (also termed BHC80a or BRAF35-HDAC ...

1156-1201

1.46e-08

PHD finger found in PHD finger protein 21A (PHF21A); PHF21A (also termed BHC80a or BRAF35-HDAC complex protein BHC80) along with HDAC1/2, CtBP1, CoREST, and BRAF35, is associated with LSD1, a lysine (K)-specific histone demethylase. It inhibits LSD1-mediated histone demethylation in vitro. PHF21A is predominantly present in the central nervous system and spermatogenic cells and is one of the six components of BRAF-HDAC complex (BHC) involved in REST-dependent transcriptional repression of neuron-specific genes in non-neuronal cells. It acts as a scaffold protein in BHC in neuronal as well as non-neuronal cells and also plays a role in spermatogenesis. PHF21A contains a C-terminal plant homeodomain (PHD) finger that is responsible for the binding directly to each of five other components of BHC, and of organizing BHC mediating transcriptional repression.

Pssm-ID: 276998 [Multi-domain] Cd Length: 43 Bit Score: 53.55 E-value: 1.46e-08

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628 1156 VCEVCGQASDpsrLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15523     1 FCSVCRKSGE---LLMCDTCSLVYHLDCLDPPLKTIPKGMWICPKC 43

PHD_BAZ2B

cd15630

PHD finger found in bromodomain adjacent to zinc finger domain protein 2B (BAZ2B); BAZ2B, also ...

1155-1203

2.62e-08

Pssm-ID: 277100 Cd Length: 49 Bit Score: 53.05 E-value: 2.62e-08

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 558137628 1155 IVCEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWCVS 1203
Cdd:cd15630     1 VYCQICRKGDNEELLLLCDGCDKGCHTYCHRPKITTIPEGDWFCPACIA 49

SET

cd08161

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...

5164-5278

2.76e-08

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, Enhancer-of-zeste, Trithorax (SET) domain superfamily corresponds to SET domain-containing lysine methyltransferases, which catalyze site and state-specific methylation of lysine residues in histones that are fundamental in epigenetic regulation of gene activation and silencing in eukaryotic organisms. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains has been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as N-SET and C-SET. C-SET forms an unusual and conserved knot-like structure of probable functional importance. In addition to N-SET and C-SET, an insert region (I-SET) and flanking regions of high structural variability form part of the overall structure. Some family members contain a pre-SET domain, which is found in a number of histone methyltransferases (HMTase), and a post-SET domain, which harbors a zinc-binding site.

Pssm-ID: 380914 [Multi-domain] Cd Length: 72 Bit Score: 53.41 E-value: 2.76e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5164 NVYLARSRIQGLGLYAAKDLEKhtmvieyiGTIIrnevanrrekiyeeqnrgiymfrinnehvidatltgGPARYINHSC 5243
Cdd:cd08161     1 EIRPSTIPGAGFGLFATRDIPK--------GEVI------------------------------------GLARFINHSC 36

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 558137628 5244 APNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDY 5278
Cdd:cd08161    37 EPNCEFEEVYVGGKPRVFIVALRDIKAGEELTVDY 71

PHD3_PHF14

cd15563

PHD finger 3 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...

1156-1201

2.79e-08

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

Pssm-ID: 277038 Cd Length: 49 Bit Score: 52.78 E-value: 2.79e-08

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 558137628 1156 VCEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKG---GWKCKWC 1201
Cdd:cd15563     1 ECCVCKQTGDNSQLVRCDECKLCYHFGCLDPPLKKSPKQrgyGWVCEEC 49

PHD1_AIRE

cd15539

PHD finger 1 found in autoimmune regulator (AIRE); AIRE, also termed autoimmune ...

1157-1201

2.95e-08

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: 52.45 E-value: 2.95e-08

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628 1157 CEVCGqasDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15539     2 CAVCG---DGGELLCCDGCPRAFHLACLVPPLTLIPSGTWRCSSC 43

PHD_SF

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...

1233-1283

3.15e-08

Pssm-ID: 276966 [Multi-domain] Cd Length: 48 Bit Score: 52.70 E-value: 3.15e-08

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 558137628 1233 TCPICHAPYVEEDLLIQCRHCERWMHAGCESLFTEddvEQAADEGFDCVSC 1283
Cdd:cd15489     1 SCIVCGKGGDLGGELLQCDGCGKWFHADCLGPPLS---SFVPNGKWICPVC 48

PHD_SF

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...

228-273

4.19e-08

Pssm-ID: 276966 [Multi-domain] Cd Length: 48 Bit Score: 52.32 E-value: 4.19e-08

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 558137628  228 RCAVCEGPGELCD-LFFCTSCGHHYHGACLDTAL-TARKRAGWQCPEC 273
Cdd:cd15489     1 SCIVCGKGGDLGGeLLQCDGCGKWFHADCLGPPLsSFVPNGKWICPVC 48

PHD1_BPTF

cd15559

PHD finger 1 found in bromodomain and PHD finger-containing transcription factor (BPTF); BPTF, ...

276-320

7.38e-08

PHD finger 1 found in bromodomain and PHD finger-containing transcription factor (BPTF); BPTF, also termed nucleosome-remodeling factor subunit BPTF, or fetal Alz-50 clone 1 protein (FAC1), or fetal Alzheimer antigen, functions as a transcriptional regulator that exhibits altered expression and subcellular localization during neuronal development and neurodegenerative diseases such as Alzheimer's disease. It interacts with the human orthologue of the Kelch-like Ech-associated protein (Keap1). Its function and subcellular localization can be regulated by Keap1. Moreover, BPTF is a novel DNA-binding protein that recognizes the DNA sequence CACAACAC and represses transcription through this site in a phosphorylation-dependent manner. Furthermore, BPTF interacts with the Myc-associated zinc finger protein (ZF87/MAZ) and alters its transcriptional activity, which has been implicated in gene regulation in neurodegeneration. Some family members contain two or three plant homeodomain (PHD) fingers, which may be involved in complex formation with histone H3 trimethylated at K4 (H3K4me3). This family corresponds to the first PHD finger.

Pssm-ID: 277034 [Multi-domain] Cd Length: 43 Bit Score: 51.65 E-value: 7.38e-08

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628  276 CQACRKPGNdskMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15559     2 CRVCHKLGD---LLCCETCSAVYHLECVDPPLEEVPEEDWQCEVC 43

PHD_SF

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...

1106-1154

1.13e-07

Pssm-ID: 276966 [Multi-domain] Cd Length: 48 Bit Score: 51.16 E-value: 1.13e-07

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 558137628 1106 MCVVCGSfGRGAEGHLLACSQCSQCYHPYCVNSKITKVMLLKGWRCVEC 1154
Cdd:cd15489     1 SCIVCGK-GGDLGGELLQCDGCGKWFHADCLGPPLSSFVPNGKWICPVC 48

PHA03307

transcriptional regulator ICP4; Provisional

1825-2243

4.71e-07

transcriptional regulator ICP4; Provisional

Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 56.72 E-value: 4.71e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1825 DRPALHLRIPPQPGALGSPPPAAAPTIFIGSPTTPAGLSTSadgflKPPAGTVPGPDSPGELFLKLPPQVPAQvpsqdPF 1904
Cdd:PHA03307   29 GDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPT-----GPPPGPGTEAPANESRSTPTWSLSTLA-----PA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1905 GLAPAYALEPRFPTAPSTYPPYPSPAG-APVQPPTLGTSSRPGTGQPGEFHTTPPGTPRHQPSTPDPFLKPRCPSLDNLA 1983
Cdd:PHA03307   99 SPAREGSPTPPGPSSPDPPPPTPPPASpPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSS 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1984 VPES-PGVGGGKASEPLLSPPPFGESRKALEVKKEELGASSPSYGPP---NLGFVDSPSSGPHLGSLELKAPDVFKAPLT 2059
Cdd:PHA03307  179 PEETaRAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGrsaADDAGASSSDSSSSESSGCGWGPENECPLP 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2060 PRASQVEPQSPGLGLRPQEPSPaqaLAPSPPSHSDIFRPGPYPDPYAqppltprpqppapESCCALPPRSLPSDPFSRVP 2139
Cdd:PHA03307  259 RPAPITLPTRIWEASGWNGPSS---RPGPASSSSSPRERSPSPSPSS-------------PGSGPAPSSPRASSSSSSSR 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2140 ASPQSQSSSQSPlTPRPLSAEAFCPSPVTPRFQSPDPYSRPPSRPQ----SRDPFAPLHKPPRPQPPEVAFKSGPLAHTP 2215
Cdd:PHA03307  323 ESSSSSTSSSSE-SSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKrprpSRAPSSPAASAGRPTRRRARAAVAGRARRR 401

                         410       420
                  ....*....|....*....|....*...
gi 558137628 2216 LGAGGFPAALPsgPAGELHAKVPSGQPP 2243
Cdd:PHA03307  402 DATGRFPAGRP--RPSPLDAGAASGAFY 427

HMG

smart00398

high mobility group;

1748-1799

5.08e-07

high mobility group;

Pssm-ID: 197700 [Multi-domain] Cd Length: 70 Bit Score: 50.01 E-value: 5.08e-07

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 558137628   1748 VLYANINFPNLKQDYPDWSS--RCKQIMKLWRKVPAADKAPYLQKAKDNRAAHR 1799
Cdd:smart00398   10 MLFSQENRAKIKAENPDLSNaeISKKLGERWKLLSEEEKAPYEEKAKKDKERYE 63

PHD2_PHF12_Rco1

cd15534

PHD finger 2 found in PHD finger protein 12 (PHF12), yeast Rco1, and similar proteins; PHF12, ...

1156-1198

5.33e-07

PHD finger 2 found in PHD finger protein 12 (PHF12), yeast Rco1, and similar proteins; PHF12, also termed PHD factor 1 (Pf1), is a plant homeodomain (PHD) zinc finger-containing protein that bridges the transducin-like enhancer of split (TLE) corepressor to the mSin3A-histone deacetylase (HDAC)-complex, and further represses transcription at targeted genes. PHF12 also interacts with MRG15 (mortality factor-related genes on chromosome 15), a member of the mortality factor (MORF) family of proteins implicated in regulating cellular senescence. PHF12 contains two plant homeodomain (PHD) zinc fingers followed by a polybasic region. The PHD fingers function downstream of phosphoinositide signaling triggered by the interaction between polybasic regions and phosphoinositides. This subfamily also includes yeast transcriptional regulatory protein Rco1 and similar proteins. Rco1 is a component of the Rpd3S histone deacetylase complex that plays an important role at actively transcribed genes. Rco1 contains two PHD fingers, which are required for the methylation of histone H3 lysine 36 (H3K36) nucleosome recognition by Rpd3S. This model corresponds to the second PHD finger.

Pssm-ID: 277009 Cd Length: 47 Bit Score: 49.27 E-value: 5.33e-07

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 558137628 1156 VCEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGG-WKC 1198
Cdd:cd15534     1 VCFKCNRSCRVAPLIQCDYCPLLFHLDCLDPPLTHPPATGrWMC 44

PHA03247

large tegument protein UL36; Provisional

3928-4214

5.65e-07

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.87 E-value: 5.65e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 3928 RPLQNNAGPQPAKPGSVPQSGQglPGAGVMPTvGQFRAQLQGvlAKNPQLRHLSPQQQQQLQALLMQRQLQQSQAirqAP 4007
Cdd:PHA03247 2576 RPSEPAVTSRARRPDAPPQSAR--PRAPVDDR-GDPRGPAPP--SPLPPDTHAPDPPPPSPSPAANEPDPHPPPT---VP 2647

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4008 SYQEPGTQPSPLQGLLGRQPQVGGFPGSQTGPLQ------------ELGAGLRPQGPPRLPAPQ-GALSTGPVPGPVHPT 4074
Cdd:PHA03247 2648 PPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQrprrraarptvgSLTSLADPPPPPPTPEPApHALVSATPLPPGPAA 2727

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4075 PPPSSPQEPKRPSQLPSPSSQLPSEAQLPPTQPGT------PKPQALPLELPPGKISPAAAQLADTLFGKGLGPWDPPDN 4148
Cdd:PHA03247 2728 ARQASPALPAAPAPPAVPAGPATPGGPARPARPPTtagppaPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADP 2807

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 558137628 4149 PAEAQKP---EQSSLVPGHPEQVNGQAVPEPSylSIKQEPREEPCALGAQVV------KREANGEPIGTPGTSNH 4214
Cdd:PHA03247 2808 PAAVLAPaaaLPPAASPAGPLPPPTSAQPTAP--PPPPGPPPPSLPLGGSVApggdvrRRPPSRSPAAKPAAPAR 2880

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

1233-1283

6.07e-07

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 49.13 E-value: 6.07e-07

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 558137628   1233 TCPICHAPYvEEDLLIQCRHCERWMHAGCESLFTEDDVEqaaDEGFDCVSC 1283
Cdd:smart00249    1 YCSVCGKPD-DGGELLQCDGCDRWYHQTCLGPPLLEEEP---DGKWYCPKC 47

PHD1_CHD_II

cd15531

PHD finger 1 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...

1157-1201

6.30e-07

PHD finger 1 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD proteins includes chromodomain-helicase-DNA-binding protein CHD3, CHD4, and CHD5, which are nuclear and ubiquitously expressed chromatin remodelling ATPases generally associated with histone deacetylases (HDACs). They are involved in DNA Double Strand Break (DSB) signaling, DSB repair and/or p53-dependent pathways such as apoptosis and senescence, as well as in the maintenance of genomic stability, and/or cancer prevention. They function as subunits of the Nucleosome Remodelling and Deacetylase (NuRD) complex, which is generally associated with gene repression, heterochromatin formation, and overall chromatin compaction. In contrast to the class I CHD enzymes (CHD1 and CHD2), class II CHD proteins lack identifiable DNA-binding domains, but possess a C-terminal coiled-coil region. Moreover, in addition to the tandem chromodomains and a helicase domain, they all harbor tandem plant homeodomain (PHD) zinc fingers involved in the recognition of methylated histone tails. This model corresponds to the first PHD finger.

Pssm-ID: 277006 [Multi-domain] Cd Length: 43 Bit Score: 48.75 E-value: 6.30e-07

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628 1157 CEVCGQASDpsrLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15531     2 CEVCQQGGE---IILCDTCPRAYHLVCLDPELEKAPEGKWSCPHC 43

PHD1_Snt2p_like

cd15497

PHD finger 1 found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and ...

1157-1201

6.69e-07

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

Pssm-ID: 276972 Cd Length: 48 Bit Score: 48.84 E-value: 6.69e-07

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 558137628 1157 CEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGG--WKCKWC 1201
Cdd:cd15497     2 CKVCKEWCASDDSVRCDECKVSYHLLCVDPPLTKKPNRGfvWSCAPC 48

PHD_PRHA_like

cd15504

PHD finger found in Arabidopsis thaliana pathogenesis-related homeodomain protein (PRHA) and ...

1156-1201

6.90e-07

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: 48.97 E-value: 6.90e-07

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 558137628 1156 VCEVC--GQASDPSRLLLCD-DCDISYHTYCLDPPLLT--VPKG--GWKCKWC 1201
Cdd:cd15504     1 FCAKCqsGEASPDNDILLCDgGCNRAYHQKCLEPPLLTedIPPEdeGWLCPLC 53

PHD1_PHF12

cd15533

PHD finger 1 found in PHD finger protein 12 (PHF12); PHF12, also termed PHD factor 1 (Pf1), is ...

1156-1201

7.17e-07

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

Pssm-ID: 277008 [Multi-domain] Cd Length: 45 Bit Score: 48.89 E-value: 7.17e-07

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 558137628 1156 VCEVCGQASDpsrLLLCDDCDISYHTYCLDPPL--LTVPKGGWKCKWC 1201
Cdd:cd15533     1 YCDSCGEGGD---LLCCDRCPASFHLQCCNPPLdeEDLPPGEWLCHRC 45

PHD1_KMT2C_like

PHD finger 1 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...

1157-1201

8.63e-07

Pssm-ID: 276984 Cd Length: 48 Bit Score: 48.46 E-value: 8.63e-07

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 558137628 1157 CEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVP--KGGWKCKWC 1201
Cdd:cd15509     2 CAVCDSPGDLSDLLFCTSCGQHYHGSCLDPAVRPTPlvRAGWQCPEC 48

ePHD_PHF6_like

cd15673

Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11); ...

136-217

1.10e-06

Pssm-ID: 277143 Cd Length: 116 Bit Score: 50.47 E-value: 1.10e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  136 CWAHHWCAVWSAGVWGK--------GGPELCGVDKAIFSGISQRCSHCTRLGASIPCRSPGCPRLYHFPCATASGSFLSM 207
Cdd:cd15673    23 IAAHHNCMLFSSGLVQYvspnendfGGFDIEDVKKEIKRGRKLKCNLCKKTGATIGCDVKQCKKTYHYHCAKKDDAKIIE 102

                          90
                  ....*....|....
gi 558137628  208 KTLQ----LLCPEH 217
Cdd:cd15673   103 RNSQgiyrVYCKNH 116

PHD_Phf1p_Phf2p_like

cd15502

PHD finger found in Schizosaccharomyces pombe SWM histone demethylase complex subunits Phf1 ...

1154-1201

1.33e-06

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: 48.20 E-value: 1.33e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 558137628 1154 CIVCEvCGQASDPSRLLLCDDCDISYHTYCLDPP----LLTVPKGGWKCKWC 1201
Cdd:cd15502     2 CIVCQ-RGHSPKSNRIVFCDGCNTPYHQLCHDPSiddeVVEDPDAEWFCKKC 52

PHD_TIF1_like

cd15541

PHD finger found in the transcriptional intermediary factor 1 (TIF1) family and similar ...

1156-1201

1.38e-06

PHD finger found in the transcriptional intermediary factor 1 (TIF1) family and similar proteins; The TIF1 family of transcriptional cofactors includes TIF1alpha (TRIM24), TIF1beta (TRIM28), TIF1gamma (TRIM33), and TIF1delta (TRIM66), which are characterized by an N-terminal RING-finger B-box coiled-coil (RBCC/TRIM) motif and plant homeodomain (PHD) finger followed by a bromodomain in the C-terminal region. TIF1 proteins couple chromatin modifications to transcriptional regulation, signaling, and tumor suppression. They exert a deacetylase-dependent silencing effect when tethered to a promoter region. TIF1alpha, TIF1beta, and TIF1delta can homodimerize and contain a PXVXL motif necessary and sufficient for heterochromatin protein 1(HP1) binding. TIF1alpha and TIF1beta bind nuclear receptors and Kruppel-associated boxes (KRAB) specifically and respectively. In contrast, TIF1delta appears to lack nuclear receptor- and KRAB-binding activity. Moreover, TIF1delta is specifically involved in heterochromatin-mediated gene silencing during postmeiotic phases of spermatogenesis. TIF1gamma is structurally closely related to TIF1alpha and TIF1beta, but has very little functional features in common with them. It does not interact with the KRAB silencing domain of KOX1 or the heterochromatinic proteins HP1alpha, beta, and gamma. It cannot bind to nuclear receptors (NRs). This family also includes Sp100/Sp140 family proteins, the nuclear body SP100 and SP140. Sp110 is a leukocyte-specific component of the nuclear body. It may function as a nuclear hormone receptor transcriptional coactivator that may play a role in inducing differentiation of myeloid cells. It is also involved in resisting intracellular pathogens and functions as an important drug target for preventing intracellular pathogen diseases, such as tuberculosis, hepatic veno-occlusive disease, and intracellular cancers. SP140 is an interferon inducible nuclear leukocyte-specific protein involved in primary biliary cirrhosis and a risk factor in chronic lymphocytic leukemia. It is also implicated in innate immune response to human immunodeficiency virus type 1 (HIV-1) by binding to the virus viral infectivity factor (Vif) protein. Both Sp110 and Sp140 contain a SAND domain, a plant homeodomain (PHD) finger, and a bromodomain (BRD).

Pssm-ID: 277016 [Multi-domain] Cd Length: 43 Bit Score: 47.72 E-value: 1.38e-06

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628 1156 VCEVCGqasDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15541     1 WCAVCQ---NGGELLCCDKCPRVFHLDCHIPPIPEFPSGEWSCSLC 43

PHD3_PHF14

cd15563

PHD finger 3 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...

275-320

1.61e-06

Pssm-ID: 277038 Cd Length: 49 Bit Score: 47.77 E-value: 1.61e-06

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 558137628  275 VCQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELP---AHSWKCKAC 320
Cdd:cd15563     1 ECCVCKQTGDNSQLVRCDECKLCYHFGCLDPPLKKSPkqrGYGWVCEEC 49

SET_SpSET3-like

cd19183

SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...

5175-5289

2.18e-06

SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET domain-containing protein 3 (SETD3) and similar proteins; Schizosaccharomyces pombe SETD3 functions as a transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. It is required for both, gene activation and repression.

Pssm-ID: 380960 Cd Length: 173 Bit Score: 51.25 E-value: 2.18e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5175 LGLYAAKDLEKHTMVIEYIGtiirnEVANRREKIYEEQNRgiY----------MFRINNEHVIDATLTGGPARYINHSCA 5244
Cdd:cd19183    14 FGLFADRPIPAGDPIQELLG-----EIGLQSEYIADPENQ--YqilgapkphvFFHPQSPLYIDTRRSGSVARFIRRSCR 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 558137628 5245 PNCVAEVVTFDK--EDKIIIISSRRIPKGEELTYDYQFDFEDDQHKI 5289
Cdd:cd19183    87 PNAELVTVASDSgsVLKFVLYASRDISPGEEITIGWDWDNPHPFRRF 133

SET_AtSUVH-like

cd10545

SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...

5189-5278

2.28e-06

SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar proteins; Arabidopsis thaliana SUVH protein (also termed suppressor of variegation 3-9 homolog protein) is a histone-lysine N-methyltransferase that methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression. Some family members contain a post-SET domain which binds a Zn2+ ion. Most family members, except for Arabidopsis thaliana SUVH9, contain a post-SET domain which harbors a zinc-binding site.

Pssm-ID: 380943 [Multi-domain] Cd Length: 232 Bit Score: 52.41 E-value: 2.28e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5189 VIEYIGTIIRNEVANRREKiyeeqnRGIYMFRINN-------------------------------EHVIDATLTGGPAR 5237
Cdd:cd10545   112 ICEYVGELLDTSEADTRSG------NDDYLFDIDNrqtnrgwdggqrldvgmsdgerssaedeessEFTIDAGSFGNVAR 185

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 558137628 5238 YINHSCAPNCVAEVVTFDKEDKIIII----SSRRIPKGEELTYDY 5278
Cdd:cd10545   186 FINHSCSPNLFVQCVLYDHNDLRLPRvmlfAADNIPPLQELTYDY 230

PHD1_MTF2_PHF19_like

cd15499

PHD finger 1 found in polycomb repressive complex 2 (PRC2)-associated polycomb-like (PCL) ...

1156-1204

2.63e-06

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: 47.49 E-value: 2.63e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 558137628 1156 VCEVCG--QASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWCVSC 1204
Cdd:cd15499     1 TCSICGgaEARDGNEILICDKCDKGYHQLCHSPKVRTSPLEGDEKWFCSRC 51

PHD2_PHF14

cd15562

PHD finger 2 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...

229-273

3.13e-06

Pssm-ID: 277037 Cd Length: 50 Bit Score: 47.02 E-value: 3.13e-06

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 558137628  229 CAVCEGPGELCDLFFCTSCGHHYHGACLDTALT----ARKRAGWQCPEC 273
Cdd:cd15562     2 CGICKKSNDQHLLALCDTCKLYYHLGCLDPPLTrmpkKTKNSGWQCSEC 50

ePHD1_PHF6

cd15710

Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...

4825-4888

3.34e-06

Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. PHF6 contains two non-canonical ePHD fingers, this model corresponds to the first ePHD finger. PHF6, also termed the X-linked mental retardation disorder Borjeson-Forssman-Lehmann syndrome-associated protein, is a nucleolus, ribosomal RNA promoter-associated protein that regulates cell cycle progression by suppressing ribosomal RNA synthesis. It has been implicated in cell cycle control, genomic maintenance, and tumor suppression. PHF6 shows transcriptional repression activity through directly interacting with the nucleosome remodeling and deacetylation complex component RBBP4. .

Pssm-ID: 277180 Cd Length: 115 Bit Score: 49.19 E-value: 3.34e-06

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 558137628 4825 HLNCALWSTEVYETQ-------GGALMNVEVALHRGLLTKCSLCQRTGATSSCNRMRCPNVYHFACAIRAK 4888
Cdd:cd15710    26 HHKCMLFSSALVSSHsdsenlgGFSIEDVQKEIKRGTKLMCSLCHCPGATIGCDVKTCHRTYHYYCALHDK 96

SET_SETD5

cd19181

SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...

5177-5298

3.37e-06

SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and similar proteins; SETD5 is a probable transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. SETD5 loss-of-function mutations are a likely cause of a familial syndromic intellectual disability with variable phenotypic expression.

Pssm-ID: 380958 Cd Length: 150 Bit Score: 50.01 E-value: 3.37e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5177 LYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINN--EHVIDATLTGGPARYINHSCAPNCVAEVVTF 5254
Cdd:cd19181    21 LRAARDLALDTLIIEYRGKVMLRQQFEVNGHFFKRPYPFVLFYSKFNgvEMCVDARTFGNDARFIRRSCTPNAEVRHMIA 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628 5255 DKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIPCHC--GAWNC 5298
Cdd:cd19181   101 DGMIHLCIYAVAAIAKDAEVTIAFDYEYSNCNYKVDCAChkGNRNC 146

PHD1_Rco1

cd15535

PHD finger 1 found in Saccharomyces cerevisiae transcriptional regulatory protein Rco1 and ...

276-320

3.97e-06

PHD finger 1 found in Saccharomyces cerevisiae transcriptional regulatory protein Rco1 and similar proteins; Rco1 is a component of the Rpd3S histone deacetylase complex that plays an important role at actively transcribed genes. Rco1 contains two plant homeodomain (PHD) fingers, which are required for the methylation of histone H3 lysine 36 (H3K36) nucleosome recognition by Rpd3S. This model corresponds to the first PHD finger.

Pssm-ID: 277010 [Multi-domain] Cd Length: 45 Bit Score: 46.64 E-value: 3.97e-06

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 558137628  276 CQACRKPGNdskMLVCETCDKGYHTFCLKPPMEE--LPAHSWKCKAC 320
Cdd:cd15535     2 CSACGGYGS---FLCCDGCPRSFHFSCLDPPLEEdnLPDDEWFCNEC 45

PHD2_KMT2A_like

cd15507

PHD finger 2 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...

1154-1204

5.24e-06

PHD finger 2 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This family includes histone-lysine N-methyltransferase trithorax (Trx) like proteins, KMT2A (MLL1) and KMT2B (MLL2), which comprise the mammalian Trx branch of the 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 through 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 plant homeodomain (PHD) fingers, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the second PHD finger.

Pssm-ID: 276982 Cd Length: 50 Bit Score: 46.31 E-value: 5.24e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 558137628 1154 CIVCEVCGQASDPsrLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWCVSC 1204
Cdd:cd15507     2 CHVCGRKGQAQKQ--LLECEKCQRGYHVDCLGPSYPTKPTRKKKTWICSKC 50

PHD_Phf1p_Phf2p_like

cd15502

PHD finger found in Schizosaccharomyces pombe SWM histone demethylase complex subunits Phf1 ...

273-320

5.37e-06

Pssm-ID: 276977 Cd Length: 52 Bit Score: 46.66 E-value: 5.37e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 558137628  273 CKVCQACRKPGNDsKMLVCETCDKGYHTFCLKPPME----ELPAHSWKCKAC 320
Cdd:cd15502     2 CIVCQRGHSPKSN-RIVFCDGCNTPYHQLCHDPSIDdevvEDPDAEWFCKKC 52

PHD2_KAT6A_6B

cd15527

PHD finger 2 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ, ...

229-273

6.98e-06

Pssm-ID: 277002 Cd Length: 46 Bit Score: 45.83 E-value: 6.98e-06

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628  229 CAVCEGPGELCDLFFCTSCGHHYHGACLDTALTARKRAGWQCPEC 273
Cdd:cd15527     2 CSVCQDSGNADNLLFCDACDKGFHMECHDPPLTRMPKGKWVCQIC 46

PHD2_PHF14

cd15562

PHD finger 2 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...

275-320

7.56e-06

Pssm-ID: 277037 Cd Length: 50 Bit Score: 45.86 E-value: 7.56e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 558137628  275 VCQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHS----WKCKAC 320
Cdd:cd15562     1 SCGICKKSNDQHLLALCDTCKLYYHLGCLDPPLTRMPKKTknsgWQCSEC 50

Atrophin-1

pfam03154

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...

1937-2372

8.18e-06

Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 52.46 E-value: 8.18e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  1937 PTLGTSSRPGTGQPGEFHTTPPGTPRHQPSTPDPFLKPRCPSLDNLAVPESPGVGGGKASEPLLSPPPfgeSRKALEVKK 2016
Cdd:pfam03154  151 PQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPP---NQTQSTAAP 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  2017 EELGASSPSYGPPNLgfvdsPSsgPHlgslelkaPDVFKAPLTPRASQVEPQS-PGLGLRPQEPSPAQALAPSPPSHSDI 2095
Cdd:pfam03154  228 HTLIQQTPTLHPQRL-----PS--PH--------PPLQPMTQPPPPSQVSPQPlPQPSLHGQMPPMPHSLQTGPSHMQHP 292

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  2096 FRPGPYPDPyaqPPLTPRPQPPAPESCCALPPRSLPSDPFSRvPASPQSQSSSQSPLTPRPLSAEAFCPSPVTPRFQSPD 2175
Cdd:pfam03154  293 VPPQPFPLT---PQSSQSQVPPGPSPAAPGQSQQRIHTPPSQ-SQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPN 368

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  2176 PYS-RPPSRPQSRDPFA-PLHKPPrpqPPEVAFKSGPLAHTPLGAggFPAALPSGPAGElHAKVPSGQPPNFARS---PG 2250
Cdd:pfam03154  369 PQShKHPPHLSGPSPFQmNSNLPP---PPALKPLSSLSTHHPPSA--HPPPLQLMPQSQ-QLPPPPAQPPVLTQSqslPP 442

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  2251 TGAFVGTPSPMRFTFPQAVGEPSSLKPPVPQPGLPPPHGINSHFGPGPTLGKPQSTNYSVATGNFHPSGSPLGPSsgSTG 2330
Cdd:pfam03154  443 PAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPV--QIK 520

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 558137628  2331 EGYGLSPLRPQSVLPP---PVPDGSLPYPPHGASQRAGITSPVDK 2372
Cdd:pfam03154  521 EEALDEAEEPESPPPPprsPSPEPTVVNTPSHASQSARFYKHLDR 565

PHA03307

transcriptional regulator ICP4; Provisional

1841-2217

8.71e-06

transcriptional regulator ICP4; Provisional

Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 52.48 E-value: 8.71e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1841 GSPPPAAAPTIFIGSP----TTPAGLSTSADGFLKPPAGTVPGPDSP-GELFLKLPPQVPAQVPSQDPFGLAPAYALEPR 1915
Cdd:PHA03307   25 PATPGDAADDLLSGSQgqlvSDSAELAAVTVVAGAAACDRFEPPTGPpPGPGTEAPANESRSTPTWSLSTLAPASPAREG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1916 FPTAPSTYPPypspAGAPVQPPTLGTSSRPGTGQPGEFHTTPPGTPRHQPSTPDPFLKPRCP---------SLDNLAVPE 1986
Cdd:PHA03307  105 SPTPPGPSSP----DPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVasdaassrqAALPLSSPE 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1987 S--PGVGGGKASEPLLSPPPFGESRKALEVKKEELGASSPSYGPP---NLGFVDSPSSGPHLGSLELKAPDVFKAPLTPR 2061
Cdd:PHA03307  181 EtaRAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGrsaADDAGASSSDSSSSESSGCGWGPENECPLPRP 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2062 ASQVEPQSPGLGLRPQEPSPaqaLAPSPPSHSDIFRPGPYPDPYAQPPLTPRPQPPA----------------------- 2118
Cdd:PHA03307  261 APITLPTRIWEASGWNGPSS---RPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRAsssssssressssstssssessr 337

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2119 ------PESCCALPPRSLPSDPF------SRVPASPQSQSSSQSPLTPRPLSAEAFCPSPVTPRfqspdpySRPPSRPQS 2186
Cdd:PHA03307  338 gaavspGPSPSRSPSPSRPPPPAdpssprKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRR-------DATGRFPAG 410

                         410       420       430
                  ....*....|....*....|....*....|.
gi 558137628 2187 RdpfaplhkPPRPQPPEVAFKSGPLAHTPLG 2217
Cdd:PHA03307  411 R--------PRPSPLDAGAASGAFYARYPLL 433

PHD_PHF21A

cd15523

PHD finger found in PHD finger protein 21A (PHF21A); PHF21A (also termed BHC80a or BRAF35-HDAC ...

275-320

9.31e-06

Pssm-ID: 276998 [Multi-domain] Cd Length: 43 Bit Score: 45.46 E-value: 9.31e-06

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  275 VCQACRKPGndsKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15523     1 FCSVCRKSG---ELLMCDTCSLVYHLDCLDPPLKTIPKGMWICPKC 43

PHD1_AIRE

cd15539

PHD finger 1 found in autoimmune regulator (AIRE); AIRE, also termed autoimmune ...

276-320

9.60e-06

Pssm-ID: 277014 [Multi-domain] Cd Length: 43 Bit Score: 45.52 E-value: 9.60e-06

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628  276 CQACRKPGNdskMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15539     2 CAVCGDGGE---LLCCDGCPRAFHLACLVPPLTLIPSGTWRCSSC 43

PHD1_MTF2_PHF19_like

cd15499

PHD finger 1 found in polycomb repressive complex 2 (PRC2)-associated polycomb-like (PCL) ...

273-320

9.78e-06

Pssm-ID: 276974 Cd Length: 53 Bit Score: 45.95 E-value: 9.78e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 558137628  273 CKVCQACR-KPGNDskMLVCETCDKGYHTFCLKPPMEELPAHS---WKCKAC 320
Cdd:cd15499     2 CSICGGAEaRDGNE--ILICDKCDKGYHQLCHSPKVRTSPLEGdekWFCSRC 51

PHD1_CHD_II

cd15531

PHD finger 1 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...

276-320

1.09e-05

Pssm-ID: 277006 [Multi-domain] Cd Length: 43 Bit Score: 45.29 E-value: 1.09e-05

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628  276 CQACRKPGndsKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15531     2 CEVCQQGG---EIILCDTCPRAYHLVCLDPELEKAPEGKWSCPHC 43

PHD1_Rco1

cd15535

PHD finger 1 found in Saccharomyces cerevisiae transcriptional regulatory protein Rco1 and ...

1157-1201

1.16e-05

Pssm-ID: 277010 [Multi-domain] Cd Length: 45 Bit Score: 45.49 E-value: 1.16e-05

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 558137628 1157 CEVCGQasdPSRLLLCDDCDISYHTYCLDPPL--LTVPKGGWKCKWC 1201
Cdd:cd15535     2 CSACGG---YGSFLCCDGCPRSFHFSCLDPPLeeDNLPDDEWFCNEC 45

PHD1_BPTF

cd15559

PHD finger 1 found in bromodomain and PHD finger-containing transcription factor (BPTF); BPTF, ...

1157-1201

1.48e-05

Pssm-ID: 277034 [Multi-domain] Cd Length: 43 Bit Score: 45.10 E-value: 1.48e-05

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628 1157 CEVCGQASDpsrLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15559     2 CRVCHKLGD---LLCCETCSAVYHLECVDPPLEEVPEEDWQCEVC 43

PHD_UHRF1

cd15616

PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein 1 (UHRF1); ...

276-320

1.51e-05

Pssm-ID: 277088 Cd Length: 47 Bit Score: 44.96 E-value: 1.51e-05

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  276 CQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPA-HSWKCKAC 320
Cdd:cd15616     2 CHVCGGKQDPDKQLMCDECDMAFHIYCLNPPLSSIPDdEDWYCPEC 47

HMG_box

pfam00505

HMG (high mobility group) box;

1748-1799

1.61e-05

HMG (high mobility group) box;

Pssm-ID: 459837 [Multi-domain] Cd Length: 68 Bit Score: 45.68 E-value: 1.61e-05

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 558137628  1748 VLYANINFPNLKQDYPDWSSR--CKQIMKLWRKVPAADKAPYLQKAKDNRAAHR 1799
Cdd:pfam00505    9 FLFSKEQRAKLKAENPGLKNAeiSKILGEKWKALSEEEKKPYEEKAEKEKARYE 62

PHD1_Snt2p_like

cd15497

PHD finger 1 found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and ...

273-320

1.88e-05

Pssm-ID: 276972 Cd Length: 48 Bit Score: 44.99 E-value: 1.88e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 558137628  273 CKVC-QACrkPGNDSkmLVCETCDKGYHTFCLKPPMEELPAH--SWKCKAC 320
Cdd:cd15497     2 CKVCkEWC--ASDDS--VRCDECKVSYHLLCVDPPLTKKPNRgfVWSCAPC 48

HMG-box_SF

cd00084

high mobility group (HMG)-box domain superfamily; The High Mobility Group (HMG)-box is found ...

1749-1798

2.63e-05

high mobility group (HMG)-box domain superfamily; The High Mobility Group (HMG)-box is found in a variety of eukaryotic chromosomal proteins and transcription factors. HMGs bind to the minor groove of DNA and have been classified by DNA binding preferences. Two phylogenetically distinct groups of Class I proteins bind DNA in a sequence specific fashion and contain a single HMG box. One group (SOX-TCF) includes transcription factors, TCF-1, -3, -4, and also SRY and LEF-1, which bind four-way DNA junctions and duplex DNA targets. The second group (MATA) includes fungal mating type gene products MC, MATA1 and Ste11. Class II and III proteins (HMGB-UBF) bind DNA in a non-sequence specific fashion and contain two or more tandem HMG boxes. Class II members include non-histone chromosomal proteins, HMG1 and HMG2, which bind to bent or distorted DNA such as four-way DNA junctions, synthetic DNA cruciforms, kinked cisplatin-modified DNA, DNA bulges, cross-overs in supercoiled DNA, and can cause looping of linear DNA. Class III members include nucleolar and mitochondrial transcription factors, UBF and mtTF1, which bind four-way DNA junctions.

Pssm-ID: 438789 [Multi-domain] Cd Length: 59 Bit Score: 44.82 E-value: 2.63e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 558137628 1749 LYANINFPNLKQDYPDWSSrcKQIMKL----WRKVPAADKAPYLQKAKDNRAAH 1798
Cdd:cd00084     8 LFSKEKRPKLKKENPDLSF--TEISKLlgerWKELSEEEKQPYEEKAKEDKERY 59

ePHD_PHF11

cd15712

Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain ...

4821-4902

3.57e-05

Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of PHF11. PHF11, also termed BRCA1 C-terminus-associated protein, or renal carcinoma antigen NY-REN-34, is a transcriptional co-activator of the Th1 effector cytokine genes, interleukin-2 (IL2) and interferon-gamma (IFNG), co-operating with nuclear factor kappa B (NF-kappaB). It is involved in T-cell activation and viability. Polymorphisms within PHF11 are associated with total IgE, allergic asthma and eczema.

Pssm-ID: 277182 [Multi-domain] Cd Length: 115 Bit Score: 46.04 E-value: 3.57e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4821 DLWVHLNCALWSTEVYETQGGALMNVEVA---------LHRGLLTKCSLCQRTGATSSCNRMRCPNVYHFACAIRAKCMF 4891
Cdd:cd15712    20 NIAAHQNCLLYSSGFVESEEYNPLNLDRRfdvesvlneIKRGKRLKCNFCRKKGATVGCEERACRRSYHYFCALCDDAAI 99

                          90
                  ....*....|....*.
gi 558137628 4892 FKDKT-----MLCPMH 4902
Cdd:cd15712   100 ETDEVrgiyrVFCQKH 115

PHD_UHRF2

cd15617

PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein 2 (UHRF2); ...

273-320

4.80e-05

Pssm-ID: 277089 Cd Length: 47 Bit Score: 43.79 E-value: 4.80e-05

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 558137628  273 CKVCQACRKPgndSKMLVCETCDKGYHTFCLKPPMEELPA-HSWKCKAC 320
Cdd:cd15617     2 CYVCGGKQDA---HMQLLCDECNMAYHIYCLNPPLDKIPEdEDWYCPSC 47

PHD3_PHF14

cd15563

PHD finger 3 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...

229-273

5.46e-05

Pssm-ID: 277038 Cd Length: 49 Bit Score: 43.54 E-value: 5.46e-05

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 558137628  229 CAVCEGPGELCDLFFCTSCGHHYHGACLDTAL--TARKRA-GWQCPEC 273
Cdd:cd15563     2 CCVCKQTGDNSQLVRCDECKLCYHFGCLDPPLkkSPKQRGyGWVCEEC 49

PHD_ARID4_like

cd15615

PHD finger found in Arabidopsis thaliana AT-rich interactive domain-containing protein 4 ...

1233-1283

6.51e-05

PHD finger found in Arabidopsis thaliana AT-rich interactive domain-containing protein 4 (ARID4) and similar proteins; This family includes A. thaliana ARID4 (ARID domain-containing protein 4) and similar proteins. Their biological roles remain unclear, but they all contain an AT-rich interactive domain (ARID) and a plant homeodomain (PHD) finger at the C-terminus. ARID is a helix-turn-helix motif-based DNA-binding domain conserved in all eukaryotes. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins.

Pssm-ID: 277087 Cd Length: 57 Bit Score: 43.62 E-value: 6.51e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 558137628 1233 TCPICHAPYVE----EDLLIQCRHCERWMHAGCESLFTEDDVEQAADEG--FDCVSC 1283
Cdd:cd15615     1 FCILCGQVYEEnegdEKEWVQCDSCSEWVHFECDGRTGLGAFKYAKSDGlqYVCPRC 57

PHD3_KMT2A_like

cd15508

PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...

1234-1285

6.87e-05

PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This family includes histone-lysine N-methyltransferase trithorax (Trx) like proteins, KMT2A (MLL1) and KMT2B (MLL2), which comprise the mammalian Trx branch of the 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 through 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 plant homeodomain (PHD) fingers, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the third PHD finger.

Pssm-ID: 276983 Cd Length: 57 Bit Score: 43.59 E-value: 6.87e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 558137628 1234 CPICHAPYVEEDL---LIQCRHCERWMHAGCESLfteddveqaADEGFDCVSCQP 1285
Cdd:cd15508     2 CPLCEKCYDDDDYdskMMQCSQCDHWVHAKCEGL---------SDEMYEILSYLP 47

SET_SMYD

cd20071

SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...

5174-5278

7.15e-05

SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing protein, and similar proteins; The family includes SET and MYND domain-containing proteins, SMYD1-SYMD5. SMYD1 (EC 2.1.1.43; also termed BOP) is a heart and muscle specific SET-MYND domain containing protein, which functions as a histone methyltransferase and regulates downstream gene transcription. It methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. SMYD2 (also termed HSKM-B, or lysine N-methyltransferase 3C (KMT3C)) functions as a histone methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. It specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). SMYD3 (also termed zinc finger MYND domain-containing protein 1) functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex. SMYD4 functions as a potential tumor suppressor that plays a critical role in breast carcinogenesis at least partly through inhibiting the expression of PDGFR-alpha. SMYD5 (also termed protein NN8-4AG, or retinoic acid-induced protein 15) functions as histone lysine methyltransferase that mediates H4K20me3 at heterochromatin regions.

Pssm-ID: 380997 [Multi-domain] Cd Length: 122 Bit Score: 45.45 E-value: 7.15e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5174 GLGLYAAKDLEKhtmvieyiGTIIRNE------VANRREKIYEEQNRGIYMFRInnehvidatltggpARYINHSCAPNC 5247
Cdd:cd20071    10 GRGLVATRDIEP--------GELILVEkplvsvPSNSFSLTDGLNEIGVGLFPL--------------ASLLNHSCDPNA 67

                          90       100       110
                  ....*....|....*....|....*....|.
gi 558137628 5248 VaevVTFDKEDKIIIISSRRIPKGEELTYDY 5278
Cdd:cd20071    68 V---VVFDGNGTLRVRALRDIKAGEELTISY 95

PHD

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...

1234-1285

7.49e-05

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 43.25 E-value: 7.49e-05

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 558137628  1234 CPICHAPyVEEDLLIQCRHCERWMHAGCESLftEDDVEQAADEGFDCVSCQP 1285
Cdd:pfam00628    2 CAVCGKS-DDGGELVQCDGCDDWFHLACLGP--PLDPAEIPSGEWLCPECKP 50

PHD2_KMT2B

cd15591

PHD domain 2 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...

1107-1154

8.00e-05

PHD domain 2 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed trithorax homolog 2 or WW domain-binding protein 7 (WBP-7), 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 3lysine 4 (H3K4) methylation, which stimulates chromatin transcription in a SAM- and H3K4-dependent manner. Moreover, KMT2B plays a critical role in memory formation through 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 plant homeodomain (PHD), an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the second PHD finger.

Pssm-ID: 277066 Cd Length: 50 Bit Score: 43.00 E-value: 8.00e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 558137628 1107 CVVCGSFGRGAEgHLLACSQCSQCYHPYCVNSKITKVMLLK--GWRCVEC 1154
Cdd:cd15591     2 CHVCGRKNKESK-PLLECERCRNCYHPACLGPNYPKPANRKkrPWICSAC 50

PHD_TIF1beta

cd15623

PHD finger found in transcription intermediary factor 1-beta (TIF1-beta); TIF1-beta, also ...

276-320

8.30e-05

PHD finger found in transcription intermediary factor 1-beta (TIF1-beta); TIF1-beta, also termed Kruppel-associated Box (KRAB)-associated protein 1 (KAP-1), or KRAB-interacting protein 1 (KRIP-1), or nuclear co-repressor KAP-1, or RING finger protein 96, or tripartite motif-containing protein 28 (TRIM28), or E3 SUMO-protein ligase TRIM28, acts as a nuclear co-repressor that plays a role in transcription and in DNA damage response. Upon DNA damage, the phosphorylation of KAP-1 on serine 824 by the ataxia telangiectasia-mutated (ATM) kinase enhances cell survival and facilitates chromatin relaxation and heterochromatic DNA repair. It also regulates CHD3 nucleosome remodeling during DNA double-strand break (DSB) response. Meanwhile, KAP-1 can be dephosphorylated by protein phosphatase PP4C in the DNA damage response. In addition, KAP-1 is a co-activator of the orphan nuclear receptor NGFI-B (or Nur77) and is involved in NGFI-B-dependent transcription. It is also a coiled-coil binding partner, substrate and activator of the c-Fes protein tyrosine kinase. TIF1-beta contains an N-terminal RBCC (RING finger, B-box zinc-fingers, coiled-coil), which can interact with KRAB zinc finger proteins (KRAB-ZFPs), MDM2, MM1, C/EBPbeta, and mediates homo- and heterodimerization, a plant homeodomain (PHD) finger followed by a bromodomain in the C-terminal region, which interact with SETDB1, Mi-2alpha and other proteins to form complexes with histone deacetylase or methyltransferase activity.

Pssm-ID: 277093 Cd Length: 43 Bit Score: 42.87 E-value: 8.30e-05

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628  276 CQACRKPGNdskMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15623     2 CRVCQKAGA---LVMCDQCEFCFHLDCHLPALQEVPGEDWKCLLC 43

PHD2_KMT2C

cd15594

PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...

229-273

8.89e-05

Pssm-ID: 277069 Cd Length: 46 Bit Score: 43.00 E-value: 8.89e-05

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628  229 CAVCEGPGELCDLFFCTSCGHHYHGACLDTALTARKRAGWQCPEC 273
Cdd:cd15594     2 CQTCRQPGDDNKMLVCDTCDKGYHTFCLQPVMTTIPKNGWKCKNC 46

PHD_TCF19_like

cd15517

PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ...

275-320

9.20e-05

PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and KDM5B, and other similar proteins; TCF-19 was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. KDM5A was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interaction with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK, and BMAL1. KDM5B has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. Both KDM5A and KDM5B function as trimethylated histone H3 lysine 4 (H3K4me3) demethylases. This family also includes Caenorhabditis elegans Lysine-specific demethylase 7 homolog (ceKDM7A). ceKDM7A (also termed JmjC domain-containing protein 1.2, PHD finger protein 8 homolog, or PHF8 homolog) is a plant homeodomain (PHD)- and JmjC domain-containing protein that functions as a histone demethylase specific for H3K9me2 and H3K27me2. The binding of the PHD finger to H3K4me3 guides H3K9me2- and H3K27me2-specific demethylation by its catalytic JmjC domain in a trans-histone regulation mechanism. In addition, this family includes plant protein OBERON 1 and OBERON 2, Alfin1-like (AL) proteins, histone acetyltransferases (HATs) HAC, and AT-rich interactive domain-containing protein 4 (ARID4).

Pssm-ID: 276992 [Multi-domain] Cd Length: 49 Bit Score: 42.92 E-value: 9.20e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 558137628  275 VCQACRKPGNDSKML--VCETCDKGYHTFCLK--PPMEELPAhSWKCKAC 320
Cdd:cd15517     1 VCGICNLETAAVDELwvQCDGCDKWFHQFCLGlsNERYADED-KFKCPNC 49

PRK12323

DNA polymerase III subunit gamma/tau;

687-892

1.02e-04

DNA polymerase III subunit gamma/tau;

Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 48.72 E-value: 1.02e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  687 PFGAKGDSDPESPLAAPILETPISPPPEANCTDPEPVPPMILPPSPGSPMGLASPILME-PLPPRCSPLLQHSLPPQNSP 765
Cdd:PRK12323  365 PGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPaRRSPAPEALAAARQASARGP 444

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  766 PSQCSPPALPLSIPSPLSPIEKAmevshEAEPPEMEIEKAPEPECPALEPSPTSPLPSPMGNLSCPAPSPAPALEDFSGM 845
Cdd:PRK12323  445 GGAPAPAPAPAAAPAAAARPAAA-----GPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPA 519

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 558137628  846 GEDTAPL-DGTDTPDSQPEAGQTPGSLASELkgSPVLLDPEELAPVTP 892
Cdd:PRK12323  520 GWVAESIpDPATADPDDAFETLAPAPAAAPA--PRAAAATEPVVAPRP 565

PHD_TIF1_like

cd15541

PHD finger found in the transcriptional intermediary factor 1 (TIF1) family and similar ...

275-320

1.31e-04

Pssm-ID: 277016 [Multi-domain] Cd Length: 43 Bit Score: 42.33 E-value: 1.31e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  275 VCQACRKPGNdskMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15541     1 WCAVCQNGGE---LLCCDKCPRVFHLDCHIPPIPEFPSGEWSCSLC 43

PHD_PRHA_like

cd15504

PHD finger found in Arabidopsis thaliana pathogenesis-related homeodomain protein (PRHA) and ...

275-320

1.42e-04

Pssm-ID: 276979 Cd Length: 53 Bit Score: 42.42 E-value: 1.42e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 558137628  275 VCQACRKP--GNDSKMLVCE-TCDKGYHTFCLKPPM--EELPA--HSWKCKAC 320
Cdd:cd15504     1 FCAKCQSGeaSPDNDILLCDgGCNRAYHQKCLEPPLltEDIPPedEGWLCPLC 53

PHA03307

transcriptional regulator ICP4; Provisional

1866-2260

1.66e-04

transcriptional regulator ICP4; Provisional

Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 48.24 E-value: 1.66e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1866 ADGFLKPPAGTVPGPDSPGELFLKLPPQVPAQVPSQDPFGLAPAYALEPRFPTAPSTYPPYPSPAGAPVQPPTLGTSSRP 1945
Cdd:PHA03307   16 EGGEFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1946 GTGQPGEFHTTPPGTPRHQPSTPDPFLKPRCPSLDNLAVPESPGVGGGKASEPLLSPPPFGESRKALEVKKEELGASS-- 2023
Cdd:PHA03307   96 APASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAAlp 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2024 ------PSYGPPNLGFVDSPSSGPHLGSLELKAPDVFKAPLTPRASQVEPQSPGLGLRPQEPSPAQALAPSPPSHSDIFR 2097
Cdd:PHA03307  176 lsspeeTARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENEC 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2098 PGPYPDPYAQPPLTPRPQPPAPESCCALPPRSLPSDPFSRVPASPQSQSSSQSPLTPRPLSAEAFCPSPVTPrfqSPDPy 2177
Cdd:PHA03307  256 PLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSS---STSS- 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2178 SRPPSRPQSRDPFAPLHKPPRPQPPEVAFKSGPLAHTPLGAGGFPAALPSGPAGELHAKVPSGQPPNFARSpGTGAFVGT 2257
Cdd:PHA03307  332 SSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRD-ATGRFPAG 410


                  ...
gi 558137628 2258 PSP 2260
Cdd:PHA03307  411 RPR 413

ePHD2_PHF6

cd15711

Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...

4798-4894

1.68e-04

Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. PHF6 contains two non-canonical ePHD fingers, this model corresponds to the second ePHD finger. PHF6, also termed the X-linked mental retardation disorder Borjeson-Forssman-Lehmann syndrome-associated protein, is a nucleolus, ribosomal RNA promoter-associated protein that regulates cell cycle progression by suppressing ribosomal RNA synthesis. It has been implicated in cell cycle control, genomic maintenance, and tumor suppression. PHF6 shows transcriptional repression activity through directly interacting with the nucleosome remodeling and deacetylation complex component RBBP4.

Pssm-ID: 277181 Cd Length: 118 Bit Score: 44.30 E-value: 1.68e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4798 CCFCHE-EGDGATDGPARLLNLDlDLWVHLNCALWST---EVYETQGGALMNVEVA-----LHRGLLTKCSLCQRTGATS 4868
Cdd:cd15711     1 CGFCHAgEEENETRGKLHIFNAK-KAAAHYKCMLFSSgtvQLTTTSRAEFGDFDIKtviqeIKRGKRMKCTLCSQLGATI 79

                          90       100
                  ....*....|....*....|....*.
gi 558137628 4869 SCNRMRCPNVYHFACAIRAKCMFFKD 4894
Cdd:cd15711    80 GCEIKACVKTYHYHCGVQDKAKYIEN 105

ePHD1_PHF6

cd15710

Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...

138-198

1.71e-04

Pssm-ID: 277180 Cd Length: 115 Bit Score: 44.18 E-value: 1.71e-04

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 558137628  138 AHHWCAVWSAGVWGK-------GGPELCGVDKAIFSGISQRCSHCTRLGASIPCRSPGCPRLYHFPCA 198
Cdd:cd15710    25 AHHKCMLFSSALVSShsdsenlGGFSIEDVQKEIKRGTKLMCSLCHCPGATIGCDVKTCHRTYHYYCA 92

PABP-1234

TIGR01628

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...

4004-4132

1.88e-04

Pssm-ID: 130689 [Multi-domain] Cd Length: 562 Bit Score: 47.88 E-value: 1.88e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  4004 RQAPSYQEPgtQPSPLQGLLGRQPQVGGFPGSQTGPLQELGAGLRPQGPPRLPapqGALSTGPVPGPVHPTPPPSSPQEP 4083
Cdd:TIGR01628  378 LQPRMRQLP--MGSPMGGAMGQPPYYGQGPQQQFNGQPLGWPRMSMMPTPMGP---GGPLRPNGLAPMNAVRAPSRNAQN 452

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 558137628  4084 kRPSQLPSPSSQLPSEAQLPPTQPGTPKPQALPLELppGKISPAAAQLA 4132
Cdd:TIGR01628  453 -AAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTASQG--GQNKKLAQVLA 498

PHD3_KMT2B

cd15593

PHD finger 3 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...

1234-1271

1.99e-04

PHD finger 3 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed trithorax homolog 2 or WW domain-binding protein 7 (WBP-7), 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 through 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 plant homeodomain (PHD) fingers, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the third PHD finger.

Pssm-ID: 277068 Cd Length: 57 Bit Score: 42.14 E-value: 1.99e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 558137628 1234 CPICHAPYVEEDL---LIQCRHCERWMHAGCESLfTEDDVE 1271
Cdd:cd15593     2 CPICLKCYEDNDYeskMMQCAKCDHWVHAKCEGL-SDELYE 41

PHD_BRPF_JADE_like

cd15492

PHD finger found in BRPF proteins, Jade proteins, protein AF-10, AF-17, and similar proteins; ...

1156-1201

2.11e-04

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: 41.84 E-value: 2.11e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 558137628 1156 VCEVCGQAS--DPSRLLLCDDCDISYHTYCLDppLLTVPKGGWKCKWC 1201
Cdd:cd15492     1 VCDVCLDGEseDDNEIVFCDGCNVAVHQSCYG--IPLIPEGDWFCRKC 46

PHD_JADE2

cd15680

PHD finger found in protein Jade-2 and similar proteins; Jade-2, also termed PHD finger ...

1156-1201

2.11e-04

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: 41.92 E-value: 2.11e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 558137628 1156 VCEVC--GQASDPSRLLLCDDCDISYHTYCLDppLLTVPKGGWKCKWC 1201
Cdd:cd15680     1 VCDVCrsPEGEDGNEMVFCDKCNVCVHQACYG--ILKVPTGSWLCRTC 46

PHA03247

large tegument protein UL36; Provisional

517-904

2.25e-04

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.01 E-value: 2.25e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  517 PLSPPPEASPLNPP--FEESPLSPPPEELPTSP--PPEASRLSPPPEESPMSPPPEESPMSPPPEASRMFPPFEESPLSP 592
Cdd:PHA03247 2557 PAAPPAAPDRSVPPprPAPRPSEPAVTSRARRPdaPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAAN 2636

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  593 PPEESPLSPPAE------------------ASRLSAPPEESSTLSRllGEPVLSEPRVPPLSPLPEELPLSPTREPSLSP 654
Cdd:PHA03247 2637 EPDPHPPPTVPPperprddpapgrvsrprrARRLGRAAQASSPPQR--PRRRAARPTVGSLTSLADPPPPPPTPEPAPHA 2714

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  655 QLMPPDPLPPPLSPIITAVAPPAlSPLGeleyPFGAKGDSDPESPLAAPILETPISPPPEANCTDPEPVPPMILPPSPGS 734
Cdd:PHA03247 2715 LVSATPLPPGPAAARQASPALPA-APAP----PAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVA 2789

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  735 PMGLASPILMEPL----PPRCSPLLQHSLPPQNSPPSQCSPP--ALPLSIPSPLSPIEKAMEVSHEAEPPEMEIEKAPEP 808
Cdd:PHA03247 2790 SLSESRESLPSPWdpadPPAAVLAPAAALPPAASPAGPLPPPtsAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSR 2869

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  809 ECPALEPSPTSPLPSPMgnlscPAPSPAPALEDFSGMGEDTAPLdgtDTPDSQPEAGQTPGSLASELKGSPVLLDPEELA 888
Cdd:PHA03247 2870 SPAAKPAAPARPPVRRL-----ARPAVSRSTESFALPPDQPERP---PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQP 2941

                         410
                  ....*....|....*.
gi 558137628  889 PVTPMEVYGPECKQTG 904
Cdd:PHA03247 2942 PLAPTTDPAGAGEPSG 2957

ePHD_BRPF

cd15670

Extended PHD finger found in BRPF proteins; The extended plant homeodomain (ePHD) zinc finger ...

4798-4887

2.42e-04

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: 43.86 E-value: 2.42e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4798 CCFCHEEGdGA----TDGParllnldldlWVHLNCALWSTEVY-------EtqggALMNVE-VALHRGLLTkCSLC-QRT 4864
Cdd:cd15670     1 CVLCPNKG-GAfkqtDDGR----------WAHVVCALWIPEVSfantvflE----PIDGIQnIPKARWKLT-CYICkKRM 64

                          90       100
                  ....*....|....*....|...
gi 558137628 4865 GATSSCNRMRCPNVYHFACAIRA 4887
Cdd:cd15670    65 GACIQCHKKNCYTAFHVTCAQQA 87

PHD_PRKCBP1

cd15538

PHD finger found in protein kinase C-binding protein 1 (PRKCBP1); PRKCBP1, also termed ...

1118-1154

2.43e-04

PHD finger found in protein kinase C-binding protein 1 (PRKCBP1); PRKCBP1, also termed cutaneous T-cell lymphoma-associated antigen se14-3 (CTCL-associated antigen se14-3), or Rack7, or zinc finger MYND domain-containing protein 8 (ZMYND8), is a novel receptor for activated C-kinase (RACK)-like protein that may play an important role in the activation and regulation of PKC-beta I, and the PKC signaling cascade. It also has been identified as a formin homology-2-domain containing protein 1 (FHOD1)-binding protein that may be involved in FHOD1-regulated actin polymerization and transcription. Moreover, PRKCBP1 may function as a REST co-repressor 2 (RCOR2) interacting factor; the RCOR2/ZMYND8 complex which might be involved in the regulation of neural differentiation. PRKCBP1 contains a plant homeodomain (PHD) finger, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain.

Pssm-ID: 277013 Cd Length: 41 Bit Score: 41.54 E-value: 2.43e-04

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 558137628 1118 EGHLLACSQCSQCYHPYCVNSKItkvMLLKGWRCVEC 1154
Cdd:cd15538     8 EGQVLCCSLCPRVYHKKCLKLTS---EPDEDWVCPEC 41

PHD_TCF19_like

cd15517

PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ...

1234-1283

2.85e-04

Pssm-ID: 276992 [Multi-domain] Cd Length: 49 Bit Score: 41.38 E-value: 2.85e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 558137628 1234 CPICHAPYVEEDLL-IQCRHCERWMHAGCESLftedDVEQAADEG-FDCVSC 1283
Cdd:cd15517     2 CGICNLETAAVDELwVQCDGCDKWFHQFCLGL----SNERYADEDkFKCPNC 49

PHA03307

transcriptional regulator ICP4; Provisional

2078-2401

3.05e-04

transcriptional regulator ICP4; Provisional

Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 47.47 E-value: 3.05e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2078 EPSPAQALAPSPPSHSDIFRPGPYPDPYAQPPLTPRPQPPAPESCCALPPRSLPSDPFSRVPASPQSQSSSQSPLTPRPL 2157
Cdd:PHA03307   19 EFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2158 SAEAfCPSPVTPRFQSPDPYSRPPSRPQSRDPFAPLHKPPRPQPPEVAF------KSGPLAHTPLGAGGFPAALPSGPA- 2230
Cdd:PHA03307   99 SPAR-EGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPppaaspPAAGASPAAVASDAASSRQAALPLs 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2231 -GELHAKVPSGQPPNFARSPGTGAFVGTPSPMRFTFPQAVGEPSSLKPPVPQPGLPPPHGINSHFGPGPTLGKPQSTNys 2309
Cdd:PHA03307  178 sPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENEC-- 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2310 vATGNFHPSGSPLGPSSGSTGEGYGLSPLRPQSVLPPPVPDGSLPYPPHGASQRAGITSPVDKRE-DPGAGMAGSLAAPE 2388
Cdd:PHA03307  256 -PLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSsSRESSSSSTSSSSE 334

                         330
                  ....*....|...
gi 558137628 2389 LPGTQDPGISSLS 2401
Cdd:PHA03307  335 SSRGAAVSPGPSP 347

PHA03307

transcriptional regulator ICP4; Provisional

2020-2390

3.18e-04

transcriptional regulator ICP4; Provisional

Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 47.47 E-value: 3.18e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2020 GASSPSYGPPNLGFVDSPSSGPHLGSLELKAPDVFKAPL-TPRASQVEPQSPGLGLRPQEPSPAQALAPSPPShSDIFRP 2098
Cdd:PHA03307   24 PPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACdRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLA-PASPAR 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2099 GPYPDPYAQPPLTPRPQPPAPESCCALPPRSLPSDPFSRVPASPQSQSSSQSPLTPRPLSAEAFCPSPVTPRF-QSPDPY 2177
Cdd:PHA03307  103 EGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPlSSPEET 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2178 SRPPSRPQSRDPF--APLHKPPRPQPPEVAFKSGPLAHTPLGAGgfpaalpsGPAGELHAKVPSGQPPNFARSP-GTGAF 2254
Cdd:PHA03307  183 ARAPSSPPAEPPPstPPAAASPRPPRRSSPISASASSPAPAPGR--------SAADDAGASSSDSSSSESSGCGwGPENE 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2255 VGTPSPMRFTFPQAVGEPSSLKPPVPQPGLPPPHGINSHFGPGPTLGKPQSTnySVATGNFH------------PSGSPL 2322
Cdd:PHA03307  255 CPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSG--PAPSSPRAsssssssresssSSTSSS 332

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 558137628 2323 GPSSGSTGEGYGLSPLRPQSVLPPPVPDGSLPYPPHGASQRAGITSPVDKREDPGAGMAGSLAAPELP 2390
Cdd:PHA03307  333 SESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARR 400

PHD_JADE1

cd15679

PHD finger found in protein Jade-1 and similar proteins; Jade-1, also termed PHD finger ...

1156-1201

3.47e-04

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: 41.21 E-value: 3.47e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 558137628 1156 VCEVCGQ--ASDPSRLLLCDDCDISYHTYCLDppLLTVPKGGWKCKWC 1201
Cdd:cd15679     1 VCDVCQSpdGEDGNEMVFCDKCNICVHQACYG--ILKVPEGSWLCRTC 46

PHD_TIF1beta

cd15623

PHD finger found in transcription intermediary factor 1-beta (TIF1-beta); TIF1-beta, also ...

1157-1201

3.70e-04

Pssm-ID: 277093 Cd Length: 43 Bit Score: 40.94 E-value: 3.70e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628 1157 CEVCGQASDpsrLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15623     2 CRVCQKAGA---LVMCDQCEFCFHLDCHLPALQEVPGEDWKCLLC 43

PHD

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...

4858-4902

3.73e-04

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 41.04 E-value: 3.73e-04

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 558137628   4858 CSLCQRTGATS---SCNRmrCPNVYHFACAIRAKCMFFKDKTMLCPMH 4902
Cdd:smart00249    2 CSVCGKPDDGGellQCDG--CDRWYHQTCLGPPLLEEEPDGKWYCPKC 47

RING-H2

cd16448

H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type ...

229-274

3.80e-04

H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). This family corresponds to the H2 subclass of RING (RING-H2) finger proteins that are characterized by containing C3H2C3-type canonical RING-H2 fingers or noncanonical RING-H2 finger variants, including C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type modified RING-H2 fingers. The canonical RING-H2 finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-X2-C-X(4-48)-C-X2-C, X is any amino acid and the number of X residues varies in different fingers. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-H2 finger can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serves as a scaffold for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.

Pssm-ID: 438112 [Multi-domain] Cd Length: 43 Bit Score: 40.85 E-value: 3.80e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  229 CAVCEGPGELCDLFFCTSCGHHYHGACLDTALTARKRagwQCPECK 274
Cdd:cd16448     1 CVICLEEFEEGDVVRLLPCGHVFHLACILRWLESGNN---TCPLCR 43

ePHD_JADE

cd15671

Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended ...

133-217

4.33e-04

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: 42.82 E-value: 4.33e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  133 GGSCWAHHWCAVWSAGVwGKGGPE----LCGVDKAIFSGISQRCSHC-TRLGASIPCRSPGCPRLYHFPCATASGsfLSM 207
Cdd:cd15671    16 SGTKWVHVSCALWIPEV-SIGCPEkmepITKISHIPMSRWALVCVLCkEKTGACIQCSVKSCKTAFHVTCAFQHG--LEM 92

                          90       100
                  ....*....|....*....|
gi 558137628  208 KT--------LQLL--CPEH 217
Cdd:cd15671    93 KTilededdeVKFKsyCPKH 112

PHD1_KMT2A_like

cd15506

PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...

275-320

4.36e-04

PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This family includes histone-lysine N-methyltransferase trithorax (Trx) like proteins, KMT2A (MLL1) and KMT2B (MLL2), which comprise the mammalian Trx branch of the 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 through 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 plant homeodomain (PHD) fingers, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the first PHD finger.

Pssm-ID: 276981 Cd Length: 47 Bit Score: 40.81 E-value: 4.36e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 558137628  275 VCQACRKPGNDsKMLVCETCDKGYHTFCLKPPMEELPAH--SWKCKAC 320
Cdd:cd15506     1 LCFLCGSAGLN-ELLYCSVCCEPYHTFCLEEAERPLNINkdNWCCRRC 47

PHD_PHF21A

cd15523

PHD finger found in PHD finger protein 21A (PHF21A); PHF21A (also termed BHC80a or BRAF35-HDAC ...

229-273

4.83e-04

Pssm-ID: 276998 [Multi-domain] Cd Length: 43 Bit Score: 40.84 E-value: 4.83e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628  229 CAVCEGPGELcdlFFCTSCGHHYHGACLDTALTARKRAGWQCPEC 273
Cdd:cd15523     2 CSVCRKSGEL---LMCDTCSLVYHLDCLDPPLKTIPKGMWICPKC 43

ePHD_JMJD2A

cd15713

Extended PHD finger (ePHD) found in Jumonji domain-containing protein 2A (JMJD2A); The ...

4798-4894

4.85e-04

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: 42.65 E-value: 4.85e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4798 CCFCHEEGdGAtdgparLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVA---LHRGLLtKCSLCQR-----TGATSS 4869
Cdd:cd15713     1 CCLCSLRG-GA------LQRANDDKWVHVMCAVAVLEARFVNIAERSPVDVSkipLQRFKL-KCIFCKKrrkrtAGCCVQ 72

                          90       100
                  ....*....|....*....|....*
gi 558137628 4870 CNRMRCPNVYHFACAIRAKCMFFKD 4894
Cdd:cd15713    73 CSHGRCPTSFHASCAQAAGVMMQPD 97

PHD_PHF21B

cd15524

PHD finger found in PHD finger protein 21B (PHF21B); PHF21B is a plant homeodomain (PHD) ...

1157-1201

5.47e-04

PHD finger found in PHD finger protein 21B (PHF21B); PHF21B is a plant homeodomain (PHD) finger-containing protein whose biological function remains unclear. It shows high sequence similarity with PHF21A, which is associated with LSD1, a lysine (K)-specific histone demethylase and inhibits LSD1-mediated histone demethylation in vitro. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins.

Pssm-ID: 276999 [Multi-domain] Cd Length: 43 Bit Score: 40.65 E-value: 5.47e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628 1157 CEVCGQASDpsrLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWC 1201
Cdd:cd15524     2 CAACKRGGN---LQPCGTCPRAYHLDCLDPPLKTAPKGVWVCPKC 43

PHD1_MTF2

cd15578

PHD finger 1 found in metal-response element-binding transcription factor 2 (MTF2); MTF2, also ...

1156-1203

5.74e-04

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: 40.84 E-value: 5.74e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 558137628 1156 VCEVC--GQASDPSRLLLCDDCDISYHTYCLDPPLLTV---PKGGWKCKWCVS 1203
Cdd:cd15578     1 VCTVCqdGSSESPNEIVLCDKCGQGYHQLCHNPKIDSSvldPDVPWLCRQCVF 53

SET_KMT2E

cd19182

SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...

5177-5282

5.77e-04

SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar proteins; KMT2E (also termed inactive lysine N-methyltransferase 2E, myeloid/lymphoid or mixed-lineage leukemia protein 5 (MLL5)) plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. It associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription. Lack of key residues in the SET domain as well as the presence of an unusually large loop in the SET-I subdomain preclude the interaction of MLL5 SET with its cofactor and substrate thus making MLL5 devoid of any in vitro methyltransferase activity on full-length histones and histone H3 peptide.

Pssm-ID: 380959 Cd Length: 129 Bit Score: 42.96 E-value: 5.77e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 5177 LYAAKDLEKHTMVIEYIGTIIRNEV--AN----RREK---IYEEQNRGIYMfrinnehVIDATLTGGPARYINHSCAPNC 5247
Cdd:cd19182    21 LKAAKDLPPDTLIIEYRGKFMLREQfeANgyffKRPYpfvLFYSKFHGLEM-------CVDARTFGNEARFIRRSCTPNA 93

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 558137628 5248 VAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDF 5282
Cdd:cd19182    94 EVRHVIEDGTIHLYIYSIRSIPKGTEITIAFDFDY 128

PHD_BRPF2

cd15677

PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and similar ...

1156-1203

6.44e-04

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: 40.77 E-value: 6.44e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 558137628 1156 VCEVC--GQASDPSRLLLCDDCDISYHTYCLDPPLltVPKGGWKCKWCVS 1203
Cdd:cd15677     3 VCCICmdGECQNSNVILFCDMCNLAVHQECYGVPY--IPEGQWLCRHCLQ 50

PHD_BAZ1A

cd15627

PHD finger found in bromodomain adjacent to zinc finger domain protein 1A (BAZ1A); BAZ1A, also ...

228-273

8.35e-04

Pssm-ID: 277097 [Multi-domain] Cd Length: 46 Bit Score: 40.07 E-value: 8.35e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  228 RCAVCEGPGELCDLFFCTSCGHHYHGACLDTALTARKRAGWQCPEC 273
Cdd:cd15627     1 RCRICRRKGDAEKMLLCDGCDRGHHMYCLRPPLKKVPEGDWFCPDC 46

PHA03247

large tegument protein UL36; Provisional

3763-4183

8.46e-04

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.08 E-value: 8.46e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 3763 PGMPAKPLQQHFSSPGALGPTLLLSgkeqsivETTLPPEATEGPSTHQGGVAIGTVPEAVPTEPGEVKPSLSGDSQLLLV 3842
Cdd:PHA03247 2595 SARPRAPVDDRGDPRGPAPPSPLPP-------DTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRA 2667

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 3843 QPQAQPQPNSVPLQPPLRLQGQQQQQQVnllhTAGVGSHGQSNSGSSSEASSVPHLLTQSSVSLGEQPGP-ITQNPLGSQ 3921
Cdd:PHA03247 2668 RRLGRAAQASSPPQRPRRRAARPTVGSL----TSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPaLPAAPAPPA 2743

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 3922 QHHGLERPLQNNAGPQPAKPgsvpqSGQGLPGAGVMPTVGQFRAQLQGVLAKNPQLRHLSPQQQQQLQALLMQRQLQQSQ 4001
Cdd:PHA03247 2744 VPAGPATPGGPARPARPPTT-----AGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAAL 2818

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4002 AIRQAPSYQEPG------TQPSPLQGLLGRQPQVGGF--PG---SQTGPLQELGAG-LRPQGPP--RLPAPQGALSTGPV 4067
Cdd:PHA03247 2819 PPAASPAGPLPPptsaqpTAPPPPPGPPPPSLPLGGSvaPGgdvRRRPPSRSPAAKpAAPARPPvrRLARPAVSRSTESF 2898

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 4068 PGPVHPTPPPSSPQEPKRPsqLPSPSSQLPSEAQLPPTQPGTPKPQALPLELPPGKISPAAAQLADTLFGKGLG------ 4141
Cdd:PHA03247 2899 ALPPDQPERPPQPQAPPPP--QPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGrvavpr 2976

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 558137628 4142 -----PWDPPDNPAEAQKPEQSSLVPGHPEQVNGQAV---PEPSYLSIKQ 4183
Cdd:PHA03247 2977 frvpqPAPSREAPASSTPPLTGHSLSRVSSWASSLALheeTDPPPVSLKQ 3026

PHD1_MOZ_d4

cd15526

PHD finger 1 found in monocytic leukemia zinc-finger protein (MOZ), its factor (MORF), and d4 ...

228-273

9.45e-04

PHD finger 1 found in monocytic leukemia zinc-finger protein (MOZ), its factor (MORF), and d4 gene family proteins; MOZ 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 and 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) 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 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 lymphoma genesis and bone development, and its homologs. This family also includes three members of the d4 gene family, DPF1 (neuro-d4), DPF2 (ubi-d4/Requiem), and DPF3 (cer-d4), which function as transcription factors and are involved in transcriptional regulation of genes via changing the condensed/decondensed state of chromatin in nucleus. DPF2 is ubiquitously expressed and it acts as a transcription factor that may participate in developmentally programmed cell death. DPF1 and DPF3 are expressed predominantly in neural tissues, and they may be involved in the transcription regulation of neuro specific gene clusters. All family members contain two plant homeodomain (PHD) fingers. This model corresponds to the first PHD finger.

Pssm-ID: 277001 Cd Length: 56 Bit Score: 40.42 E-value: 9.45e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 558137628  228 RCAVCEGPGELC-------DLFFCTSCGHHYHGACLD---TALTARKRAGWQCPEC 273
Cdd:cd15526     1 ICDFCLGTDEKNnktgepeELISCADCGSSGHPSCLKfspGLTDAVKSYRWQCIEC 56

PHD3_KMT2A

cd15592

PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, ...

1234-1283

1.02e-03

PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, CXXC-type zinc finger protein 7, myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), 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 H3K4 methylation. KMT2A contains a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD) fingers, a Bromodomain domain, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the third PHD finger.

Pssm-ID: 277067 Cd Length: 57 Bit Score: 40.36 E-value: 1.02e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 558137628 1234 CPICHAPYVEEDL---LIQCRHCERWMHAGCESLftEDDVEQAADE-----GFDCVSC 1283
Cdd:cd15592     2 CPLCDKCYDDDDYeskMMQCGKCDRWVHSKCENL--SDEMYEILSNlpesvAYTCINC 57

PHD_JADE3

cd15681

PHD finger found in protein Jade-3 and similar proteins; Jade-3, also termed PHD finger ...

1156-1202

1.24e-03

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: 39.95 E-value: 1.24e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 558137628 1156 VCEVCGQ--ASDPSRLLLCDDCDISYHTYCLDppLLTVPKGGWKCKWCV 1202
Cdd:cd15681     1 ICDVCRSpdSEEGNDMVFCDKCNICVHQACYG--ILKVPEGSWLCRTCV 47

PHD1_PHF12

cd15533

PHD finger 1 found in PHD finger protein 12 (PHF12); PHF12, also termed PHD factor 1 (Pf1), is ...

275-320

1.25e-03

Pssm-ID: 277008 [Multi-domain] Cd Length: 45 Bit Score: 39.65 E-value: 1.25e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 558137628  275 VCQACRKPGNdskMLVCETCDKGYHTFCLKPPMEE--LPAHSWKCKAC 320
Cdd:cd15533     1 YCDSCGEGGD---LLCCDRCPASFHLQCCNPPLDEedLPPGEWLCHRC 45

PHD_BAZ1B

cd15628

PHD finger found in bromodomain adjacent to zinc finger domain protein 1B (BAZ1B); BAZ1B, also ...

228-273

1.30e-03

Pssm-ID: 277098 Cd Length: 46 Bit Score: 39.73 E-value: 1.30e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  228 RCAVCEGPGELCDLFFCTSCGHHYHGACLDTALTARKRAGWQCPEC 273
Cdd:cd15628     1 KCKVCRKKGEDDKLILCDECNQAFHLFCLRPALYEVPDGEWMCPAC 46

PHD_SF

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...

4858-4902

1.45e-03

Pssm-ID: 276966 [Multi-domain] Cd Length: 48 Bit Score: 39.61 E-value: 1.45e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 558137628 4858 CSLCQRTGATS----SCNRmrCPNVYHFACAIRAKCMFFKDKTMLCPMH 4902
Cdd:cd15489     2 CIVCGKGGDLGgellQCDG--CGKWFHADCLGPPLSSFVPNGKWICPVC 48

PHA02682

ORF080 virion core protein; Provisional

702-840

1.45e-03

ORF080 virion core protein; Provisional

Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 44.08 E-value: 1.45e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  702 APILETPISPPPEANCtdPEPVPPMILP------PSPGSPmglasPILMEPLPPRCSPLLQHSLPPQNSPPSQCSPPALP 775
Cdd:PHA02682   80 SPLAPSPACAAPAPAC--PACAPAAPAPavtcpaPAPACP-----PATAPTCPPPAVCPAPARPAPACPPSTRQCPPAPP 152

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 558137628  776 LSIPSPLsPIEKAMEVSHEAEPPEMeiekaPEPECPALEPsptsplpspmgnlscpAPSPAPALE 840
Cdd:PHA02682  153 LPTPKPA-PAAKPIFLHNQLPPPDY-----PAASCPTIET----------------APAASPVLE 195

PHD_TAF3

cd15522

PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3); TAF3 (also termed ...

275-320

1.75e-03

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: 39.19 E-value: 1.75e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  275 VCQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15522     1 ICPICKKPDDGSPMIGCDECDDWYHWECVGITDEPPEEDDWFCPKC 46

PHD1_NSD

cd15564

PHD finger 1 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...

229-274

1.90e-03

PHD finger 1 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 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 first PHD finger.

Pssm-ID: 277039 Cd Length: 43 Bit Score: 38.86 E-value: 1.90e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 558137628  229 CAVCEGPGElcdLFFCT-SCGHHYHGACLdtALTARKRAGWQCPECK 274
Cdd:cd15564     2 CQICEKPGK---LLTCEgPCCGHFHLDCL--GLSEQPDEPFKCDECT 43

PHD5_NSD

cd15568

PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...

4858-4902

1.91e-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: 38.85 E-value: 1.91e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628 4858 CSLCQRTGATSSCNRMRCPNVYHFACAIRAKcmfFKDKTMLCPMH 4902
Cdd:cd15568     2 CFRCGDGGDLVLCDFKGCPKVYHLSCLGLEK---PPGGKWICPWH 43

PHD3_KMT2D

PHD finger 3 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...

229-273

2.05e-03

Pssm-ID: 277072 Cd Length: 51 Bit Score: 39.25 E-value: 2.05e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 558137628  229 CAVCE--GPGELCDLFFCTSCGHHYHGACLDTALTARK-RAGWQCPEC 273
Cdd:cd15597     3 CVVCGsfGRGSEGHLLACSQCSQCYHPYCVNSKITKVMlLKGWRCVEC 50

PHD2_PHF12_Rco1

cd15534

PHD finger 2 found in PHD finger protein 12 (PHF12), yeast Rco1, and similar proteins; PHF12, ...

275-317

2.10e-03

Pssm-ID: 277009 Cd Length: 47 Bit Score: 38.87 E-value: 2.10e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 558137628  275 VCQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHS-WKC 317
Cdd:cd15534     1 VCFKCNRSCRVAPLIQCDYCPLLFHLDCLDPPLTHPPATGrWMC 44

RING-H2_RNF167

cd16797

RING finger, H2 subclass, found in RING finger protein 167 (RNF167) and similar proteins; ...

229-274

2.14e-03

RING finger, H2 subclass, found in RING finger protein 167 (RNF167) and similar proteins; RNF167, also known as RING105, is an endosomal/lysosomal E3 ubiquitin-protein ligase involved in alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) ubiquitination. It ubiquitinates AMPA-type glutamate receptor subunit GluA2 and regulates its surface expression, and thus acts as a selective regulator of AMPAR-mediated neurotransmission. It acts as an endosomal membrane protein which ubiquitylates vesicle-associated membrane protein 3 (VAMP3) and regulates endosomal trafficking. Moreover, RNF167 plays a role in the regulation of TSSC5 (tumor-suppressing subchromosomal transferable fragment cDNA, also known as ORCTL2/IMPT1/BWR1A/SLC22A1L), which can function in concert with the ubiquitin-conjugating enzyme UbcH6. RNF167 is widely conserved in metazoans and contains an N-terminal signal peptide, a protease-associated (PA) domain, two transmembrane domains (TM1 and TM2), and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.

Pssm-ID: 319711 [Multi-domain] Cd Length: 46 Bit Score: 38.87 E-value: 2.14e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  229 CAVCEGPGELCDLFFCTSCGHHYHGACLDTALTARKRAgwqCPECK 274
Cdd:cd16797     3 CAICLDEYEEGDKLRVLPCSHAYHSKCVDPWLTQTKKT---CPVCK 45

PHA03247

large tegument protein UL36; Provisional

1821-2161

2.16e-03

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 2.16e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1821 ARKTDRPALHLRIPPQPGALGSPPPAAAPTIFigSPTTPAGLSTSAdgflkpPAGTVPGPDSPGELflkLPPQVPAQVPS 1900
Cdd:PHA03247 2780 PRRLTRPAVASLSESRESLPSPWDPADPPAAV--LAPAAALPPAAS------PAGPLPPPTSAQPT---APPPPPGPPPP 2848

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1901 QDPFG--LAPAYALEPRFPTapstyPPYPSPAGAPVQPPtLGTSSRPGTGQPGEFHTTPPGTPRHQPsTPDPFLKPRCPs 1978
Cdd:PHA03247 2849 SLPLGgsVAPGGDVRRRPPS-----RSPAAKPAAPARPP-VRRLARPAVSRSTESFALPPDQPERPP-QPQAPPPPQPQ- 2920

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 1979 ldnlavPESPgvgggKASEPLLSPPPFGESRKALEVKKEELGASSPSYGPPNlgfvdspssgPHLGSLelkAPDVFKAPL 2058
Cdd:PHA03247 2921 ------PQPP-----PPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQ----------PWLGAL---VPGRVAVPR 2976

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2059 T----PRASQVEPQSPGLGLR----PQEPSPAQALA----PSPPSHS---DIFRPGPYPDPYAQPPLTPRPQPPAPESCC 2123
Cdd:PHA03247 2977 FrvpqPAPSREAPASSTPPLTghslSRVSSWASSLAlheeTDPPPVSlkqTLWPPDDTEDSDADSLFDSDSERSDLEALD 3056

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 558137628 2124 ALPPRslPSDPFSRVPASPQSQ----SSSQSPLTPRPLSAEA 2161
Cdd:PHA03247 3057 PLPPE--PHDPFAHEPDPATPEagarESPSSQFGPPPLSANA 3096

zf-HC5HC2H_2

pfam13832

PHD-zinc-finger like domain;

137-202

2.21e-03

PHD-zinc-finger like domain;

Pssm-ID: 463991 [Multi-domain] Cd Length: 109 Bit Score: 40.79 E-value: 2.21e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 558137628   137 WAHHWCAVWSagvwgkggPELCGVD-----KAIFSGI-----SQRCSHC-TRLGASIPCRSPGCPRLYHFPCATASG 202
Cdd:pfam13832   21 WVHVLCAIFV--------PEVRFGNvatmePIDVSRIpperwKLKCVFCkKRSGACIQCSKGRCTTAFHVTCAQAAG 89

SET_Suv4-20-like

cd10524

SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...

5234-5300

2.23e-03

SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of variegation 4-20 (Suv4-20) and similar proteins; Suv4-20 (also termed Su(var)4-20) is a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-20' of histone H4. It acts as a dominant suppressor of position-effect variegation. The family also includes Suv4-20 homologs, lysine N-methyltransferase 5B (KMT5B) and lysine N-methyltransferase 5C (KMT5C). Both KMT5B (also termed lysine-specific methyltransferase 5B, or suppressor of variegation 4-20 homolog 1, or Su(var)4-20 homolog 1, or Suv4-20h1) and KMT5C (also termed lysine-specific methyltransferase 5C, or suppressor of variegation 4-20 homolog 2, or Su(var)4-20 homolog 2, or Suv4-20h2) are histone methyltransferases that specifically trimethylate 'Lys-20' of histone H4 (H4K20me3). They play central roles in the establishment of constitutive heterochromatin in pericentric heterochromatin regions.

Pssm-ID: 380922 [Multi-domain] Cd Length: 141 Bit Score: 41.50 E-value: 2.23e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 558137628 5234 GPARYINHSCAPNCVaevvtFDKEDKIIIISSRRIP--KGEELTYDYQFDFEDDQHkipCHCGAWNCRK 5300
Cdd:cd10524    75 GPAAFINHDCRPNCK-----FVPTGKSTACVKVLRDiePGEEITVYYGDNYFGENN---EECECETCER 135

PHD_BRPF

cd15572

PHD finger found in bromodomain and PHD finger-containing (BRPF) proteins; The family of BRPF ...

1156-1202

2.34e-03

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: 39.14 E-value: 2.34e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 558137628 1156 VCEVC--GQASDPSRLLLCDDCDISYHTYCLDPPLltVPKGGWKCKWCV 1202
Cdd:cd15572     3 VCCICldGECQNSNVILFCDMCNLAVHQECYGVPY--IPEGQWLCRRCL 49

PHD2_KMT2C_like

cd15510

PHD finger 2 found in Histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); KMT2C, ...

1107-1154

2.42e-03

Pssm-ID: 276985 Cd Length: 46 Bit Score: 38.95 E-value: 2.42e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 558137628 1107 CVVCGSfgRGAEGHLLACSQCSQCYHPYCVNSKITKVMLLkGWRCVEC 1154
Cdd:cd15510     2 CQACRQ--PGDDTKMLVCETCDKGYHTSCLRPVMSSIPKY-GWKCKNC 46

ePHD_BRPF3

cd15703

Extended PHD finger found in bromodomain and PHD finger-containing protein 3 (BRPF3) and ...

137-233

2.83e-03

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: 40.81 E-value: 2.83e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  137 WAHHWCAVWSagvwgkggPELC-----------GVDKAIFSGISQRCSHCTR--LGASIPCRSPGCPRLYHFPCATASGS 203
Cdd:cd15703    19 WAHVVCAIWI--------PEVCfantvflepveGVNNIPPARWKLTCYLCKQkgRGAAIQCHKVNCYTAFHVTCAQRAGL 90

                          90       100       110
                  ....*....|....*....|....*....|
gi 558137628  204 FLSMKTLQllcpEHSEGAAHLEEARCAVCE 233
Cdd:cd15703    91 FMKIEPVR----ETGLNGTTFTVRKTAYCE 116

PHD1_Lid2p_like

cd15519

PHD finger 1 found in Schizosaccharomyces pombe Lid2 complex component Lid2p and similar ...

229-273

3.00e-03

Pssm-ID: 276994 [Multi-domain] Cd Length: 46 Bit Score: 38.60 E-value: 3.00e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 558137628  229 CAVC---EGPGELcdlFFCTSCGHHYHGACLDTALTARKRAGWQCPEC 273
Cdd:cd15519     2 CEVCgldDNEGEV---LLCDGCDAEYHTSCLDPPLGEIPPGTWFCPSC 46

ePHD_BRPF3

cd15703

Extended PHD finger found in bromodomain and PHD finger-containing protein 3 (BRPF3) and ...

4823-4887

3.08e-03

Pssm-ID: 277173 [Multi-domain] Cd Length: 118 Bit Score: 40.81 E-value: 3.08e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 558137628 4823 WVHLNCALWSTEVYETQGGALMNVE----VALHRGLLTkCSLCQRT--GATSSCNRMRCPNVYHFACAIRA 4887
Cdd:cd15703    19 WAHVVCAIWIPEVCFANTVFLEPVEgvnnIPPARWKLT-CYLCKQKgrGAAIQCHKVNCYTAFHVTCAQRA 88

PHD_PHF21B

cd15524

PHD finger found in PHD finger protein 21B (PHF21B); PHF21B is a plant homeodomain (PHD) ...

276-320

3.12e-03

Pssm-ID: 276999 [Multi-domain] Cd Length: 43 Bit Score: 38.34 E-value: 3.12e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628  276 CQACRKPGNdskMLVCETCDKGYHTFCLKPPMEELPAHSWKCKAC 320
Cdd:cd15524     2 CAACKRGGN---LQPCGTCPRAYHLDCLDPPLKTAPKGVWVCPKC 43

PHD_UHRF1_2

cd15525

PHD finger found in ubiquitin-like PHD and RING finger domain-containing protein UHRF1 and ...

1107-1154

3.16e-03

Pssm-ID: 277000 Cd Length: 47 Bit Score: 38.50 E-value: 3.16e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 558137628 1107 CVVCGsfGRGAEGHLLACSQCSQCYHPYCVNSKITKVMLLKGWRCVEC 1154
Cdd:cd15525     2 CHVCG--GKQDPEKQLLCDECDMAYHLYCLDPPLTSLPDDDEWYCPDC 47

PHD1_KMT2A_like

cd15506

PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...

1106-1154

3.24e-03

Pssm-ID: 276981 Cd Length: 47 Bit Score: 38.49 E-value: 3.24e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 558137628 1106 MCVVCGSFGRGaegHLLACSQCSQCYHPYCVNSKITKVMLLKG-WRCVEC 1154
Cdd:cd15506     1 LCFLCGSAGLN---ELLYCSVCCEPYHTFCLEEAERPLNINKDnWCCRRC 47

PHD5_KMT2C_like

PHD finger 5 found in Histone-lysine N-methyltransferase 2C (KMT2C) and PHD finger 4 found in ...

231-273

3.33e-03

Pssm-ID: 276988 Cd Length: 47 Bit Score: 38.61 E-value: 3.33e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 558137628  231 VCEGPGELCD---LFFCTSCGHHYHGACLDTALTARKRAGWQCPEC 273
Cdd:cd15513     1 VCEGCGKASDesrLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWC 46

PHD1_AIRE

cd15539

PHD finger 1 found in autoimmune regulator (AIRE); AIRE, also termed autoimmune ...

229-273

3.39e-03

Pssm-ID: 277014 [Multi-domain] Cd Length: 43 Bit Score: 38.20 E-value: 3.39e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 558137628  229 CAVCEGPGELcdlFFCTSCGHHYHGACLDTALTARKRAGWQCPEC 273
Cdd:cd15539     2 CAVCGDGGEL---LCCDGCPRAFHLACLVPPLTLIPSGTWRCSSC 43

PRK12323

DNA polymerase III subunit gamma/tau;

2031-2253

3.45e-03

DNA polymerase III subunit gamma/tau;

Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 43.71 E-value: 3.45e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2031 LGFVDSPSSGPHLGSLELKAPDVFKAPLTPRASQVEPQSPglglrPQEPSPAQALAPSPPSHSDIFRPGPYPDPYAQPPL 2110
Cdd:PRK12323  361 LAFRPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPA-----APPAAPAAAPAAAAAARAVAAAPARRSPAPEALAA 435

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628 2111 TPRPQPPAPESCCALPPRSLPsdpfsrVPASPQSQSSSQSPltPRPLSAEAFCPSPVTPRFQSPDPYSRPPSRPQSRDPF 2190
Cdd:PRK12323  436 ARQASARGPGGAPAPAPAPAA------APAAAARPAAAGPR--PVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFA 507

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 558137628 2191 APLHKPPRPQPPEVAFKSGPLAHTPLGAGGFPAALPSGPAGELHAKVPSGQPPNFARSPGTGA 2253
Cdd:PRK12323  508 SPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASA 570

RING

smart00184

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...

229-273

3.48e-03

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)

Pssm-ID: 214546 [Multi-domain] Cd Length: 40 Bit Score: 38.26 E-value: 3.48e-03

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 558137628    229 CAVCEGpgELCDLFFCTSCGHHYHGACLDTALtarKRAGWQCPEC 273
Cdd:smart00184    1 CPICLE--EYLKDPVILPCGHTFCRSCIRKWL---ESGNNTCPIC 40

PHD_PHF2_like

cd15554

PHD finger found in PHF2, PHF8 and KDM7; This family includes PHF2, PHF8, KDM7, and similar ...

1236-1283

3.88e-03

PHD finger found in PHF2, PHF8 and KDM7; This family includes PHF2, PHF8, KDM7, and similar proteins. PHF2, also termed GRC5, or PHD finger protein 2, is a histone lysine demethylase ubiquitously expressed in various tissues. PHF8, also termed PHD finger protein 8, or KDM7B, is a monomethylated histone H4 lysine 20(H4K20me1) demethylase that transcriptionally regulates many cell cycle genes. It also preferentially acts on H3K9me2 and H3K9me1. PHF8 is modulated by CDC20-containing anaphase-promoting complex (APC (cdc20)) and plays an important role in the G2/M transition. It acts as a critical molecular sensor for mediating retinoic acid (RA) treatment response in RAR alpha-fusion-induced leukemia. Moreover, PHF8 is essential for cytoskeleton dynamics and is associated with X-linked mental retardation. KDM7, also termed JmjC domain-containing histone demethylation protein 1D (JHDM1D), or KIAA1718, is a dual histone demethylase that catalyzes demethylation of monomethylated and dimethylated H3K9 (H3K9me2/me1) and H3K27 (H3K27me2/me1), which functions as an eraser of silencing marks on chromatin during brain development. It also plays a tumor-suppressive role by regulating angiogenesis. All family members contain a plant homeodomain (PHD) finger and a JmjC domain.

Pssm-ID: 277029 Cd Length: 47 Bit Score: 38.13 E-value: 3.88e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 558137628 1236 ICHAPYVEEDLLIQCRHCERWMHAGCeslfTEDDVEQAAD-EGFDCVSC 1283
Cdd:cd15554     3 ICRQPYDVTRFMIECDVCKDWFHGSC----VGVEEHQANDiERYHCPNC 47

Med15

pfam09606

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...

3761-4110

3.91e-03

Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 43.84 E-value: 3.91e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  3761 LGPGmPAKPLQQHFSSPGALGPTLLLSGKEQSIVETTLPPE-----ATEGPSTHQGGVAIGTVPEAVPTEPGEVKPSlSG 3835
Cdd:pfam09606  102 MGPG-PGGPMGQQMGGPGTASNLLASLGRPQMPMGGAGFPSqmsrvGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPN-GG 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  3836 DSQLLLVQPQAQpQPNSVPLQPPLRLQGQqqqqqvNLLHTAGVGSHGQSNSGSSSEASsvPHLLTQSSVSLGEQPGPITQ 3915
Cdd:pfam09606  180 PGQGQAGGMNGG-QQGPMGGQMPPQMGVP------GMPGPADAGAQMGQQAQANGGMN--PQQMGGAPNQVAMQQQQPQQ 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  3916 NPLGSQQHHGLERPLQNNAGPQPAKPGSVPQSGQGLPGAGVMPTVGQFRAQLQGVLAKNPQlrhlSPQQQQQLQALLMQR 3995
Cdd:pfam09606  251 QGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQT----RQQQQQQGGNHPAAH 326

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558137628  3996 QLQQSQAIRQA------PSYQEPGTQPSPLQGLLGRQPQVGGFPGSQTGPLQELGAGLRPQGPPRLPAPQGALSTGPVPG 4069
Cdd:pfam09606  327 QQQMNQSVGQGgqvvalGGLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQG 406

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 558137628  4070 PVHPTPPPSSPQEPKRPSQLPSPS---SQLPSEAQLPPTQ-PGTP 4110
Cdd:pfam09606  407 PGSQPPQSHPGGMIPSPALIPSPSpqmSQQPAQQRTIGQDsPGGS 451

PHD1_KMT2C_like