NCBI Conserved Domain Search

Conserved domains on [gi|1907184719|ref|XP_036009397|]

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histone-lysine N-methyltransferase 2B isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

SET_KMT2A_2B

cd19170

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

1500-1653

5.08e-114

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: 356.32 E-value: 5.08e-114

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1500 MAMRFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIGCYMFRMDDFDVVDA 1579
Cdd:cd19170      1 MAMRFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKYYESKGIGCYMFRIDDDEVVDA 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907184719 1580 TMHGNAARFINHSCEPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEDasNKLPCNCGAKRCRRFLN 1653
Cdd:cd19170     81 TMHGNAARFINHSCEPNCYSRVVNIDGKKHIVIFALRRILRGEELTYDYKFPIED--VKIPCTCGSKKCRKYLN 152

ePHD_KMT2B

cd15694

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

518-622

1.79e-73

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: 239.56 E-value: 1.79e-73

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALCLKYGDADSKEAGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCELCLKPGATVGCCLSSCLS 597
Cdd:cd15694      1 CALCLKYGDADSKDAGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCEHCQKIGATVGCCLSACLS 80

                           90       100
                   ....*....|....*....|....*
gi 1907184719  598 NFHFMCARASYCIFQDDKKVFCQKH 622
Cdd:cd15694     81 NFHFMCARASRCCFQDDKKVFCQKH 105

Bromo_ALL-1

cd05493

Bromodomain, ALL-1 like proteins. ALL-1 is a vertebrate homologue of Drosophila trithorax and ...

311-453

6.04e-46

Bromodomain, ALL-1 like proteins. ALL-1 is a vertebrate homologue of Drosophila trithorax and is often affected in chromosomal rearrangements that are linked to acute leukemias, such as acute lymphocytic leukemia (ALL). Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.

Pssm-ID: 99925 Cd Length: 131 Bit Score: 161.83 E-value: 6.04e-46

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  311 EDYEILSGLPDSVLYTCGPCAGATQPRWREALSGALQGGLRQVLQGLLSSKVAGPLLLCTQCGQDGKQLHPGpcdlqavg 390
Cdd:cd05493      1 ELEELLDSRTKSHLLRCGPKPPALLPETEESLPGRKSPVTPEVLQGLLSSEVKQEELPPLDLEAVGKKLEAG-------- 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907184719  391 krFEEGLYKSVHSFMEDVVAILMRHSEEGETpeRRAGSQMKGLLLKLLESAFCWFDAHDPKYW 453
Cdd:cd05493     73 --FYTSVLDFSDDIVKIIQAALNSEGGQPEI--KKANSMAKSFFIKLMESVFPWFNSEDPKLW 131

PHD3_KMT2B

cd15593

PHD finger 3 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...

274-330

5.93e-36

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: 130.35 E-value: 5.93e-36

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907184719  274 YCPICTRCYEDNDYESKMMQCAQCDHWVHAKCEGLSDEDYEILSGLPDSVLYTCGPC 330
Cdd:cd15593      1 YCPICLKCYEDNDYESKMMQCAKCDHWVHAKCEGLSDELYEILSSLPDSVVYSCAPC 57

FYRC

smart00542

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

1351-1435

8.04e-32

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: 119.71 E-value: 8.04e-32

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  1351 HLRFEISSDDGFSVEAESLEVAWRTLIEKVQEARGHARLRHLSFSGMSGARLLGIHHDAVIFLAEQLPGAQRCQHYKFRY 1430
Cdd:smart00542    1 LFRVEIESDPGEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNYWFRY 80


                    ....*
gi 1907184719  1431 HQQGE 1435
Cdd:smart00542   81 HRSPL 85

PHD2_KMT2B

cd15591

PHD domain 2 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...

188-237

6.26e-30

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: 113.11 E-value: 6.26e-30

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907184719  188 FCHVCGRKGRGSKHLLECERCRHAYHPACLGPSYPTRATRRRRHWICSAC 237
Cdd:cd15591      1 FCHVCGRKNKESKPLLECERCRNCYHPACLGPNYPKPANRKKRPWICSAC 50

PHD1_KMT2B

cd15589

PHD finger 1 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...

140-186

1.46e-25

PHD finger 1 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 first PHD finger.

Pssm-ID: 277064 Cd Length: 47 Bit Score: 100.32 E-value: 1.46e-25

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1907184719  140 VCLLCASKGLHELVFCQVCCDPFHPFCLEEAERPSPQHRDTWCCRRC 186
Cdd:cd15589      1 VCLLCASKGQHELLFCQVCCEPFHRFCLEESERPLPEQEENWCCRRC 47

FYRN

pfam05964

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

670-717

7.02e-17

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: 76.00 E-value: 7.02e-17

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907184719  670 GSIRINSLGTL---SDLSDCEGRLFPIGYQCSRLYWSTVDARRRCWYRCRI 717
Cdd:pfam05964    1 GSLTVLSLGEIvpdRPAFHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51

PHA03247 super family

cl33720

large tegument protein UL36; Provisional

729-1153

2.27e-06

large tegument protein UL36; Provisional

The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.02 E-value: 2.27e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  729 PVHLEAAEENQTIVHSPTP---SSEPPNHDDLPDTDSLIP--------GDPVHH---SPIQNLDPpLRTDSSNGP----P 790
Cdd:PHA03247  2478 PVYRRPAEARFPFAAGAAPdpgGGGPPDPDAPPAPSRLAPailpdepvGEPVHPrmlTWIRGLEE-LASDDAGDPppplP 2556

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  791 PTPRSFSGARiKVPNYSPSRRPLGGVSFGPLPSPGSPSSLTHHIPTVGDSDFPAPPRRSRRPSPLATRPPPSRRTSSPLR 870
Cdd:PHA03247  2557 PAAPPAAPDR-SVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAA 2635

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  871 TSPQLRVPLSTSVTAL---TPTSGELAPPDLAPSPLPPSEDLGPDFEDMEVVSGLSAADLDFAASLLGTEPFQEEIVAAg 947
Cdd:PHA03247  2636 NEPDPHPPPTVPPPERprdDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHA- 2714

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  948 AVGSSQGGPGDSSEEEASPTTHYVHFPVTVVSGPALaPSSLAGAPRIEQLDGVDDGTDSEAEAVQQPRGQGTPPSGPGVG 1027
Cdd:PHA03247  2715 LVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAT-PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSE 2793

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1028 RGGVLGAAGDRAQPPEDLPSeivdfvlknlggPGEGAAGPREDSLPSAPPLANGSQPPQSLSTSPADPTRTFAWLpgAPG 1107
Cdd:PHA03247  2794 SRESLPSPWDPADPPAAVLA------------PAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSV--APG 2859

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1907184719 1108 VRVLSLGPA-PEPPKPATSKIILVNKLGQVFVKMAGEGEPVAPPVKQ 1153
Cdd:PHA03247  2860 GDVRRRPPSrSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPE 2906

Name

Accession

Description

Interval

E-value

SET_KMT2A_2B

cd19170

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

1500-1653

5.08e-114

Pssm-ID: 380947 [Multi-domain] Cd Length: 152 Bit Score: 356.32 E-value: 5.08e-114

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1500 MAMRFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIGCYMFRMDDFDVVDA 1579
Cdd:cd19170      1 MAMRFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKYYESKGIGCYMFRIDDDEVVDA 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907184719 1580 TMHGNAARFINHSCEPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEDasNKLPCNCGAKRCRRFLN 1653
Cdd:cd19170     81 TMHGNAARFINHSCEPNCYSRVVNIDGKKHIVIFALRRILRGEELTYDYKFPIED--VKIPCTCGSKKCRKYLN 152

ePHD_KMT2B

cd15694

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

518-622

1.79e-73

Pssm-ID: 277164 Cd Length: 105 Bit Score: 239.56 E-value: 1.79e-73

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALCLKYGDADSKEAGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCELCLKPGATVGCCLSSCLS 597
Cdd:cd15694      1 CALCLKYGDADSKDAGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCEHCQKIGATVGCCLSACLS 80

                           90       100
                   ....*....|....*....|....*
gi 1907184719  598 NFHFMCARASYCIFQDDKKVFCQKH 622
Cdd:cd15694     81 NFHFMCARASRCCFQDDKKVFCQKH 105

Bromo_ALL-1

cd05493

Bromodomain, ALL-1 like proteins. ALL-1 is a vertebrate homologue of Drosophila trithorax and ...

311-453

6.04e-46

Pssm-ID: 99925 Cd Length: 131 Bit Score: 161.83 E-value: 6.04e-46

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  311 EDYEILSGLPDSVLYTCGPCAGATQPRWREALSGALQGGLRQVLQGLLSSKVAGPLLLCTQCGQDGKQLHPGpcdlqavg 390
Cdd:cd05493      1 ELEELLDSRTKSHLLRCGPKPPALLPETEESLPGRKSPVTPEVLQGLLSSEVKQEELPPLDLEAVGKKLEAG-------- 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907184719  391 krFEEGLYKSVHSFMEDVVAILMRHSEEGETpeRRAGSQMKGLLLKLLESAFCWFDAHDPKYW 453
Cdd:cd05493     73 --FYTSVLDFSDDIVKIIQAALNSEGGQPEI--KKANSMAKSFFIKLMESVFPWFNSEDPKLW 131

SET

smart00317

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

1515-1635

4.65e-40

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: 144.78 E-value: 4.65e-40

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  1515 VGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGI-GCYMFRMDDFDVVDATMHGNAARFINHSC 1593
Cdd:smart00317    3 LEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkAFYLFDIDSDLCIDARRKGNLARFINHSC 82

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 1907184719  1594 EPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEDA 1635
Cdd:smart00317   83 EPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124

SET

COG2940

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

1500-1649

1.75e-36

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

Pssm-ID: 442183 [Multi-domain] Cd Length: 134 Bit Score: 134.70 E-value: 1.75e-36

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1500 MAMRFRHLKktskeavgVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRsvlTDKREKFYDGKGIGC-YMFRMDDFDVVD 1578
Cdd:COG2940      1 MAMLHPRIE--------VRPSPIHGRGVFATRDIPKGTLIGEYPGEVIT---WAEAERREPHKEPLHtYLFELDDDGVID 69

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907184719 1579 ATMHGNAARFINHSCEPNCFSRvihvEGQKHIVIFALRRILRGEELTYDYKFPIEDAsnKLPCNCgaKRCR 1649
Cdd:COG2940     70 GALGGNPARFINHSCDPNCEAD----EEDGRIFIVALRDIAAGEELTYDYGLDYDEE--EYPCRC--PNCR 132

PHD3_KMT2B

cd15593

PHD finger 3 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...

274-330

5.93e-36

Pssm-ID: 277068 Cd Length: 57 Bit Score: 130.35 E-value: 5.93e-36

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907184719  274 YCPICTRCYEDNDYESKMMQCAQCDHWVHAKCEGLSDEDYEILSGLPDSVLYTCGPC 330
Cdd:cd15593      1 YCPICLKCYEDNDYESKMMQCAKCDHWVHAKCEGLSDELYEILSSLPDSVVYSCAPC 57

SET

pfam00856

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

1524-1629

2.40e-33

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: 124.94 E-value: 2.40e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1524 GRGLFCKRNIDAGEMVIEYSG-IVIRSVLTDKREKFYDGKGI----GCYMFRMDDFD--VVDAT--MHGNAARFINHSCE 1594
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEvLLITKEEADKRELLYYDKLElrlwGPYLFTLDEDSeyCIDARalYYGNWARFINHSCD 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1907184719 1595 PNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYK 1629
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115

FYRC

smart00542

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

1351-1435

8.04e-32

Pssm-ID: 197781 Cd Length: 86 Bit Score: 119.71 E-value: 8.04e-32

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  1351 HLRFEISSDDGFSVEAESLEVAWRTLIEKVQEARGHARLRHLSFSGMSGARLLGIHHDAVIFLAEQLPGAQRCQHYKFRY 1430
Cdd:smart00542    1 LFRVEIESDPGEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNYWFRY 80


                    ....*
gi 1907184719  1431 HQQGE 1435
Cdd:smart00542   81 HRSPL 85

PHD2_KMT2B

cd15591

PHD domain 2 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...

188-237

6.26e-30

Pssm-ID: 277066 Cd Length: 50 Bit Score: 113.11 E-value: 6.26e-30

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907184719  188 FCHVCGRKGRGSKHLLECERCRHAYHPACLGPSYPTRATRRRRHWICSAC 237
Cdd:cd15591      1 FCHVCGRKNKESKPLLECERCRNCYHPACLGPNYPKPANRKKRPWICSAC 50

FYRC

pfam05965

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

1349-1431

8.06e-27

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: 105.38 E-value: 8.06e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1349 GPHLRFEISSDDGFSVEAESLEVAWRTLIEKVQEARGHARLRHLSFSGMSGARLLGIHHDAVIFLAEQLPGAQRCQHYKF 1428
Cdd:pfam05965    1 GPLFRVTVEEDPDESFEGSSPTKCWSMVLERVQELRREAGLKLKLPESISGEDMFGLTHPAVVRLIESLPGAEKCTNYKF 80


                   ...
gi 1907184719 1429 RYH 1431
Cdd:pfam05965   81 RYG 83

PHD1_KMT2B

cd15589

PHD finger 1 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...

140-186

1.46e-25

Pssm-ID: 277064 Cd Length: 47 Bit Score: 100.32 E-value: 1.46e-25

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1907184719  140 VCLLCASKGLHELVFCQVCCDPFHPFCLEEAERPSPQHRDTWCCRRC 186
Cdd:cd15589      1 VCLLCASKGQHELLFCQVCCEPFHRFCLEESERPLPEQEENWCCRRC 47

FYRN

pfam05964

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

670-717

7.02e-17

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: 76.00 E-value: 7.02e-17

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907184719  670 GSIRINSLGTL---SDLSDCEGRLFPIGYQCSRLYWSTVDARRRCWYRCRI 717
Cdd:pfam05964    1 GSLTVLSLGEIvpdRPAFHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51

zf-HC5HC2H

pfam13771

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

545-622

2.59e-16

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: 75.44 E-value: 2.59e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  545 HVNCAIWSAEVFEENDGS----LKNVHAAVARGRQMRCELC-LKPGATVGCCLSSCLSNFHFMCARASYCIFQ-----DD 614
Cdd:pfam13771    1 HVVCALWSPELVQRGNDSmgfpIEDIEKIPKRRWKLKCYLCkKKGGACIQCSKKNCRRAFHVTCALEAGLLMQfdednGT 80


                   ....*...
gi 1907184719  615 KKVFCQKH 622
Cdd:pfam13771   81 FKSYCKKH 88

FYRN

smart00541

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

677-719

4.94e-15

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: 70.39 E-value: 4.94e-15

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1907184719   677 LGTLSDLSDCEGRLFPIGYQCSRLYWSTVDARRRCWYRCRILE 719
Cdd:smart00541    2 LPIQGKLFHSESAIFPVGYKSTRKYWSVKDPNRRCLYSCVIDE 44

PHD

pfam00628

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

140-189

2.99e-09

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

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 54.42 E-value: 2.99e-09

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907184719  140 VCLLCASKGLH-ELVFCQVCCDPFHPFCLEEAERPSPQHRDTWCCRRCKFC 189
Cdd:pfam00628    1 YCAVCGKSDDGgELVQCDGCDDWFHLACLGPPLDPAEIPSGEWLCPECKPK 51

PHD

pfam00628

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

274-330

1.71e-08

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 52.11 E-value: 1.71e-08

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907184719  274 YCPICTRcyedNDYESKMMQCAQCDHWVHAKCEGLSDEDYEILSGlpdsvLYTCGPC 330
Cdd:pfam00628    1 YCAVCGK----SDDGGELVQCDGCDDWFHLACLGPPLDPAEIPSG-----EWLCPEC 48

PHD

pfam00628

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

188-240

4.73e-08

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 50.95 E-value: 4.73e-08

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907184719  188 FCHVCGRKGRGSKhLLECERCRHAYHPACLGPSyPTRATRRRRHWICSACVRC 240
Cdd:pfam00628    1 YCAVCGKSDDGGE-LVQCDGCDDWFHLACLGPP-LDPAEIPSGEWLCPECKPK 51

PHD

smart00249

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

188-237

5.29e-08

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: 50.67 E-value: 5.29e-08

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1907184719   188 FCHVCGRKGRGSKhLLECERCRHAYHPACLGPSYPTRATrrRRHWICSAC 237
Cdd:smart00249    1 YCSVCGKPDDGGE-LLQCDGCDRWYHQTCLGPPLLEEEP--DGKWYCPKC 47

PHA03247

large tegument protein UL36; Provisional

729-1153

2.27e-06

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.02 E-value: 2.27e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  729 PVHLEAAEENQTIVHSPTP---SSEPPNHDDLPDTDSLIP--------GDPVHH---SPIQNLDPpLRTDSSNGP----P 790
Cdd:PHA03247  2478 PVYRRPAEARFPFAAGAAPdpgGGGPPDPDAPPAPSRLAPailpdepvGEPVHPrmlTWIRGLEE-LASDDAGDPppplP 2556

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  791 PTPRSFSGARiKVPNYSPSRRPLGGVSFGPLPSPGSPSSLTHHIPTVGDSDFPAPPRRSRRPSPLATRPPPSRRTSSPLR 870
Cdd:PHA03247  2557 PAAPPAAPDR-SVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAA 2635

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  871 TSPQLRVPLSTSVTAL---TPTSGELAPPDLAPSPLPPSEDLGPDFEDMEVVSGLSAADLDFAASLLGTEPFQEEIVAAg 947
Cdd:PHA03247  2636 NEPDPHPPPTVPPPERprdDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHA- 2714

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  948 AVGSSQGGPGDSSEEEASPTTHYVHFPVTVVSGPALaPSSLAGAPRIEQLDGVDDGTDSEAEAVQQPRGQGTPPSGPGVG 1027
Cdd:PHA03247  2715 LVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAT-PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSE 2793

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1028 RGGVLGAAGDRAQPPEDLPSeivdfvlknlggPGEGAAGPREDSLPSAPPLANGSQPPQSLSTSPADPTRTFAWLpgAPG 1107
Cdd:PHA03247  2794 SRESLPSPWDPADPPAAVLA------------PAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSV--APG 2859

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1907184719 1108 VRVLSLGPA-PEPPKPATSKIILVNKLGQVFVKMAGEGEPVAPPVKQ 1153
Cdd:PHA03247  2860 GDVRRRPPSrSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPE 2906

PHD

smart00249

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

140-186

6.15e-06

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 44.90 E-value: 6.15e-06

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1907184719   140 VCLLCASK-GLHELVFCQVCCDPFHPFCLEEAERPSPQhRDTWCCRRC 186
Cdd:smart00249    1 YCSVCGKPdDGGELLQCDGCDRWYHQTCLGPPLLEEEP-DGKWYCPKC 47

PHD

smart00249

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

274-330

1.53e-05

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 43.74 E-value: 1.53e-05

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907184719   274 YCPICTRCYEDNDyeskMMQCAQCDHWVHAKCEGLSDEDYeilsglPDSVLYTCGPC 330
Cdd:smart00249    1 YCSVCGKPDDGGE----LLQCDGCDRWYHQTCLGPPLLEE------EPDGKWYCPKC 47

COG5141

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

541-625

5.45e-04

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

Pssm-ID: 227470 [Multi-domain] Cd Length: 669 Bit Score: 44.59 E-value: 5.45e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  541 NEWTHVNCAIWSAEVFEENDGSLKNVH--AAVARGR-QMRCELC-LKPGATVGCCLSSCLSNFHFMCAR----------- 605
Cdd:COG5141    266 GRWGHVICAMFNPELSFGHLLSKDPIDniASVSSSRwKLGCLICkEFGGTCIQCSYFNCTRAYHVTCARragyfdlniys 345

                           90       100
                   ....*....|....*....|...
gi 1907184719  606 ---ASYCIfqdDKKVFCQKHTDL 625
Cdd:COG5141    346 hngISYCI---DHEPLCRKHYPL 365

Name

Accession

Description

Interval

E-value

SET_KMT2A_2B

cd19170

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

1500-1653

5.08e-114

Pssm-ID: 380947 [Multi-domain] Cd Length: 152 Bit Score: 356.32 E-value: 5.08e-114

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1500 MAMRFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIGCYMFRMDDFDVVDA 1579
Cdd:cd19170      1 MAMRFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKYYESKGIGCYMFRIDDDEVVDA 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907184719 1580 TMHGNAARFINHSCEPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEDasNKLPCNCGAKRCRRFLN 1653
Cdd:cd19170     81 TMHGNAARFINHSCEPNCYSRVVNIDGKKHIVIFALRRILRGEELTYDYKFPIED--VKIPCTCGSKKCRKYLN 152

SET_KMT2B

cd19207

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

1500-1653

2.36e-106

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: 335.07 E-value: 2.36e-106

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1500 MAMRFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIGCYMFRMDDFDVVDA 1579
Cdd:cd19207      1 MAMRFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDSKGIGCYMFRIDDFDVVDA 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907184719 1580 TMHGNAARFINHSCEPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEDASNKLPCNCGAKRCRRFLN 1653
Cdd:cd19207     81 TMHGNAARFINHSCEPNCYSRVIHVEGQKHIVIFALRKIYRGEELTYDYKFPIEDASNKLPCNCGAKRCRRFLN 154

SET_KMT2A

cd19206

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

1500-1653

5.98e-103

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: 325.44 E-value: 5.98e-103

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1500 MAMRFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIGCYMFRMDDFDVVDA 1579
Cdd:cd19206      1 MPMRFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREKYYDSKGIGCYMFRIDDSEVVDA 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907184719 1580 TMHGNAARFINHSCEPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEDASNKLPCNCGAKRCRRFLN 1653
Cdd:cd19206     81 TMHGNAARFINHSCEPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDASNKLPCNCGAKKCRKFLN 154

SET_SETD1-like

cd10518

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

1500-1649

2.01e-85

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: 275.24 E-value: 2.01e-85

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1500 MAMRFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGI-GCYMFRMDDFDVVD 1578
Cdd:cd10518      1 MSKRFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKRYDEEGGgGTYMFRIDEDLVID 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907184719 1579 ATMHGNAARFINHSCEPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEDAsNKLPCNCGAKRCR 1649
Cdd:cd10518     81 ATKKGNIARFINHSCDPNCYAKIITVDGEKHIVIFAKRDIAPGEELTYDYKFPIEDE-EKIPCLCGAPNCR 150

ePHD_KMT2B

cd15694

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

518-622

1.79e-73

Pssm-ID: 277164 Cd Length: 105 Bit Score: 239.56 E-value: 1.79e-73

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALCLKYGDADSKEAGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCELCLKPGATVGCCLSSCLS 597
Cdd:cd15694      1 CALCLKYGDADSKDAGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCEHCQKIGATVGCCLSACLS 80

                           90       100
                   ....*....|....*....|....*
gi 1907184719  598 NFHFMCARASYCIFQDDKKVFCQKH 622
Cdd:cd15694     81 NFHFMCARASRCCFQDDKKVFCQKH 105

ePHD_KMT2A_like

cd15664

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

518-622

5.35e-69

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: 226.52 E-value: 5.35e-69

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALCLKYGDADSKEAGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCELCLKPGATVGCCLSSCLS 597
Cdd:cd15664      1 CALCGVYGDDEPNDAGRLLYCGQDEWVHINCALWSAEVFEEDDGSLQNVHSAVSRGRMMKCELCGKPGATVGCCLKSCPA 80

                           90       100
                   ....*....|....*....|....*
gi 1907184719  598 NFHFMCARASYCIFQDDKKVFCQKH 622
Cdd:cd15664     81 NYHFMCARKAECVFQDDKKVFCPAH 105

ePHD_KMT2A

cd15693

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

516-628

2.04e-67

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: 222.57 E-value: 2.04e-67

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  516 RQCALCLKYGDADSKEAGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCELCLKPGATVGCCLSSC 595
Cdd:cd15693      1 RQCALCLKYGDDSANDAGRLLYIGQNEWTHVNCALWSAEVFEDDDGSLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSC 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1907184719  596 LSNFHFMCARASYCIFQDDKKVFCQKHTDLLDG 628
Cdd:cd15693     81 TSNYHFMCSRAKNCVFLEDKKVYCQRHKDLIKG 113

SET_SETD1

cd19169

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

1502-1649

6.08e-62

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: 208.35 E-value: 6.08e-62

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1502 MRFRHLKkTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIG-CYMFRMDDFDVVDAT 1580
Cdd:cd19169      3 LKFNQLK-FRKKQLKFAKSRIHDWGLFALEPIAADEMVIEYVGQVIRQSVADEREKRYEAIGIGsSYLFRVDDDTIIDAT 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907184719 1581 MHGNAARFINHSCEPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEDasNKLPCNCGAKRCR 1649
Cdd:cd19169     82 KCGNLARFINHSCNPNCYAKIITVESQKKIVIYSKRPIAVNEEITYDYKFPIED--EKIPCLCGAPQCR 148

SET_KMT2C_2D

cd19171

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

1504-1652

1.27e-59

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: 201.89 E-value: 1.27e-59

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1504 FRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIGCYMFRMDDFDVVDATMHG 1583
Cdd:cd19171      5 YRKLKTEWRSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNRGIYMFRIDNDWVIDATMTG 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907184719 1584 NAARFINHSCEPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEDASNKLPCNCGAKRCRRFL 1652
Cdd:cd19171     85 GPARYINHSCNPNCVAEVVTFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQHKIPCLCGAPNCRKWM 153

SET_SET1

cd20072

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

1502-1649

9.51e-57

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: 193.41 E-value: 9.51e-57

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1502 MRFRHLKKTSKEaVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIG-CYMFRMDDFDVVDAT 1580
Cdd:cd20072      3 LRFNQLKKRKKQ-LKFARSAIHNWGLYAMENISAKDMVIEYVGEVIRQQVADEREKRYLRQGIGsSYLFRIDDDTVVDAT 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907184719 1581 MHGNAARFINHSCEPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEDasNKLPCNCGAKRCR 1649
Cdd:cd20072     82 KKGNIARFINHCCDPNCTAKIIKVEGEKRIVIYAKRDIAAGEELTYDYKFPREE--DKIPCLCGAPNCR 148

SET_KMT2C

cd19208

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

1503-1652

5.36e-47

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: 165.57 E-value: 5.36e-47

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1503 RFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIGCYMFRMDDFDVVDATMH 1582
Cdd:cd19208      5 QYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRIDNDHVIDATLT 84

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1583 GNAARFINHSCEPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEDASNKLPCNCGAKRCRRFL 1652
Cdd:cd19208     85 GGPARYINHSCAPNCVAEVVTFEKGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWM 154

Bromo_ALL-1

cd05493

Bromodomain, ALL-1 like proteins. ALL-1 is a vertebrate homologue of Drosophila trithorax and ...

311-453

6.04e-46

Pssm-ID: 99925 Cd Length: 131 Bit Score: 161.83 E-value: 6.04e-46

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  311 EDYEILSGLPDSVLYTCGPCAGATQPRWREALSGALQGGLRQVLQGLLSSKVAGPLLLCTQCGQDGKQLHPGpcdlqavg 390
Cdd:cd05493      1 ELEELLDSRTKSHLLRCGPKPPALLPETEESLPGRKSPVTPEVLQGLLSSEVKQEELPPLDLEAVGKKLEAG-------- 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907184719  391 krFEEGLYKSVHSFMEDVVAILMRHSEEGETpeRRAGSQMKGLLLKLLESAFCWFDAHDPKYW 453
Cdd:cd05493     73 --FYTSVLDFSDDIVKIIQAALNSEGGQPEI--KKANSMAKSFFIKLMESVFPWFNSEDPKLW 131

SET_SETD1A

cd19204

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

1509-1653

1.37e-45

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: 161.73 E-value: 1.37e-45

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1509 KTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIGC-YMFRMDDFDVVDATMHGNAAR 1587
Cdd:cd19204     10 KFRKKKLRFGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQVVADMREKRYVQEGIGSsYLFRVDHDTIIDATKCGNLAR 89

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907184719 1588 FINHSCEPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEDasNKLPCNCGAKRCRRFLN 1653
Cdd:cd19204     90 FINHCCTPNCYAKVITIESQKKIVIYSKQPIGVNEEITYDYKFPIED--NKIPCLCGTENCRGTLN 153

SET_SETD1B

cd19205

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

1502-1653

4.42e-45

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: 160.22 E-value: 4.42e-45

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1502 MRFRHLKkTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIGC-YMFRMDDFDVVDAT 1580
Cdd:cd19205      4 LKFNQLK-FRKKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKRYEDEGIGSsYMFRVDHDTIIDAT 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907184719 1581 MHGNAARFINHSCEPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEDasNKLPCNCGAKRCRRFLN 1653
Cdd:cd19205     83 KCGNFARFINHSCNPNCYAKVITVESQKKIVIYSKQHINVNEEITYDYKFPIED--VKIPCLCGSENCRGTLN 153

SET_KMT2D

cd19209

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

1503-1652

1.01e-42

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) and similar proteins; KMT2D (EC2.1.1.43; also termed lysine N-methyltransferase 2D, ALL1-related protein (ALR), or myeloid/lymphoid or mixed-lineage leukemia protein 2 (MLL2)), acts as histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me). It is a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription. KMT2D is a subunit of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation.

Pssm-ID: 380986 [Multi-domain] Cd Length: 155 Bit Score: 153.70 E-value: 1.01e-42

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1503 RFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIGCYMFRMDDFDVVDATMH 1582
Cdd:cd19209      6 QYRRLKTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVIDATLT 85

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1583 GNAARFINHSCEPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEDASNKLPCNCGAKRCRRFL 1652
Cdd:cd19209     86 GGPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIPCHCGAWNCRKWM 155

SET

smart00317

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

1515-1635

4.65e-40

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: 144.78 E-value: 4.65e-40

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  1515 VGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGI-GCYMFRMDDFDVVDATMHGNAARFINHSC 1593
Cdd:smart00317    3 LEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkAFYLFDIDSDLCIDARRKGNLARFINHSC 82

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 1907184719  1594 EPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEDA 1635
Cdd:smart00317   83 EPNCELLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124

SET

COG2940

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

1500-1649

1.75e-36

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

Pssm-ID: 442183 [Multi-domain] Cd Length: 134 Bit Score: 134.70 E-value: 1.75e-36

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1500 MAMRFRHLKktskeavgVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRsvlTDKREKFYDGKGIGC-YMFRMDDFDVVD 1578
Cdd:COG2940      1 MAMLHPRIE--------VRPSPIHGRGVFATRDIPKGTLIGEYPGEVIT---WAEAERREPHKEPLHtYLFELDDDGVID 69

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907184719 1579 ATMHGNAARFINHSCEPNCFSRvihvEGQKHIVIFALRRILRGEELTYDYKFPIEDAsnKLPCNCgaKRCR 1649
Cdd:COG2940     70 GALGGNPARFINHSCDPNCEAD----EEDGRIFIVALRDIAAGEELTYDYGLDYDEE--EYPCRC--PNCR 132

PHD3_KMT2B

cd15593

PHD finger 3 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...

274-330

5.93e-36

Pssm-ID: 277068 Cd Length: 57 Bit Score: 130.35 E-value: 5.93e-36

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907184719  274 YCPICTRCYEDNDYESKMMQCAQCDHWVHAKCEGLSDEDYEILSGLPDSVLYTCGPC 330
Cdd:cd15593      1 YCPICLKCYEDNDYESKMMQCAKCDHWVHAKCEGLSDELYEILSSLPDSVVYSCAPC 57

PHD3_KMT2A_like

cd15508

PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...

274-330

1.17e-34

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: 126.79 E-value: 1.17e-34

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907184719  274 YCPICTRCYEDNDYESKMMQCAQCDHWVHAKCEGLSDEDYEILSGLPDSVLYTCGPC 330
Cdd:cd15508      1 YCPLCEKCYDDDDYDSKMMQCSQCDHWVHAKCEGLSDEMYEILSYLPESIEYTCSLC 57

SET_SETD2-like

cd10531

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

1524-1649

2.26e-34

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: 128.91 E-value: 2.26e-34

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1524 GRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIGC-YMFRMDDFDVVDATMHGNAARFINHSCEPNCFSRVI 1602
Cdd:cd10531     11 GWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERLDEYEELGKSNfYILSLSDDVVIDATRKGNLSRFINHSCEPNCETQKW 90

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1907184719 1603 HVEGQKHIVIFALRRILRGEELTYDYKFPIEDASNKLpCNCGAKRCR 1649
Cdd:cd10531     91 IVNGEYRIGIFALRDIPAGEELTFDYNFVNYNEAKQV-CLCGAQNCR 136

SET

pfam00856

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

1524-1629

2.40e-33

Pssm-ID: 459965 [Multi-domain] Cd Length: 115 Bit Score: 124.94 E-value: 2.40e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1524 GRGLFCKRNIDAGEMVIEYSG-IVIRSVLTDKREKFYDGKGI----GCYMFRMDDFD--VVDAT--MHGNAARFINHSCE 1594
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEvLLITKEEADKRELLYYDKLElrlwGPYLFTLDEDSeyCIDARalYYGNWARFINHSCD 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1907184719 1595 PNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYK 1629
Cdd:pfam00856   81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDYG 115

SET_EZH

cd10519

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

1513-1628

1.00e-32

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: 123.51 E-value: 1.00e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1513 EAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIGcYMFRMDDFDVVDATMHGNAARFINHS 1592
Cdd:cd10519      1 KRLLLGKSDVAGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGKIYDKYNSS-YLFNLNDQFVVDATRKGNKIRFANHS 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1907184719 1593 CEPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDY 1628
Cdd:cd10519     80 SNPNCYAKVMMVNGDHRIGIFAKRDIEAGEELFFDY 115

SET_ASHR3-like

cd19175

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

1524-1652

1.52e-32

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: 123.68 E-value: 1.52e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1524 GRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKG-IGCYMFRMDDFDVVDATMHGNAARFINHSCEPNCFSRVI 1602
Cdd:cd19175     11 GWGLVADEDINAGEFIIEYVGEVIDDKTCEERLWDMKHKGeKNFYMCEIDKDMVIDATFKGNLSRFINHSCDPNCELQKW 90

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1603 HVEGQKHIVIFALRRILRGEELTYDYKFpiEDASNKLPCNCGAKRCRRFL 1652
Cdd:cd19175     91 QVDGETRIGVFAIRDIKKGEELTYDYQF--VQFGADQDCHCGSKNCRGKL 138

ePHD2_KMT2C_like

cd15666

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

518-622

5.46e-32

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: 120.87 E-value: 5.46e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALCLKYGDADSKEAGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCELCLKPGATVGCCLSSCLS 597
Cdd:cd15666      1 CVLCGGEGDGDTDGPGRLLNLDVDKWVHLNCALWSYEVYETQNGALMNVEEALRRALTTTCSHCGRTGATVPCFKPRCAN 80

                           90       100
                   ....*....|....*....|....*
gi 1907184719  598 NFHFMCARASYCIFQDDKKVFCQKH 622
Cdd:cd15666     81 VYHLPCAIKDGCMFFKDKTMLCPSH 105

SET_ASH1L

cd19174

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

1517-1653

6.50e-32

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: 122.02 E-value: 6.50e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1517 VYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKR--EKFYDGKGIgcYMFRMDDFDVVDATMHGNAARFINHSCE 1594
Cdd:cd19174      4 RFRTEDKGWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRmiEQYHNHSHH--YCLNLDSGMVIDGYRMGNEARFVNHSCD 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907184719 1595 PNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEDASNKLPCNCGAKRCRRFLN 1653
Cdd:cd19174     82 PNCEMQKWSVNGVYRIGLFALKDIPAGEELTYDYNFHSFNVEKQQPCKCGSPNCRGVIG 140

FYRC

smart00542

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

1351-1435

8.04e-32

Pssm-ID: 197781 Cd Length: 86 Bit Score: 119.71 E-value: 8.04e-32

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  1351 HLRFEISSDDGFSVEAESLEVAWRTLIEKVQEARGHARLRHLSFSGMSGARLLGIHHDAVIFLAEQLPGAQRCQHYKFRY 1430
Cdd:smart00542    1 LFRVEIESDPGEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEGVSGEEMFGLSSPAVVKLIEALPGVHQCTNYWFRY 80


                    ....*
gi 1907184719  1431 HQQGE 1435
Cdd:smart00542   81 HRSPL 85

SET_SETD2

cd19172

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

1515-1652

1.62e-31

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: 120.76 E-value: 1.62e-31

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1515 VGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIGCYMFRMDDFD-VVDATMHGNAARFINHSC 1593
Cdd:cd19172      4 VEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLDEKEFKRRMKEYAREGNRHYYFMALKSDeIIDATKKGNLSRFINHSC 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907184719 1594 EPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEDASNKlPCNCGAKRCRRFL 1652
Cdd:cd19172     84 EPNCETQKWTVNGELRVGFFAKRDIPAGEELTFDYQFERYGKEAQ-KCYCGSPNCRGYI 141

PHD2_KMT2B

cd15591

PHD domain 2 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...

188-237

6.26e-30

Pssm-ID: 277066 Cd Length: 50 Bit Score: 113.11 E-value: 6.26e-30

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907184719  188 FCHVCGRKGRGSKHLLECERCRHAYHPACLGPSYPTRATRRRRHWICSAC 237
Cdd:cd15591      1 FCHVCGRKNKESKPLLECERCRNCYHPACLGPNYPKPANRKKRPWICSAC 50

SET_SETDB-like

cd10538

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

1505-1628

3.44e-28

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: 114.01 E-value: 3.44e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1505 RHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGiGCYMFRMDDFD--------- 1575
Cdd:cd10538     81 RVVQRGLQARLQVFRTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRGKIYDKSG-GSYLFDLDEFSdsdgdgeel 159

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907184719 1576 VVDATMHGNAARFINHSCEPNCFSRVIHVEGQKH----IVIFALRRILRGEELTYDY 1628
Cdd:cd10538    160 CVDATFCGNVSRFINHSCDPNLFPFNVVIDHDDLryprIALFATRDILPGEELTFDY 216

SET_NSD

cd19173

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

1517-1652

6.01e-28

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: 110.87 E-value: 6.01e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1517 VYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGI-GCYMFRMDDFDVVDATMHGNAARFINHSCEP 1595
Cdd:cd19173      6 PFKTGDRGWGLRTKRDIKKGDFVIEYVGELIDEEECRRRLKKAHENNItNFYMLTLDKDRIIDAGPKGNLSRFMNHSCQP 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907184719 1596 NCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFpiEDASN-KLPCNCGAKRCRRFL 1652
Cdd:cd19173     86 NCETQKWTVNGDTRVGLFAVRDIPAGEELTFNYNL--DCLGNeKKVCRCGAPNCSGFL 141

PHD3_KMT2A

cd15592

PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, ...

274-330

1.49e-27

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: 106.61 E-value: 1.49e-27

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907184719  274 YCPICTRCYEDNDYESKMMQCAQCDHWVHAKCEGLSDEDYEILSGLPDSVLYTCGPC 330
Cdd:cd15592      1 FCPLCDKCYDDDDYESKMMQCGKCDRWVHSKCENLSDEMYEILSNLPESVAYTCINC 57

SET_SUV39H

cd10542

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

1524-1652

2.75e-27

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: 112.39 E-value: 2.75e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1524 GRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIgCYMFRMDDFD-----VVDATMHGNAARFINHSCEPN-- 1596
Cdd:cd10542     99 GWGVKTLEDIKKGTFVMEYVGEIITSEEAERRGKIYDANGR-TYLFDLDYNDddceyTVDAAYYGNISHFINHSCDPNla 177

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907184719 1597 CFSRVI-HVEGQK-HIVIFALRRILRGEELTYDYKFPIEDASN----------KLPCNCGAKRCRRFL 1652
Cdd:cd10542    178 VYAVWInHLDPRLpRIAFFAKRDIKAGEELTFDYLMTGTGGSSestipkpkdvRVPCLCGSKNCRKYL 245

FYRC

pfam05965

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

1349-1431

8.06e-27

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: 105.38 E-value: 8.06e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1349 GPHLRFEISSDDGFSVEAESLEVAWRTLIEKVQEARGHARLRHLSFSGMSGARLLGIHHDAVIFLAEQLPGAQRCQHYKF 1428
Cdd:pfam05965    1 GPLFRVTVEEDPDESFEGSSPTKCWSMVLERVQELRREAGLKLKLPESISGEDMFGLTHPAVVRLIESLPGAEKCTNYKF 80


                   ...
gi 1907184719 1429 RYH 1431
Cdd:pfam05965   81 RYG 83

SET_LegAS4-like

cd10522

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

1524-1628

1.28e-26

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: 106.27 E-value: 1.28e-26

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1524 GRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKgigCYMFRMDDFD-VVDATMHGNAARFINHSCEPNCFSRVI 1602
Cdd:cd10522     14 GLGLFAAETIAKGEFVGEYTGEVLDRWEEDRDSVYHYDP---LYPFDLNGDIlVIDAGKKGNLTRFINHSDQPNLELIVR 90

                           90       100
                   ....*....|....*....|....*.
gi 1907184719 1603 HVEGQKHIVIFALRRILRGEELTYDY 1628
Cdd:cd10522     91 TLKGEQHIGFVAIRDIKPGEELFISY 116

PHD1_KMT2B

cd15589

PHD finger 1 found in Histone-lysine N-methyltransferase 2B (KMT2B); KMT2B, also termed ...

140-186

1.46e-25

Pssm-ID: 277064 Cd Length: 47 Bit Score: 100.32 E-value: 1.46e-25

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1907184719  140 VCLLCASKGLHELVFCQVCCDPFHPFCLEEAERPSPQHRDTWCCRRC 186
Cdd:cd15589      1 VCLLCASKGQHELLFCQVCCEPFHRFCLEESERPLPEQEENWCCRRC 47

ePHD

cd15571

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

518-622

2.56e-25

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: 102.28 E-value: 2.56e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALCLKYGDAdSKEAGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLK--NVHAAVARGRQMRCELCLKP-GATVGCCLSS 594
Cdd:cd15571      1 CALCPRSGGA-LKGGGALKTTSDGLWVHVVCALWSPEVYFDDGTLLEveGVSKIPKRRKKLKCSICGKRgGACIQCSYPG 79

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1907184719  595 CLSNFHFMCARASYCIF-----QDDKKVFCQKH 622
Cdd:cd15571     80 CPRSFHVSCAIRAGCLFefedgPGNFVVYCPKH 112

ePHD2_KMT2C

cd15697

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

518-622

1.13e-24

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: 100.12 E-value: 1.13e-24

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALCLKYGDADSKEAGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCELCLKPGATVGCCLSSCLS 597
Cdd:cd15697      1 CCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVYETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRLRCTN 80

                           90       100
                   ....*....|....*....|....*
gi 1907184719  598 NFHFMCARASYCIFQDDKKVFCQKH 622
Cdd:cd15697     81 VYHFTCAIKAQCMFFKDKTMLCPMH 105

PHD2_KMT2A_like

cd15507

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

188-237

1.19e-24

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: 97.92 E-value: 1.19e-24

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907184719  188 FCHVCGRKGRGSKHLLECERCRHAYHPACLGPSYPTRATRRRRHWICSAC 237
Cdd:cd15507      1 FCHVCGRKGQAQKQLLECEKCQRGYHVDCLGPSYPTKPTRKKKTWICSKC 50

ePHD2_KMT2D

cd15698

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

518-622

2.87e-23

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: 95.89 E-value: 2.87e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALCLKYGDADSKEAGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCELCLKPGATVGCCLSSCLS 597
Cdd:cd15698      1 CCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQKTGATNSCNRLRCPN 80

                           90       100
                   ....*....|....*....|....*
gi 1907184719  598 NFHFMCARASYCIFQDDKKVFCQKH 622
Cdd:cd15698     81 VYHFACAIRAKCMFFKDKTMLCPMH 105

SET_EZH1

cd19217

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

1520-1635

1.21e-22

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: 95.52 E-value: 1.21e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1520 SAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDgKGIGCYMFRMDDFDVVDATMHGNAARFINHSCEPNCFS 1599
Cdd:cd19217     13 SDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYD-KYMSSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYA 91

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1907184719 1600 RVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEDA 1635
Cdd:cd19217     92 KVVMVNGDHRIGIFAKRAIQQGEELFFDYRYSQADA 127

SET_EZH2

cd19218

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

1520-1630

1.22e-22

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: 94.59 E-value: 1.22e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1520 SAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDgKGIGCYMFRMDDFDVVDATMHGNAARFINHSCEPNCFS 1599
Cdd:cd19218     11 SDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYD-KYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYA 89

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1907184719 1600 RVIHVEGQKHIVIFALRRILRGEELTYDYKF 1630
Cdd:cd19218     90 KVMMVNGDHRIGIFAKRAIQTGEELFFDYRY 120

SET_NSD1

cd19210

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

1515-1652

2.01e-22

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: 94.99 E-value: 2.01e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1515 VGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGI-GCYMFRMDDFDVVDATMHGNAARFINHSC 1593
Cdd:cd19210      4 VEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDItNFYMLTLDKDRIIDAGPKGNYARFMNHCC 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1594 EPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKfpIEDASN-KLPCNCGAKRCRRFL 1652
Cdd:cd19210     84 QPNCETQKWTVNGDTRVGLFALCDIKAGTELTFNYN--LECLGNgKTVCKCGAPNCSGFL 141

SET_SETD8

cd10528

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

1517-1628

7.56e-22

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: 93.02 E-value: 7.56e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1517 VYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFY-DGKGIGCYM--FRMDDFDV-VDATMH-GNAARFINH 1591
Cdd:cd10528     21 VIEIDGKGRGVIATRPFEKGDFVVEYHGDLITITEAKKREALYaKDPSTGCYMyyFQYKGKTYcVDATKEsGRLGRLINH 100

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907184719 1592 SC-EPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDY 1628
Cdd:cd10528    101 SKkKPNLKTKLLVIDGVPHLILVAKRDIKPGEELLYDY 138

PHD1_KMT2A_like

cd15506

PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...

140-186

1.38e-21

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: 88.96 E-value: 1.38e-21

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1907184719  140 VCLLCASKGLHELVFCQVCCDPFHPFCLEEAERPSPQHRDTWCCRRC 186
Cdd:cd15506      1 LCFLCGSAGLNELLYCSVCCEPYHTFCLEEAERPLNINKDNWCCRRC 47

SET_NSD2

cd19211

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

1517-1652

2.13e-21

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: 91.98 E-value: 2.13e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1517 VYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIG-CYMFRMDDFDVVDATMHGNAARFINHSCEP 1595
Cdd:cd19211      6 IIKTEGKGWGLIAKRDIKKGEFVNEYVGELIDEEECMARIKHAHENDIThFYMLTIDKDRIIDAGPKGNYSRFMNHSCQP 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907184719 1596 NCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEdASNKLPCNCGAKRCRRFL 1652
Cdd:cd19211     86 NCETQKWTVNGDTRVGLFAVCDIPAGTELTFNYNLDCL-GNEKTVCRCGAPNCSGFL 141

SET_SETMAR

cd10544

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

1517-1652

1.65e-20

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: 92.75 E-value: 1.65e-20

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1517 VYRSAIHGRGLFCKRNIDAGEMVIEYSGIVI------RSVLTDK----------REKFYDGKGIGCYmfrmddfdvVDAT 1580
Cdd:cd10544     94 VFKTPKKGWGLRTLEFIPKGRFVCEYAGEVIgfeearRRTKSQTkgdmnyiivlREHLSSGKVLETF---------VDPT 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1581 MHGNAARFINHSCEPNCFSRVIHVEGQ-KHIVIFALRRILRGEELTYDY------------KFPIEDASNKLPCNCGAKR 1647
Cdd:cd10544    165 YIGNIGRFLNHSCEPNLFMVPVRVDSMvPKLALFAARDIVAGEELSFDYsgefsnsvesvtLARQDESKSRKPCLCGAEN 244


                   ....*
gi 1907184719 1648 CRRFL 1652
Cdd:cd10544    245 CRGFL 249

PHD2_KMT2A

cd15590

PHD finger 2 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, ...

188-237

1.70e-20

PHD finger 2 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 second PHD finger.

Pssm-ID: 277065 Cd Length: 50 Bit Score: 86.23 E-value: 1.70e-20

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907184719  188 FCHVCGRKGRGSKHLLECERCRHAYHPACLGPSYPTRATRRRRHWICSAC 237
Cdd:cd15590      1 FCHVCGRQHQATKQLLECNKCRNSYHPECLGPNYPTKPTKKKRVWICTKC 50

SET_SUV39H_Clr4-like

cd20073

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

1517-1652

4.50e-20

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: 91.86 E-value: 4.50e-20

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1517 VYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIgCYMFRMDDFD-------VVDATMHGNAARFI 1589
Cdd:cd20073     97 IFKTKHKGWGLRCPRFIKAGTFIGVYLGEVITQSEAEIRGKKYDNVGV-TYLFDLDLFEdqvdeyyTVDAQYCGDVTRFI 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1590 NHSCEPNCFSRVIHVE-GQK---HIVIFALRRILRGEELTYDYKFPIED----------------ASNKLPCNCGAKRCR 1649
Cdd:cd20073    176 NHSCDPNLAIYSVLRDkSDSkiyDLAFFAIKDIPALEELTFDYSGRNNFdqlgfignrsnskyinLKNKRPCYCGSANCR 255


                   ...
gi 1907184719 1650 RFL 1652
Cdd:cd20073    256 GWL 258

PHD1_KMT2A

cd15588

PHD finger 1 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, ...

140-186

1.11e-19

PHD finger 1 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 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 first PHD finger.

Pssm-ID: 277063 Cd Length: 47 Bit Score: 83.85 E-value: 1.11e-19

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1907184719  140 VCLLCASKGLHELVFCQVCCDPFHPFCLEEAERPSPQHRDTWCCRRC 186
Cdd:cd15588      1 VCFLCASSGHVEFVYCQVCCEPFHKFCLEEAERPLEDQLENWCCRRC 47

SET_SETD5-like

cd10529

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

1525-1628

1.19e-19

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: 86.56 E-value: 1.19e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1525 RGLFCKRNIDAGEMVIEYSGIVirSVLTDKREKFYDGKGIGCYMFRMDDFD----VVDATMHGNAARFINHSCEPNCFSR 1600
Cdd:cd10529     17 KGLVATEDISPGEPILEYKGEV--SLRSEFKEDNGFFKRPSPFVFFYDGFEglplCVDARKYGNEARFIRRSCRPNAELR 94

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1907184719 1601 -VIHVEGQKHIVIFALRRILRGEELT--YDY 1628
Cdd:cd10529     95 hVVVSNGELRLFIFALKDIRKGTEITipFDY 125

ePHD_PHF6_like

cd15673

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

518-622

3.43e-19

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: 84.75 E-value: 3.43e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALClKYGDaDSKEAGRLLYIGQNEWTHVNCAIWSAEVFEENDGS--------LKNVHAAVARGRQMRCELCLKPGATVG 589
Cdd:cd15673      1 CGFC-KSGE-ENKETGGKLASGEKIAAHHNCMLFSSGLVQYVSPNendfggfdIEDVKKEIKRGRKLKCNLCKKTGATIG 78

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907184719  590 CCLSSCLSNFHFMCARASYCIFQDDK-----KVFCQKH 622
Cdd:cd15673     79 CDVKQCKKTYHYHCAKKDDAKIIERNsqgiyRVYCKNH 116

SET_NSD3

cd19212

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

1524-1652

7.27e-19

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: 84.59 E-value: 7.27e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1524 GRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKR-EKFYDGKGIGCYMFRMDDFDVVDATMHGNAARFINHSCEPNCFSRVI 1602
Cdd:cd19212     13 GWGLRTKRSIKKGEFVNEYVGELIDEEECRLRiKRAHENSVTNFYMLTVTKDRIIDAGPKGNYSRFMNHSCNPNCETQKW 92

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1603 HVEGQKHIVIFALRRILRGEELTYDYKFPIEdASNKLPCNCGAKRCRRFL 1652
Cdd:cd19212     93 TVNGDVRVGLFALCDIPAGMELTFNYNLDCL-GNGRTECHCGADNCSGFL 141

SET

cd08161

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...

1517-1628

7.81e-18

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: 79.22 E-value: 7.81e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1517 VYRSAI--HGRGLFCKRNIDAGEMVIEysgivirsvltdkrekfydgkgigcymfrmddfdvvdatmhgnaARFINHSCE 1594
Cdd:cd08161      2 IRPSTIpgAGFGLFATRDIPKGEVIGL--------------------------------------------ARFINHSCE 37

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1907184719 1595 PNCFSRVIHVEGQKHIVIFALRRILRGEELTYDY 1628
Cdd:cd08161     38 PNCEFEEVYVGGKPRVFIVALRDIKAGEELTVDY 71

SET_SUV39H2

cd10532

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

1505-1652

1.76e-17

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: 83.79 E-value: 1.76e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1505 RHLKKTSKEAVGVYRSAiHGRGLFCK--RNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIgCYMFRMD---DFDVVDA 1579
Cdd:cd10532     76 RVVQKGTQYSLCIFRTS-NGRGWGVKtlQKIKKNSFVMEYVGEVITSEEAERRGQFYDSKGI-TYLFDLDyesDEFTVDA 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1580 TMHGNAARFINHSCEPNCFSRVIHVEGQK----HIVIFALRRILRGEELTYDYKF------PIEDASN-------KLPCN 1642
Cdd:cd10532    154 ARYGNVSHFVNHSCDPNLQVFNVFIDNLDtrlpRIALFSTRTIKAGEELTFDYQMkgsgdlSSDSIDNspakkrvRTVCK 233

                          170
                   ....*....|
gi 1907184719 1643 CGAKRCRRFL 1652
Cdd:cd10532    234 CGAVTCRGYL 243

FYRN

pfam05964

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

670-717

7.02e-17

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: 76.00 E-value: 7.02e-17

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907184719  670 GSIRINSLGTL---SDLSDCEGRLFPIGYQCSRLYWSTVDARRRCWYRCRI 717
Cdd:pfam05964    1 GSLTVLSLGEIvpdRPAFHTERYIYPVGYKSTRLYWSTKDPRKRCRYTCEI 51

ePHD_RAI1_like

cd15668

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

543-622

7.36e-17

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: 77.73 E-value: 7.36e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  543 WTHVNCAIWSAEVFEENdGSLKNVHAAVARGRQMRCELCLKPGATVGCCLSSCLSNFHFMCARASYCIFQDDK-KVFCQK 621
Cdd:cd15668     24 WVHEDCAVWAPGVYLVG-GKLYGLEEAVWVAKQSVCSSCQQTGATIGCLHKGCKAKYHYPCAVESGCQLDEENfSLLCPK 102


                   .
gi 1907184719  622 H 622
Cdd:cd15668    103 H 103

ePHD1_KMT2C_like

cd15665

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

543-622

8.83e-17

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: 76.97 E-value: 8.83e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  543 WTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCELCLKPGATVGCCLSSCLSNFHFMCARASYCiFQDDKK--VFCQ 620
Cdd:cd15665     10 YAHHCCAAWSEGVCQTEDGALENVDKAVAKALSQKCSFCLRYGASISCRMPSCSKSFHFPCAAAAGC-FQDIKTltLFCP 88


                   ..
gi 1907184719  621 KH 622
Cdd:cd15665     89 EH 90

ePHD_PHF7_G2E3_like

cd15669

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

518-622

1.40e-16

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: 77.29 E-value: 1.40e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALCLKyGDADSKEAGRLLYIGqNEWTHVNCAIWSAEVF---EENDG----SLKNVHAAVARGRQMRCELCLKPGATVGC 590
Cdd:cd15669      1 CVLCGR-SDDDPDKYGEKLQKD-GICAHYFCLLFSSGLPqrgEDNEGiygfLPEDIRKEVRRASRLRCFYCKKKGASIGC 78

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1907184719  591 CLSSCLSNFHFMCARASYCIFQ--DDKKVFCQKH 622
Cdd:cd15669     79 AVKGCRRSFHFPCGLENGCVTQffGEYRSFCWEH 112

SET_EZH-like

cd19168

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

1513-1628

1.73e-16

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: 77.23 E-value: 1.73e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1513 EAVGVYRSAIH-GRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGiGCYMFRMDDFDVVDATMHGNAARFINH 1591
Cdd:cd19168      1 KAVVLGKSQLEcGLGLFAAEDIKEGEFVIEYTGELISHDEGVRREHRRGDVS-YLYLFEEQEGIWVDAAIYGNLSRYINH 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1907184719 1592 SCEP----NCFSRVIHVEGQKHIVIFALRRILRGEELTYDY 1628
Cdd:cd19168     80 ATDKvktgNCMPKIMYVNHEWRIKFTAIKDIKIGEELFFNY 120

zf-HC5HC2H

pfam13771

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

545-622

2.59e-16

Pssm-ID: 463977 [Multi-domain] Cd Length: 88 Bit Score: 75.44 E-value: 2.59e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  545 HVNCAIWSAEVFEENDGS----LKNVHAAVARGRQMRCELC-LKPGATVGCCLSSCLSNFHFMCARASYCIFQ-----DD 614
Cdd:pfam13771    1 HVVCALWSPELVQRGNDSmgfpIEDIEKIPKRRWKLKCYLCkKKGGACIQCSKKNCRRAFHVTCALEAGLLMQfdednGT 80


                   ....*...
gi 1907184719  615 KKVFCQKH 622
Cdd:pfam13771   81 FKSYCKKH 88

SET_SUV39H1

cd10525

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

1524-1652

7.18e-16

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: 79.17 E-value: 7.18e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1524 GRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIgCYMFRMD---DFDVVDATMHGNAARFINHSCEPNCfsR 1600
Cdd:cd10525     98 GWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGA-TYLFDLDyveDVYTVDAAYYGNISHFVNHSCDPNL--Q 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1601 VIHV------EGQKHIVIFALRRILRGEELTYDYKF---PIEDASNKL-------------------PCNCGAKRCRRFL 1652
Cdd:cd10525    175 VYNVfidnldERLPRIALFATRTIRAGEELTFDYNMqvdPVDAESTKMdsnfglaglpgspkkrvriECKCGVRSCRKYL 254

SET_SETDB1

cd10517

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

1517-1649

1.84e-15

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: 78.87 E-value: 1.84e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1517 VYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKR------------------EKFYDGKGIG----CYmfrmddf 1574
Cdd:cd10517    133 VFKTEKKGWGIRCLDDIPKGSFVCIYAGQILTEDEANEEglqygdeyfaeldyievvEKLKEGYESDveehCY------- 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1575 dVVDATMHGNAARFINHSCEPNCFSRVIHVEGQK----HIVIFALRRILRGEELTYDYKFPIEDASNK-LPCNCGAKRCR 1649
Cdd:cd10517    206 -IIDAKSEGNLGRYLNHSCSPNLFVQNVFVDTHDlrfpWVAFFASRYIRAGTELTWDYNYEVGSVPGKvLYCYCGSSNCR 284

SET_EHMT2

cd10533

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

1517-1649

2.94e-15

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: 76.98 E-value: 2.94e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1517 VYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKfydgkgiGCYMFRMDDFD----VVDATMHGNAARFINHS 1592
Cdd:cd10533     95 LYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRED-------DSYLFDLDNKDgevyCIDARYYGNISRFINHL 167

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907184719 1593 CEPNCFSRVIHVEGQK----HIVIFALRRILRGEELTYDYKFPIEDASNK-LPCNCGAKRCR 1649
Cdd:cd10533    168 CDPNIIPVRVFMLHQDlrfpRIAFFSSRDIRTGEELGFDYGDRFWDIKSKyFTCQCGSEKCK 229

SET_SUV39H_DIM5-like

cd19473

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

1524-1652

3.93e-15

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: 77.36 E-value: 3.93e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1524 GRGLFCKRNIDAGEMVIEYSGIVIRSVLTD-KREKFYDGKGIGCYMFRMDDF---DVVDATMHGNA-----------ARF 1588
Cdd:cd19473    117 GWGVRSTVDIKRGQFVDCYVGEIITPEEAQrRRDAATIAQRKDVYLFALDKFsdpDSLDPRLRGDPyeidgefmsgpTRF 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1589 INHSCEPN--CFSRVI-HVEgqKHI---VIFALRRILRGEELTYDY----------KFPIEDASNKLPCNCGAKRCRRFL 1652
Cdd:cd19473    197 INHSCDPNlrIFARVGdHAD--KHIhdlAFFAIKDIPRGTELTFDYvdgvtgldddAGDEEKEKEMTKCLCGSPKCRGYL 274

FYRN

smart00541

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

677-719

4.94e-15

Pssm-ID: 128814 Cd Length: 44 Bit Score: 70.39 E-value: 4.94e-15

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1907184719   677 LGTLSDLSDCEGRLFPIGYQCSRLYWSTVDARRRCWYRCRILE 719
Cdd:smart00541    2 LPIQGKLFHSESAIFPVGYKSTRKYWSVKDPNRRCLYSCVIDE 44

SET_SETDB

cd10541

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

1517-1649

4.95e-15

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: 76.43 E-value: 4.95e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1517 VYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKrEKFYDGKGigcYMFRMDDFD----VVDATMHGNAARFINHS 1592
Cdd:cd10541     96 LFKTQNKGWGIRCLDDIAKGTFVCIYAGKILTDDFADK-EGLEMGDE---YFANLDHIEescyIIDAKLEGNLGRYLNHS 171

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907184719 1593 CEPNCFSRVIHVEGQKH----IVIFALRRILRGEELTYDYKFPIEDASNK-LPCNCGAKRCR 1649
Cdd:cd10541    172 CSPNLFVQNVFVDTHDLrfpwVAFFASKRIKAGTELTWDYNYEVGSVEGKeLLCCCGSNECR 233

SET_EHMT1

cd10535

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

1517-1649

7.50e-15

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: 75.74 E-value: 7.50e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1517 VYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKfydgkgiGCYMFRMDDFD----VVDATMHGNAARFINHS 1592
Cdd:cd10535     95 LYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREE-------DSYLFDLDNKDgevyCIDARFYGNVSRFINHH 167

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907184719 1593 CEPNCFSRVIHVEGQK----HIVIFALRRILRGEELTYDYKFPIEDASNKL-PCNCGAKRCR 1649
Cdd:cd10535    168 CEPNLVPVRVFMAHQDlrfpRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLfSCRCGSPKCR 229

SET_EHMT

cd10543

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

1517-1649

9.42e-15

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: 75.45 E-value: 9.42e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1517 VYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKfydgkgiGCYMFRMDDFDV----VDATMHGNAARFINHS 1592
Cdd:cd10543     95 LFRTRGMGWGVRALQDIPKGTFVCEYIGELISDSEADSRED-------DSYLFDLDNKDGetycIDARRYGNISRFINHL 167

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907184719 1593 CEPNCFSRVIHVEGQK----HIVIFALRRILRGEELTYDY--KF-PIEdaSNKLPCNCGAKRCR 1649
Cdd:cd10543    168 CEPNLIPVRVFVEHQDlrfpRIAFFASRDIKAGEELGFDYgeKFwRIK--GKYFTCRCGSPKCK 229

ePHD_PHF11

cd15712

Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain ...

518-622

1.27e-13

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: 68.77 E-value: 1.27e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALCLKygdadsKEAGRLLYIG--QNEWTHVNCAIWSAEVFEENDGSLKN---------VHAAVARGRQMRCELCLKPGA 586
Cdd:cd15712      1 CAFCPK------GEEYSIMYFAqeQNIAAHQNCLLYSSGFVESEEYNPLNldrrfdvesVLNEIKRGKRLKCNFCRKKGA 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1907184719  587 TVGCCLSSCLSNFHFMCARASYCIFQDDK-----KVFCQKH 622
Cdd:cd15712     75 TVGCEERACRRSYHYFCALCDDAAIETDEvrgiyRVFCQKH 115

SET_SMYD

cd20071

SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...

1523-1628

4.50e-13

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: 67.40 E-value: 4.50e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1523 HGRGLFCKRNIDAGEMVIEYSGIVirSVLTDKREKFYDGKGIGCYMFRMddfdvvdatmhgnaARFINHSCEPNCfsrVI 1602
Cdd:cd20071      9 KGRGLVATRDIEPGELILVEKPLV--SVPSNSFSLTDGLNEIGVGLFPL--------------ASLLNHSCDPNA---VV 69

                           90       100
                   ....*....|....*....|....*.
gi 1907184719 1603 HVEGQKHIVIFALRRILRGEELTYDY 1628
Cdd:cd20071     70 VFDGNGTLRVRALRDIKAGEELTISY 95

SET_SETDB2

cd10523

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

1517-1652

4.67e-13

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: 71.40 E-value: 4.67e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1517 VYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLT--------------DKREKFYDGKGIGCYMFRMDDFDVVDATMH 1582
Cdd:cd10523    112 VFKTEKKGWGVRCLDDIDKGTFVCIYAGRVLSRARSpteplppklelpseNEVEVVTSWLILSKKRKLRENVCFLDASKE 191

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907184719 1583 GNAARFINHSCEPNCFSRVIHVEGQKH----IVIFALRRILRGEELTYDYKFPIEDASNK-LPCNCGAKRCRRFL 1652
Cdd:cd10523    192 GNVGRFLNHSCCPNLFVQNVFVDTHDKnfpwVAFFTNRVVKAGTELTWDYSYDAGTSPEQeIPCLCGVNKCQKKI 266

SET_AtSUVH-like

cd10545

SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...

1517-1628

2.39e-12

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: 68.58 E-value: 2.39e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1517 VYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREK----------FYDGKGIGCYMFRMDDFD----------- 1575
Cdd:cd10545     90 VFKTAERGWGVRSWDSIPAGSFICEYVGELLDTSEADTRSGnddylfdidnRQTNRGWDGGQRLDVGMSdgerssaedee 169

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907184719 1576 ----VVDATMHGNAARFINHSCEPNCFSRVIHVEGQK----HIVIFALRRILRGEELTYDY 1628
Cdd:cd10545    170 ssefTIDAGSFGNVARFINHSCSPNLFVQCVLYDHNDlrlpRVMLFAADNIPPLQELTYDY 230

ePHD_RAI1

cd15700

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

518-622

8.01e-12

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: 63.36 E-value: 8.01e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALCLKygDADSKEAGRLL--YIGQNeWTHVNCAIWSAEVFEENdGSLKNVHAAVARGRQMRCELCLKPGATVGCCLSSC 595
Cdd:cd15700      1 CCLCRN--PANYKDLGDLCgpYYPEH-WVHEACAVWTTGVYLVA-GKLFGLQEAVQKAADAKCSSCQGAGATVGCCHKGC 76

                           90       100
                   ....*....|....*....|....*...
gi 1907184719  596 LSNFHFMCARASYCIFQDDK-KVFCQKH 622
Cdd:cd15700     77 TQSYHYICAVEAGCLFEEENfSLRCPKH 104

ePHD_TCF20

cd15699

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

518-622

1.80e-11

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: 62.24 E-value: 1.80e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALCLKYgdADSKEAGRLLYIGQNEWTHVNCAIWSAEVFEENdGSLKNVHAAVARGRQMRCELCLKPGATVGCCLSSCLS 597
Cdd:cd15699      1 CCLCGKW--ANYRNLGDLFGPFYEFWVHEGCILWANGIYLVC-GRLYGLQEALDIAREMKCSHCQEAGATLGCYNKGCSF 77

                           90       100
                   ....*....|....*....|....*.
gi 1907184719  598 NFHFMCARASYCIFQDDK-KVFCQKH 622
Cdd:cd15699     78 RYHYPCAIDADCLLNEENfSVRCPKH 103

SET_SpSET3-like

cd19183

SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...

1526-1632

4.07e-10

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: 60.49 E-value: 4.07e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1526 GLFCKRNIDAGEMVIEYSGIVIR--SVLTDKREKFYDGKGIGCYMFRMDDFD-VVDATMHGNAARFINHSCEPNC--FSR 1600
Cdd:cd19183     15 GLFADRPIPAGDPIQELLGEIGLqsEYIADPENQYQILGAPKPHVFFHPQSPlYIDTRRSGSVARFIRRSCRPNAelVTV 94

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1907184719 1601 VIHVEGQKHIVIFALRRILRGEELTYDYKFPI 1632
Cdd:cd19183     95 ASDSGSVLKFVLYASRDISPGEEITIGWDWDN 126

ePHD1_KMT2D

cd15695

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

543-622

4.31e-10

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: 58.00 E-value: 4.31e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  543 WTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCELCLKPGATVGCCLSSCLSNFHFMCARASYCiFQDDK--KVFCQ 620
Cdd:cd15695     10 WVHHWCAAWSAGVKQHEGDGLIGVDKAVFSGISQKCEHCKRLGATIQCHAEGCPRFYHFPCAAASGS-FQSMKtlLLLCP 88


                   ..
gi 1907184719  621 KH 622
Cdd:cd15695     89 EH 90

ePHD1_PHF6

cd15710

Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...

518-622

5.66e-10

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: 58.43 E-value: 5.66e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALCLKYGDadsKEAGRLLyIGQNE--WTHVNCAIWSAEVF-----EENDG--SLKNVHAAVARGRQMRCELCLKPGATV 588
Cdd:cd15710      1 CGFCRSNRE---KECGQLL-ISENQkvAAHHKCMLFSSALVsshsdSENLGgfSIEDVQKEIKRGTKLMCSLCHCPGATI 76

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907184719  589 GCCLSSCLSNFHFMCARASYCIFQDDKK-----VFCQKH 622
Cdd:cd15710     77 GCDVKTCHRTYHYYCALHDKAQIRENPSqgiymIYCRKH 115

ePHD2_PHF6

cd15711

Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...

518-622

1.06e-09

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: 57.79 E-value: 1.06e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALClKYGDADSKEAGRL-LYIGQNEWTHVNCAIWSAEVF--------EENDGSLKNVHAAVARGRQMRCELCLKPGATV 588
Cdd:cd15711      1 CGFC-HAGEEENETRGKLhIFNAKKAAAHYKCMLFSSGTVqltttsraEFGDFDIKTVIQEIKRGKRMKCTLCSQLGATI 79

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907184719  589 GCCLSSCLSNFHFMCA---RASYC--IFQDDKKVFCQKH 622
Cdd:cd15711     80 GCEIKACVKTYHYHCGvqdKAKYIenMSRGIYKLYCKNH 118

ePHD1_KMT2C

cd15696

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

543-622

1.61e-09

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: 56.49 E-value: 1.61e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  543 WTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCELCLKPGATVGCCLSSCLSNFHFMCArASYCIFQDDKKVF--CQ 620
Cdd:cd15696     10 WAHLRCAEWSLGVCQGEEQLLVNVDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCA-AGAGTFQDFSRRLllCP 88


                   ..
gi 1907184719  621 KH 622
Cdd:cd15696     89 TH 90

PHD

pfam00628

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

140-189

2.99e-09

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 54.42 E-value: 2.99e-09

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907184719  140 VCLLCASKGLH-ELVFCQVCCDPFHPFCLEEAERPSPQHRDTWCCRRCKFC 189
Cdd:pfam00628    1 YCAVCGKSDDGgELVQCDGCDDWFHLACLGPPLDPAEIPSGEWLCPECKPK 51

PHD6_KMT2C_like

cd15514

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

274-330

6.71e-09

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: 53.06 E-value: 6.71e-09

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907184719  274 YCPICTRCYEDNDyesKMMQCAQCDHWVHAKCEGL-SDEDYEILsglpDSVLYTCGPC 330
Cdd:cd15514      1 KCPVCSRSYNEGE---LIIQCSQCERWLHGACDSLrTEEEAERA----ADNGYRCLLC 51

zf-HC5HC2H_2

pfam13832

PHD-zinc-finger like domain;

516-622

1.08e-08

PHD-zinc-finger like domain;

Pssm-ID: 463991 [Multi-domain] Cd Length: 109 Bit Score: 54.66 E-value: 1.08e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  516 RQCALCLKYGDAdskeagrLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNV---HAAVARGRQmRCELCLKP-GATVGCC 591
Cdd:pfam13832    1 VRCCLCPLRGGA-------LKQTSDGRWVHVLCAIFVPEVRFGNVATMEPIdvsRIPPERWKL-KCVFCKKRsGACIQCS 72

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907184719  592 LSSCLSNFHFMCARAS------YCIFQDDKKVFCQKH 622
Cdd:pfam13832   73 KGRCTTAFHVTCAQAAgvymepEDWPNVVVIAYCQKH 109

PHD_SF

cd15489

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

188-237

1.49e-08

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) finger typically characterized as Cys4HisCys3, and a non-canonical extended PHD finger, characterized as Cys2HisCys5HisCys2His. Variations include the RAG2 PHD finger characterized by Cys3His2Cys2His and the PHD finger 5 found in nuclear receptor-binding SET domain-containing proteins characterized by Cys4HisCys2His. The PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. Single or multiple copies of PHD fingers have been found in a variety of eukaryotic proteins involved in the control of gene transcription and chromatin dynamics. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. They also function as epigenome readers controlling gene expression through molecular recruitment of multi-protein complexes of chromatin regulators and transcription factors. The PHD finger domain SF is structurally similar to the RING and FYVE_like superfamilies.

Pssm-ID: 276966 [Multi-domain] Cd Length: 48 Bit Score: 52.32 E-value: 1.49e-08

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907184719  188 FCHVCGRKGRGSKHLLECERCRHAYHPACLGPSYPTraTRRRRHWICSAC 237
Cdd:cd15489      1 SCIVCGKGGDLGGELLQCDGCGKWFHADCLGPPLSS--FVPNGKWICPVC 48

PHD

pfam00628

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

274-330

1.71e-08

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 52.11 E-value: 1.71e-08

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907184719  274 YCPICTRcyedNDYESKMMQCAQCDHWVHAKCEGLSDEDYEILSGlpdsvLYTCGPC 330
Cdd:pfam00628    1 YCAVCGK----SDDGGELVQCDGCDDWFHLACLGPPLDPAEIPSG-----EWLCPEC 48

SET_SpSet7-like

cd10540

SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...

1524-1628

1.84e-08

SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces pombe Set7 is a novel histone-lysine N-methyltransferase. The family also includes a viral histone H3 lysine 27 methyltransferase from Paramecium bursaria Chlorella virus 1 (PBCV-1).

Pssm-ID: 380938 Cd Length: 112 Bit Score: 53.80 E-value: 1.84e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1524 GRGLFCKRNIDAGEmVIEYSGIVirsVLTDKREKFYDGKGIGCYMFRmddfdvVDATMHGNAARF---INHSCEPNCfSR 1600
Cdd:cd10540     11 GRGVFATRPIKKGE-VIEEAPVI---VLPKEEYQHLCKTVLDHYVFS------WGDGCLALALGYgsmFNHSYTPNA-EY 79

                           90       100
                   ....*....|....*....|....*...
gi 1907184719 1601 VIHVEGQKhIVIFALRRILRGEELTYDY 1628
Cdd:cd10540     80 EIDFENQT-IVFYALRDIEAGEELTINY 106

SET_SETD5

cd19181

SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...

1517-1648

2.38e-08

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: 54.63 E-value: 2.38e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1517 VYRSAIHGRGLFCKRNIDAGEMVIEYSG-IVIRSVLTDKREKFYDGKGIGCYMFRMDDFDV-VDATMHGNAARFINHSCE 1594
Cdd:cd19181     11 VTRVQKHRKILRAARDLALDTLIIEYRGkVMLRQQFEVNGHFFKRPYPFVLFYSKFNGVEMcVDARTFGNDARFIRRSCT 90

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907184719 1595 PNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEDASNKLPCNC--GAKRC 1648
Cdd:cd19181     91 PNAEVRHMIADGMIHLCIYAVAAIAKDAEVTIAFDYEYSNCNYKVDCAChkGNRNC 146

PHD

pfam00628

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

188-240

4.73e-08

Pssm-ID: 425785 [Multi-domain] Cd Length: 51 Bit Score: 50.95 E-value: 4.73e-08

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907184719  188 FCHVCGRKGRGSKhLLECERCRHAYHPACLGPSyPTRATRRRRHWICSACVRC 240
Cdd:pfam00628    1 YCAVCGKSDDGGE-LVQCDGCDDWFHLACLGPP-LDPAEIPSGEWLCPECKPK 51

PHD

smart00249

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

188-237

5.29e-08

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 50.67 E-value: 5.29e-08

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1907184719   188 FCHVCGRKGRGSKhLLECERCRHAYHPACLGPSYPTRATrrRRHWICSAC 237
Cdd:smart00249    1 YCSVCGKPDDGGE-LLQCDGCDRWYHQTCLGPPLLEEEP--DGKWYCPKC 47

ePHD_JADE

cd15671

Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended ...

518-622

1.69e-07

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: 51.29 E-value: 1.69e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALCLKYGDA-DSKEAGRllyigqnEWTHVNCAIWSAEVFEENDGSLKNV----HAAVARgRQMRCELC-LKPGATVGCC 591
Cdd:cd15671      1 CVLCPKKGGAmKSTKSGT-------KWVHVSCALWIPEVSIGCPEKMEPItkisHIPMSR-WALVCVLCkEKTGACIQCS 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1907184719  592 LSSCLSNFHFMCA-----RASYCIFQDDKKV----FCQKH 622
Cdd:cd15671     73 VKSCKTAFHVTCAfqhglEMKTILEDEDDEVkfksYCPKH 112

SET_Suv4-20-like

cd10524

SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...

1523-1628

1.90e-07

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: 51.90 E-value: 1.90e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1523 HGRGLFCKRNIDAGEMVIEYSGIVirSVLTDKREKFYDGKGigcymfrmDDFDVVDATMHGNA------ARFINHSCEPN 1596
Cdd:cd10524     18 YGAKIIATKPIKKGEKIHELCGCI--AELSEEEEALLRPGG--------NDFSVMYSSRKKCSqlwlgpAAFINHDCRPN 87

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1907184719 1597 CfsRVIHVeGQKHIVIFALRRILRGEELTYDY 1628
Cdd:cd10524     88 C--KFVPT-GKSTACVKVLRDIEPGEEITVYY 116

SET_KMT2E

cd19182

SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...

1577-1630

3.55e-07

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: 50.66 E-value: 3.55e-07

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907184719 1577 VDATMHGNAARFINHSCEPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKF 1630
Cdd:cd19182     73 VDARTFGNEARFIRRSCTPNAEVRHVIEDGTIHLYIYSIRSIPKGTEITIAFDF 126

ePHD_JADE3

cd15706

Extended PHD finger found in protein Jade-3 and similar proteins; The extended plant ...

518-604

5.82e-07

Extended PHD finger found in protein Jade-3 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-3. Jade-3, also termed PHD finger protein 16 (PHF16), is a plant homeodomain (PHD) zinc finger protein that is close related to Jade-1, which functions as an essential regulator of multiple cell signaling pathways. Like Jade-1, Jade-3 is required for ING4 and ING5 to associate with histone acetyl transferase (HAT) HBO1 and Eaf6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. Jade-3 contains a canonical PHD domain followed by this non-canonical ePHD domain, both of which are zinc-binding motifs.

Pssm-ID: 277176 Cd Length: 111 Bit Score: 49.72 E-value: 5.82e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALCLKYGDA-DSKEAGrllyigqNEWTHVNCAIWSAEVF----EENDGSLKNVHAAVARGrQMRCELC-LKPGATVGCC 591
Cdd:cd15706      1 CLLCPKTGGAmKATRTG-------TKWAHVSCALWIPEVSiacpERMEPITKVSHIPPSRW-ALVCSLCkLKTGACIQCS 72

                           90
                   ....*....|...
gi 1907184719  592 LSSCLSNFHFMCA 604
Cdd:cd15706     73 VKSCITAFHVTCA 85

PHA03247

large tegument protein UL36; Provisional

729-1153

2.27e-06

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.02 E-value: 2.27e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  729 PVHLEAAEENQTIVHSPTP---SSEPPNHDDLPDTDSLIP--------GDPVHH---SPIQNLDPpLRTDSSNGP----P 790
Cdd:PHA03247  2478 PVYRRPAEARFPFAAGAAPdpgGGGPPDPDAPPAPSRLAPailpdepvGEPVHPrmlTWIRGLEE-LASDDAGDPppplP 2556

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  791 PTPRSFSGARiKVPNYSPSRRPLGGVSFGPLPSPGSPSSLTHHIPTVGDSDFPAPPRRSRRPSPLATRPPPSRRTSSPLR 870
Cdd:PHA03247  2557 PAAPPAAPDR-SVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAA 2635

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  871 TSPQLRVPLSTSVTAL---TPTSGELAPPDLAPSPLPPSEDLGPDFEDMEVVSGLSAADLDFAASLLGTEPFQEEIVAAg 947
Cdd:PHA03247  2636 NEPDPHPPPTVPPPERprdDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHA- 2714

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  948 AVGSSQGGPGDSSEEEASPTTHYVHFPVTVVSGPALaPSSLAGAPRIEQLDGVDDGTDSEAEAVQQPRGQGTPPSGPGVG 1027
Cdd:PHA03247  2715 LVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAT-PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSE 2793

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1028 RGGVLGAAGDRAQPPEDLPSeivdfvlknlggPGEGAAGPREDSLPSAPPLANGSQPPQSLSTSPADPTRTFAWLpgAPG 1107
Cdd:PHA03247  2794 SRESLPSPWDPADPPAAVLA------------PAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSV--APG 2859

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1907184719 1108 VRVLSLGPA-PEPPKPATSKIILVNKLGQVFVKMAGEGEPVAPPVKQ 1153
Cdd:PHA03247  2860 GDVRRRPPSrSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPE 2906

PHD6_KMT2C

cd15600

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

275-312

2.55e-06

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: 46.08 E-value: 2.55e-06

                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1907184719  275 CPICTRCYEDndyESKMMQCAQCDHWVHAKCEGLSDED 312
Cdd:cd15600      2 CPICYRNYRE---EELILQCRQCDRWMHASCQNLNTEE 36

PHA03307

transcriptional regulator ICP4; Provisional

722-1124

4.49e-06

transcriptional regulator ICP4; Provisional

Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 51.71 E-value: 4.49e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  722 PWGPREEPVHLEAAEENQT--IVHSPTPSSEPPNHDDLPDTDSLIPGDPvhhspiqnldpPLRTDSSNGPPPTPrsfsga 799
Cdd:PHA03307    68 PTGPPPGPGTEAPANESRStpTWSLSTLAPASPAREGSPTPPGPSSPDP-----------PPPTPPPASPPPSP------ 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  800 rikVPNYSPSRRPLGGVSfgplpspgspsslthhiPTVGDSDFPAPPRRSRRPSPLATRPPPSRRTSSPLRT-----SPQ 874
Cdd:PHA03307   131 ---APDLSEMLRPVGSPG-----------------PPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETarapsSPP 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  875 LRVPLSTSVTALTPTSGELAPPDLAPSPLPP-----SEDLGPDFEDMevvSGLSAADLDFAASLLGTEPFQEEIVAAGAV 949
Cdd:PHA03307   191 AEPPPSTPPAAASPRPPRRSSPISASASSPApapgrSAADDAGASSS---DSSSSESSGCGWGPENECPLPRPAPITLPT 267

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  950 GSSQGGPGDSSEEEASPTTHYVHFPvtvVSGPALAPSSLAGAPRIEQLDGVDDGTDSEAEAVQQPRGQGTPPSGPGVGRG 1029
Cdd:PHA03307   268 RIWEASGWNGPSSRPGPASSSSSPR---ERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPG 344

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1030 GVLGAAGDRAQPPEDLPSeivdfvlknlggpgegaagpreDSLPSAPPlanGSQPPQSLSTSPADPT-RTFAWLPGAPGV 1108
Cdd:PHA03307   345 PSPSRSPSPSRPPPPADP----------------------SSPRKRPR---PSRAPSSPAASAGRPTrRRARAAVAGRAR 399

                          410
                   ....*....|....*.
gi 1907184719 1109 RVLSLGPAPEPPKPAT 1124
Cdd:PHA03307   400 RRDATGRFPAGRPRPS 415

PHD

smart00249

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

140-186

6.15e-06

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 44.90 E-value: 6.15e-06

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1907184719   140 VCLLCASK-GLHELVFCQVCCDPFHPFCLEEAERPSPQhRDTWCCRRC 186
Cdd:smart00249    1 YCSVCGKPdDGGELLQCDGCDRWYHQTCLGPPLLEEEP-DGKWYCPKC 47

PHD

smart00249

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

274-330

1.53e-05

Pssm-ID: 214584 [Multi-domain] Cd Length: 47 Bit Score: 43.74 E-value: 1.53e-05

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907184719   274 YCPICTRCYEDNDyeskMMQCAQCDHWVHAKCEGLSDEDYeilsglPDSVLYTCGPC 330
Cdd:smart00249    1 YCSVCGKPDDGGE----LLQCDGCDRWYHQTCLGPPLLEE------EPDGKWYCPKC 47

ePHD_BRPF

cd15670

Extended PHD finger found in BRPF proteins; The extended plant homeodomain (ePHD) zinc finger ...

541-622

1.61e-05

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: 45.79 E-value: 1.61e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  541 NEWTHVNCAIWSAEVFEENDGSLK---NVHAAVARGRQMRCELC-LKPGATVGCCLSSCLSNFHFMCAR----------- 605
Cdd:cd15670     17 GRWAHVVCALWIPEVSFANTVFLEpidGIQNIPKARWKLTCYICkKRMGACIQCHKKNCYTAFHVTCAQqaglymkiepv 96

                           90       100
                   ....*....|....*....|
gi 1907184719  606 -ASYCIFQDD--KKVFCQKH 622
Cdd:cd15670     97 kDPGNGTSDSvrKEAYCDKH 116

SET_SETD7

cd10530

SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins; SETD7 (EC 2. ...

1513-1628

2.18e-05

SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins; SETD7 (EC 2.1.1.43; also termed histone H3-K4 methyltransferase SETD7, H3-K4-HMTase SETD7, lysine N-methyltransferase 7 (KMT7) or SET7/9) is a histone-lysine N-methyltransferase that specifically monomethylates 'Lys-4' of histone H3. It plays a central role in the transcriptional activation of genes such as collagenase or insulin. Set7/9 also methylates non-histone proteins, including estrogen receptor alpha (ERa), suggesting it has a role in diverse biological processes. ERa methylation by Set7/9 stabilizes ERa and activates its transcriptional activities, which are involved in the carcinogenesis of breast cancer. In a high-throughput screen, treatment of human breast cancer cells (MCF7 cells) with cyproheptadine, a Set7/9 inhibitor, decreased the expression and transcriptional activity of ERa, thereby inhibiting estrogen-dependent cell growth.

Pssm-ID: 380928 Cd Length: 130 Bit Score: 45.75 E-value: 2.18e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1513 EAVGVYRSAIH--GRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIGcymfrMDDFDVVDATMHGNAARF-- 1588
Cdd:cd10530      7 ERVYVAESLIPsaGEGLFAKVAVGPNTVMSFYNGVRITHQEVDSRDWSLNGNTIS-----LDEETVIDVPEPYNSVSKyc 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1907184719 1589 ------INHSCEPNC-FSRVIHVEGQKHIVIFALRRILRGEELTYDY 1628
Cdd:cd10530     82 aslghkANHSFTPNCiYDPFVHPRFGPIKCIRTLRAVEAGEELTVAY 128

PHD3_KMT2D

cd15597

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

189-238

2.74e-05

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: 43.10 E-value: 2.74e-05

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907184719  189 CHVCGRKGRGSK-HLLECERCRHAYHPACLGPSypTRATRRRRHWICSACV 238
Cdd:cd15597      3 CVVCGSFGRGSEgHLLACSQCSQCYHPYCVNSK--ITKVMLLKGWRCVECI 51

SET_SMYD4

cd10536

SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...

1588-1628

3.44e-05

SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing protein 4 (SMYD4) and similar proteins; 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. In zebrafish, SMYD4 is ubiquitously expressed in early embryos and becomes enriched in the developing heart; mutants show a strong defect in cardiomyocyte proliferation, which lead to a severe cardiac malformation.

Pssm-ID: 380934 [Multi-domain] Cd Length: 218 Bit Score: 46.91 E-value: 3.44e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1907184719 1588 FINHSCEPNCFSrviHVEGQKhIVIFALRRILRGEELTYDY 1628
Cdd:cd10536    153 LLNHSCDPNTIR---SFYGNT-IVVRATRPIKKGEEITICY 189

PHD_SF

cd15489

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

274-330

4.94e-05

Pssm-ID: 276966 [Multi-domain] Cd Length: 48 Bit Score: 42.30 E-value: 4.94e-05

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907184719  274 YCPICTRCYEDNDyesKMMQCAQCDHWVHAKCEGLSDEDYeilsglPDSVLYTCGPC 330
Cdd:cd15489      1 SCIVCGKGGDLGG---ELLQCDGCGKWFHADCLGPPLSSF------VPNGKWICPVC 48

ePHD_JADE2

cd15705

Extended PHD finger found in protein Jade-2 and similar proteins; The extended plant ...

518-622

5.85e-05

Extended PHD finger found in protein Jade-2 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Jade-2. Jade-2, also termed PHD finger protein 15 (PHF15), is a plant homeodomain (PHD) zinc finger protein that is closely related to Jade-1, which functions as an essential regulator of multiple cell signaling pathways. Like Jade-1, Jade-2 is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and Eaf6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. Jade-2 contains a canonical PHD finger followed by this non-canonical ePHD finger, both of which are zinc-binding motifs.

Pssm-ID: 277175 Cd Length: 111 Bit Score: 43.93 E-value: 5.85e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALCLKYGDA-DSKEAGrllyigqNEWTHVNCAIWSAEVF----EENDGSLKNVHAAVARGrQMRCELCLK-PGATVGCC 591
Cdd:cd15705      1 CLLCPKRGGAlKPTRSG-------TKWVHVSCALWIPEVSigcpEKMEPITKISHIPASRW-ALSCSLCKEcTGTCIQCS 72

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907184719  592 LSSCLSNFHFMCA----RASYCIFQDDKKV----FCQKH 622
Cdd:cd15705     73 MPSCITAFHVTCAfdhgLEMRTTLADNDEVkfksFCLEH 111

PHD1_KMT2C_like

cd15509

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

141-186

6.00e-05

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: 41.91 E-value: 6.00e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1907184719  141 CLLCASKG-LHELVFCQVCCDPFHPFCLEEAERPSPQHRDTWCCRRC 186
Cdd:cd15509      2 CAVCDSPGdLSDLLFCTSCGQHYHGSCLDPAVRPTPLVRAGWQCPEC 48

PHD5_KMT2D

cd15601

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

275-312

1.29e-04

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: 41.04 E-value: 1.29e-04

                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1907184719  275 CPICTRCYEDNDYeskMMQCAQCDHWVHAKCEGLSDED 312
Cdd:cd15601      2 CPVCRAKYVEEDL---LIQCRHCDRWVHAVCESLFTED 36

ePHD_BRPF3

cd15703

Extended PHD finger found in bromodomain and PHD finger-containing protein 3 (BRPF3) and ...

518-622

1.48e-04

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: 43.12 E-value: 1.48e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALCLKYGDADSKEAgrllyigQNEWTHVNCAIWSAE------VFEENDGSLKNVHAAVARgrqMRCELCLKP--GATVG 589
Cdd:cd15703      1 CVLCPNKGGAFKQTS-------DGRWAHVVCAIWIPEvcfantVFLEPVEGVNNIPPARWK---LTCYLCKQKgrGAAIQ 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1907184719  590 CCLSSCLSNFHFMCA-RASY--------------CIFQDDKKVFCQKH 622
Cdd:cd15703     71 CHKVNCYTAFHVTCAqRAGLfmkiepvretglngTTFTVRKTAYCENH 118

PHD_ARID4_like

cd15615

PHD finger found in Arabidopsis thaliana AT-rich interactive domain-containing protein 4 ...

274-330

2.33e-04

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: 40.54 E-value: 2.33e-04

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907184719  274 YCPICTRCYEDNDYESK-MMQCAQCDHWVHAKCEGLSDEDYEILSgLPDSVLYTCGPC 330
Cdd:cd15615      1 FCILCGQVYEENEGDEKeWVQCDSCSEWVHFECDGRTGLGAFKYA-KSDGLQYVCPRC 57

PHD_TCF19_like

cd15517

PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ...

275-330

2.46e-04

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: 40.22 E-value: 2.46e-04

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907184719  275 CPICTRCYEDNDyeSKMMQCAQCDHWVHAKCEGLSDEDYEILSglpdsvLYTCGPC 330
Cdd:cd15517      2 CGICNLETAAVD--ELWVQCDGCDKWFHQFCLGLSNERYADED------KFKCPNC 49

SET_ATXR5_6-like

cd10539

SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The ...

1531-1634

3.28e-04

SET domain found in fungal protein lysine methyltransferase SET5 and similar protein; The family includes Arabidopsis thaliana ATXR5 and ATXR6. Both ATXR5 (also termed protein SET DOMAIN GROUP 15, or TRX-related protein 5) and ATXR6 (also termed protein SET DOMAIN GROUP 34, or TRX-related protein 6) function as histone methyltransferase that specifically monomethylates 'Lys-37' of histone H3 (H3K27me1). They are required for chromatin structure and gene silencing.

Pssm-ID: 380937 Cd Length: 138 Bit Score: 42.40 E-value: 3.28e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719 1531 RNIDAGEMVIEYSGivirSVLTDKREKFYDGKGIGCYMFRMDDFD--VVDATMHGNAARFI----NHSCE----PNCFSR 1600
Cdd:cd10539     22 GFIKDLTIIAEYTG----DVDYIRNREFDDNDSIMTLLLAGDPSKslVICPDKRGNIARFIsginNHTKDgkkkQNCKCV 97

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907184719 1601 VIHVEGQKHIVIFALRRILRGEELTYDY-----KFPIED 1634
Cdd:cd10539     98 RYSINGEARVLLVATRDIAKGERLYYDYngyehEYPTEH 136

ePHD_BRPF1

cd15701

Extended PHD finger found in bromodomain and PHD finger-containing protein 1 (BRPF1) and ...

518-607

4.89e-04

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

Pssm-ID: 277171 [Multi-domain] Cd Length: 121 Bit Score: 41.60 E-value: 4.89e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALCLKYGDA-DSKEAGRllyigqneWTHVNCAIWSAEVFEENDGSLKNV----HAAVARGRqMRCELCLK--PGATVGC 590
Cdd:cd15701      1 CALCPNKGGAfKQTDDGR--------WAHVVCALWIPEVCFANTVFLEPIdsieHIPPARWK-LTCYICKQrgSGACIQC 71

                           90
                   ....*....|....*..
gi 1907184719  591 CLSSCLSNFHFMCARAS 607
Cdd:cd15701     72 HKANCYTAFHVTCAQQA 88

PHD3_NSD

cd15566

PHD finger 3 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...

188-236

5.40e-04

PHD finger 3 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 third PHD finger.

Pssm-ID: 277041 Cd Length: 48 Bit Score: 39.33 E-value: 5.40e-04

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907184719  188 FCHVCGRKGRGSKH-LLECERCRHAYHPACLGPSYPTRATRRrrhWICSA 236
Cdd:cd15566      1 TCATCEASGDGSSGkLVRCIRCPRAYHAGCIPAGSKLLNKKL---IICPK 47

COG5141

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

541-625

5.45e-04

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

Pssm-ID: 227470 [Multi-domain] Cd Length: 669 Bit Score: 44.59 E-value: 5.45e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  541 NEWTHVNCAIWSAEVFEENDGSLKNVH--AAVARGR-QMRCELC-LKPGATVGCCLSSCLSNFHFMCAR----------- 605
Cdd:COG5141    266 GRWGHVICAMFNPELSFGHLLSKDPIDniASVSSSRwKLGCLICkEFGGTCIQCSYFNCTRAYHVTCARragyfdlniys 345

                           90       100
                   ....*....|....*....|...
gi 1907184719  606 ---ASYCIfqdDKKVFCQKHTDL 625
Cdd:COG5141    346 hngISYCI---DHEPLCRKHYPL 365

PHD_UHRF1_2

cd15525

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

189-237

9.54e-04

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: 38.50 E-value: 9.54e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1907184719  189 CHVCGRKGRGSKHLLeCERCRHAYHPACLGPsyPTRATRRRRHWICSAC 237
Cdd:cd15525      2 CHVCGGKQDPEKQLL-CDECDMAYHLYCLDP--PLTSLPDDDEWYCPDC 47

SET_SMYD3

cd19203

SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 ...

1590-1648

9.77e-04

SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 (SMYD3) and similar proteins; 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. It is overexpressed in colorectal, breast, prostate, and hepatocellular tumors, and has been implicated as an oncogene in human malignancies. Methylation of MEKK2 by SMYD3 is important for regulation of the MEK/ERK pathway, suggesting the possibility of selectively targeting SMYD3 in RAS-driven cancers.

Pssm-ID: 380980 [Multi-domain] Cd Length: 210 Bit Score: 42.35 E-value: 9.77e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907184719 1590 NHSCEPNCfsrVIHVEGqKHIVIFALRRILRGEELTYDY---KFPIEDASNKL------PCNCgaKRC 1648
Cdd:cd19203    147 NHSCDPNC---VIVFNG-PHLLLRAIREIEVGEELTISYidmLMPSEERRKQLrdqycfECDC--FRC 208

PHD1_Rco1

cd15535

PHD finger 1 found in Saccharomyces cerevisiae transcriptional regulatory protein Rco1 and ...

188-237

1.05e-03

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: 38.55 E-value: 1.05e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907184719  188 FCHVCGRKGrgskHLLECERCRHAYHPACLGPSYpTRATRRRRHWICSAC 237
Cdd:cd15535      1 FCSACGGYG----SFLCCDGCPRSFHFSCLDPPL-EEDNLPDDEWFCNEC 45

ePHD_JMJD2

cd15675

Extended PHD finger found in Jumonji domain-containing protein 2 (JMJD2) family of histone ...

518-622

1.16e-03

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

Pssm-ID: 277145 [Multi-domain] Cd Length: 112 Bit Score: 40.42 E-value: 1.16e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALCLKYGdadskeaGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNV---HAAVARGRqMRCELC---LKPGATVGCC 591
Cdd:cd15675      1 CCLCCLRG-------GALKPTTDGRWAHVVCAIAIPEVRFSNVPERGPIdisKIPPARLK-LKCIYCskiTKSMSHMGAC 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1907184719  592 LS----SCLSNFHFMCARASYCIFQDDK-----KVFCQKH 622
Cdd:cd15675     73 IQcstgKCTTSFHVTCAHAAGVQMEPDDwpypvYVTCTKH 112

ePHD_ATX1_2_like

cd15662

Extended PHD finger found in Arabidopsis thaliana ATX1, -2, and similar proteins; The extended ...

543-607

1.58e-03

Extended PHD finger found in Arabidopsis thaliana ATX1, -2, and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of A. thaliana histone-lysine N-methyltransferase arabidopsis trithorax-like proteins ATX1, -2, and similar proteins. ATX1 and -2 are sister paralogs originating from a segmental chromosomal duplication; they are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1 (also known as protein SET domain group 27, or trithorax-homolog protein 1/TRX-homolog protein 1), is a methyltransferase that trimethylates histone H3 at lysine 4 (H3K4me3). It also acts as a histone modifier and as a positive effector of gene expression. ATX1 regulates transcription from diverse classes of genes implicated in biotic and abiotic stress responses. It is involved in dehydration stress signaling in both abscisic acid (ABA)-dependent and ABA-independent pathways. ATX2 (also known as protein SET domain group 30, or trithorax-homolog protein 2/TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). ATX1 and ATX2 are multi-domain proteins that consist of an N-terminal PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical PHD finger, this non-canonical ePHD finger, and a C-terminal SET domain.

Pssm-ID: 277132 Cd Length: 115 Bit Score: 40.15 E-value: 1.58e-03

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907184719  543 WTHVNCAIWSAE--VFEENDGSLKNVHAAVARGR-QMRCELCLKP-GATVGCCLSSCLSNFHFMCARAS 607
Cdd:cd15662     19 WAHLACAIWIPEtcLLDVKTMEPVDGINAISKERwELSCTICKQRyGACIQCSNNSCRVAYHPLCARAA 87

PHD_TAF3

cd15522

PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3); TAF3 (also termed ...

274-311

1.73e-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: 37.65 E-value: 1.73e-03

                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1907184719  274 YCPICTRCYEDndyeSKMMQCAQCDHWVHAKCEGLSDE 311
Cdd:cd15522      1 ICPICKKPDDG----SPMIGCDECDDWYHWECVGITDE 34

PHD_UHRF2

cd15617

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

189-237

2.28e-03

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: 37.63 E-value: 2.28e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1907184719  189 CHVCGRKGRGSKHLLeCERCRHAYHPACLGPsyPTRATRRRRHWICSAC 237
Cdd:cd15617      2 CYVCGGKQDAHMQLL-CDECNMAYHIYCLNP--PLDKIPEDEDWYCPSC 47

ePHD_JADE1

cd15704

Extended PHD finger found in protein Jade-1 and similar proteins; The extended plant ...

517-623

2.46e-03

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

Pssm-ID: 277174 Cd Length: 118 Bit Score: 39.67 E-value: 2.46e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  517 QCALCLKYGDA-DSKEAGrllyigqNEWTHVNCAIWSAEVF----EENDGSLKNVHAAVARGrQMRCELC-LKPGATVGC 590
Cdd:cd15704      3 KCLLCPKKGGAmKPTRSG-------TKWVHVSCALWIPEVSigspEKMEPITKVSHIPSSRW-ALVCSLCnEKVGASIQC 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1907184719  591 CLSSCLSNFHFMCA-----RASYCIFQDDK---KVFCQKHT 623
Cdd:cd15704     75 SVKNCRTAFHVTCAfdrglEMKTILAENDEvkfKSYCPKHS 115

PHD_UHRF1

cd15616

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

189-237

2.47e-03

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: 37.25 E-value: 2.47e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1907184719  189 CHVCGRKGRGSKHLLeCERCRHAYHPACLGPsyPTRATRRRRHWICSAC 237
Cdd:cd15616      2 CHVCGGKQDPDKQLM-CDECDMAFHIYCLNP--PLSSIPDDEDWYCPEC 47

PHD4_NSD3

cd15658

PHD finger 4 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed ...

188-237

2.79e-03

PHD finger 4 found in nuclear SET domain-containing protein 3 (NSD3); NSD3, also termed histone-lysine N-methyltransferase NSD3, or protein whistle, or WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, or Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1-like protein 1, or WHSC1L1), is a lysine methyltransferase encoded by gene NSD3, which is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD3 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, five plant-homeodomain (PHD) zinc fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the fourth PHD finger.

Pssm-ID: 277128 Cd Length: 40 Bit Score: 37.20 E-value: 2.79e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907184719  188 FCHVCGRKGRgskhLLECERCRHAYHPACLGPSYPTRAtrrrrhWICSAC 237
Cdd:cd15658      1 FCFVCARGGR----LLCCESCPASFHPECLSIEMPEGC------WNCNEC 40

ePHD_RNO

cd15707

Extended PHD finger found in Drosophila melanogaster PHD finger protein rhinoceros (RNO) and ...

518-622

3.15e-03

Extended PHD finger found in Drosophila melanogaster PHD finger protein rhinoceros (RNO) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of Drosophila melanogaster RNO. RNO is a novel plant homeodomain (PHD)-containing nuclear protein that may function as a transcription factor that antagonizes Ras signaling by regulating the transcription of key EGFR/Ras pathway regulators in the Drosophila eye. RNO contains a canonical PHD domain followed by this non-canonical ePHD domain, both of which are zinc-binding motifs.

Pssm-ID: 277177 [Multi-domain] Cd Length: 113 Bit Score: 39.11 E-value: 3.15e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALCLKYGDA-DSKEAGrllyigqNEWTHVNCAIWSAEVF---EENDGSLKNVHAAVARGRQMRCELCL-KPGATVGCCL 592
Cdd:cd15707      1 CILCPNKGGAmKSTRSG-------TKWAHVSCALWIPEVSigcVEKMEPITKISSIPASRWALICVLCReRTGACIQCSV 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1907184719  593 SSCLSNFHFMCArasyciFQ--------------DDKKV--FCQKH 622
Cdd:cd15707     74 KTCKTAYHVTCG------FQhglemktildeeseDGVKLrsYCQKH 113

ePHD_BRPF2

cd15702

Extended PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and ...

518-607

3.68e-03

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

Pssm-ID: 277172 Cd Length: 118 Bit Score: 38.87 E-value: 3.68e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALCLKYGDADSKEAgrllyigQNEWTHVNCAIWSAEV------FEENDGSLKNVHAAVARgrqMRCELCLKP--GATVG 589
Cdd:cd15702      1 CVLCPNKGGAFKKTD-------DDRWGHVVCALWIPEVgfantvFIEPIDGVRNIPPARWK---LTCYLCKQKgvGACIQ 70

                           90
                   ....*....|....*...
gi 1907184719  590 CCLSSCLSNFHFMCARAS 607
Cdd:cd15702     71 CHKANCYTAFHVTCAQKA 88

PHD1_PHF1

cd15500

PHD finger 1 found in PHD finger protein1 (PHF1); PHF1, also termed polycomb-like protein 1 ...

202-237

3.83e-03

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

Pssm-ID: 276975 Cd Length: 51 Bit Score: 37.12 E-value: 3.83e-03

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1907184719  202 LLECERCRHAYHPACLGPSYPTRATRRRRHWICSAC 237
Cdd:cd15500     16 LVNCEKCHHAYHQECHVPRVPLESAGDGDSWMCRQC 51

PHD_Hop1p_like

cd15558

PHD finger found in Schizosaccharomyces pombe meiosis-specific protein hop1 (Hop1p) and ...

284-327

5.03e-03

PHD finger found in Schizosaccharomyces pombe meiosis-specific protein hop1 (Hop1p) and similar proteins; Fission yeast Hop1p, also termed linear element-associated protein hop1, is an S. pombe homolog of the synaptonemal complex (SC)-associated protein Hop1 in Saccharomyces cerevisiae. In contrast to S. cerevisiae, S. pombe forms thin threads, known as linear elements (LinEs), in meiotic nuclei, instead of a canonical synaptonemal complex. LinEs contain Rec10 protein and are evolutionary relics of SC axial elements. Fission yeast Hop1p is a linear element (LinE)-associated protein. It also associates with Rec10, which plays a role in recruiting the recombination machinery to chromatin. Hop1p contains an N-terminal HORMA (for Hop1p, Rev7p, and MAD2) domain and a C-terminal plant homeodomain (PHD) finger.

Pssm-ID: 277033 Cd Length: 47 Bit Score: 36.65 E-value: 5.03e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1907184719  284 DNDYESKMMQCAQCDHWVHAKCEGL-SDEDyeilSGLPDS-VLYTC 327
Cdd:cd15558      6 DWGEDGAMIQCAFCDTWQHLLCYGFeSAKD----PRIPDIhVCYRC 47

PHD_PYGO1

cd15635

PHD finger found in pygopus homolog 1 (PYGO1); PYGO1 is a homolog of Drosophila melanogaster ...

275-330

5.05e-03

PHD finger found in pygopus homolog 1 (PYGO1); PYGO1 is a homolog of Drosophila melanogaster protein pygopus (dPYGO), which is a fundamental Wnt signaling transcriptional component in Drosophila. It functions as a context-dependent beta-catenin coactivator, and binds di- and trimethylated lysine 4 of histone H3 (H3K4me2/3). PYGO1 is essential for the association with Legless (Lgs)/Bcl9 that acts as an adaptor between Pygopus (Pygo) and Arm/beta-catenin. PYGO1 contains a plant homeodomain (PHD) finger, which is important for Lgs/Bcl9 recognition as well as for the regulation of the Wnt/beta-catenin signaling pathway.

Pssm-ID: 277105 Cd Length: 57 Bit Score: 37.00 E-value: 5.05e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907184719  275 CPICTrcYEDNDYESKMMQCAQCDHWVHAKCEGLSDEDYEILSGlPDSVLYTCGPC 330
Cdd:cd15635      3 CGICT--NEVNDDQDAILCEASCQKWFHRICTGMTETAYGLLTA-EASAVWGCDTC 55

PHD4_KMT2C

cd15596

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

189-237

5.34e-03

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: 36.92 E-value: 5.34e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907184719  189 CHVCGRKGRGSK-HLLECERCRHAYHPACLgpSYPTRATRRRRHWICSAC 237
Cdd:cd15596      9 CVVCGSFGQGAEgRLLACSQCGQCYHPYCV--SIKITKVVLSKGWRCLEC 56

PHD5_NSD

cd15568

PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...

188-235

5.40e-03

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

Pssm-ID: 277043 [Multi-domain] Cd Length: 43 Bit Score: 36.15 E-value: 5.40e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907184719  188 FCHVCGRKGRgskhLLECER--CRHAYHPACLGpsyptRATRRRRHWICS 235
Cdd:cd15568      1 ECFRCGDGGD----LVLCDFkgCPKVYHLSCLG-----LEKPPGGKWICP 41

PHD_UBR7

cd15542

PHD finger found in putative E3 ubiquitin-protein ligase UBR7; UBR7, also termed N-recognin-7, ...

274-316

6.84e-03

PHD finger found in putative E3 ubiquitin-protein ligase UBR7; UBR7, also termed N-recognin-7, is a UBR box-containing protein that belongs to the E3 ubiquitin ligase family that recognizes N-degrons or structurally related molecules for ubiquitin-dependent proteolysis or related processes through the UBR box motif. In addition to the UBR box, UBR7 also harbors a plant homeodomain (PHD) finger. The biochemical properties of UBR7 remain unclear.

Pssm-ID: 277017 Cd Length: 54 Bit Score: 36.19 E-value: 6.84e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907184719  274 YCpICTRCYEDNDYESK--MMQCAQCDHWVHAKCEGL-----SDEDYEIL 316
Cdd:cd15542      1 YC-TCDRPYPDPEDEVEdeMIQCVLCEDWFHGRHLGLtppepDPDEFDEM 49

PHD1_MTF2_PHF19_like

cd15499

PHD finger 1 found in polycomb repressive complex 2 (PRC2)-associated polycomb-like (PCL) ...

140-188

7.20e-03

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: 36.32 E-value: 7.20e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907184719  140 VCLLCASKGLHELVFCQVCCDPFHPFCLEEAERPSPQHRDT-WCCRRCKF 188
Cdd:cd15499      4 ICGGAEARDGNEILICDKCDKGYHQLCHSPKVRTSPLEGDEkWFCSRCVF 53

PHD1_PHF10

cd15528

PHD finger 1 found in PHD finger protein 10 (PHF10) and similar proteins; PHF10, also termed ...

275-311

8.41e-03

PHD finger 1 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 first PHD finger.

Pssm-ID: 277003 Cd Length: 54 Bit Score: 36.24 E-value: 8.41e-03

                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1907184719  275 CPICTRCYEDNDYESKMM-QCAQCDHWVHAKCEGLSDE 311
Cdd:cd15528      2 CGICEKGGKSNKGEPEELiHCSQCGNSGHPSCLEMSDE 39

PHD2_PHF14

cd15562

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

188-237

8.50e-03

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: 35.84 E-value: 8.50e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907184719  188 FCHVCgrKGRGSKHLL-ECERCRHAYHPACLGPSYpTRATRRRRH--WICSAC 237
Cdd:cd15562      1 SCGIC--KKSNDQHLLaLCDTCKLYYHLGCLDPPL-TRMPKKTKNsgWQCSEC 50

ePHD_JMJD2B

cd15714

Extended PHD finger found in Jumonji domain-containing protein 2B (JMJD2B); The extended plant ...

518-622

9.59e-03

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

Pssm-ID: 277184 Cd Length: 110 Bit Score: 37.61 E-value: 9.59e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184719  518 CALClkygdadSKEAGRLLYIGQNEWTHVNCAIWSAEVFEEN--DGSLKNVHAAVARGRQMRCELCLKP-----GATVGC 590
Cdd:cd15714      1 CCLC-------NLRGGALQMTTDERWVHVICAIAVPEARFLNviERHPVDVSAIPEQRWKLKCVYCRKRmkkvsGACIQC 73

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907184719  591 CLSSCLSNFHFMCARASYCIFQDDK-----KVFCQKH 622
Cdd:cd15714     74 SYDHCSTSFHVTCAHAAGVVMEPDDwpyvvSITCFKH 110

Blast search parameters

Data Source:	Precalculated data, version = cdd.v.3.21
Preset Options:	Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01