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Conserved domains on  [gi|332646729|gb|AEE80250|]
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SET domain protein 14 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SET_SETD1-like cd10518
SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...
 862-1014 9.97e-71

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: 231.33  E-value: 9.97e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  862 FRERLKHLQRTENFRVCFGKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQG-KDCYLFKISEEIVID 940
Cdd:cd10518     1 MSKRFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKRYDEEGgGGTYMFRIDEDLVID 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332646729  941 ATDSGNIARLINHSCMPNCYARIVSMGDgeDNRIVLIAKTNVAAGEELTYDYLFEVDESEeiKVPCLCKAPNCR 1014
Cdd:cd10518    81 ATKKGNIARFINHSCDPNCYAKIITVDG--EKHIVIFAKRDIAPGEELTYDYKFPIEDEE--KIPCLCGAPNCR 150
ePHD_ATX3_4_5_like cd15663
Extended PHD finger found in Arabidopsis thaliana ATX3, -4, -5, and similar proteins; The ...
 603-714 6.08e-70

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


:

Pssm-ID: 277133  Cd Length: 112  Bit Score: 227.78  E-value: 6.08e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALKPSDVEGLWVHVTCAWFRPEVGFLNHENMEPAVGLFKIPANSFLKVCTICKQTHGSCVHCCKCATHFHA 682
Cdd:cd15663     1 CCLCPVKGGALKPTDVEGLWVHVTCAWFRPEVCFKNEEKMEPAVGLLRIPLSTFLKACVICKQIHGSCTQCCKCATYFHA 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 332646729  683 MCASRAGYNMELHCLEKNGVQRTRKSVYCSFH 714
Cdd:cd15663    81 MCASRAGYHMELHCLEKNGVQITRMVSYCSFH 112
PWWP_AtATX3-like cd20143
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
 188-292 1.36e-42

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


:

Pssm-ID: 438971 [Multi-domain]  Cd Length: 100  Bit Score: 150.21  E-value: 1.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  188 TVGDLVWAKCGKrFPAWPAVVIDPISQAPdGVLKHCVPGAICVMFFGYskdGTQRDYAWVRQGMVYPFTEFMDKFQDQTN 267
Cdd:cd20143     1 VEGDLVWAKVGT-HPFWPARVVEPAEQAE-EVRRRCVPGSLCVYFFGP---GGSRDYGWVRRSMIFPFTDDLARFQTQKI 75

                          90       100
                  ....*....|....*....|....*
gi 332646729  268 LFNYKASEFNKALEEAVLAENGNFG 292
Cdd:cd20143    76 KNKKRPQEFQEALEEAKLADAGFEE 100
COG5141 super family cl34917
PHD zinc finger-containing protein [General function prediction only];
518-765 4.59e-29

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


The actual alignment was detected with superfamily member COG5141:

Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 124.32  E-value: 4.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  518 TLETQMLDKQKmlSLLEEKYEPVRAK-WTTERCAVCRWVEDWEENKMIICNRCQVAVHQECYGVsksQDLTS--WVCRAC 594
Cdd:COG5141   166 RLEKEWFFFEH--GLPDKHVEPIEPSdEFDDICTKCTSTHNENSNAIVFCDGCEICVHQSCYGI---QFLPEgfWLCRKC 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  595 ETPDIERDCCL-CPVKGGALKPSDvEGLWVHVTCAWFRPEVGFLNHENMEPAVGLFKIPANSFLKVCTICKQTHGSCVHC 673
Cdd:COG5141   241 IYGEYQIRCCSfCPSSDGAFKQTS-DGRWGHVICAMFNPELSFGHLLSKDPIDNIASVSSSRWKLGCLICKEFGGTCIQC 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  674 CK--CATHFHAMCASRAGYNMeLHCLEKNGvqrtrksvycsFHRKPDPDSVVVVHTPSGvfgsrnllqnqYGRAKGSRLV 751
Cdd:COG5141   320 SYfnCTRAYHVTCARRAGYFD-LNIYSHNG-----------ISYCIDHEPLCRKHYPLG-----------YGRMNGLRYF 376

                         250
                  ....*....|....
gi 332646729  752 LTKKMKLPGFQTQT 765
Cdd:COG5141   377 GYEKLRYKNPPTAI 390
PHD_TCF19_like cd15517
PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ...
 365-415 6.44e-10

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: 55.63  E-value: 6.44e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 332646729  365 CGICKRIWHPsDDGDWVCCDGCDVWVHAECDNITNERFKELEhnNYYCPDC 415
Cdd:cd15517     2 CGICNLETAA-VDELWVQCDGCDKWFHQFCLGLSNERYADED--KFKCPNC 49
 
Name Accession Description Interval E-value
SET_SETD1-like cd10518
SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...
 862-1014 9.97e-71

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: 231.33  E-value: 9.97e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  862 FRERLKHLQRTENFRVCFGKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQG-KDCYLFKISEEIVID 940
Cdd:cd10518     1 MSKRFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKRYDEEGgGGTYMFRIDEDLVID 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332646729  941 ATDSGNIARLINHSCMPNCYARIVSMGDgeDNRIVLIAKTNVAAGEELTYDYLFEVDESEeiKVPCLCKAPNCR 1014
Cdd:cd10518    81 ATKKGNIARFINHSCDPNCYAKIITVDG--EKHIVIFAKRDIAPGEELTYDYKFPIEDEE--KIPCLCGAPNCR 150
ePHD_ATX3_4_5_like cd15663
Extended PHD finger found in Arabidopsis thaliana ATX3, -4, -5, and similar proteins; The ...
 603-714 6.08e-70

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


Pssm-ID: 277133  Cd Length: 112  Bit Score: 227.78  E-value: 6.08e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALKPSDVEGLWVHVTCAWFRPEVGFLNHENMEPAVGLFKIPANSFLKVCTICKQTHGSCVHCCKCATHFHA 682
Cdd:cd15663     1 CCLCPVKGGALKPTDVEGLWVHVTCAWFRPEVCFKNEEKMEPAVGLLRIPLSTFLKACVICKQIHGSCTQCCKCATYFHA 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 332646729  683 MCASRAGYNMELHCLEKNGVQRTRKSVYCSFH 714
Cdd:cd15663    81 MCASRAGYHMELHCLEKNGVQITRMVSYCSFH 112
PWWP_AtATX3-like cd20143
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
 188-292 1.36e-42

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


Pssm-ID: 438971 [Multi-domain]  Cd Length: 100  Bit Score: 150.21  E-value: 1.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  188 TVGDLVWAKCGKrFPAWPAVVIDPISQAPdGVLKHCVPGAICVMFFGYskdGTQRDYAWVRQGMVYPFTEFMDKFQDQTN 267
Cdd:cd20143     1 VEGDLVWAKVGT-HPFWPARVVEPAEQAE-EVRRRCVPGSLCVYFFGP---GGSRDYGWVRRSMIFPFTDDLARFQTQKI 75

                          90       100
                  ....*....|....*....|....*
gi 332646729  268 LFNYKASEFNKALEEAVLAENGNFG 292
Cdd:cd20143    76 KNKKRPQEFQEALEEAKLADAGFEE 100
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
874-1015 3.91e-36

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 133.16  E-value: 3.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  874 NFRVCFGKSGIHGWGLFARKSIQEGEMIIEYRGVkvRRSVADLREANYRSQGKDCYLFKISEEIVIDATDSGNIARLINH 953
Cdd:COG2940     5 HPRIEVRPSPIHGRGVFATRDIPKGTLIGEYPGE--VITWAEAERREPHKEPLHTYLFELDDDGVIDGALGGNPARFINH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332646729  954 SCMPNCYARIvsmgdgEDNRIVLIAKTNVAAGEELTYDYLFEVDESEeikVPCLCkaPNCRK 1015
Cdd:COG2940    83 SCDPNCEADE------EDGRIFIVALRDIAAGEELTYDYGLDYDEEE---YPCRC--PNCRG 133
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 875-992 1.95e-35

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: 130.92  E-value: 1.95e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729    875 FRVCFGKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQG-KDCYLFKISEEIVIDATDSGNIARLINH 953
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGaKAFYLFDIDSDLCIDARRKGNLARFINH 80

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 332646729    954 SCMPNCYARIVSMGDgeDNRIVLIAKTNVAAGEELTYDY 992
Cdd:smart00317   81 SCEPNCELLFVEVNG--DDRIVIFALRDIKPGEELTIDY 117
zf-HC5HC2H_2 pfam13832
PHD-zinc-finger like domain;
601-714 2.53e-32

PHD-zinc-finger like domain;


Pssm-ID: 463991 [Multi-domain]  Cd Length: 109  Bit Score: 121.30  E-value: 2.53e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729   601 RDCCLCPVKGGALKPSDvEGLWVHVTCAWFRPEVGFLNHENMEPaVGLFKIPANSFLKVCTICKQTHGSCVHCCK--CAT 678
Cdd:pfam13832    1 VRCCLCPLRGGALKQTS-DGRWVHVLCAIFVPEVRFGNVATMEP-IDVSRIPPERWKLKCVFCKKRSGACIQCSKgrCTT 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 332646729   679 HFHAMCASRAGYNMELHCLEkngvqRTRKSVYCSFH 714
Cdd:pfam13832   79 AFHVTCAQAAGVYMEPEDWP-----NVVVIAYCQKH 109
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 886-992 3.17e-29

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: 112.62  E-value: 3.17e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729   886 GWGLFARKSIQEGEMIIEY-RGVKVRRSVADLREANYRSQGKD----CYLFKISEEI--VIDATD--SGNIARLINHSCM 956
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYvEVLLITKEEADKRELLYYDKLELrlwgPYLFTLDEDSeyCIDARAlyYGNWARFINHSCD 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 332646729   957 PNCYARIVSMGDGedNRIVLIAKTNVAAGEELTYDY 992
Cdd:pfam00856   81 PNCEVRVVYVNGG--PRIVIFALRDIKPGEELTIDY 114
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
518-765 4.59e-29

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


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 124.32  E-value: 4.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  518 TLETQMLDKQKmlSLLEEKYEPVRAK-WTTERCAVCRWVEDWEENKMIICNRCQVAVHQECYGVsksQDLTS--WVCRAC 594
Cdd:COG5141   166 RLEKEWFFFEH--GLPDKHVEPIEPSdEFDDICTKCTSTHNENSNAIVFCDGCEICVHQSCYGI---QFLPEgfWLCRKC 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  595 ETPDIERDCCL-CPVKGGALKPSDvEGLWVHVTCAWFRPEVGFLNHENMEPAVGLFKIPANSFLKVCTICKQTHGSCVHC 673
Cdd:COG5141   241 IYGEYQIRCCSfCPSSDGAFKQTS-DGRWGHVICAMFNPELSFGHLLSKDPIDNIASVSSSRWKLGCLICKEFGGTCIQC 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  674 CK--CATHFHAMCASRAGYNMeLHCLEKNGvqrtrksvycsFHRKPDPDSVVVVHTPSGvfgsrnllqnqYGRAKGSRLV 751
Cdd:COG5141   320 SYfnCTRAYHVTCARRAGYFD-LNIYSHNG-----------ISYCIDHEPLCRKHYPLG-----------YGRMNGLRYF 376

                         250
                  ....*....|....
gi 332646729  752 LTKKMKLPGFQTQT 765
Cdd:COG5141   377 GYEKLRYKNPPTAI 390
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 190-283 9.01e-23

PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain binds to Histone-4 methylated at lysine-20, H4K20me, suggesting that it is methyl-lysine recognition motif. Removal of two conserved aromatic residues in a hydrophobic cavity created by this domain within the full-length protein, Pdp1, abolishes the interaction o f the protein with H4K20me3. In fission yeast, Set9 is the sole enzyme that catalyzes all three states of H4K20me, and Set9-mediated H4K20me is required for efficient recruitment of checkpoint protein Crb2 to sites of DNA damage. The methylation of H4K20 is involved in a diverse array of cellular processes, such as organizing higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression.


Pssm-ID: 459964 [Multi-domain]  Cd Length: 92  Bit Score: 93.26  E-value: 9.01e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729   190 GDLVWAKCgKRFPAWPAVVIDPISQAPDGVLKHCVPGAICVMFFGYSkdgtqrDYAWVRQGMVYPFTEFMDKFQDQTNLF 269
Cdd:pfam00855    1 GDLVWAKL-KGYPWWPARVVDPEELPENVLKPKKKDGEYLVRFFGDS------EFAWVKPKDLKPFDEGDEFEYLKKKKK 73

                           90
                   ....*....|....
gi 332646729   270 NYKASEFNKALEEA 283
Cdd:pfam00855   74 KKKKKAFKKALEEA 87
PHD_ATX3_4_5_like cd15495
PHD finger found in Arabidopsis thaliana histone-lysine N-methyltransferase arabidopsis ...
 548-594 1.46e-20

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


Pssm-ID: 276970 [Multi-domain]  Cd Length: 47  Bit Score: 85.50  E-value: 1.46e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 332646729  548 RCAVCRWVEDWEENKMIICNRCQVAVHQECYGVSKSQDLTSWVCRAC 594
Cdd:cd15495     1 RCAVCNEGEDDDNNPLITCNRCQISVHQKCYGIREVDPDGSWVCRAC 47
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 187-256 4.40e-10

domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 56.20  E-value: 4.40e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332646729    187 FTVGDLVWAKCgKRFPAWPAVVIDPiSQAPDGVLK-----HCVPgaicVMFFGyskdgtQRDYAWVRQGMVYPFT 256
Cdd:smart00293    1 FKPGDLVWAKM-KGFPWWPALVISP-KMTPDNIMKrksdeNLYP----VLFFG------DKDTAWIPSSKLFPLT 63
PHD_TCF19_like cd15517
PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ...
 365-415 6.44e-10

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: 55.63  E-value: 6.44e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 332646729  365 CGICKRIWHPsDDGDWVCCDGCDVWVHAECDNITNERFKELEhnNYYCPDC 415
Cdd:cd15517     2 CGICNLETAA-VDELWVQCDGCDKWFHQFCLGLSNERYADED--KFKCPNC 49
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 364-417 8.13e-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: 52.49  E-value: 8.13e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 332646729   364 YCGICKRiwhPSDDGDWVCCDGCDVWVHAECDNITnERFKELEHNNYYCPDCKV 417
Cdd:pfam00628    1 YCAVCGK---SDDGGELVQCDGCDDWFHLACLGPP-LDPAEIPSGEWLCPECKP 50
PHD_2 pfam13831
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 561-594 8.61e-09

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


Pssm-ID: 463990 [Multi-domain]  Cd Length: 35  Bit Score: 51.96  E-value: 8.61e-09
                           10        20        30
                   ....*....|....*....|....*....|....
gi 332646729   561 NKMIICNRCQVAVHQECYGVSKSQDLTSWVCRAC 594
Cdd:pfam13831    2 SPLVYCSKCSVQVHASCYGVPPIPDGDGWKCRRC 35
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 364-415 1.67e-07

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: 48.75  E-value: 1.67e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 332646729    364 YCGICKRiwhPSDDGDWVCCDGCDVWVHAECDNITNERFKELEHnnYYCPDC 415
Cdd:smart00249    1 YCSVCGK---PDDGGELLQCDGCDRWYHQTCLGPPLLEEEPDGK--WYCPKC 47
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 548-594 1.48e-04

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: 40.27  E-value: 1.48e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 332646729    548 RCAVCRwvEDWEENKMIICNRCQVAVHQECYGVSKSQDL--TSWVCRAC 594
Cdd:smart00249    1 YCSVCG--KPDDGGELLQCDGCDRWYHQTCLGPPLLEEEpdGKWYCPKC 47
 
Name Accession Description Interval E-value
SET_SETD1-like cd10518
SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...
 862-1014 9.97e-71

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: 231.33  E-value: 9.97e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  862 FRERLKHLQRTENFRVCFGKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQG-KDCYLFKISEEIVID 940
Cdd:cd10518     1 MSKRFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKRYDEEGgGGTYMFRIDEDLVID 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332646729  941 ATDSGNIARLINHSCMPNCYARIVSMGDgeDNRIVLIAKTNVAAGEELTYDYLFEVDESEeiKVPCLCKAPNCR 1014
Cdd:cd10518    81 ATKKGNIARFINHSCDPNCYAKIITVDG--EKHIVIFAKRDIAPGEELTYDYKFPIEDEE--KIPCLCGAPNCR 150
ePHD_ATX3_4_5_like cd15663
Extended PHD finger found in Arabidopsis thaliana ATX3, -4, -5, and similar proteins; The ...
 603-714 6.08e-70

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


Pssm-ID: 277133  Cd Length: 112  Bit Score: 227.78  E-value: 6.08e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALKPSDVEGLWVHVTCAWFRPEVGFLNHENMEPAVGLFKIPANSFLKVCTICKQTHGSCVHCCKCATHFHA 682
Cdd:cd15663     1 CCLCPVKGGALKPTDVEGLWVHVTCAWFRPEVCFKNEEKMEPAVGLLRIPLSTFLKACVICKQIHGSCTQCCKCATYFHA 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 332646729  683 MCASRAGYNMELHCLEKNGVQRTRKSVYCSFH 714
Cdd:cd15663    81 MCASRAGYHMELHCLEKNGVQITRMVSYCSFH 112
SET_SETD1 cd19169
SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...
 859-1014 1.48e-52

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: 180.61  E-value: 1.48e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  859 FTSFRERLKHLQrtenfrvcFGKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQG-KDCYLFKISEEI 937
Cdd:cd19169     5 FNQLKFRKKQLK--------FAKSRIHDWGLFALEPIAADEMVIEYVGQVIRQSVADEREKRYEAIGiGSSYLFRVDDDT 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332646729  938 VIDATDSGNIARLINHSCMPNCYARIVSMGDgeDNRIVLIAKTNVAAGEELTYDYLFEVdesEEIKVPCLCKAPNCR 1014
Cdd:cd19169    77 IIDATKCGNLARFINHSCNPNCYAKIITVES--QKKIVIYSKRPIAVNEEITYDYKFPI---EDEKIPCLCGAPQCR 148
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
 876-1017 4.91e-52

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: 179.16  E-value: 4.91e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  876 RVCFGKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQGKDCYLFKISEEIVIDATDSGNIARLINHSC 955
Cdd:cd19171    15 NVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNRGIYMFRIDNDWVIDATMTGGPARYINHSC 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332646729  956 MPNCYARIVSMgdGEDNRIVLIAKTNVAAGEELTYDYLFEVdESEEIKVPCLCKAPNCRKFM 1017
Cdd:cd19171    95 NPNCVAEVVTF--DKEKKIIIISNRRIAKGEELTYDYKFDF-EDDQHKIPCLCGAPNCRKWM 153
SET_SET1 cd20072
SET domain (including post-SET domain) found in catalytic component of the Saccharomyces ...
 876-1014 4.07e-51

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: 176.46  E-value: 4.07e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  876 RVCFGKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQG-KDCYLFKISEEIVIDATDSGNIARLINHS 954
Cdd:cd20072    14 QLKFARSAIHNWGLYAMENISAKDMVIEYVGEVIRQQVADEREKRYLRQGiGSSYLFRIDDDTVVDATKKGNIARFINHC 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  955 CMPNCYARIVSMGDgeDNRIVLIAKTNVAAGEELTYDYLFevdESEEIKVPCLCKAPNCR 1014
Cdd:cd20072    94 CDPNCTAKIIKVEG--EKRIVIYAKRDIAAGEELTYDYKF---PREEDKIPCLCGAPNCR 148
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
 865-1018 1.67e-49

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: 172.19  E-value: 1.67e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  865 RLKHLQRTENFRVCFGKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQGKDCYLFKISEEIVIDATDS 944
Cdd:cd19170     4 RFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKYYESKGIGCYMFRIDDDEVVDATMH 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332646729  945 GNIARLINHSCMPNCYARIVSMgDGEdNRIVLIAKTNVAAGEELTYDYLFEVdesEEIKVPCLCKAPNCRKFMN 1018
Cdd:cd19170    84 GNAARFINHSCEPNCYSRVVNI-DGK-KHIVIFALRRILRGEELTYDYKFPI---EDVKIPCTCGSKKCRKYLN 152
SET_KMT2A cd19206
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...
 864-1018 8.78e-43

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: 152.87  E-value: 8.78e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  864 ERLKHLQRTENFRVCFGKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQGKDCYLFKISEEIVIDATD 943
Cdd:cd19206     3 MRFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREKYYDSKGIGCYMFRIDDSEVVDATM 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332646729  944 SGNIARLINHSCMPNCYARIVSMgDGEDNrIVLIAKTNVAAGEELTYDYLFEVDESEEiKVPCLCKAPNCRKFMN 1018
Cdd:cd19206    83 HGNAARFINHSCEPNCYSRVINI-DGQKH-IVIFAMRKIYRGEELTYDYKFPIEDASN-KLPCNCGAKKCRKFLN 154
PWWP_AtATX3-like cd20143
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
 188-292 1.36e-42

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


Pssm-ID: 438971 [Multi-domain]  Cd Length: 100  Bit Score: 150.21  E-value: 1.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  188 TVGDLVWAKCGKrFPAWPAVVIDPISQAPdGVLKHCVPGAICVMFFGYskdGTQRDYAWVRQGMVYPFTEFMDKFQDQTN 267
Cdd:cd20143     1 VEGDLVWAKVGT-HPFWPARVVEPAEQAE-EVRRRCVPGSLCVYFFGP---GGSRDYGWVRRSMIFPFTDDLARFQTQKI 75

                          90       100
                  ....*....|....*....|....*
gi 332646729  268 LFNYKASEFNKALEEAVLAENGNFG 292
Cdd:cd20143    76 KNKKRPQEFQEALEEAKLADAGFEE 100
SET_SETD1A cd19204
SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...
 865-1018 9.24e-41

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: 147.09  E-value: 9.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  865 RLKHLQ-RTENFRvcFGKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQG-KDCYLFKISEEIVIDAT 942
Cdd:cd19204     5 KLNQLKfRKKKLR--FGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQVVADMREKRYVQEGiGSSYLFRVDHDTIIDAT 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332646729  943 DSGNIARLINHSCMPNCYARIVSMgdGEDNRIVLIAKTNVAAGEELTYDYLFEVDESeeiKVPCLCKAPNCRKFMN 1018
Cdd:cd19204    83 KCGNLARFINHCCTPNCYAKVITI--ESQKKIVIYSKQPIGVNEEITYDYKFPIEDN---KIPCLCGTENCRGTLN 153
SET_KMT2B cd19207
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...
 865-1018 9.82e-37

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


Pssm-ID: 380984 [Multi-domain]  Cd Length: 154  Bit Score: 135.54  E-value: 9.82e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  865 RLKHLQRTENFRVCFGKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQGKDCYLFKISEEIVIDATDS 944
Cdd:cd19207     4 RFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDSKGIGCYMFRIDDFDVVDATMH 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332646729  945 GNIARLINHSCMPNCYARIVSMgDGEDNrIVLIAKTNVAAGEELTYDYLFEVDESEEiKVPCLCKAPNCRKFMN 1018
Cdd:cd19207    84 GNAARFINHSCEPNCYSRVIHV-EGQKH-IVIFALRKIYRGEELTYDYKFPIEDASN-KLPCNCGAKRCRRFLN 154
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
874-1015 3.91e-36

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 133.16  E-value: 3.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  874 NFRVCFGKSGIHGWGLFARKSIQEGEMIIEYRGVkvRRSVADLREANYRSQGKDCYLFKISEEIVIDATDSGNIARLINH 953
Cdd:COG2940     5 HPRIEVRPSPIHGRGVFATRDIPKGTLIGEYPGE--VITWAEAERREPHKEPLHTYLFELDDDGVIDGALGGNPARFINH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332646729  954 SCMPNCYARIvsmgdgEDNRIVLIAKTNVAAGEELTYDYLFEVDESEeikVPCLCkaPNCRK 1015
Cdd:COG2940    83 SCDPNCEADE------EDGRIFIVALRDIAAGEELTYDYGLDYDEEE---YPCRC--PNCRG 133
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 875-992 1.95e-35

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: 130.92  E-value: 1.95e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729    875 FRVCFGKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQG-KDCYLFKISEEIVIDATDSGNIARLINH 953
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGaKAFYLFDIDSDLCIDARRKGNLARFINH 80

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 332646729    954 SCMPNCYARIVSMGDgeDNRIVLIAKTNVAAGEELTYDY 992
Cdd:smart00317   81 SCEPNCELLFVEVNG--DDRIVIFALRDIKPGEELTIDY 117
SET_SETD1B cd19205
SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...
 871-1018 1.97e-35

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: 132.10  E-value: 1.97e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  871 RTENFRVCfgKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQG-KDCYLFKISEEIVIDATDSGNIAR 949
Cdd:cd19205    12 RKKKLKFC--KSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKRYEDEGiGSSYMFRVDHDTIIDATKCGNFAR 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332646729  950 LINHSCMPNCYARIVSMgdGEDNRIVLIAKTNVAAGEELTYDYLFEVdesEEIKVPCLCKAPNCRKFMN 1018
Cdd:cd19205    90 FINHSCNPNCYAKVITV--ESQKKIVIYSKQHINVNEEITYDYKFPI---EDVKIPCLCGSENCRGTLN 153
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
 876-992 6.56e-35

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: 128.90  E-value: 6.56e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  876 RVCFGKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQGKDcYLFKISEEIVIDATDSGNIARLINHSC 955
Cdd:cd10519     2 RLLLGKSDVAGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGKIYDKYNSS-YLFNLNDQFVVDATRKGNKIRFANHSS 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 332646729  956 MPNCYARIVsMGDGeDNRIVLIAKTNVAAGEELTYDY 992
Cdd:cd10519    81 NPNCYAKVM-MVNG-DHRIGIFAKRDIEAGEELFFDY 115
SET_KMT2D cd19209
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...
 877-1017 3.41e-33

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: 125.58  E-value: 3.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  877 VCFGKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQGKDCYLFKISEEIVIDATDSGNIARLINHSCM 956
Cdd:cd19209    18 VYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVIDATLTGGPARYINHSCA 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332646729  957 PNCYARIVSMgDGEDnRIVLIAKTNVAAGEELTYDYLFEVdESEEIKVPCLCKAPNCRKFM 1017
Cdd:cd19209    98 PNCVAEVVTF-DKED-KIIIISSRRIPKGEELTYDYQFDF-EDDQHKIPCHCGAWNCRKWM 155
SET_KMT2C cd19208
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...
 877-1017 1.57e-32

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: 123.58  E-value: 1.57e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  877 VCFGKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQGKDCYLFKISEEIVIDATDSGNIARLINHSCM 956
Cdd:cd19208    17 VYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRIDNDHVIDATLTGGPARYINHSCA 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332646729  957 PNCYARIVSMGDGedNRIVLIAKTNVAAGEELTYDYLFEVdESEEIKVPCLCKAPNCRKFM 1017
Cdd:cd19208    97 PNCVAEVVTFEKG--HKIIISSSRRIQKGEELCYDYKFDF-EDDQHKIPCHCGAVNCRKWM 154
zf-HC5HC2H_2 pfam13832
PHD-zinc-finger like domain;
601-714 2.53e-32

PHD-zinc-finger like domain;


Pssm-ID: 463991 [Multi-domain]  Cd Length: 109  Bit Score: 121.30  E-value: 2.53e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729   601 RDCCLCPVKGGALKPSDvEGLWVHVTCAWFRPEVGFLNHENMEPaVGLFKIPANSFLKVCTICKQTHGSCVHCCK--CAT 678
Cdd:pfam13832    1 VRCCLCPLRGGALKQTS-DGRWVHVLCAIFVPEVRFGNVATMEP-IDVSRIPPERWKLKCVFCKKRSGACIQCSKgrCTT 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 332646729   679 HFHAMCASRAGYNMELHCLEkngvqRTRKSVYCSFH 714
Cdd:pfam13832   79 AFHVTCAQAAGVYMEPEDWP-----NVVVIAYCQKH 109
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 886-992 3.17e-29

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: 112.62  E-value: 3.17e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729   886 GWGLFARKSIQEGEMIIEY-RGVKVRRSVADLREANYRSQGKD----CYLFKISEEI--VIDATD--SGNIARLINHSCM 956
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYvEVLLITKEEADKRELLYYDKLELrlwgPYLFTLDEDSeyCIDARAlyYGNWARFINHSCD 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 332646729   957 PNCYARIVSMGDGedNRIVLIAKTNVAAGEELTYDY 992
Cdd:pfam00856   81 PNCEVRVVYVNGG--PRIVIFALRDIKPGEELTIDY 114
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
518-765 4.59e-29

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


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 124.32  E-value: 4.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  518 TLETQMLDKQKmlSLLEEKYEPVRAK-WTTERCAVCRWVEDWEENKMIICNRCQVAVHQECYGVsksQDLTS--WVCRAC 594
Cdd:COG5141   166 RLEKEWFFFEH--GLPDKHVEPIEPSdEFDDICTKCTSTHNENSNAIVFCDGCEICVHQSCYGI---QFLPEgfWLCRKC 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  595 ETPDIERDCCL-CPVKGGALKPSDvEGLWVHVTCAWFRPEVGFLNHENMEPAVGLFKIPANSFLKVCTICKQTHGSCVHC 673
Cdd:COG5141   241 IYGEYQIRCCSfCPSSDGAFKQTS-DGRWGHVICAMFNPELSFGHLLSKDPIDNIASVSSSRWKLGCLICKEFGGTCIQC 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  674 CK--CATHFHAMCASRAGYNMeLHCLEKNGvqrtrksvycsFHRKPDPDSVVVVHTPSGvfgsrnllqnqYGRAKGSRLV 751
Cdd:COG5141   320 SYfnCTRAYHVTCARRAGYFD-LNIYSHNG-----------ISYCIDHEPLCRKHYPLG-----------YGRMNGLRYF 376

                         250
                  ....*....|....
gi 332646729  752 LTKKMKLPGFQTQT 765
Cdd:COG5141   377 GYEKLRYKNPPTAI 390
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
 886-1014 1.36e-28

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: 111.58  E-value: 1.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  886 GWGLFARKSIQEGEMIIEYRGvkvrrSVADLREANYRSQG------KDCYLFKISEEIVIDATDSGNIARLINHSCMPNC 959
Cdd:cd10531    11 GWGVKAKEDIQKGEFIIEYVG-----EVIDKKEFKERLDEyeelgkSNFYILSLSDDVVIDATRKGNLSRFINHSCEPNC 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 332646729  960 YARiVSMGDGEdNRIVLIAKTNVAAGEELTYDYLFEvdESEEIKVPCLCKAPNCR 1014
Cdd:cd10531    86 ETQ-KWIVNGE-YRIGIFALRDIPAGEELTFDYNFV--NYNEAKQVCLCGAQNCR 136
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
 886-1018 6.99e-27

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: 106.99  E-value: 6.99e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  886 GWGLFARKSIQEGEMIIEYRGVKVrrSVADLR---EANYRSQgKDCYLFKISEEIVIDATDSGNIARLINHSCMPNCYAR 962
Cdd:cd19174    11 GWGVRTKEPIKAGQFIIEYVGEVV--SEQEFRrrmIEQYHNH-SHHYCLNLDSGMVIDGYRMGNEARFVNHSCDPNCEMQ 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 332646729  963 IVSMgDGEdNRIVLIAKTNVAAGEELTYDYLFEVdESEEIKVPCLCKAPNCRKFMN 1018
Cdd:cd19174    88 KWSV-NGV-YRIGLFALKDIPAGEELTYDYNFHS-FNVEKQQPCKCGSPNCRGVIG 140
ePHD cd15571
Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is ...
 603-714 1.16e-26

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: 105.36  E-value: 1.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALKPSDV-----EGLWVHVTCAWFRPEVGFLNHENMEPaVGLFKIPANSFLKVCTICKQTHGSCVHCC--K 675
Cdd:cd15571     1 CALCPRSGGALKGGGAlkttsDGLWVHVVCALWSPEVYFDDGTLLEV-EGVSKIPKRRKKLKCSICGKRGGACIQCSypG 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 332646729  676 CATHFHAMCASRAGYNMELHClekngvQRTRKSVYCSFH 714
Cdd:cd15571    80 CPRSFHVSCAIRAGCLFEFED------GPGNFVVYCPKH 112
SET_ASHR3-like cd19175
SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...
 881-1017 1.59e-26

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: 105.96  E-value: 1.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  881 KSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQG-KDCYLFKISEEIVIDATDSGNIARLINHSCMPNC 959
Cdd:cd19175     6 KTEKCGWGLVADEDINAGEFIIEYVGEVIDDKTCEERLWDMKHKGeKNFYMCEIDKDMVIDATFKGNLSRFINHSCDPNC 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  960 YAR--IVsmgDGEdNRIVLIAKTNVAAGEELTYDYLFeVDESEEIKvpCLCKAPNCRKFM 1017
Cdd:cd19175    86 ELQkwQV---DGE-TRIGVFAIRDIKKGEELTYDYQF-VQFGADQD--CHCGSKNCRGKL 138
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
 881-1017 5.30e-25

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: 101.50  E-value: 5.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  881 KSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQGKDCYLF-KISEEIVIDATDSGNIARLINHSCMPNC 959
Cdd:cd19172     8 RTEKKGWGLRAAEDLPKGTFVIEYVGEVLDEKEFKRRMKEYAREGNRHYYFmALKSDEIIDATKKGNLSRFINHSCEPNC 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 332646729  960 YARIVSMGDgeDNRIVLIAKTNVAAGEELTYDYLFEVDESEeiKVPCLCKAPNCRKFM 1017
Cdd:cd19172    88 ETQKWTVNG--ELRVGFFAKRDIPAGEELTFDYQFERYGKE--AQKCYCGSPNCRGYI 141
ePHD_JADE cd15671
Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended ...
 603-714 2.92e-24

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: 98.28  E-value: 2.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALKPSDVEGLWVHVTCAWFRPEVGFLNHENMEPAVGLFKIPANSFLKVCTICKQTHGSCVHCC--KCATHF 680
Cdd:cd15671     1 CVLCPKKGGAMKSTKSGTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPMSRWALVCVLCKEKTGACIQCSvkSCKTAF 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 332646729  681 HAMCASRAGYNMELH-CLEKNGVQrtRKSvYCSFH 714
Cdd:cd15671    81 HVTCAFQHGLEMKTIlEDEDDEVK--FKS-YCPKH 112
ePHD_BRPF cd15670
Extended PHD finger found in BRPF proteins; The extended plant homeodomain (ePHD) zinc finger ...
 603-714 2.95e-24

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: 98.56  E-value: 2.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALKPSDvEGLWVHVTCAWFRPEVGFLNHENMEPAVGLFKIPANSFLKVCTICKQTHGSCVHCCK--CATHF 680
Cdd:cd15670     1 CVLCPNKGGAFKQTD-DGRWAHVVCALWIPEVSFANTVFLEPIDGIQNIPKARWKLTCYICKKRMGACIQCHKknCYTAF 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 332646729  681 HAMCASRAGYNMEL-HCLEKNGV--QRTRKSVYCSFH 714
Cdd:cd15670    80 HVTCAQQAGLYMKIePVKDPGNGtsDSVRKEAYCDKH 116
SET_NSD cd19173
SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...
 881-1017 4.00e-23

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: 96.23  E-value: 4.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  881 KSGIHGWGLFARKSIQEGEMIIEYRG-----VKVRRSVADLREANYRsqgkDCYLFKISEEIVIDATDSGNIARLINHSC 955
Cdd:cd19173     8 KTGDRGWGLRTKRDIKKGDFVIEYVGelideEECRRRLKKAHENNIT----NFYMLTLDKDRIIDAGPKGNLSRFMNHSC 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332646729  956 MPNCYARIVSMGDgeDNRIVLIAKTNVAAGEELTYDYLFEVDESEeiKVPCLCKAPNCRKFM 1017
Cdd:cd19173    84 QPNCETQKWTVNG--DTRVGLFAVRDIPAGEELTFNYNLDCLGNE--KKVCRCGAPNCSGFL 141
ePHD_BRPF1 cd15701
Extended PHD finger found in bromodomain and PHD finger-containing protein 1 (BRPF1) and ...
 603-717 7.11e-23

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: 94.76  E-value: 7.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALKPSDvEGLWVHVTCAWFRPEVGFLNHENMEPAVGLFKIPANSFLKVCTICKQT-HGSCVHCCK--CATH 679
Cdd:cd15701     1 CALCPNKGGAFKQTD-DGRWAHVVCALWIPEVCFANTVFLEPIDSIEHIPPARWKLTCYICKQRgSGACIQCHKanCYTA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 332646729  680 FHAMCASRAGYNMELHCLEKNGVQRT----RKSVYCSFHRKP 717
Cdd:cd15701    80 FHVTCAQQAGLYMKMEPVRETGANGTsfsvRKTAYCDIHTPP 121
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 190-283 9.01e-23

PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain binds to Histone-4 methylated at lysine-20, H4K20me, suggesting that it is methyl-lysine recognition motif. Removal of two conserved aromatic residues in a hydrophobic cavity created by this domain within the full-length protein, Pdp1, abolishes the interaction o f the protein with H4K20me3. In fission yeast, Set9 is the sole enzyme that catalyzes all three states of H4K20me, and Set9-mediated H4K20me is required for efficient recruitment of checkpoint protein Crb2 to sites of DNA damage. The methylation of H4K20 is involved in a diverse array of cellular processes, such as organizing higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression.


Pssm-ID: 459964 [Multi-domain]  Cd Length: 92  Bit Score: 93.26  E-value: 9.01e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729   190 GDLVWAKCgKRFPAWPAVVIDPISQAPDGVLKHCVPGAICVMFFGYSkdgtqrDYAWVRQGMVYPFTEFMDKFQDQTNLF 269
Cdd:pfam00855    1 GDLVWAKL-KGYPWWPARVVDPEELPENVLKPKKKDGEYLVRFFGDS------EFAWVKPKDLKPFDEGDEFEYLKKKKK 73

                           90
                   ....*....|....
gi 332646729   270 NYKASEFNKALEEA 283
Cdd:pfam00855   74 KKKKKAFKKALEEA 87
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 870-1017 2.82e-21

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: 94.28  E-value: 2.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  870 QRTENFRVC-FGKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQGkDCYLF-----KISEEIVIDATD 943
Cdd:cd10542    82 QRGRKVPLCiFRTSNGRGWGVKTLEDIKKGTFVMEYVGEIITSEEAERRGKIYDANG-RTYLFdldynDDDCEYTVDAAY 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  944 SGNIARLINHSCMPN--CYARIVSMGDGEDNRIVLIAKTNVAAGEELTYDYLFEVDE---------SEEIKVPCLCKAPN 1012
Cdd:cd10542   161 YGNISHFINHSCDPNlaVYAVWINHLDPRLPRIAFFAKRDIKAGEELTFDYLMTGTGgssestipkPKDVRVPCLCGSKN 240


                  ....*
gi 332646729 1013 CRKFM 1017
Cdd:cd10542   241 CRKYL 245
ePHD_BRPF3 cd15703
Extended PHD finger found in bromodomain and PHD finger-containing protein 3 (BRPF3) and ...
 603-714 5.07e-21

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: 89.34  E-value: 5.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALKPSDvEGLWVHVTCAWFRPEVGFLNHENMEPAVGLFKIPANSFLKVCTICKQT-HGSCVHCCK--CATH 679
Cdd:cd15703     1 CVLCPNKGGAFKQTS-DGRWAHVVCAIWIPEVCFANTVFLEPVEGVNNIPPARWKLTCYLCKQKgRGAAIQCHKvnCYTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 332646729  680 FHAMCASRAGYNMELHCLEKNGVQRT----RKSVYCSFH 714
Cdd:cd15703    80 FHVTCAQRAGLFMKIEPVRETGLNGTtftvRKTAYCENH 118
SET_EZH2 cd19218
SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...
 882-992 8.41e-21

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: 88.82  E-value: 8.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  882 SGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYrSQGKDCYLFKISEEIVIDATDSGNIARLINHSCMPNCYA 961
Cdd:cd19218    11 SDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVY-DKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYA 89

                          90       100       110
                  ....*....|....*....|....*....|.
gi 332646729  962 RiVSMGDGeDNRIVLIAKTNVAAGEELTYDY 992
Cdd:cd19218    90 K-VMMVNG-DHRIGIFAKRAIQTGEELFFDY 118
ePHD_ATX1_2_like cd15662
Extended PHD finger found in Arabidopsis thaliana ATX1, -2, and similar proteins; The extended ...
 603-714 1.44e-20

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: 87.91  E-value: 1.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALKPSdVEGLWVHVTCAWFRPEVGFLNHENMEPAVGLFKIPANSFLKVCTICKQTHGSCVHCCK--CATHF 680
Cdd:cd15662     1 CCLCPVVGGALKPT-TDGRWAHLACAIWIPETCLLDVKTMEPVDGINAISKERWELSCTICKQRYGACIQCSNnsCRVAY 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 332646729  681 HAMCASRAGYNMEL--HCLEKNGVQRTRKSVYCSFH 714
Cdd:cd15662    80 HPLCARAAGLCMEVadEGGEDPGDQGLRLLSYCPRH 115
PHD_ATX3_4_5_like cd15495
PHD finger found in Arabidopsis thaliana histone-lysine N-methyltransferase arabidopsis ...
 548-594 1.46e-20

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


Pssm-ID: 276970 [Multi-domain]  Cd Length: 47  Bit Score: 85.50  E-value: 1.46e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 332646729  548 RCAVCRWVEDWEENKMIICNRCQVAVHQECYGVSKSQDLTSWVCRAC 594
Cdd:cd15495     1 RCAVCNEGEDDDNNPLITCNRCQISVHQKCYGIREVDPDGSWVCRAC 47
SET_EZH1 cd19217
SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...
 870-994 1.69e-20

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: 88.59  E-value: 1.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  870 QRTENFRVCFGKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYrSQGKDCYLFKISEEIVIDATDSGNIAR 949
Cdd:cd19217     1 QRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVY-DKYMSSFLFNLNNDFVVDATRKGNKIR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 332646729  950 LINHSCMPNCYARIVsMGDGeDNRIVLIAKTNVAAGEELTYDYLF 994
Cdd:cd19217    80 FANHSVNPNCYAKVV-MVNG-DHRIGIFAKRAIQQGEELFFDYRY 122
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
 886-992 4.04e-20

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: 87.01  E-value: 4.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  886 GWGLFARKSIQEGEMIIEYRGVKVRRsvaDLREANYRSQGKDCYLFKIS-EEIVIDATDSGNIARLINHSCMPNCYARIV 964
Cdd:cd10522    14 GLGLFAAETIAKGEFVGEYTGEVLDR---WEEDRDSVYHYDPLYPFDLNgDILVIDAGKKGNLTRFINHSDQPNLELIVR 90

                          90       100
                  ....*....|....*....|....*...
gi 332646729  965 SmgDGEDNRIVLIAKTNVAAGEELTYDY 992
Cdd:cd10522    91 T--LKGEQHIGFVAIRDIKPGEELFISY 116
ePHD_BRPF2 cd15702
Extended PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and ...
 603-714 7.82e-20

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: 85.87  E-value: 7.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALKPSDVEgLWVHVTCAWFRPEVGFLNHENMEPAVGLFKIPANSFLKVCTICKQTH-GSCVHCCK--CATH 679
Cdd:cd15702     1 CVLCPNKGGAFKKTDDD-RWGHVVCALWIPEVGFANTVFIEPIDGVRNIPPARWKLTCYLCKQKGvGACIQCHKanCYTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 332646729  680 FHAMCASRAGYNMELHCL-EKNGVQRT---RKSVYCSFH 714
Cdd:cd15702    80 FHVTCAQKAGLYMKMEPVkEVTGGGTTfsvRKTAYCDAH 118
ePHD_AF10_like cd15672
Extended PHD finger found in protein AF-10 and AF-17; The extended plant homeodomain (ePHD) ...
 603-714 9.77e-20

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


Pssm-ID: 277142  Cd Length: 116  Bit Score: 85.59  E-value: 9.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALKPSDVEGlWVHVTCAWFRPEVGFLNHENMEPAVgLFKIPANSFLKVCTIC-------KQTHGSCVHCCK 675
Cdd:cd15672     1 CELCPHKDGALKRTDNGG-WAHVVCALYIPEVRFGNVATMEPII-LQDVPQDRFNKTCYICeeqgresKASTGACMQCNK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 332646729  676 --CATHFHAMCASRAGynmeLHCLEK-NGVQRTRKSVYCSFH 714
Cdd:cd15672    79 sgCKQSFHVTCAQMAG----LLCEEAgNYSDNVKYCGYCSYH 116
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
 886-1017 1.04e-19

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


Pssm-ID: 380988 [Multi-domain]  Cd Length: 142  Bit Score: 86.58  E-value: 1.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  886 GWGLFARKSIQEGEMIIEYRGVKVRRSvaDLREANYRSQGKDC---YLFKISEEIVIDATDSGNIARLINHSCMPNCYAR 962
Cdd:cd19211    13 GWGLIAKRDIKKGEFVNEYVGELIDEE--ECMARIKHAHENDIthfYMLTIDKDRIIDAGPKGNYSRFMNHSCQPNCETQ 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 332646729  963 IVSMGDgeDNRIVLIAKTNVAAGEELTYDYLFEVDESEeiKVPCLCKAPNCRKFM 1017
Cdd:cd19211    91 KWTVNG--DTRVGLFAVCDIPAGTELTFNYNLDCLGNE--KTVCRCGAPNCSGFL 141
ePHD_JADE2 cd15705
Extended PHD finger found in protein Jade-2 and similar proteins; The extended plant ...
 603-714 4.80e-19

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: 83.61  E-value: 4.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALKPSDVEGLWVHVTCAWFRPEVGFLNHENMEPAVGLFKIPANSFLKVCTICKQTHGSCVHCC--KCATHF 680
Cdd:cd15705     1 CLLCPKRGGALKPTRSGTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKECTGTCIQCSmpSCITAF 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 332646729  681 HAMCAsrAGYNMELHCLEKNGVQRTRKSvYCSFH 714
Cdd:cd15705    81 HVTCA--FDHGLEMRTTLADNDEVKFKS-FCLEH 111
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
 881-1017 1.08e-18

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: 86.97  E-value: 1.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  881 KSGIHGWGLFARKSIQEGEMIIEYRGvkvrrSVADLREANYRSQ----GKDCYLFKISE--------EIVIDATDSGNIA 948
Cdd:cd10544    96 KTPKKGWGLRTLEFIPKGRFVCEYAG-----EVIGFEEARRRTKsqtkGDMNYIIVLREhlssgkvlETFVDPTYIGNIG 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  949 RLINHSCMPNCY---ARIVSMGDgednRIVLIAKTNVAAGEELTYDYLFEVDESEEIKV-----------PCLCKAPNCR 1014
Cdd:cd10544   171 RFLNHSCEPNLFmvpVRVDSMVP----KLALFAARDIVAGEELSFDYSGEFSNSVESVTlarqdesksrkPCLCGAENCR 246


                  ...
gi 332646729 1015 KFM 1017
Cdd:cd10544   247 GFL 249
SET_SETDB-like cd10538
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
 867-992 3.92e-18

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: 84.34  E-value: 3.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  867 KHLQRTENFRVCFGKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQGkDCYLFKIS---------EEI 937
Cdd:cd10538    81 RVVQRGLQARLQVFRTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRGKIYDKSG-GSYLFDLDefsdsdgdgEEL 159

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 332646729  938 VIDATDSGNIARLINHSCMPNCYARIVSMgDGEDN---RIVLIAKTNVAAGEELTYDY 992
Cdd:cd10538   160 CVDATFCGNVSRFINHSCDPNLFPFNVVI-DHDDLrypRIALFATRDILPGEELTFDY 216
SET_SETD8 cd10528
SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2. ...
 886-992 6.19e-18

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: 81.47  E-value: 6.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  886 GWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANY-RSQGKDCYLFKI---SEEIVIDAT-DSGNIARLINHSCM-PNC 959
Cdd:cd10528    28 GRGVIATRPFEKGDFVVEYHGDLITITEAKKREALYaKDPSTGCYMYYFqykGKTYCVDATkESGRLGRLINHSKKkPNL 107

                          90       100       110
                  ....*....|....*....|....*....|...
gi 332646729  960 YARIVSMGDGEdnRIVLIAKTNVAAGEELTYDY 992
Cdd:cd10528   108 KTKLLVIDGVP--HLILVAKRDIKPGEELLYDY 138
ePHD_JADE1 cd15704
Extended PHD finger found in protein Jade-1 and similar proteins; The extended plant ...
 603-714 8.27e-18

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: 80.12  E-value: 8.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALKPSDVEGLWVHVTCAWFRPEVGFLNHENMEPAVGLFKIPANSFLKVCTICKQTHGSCVHCC--KCATHF 680
Cdd:cd15704     4 CLLCPKKGGAMKPTRSGTKWVHVSCALWIPEVSIGSPEKMEPITKVSHIPSSRWALVCSLCNEKVGASIQCSvkNCRTAF 83

                          90       100       110
                  ....*....|....*....|....*....|....
gi 332646729  681 HAMCASRAGYNMELHCLEKNGVqrtRKSVYCSFH 714
Cdd:cd15704    84 HVTCAFDRGLEMKTILAENDEV---KFKSYCPKH 114
ePHD_RNO cd15707
Extended PHD finger found in Drosophila melanogaster PHD finger protein rhinoceros (RNO) and ...
 603-714 1.02e-17

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: 79.95  E-value: 1.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALKPSDVEGLWVHVTCAWFRPEVGFLNHENMEPAVGLFKIPANSFLKVCTICKQTHGSCVHCC--KCATHF 680
Cdd:cd15707     1 CILCPNKGGAMKSTRSGTKWAHVSCALWIPEVSIGCVEKMEPITKISSIPASRWALICVLCRERTGACIQCSvkTCKTAY 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 332646729  681 HAMCASRAGYNMELHcLEKNGVQRTRKSVYCSFH 714
Cdd:cd15707    81 HVTCGFQHGLEMKTI-LDEESEDGVKLRSYCQKH 113
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
 886-1017 1.02e-17

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: 80.74  E-value: 1.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  886 GWGLFARKSIQEGEMIIEYRGvkvrrSVADLREANYR---SQGKDC---YLFKISEEIVIDATDSGNIARLINHSCMPNC 959
Cdd:cd19210    13 GWGLRCKTDIKKGEFVNEYVG-----ELIDEEECRARiryAQEHDItnfYMLTLDKDRIIDAGPKGNYARFMNHCCQPNC 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 332646729  960 YARIVSMGDgeDNRIVLIAKTNVAAGEELTYDYLFEVDESEeiKVPCLCKAPNCRKFM 1017
Cdd:cd19210    88 ETQKWTVNG--DTRVGLFALCDIKAGTELTFNYNLECLGNG--KTVCKCGAPNCSGFL 141
ePHD_JADE3 cd15706
Extended PHD finger found in protein Jade-3 and similar proteins; The extended plant ...
 603-693 2.99e-17

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: 78.61  E-value: 2.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALKPSDVEGLWVHVTCAWFRPEVGFLNHENMEPAVGLFKIPANSFLKVCTICKQTHGSCVHCC--KCATHF 680
Cdd:cd15706     1 CLLCPKTGGAMKATRTGTKWAHVSCALWIPEVSIACPERMEPITKVSHIPPSRWALVCSLCKLKTGACIQCSvkSCITAF 80

                          90
                  ....*....|...
gi 332646729  681 HAMCASRAGYNME 693
Cdd:cd15706    81 HVTCAFEHSLEMK 93
ePHD_JMJD2 cd15675
Extended PHD finger found in Jumonji domain-containing protein 2 (JMJD2) family of histone ...
 603-693 5.58e-17

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: 77.79  E-value: 5.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALKPSdVEGLWVHVTCAWFRPEVGFLNHENMEPaVGLFKIPANSFLKVCTICKQ------THGSCVHCC-- 674
Cdd:cd15675     1 CCLCCLRGGALKPT-TDGRWAHVVCAIAIPEVRFSNVPERGP-IDISKIPPARLKLKCIYCSKitksmsHMGACIQCStg 78

                          90
                  ....*....|....*....
gi 332646729  675 KCATHFHAMCASRAGYNME 693
Cdd:cd15675    79 KCTTSFHVTCAHAAGVQME 97
SET_NSD3 cd19212
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
 886-1017 1.11e-16

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: 77.66  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  886 GWGLFARKSIQEGEMIIEYRGVKVRRSVADLR-EANYRSQGKDCYLFKISEEIVIDATDSGNIARLINHSCMPNCYARIV 964
Cdd:cd19212    13 GWGLRTKRSIKKGEFVNEYVGELIDEEECRLRiKRAHENSVTNFYMLTVTKDRIIDAGPKGNYSRFMNHSCNPNCETQKW 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 332646729  965 SMGDgeDNRIVLIAKTNVAAGEELTYDYlfEVDESEEIKVPCLCKAPNCRKFM 1017
Cdd:cd19212    93 TVNG--DVRVGLFALCDIPAGMELTFNY--NLDCLGNGRTECHCGADNCSGFL 141
SET_EZH-like cd19168
SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb ...
 876-992 1.35e-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: 76.84  E-value: 1.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  876 RVCFGKSGIH-GWGLFARKSIQEGEMIIEYRGvkvrRSVADLrEANYRSQGKD----CYLFKISEEIVIDATDSGNIARL 950
Cdd:cd19168     2 AVVLGKSQLEcGLGLFAAEDIKEGEFVIEYTG----ELISHD-EGVRREHRRGdvsyLYLFEEQEGIWVDAAIYGNLSRY 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 332646729  951 INH----SCMPNCYARIvsMGDGEDNRIVLIAKTNVAAGEELTYDY 992
Cdd:cd19168    77 INHatdkVKTGNCMPKI--MYVNHEWRIKFTAIKDIKIGEELFFNY 120
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
 881-992 4.26e-16

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: 78.60  E-value: 4.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  881 KSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANyrsqgkDCYLFKI--------------------------- 933
Cdd:cd10545    92 KTAERGWGVRSWDSIPAGSFICEYVGELLDTSEADTRSGN------DDYLFDIdnrqtnrgwdggqrldvgmsdgerssa 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332646729  934 ----SEEIVIDATDSGNIARLINHSCMPNCYARIVSMgDGEDNRI---VLIAKTNVAAGEELTYDY 992
Cdd:cd10545   166 edeeSSEFTIDAGSFGNVARFINHSCSPNLFVQCVLY-DHNDLRLprvMLFAADNIPPLQELTYDY 230
PWWP cd05162
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
 190-286 9.01e-16

PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, is a small domain consisting of 100-150 amino acids and is composed of a five-stranded antiparallel beta-barrel followed by a helical region. It is found in numerous proteins that are involved in cell division, growth, and differentiation. Most PWWP-domain proteins seem to be nuclear, often DNA-binding, proteins that function as transcription factors regulating a variety of developmental processes. PWWP domains specifically recognize DNA and histone methylated lysines at the level of the nucleosome. Based on the fact that other regions of PWWP-domain proteins are responsible for nuclear localization and DNA-binding, is likely that the PWWP domain acts as a site for protein-protein binding interactions, influencing chromatin remodeling and thereby regulating transcriptional processes. Some PWWP-domain proteins have been linked to cancer or other diseases; some are known to function as growth factors.


Pssm-ID: 438958 [Multi-domain]  Cd Length: 86  Bit Score: 73.30  E-value: 9.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  190 GDLVWAKCgKRFPAWPAVVIDPiSQAPDGVLKHCVPGAICVMFFGYskdgtqRDYAWVRQGMVYPFTEFMDKFQdqtNLF 269
Cdd:cd05162     1 GDLVWAKL-KGYPWWPARVVDP-EELPEEVGKKKKKGGVLVQFFGD------NDYAWVKSKNIKPFEEGFKKEF---KKK 69

                          90
                  ....*....|....*..
gi 332646729  270 NYKASEFNKALEEAVLA 286
Cdd:cd05162    70 KKKSKKFKKAVEEAEEA 86
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 876-992 9.31e-16

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: 72.67  E-value: 9.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  876 RVCFGKSGIHGWGLFARKSIQEGEMIIeyrgvkvrrsvadlreanyrsqgkdcylfkiseeividatdsgnIARLINHSC 955
Cdd:cd08161     1 EIRPSTIPGAGFGLFATRDIPKGEVIG--------------------------------------------LARFINHSC 36

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 332646729  956 MPNCyaRIVSMGDGEDNRIVLIAKTNVAAGEELTYDY 992
Cdd:cd08161    37 EPNC--EFEEVYVGGKPRVFIVALRDIKAGEELTVDY 71
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
 888-994 1.54e-15

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: 73.85  E-value: 1.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  888 GLFARKSIQEGEMIIEYRGVKVRRSvaDLREANYRSQGKDCYLFKIS----EEIVIDATDSGNIARLINHSCMPNCYARI 963
Cdd:cd10529    18 GLVATEDISPGEPILEYKGEVSLRS--EFKEDNGFFKRPSPFVFFYDgfegLPLCVDARKYGNEARFIRRSCRPNAELRH 95

                          90       100       110
                  ....*....|....*....|....*....|...
gi 332646729  964 VSMGDGEdNRIVLIAKTNVAAGEELT--YDYLF 994
Cdd:cd10529    96 VVVSNGE-LRLFIFALKDIRKGTEITipFDYDY 127
ePHD_AF10 cd15708
Extended PHD finger found in protein AF-10 and similar proteins; The extended plant ...
 603-714 1.61e-15

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


Pssm-ID: 277178  Cd Length: 129  Bit Score: 73.96  E-value: 1.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALKPSDvEGLWVHVTCAWFRPEVGFLNHENMEPAVgLFKIPANSFLKVCTIC-------KQTHGSCVHCCK 675
Cdd:cd15708     5 CELCPHKDGALKRTD-NGGWAHVVCALYIPEVQFANVSTMEPIV-LQSVPHERYNKTCYICdeqgresKAATGACMTCNK 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 332646729  676 --CATHFHAMCASRAGynmeLHCLEK-NGVQRTRKSVYCSFH 714
Cdd:cd15708    83 hgCRQAFHVTCAQLAG----LLCEEEgNGADNVQYCGYCKYH 120
SET_SUV39H_DIM5-like cd19473
SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...
 886-1017 3.27e-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: 76.97  E-value: 3.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  886 GWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYR-SQGKDCYLF---KISEEIVIDATDSGNI-----------ARL 950
Cdd:cd19473   117 GWGVRSTVDIKRGQFVDCYVGEIITPEEAQRRRDAATiAQRKDVYLFaldKFSDPDSLDPRLRGDPyeidgefmsgpTRF 196

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332646729  951 INHSCMPNC--YARIVSMGDGEDNRIVLIAKTNVAAGEELTYDYL---------FEVDESEEIKVPCLCKAPNCRKFM 1017
Cdd:cd19473   197 INHSCDPNLriFARVGDHADKHIHDLAFFAIKDIPRGTELTFDYVdgvtgldddAGDEEKEKEMTKCLCGSPKCRGYL 274
PWWP_NSD_rpt2 cd05838
second PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
 188-286 4.29e-15

second PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein family consists 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 in suppressing cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play nonredundant 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 (C5HCH). This model corresponds to the second PWWP domain. The family also includes Drosophila melanogaster maternal-effect sterile 4 (dMes4) that may act as a histone-lysine N-methyltransferase required for wing morphogenesis. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438963 [Multi-domain]  Cd Length: 96  Bit Score: 71.50  E-value: 4.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  188 TVGDLVWAKCGkRFPAWPAVVIDPiSQAPDGVLK-HCVPGAICVMFFGyskdgtQRDYAWVRQGMVYPFTEfMDKFQDQT 266
Cdd:cd05838     1 LYGDIVWVKLG-NYRWWPAEILHP-REVPDNIQSlPHPPGEFPVRFFG------SHDYYWVHRGRVFLFEE-GDKGSKEK 71

                          90       100
                  ....*....|....*....|
gi 332646729  267 NLFNYKASeFNKALEEAVLA 286
Cdd:cd05838    72 SKKSLDKS-FKRALKEANEA 90
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 869-1017 8.94e-15

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: 75.31  E-value: 8.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  869 LQRTENFRVC-FGKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQGKdCYLFK---ISEEIVIDATDS 944
Cdd:cd10525    80 VQKGIQYDLCiFRTDNGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGA-TYLFDldyVEDVYTVDAAYY 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  945 GNIARLINHSCMPN--CYARIVSMGDGEDNRIVLIAKTNVAAGEELTYDYLFEVD----ES-----------------EE 1001
Cdd:cd10525   159 GNISHFVNHSCDPNlqVYNVFIDNLDERLPRIALFATRTIRAGEELTFDYNMQVDpvdaEStkmdsnfglaglpgspkKR 238

                         170
                  ....*....|....*.
gi 332646729 1002 IKVPCLCKAPNCRKFM 1017
Cdd:cd10525   239 VRIECKCGVRSCRKYL 254
ePHD_PHF14 cd15674
Extended PHD finger found in PHD finger protein 14 (PHF14) and similar proteins; The extended ...
 603-689 1.50e-14

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


Pssm-ID: 277144  Cd Length: 114  Bit Score: 70.87  E-value: 1.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALKPSDVeGLWVHVTCAWFRPEVGFLNHENMEPaVGLFKIPANSF-LKVCTICKQ----THGSCVHC--CK 675
Cdd:cd15674     1 CELCPNRGGIFKETDT-GRWVHLVCALYTPGVAFGDVDKLSP-VTLTEMNYSKWgARECSLCEDprfaRTGVCISCdaGM 78

                          90
                  ....*....|....
gi 332646729  676 CATHFHAMCASRAG 689
Cdd:cd15674    79 CKSYFHVTCAQREG 92
SET_SETDB1 cd10517
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
 938-1015 1.75e-14

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: 75.02  E-value: 1.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  938 VIDATDSGNIARLINHSCMPNCYARIVsMGDGEDNR---IVLIAKTNVAAGEELTYDYLFEVDESEEIKVPCLCKAPNCR 1014
Cdd:cd10517   206 IIDAKSEGNLGRYLNHSCSPNLFVQNV-FVDTHDLRfpwVAFFASRYIRAGTELTWDYNYEVGSVPGKVLYCYCGSSNCR 284


                  .
gi 332646729 1015 K 1015
Cdd:cd10517   285 G 285
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
 187-283 1.79e-14

PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called 3-hydroxyisobutyrate dehydrogenase-like protein, cytokine-like nuclear factor N-PAC, nuclear protein NP60, or nuclear protein of 60 kDa, is a putative oxidoreductase that is recruited on chromatin and promotes KDM1B demethylase activity. It recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3). GLYR1 enhances the activity of MAP2K4 and MAP2K6 kinases to phosphorylate p38-alpha. In addition to the PWWP domain, GLYR1 also contains an AT-hook and a C-terminal NAD-binding domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438961 [Multi-domain]  Cd Length: 86  Bit Score: 69.56  E-value: 1.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  187 FTVGDLVWAKCgKRFPAWPAVVIDPisqaPDGVLKhcvPGAI----CVMFFGyskdgtQRDYAWVRQGMVYPFTEFMDKF 262
Cdd:cd05836     1 FKIGDLVWAKM-KGFPPWPGKIVNP----PPDLKK---PPRKkkmhCVYFFG------SENYAWIEDENIKPYEEFKEEM 66

                          90       100
                  ....*....|....*....|.
gi 332646729  263 qdqtnLFNYKASEFNKALEEA 283
Cdd:cd05836    67 -----LKSKKSAGFKDAVEAI 82
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 869-1017 3.75e-14

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: 73.39  E-value: 3.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  869 LQRTENFRVC-FGKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQGkDCYLFKI---SEEIVIDATDS 944
Cdd:cd10532    78 VQKGTQYSLCiFRTSNGRGWGVKTLQKIKKNSFVMEYVGEVITSEEAERRGQFYDSKG-ITYLFDLdyeSDEFTVDAARY 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  945 GNIARLINHSCMPN--CYARIVSMGDGEDNRIVLIAKTNVAAGEELTYDYLF---------EVDES---EEIKVPCLCKA 1010
Cdd:cd10532   157 GNVSHFVNHSCDPNlqVFNVFIDNLDTRLPRIALFSTRTIKAGEELTFDYQMkgsgdlssdSIDNSpakKRVRTVCKCGA 236


                  ....*..
gi 332646729 1011 PNCRKFM 1017
Cdd:cd10532   237 VTCRGYL 243
ePHD_JMJD2B cd15714
Extended PHD finger found in Jumonji domain-containing protein 2B (JMJD2B); The extended plant ...
 603-693 6.35e-14

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: 68.81  E-value: 6.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALKPSdVEGLWVHVTCAWFRPEVGFLNHENMEPaVGLFKIPANSFLKVCTIC----KQTHGSCVHCC--KC 676
Cdd:cd15714     1 CCLCNLRGGALQMT-TDERWVHVICAIAVPEARFLNVIERHP-VDVSAIPEQRWKLKCVYCrkrmKKVSGACIQCSydHC 78

                          90
                  ....*....|....*..
gi 332646729  677 ATHFHAMCASRAGYNME 693
Cdd:cd15714    79 STSFHVTCAHAAGVVME 95
SET_SUV39H_Clr4-like cd20073
SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 ...
 886-1017 8.78e-14

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: 72.60  E-value: 8.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  886 GWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQGKdCYLF-------KISEEIVIDATDSGNIARLINHSCMPN 958
Cdd:cd20073   104 GWGLRCPRFIKAGTFIGVYLGEVITQSEAEIRGKKYDNVGV-TYLFdldlfedQVDEYYTVDAQYCGDVTRFINHSCDPN 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332646729  959 --CYARIVSMGDGEDNRIVLIAKTNVAAGEELTYDYLFEVDESE---------------EIKVPCLCKAPNCRKFM 1017
Cdd:cd20073   183 laIYSVLRDKSDSKIYDLAFFAIKDIPALEELTFDYSGRNNFDQlgfignrsnskyinlKNKRPCYCGSANCRGWL 258
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
 886-1015 2.03e-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: 2.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  886 GWGLFARKSIQEGEMIIEYRGVKVRRSVA---------DLREANYRSQGKDCYLF----KISEEI-VIDATDSGNIARLI 951
Cdd:cd10523   119 GWGVRCLDDIDKGTFVCIYAGRVLSRARSpteplppklELPSENEVEVVTSWLILskkrKLRENVcFLDASKEGNVGRFL 198

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332646729  952 NHSCMPNCYARIVSMGDGEDNRIVLIAKTN--VAAGEELTYDYLFEVDESEEIKVPCLCKAPNCRK 1015
Cdd:cd10523   199 NHSCCPNLFVQNVFVDTHDKNFPWVAFFTNrvVKAGTELTWDYSYDAGTSPEQEIPCLCGVNKCQK 264
ePHD_JMJD2A cd15713
Extended PHD finger (ePHD) found in Jumonji domain-containing protein 2A (JMJD2A); The ...
 603-693 2.05e-13

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


Pssm-ID: 277183  Cd Length: 110  Bit Score: 67.31  E-value: 2.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALKPSDvEGLWVHVTCAWFRPEVGFLNHENMEPaVGLFKIPANSFLKVCTIC----KQTHGSCVHCC--KC 676
Cdd:cd15713     1 CCLCSLRGGALQRAN-DDKWVHVMCAVAVLEARFVNIAERSP-VDVSKIPLQRFKLKCIFCkkrrKRTAGCCVQCShgRC 78

                          90
                  ....*....|....*..
gi 332646729  677 ATHFHAMCASRAGYNME 693
Cdd:cd15713    79 PTSFHASCAQAAGVMMQ 95
ePHD_AF17 cd15709
Extended PHD finger found in protein AF-17 and similar proteins; The extended plant ...
 603-714 4.47e-13

Extended PHD finger found in protein AF-17 and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of AF-17. AF-17, also termed ALL1-fused gene from chromosome 17 protein, is encoded by gene AF17 that has been identified in hematological malignancies as a translocation partner of the mixed lineage leukemia gene MLL. It is a putative transcription factor that may play a role in multiple signaling pathways. It is involved in chromatin-mediated gene regulation mechanisms. It functions as a component of the multi-subunit Dot1 complex (Dotcom) and plays a role in the Wnt/Wingless signaling pathway. It also seems to be a downstream target of the beta-catenin/T-cell factor pathway, and participates in G2-M progression. Moreover, it may function as an important regulator of ENaC-mediated Na+ transport and thus blood pressure. AF-17 contains an N-terminal plant homeodomain (PHD) finger followed by a non-canonical ePHD finger.


Pssm-ID: 277179  Cd Length: 125  Bit Score: 67.01  E-value: 4.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALKPSDvEGLWVHVTCAWFRPEVGFLNHENMEPAVGLFkIPANSFLKVCTIC-------KQTHGSCVHCCK 675
Cdd:cd15709     5 CELCPHKDGALKRTD-NGGWAHVVCALYIPEVQFANVLTMEPIVLQY-VPHDRFNKTCYICeeqgresKAASGACMTCNR 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 332646729  676 --CATHFHAMCASRAGYNMELHCLEKNGVQRTRksvYCSFH 714
Cdd:cd15709    83 hgCRQAFHVTCAQMAGLLCEEEVLEVDNVKYCG---YCKYH 120
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
 624-714 5.01e-13

PHD-like zinc-binding domain; The members of this family are annotated as containing PHD domain, but the zinc-binding region here is not typical of PHD domains. The conformation here is a well-conserved cysteine-histidine rich region spanning 90 residues, where the Cys and His are arranged as HxxC(31)CxxC(6)CxxCxxxxCxxxxHxxC (21)CxxH.


Pssm-ID: 463977 [Multi-domain]  Cd Length: 88  Bit Score: 65.43  E-value: 5.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729   624 HVTCAWFRPEVGFL-NHENMEPAVGLFKIPANSFLKVCTICKQTHGSCVHCCK--CATHFHAMCASRAGYNMELhclekN 700
Cdd:pfam13771    1 HVVCALWSPELVQRgNDSMGFPIEDIEKIPKRRWKLKCYLCKKKGGACIQCSKknCRRAFHVTCALEAGLLMQF-----D 75

                           90
                   ....*....|....
gi 332646729   701 GVQRTRKSvYCSFH 714
Cdd:pfam13771   76 EDNGTFKS-YCKKH 88
ePHD_JMJD2C cd15715
Extended PHD finger found in Jumonji domain-containing protein 2C (JMJD2C); The extended plant ...
 603-693 1.01e-12

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


Pssm-ID: 277185  Cd Length: 110  Bit Score: 65.36  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALKPSDvEGLWVHVTCAWFRPEVGFLNHENMEPaVGLFKIPANSFLKVCTIC----KQTHGSCVHCC--KC 676
Cdd:cd15715     1 CCLCNLRGGALKQTS-DDKWAHVMCAVALPEVRFINVVERTP-IDISRIPLQRLKLKCIFCrnriKRVSGACIQCSygRC 78

                          90
                  ....*....|....*..
gi 332646729  677 ATHFHAMCASRAGYNME 693
Cdd:cd15715    79 PASFHVTCAHAAGVLME 95
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 886-1014 1.80e-12

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


Pssm-ID: 380933 [Multi-domain]  Cd Length: 231  Bit Score: 68.04  E-value: 1.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  886 GWGLFARKSIQEGEMIIEYRGVKVRRSVADLREanyrsqgKDCYLF----KISEEIVIDATDSGNIARLINHSCMPNCYA 961
Cdd:cd10535   102 GWGVRSLQDIPPGTFVCEYVGELISDSEADVRE-------EDSYLFdldnKDGEVYCIDARFYGNVSRFINHHCEPNLVP 174

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 332646729  962 RIVSMG--DGEDNRIVLIAKTNVAAGEELTYDYLFEVDESEEIKVPCLCKAPNCR 1014
Cdd:cd10535   175 VRVFMAhqDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCR 229
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 886-1014 1.87e-12

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: 68.13  E-value: 1.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  886 GWGLFARKSIQEGEMIIEYRGVKVRRSVADLREanyrsqgKDCYLF----KISEEIVIDATDSGNIARLINHSCMPNCYA 961
Cdd:cd10543   102 GWGVRALQDIPKGTFVCEYIGELISDSEADSRE-------DDSYLFdldnKDGETYCIDARRYGNISRFINHLCEPNLIP 174

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 332646729  962 RIVSMG--DGEDNRIVLIAKTNVAAGEELTYDYlfeVDESEEIK---VPCLCKAPNCR 1014
Cdd:cd10543   175 VRVFVEhqDLRFPRIAFFASRDIKAGEELGFDY---GEKFWRIKgkyFTCRCGSPKCK 229
SET_SpSET3-like cd19183
SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...
 888-998 1.87e-12

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: 66.66  E-value: 1.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  888 GLFARKSIQEGEMIIEYRGVkvrrsVAdlREANYRSQGKDCY----------LFKISEEIVIDATDSGNIARLINHSCMP 957
Cdd:cd19183    15 GLFADRPIPAGDPIQELLGE-----IG--LQSEYIADPENQYqilgapkphvFFHPQSPLYIDTRRSGSVARFIRRSCRP 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 332646729  958 NCYARIVSMGDGEDNRIVLIAKTNVAAGEELTYDYLFEVDE 998
Cdd:cd19183    88 NAELVTVASDSGSVLKFVLYASRDISPGEEITIGWDWDNPH 128
SET_SETDB cd10541
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...
 886-1015 2.21e-11

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: 64.87  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  886 GWGLFARKSIQEGEMIIEYRGVKVRRsvaDLREANYRSQGKDCY--LFKISEEI-VIDATDSGNIARLINHSCMPNCYAR 962
Cdd:cd10541   103 GWGIRCLDDIAKGTFVCIYAGKILTD---DFADKEGLEMGDEYFanLDHIEESCyIIDAKLEGNLGRYLNHSCSPNLFVQ 179

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 332646729  963 IVSMgDGEDNRIVLIA---KTNVAAGEELTYDYLFEVDESEEIKVPCLCKAPNCRK 1015
Cdd:cd10541   180 NVFV-DTHDLRFPWVAffaSKRIKAGTELTWDYNYEVGSVEGKELLCCCGSNECRG 234
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 886-1014 2.47e-11

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: 65.04  E-value: 2.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  886 GWGLFARKSIQEGEMIIEYRGVKVRRSVADLREanyrsqgKDCYLF----KISEEIVIDATDSGNIARLINHSCMPNCYA 961
Cdd:cd10533   102 GWGVRALQTIPQGTFICEYVGELISDAEADVRE-------DDSYLFdldnKDGEVYCIDARYYGNISRFINHLCDPNIIP 174

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 332646729  962 RIVSM--GDGEDNRIVLIAKTNVAAGEELTYDYLFEVDESEEIKVPCLCKAPNCR 1014
Cdd:cd10533   175 VRVFMlhQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCK 229
ePHD_Snt2p_like cd15667
Extended PHD finger found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) ...
 590-685 3.48e-11

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


Pssm-ID: 277137  Cd Length: 141  Bit Score: 62.01  E-value: 3.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  590 VCRACETPDIERDCCLCPVKGGALKPSDVeGLWVHVTCAWFRPEVGFLNHENMEPAVGLFKIPANSFLKVCTICKQTHGS 669
Cdd:cd15667     3 LCNAKESNYELAKKQSPRTRPDALKCTSN-GTWCHVLCALFNEDIKFGNSKSLQPILNTESVLLKGSRQKCEICKVSGGG 81

                          90
                  ....*....|....*.
gi 332646729  670 CVHCCKCATHFHAMCA 685
Cdd:cd15667    82 LVKCEVCDDRFHVSCA 97
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 187-256 4.40e-10

domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 56.20  E-value: 4.40e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332646729    187 FTVGDLVWAKCgKRFPAWPAVVIDPiSQAPDGVLK-----HCVPgaicVMFFGyskdgtQRDYAWVRQGMVYPFT 256
Cdd:smart00293    1 FKPGDLVWAKM-KGFPWWPALVISP-KMTPDNIMKrksdeNLYP----VLFFG------DKDTAWIPSSKLFPLT 63
PHD_TCF19_like cd15517
PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ...
 365-415 6.44e-10

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: 55.63  E-value: 6.44e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 332646729  365 CGICKRIWHPsDDGDWVCCDGCDVWVHAECDNITNERFKELEhnNYYCPDC 415
Cdd:cd15517     2 CGICNLETAA-VDELWVQCDGCDKWFHQFCLGLSNERYADED--KFKCPNC 49
PHD_BRPF_JADE_like cd15492
PHD finger found in BRPF proteins, Jade proteins, protein AF-10, AF-17, and similar proteins; ...
 548-594 1.13e-09

PHD finger found in BRPF proteins, Jade proteins, protein AF-10, AF-17, and similar proteins; The family includes BRPF proteins, Jade proteins, protein AF-10 and AF-17. BRPF proteins are scaffold proteins that form monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complexes with other regulatory subunits, such as inhibitor of growth 5 (ING5) and Esa1-associated factor 6 ortholog (EAF6). BRPF proteins have multiple domains, including a canonical Cys4HisCys3 plant homeodomain (PHD) zinc finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. PHD and ePHD fingers both bind to lysine 4 of histone H3 (K4H3), bromodomains interact with acetylated lysines on N-terminal tails of histones and other proteins, and PWWP domains show histone-binding and chromatin association properties. Jade proteins are required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and EAF6, to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. AF-10, also termed ALL1 (acute lymphoblastic leukemia)-fused gene from chromosome 10 protein, is a transcription factor that has been implicated in the development of leukemia following chromosomal rearrangements between the AF10 gene and one of at least two other genes, MLL and CALM. AF-17, also termed ALL1-fused gene from chromosome 17 protein, is a putative transcription factor that may play a role in multiple signaling pathways. All Jade proteins, AF-10, and AF-17 contain a canonical PHD finger followed by a non-canonical ePHD finger. This model corresponds to the canonical PHD finger.


Pssm-ID: 276967 [Multi-domain]  Cd Length: 46  Bit Score: 54.55  E-value: 1.13e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 332646729  548 RCAVCRWVEDWEENKMIICNRCQVAVHQECYGVSKSQDlTSWVCRAC 594
Cdd:cd15492     1 VCDVCLDGESEDDNEIVFCDGCNVAVHQSCYGIPLIPE-GDWFCRKC 46
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
 882-1001 2.60e-09

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: 56.23  E-value: 2.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  882 SGIHGWGLFARKSIQEGEMIIEYRgvKVRRSVADLREANYRSQGKDCYLFKIseeividatdsgniARLINHSCMPNCYA 961
Cdd:cd20071     6 EGSKGRGLVATRDIEPGELILVEK--PLVSVPSNSFSLTDGLNEIGVGLFPL--------------ASLLNHSCDPNAVV 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 332646729  962 RIVsmgdgEDNRIVLIAKTNVAAGEELTYDYLFEVDESEE 1001
Cdd:cd20071    70 VFD-----GNGTLRVRALRDIKAGEELTISYIDPLLPRTE 104
PWWP_BRPF cd05839
PWWP domain found in the bromodomain and PHD finger-containing (BRPF) protein family; The BRPF ...
 187-283 5.23e-09

PWWP domain found in the bromodomain and PHD finger-containing (BRPF) protein family; The BRPF family of proteins includes BRPF1, BRD1/BRPF2, and BRPF3. They are scaffold proteins that form monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complexes with other regulatory subunits, such as inhibitor of growth 5 (ING5) and Esa1-associated factor 6 ortholog (EAF6). BRPF proteins have multiple domains, including a plant homeodomain (PHD) zinc finger followed by a non-canonical extended PHD (ePHD) finger, C2HC5HC2H, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. The 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: 438964  Cd Length: 106  Bit Score: 54.58  E-value: 5.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  187 FTVGDLVWAKCGKrFPAWPAVVID----------PISQAPDGVLKHCVPGAICVMFFgyskdGTQRDYAWVRQGMVYPFt 256
Cdd:cd05839     1 LEPGDLVWAKCRG-YPWYPAEIVDpkdpkegngvPIPVPPDRVLKKSNEKLYLVLFF-----DAKRTWGWLPRNKLRPL- 73

                          90       100
                  ....*....|....*....|....*..
gi 332646729  257 eFMDKFQDQTNLFNYKASEFNKALEEA 283
Cdd:cd05839    74 -GVDEELDKLKLSEAKKSKRRKEVRKA 99
PWWP_HRP cd05834
PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The ...
 187-282 5.74e-09

PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The HRP family includes hepatoma-derived growth factor (HDGF), and HDGF-related proteins (HRPs). HDGF, also called high mobility group protein 1-like 2 (HMG-1L2), is a heparin-binding protein that acts as a transcriptional repressor with mitogenic activity for fibroblasts. It is a prognostic factor in several types of cancer. HDGFL1 is also called PWWP domain-containing protein 1 (PWWP1). Its biological function remains unclear. HDGFL2, also called HDGF-related protein 2 (HRP-2), or hepatoma-derived growth factor 2 (HDGF-2), is involved in cellular growth control, through the regulation of cyclin D1 expression. HDGFL3, also called HDGF-related protein 3 (HRP-3), enhances DNA synthesis and may play a role in cell proliferation. The family also includes PC4 and SFRS1-interacting protein (PSIP) and similar proteins. PSIP, also called CLL-associated antigen KW-7, dense fine speckles 70 kDa protein (DFS 70), lens epithelium-derived growth factor (LEDGF), or transcriptional coactivator p75/p52, acts as a transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Members of the HRP family contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438959 [Multi-domain]  Cd Length: 82  Bit Score: 53.71  E-value: 5.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  187 FTVGDLVWAKCgKRFPAWPAVVIDPISQAPDGVLKHcvPgaicVMFFgyskdGTQrDYAWVRQGMVYPFTEFMDKFQDQT 266
Cdd:cd05834     1 FKPGDLVFAKV-KGYPPWPARIDEIPEGAKIPKNKY--P----VFFY-----GTH-ETAFLKPKDLFPYEENKEKYGKPR 67

                          90
                  ....*....|....*.
gi 332646729  267 nlfNYKAseFNKALEE 282
Cdd:cd05834    68 ---KRKG--FNEGLWE 78
PWWP_ScIOC4-like cd05840
PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar ...
 190-283 7.12e-09

PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar proteins; ScIOC4 functions as a component of the ISW1B complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW1B complex acts within coding regions to control the amount of RNA polymerase II released into productive elongation and to coordinate elongation with termination and pre-mRNA processing. The family also includes Schizosaccharomyces pombe PWWP domain-containing proteins 1 and 2 (SpPDP1 and SpPDP2). SpPDP1 associates with Set9 to regulate its chromatin localization and methyltransferase activity towards H4K20. Members of this family contain a PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438965  Cd Length: 94  Bit Score: 53.84  E-value: 7.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  190 GDLVWAKCgKRFPAWPAVVIdPISQAPDGVLKHCV------PGAICVMFFGyskDGtqrDYAWVRQGMVYPFT-EFMDKF 262
Cdd:cd05840     1 GDLVLAKV-KGYPPWPAMVL-PEELLPKNVLKAKKrkpkskKTVYPVQFFP---DN---EYYWVSPSSLKPLTkEEIDKF 72

                          90       100
                  ....*....|....*....|.
gi 332646729  263 QDqtnlfnyKASEFNKALEEA 283
Cdd:cd05840    73 LS-------KSKRKNKDLIEA 86
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 364-417 8.13e-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: 52.49  E-value: 8.13e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 332646729   364 YCGICKRiwhPSDDGDWVCCDGCDVWVHAECDNITnERFKELEHNNYYCPDCKV 417
Cdd:pfam00628    1 YCAVCGK---SDDGGELVQCDGCDDWFHLACLGPP-LDPAEIPSGEWLCPECKP 50
PHD_2 pfam13831
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 561-594 8.61e-09

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


Pssm-ID: 463990 [Multi-domain]  Cd Length: 35  Bit Score: 51.96  E-value: 8.61e-09
                           10        20        30
                   ....*....|....*....|....*....|....
gi 332646729   561 NKMIICNRCQVAVHQECYGVSKSQDLTSWVCRAC 594
Cdd:pfam13831    2 SPLVYCSKCSVQVHASCYGVPPIPDGDGWKCRRC 35
PWWP_ZCWPW2 cd20146
PWWP domain found in zinc finger CW-type PWWP domain protein 2 (ZCWPW2) and similar proteins; ...
 179-283 1.87e-08

PWWP domain found in zinc finger CW-type PWWP domain protein 2 (ZCWPW2) and similar proteins; ZCWPW2 is a histone H3K4me3 reader. In addition to the PWWP domain, ZCWPW2 contains a zinc finger CW (zf-CW) domain that is a histone modification reader for the histone H3 tail with trimethylated K4. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438974  Cd Length: 113  Bit Score: 53.45  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  179 KGVYkpEEFTVGDLVWAK-CGkrFPAWPAVVI-DPIS------QAPDGVLK-HcvpgaicVMFFGYSkdgtqRDYAWVRQ 249
Cdd:cd20146     3 KYVY--SQLPLGSLVWAKmTG--YPRWPAILTpDPICgeyvdyDEDGEVEKyH-------VEFLGKP-----HSHAWISA 66

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 332646729  250 GMVYPF-TEFMDKFQDQTNLFNYKASeFNKALEEA 283
Cdd:cd20146    67 KSVEPYnSNTKTPKCKTKKSKKRKKS-YESALEEA 100
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
 876-992 2.11e-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: 53.03  E-value: 2.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  876 RVCFGKSGIHGWGLFARKSIQEGEmIIEYRGVKVRRsvadlREANYRSQGK--DCYLFKISEeividatDSGNIA----R 949
Cdd:cd10540     1 RLEVKPSTLKGRGVFATRPIKKGE-VIEEAPVIVLP-----KEEYQHLCKTvlDHYVFSWGD-------GCLALAlgygS 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 332646729  950 LINHSCMPNCYARIvsmgDGEDNRIVLIAKTNVAAGEELTYDY 992
Cdd:cd10540    68 MFNHSYTPNAEYEI----DFENQTIVFYALRDIEAGEELTINY 106
PWWP_NSD3_rpt2 cd20166
second PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar ...
 191-283 3.01e-08

second PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar proteins; NSD3, also called histone-lysine N-methyltransferase NSD3, protein whistle, 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 finger motifs, and an NSD-specific Cys-His rich domain (C5HCH). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD domains are involved in protein-protein interactions. This model corresponds to the second PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438994  Cd Length: 95  Bit Score: 52.28  E-value: 3.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  191 DLVWAKCGKrFPAWPAVVIDPISqAPDGV--LKHCVpGAICVMFFGyskdgtQRDYAWVRQGMVYPFTEFMDKFQDQTNL 268
Cdd:cd20166     4 QIVWVKLGN-YRWWPAEICNPRS-VPLNIqgLKHDI-GDFPVFFFG------SHDYYWVHQGRVFPYVEGDKSFAEGQTS 74

                          90
                  ....*....|....*
gi 332646729  269 FNykaSEFNKALEEA 283
Cdd:cd20166    75 IN---KTFKKALEEA 86
PHD_JADE cd15573
PHD finger found in proteins Jade-1, Jade-2, Jade-3, and similar proteins; This family ...
 549-594 3.41e-08

PHD finger found in proteins Jade-1, Jade-2, Jade-3, and similar proteins; This family includes proteins Jade-1 (PHF17), Jade-2 (PHF15), and Jade-3 (PHF16), each of which is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and EAF6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. This family also contains Drosophila melanogaster PHD finger protein rhinoceros (RNO). It is a novel plant homeodomain (PHD)-containing nuclear protein that may function as a transcription factor that antagonizes Ras signaling by regulating transcription of key EGFR/Ras pathway regulators in the Drosophila eye. All Jade proteins contain a canonical Cys4HisCys3 PHD finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, both of which are zinc-binding motifs. This model corresponds to the canonical Cys4HisCys3 PHD finger.


Pssm-ID: 277048 [Multi-domain]  Cd Length: 46  Bit Score: 50.49  E-value: 3.41e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 332646729  549 CAVCRWVEDWEENKMIICNRCQVAVHQECYGVSKSQDlTSWVCRAC 594
Cdd:cd15573     2 CDVCRSPDSEEGNEMVFCDKCNICVHQACYGIQKIPE-GSWLCRTC 46
PHD_JADE3 cd15681
PHD finger found in protein Jade-3 and similar proteins; Jade-3, also termed PHD finger ...
 549-594 4.44e-08

PHD finger found in protein Jade-3 and similar proteins; Jade-3, also termed PHD finger protein 16 (PHF16), is a plant homeodomain (PHD) zinc finger protein that is closely related to Jade-1, which functions as an essential regulator of multiple cell signaling pathways. Like Jade-1, Jade-3 is required for ING4 and ING5 to associate with histone acetyl transferase (HAT) HBO1 and Eaf6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. Jade-3 contains a canonical Cys4HisCys3 PHD domain followed by a non-canonical extended PHD (ePHD) domain, Cys2HisCys5HisCys2His, both of which are zinc-binding motifs. This model corresponds to the canonical Cys4HisCys3 PHD finger.


Pssm-ID: 277151 [Multi-domain]  Cd Length: 50  Bit Score: 50.35  E-value: 4.44e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 332646729  549 CAVCRWVEDWEENKMIICNRCQVAVHQECYGVSKSQDlTSWVCRAC 594
Cdd:cd15681     2 CDVCRSPDSEEGNDMVFCDKCNICVHQACYGILKVPE-GSWLCRTC 46
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 364-415 1.67e-07

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: 48.75  E-value: 1.67e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 332646729    364 YCGICKRiwhPSDDGDWVCCDGCDVWVHAECDNITNERFKELEHnnYYCPDC 415
Cdd:smart00249    1 YCSVCGK---PDDGGELLQCDGCDRWYHQTCLGPPLLEEEPDGK--WYCPKC 47
PHD_ARID4_like cd15615
PHD finger found in Arabidopsis thaliana AT-rich interactive domain-containing protein 4 ...
 364-415 2.81e-07

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: 48.24  E-value: 2.81e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 332646729  364 YCGICKRIWHPS--DDGDWVCCDGCDVWVHAECDNITN-ERFKELEHNN--YYCPDC 415
Cdd:cd15615     1 FCILCGQVYEENegDEKEWVQCDSCSEWVHFECDGRTGlGAFKYAKSDGlqYVCPRC 57
PHD_JADE2 cd15680
PHD finger found in protein Jade-2 and similar proteins; Jade-2, also termed PHD finger ...
 549-594 3.50e-07

PHD finger found in protein Jade-2 and similar proteins; Jade-2, also termed PHD finger protein 15 (PHF15), is a plant homeodomain (PHD) zinc finger protein that is closely related to Jade-1, which functions as an essential regulator of multiple cell signaling pathways. Like Jade-1, Jade-2 is required for ING4 and ING5 to associate with histone acetyltransferase (HAT) HBO1 and Eaf6 to form a HBO1 complex that has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3, and is responsible for the bulk of histone H4 acetylation in vivo. Jade-2 contains a canonical Cys4HisCys3 PHD finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, both of which are zinc-binding motifs. This model corresponds to the canonical Cys4HisCys3 PHD finger.


Pssm-ID: 277150 [Multi-domain]  Cd Length: 46  Bit Score: 47.69  E-value: 3.50e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 332646729  549 CAVCRWVEDWEENKMIICNRCQVAVHQECYGVSKSQdLTSWVCRAC 594
Cdd:cd15680     2 CDVCRSPEGEDGNEMVFCDKCNVCVHQACYGILKVP-TGSWLCRTC 46
SET_SETD7 cd10530
SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins; SETD7 (EC 2. ...
 873-992 5.79e-07

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: 49.61  E-value: 5.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  873 ENFRVCFGKSGIH--GWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSqgkdcYLFKISEEIVID------ATD- 943
Cdd:cd10530     5 ESERVYVAESLIPsaGEGLFAKVAVGPNTVMSFYNGVRITHQEVDSRDWSLNG-----NTISLDEETVIDvpepynSVSk 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 332646729  944 -SGNIARLINHSCMPNC-YARIVSMGDGEDNRIVLIakTNVAAGEELTYDY 992
Cdd:cd10530    80 yCASLGHKANHSFTPNCiYDPFVHPRFGPIKCIRTL--RAVEAGEELTVAY 128
PHD_JADE1 cd15679
PHD finger found in protein Jade-1 and similar proteins; Jade-1, also termed PHD finger ...
 549-594 5.90e-07

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


Pssm-ID: 277149 [Multi-domain]  Cd Length: 46  Bit Score: 46.99  E-value: 5.90e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 332646729  549 CAVCRWVEDWEENKMIICNRCQVAVHQECYGVSKSQDlTSWVCRAC 594
Cdd:cd15679     2 CDVCQSPDGEDGNEMVFCDKCNICVHQACYGILKVPE-GSWLCRTC 46
PWWP_MSH6 cd05837
PWWP domain found in DNA mismatch repair protein MSH6 and similar proteins; MSH6, also called ...
 187-283 2.89e-06

PWWP domain found in DNA mismatch repair protein MSH6 and similar proteins; MSH6, also called G/T mismatch-binding protein (GTBP or GTMBP), MutS protein homolog 6, or MutS-alpha 160 kDa subunit (p160), is a mismatch repair protein homologous to bacterial MutS. It is a component of the post-replicative DNA mismatch repair system (MMR). It heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, it forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Mutations in MSH6 have been linked to increased cancer susceptibility, particularly in hereditary nonpolyposis colorectal cancer in humans. MSH6 contains a PWWP domain, but its role in MSH6 remains unclear. MSH6 orthologs found in Saccharomyces cerevisiae, Caenorhabditis elegans, and Arabidopsis thaliana lack the PWWP domain. PWWP domains typically recognize DNA and histone methylated lysines.


Pssm-ID: 438962  Cd Length: 103  Bit Score: 46.90  E-value: 2.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  187 FTVGDLVWAKC-GkrFPAWPAVVID-PISqapDGVLKHCVPGAICVMFFGyskDGTQRdyAWVRQGMVYPFTEFMDKFQD 264
Cdd:cd05837     1 FSPGDLVWAKLeG--YPWWPSLVCNhPTT---GFHKKFGKKGEVHVQFFD---DPPSR--AWVKAKNVKPFTGSDDKEFQ 70

                          90
                  ....*....|....*....
gi 332646729  265 QTNLFNYKASEFNKALEEA 283
Cdd:cd05837    71 KGGMFFSKDPKWKKAVKEA 89
PWWP_HULK cd20147
PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family ...
 190-282 3.24e-06

PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family includes HUA2-like proteins 1-3 (HULK1-3), which are probable transcription factors that act with partial redundancy with each other. They may play diverse and essential roles in the control of plant development, physiology and flowering time. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438975 [Multi-domain]  Cd Length: 92  Bit Score: 46.33  E-value: 3.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  190 GDLVWAKCgKRFPAWPAVVIDPISQApdgvlKHCVPGAICVMFFgyskdGTQRdYAWVRQGMVYPFTEFMDKFQDQTNLF 269
Cdd:cd20147     1 GDLVLAKV-KGFPAWPAQVSEPEDWG-----SAPDPKKVFVHFF-----GTQQ-IGFCNPGELSEFTEEIKQSLLARTLK 68

                          90
                  ....*....|...
gi 332646729  270 NYKASEFNKALEE 282
Cdd:cd20147    69 KKKGSDFSRAVKE 81
PHD_PHF3_like cd15552
PHD finger found in PHD finger protein 3 (PHF3), and death-inducer obliterator variants Dido1, ...
 364-415 6.15e-06

PHD finger found in PHD finger protein 3 (PHF3), and death-inducer obliterator variants Dido1, Dido2, and Dido3; PHF3 is a human homolog of yeast protein bypass of Ess1 (Bye1), a nuclear protein with a domain resembling the central domain in the transcription elongation factor TFIIS. It is ubiquitously expressed in normal tissues including brain, but its expression is significantly reduced or lost in glioblastomas. PHF3 contains an N-terminal plant homeodomain (PHD) finger, a central RNA polymerase II (Pol II)-binding TFIIS-like domain (TLD) domain, and a C-terminal Spen paralogue and orthologue C-terminal (SPOC) domain. This family also includes Dido gene encoding three alternative splicing variants (Dido1, 2, and 3), which have been implicated in a number of cellular processes such as apoptosis and chromosomal segregation, particularly in the hematopoietic system. Dido1 is important for maintaining embryonic stem (ES) cells and directly regulates the expression of pluripotency factors. It is the shortest isoform that contains only a highly conserved PHD finger responsible for the binding of histone H3 with a higher affinity for trimethylated lysine4 (H3K4me3). Gene Dido1 is a Bone morphogenetic protein (BMP) target gene and promotes BMP-induced melanoma progression. It also triggers apoptosis after nuclear translocation and caspase upregulation. Dido3 is the largest isoform and is ubiquitously expressed in all human tissues. It is dispensable for ES cell self-renewal and pluripotency, but is involved in the maintenance of stem cell genomic stability and tumorigenesis. Dido3 contains a PHD finger, a transcription elongation factor S-II subunit M (TFSIIM) domain, a SPOC module, and a long C-terminal region (CT) of unknown homology.


Pssm-ID: 277027  Cd Length: 50  Bit Score: 44.31  E-value: 6.15e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 332646729  364 YCgICKRiwhPSDDGDWVCCDGCDVWVHAECDNITNERFKELEHN--NYYCPDC 415
Cdd:cd15552     1 YC-ICRK---PHNNRFMICCDRCEEWFHGDCVGITEAQGKEMEENieEYVCPKC 50
PWWP_DNMT3 cd05835
PWWP domain found in the DNA (cytosine-5)-methyltransferase 3 (DNMT3) family; The DNMT3 family ...
 189-283 6.27e-06

PWWP domain found in the DNA (cytosine-5)-methyltransferase 3 (DNMT3) family; The DNMT3 family includes DNMT3A and DNMT3B, which are required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNMT3A, also called DNA methyltransferase HsaIIIA, DNA MTase HsaIIIA, or M.HsaIIIA, modifies DNA in a non-processive manner and also methylates non-CpG sites. It may preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. DNMT3A is recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. DNMT3B, also called DNA methyltransferase HsaIIIB, DNA MTase HsaIIIB, or M.HsaIIIB, may preferentially methylate nucleosomal DNA within the nucleosome core region. DNMT3B may function as a transcriptional co-repressor by associating with CBX4 and independently of DNA methylation. Members of this family contains a PWWP domain that is responsible for establishing DNA methylation patterns during embryogenesis and gametogenesis. In tumorigenesis, DNA methylation by DNMT3B is known to play a role in the inactivation of tumor suppressor genes. In addition, a point mutation in the PWWP domain of DNMT3B has been identified in patients with ICF (immunodeficiency, centromeric instability, and facial anomalie) syndrome , a rare autosomal recessive disorder characterized by hypomethylation of classical satellite DNA.


Pssm-ID: 438960 [Multi-domain]  Cd Length: 89  Bit Score: 45.33  E-value: 6.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  189 VGDLVWAKCgKRFPAWPAVVIDPIsqapDGVLKHCVPGAICVMFFG---YSKdgtqrdyawVRQGMVYPFTEFMDKF-QD 264
Cdd:cd05835     2 IGDLVWAKL-KGSPWWPGIVVSHK----DCGQKPPAEGSVWVFWFGdhkVSE---------VPLDKILPFAEFFNKFyIS 67

                          90
                  ....*....|....*....
gi 332646729  265 QTNLFNYKASeFNKALEEA 283
Cdd:cd05835    68 KNSSKLYKKA-VYEALKEA 85
PWWP_NSD_rpt1 cd20144
first PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
 189-267 8.13e-06

first PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein family consists of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1 that are critical in maintaining the chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising in suppressing cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and play nonredundant 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, through 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 (C5HCH). This model corresponds to the first PWWP domain. This family also includes Drosophila melanogaster maternal-effect sterile 4 (dMes4) that may act as a histone-lysine N-methyltransferase required for wing morphogenesis. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438972  Cd Length: 114  Bit Score: 45.77  E-value: 8.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  189 VGDLVWAKCGkRFPAWPA-VVIDPISqapDGVLKHCVPGAIC-----VMFFGyskDGTQRdyAWVRQGMVYPFT---EFM 259
Cdd:cd20144     1 VGDLVWAKVS-GHPWWPCmVTYDPES---GLYTKIKGSGGRTyrqyhVQFFG---DNGER--GWVSEKSLMPFEgkeKFE 71


                  ....*...
gi 332646729  260 DKFQDQTN 267
Cdd:cd20144    72 ELVKELKK 79
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
 364-415 1.41e-05

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: 43.07  E-value: 1.41e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 332646729  364 YCGICKRiwHPSDDGDWVCCDGCDVWVHAECDNITNERFKELEHnnYYCPDC 415
Cdd:cd15489     1 SCIVCGK--GGDLGGELLQCDGCGKWFHADCLGPPLSSFVPNGK--WICPVC 48
PHD_BRPF2 cd15677
PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and similar ...
 549-594 1.84e-05

PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and similar proteins; BRPF2, also termed bromodomain-containing protein 1 (BRD1), or BR140-like protein, is encoded by BRL (BR140 Like gene). It is responsible for the bulk of the acetylation of H3K14 and forms a novel monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complex with HBO1 and ING4. The complex is required for full transcriptional activation of the erythroid-specific regulator genes essential for terminal differentiation and survival of erythroblasts in fetal liver. BRPF2 shows widespread expression and localizes to the nucleus within spermatocytes. It contains a cysteine rich region harboring a canonical Cys4HisCys3 plant homeodomain (PHD) finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. This model corresponds to the canonical Cys4HisCys3 PHD finger.


Pssm-ID: 277147 [Multi-domain]  Cd Length: 54  Bit Score: 43.08  E-value: 1.84e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 332646729  549 CAVCRWVEDWEENKMIICNRCQVAVHQECYGVSKSQDlTSWVCRAC 594
Cdd:cd15677     4 CCICMDGECQNSNVILFCDMCNLAVHQECYGVPYIPE-GQWLCRHC 48
PWWP_NSD1_rpt2 cd20164
second PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) ...
 191-283 2.41e-05

second PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and similar proteins; NSD1, also called H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, androgen receptor coactivator 267 kDa protein, 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, is a lysine methyltransferase that preferentially methylates H3 on Lysine36 (H3-K36) and H4 on Lysine20 (H4-K20), which is primarily associated with active transcription. It plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. It can alter transcription by interacting with the protein NSD1-interacting zinc finger protein 1 (NIZP1). It also mitigates caspase-1 activation by listeriolysin o (LLO) in macrophages, and requires functional LLO for the regulation of IL-1beta secretion. Moreover, NSD1 regulates RNA polymerase II (RNAP II) recruitment to bone morphogenetic protein 4 (BMP4). NSD1 contains 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 (C5HCH). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD domains are involved in protein-protein interactions. This model corresponds to the second PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438992  Cd Length: 96  Bit Score: 44.10  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  191 DLVWAKCGkRFPAWPAVVIDPISQAPDGV-LKHCVpGAICVMFFGyskdgtQRDYAWVRQGMVYPFTEFMDKFQDQTNlf 269
Cdd:cd20164     4 EVVWVKVG-RYRWWPAEVCHPKSIPTNIQkMKHDI-GEFPVLFFG------SNDYLWTHQARVFPYMEGDVSSKDKMG-- 73

                          90
                  ....*....|....*.
gi 332646729  270 nyKA--SEFNKALEEA 283
Cdd:cd20164    74 --KGvdGTYKKALQEA 87
PWWP_NSD2_rpt2 cd20165
second PWWP domain found in nuclear SET domain-containing protein 2 (NSD2) and similar ...
 191-283 2.44e-05

second PWWP domain found in nuclear SET domain-containing protein 2 (NSD2) and similar proteins; NSD2, also called histone-lysine N-methyltransferase NSD2, multiple myeloma SET domain-containing protein (MMSET), or protein trithorax-5 Wolf-Hirschhorn syndrome candidate 1 protein (WHSC1), is overexpressed frequently in the t(4;14) translocation in 15% to 20% of multiple myeloma. It plays important roles in cancer cell proliferation, survival, and tumor growth, through mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. It also enhances androgen receptor (AR)-mediated transcription. The principal chromatin-regulatory activity of NSD2 is dimethylation of histone H3 at lysine 36 (H3K36me2). NSD2 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, an high mobility group (HMG) box, five PHD (plant-homeodomain) zinc finger motifs, and an NSD-specific Cys-His rich domain (C5HCH). The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD domains mediate chromatin interaction and recognition of histone marks. This model corresponds to the second PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438993  Cd Length: 96  Bit Score: 44.18  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  191 DLVWAKCGKrFPAWPAVVIDPISQAPD-GVLKHCVpGAICVMFFGyskdgtQRDYAWVRQGMVYPFTE--FMDKFQDQTN 267
Cdd:cd20165     4 DIIWVKLGN-YRWWPAEVCHPKNVPPNiQKMKHEI-GEFPVFFFG------SKDYYWTHQARVFPYMEgdRGSKYQGGKG 75

                          90
                  ....*....|....*.
gi 332646729  268 LfnykASEFNKALEEA 283
Cdd:cd20165    76 I----GKVFKNALQEA 87
PHD_BRPF cd15572
PHD finger found in bromodomain and PHD finger-containing (BRPF) proteins; The family of BRPF ...
 549-594 2.71e-05

PHD finger found in bromodomain and PHD finger-containing (BRPF) proteins; The family of BRPF proteins includes BRPF1, BRD1/BRPF2, and BRPF3. They are scaffold proteins that form monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complexes with other regulatory subunits, such as inhibitor of growth 5 (ING5) and Esa1-associated factor 6 ortholog (EAF6). BRPF proteins have multiple domains, including a canonical Cys4HisCys3 plant homeodomain (PHD) zinc finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. PHD and ePHD fingers both bind to lysine 4 of histone H3 (K4H3), bromodomains interact with acetylated lysines on N-terminal tails of histones and other proteins, and PWWP domains show histone-binding and chromatin association properties. This model corresponds to the canonical Cys4HisCys3 PHD finger.


Pssm-ID: 277047 [Multi-domain]  Cd Length: 54  Bit Score: 42.60  E-value: 2.71e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 332646729  549 CAVCRWVEDWEENKMIICNRCQVAVHQECYGVSKSQDlTSWVCRAC 594
Cdd:cd15572     4 CCICLDGECQNSNVILFCDMCNLAVHQECYGVPYIPE-GQWLCRRC 48
PHD_DIDO1_like cd15639
PHD finger found in death-inducer obliterator variants Dido1, Dido2, and Dido3; This family ...
 364-415 2.71e-05

PHD finger found in death-inducer obliterator variants Dido1, Dido2, and Dido3; This family includes three alternative splicing variants (Dido1, 2, and 3) encoded by the Dido gene, which have been implicated in a number of cellular processes such as apoptosis and chromosomal segregation, particularly in the hematopoietic system. Dido1, also termed DIO-1, or death-associated transcription factor 1 (DATF-1), is important for maintaining embryonic stem (ES) cells and directly regulates the expression of pluripotency factors. It is the shortest isoform that contains only a highly conserved plant homeodomain (PHD) finger responsible for the binding of histone H3 with a higher affinity for trimethylated lysine 4 (H3K4me3). Gene Dido is a Bonemorphogenetic protein (BMP) target gene, which promotes BMP-induced melanoma progression. It also triggers apoptosis after nuclear translocation and caspase upregulation. Dido3 is the largest isoform ubiquitously expressed in all human tissues. It is dispensable for ES cell self-renewal and pluripotency, but involved in the maintenance of stem cell genomic stability and tumorigenesis. Dido3 contains a PHD finger, a transcription elongation factor S-II subunit M (TFSIIM) domain, aspen paralog and ortholog (SPOC) module, and a long C-terminal region (CT) of unknown homology. Its PHD finger interacts with H3K4me3.


Pssm-ID: 277109  Cd Length: 54  Bit Score: 42.64  E-value: 2.71e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 332646729  364 YCgICKRiwhPSDDGDWVCCDGCDVWVHAECDNITNERFKELEHN--NYYCPDC 415
Cdd:cd15639     5 YC-ICRQ---PHNNRFMICCDRCEEWFHGDCVGITEARGRLLERNgeDYICPNC 54
PWWP_AtATX1-like cd20142
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
 189-283 3.19e-05

PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like proteins ATX1, ATX2, and similar proteins; This family includes A. thaliana ATX1 and ATX2, which are sister paralogs originating from a segmental chromosomal duplication. They are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1, also called 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 called protein SET domain group 30, or trithorax-homolog protein 2 (TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). Both ATX1 and ATX2 are multi-domain containing proteins that consist of an N-terminal PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical plant homeodomain (PHD) domain, a non-canonical extended PHD (ePHD) domain, and a C-terminal SET domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438970 [Multi-domain]  Cd Length: 97  Bit Score: 43.50  E-value: 3.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  189 VGDLVWAKCgKRFPAWPAVVIDPISQAPDGVL------KHCVPgaicVMFFGyskdgtQRDYAWVRQGMVYPFTE-FMDK 261
Cdd:cd20142     2 PGDVVWAKV-KGYPMWPALVIDEEHAERCGLEanrpgkKGTVP----VQFFG------TYEVARLNPKKVVGFSKgLDLK 70

                          90       100
                  ....*....|....*....|..
gi 332646729  262 FQDQTnlfnyKASEFNKALEEA 283
Cdd:cd20142    71 YHSKC-----KAPVFRQALEEA 87
PHD_SPP1 cd16039
PHD finger found in Set1 complex component SPP1; Set1C component SPP1, also called COMPASS ...
 364-415 3.19e-05

PHD finger found in Set1 complex component SPP1; Set1C component SPP1, also called COMPASS component Spp1, or Complex proteins associated with set1 protein Spp1, or Suppressor of PRP protein 1, is a component of the COMPASS complex that links histone methylation to initiation of meiotic recombination. It induces double-strand break (DSB) formation by tethering to recombinationally cold regions. SPP1 interacts with H3K4me3 and Mer2, a protein required for DSB formation, to promote recruitment of potential meiotic DSB sites to the chromosomal axis. SPP1 contains a PHD finger, a zinc binding motif.


Pssm-ID: 277186  Cd Length: 46  Bit Score: 42.08  E-value: 3.19e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 332646729  364 YCgICKRiwhPSDDGDWVCCDGCDVWVHAECDNItNERFKELEhNNYYCPDC 415
Cdd:cd16039     1 YC-ICQK---PDDGRWMIACDGCDEWYHFTCVNI-PEADVELV-DSFFCPPC 46
PHD_TAF3 cd15522
PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3); TAF3 (also termed ...
 364-415 3.74e-05

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


Pssm-ID: 276997 [Multi-domain]  Cd Length: 46  Bit Score: 41.89  E-value: 3.74e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 332646729  364 YCGICKRIwhpsDDGD-WVCCDGCDVWVHAECDNITNErfkELEHNNYYCPDC 415
Cdd:cd15522     1 ICPICKKP----DDGSpMIGCDECDDWYHWECVGITDE---PPEEDDWFCPKC 46
PHD_ATX1_2_like cd15494
PHD finger found in Arabidopsis thaliana histone-lysine N-methyltransferase arabidopsis ...
 548-594 4.30e-05

PHD finger found in Arabidopsis thaliana histone-lysine N-methyltransferase arabidopsis trithorax-like protein ATX1, ATX2, and similar proteins; The family includes A. thaliana ATX1 and ATX2, both of which are sister paralogs originating from a segmental chromosomal duplication. They are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1, also termed protein SET domain group 27, or trithorax-homolog protein 1 (TRX-homolog protein 1), is a methyltransferase that trimethylates histone H3 at lysine 4 (H3K4me3). It also acts as a histone modifier and as a positive effector of gene expression. ATX1regulates transcription from diverse classes of genes implicated in biotic and abiotic stress responses. It is involved in dehydration stress signaling in both abscisic acid (ABA)-dependent and ABA-independent pathways. ATX2, also termed protein SET domain group 30, or trithorax-homolog protein 2 (TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). Both ATX1 and ATX2 are multi-domain containing proteins that consist of an N-terminal PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical Cys4HisCys3 plant homeodomain (PHD) finger, a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, and a C-terminal SET domain; this model corresponds to the Cys4HisCys3 canonical PHD finger.


Pssm-ID: 276969  Cd Length: 47  Bit Score: 41.67  E-value: 4.30e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 332646729  548 RCAVCRWVEDWEENKMIICNRCQVAVHQECYGVSKSQDLTSWVCRAC 594
Cdd:cd15494     1 KCSVCGEDEEYEDNLLLQCDKCRMMVHMRCYGVLEPPPGALWLCNLC 47
PHD_AF10_AF17 cd15574
PHD finger found in protein AF-10 and AF-17; This family includes protein AF-10 and AF-17. ...
 549-594 4.34e-05

PHD finger found in protein AF-10 and AF-17; This family includes protein AF-10 and AF-17. AF-10, also termed ALL1 (acute lymphoblastic leukemia)-fused gene from chromosome 10 protein, is a transcription factor encoded by gene AF10, a translocation partner of the MLL (mixed-lineage leukemia) oncogene in leukemia. AF-10 has been implicated in the development of leukemia following chromosomal rearrangements between the AF10 gene and one of at least two other genes, MLL and CALM. It plays a key role in the survival of uncommitted hematopoietic cells. Moreover, AF-10 functions as a follistatin-related gene (FLRG)-interacting protein. The interaction with FLRG enhances AF10-dependent transcription. It interacts with the human counterpart of the yeast Dot1, hDOT1L, and may act as a bridge for the recruitment of hDOT1L to the genes targeted by MLL-AF10. It also interacts with the synovial sarcoma associated SYT protein and may play a role in synovial sarcomas and acute leukemias. AF-17, also termed ALL1-fused gene from chromosome 17 protein, is encoded by gene AF17 that has been identified in hematological malignancies as translocation partners of the mixed lineage leukemia gene MLL. It is a putative transcription factor that may play a role in multiple signaling pathways. It is involved in chromatin-mediated gene regulation mechanisms. It functions as a component of the multi-subunit Dot1 complex (Dotcom) and plays a role in the Wnt/Wingless signaling pathway. It also seems to be a downstream target of the beta-catenin/T-cell factor pathway, and participates in G2-M progression. Moreover, it may function as an important regulator of ENaC-mediated Na+ transport and thus blood pressure. Both AF-10 and AF-17 contain an N-terminal canonical Cys4HisCys3 plant homeodomain (PHD) finger followed by a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His. The PHD finger is involved in their homo-oligomerization. In the C-terminal region, they possess a leucine zipper domain and a glutamine-rich region. This family also includes ZFP-1, the Caenorhabditis elegans AF10 homolog. It was originally identified as a factor promoting RNAi interference in C. elegans. It also acts as a Dot1-interacting protein that opposes H2B ubiquitination to reduce polymerase II (Pol II) transcription. This model corresponds to the canonical Cys4HisCys3 PHD finger.


Pssm-ID: 277049 [Multi-domain]  Cd Length: 48  Bit Score: 41.73  E-value: 4.34e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 332646729  549 CAVCRWVEDWEENKMIICN--RCQVAVHQECYGVSKSQDlTSWVCRAC 594
Cdd:cd15574     2 CCVCSDERGWAENPLVYCDghGCNVAVHQACYGIVQVPT-GPWFCRKC 48
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 548-594 5.72e-05

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: 41.71  E-value: 5.72e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 332646729   548 RCAVCRwvEDWEENKMIICNRCQVAVHQECYGVSKS---QDLTSWVCRAC 594
Cdd:pfam00628    1 YCAVCG--KSDDGGELVQCDGCDDWFHLACLGPPLDpaeIPSGEWLCPEC 48
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
 548-594 6.60e-05

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: 41.15  E-value: 6.60e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 332646729  548 RCAVCRWVEDWEEnKMIICNRCQVAVHQECYGV--SKSQDLTSWVCRAC 594
Cdd:cd15489     1 SCIVCGKGGDLGG-ELLQCDGCGKWFHADCLGPplSSFVPNGKWICPVC 48
PHD_MLL5 cd15550
PHD finger found in mixed lineage leukemia 5 (MLL5); MLL5 is a histone methyltransferase that ...
 376-415 1.02e-04

PHD finger found in mixed lineage leukemia 5 (MLL5); MLL5 is a histone methyltransferase that plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. It contains a single plant homeodomain (PHD) finger followed by a catalytic SET domain. MLL5 can be recruited to E2F1-responsive promoters to stimulate H3K4 trimethylation and transcriptional activation by binding to the cell cycle regulator host cell factor (HCF-1), thereby facilitating the cell cycle G1 to S phase transition. It is also involved in mitotic fidelity and genomic integrity by modulating the stability of the chromosomal passenger complex (CPC) via the interaction with Borealin. Moreover, MLL5 is a component of a complex associated with retinoic acid receptor that requires GlcN Acylation of its SET domain in order to activate its histone lysine methyltransferase activity. It also participates in the camptothecin (CPT)-induced p53 activation. Furthermore, MLL5 indirectly regulates H3K4 methylation, represses cyclin A2 (CycA) expression, and promotes myogenic differentiation.


Pssm-ID: 277025 [Multi-domain]  Cd Length: 44  Bit Score: 40.76  E-value: 1.02e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 332646729  376 DDGDWVCCDGCDVWVHAECDNITNERFKElehnNYYCPDC 415
Cdd:cd15550     9 DDGFMICCDKCSVWQHGDCMGIDRENIPD----SYLCEQC 44
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 548-594 1.48e-04

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: 40.27  E-value: 1.48e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 332646729    548 RCAVCRwvEDWEENKMIICNRCQVAVHQECYGVSKSQDL--TSWVCRAC 594
Cdd:smart00249    1 YCSVCG--KPDDGGELLQCDGCDRWYHQTCLGPPLLEEEpdGKWYCPKC 47
PHD3_KDM5A_like cd15610
PHD finger 3 found in Lysine-specific demethylase 5A (KDM5A), 5B (KDM5B), and similar proteins; ...
 376-415 2.12e-04

PHD finger 3 found in Lysine-specific demethylase 5A (KDM5A), 5B (KDM5B), and similar proteins; The family includes KDM5A and KDM5B, both of which belong to the JARID subfamily within the JmjC proteins. KDM5A, also termed Histone demethylase JARID1A, or Jumonji/ARID domain-containing protein 1A, or Retinoblastoma-binding protein 2 (RBBP-2 or RBP2), was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5A functions as the trimethylated histone H3 lysine 4 (H3K4me3) demethylase. It also displays DNA-binding activities that can recognize the specific DNA sequence CCGCCC. KDM5B, also termed Cancer/testis antigen 31 (CT31), or Histone demethylase JARID1B, or Jumonji/ARID domain-containing protein 1B (JARID1B), or PLU-1, or retinoblastoma-binding protein 2 homolog 1 (RBP2-H1 or RBBP2H1A), 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. KDM5B acts as a histone demethylase that catalyzes the removal of trimethylation of lysine 4 on histone H3 (H3K4me3), induced by polychlorinated biphenyls (PCBs). It also mediates demethylation of H3K4me2 and H3K4me1. Moreover, KDM5B functions as a negative regulator of hematopoietic stem cell (HSC) self-renewal and progenitor cell activity. KDM5B has also been shown to interact with the DNA binding transcription factors BF-1 and PAX9, as well asTIEG1/KLF10 (transforming growth factor-beta inducible early gene-1/Kruppel-like transcription factor 10), and possibly function as a transcriptional corepressor. The family also includes the Drosophila melanogaster protein little imaginal discs (Lid) that functions as a JmjC-dependent trimethyl histone H3K4 (H3K4me3) demethylase, which is required for dMyc-induced cell growth. It positively regulates Hox gene expression in S2 cells. Members in this family contain the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the third PHD finger.


Pssm-ID: 277083 [Multi-domain]  Cd Length: 50  Bit Score: 40.00  E-value: 2.12e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 332646729  376 DDGDWVCCDGCDVWVHAECDNITNERFKELEhnNYYCPDC 415
Cdd:cd15610    13 DEVNWVQCDGCEEWFHLLCVGLSPEEVAEDE--DYICPSC 50
PHD3_KMT2A_like cd15508
PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); This ...
 364-415 2.24e-04

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: 40.12  E-value: 2.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  364 YCGICKRIWhpsDDGDW----VCCDGCDVWVHAECDNITNERFKEL----EHNNYYCPDC 415
Cdd:cd15508     1 YCPLCEKCY---DDDDYdskmMQCSQCDHWVHAKCEGLSDEMYEILsylpESIEYTCSLC 57
PHD2_3_BPTF cd15560
PHD finger 2 and 3 found in bromodomain and PHD finger-containing transcription factor (BPTF); ...
 364-415 2.43e-04

PHD finger 2 and 3 found in bromodomain and PHD finger-containing transcription factor (BPTF); BPTF, also termed nucleosome-remodeling factor subunit BPTF, or fetal Alz-50 clone 1 protein (FAC1), or fetal Alzheimer antigen, functions as a transcriptional regulator that exhibits altered expression and subcellular localization during neuronal development and neurodegenerative diseases such as Alzheimer's disease. It interacts with the human orthologue of the Kelch-like Ech-associated protein (Keap1). Its function and subcellular localization can be regulated by Keap1. Moreover, BPTF is a novel DNA-binding protein that recognizes the DNA sequence CACAACAC and represses transcription through this site in a phosphorylation-dependent manner. Furthermore, BPTF interacts with the Myc-associated zinc finger protein (ZF87/MAZ) and alters its transcriptional activity, which has been implicated in gene regulation in neurodegeneration. Some family members contain two or three plant homeodomain (PHD) fingers, which may be involved in complex formation with histone H3 trimethylated at K4 (H3K4me3). This family corresponds to the second and third PHD fingers.


Pssm-ID: 277035  Cd Length: 47  Bit Score: 39.64  E-value: 2.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 332646729  364 YCgICKRiwhPSDDGD-WVCCDGCDVWVHAECDNITNERFKELEhnNYYCPDC 415
Cdd:cd15560     1 YC-ICRT---PYDESQfYIGCDRCQDWFHGRCVGILQSEAEKID--EYVCPQC 47
PHD1_MTF2_PHF19_like cd15499
PHD finger 1 found in polycomb repressive complex 2 (PRC2)-associated polycomb-like (PCL) ...
 549-595 2.88e-04

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: 39.79  E-value: 2.88e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 332646729  549 CAVCRWVEDWEENKMIICNRCQVAVHQECY----GVSKSQDLTSWVCRACE 595
Cdd:cd15499     2 CSICGGAEARDGNEILICDKCDKGYHQLCHspkvRTSPLEGDEKWFCSRCV 52
PWWP_BRPF1 cd20156
PWWP domain found in bromodomain and PHD finger-containing protein 1 (BRPF1); BRPF1, also ...
 191-225 3.16e-04

PWWP domain found in bromodomain and PHD finger-containing protein 1 (BRPF1); BRPF1, also called 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 may be involved in chromatin remodeling. It contains a plant homeodomain (PHD) zinc finger followed by a non-canonical extended PHD (ePHD) finger, C2HC5HC2H, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. The PHD finger binds to methylated 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: 438984  Cd Length: 120  Bit Score: 41.54  E-value: 3.16e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 332646729  191 DLVWAKCgKRFPAWPAVVIDPiSQAPDGVLKHCVP 225
Cdd:cd20156     5 DLVWAKC-RGYPSYPALIIDP-KMPREGMFHHGVP 37
SET_Suv4-20-like cd10524
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
 948-992 3.29e-04

SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of variegation 4-20 (Suv4-20) and similar proteins; Suv4-20 (also termed Su(var)4-20) is a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-20' of histone H4. It acts as a dominant suppressor of position-effect variegation. The family also includes Suv4-20 homologs, lysine N-methyltransferase 5B (KMT5B) and lysine N-methyltransferase 5C (KMT5C). Both KMT5B (also termed lysine-specific methyltransferase 5B, or suppressor of variegation 4-20 homolog 1, or Su(var)4-20 homolog 1, or Suv4-20h1) and KMT5C (also termed lysine-specific methyltransferase 5C, or suppressor of variegation 4-20 homolog 2, or Su(var)4-20 homolog 2, or Suv4-20h2) are histone methyltransferases that specifically trimethylate 'Lys-20' of histone H4 (H4K20me3). They play central roles in the establishment of constitutive heterochromatin in pericentric heterochromatin regions.


Pssm-ID: 380922 [Multi-domain]  Cd Length: 141  Bit Score: 41.88  E-value: 3.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 332646729  948 ARLINHSCMPNCyaRIVSMGdgeDNRIVLIAKTNVAAGEELTYDY 992
Cdd:cd10524    77 AAFINHDCRPNC--KFVPTG---KSTACVKVLRDIEPGEEITVYY 116
ePHD_KMT2A_like cd15664
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The ...
 603-714 3.47e-04

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: 40.85  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  603 CCLCPVKGGALkPSDVEGL-------WVHVTCAWFRPEV-----GFLNHENMEPAVGlfkipanSFLKvCTICkQTHGSC 670
Cdd:cd15664     1 CALCGVYGDDE-PNDAGRLlycgqdeWVHINCALWSAEVfeeddGSLQNVHSAVSRG-------RMMK-CELC-GKPGAT 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 332646729  671 VHCC--KCATHFHAMCASRAgynmelhclekNGVQRTRKSVYCSFH 714
Cdd:cd15664    71 VGCClkSCPANYHFMCARKA-----------ECVFQDDKKVFCPAH 105
PHD_BRPF1 cd15676
PHD finger found in bromodomain and PHD finger-containing protein 1 (BRPF1) and similar ...
 549-594 4.02e-04

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


Pssm-ID: 277146 [Multi-domain]  Cd Length: 62  Bit Score: 39.65  E-value: 4.02e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 332646729  549 CAVCRWVEDWEENKMIICNRCQVAVHQECYGVSKSQDlTSWVCRAC 594
Cdd:cd15676    10 CCICNDGECQNSNVILFCDMCNLAVHQECYGVPYIPE-GQWLCRRC 54
PHD1_PHF14 cd15561
PHD finger 1 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...
 549-594 4.20e-04

PHD finger 1 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel nuclear transcription factor that controls the proliferation of mesenchymal cells by directly repressing platelet-derived growth factor receptor-alpha (PDGFRalpha) expression. It also acts as an epigenetic regulator and plays an important role in the development of multiple organs in mammals. PHF14 contains three canonical plant homeodomain (PHD) fingers and a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His. It can interact with histones through its PHD fingers. The model corresponds to the first PHD finger.


Pssm-ID: 277036  Cd Length: 56  Bit Score: 39.34  E-value: 4.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 332646729  549 CAVCRWVEDWEENKMIICNRCQVAVHQECYGVSKSQDLTS---------WVCRAC 594
Cdd:cd15561     2 CCVCLGDRSNDADEIIECDKCGISVHEGCYGVIDESDSSSsasssstepWFCEPC 56
PHD_AL_plant cd15613
PHD finger found in plant Alfin1-like (AL) proteins; AL proteins are ubiquitously expressed ...
 365-415 7.15e-04

PHD finger found in plant Alfin1-like (AL) proteins; AL proteins are ubiquitously expressed nuclear proteins existing only in plants. They are involved in chromatin regulation by binding to tri- and dimethylated histone H3 at lysine 4 (H3K4me3/2), the active histone markers, through their plant homeodomain (PHD) fingers.


Pssm-ID: 277085  Cd Length: 51  Bit Score: 38.63  E-value: 7.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 332646729  365 CGICKRIWhpSDDGDWVCCDGCDVWVHAECDNITNERFKELEHnnYYCPDC 415
Cdd:cd15613     2 CGSCGGNY--TADEFWICCDVCEKWYHGKCVKITPAKAEHIKQ--YKCPSC 48
PHD_BRPF3 cd15678
PHD finger found in bromodomain and PHD finger-containing protein 3 (BRPF3) and similar ...
 549-594 7.97e-04

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


Pssm-ID: 277148 [Multi-domain]  Cd Length: 55  Bit Score: 38.46  E-value: 7.97e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 332646729  549 CAVCRWVEDWEENKMIICNRCQVAVHQECYGVSKSQDlTSWVCRAC 594
Cdd:cd15678     4 CCVCLDDECHNSNVILFCDICNLAVHQECYGVPYIPE-GQWLCRCC 48
PWWP_MUM1-like cd06080
PWWP domain found in mutated melanoma-associated antigen 1 (MUM-1) and similar proteins; MUM-1, ...
 187-208 8.98e-04

PWWP domain found in mutated melanoma-associated antigen 1 (MUM-1) and similar proteins; MUM-1, also called PWWP domain-containing DNA repair factor 3A (PWWP3A), or protein expandere (EXPAND1), is a melanoma-associated antigen (MAA) that belongs to the mutated or aberrantly expressed type of MAAs, along with antigens such as CDK4, beta-catenin, gp100-in4, p15, and N-acetylglucosaminyltransferase V. It is highly expressed in several types of human cancers and involved in the DNA damage response pathway by contributing to the maintenance of chromatin architecture. MUM-1 is recruited to the vicinity of DNA breaks by TP53BP1 and plays an accessory role to facilitate damage-induced chromatin changes and promoting chromatin relaxation. It is required for efficient DNA repair and cell survival following DNA damage. This subfamily also includes mutated melanoma-associated antigen 1-like protein 1 (MUM1L1), also called MUM1-like protein 1, or PWWP domain-containing DNA repair factor 3B (PWWP3B). Its biological function remains unclear. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438967  Cd Length: 90  Bit Score: 39.16  E-value: 8.98e-04
                          10        20
                  ....*....|....*....|..
gi 332646729  187 FTVGDLVWAKCgKRFPAWPAVV 208
Cdd:cd06080     1 FSKGDIVWAKY-RKYPYWPAVV 21
PHD_HAC_like cd15614
PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar ...
 380-415 1.83e-03

PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar proteins; This family includes A. thaliana HACs (HAC1/2/4/5/12), which are histone acetyltransferases of the p300/CREB-binding protein (CBP) co-activator family. CBP-type HAT proteins are also found in animals, but absent in fungi. The domain architecture of CBP-type HAT proteins differs between plants and animals. Members in this family contain an N-terminal partially conserved KIX domain, a Zf-TAZ domain, a Cysteine rich CBP-type HAT domain that harbors a plant homeodomain (PHD) finger, a Zf-ZZ domain, and a Zf-TAZ domain. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins.


Pssm-ID: 277086  Cd Length: 73  Bit Score: 38.10  E-value: 1.83e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 332646729  380 WVCCDGCDVWVHAECdNITNERFKELEHNNYYCPDC 415
Cdd:cd15614    39 WVQCDKCERWQHQIC-GLYNGRRNADETAEYVCPLC 73
PHD3_KMT2A cd15592
PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, ...
 364-415 1.92e-03

PHD finger 3 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, CXXC-type zinc finger protein 7, myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), trithorax-like protein (Htrx), or zinc finger protein HRX) is a histone methyltransferase that belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2). It regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in the MLL1 complex, which also contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL1 complex is highly active and specific for H3K4 methylation. KMT2A contains a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD) fingers, a Bromodomain domain, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the third PHD finger.


Pssm-ID: 277067  Cd Length: 57  Bit Score: 37.27  E-value: 1.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 332646729  364 YCGICKRIWHPSD-DGDWVCCDGCDVWVHAECDNITNERFKEL----EHNNYYCPDC 415
Cdd:cd15592     1 FCPLCDKCYDDDDyESKMMQCGKCDRWVHSKCENLSDEMYEILsnlpESVAYTCINC 57
PHD2_CHD_II cd15532
PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...
 364-415 2.51e-03

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


Pssm-ID: 277007 [Multi-domain]  Cd Length: 43  Bit Score: 36.49  E-value: 2.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 332646729  364 YCGICKriwhpsDDGDWVCCDGCDVWVHAECdniTNERFKELEHNNYYCPDC 415
Cdd:cd15532     1 FCRVCK------DGGELLCCDGCPSSYHLHC---LNPPLAEIPDGDWFCPRC 43
PHD1_PHF19 cd15579
PHD finger 1 found in PHD finger protein 19 (PHF19); PHF19, also termed Polycomb-like protein ...
 548-594 2.75e-03

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


Pssm-ID: 277054  Cd Length: 53  Bit Score: 36.78  E-value: 2.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 332646729  548 RCAVCRWVEDWEENKMIICNRCQVAVHQECY----GVSKSQDLTSWVCRAC 594
Cdd:cd15579     1 KCNVCLGKSSGPLNEILICGKCGLGYHQQCHipvvDSSDDPPLTPWFCRRC 51
SET_SMYD4 cd10536
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
 950-992 2.89e-03

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: 40.36  E-value: 2.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 332646729  950 LINHSCMPNCyarIVSMgdgEDNRIVLIAKTNVAAGEELTYDY 992
Cdd:cd10536   153 LLNHSCDPNT---IRSF---YGNTIVVRATRPIKKGEEITICY 189
PWWP_MBD5 cd20141
PWWP domain found in methyl-CpG-binding domain protein 5 (MBD5) and similar proteins; MBD5, is ...
 187-284 2.94e-03

PWWP domain found in methyl-CpG-binding domain protein 5 (MBD5) and similar proteins; MBD5, is a methyl-CpG-binding protein that binds to heterochromatin. It does not interact with either methylated or unmethylated DNA. MBD5 acts as a transcriptional regulator responsible for 2q23.1 deletion syndrome. It belongs to the MBD family proteins, which play central roles in transcriptional regulation and development. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438969  Cd Length: 92  Bit Score: 38.07  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  187 FTVGDLVWAKcGKRFPAWPAVVIDpisqAPDGvlKHCVPGAICVMFFGyskDGTqrdyawvrQGMVYP-----FTEFMDK 261
Cdd:cd20141     1 FNVGDLVWGQ-IRGFPSWPGKLVS----ENDV--GKTNEGKVWVSWFG---DHS--------FGQVEPdklktLSEGLEA 62

                          90       100
                  ....*....|....*....|...
gi 332646729  262 FQDQTNlFNYKASEFNKALEEAV 284
Cdd:cd20141    63 HHRARK-RTRKGRKLNNHLEAAI 84
PHD1_PHF1 cd15500
PHD finger 1 found in PHD finger protein1 (PHF1); PHF1, also termed polycomb-like protein 1 ...
 549-594 2.98e-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: 36.73  E-value: 2.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 332646729  549 CAVCRWVEDWEENKMIICNRCQVAVHQECYGVS----KSQDLTSWVCRAC 594
Cdd:cd15500     2 CCVCDSETVSPKNPLVNCEKCHHAYHQECHVPRvpleSAGDGDSWMCRQC 51
SET_SETD5 cd19181
SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...
 889-1012 3.02e-03

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: 39.22  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332646729  889 LFARKSIQEGEMIIEYRGVKVRRSVADLrEANYRSQGKDCYLF--KISE-EIVIDATDSGNIARLINHSCMPNCYARIVs 965
Cdd:cd19181    21 LRAARDLALDTLIIEYRGKVMLRQQFEV-NGHFFKRPYPFVLFysKFNGvEMCVDARTFGNDARFIRRSCTPNAEVRHM- 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 332646729  966 MGDGEDNrIVLIAKTNVAAGEELTYDYLFEVdESEEIKVPCLCKAPN 1012
Cdd:cd19181    99 IADGMIH-LCIYAVAAIAKDAEVTIAFDYEY-SNCNYKVDCACHKGN 143
PHD4_NSD cd15567
PHD finger 4 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
 364-415 3.04e-03

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


Pssm-ID: 277042 [Multi-domain]  Cd Length: 41  Bit Score: 36.46  E-value: 3.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 332646729  364 YCGICkriwhpSDDGDWVCCDGCDVWVHAECDNItnerfKELEHNNYYCPDC 415
Cdd:cd15567     1 WCFIC------SEGGSLICCESCPASFHPECLGL-----EPPPEGKFYCEDC 41
PHD_Cfp1 cd15553
PHD finger found in CXXC-type zinc finger protein 1 (Cfp1); Cfp1, also termed CpG-binding ...
 364-415 3.07e-03

PHD finger found in CXXC-type zinc finger protein 1 (Cfp1); Cfp1, also termed CpG-binding protein, or PHD finger and CXXC domain-containing protein 1 (PCCX1), is a specificity factor that binds to unmethylated CpGs and links H3K4me3 with CpG islands (CGIs). It integrates both promoter CpG content and gene activity for accurate trimethylation of histone H3 Lys 4 (H3K4me3) deposition in embryonic stem cells. Moreover, Cfp1 is an essential component of the SETD1 histone H3K4 methyltransferase complex and functions as a critical regulator of histone methylation, cytosine methylation, cellular differentiation, and vertebrate development. Cfp1 contains a plant homeodomain (PHD) finger, a CXXC domain, and a CpG binding protein zinc finger C-terminal domain. Its CXXC domain selectively binds to non-methylated CpG islands, following by a preference for a guanosine nucleotide.


Pssm-ID: 277028  Cd Length: 46  Bit Score: 36.59  E-value: 3.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 332646729  364 YCgICKRiwhPSDDGDWVCCDGCDVWVHAECDNITNERFKELEHnnYYCPDC 415
Cdd:cd15553     1 YC-ICRS---SDISRFMIGCDNCEEWYHGDCINITEKEAKAIKE--WYCQQC 46
PHD_JMJD2A cd15575
PHD finger found in Jumonji domain-containing protein 2A (JMJD2A); JMJD2A, also termed ...
 554-594 3.49e-03

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


Pssm-ID: 277050  Cd Length: 100  Bit Score: 37.96  E-value: 3.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 332646729  554 WVEDWEENKMIICNRCQVAVHQECYGVSKSQDLTSWVCRAC 594
Cdd:cd15575    60 YLEEDGTSILVTCKKCCVCVHASCYGVSPEKAAEDWMCSRC 100
PHD_JMJD2 cd15493
PHD finger found in Jumonji domain-containing protein 2 (JMJD2) family of histone demethylases; ...
 549-594 3.76e-03

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


Pssm-ID: 276968  Cd Length: 42  Bit Score: 36.14  E-value: 3.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 332646729  549 CAVCRWVedweenKMIICNRCQVAVHQECYGVSKS-QDLTSWVCRAC 594
Cdd:cd15493     2 CAICSLF------RLLVCSRCCVCVHASCYGVPDIpGDGEGWKCDRC 42
PHD3_KMT2C cd15511
PHD finger 3 found in Histone-lysine N-methyltransferase 2C (KMT2C); KMT2C, also termed ...
 365-415 5.13e-03

PHD finger 3 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 third PHD finger.


Pssm-ID: 276986  Cd Length: 52  Bit Score: 35.93  E-value: 5.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 332646729  365 CGICKRIWHPSDDGDWVCCDGCDVWVHAECDNITNERFKELEHNNYYCPDC 415
Cdd:cd15511     2 CPACKKNLDPELQKDMLHCHVCKRWIHLECEKPNDNELLDQLKEDYICSLC 52
SET_LSMT cd10527
SET domain found in Rubisco large subunit methyltransferase (LSMT) and similar proteins; ...
 950-992 7.54e-03

SET domain found in Rubisco large subunit methyltransferase (LSMT) and similar proteins; Rubisco LSMT is a non-histone protein methyl transferase responsible for the trimethylation of lysine14 in the large subunit of Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase). The family also includes SET domain-containing proteins, SETD3, SETD4 and SETD6, which belong to methyltransferase class VII that represents classical non-histone SET domain methyltransferases. Members in this family contain a SET domain and a C-terminal RubisCO LSMT substrate-binding (Rubis-subs-bind) domain.


Pssm-ID: 380925 [Multi-domain]  Cd Length: 236  Bit Score: 39.35  E-value: 7.54e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 332646729  950 LINHS-CMPNCYARIvsmgDGEDNRIVLIAKTNVAAGEELTYDY 992
Cdd:cd10527   182 MLNHSpDAPNVRYEY----DEDEGSFVLVATRDIAAGEEVFISY 221
PHD2_Snt2p_like cd15498
PHD finger 2 found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) and ...
 549-594 7.67e-03

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


Pssm-ID: 276973  Cd Length: 55  Bit Score: 35.53  E-value: 7.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 332646729  549 CAVCRWVEDWEENKMIICNRCQVAVHQECYGVSKSQDLTS--------WVCRAC 594
Cdd:cd15498     2 CSVCSEQFASNFNTSLSCYNCGLNVHASCYGITVPGKMNKvknlksykWLCDPC 55
SET_SMYD3 cd19203
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 ...
 948-1001 9.60e-03

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: 38.50  E-value: 9.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 332646729  948 ARLINHSCMPNCyariVSMGDGEDnrIVLIAKTNVAAGEELTYDYLFEVDESEE 1001
Cdd:cd19203   143 ASLLNHSCDPNC----VIVFNGPH--LLLRAIREIEVGEELTISYIDMLMPSEE 190
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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