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Conserved domains on  [gi|30696333|ref|NP_200155|]
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SET domain group 29 [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), ...
 888-1039 8.60e-76

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: 245.58  E-value: 8.60e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  888 FRERLHHLQRTEMERVCFGRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREG-KDCYLFKISEEVVVD 966
Cdd:cd10518    1 MSKRFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKRYDEEGgGGTYMFRIDEDLVID 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30696333  967 ATEKGNIARLINHSCMPNCYARIMSVgDDESRIVLIAKTTVASCEELTYDYLFDPDepDEFKVPCLCKSPNCR 1039
Cdd:cd10518   81 ATKKGNIARFINHSCDPNCYAKIITV-DGEKHIVIFAKRDIAPGEELTYDYKFPIE--DEEKIPCLCGAPNCR 150
ePHD_ATX3_4_5_like cd15663
Extended PHD finger found in Arabidopsis thaliana ATX3, -4, -5, and similar proteins; The ...
 664-775 2.27e-68

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: 223.55  E-value: 2.27e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  664 CCLCPVKGGALKPTDVETLWVHVTCAWFQPEVCFASEEKMEPALGILSIPSSNFVKICVICKQIHGSCTQCCKCSTYYHA 743
Cdd:cd15663    1 CCLCPVKGGALKPTDVEGLWVHVTCAWFRPEVCFKNEEKMEPAVGLLRIPLSTFLKACVICKQIHGSCTQCCKCATYFHA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 30696333  744 MCASRAGYRMELHCLEKNGRQITKMVSYCSYH 775
Cdd:cd15663   81 MCASRAGYHMELHCLEKNGVQITRMVSYCSFH 112
PWWP_AtATX3-like cd20143
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
 222-326 3.40e-46

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: 160.61  E-value: 3.40e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  222 YSGDLVWGKSGRnEPFWPAIVIDPMTQAPELVlRSCIPDAACVMFFGHSGTeneRDYAWVRRGMIFPFVDYVERLQEQSE 301
Cdd:cd20143    1 VEGDLVWAKVGT-HPFWPARVVEPAEQAEEVR-RRCVPGSLCVYFFGPGGS---RDYGWVRRSMIFPFTDDLARFQTQKI 75

                         90       100
                 ....*....|....*....|....*
gi 30696333  302 LRGCNPRDFQMALEEALLADQGFTE 326
Cdd:cd20143   76 KNKKRPQEFQEALEEAKLADAGFEE 100
PHD_ATX3_4_5_like cd15495
PHD finger found in Arabidopsis thaliana histone-lysine N-methyltransferase arabidopsis ...
 609-655 2.09e-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: 85.12  E-value: 2.09e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 30696333  609 RCAVCRWVEDWDYNKIIICNRCQIAVHQECYGTRNVRDFTSWVCKAC 655
Cdd:cd15495    1 RCAVCNEGEDDDNNPLITCNRCQISVHQKCYGIREVDPDGSWVCRAC 47
PHD_TCF19_like cd15517
PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ...
 415-466 6.58e-08

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: 49.85  E-value: 6.58e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30696333  415 VCGICkRIWNHLDSQSWVRCDGCKVWIHSACDQISHKHFKDlgETDYYCPTC 466
Cdd:cd15517    1 VCGIC-NLETAAVDELWVQCDGCDKWFHQFCLGLSNERYAD--EDKFKCPNC 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), ...
 888-1039 8.60e-76

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: 245.58  E-value: 8.60e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  888 FRERLHHLQRTEMERVCFGRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREG-KDCYLFKISEEVVVD 966
Cdd:cd10518    1 MSKRFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKRYDEEGgGGTYMFRIDEDLVID 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30696333  967 ATEKGNIARLINHSCMPNCYARIMSVgDDESRIVLIAKTTVASCEELTYDYLFDPDepDEFKVPCLCKSPNCR 1039
Cdd:cd10518   81 ATKKGNIARFINHSCDPNCYAKIITV-DGEKHIVIFAKRDIAPGEELTYDYKFPIE--DEEKIPCLCGAPNCR 150
ePHD_ATX3_4_5_like cd15663
Extended PHD finger found in Arabidopsis thaliana ATX3, -4, -5, and similar proteins; The ...
 664-775 2.27e-68

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: 223.55  E-value: 2.27e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  664 CCLCPVKGGALKPTDVETLWVHVTCAWFQPEVCFASEEKMEPALGILSIPSSNFVKICVICKQIHGSCTQCCKCSTYYHA 743
Cdd:cd15663    1 CCLCPVKGGALKPTDVEGLWVHVTCAWFRPEVCFKNEEKMEPAVGLLRIPLSTFLKACVICKQIHGSCTQCCKCATYFHA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 30696333  744 MCASRAGYRMELHCLEKNGRQITKMVSYCSYH 775
Cdd:cd15663   81 MCASRAGYHMELHCLEKNGVQITRMVSYCSFH 112
PWWP_AtATX3-like cd20143
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
 222-326 3.40e-46

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: 160.61  E-value: 3.40e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  222 YSGDLVWGKSGRnEPFWPAIVIDPMTQAPELVlRSCIPDAACVMFFGHSGTeneRDYAWVRRGMIFPFVDYVERLQEQSE 301
Cdd:cd20143    1 VEGDLVWAKVGT-HPFWPARVVEPAEQAEEVR-RRCVPGSLCVYFFGPGGS---RDYGWVRRSMIFPFTDDLARFQTQKI 75

                         90       100
                 ....*....|....*....|....*
gi 30696333  302 LRGCNPRDFQMALEEALLADQGFTE 326
Cdd:cd20143   76 KNKKRPQEFQEALEEAKLADAGFEE 100
zf-HC5HC2H_2 pfam13832
PHD-zinc-finger like domain;
662-775 2.76e-34

PHD-zinc-finger like domain;


Pssm-ID: 463991 [Multi-domain]  Cd Length: 109  Bit Score: 127.08  E-value: 2.76e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333    662 RECCLCPVKGGALKPTDvETLWVHVTCAWFQPEVCFASEEKMEPAlGILSIPSSNFVKICVICKQIHGSCTQCCK--CST 739
Cdd:pfam13832    1 VRCCLCPLRGGALKQTS-DGRWVHVLCAIFVPEVRFGNVATMEPI-DVSRIPPERWKLKCVFCKKRSGACIQCSKgrCTT 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 30696333    740 YYHAMCASRAGYRMELHCLEkngrqITKMVSYCSYH 775
Cdd:pfam13832   79 AFHVTCAQAAGVYMEPEDWP-----NVVVIAYCQKH 109
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 901-1024 6.45e-32

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


Pssm-ID: 214614 [Multi-domain]  Cd Length: 124  Bit Score: 120.90  E-value: 6.45e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333     901 ERVCFGRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREG-KDCYLFKISEEVVVDATEKGNIARLINH 979
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGaKAFYLFDIDSDLCIDARRKGNLARFINH 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 30696333     980 SCMPNCYARIMSVgDDESRIVLIAKTTVASCEELTYDYLFDPDEP 1024
Cdd:smart00317   81 SCEPNCELLFVEV-NGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
906-1040 4.94e-31

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 118.53  E-value: 4.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  906 GRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREGKdcYLFKISEEVVVDATEKGNIARLINHSCMPNC 985
Cdd:COG2940   11 RPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKEPLHT--YLFELDDDGVIDGALGGNPARFINHSCDPNC 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30696333  986 YARImsvgdDESRIVLIAKTTVASCEELTYDYLFDPDEPDefkVPCLCksPNCRK 1040
Cdd:COG2940   89 EADE-----EDGRIFIVALRDIAAGEELTYDYGLDYDEEE---YPCRC--PNCRG 133
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
598-778 3.14e-30

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


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 128.18  E-value: 3.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  598 YEPVNVK-WTTERCAVCRWVEDWDYNKIIICNRCQIAVHQECYGTRNVRDfTSWVCKACETPEIKRECCL-CPVKGGALK 675
Cdd:COG5141  183 VEPIEPSdEFDDICTKCTSTHNENSNAIVFCDGCEICVHQSCYGIQFLPE-GFWLCRKCIYGEYQIRCCSfCPSSDGAFK 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  676 PTDvETLWVHVTCAWFQPEVCFASEEKMEPALGILSIPSSNFVKICVICKQIHGSCTQCCK--CSTYYHAMCASRAGYRM 753
Cdd:COG5141  262 QTS-DGRWGHVICAMFNPELSFGHLLSKDPIDNIASVSSSRWKLGCLICKEFGGTCIQCSYfnCTRAYHVTCARRAGYFD 340

                        170       180
                 ....*....|....*....|....*
gi 30696333  754 ELHCLEKNGRQITKMVSYCSYHRAP 778
Cdd:COG5141  341 LNIYSHNGISYCIDHEPLCRKHYPL 365
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 912-1017 4.31e-24

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: 97.98  E-value: 4.31e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333    912 GWGLFARRNIQEGEMVLEYRGEQV-RGIIADLREARYRREGKD----CYLFKISEEV--VVDATE--KGNIARLINHSCM 982
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVLLiTKEEADKRELLYYDKLELrlwgPYLFTLDEDSeyCIDARAlyYGNWARFINHSCD 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 30696333    983 PNCYARIMSVGDDEsRIVLIAKTTVASCEELTYDY 1017
Cdd:pfam00856   81 PNCEVRVVYVNGGP-RIVIFALRDIKPGEELTIDY 114
PHD_ATX3_4_5_like cd15495
PHD finger found in Arabidopsis thaliana histone-lysine N-methyltransferase arabidopsis ...
 609-655 2.09e-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: 85.12  E-value: 2.09e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 30696333  609 RCAVCRWVEDWDYNKIIICNRCQIAVHQECYGTRNVRDFTSWVCKAC 655
Cdd:cd15495    1 RCAVCNEGEDDDNNPLITCNRCQISVHQKCYGIREVDPDGSWVCRAC 47
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 224-320 2.42e-18

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: 80.93  E-value: 2.42e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333    224 GDLVWGKsGRNEPFWPAIVIDPMTQAPELVLRSCIPDAACVMFFGHSgtenerDYAWVRRGMIFPFVDYVERLQEQSELR 303
Cdd:pfam00855    1 GDLVWAK-LKGYPWWPARVVDPEELPENVLKPKKKDGEYLVRFFGDS------EFAWVKPKDLKPFDEGDEFEYLKKKKK 73

                           90
                   ....*....|....*..
gi 30696333    304 GCNPRDFQMALEEALLA 320
Cdd:pfam00855   74 KKKKKAFKKALEEAEEA 90
PHD_TCF19_like cd15517
PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ...
 415-466 6.58e-08

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: 49.85  E-value: 6.58e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30696333  415 VCGICkRIWNHLDSQSWVRCDGCKVWIHSACDQISHKHFKDlgETDYYCPTC 466
Cdd:cd15517    1 VCGIC-NLETAAVDELWVQCDGCDKWFHQFCLGLSNERYAD--EDKFKCPNC 49
PHD_2 pfam13831
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 622-655 7.83e-07

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: 46.18  E-value: 7.83e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 30696333    622 NKIIICNRCQIAVHQECYGTRNVRDFTSWVCKAC 655
Cdd:pfam13831    2 SPLVYCSKCSVQVHASCYGVPPIPDGDGWKCRRC 35
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 224-288 1.74e-06

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 46.18  E-value: 1.74e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30696333     224 GDLVWGKSGRNePFWPAIVIDPMTQAPELVLRSCIPDAACVMFFGHsgteneRDYAWVRRGMIFP 288
Cdd:smart00293    4 GDLVWAKMKGF-PWWPALVISPKMTPDNIMKRKSDENLYPVLFFGD------KDTAWIPSSKLFP 61
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 415-469 9.67e-04

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: 38.24  E-value: 9.67e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 30696333    415 VCGICKRIWNHLDsqsWVRCDGCKVWIHSACDQIShKHFKDLGETDYYCPTCRTK 469
Cdd:pfam00628    1 YCAVCGKSDDGGE---LVQCDGCDDWFHLACLGPP-LDPAEIPSGEWLCPECKPK 51
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 415-466 4.31e-03

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 36.04  E-value: 4.31e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 30696333     415 VCGICKRiwnHLDSQSWVRCDGCKVWIHSACDQISHKhfKDLGETDYYCPTC 466
Cdd:smart00249    1 YCSVCGK---PDDGGELLQCDGCDRWYHQTCLGPPLL--EEEPDGKWYCPKC 47
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 609-655 5.68e-03

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 35.65  E-value: 5.68e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 30696333     609 RCAVCRwvEDWDYNKIIICNRCQIAVHQECYG--TRNVRDFTSWVCKAC 655
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), ...
 888-1039 8.60e-76

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: 245.58  E-value: 8.60e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  888 FRERLHHLQRTEMERVCFGRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREG-KDCYLFKISEEVVVD 966
Cdd:cd10518    1 MSKRFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKRYDEEGgGGTYMFRIDEDLVID 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30696333  967 ATEKGNIARLINHSCMPNCYARIMSVgDDESRIVLIAKTTVASCEELTYDYLFDPDepDEFKVPCLCKSPNCR 1039
Cdd:cd10518   81 ATKKGNIARFINHSCDPNCYAKIITV-DGEKHIVIFAKRDIAPGEELTYDYKFPIE--DEEKIPCLCGAPNCR 150
ePHD_ATX3_4_5_like cd15663
Extended PHD finger found in Arabidopsis thaliana ATX3, -4, -5, and similar proteins; The ...
 664-775 2.27e-68

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: 223.55  E-value: 2.27e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  664 CCLCPVKGGALKPTDVETLWVHVTCAWFQPEVCFASEEKMEPALGILSIPSSNFVKICVICKQIHGSCTQCCKCSTYYHA 743
Cdd:cd15663    1 CCLCPVKGGALKPTDVEGLWVHVTCAWFRPEVCFKNEEKMEPAVGLLRIPLSTFLKACVICKQIHGSCTQCCKCATYFHA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 30696333  744 MCASRAGYRMELHCLEKNGRQITKMVSYCSYH 775
Cdd:cd15663   81 MCASRAGYHMELHCLEKNGVQITRMVSYCSFH 112
SET_SET1 cd20072
SET domain (including post-SET domain) found in catalytic component of the Saccharomyces ...
 897-1039 6.26e-52

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: 178.77  E-value: 6.26e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  897 RTEMERVCFGRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREG-KDCYLFKISEEVVVDATEKGNIAR 975
Cdd:cd20072    9 KKRKKQLKFARSAIHNWGLYAMENISAKDMVIEYVGEVIRQQVADEREKRYLRQGiGSSYLFRIDDDTVVDATKKGNIAR 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30696333  976 LINHSCMPNCYARIMSVGdDESRIVLIAKTTVASCEELTYDYLFdpdEPDEFKVPCLCKSPNCR 1039
Cdd:cd20072   89 FINHCCDPNCTAKIIKVE-GEKRIVIYAKRDIAAGEELTYDYKF---PREEDKIPCLCGAPNCR 148
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
 891-1043 8.21e-51

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


Pssm-ID: 380947 [Multi-domain]  Cd Length: 152  Bit Score: 175.66  E-value: 8.21e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  891 RLHHLQRTEMERVCFGRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREGKDCYLFKISEEVVVDATEK 970
Cdd:cd19170    4 RFRHLRKTAKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKYYESKGIGCYMFRIDDDEVVDATMH 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30696333  971 GNIARLINHSCMPNCYARIMSVgDDESRIVLIAKTTVASCEELTYDYLFdPDEpdEFKVPCLCKSPNCRKFMN 1043
Cdd:cd19170   84 GNAARFINHSCEPNCYSRVVNI-DGKKHIVIFALRRILRGEELTYDYKF-PIE--DVKIPCTCGSKKCRKYLN 152
SET_SETD1 cd19169
SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...
 905-1039 1.29e-50

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: 175.22  E-value: 1.29e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  905 FGRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREG-KDCYLFKISEEVVVDATEKGNIARLINHSCMP 983
Cdd:cd19169   17 FAKSRIHDWGLFALEPIAADEMVIEYVGQVIRQSVADEREKRYEAIGiGSSYLFRVDDDTIIDATKCGNLARFINHSCNP 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 30696333  984 NCYARIMSVgDDESRIVLIAKTTVASCEELTYDYLFdPDEPDefKVPCLCKSPNCR 1039
Cdd:cd19169   97 NCYAKIITV-ESQKKIVIYSKRPIAVNEEITYDYKF-PIEDE--KIPCLCGAPQCR 148
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
 902-1042 4.75e-49

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: 170.69  E-value: 4.75e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  902 RVCFGRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREGKDCYLFKISEEVVVDATEKGNIARLINHSC 981
Cdd:cd19171   15 NVYLARSRIQGLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNRGIYMFRIDNDWVIDATMTGGPARYINHSC 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30696333  982 MPNCYARIMSVgDDESRIVLIAKTTVASCEELTYDYLFDPdEPDEFKVPCLCKSPNCRKFM 1042
Cdd:cd19171   95 NPNCVAEVVTF-DKEKKIIIISNRRIAKGEELTYDYKFDF-EDDQHKIPCLCGAPNCRKWM 153
PWWP_AtATX3-like cd20143
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
 222-326 3.40e-46

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: 160.61  E-value: 3.40e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  222 YSGDLVWGKSGRnEPFWPAIVIDPMTQAPELVlRSCIPDAACVMFFGHSGTeneRDYAWVRRGMIFPFVDYVERLQEQSE 301
Cdd:cd20143    1 VEGDLVWAKVGT-HPFWPARVVEPAEQAEEVR-RRCVPGSLCVYFFGPGGS---RDYGWVRRSMIFPFTDDLARFQTQKI 75

                         90       100
                 ....*....|....*....|....*
gi 30696333  302 LRGCNPRDFQMALEEALLADQGFTE 326
Cdd:cd20143   76 KNKKRPQEFQEALEEAKLADAGFEE 100
SET_KMT2A cd19206
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...
 890-1043 1.11e-44

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: 158.65  E-value: 1.11e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  890 ERLHHLQRTEMERVCFGRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREGKDCYLFKISEEVVVDATE 969
Cdd:cd19206    3 MRFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYSGNVIRSILTDKREKYYDSKGIGCYMFRIDDSEVVDATM 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30696333  970 KGNIARLINHSCMPNCYARIMSVgDDESRIVLIAKTTVASCEELTYDYLFDPDEPDEfKVPCLCKSPNCRKFMN 1043
Cdd:cd19206   83 HGNAARFINHSCEPNCYSRVINI-DGQKHIVIFAMRKIYRGEELTYDYKFPIEDASN-KLPCNCGAKKCRKFLN 154
SET_SETD1A cd19204
SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...
 901-1043 2.00e-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: 149.02  E-value: 2.00e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  901 ERVCFGRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREG-KDCYLFKISEEVVVDATEKGNIARLINH 979
Cdd:cd19204   14 KKLRFGRSRIHEWGLFAMEPIAADEMVIEYVGQNIRQVVADMREKRYVQEGiGSSYLFRVDHDTIIDATKCGNLARFINH 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30696333  980 SCMPNCYARIMSVgDDESRIVLIAKTTVASCEELTYDYLFdPDEpdEFKVPCLCKSPNCRKFMN 1043
Cdd:cd19204   94 CCTPNCYAKVITI-ESQKKIVIYSKQPIGVNEEITYDYKF-PIE--DNKIPCLCGTENCRGTLN 153
SET_KMT2B cd19207
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...
 891-1043 6.26e-38

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: 139.00  E-value: 6.26e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  891 RLHHLQRTEMERVCFGRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREGKDCYLFKISEEVVVDATEK 970
Cdd:cd19207    4 RFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDSKGIGCYMFRIDDFDVVDATMH 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30696333  971 GNIARLINHSCMPNCYARIMSVgDDESRIVLIAKTTVASCEELTYDYLFdPDEPDEFKVPCLCKSPNCRKFMN 1043
Cdd:cd19207   84 GNAARFINHSCEPNCYSRVIHV-EGQKHIVIFALRKIYRGEELTYDYKF-PIEDASNKLPCNCGAKRCRRFLN 154
SET_SETD1B cd19205
SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...
 901-1043 9.48e-37

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: 135.57  E-value: 9.48e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  901 ERVCFGRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREG-KDCYLFKISEEVVVDATEKGNIARLINH 979
Cdd:cd19205   14 KKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKRYEDEGiGSSYMFRVDHDTIIDATKCGNFARFINH 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30696333  980 SCMPNCYARIMSVgDDESRIVLIAKTTVASCEELTYDYLFdPDEPDefKVPCLCKSPNCRKFMN 1043
Cdd:cd19205   94 SCNPNCYAKVITV-ESQKKIVIYSKQHINVNEEITYDYKF-PIEDV--KIPCLCGSENCRGTLN 153
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
 901-1017 2.33e-34

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: 127.36  E-value: 2.33e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  901 ERVCFGRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREGKDcYLFKISEEVVVDATEKGNIARLINHS 980
Cdd:cd10519    1 KRLLLGKSDVAGWGLFLKEPIKKDEFIGEYTGELISQDEADRRGKIYDKYNSS-YLFNLNDQFVVDATRKGNKIRFANHS 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 30696333  981 CMPNCYARIMSVGDDEsRIVLIAKTTVASCEELTYDY 1017
Cdd:cd10519   80 SNPNCYAKVMMVNGDH-RIGIFAKRDIEAGEELFFDY 115
zf-HC5HC2H_2 pfam13832
PHD-zinc-finger like domain;
662-775 2.76e-34

PHD-zinc-finger like domain;


Pssm-ID: 463991 [Multi-domain]  Cd Length: 109  Bit Score: 127.08  E-value: 2.76e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333    662 RECCLCPVKGGALKPTDvETLWVHVTCAWFQPEVCFASEEKMEPAlGILSIPSSNFVKICVICKQIHGSCTQCCK--CST 739
Cdd:pfam13832    1 VRCCLCPLRGGALKQTS-DGRWVHVLCAIFVPEVRFGNVATMEPI-DVSRIPPERWKLKCVFCKKRSGACIQCSKgrCTT 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 30696333    740 YYHAMCASRAGYRMELHCLEkngrqITKMVSYCSYH 775
Cdd:pfam13832   79 AFHVTCAQAAGVYMEPEDWP-----NVVVIAYCQKH 109
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 901-1024 6.45e-32

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


Pssm-ID: 214614 [Multi-domain]  Cd Length: 124  Bit Score: 120.90  E-value: 6.45e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333     901 ERVCFGRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREG-KDCYLFKISEEVVVDATEKGNIARLINH 979
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGaKAFYLFDIDSDLCIDARRKGNLARFINH 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 30696333     980 SCMPNCYARIMSVgDDESRIVLIAKTTVASCEELTYDYLFDPDEP 1024
Cdd:smart00317   81 SCEPNCELLFVEV-NGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
SET_KMT2D cd19209
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...
 897-1042 7.75e-32

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: 121.73  E-value: 7.75e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  897 RTEMER-VCFGRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREGKDCYLFKISEEVVVDATEKGNIAR 975
Cdd:cd19209   11 KTEWKNnVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVIDATLTGGPAR 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30696333  976 LINHSCMPNCYARIMSVgDDESRIVLIAKTTVASCEELTYDYLFDpDEPDEFKVPCLCKSPNCRKFM 1042
Cdd:cd19209   91 YINHSCAPNCVAEVVTF-DKEDKIIIISSRRIPKGEELTYDYQFD-FEDDQHKIPCHCGAWNCRKWM 155
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
906-1040 4.94e-31

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 118.53  E-value: 4.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  906 GRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREGKdcYLFKISEEVVVDATEKGNIARLINHSCMPNC 985
Cdd:COG2940   11 RPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPHKEPLHT--YLFELDDDGVIDGALGGNPARFINHSCDPNC 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30696333  986 YARImsvgdDESRIVLIAKTTVASCEELTYDYLFDPDEPDefkVPCLCksPNCRK 1040
Cdd:COG2940   89 EADE-----EDGRIFIVALRDIAAGEELTYDYGLDYDEEE---YPCRC--PNCRG 133
SET_KMT2C cd19208
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...
 903-1042 1.54e-30

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: 117.81  E-value: 1.54e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  903 VCFGRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREGKDCYLFKISEEVVVDATEKGNIARLINHSCM 982
Cdd:cd19208   17 VYLARSRIQGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNRGVYMFRIDNDHVIDATLTGGPARYINHSCA 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  983 PNCYARIMSVgDDESRIVLIAKTTVASCEELTYDYLFDPdEPDEFKVPCLCKSPNCRKFM 1042
Cdd:cd19208   97 PNCVAEVVTF-EKGHKIIISSSRRIQKGEELCYDYKFDF-EDDQHKIPCHCGAVNCRKWM 154
COG5141 COG5141
PHD zinc finger-containing protein [General function prediction only];
598-778 3.14e-30

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


Pssm-ID: 227470 [Multi-domain]  Cd Length: 669  Bit Score: 128.18  E-value: 3.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  598 YEPVNVK-WTTERCAVCRWVEDWDYNKIIICNRCQIAVHQECYGTRNVRDfTSWVCKACETPEIKRECCL-CPVKGGALK 675
Cdd:COG5141  183 VEPIEPSdEFDDICTKCTSTHNENSNAIVFCDGCEICVHQSCYGIQFLPE-GFWLCRKCIYGEYQIRCCSfCPSSDGAFK 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  676 PTDvETLWVHVTCAWFQPEVCFASEEKMEPALGILSIPSSNFVKICVICKQIHGSCTQCCK--CSTYYHAMCASRAGYRM 753
Cdd:COG5141  262 QTS-DGRWGHVICAMFNPELSFGHLLSKDPIDNIASVSSSRWKLGCLICKEFGGTCIQCSYfnCTRAYHVTCARRAGYFD 340

                        170       180
                 ....*....|....*....|....*
gi 30696333  754 ELHCLEKNGRQITKMVSYCSYHRAP 778
Cdd:COG5141  341 LNIYSHNGISYCIDHEPLCRKHYPL 365
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
 912-1039 7.69e-30

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


Pssm-ID: 380929  Cd Length: 136  Bit Score: 115.43  E-value: 7.69e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  912 GWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREG-KDCYLFKISEEVVVDATEKGNIARLINHSCMPNCYARIM 990
Cdd:cd10531   11 GWGVKAKEDIQKGEFIIEYVGEVIDKKEFKERLDEYEELGkSNFYILSLSDDVVIDATRKGNLSRFINHSCEPNCETQKW 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 30696333  991 SVgDDESRIVLIAKTTVASCEELTYDYLFdpDEPDEFKVPCLCKSPNCR 1039
Cdd:cd10531   91 IV-NGEYRIGIFALRDIPAGEELTFDYNF--VNYNEAKQVCLCGAQNCR 136
ePHD_JADE cd15671
Extended PHD finger found in protein Jade-1, Jade-2, Jade-3 and similar proteins; The extended ...
 664-775 2.11e-29

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: 113.31  E-value: 2.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  664 CCLCPVKGGALKPTDVETLWVHVTCAWFQPEVCFASEEKMEPALGILSIPSSNFVKICVICKQIHGSCTQCC--KCSTYY 741
Cdd:cd15671    1 CVLCPKKGGAMKSTKSGTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPMSRWALVCVLCKEKTGACIQCSvkSCKTAF 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 30696333  742 HAMCASRAGYRMELhCLEKNGRQItKMVSYCSYH 775
Cdd:cd15671   81 HVTCAFQHGLEMKT-ILEDEDDEV-KFKSYCPKH 112
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
 907-1042 4.36e-28

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: 110.36  E-value: 4.36e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  907 RSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREGKDCYLF-KISEEVVVDATEKGNIARLINHSCMPNC 985
Cdd:cd19172    8 RTEKKGWGLRAAEDLPKGTFVIEYVGEVLDEKEFKRRMKEYAREGNRHYYFmALKSDEIIDATKKGNLSRFINHSCEPNC 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 30696333  986 YARIMSVGdDESRIVLIAKTTVASCEELTYDYLFD--PDEPdefkVPCLCKSPNCRKFM 1042
Cdd:cd19172   88 ETQKWTVN-GELRVGFFAKRDIPAGEELTFDYQFEryGKEA----QKCYCGSPNCRGYI 141
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
 912-1043 1.33e-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: 108.92  E-value: 1.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  912 GWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREGKDCYLFKISEEVVVDATEKGNIARLINHSCMPNCYARIMS 991
Cdd:cd19174   11 GWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRMIEQYHNHSHHYCLNLDSGMVIDGYRMGNEARFVNHSCDPNCEMQKWS 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30696333  992 VgDDESRIVLIAKTTVASCEELTYDYLFDPDEPDEfKVPCLCKSPNCRKFMN 1043
Cdd:cd19174   91 V-NGVYRIGLFALKDIPAGEELTYDYNFHSFNVEK-QQPCKCGSPNCRGVIG 140
SET_ASHR3-like cd19175
SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...
 912-1042 1.27e-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: 106.35  E-value: 1.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  912 GWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREG-KDCYLFKISEEVVVDATEKGNIARLINHSCMPNCYARIM 990
Cdd:cd19175   11 GWGLVADEDINAGEFIIEYVGEVIDDKTCEERLWDMKHKGeKNFYMCEIDKDMVIDATFKGNLSRFINHSCDPNCELQKW 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30696333  991 SVgDDESRIVLIAKTTVASCEELTYDYLFDPDEPDefkVPCLCKSPNCRKFM 1042
Cdd:cd19175   91 QV-DGETRIGVFAIRDIKKGEELTYDYQFVQFGAD---QDCHCGSKNCRGKL 138
ePHD cd15571
Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is ...
 664-775 2.57e-25

Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. The extended PHD finger is characterized as Cys2HisCys5HisCys2His, which has been found in a variety of eukaryotic proteins involved in the control of gene transcription and chromatin dynamics. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. They also function as epigenome readers controlling gene expression through molecular recruitment of multi-protein complexes of chromatin regulators and transcription factors.


Pssm-ID: 277046 [Multi-domain]  Cd Length: 112  Bit Score: 101.51  E-value: 2.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  664 CCLCPVKGGALKP-----TDVETLWVHVTCAWFQPEVCFASEEKMEPaLGILSIPSSNFVKICVICKQIHGSCTQCC--K 736
Cdd:cd15571    1 CALCPRSGGALKGggalkTTSDGLWVHVVCALWSPEVYFDDGTLLEV-EGVSKIPKRRKKLKCSICGKRGGACIQCSypG 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 30696333  737 CSTYYHAMCASRAGYRMELHclekngRQITKMVSYCSYH 775
Cdd:cd15571   80 CPRSFHVSCAIRAGCLFEFE------DGPGNFVVYCPKH 112
ePHD_RNO cd15707
Extended PHD finger found in Drosophila melanogaster PHD finger protein rhinoceros (RNO) and ...
 664-775 1.15e-24

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: 99.59  E-value: 1.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  664 CCLCPVKGGALKPTDVETLWVHVTCAWFQPEVCFASEEKMEPALGILSIPSSNFVKICVICKQIHGSCTQCC--KCSTYY 741
Cdd:cd15707    1 CILCPNKGGAMKSTRSGTKWAHVSCALWIPEVSIGCVEKMEPITKISSIPASRWALICVLCRERTGACIQCSvkTCKTAY 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 30696333  742 HAMCASRAGYRMELHcLEKNGRQITKMVSYCSYH 775
Cdd:cd15707   81 HVTCGFQHGLEMKTI-LDEESEDGVKLRSYCQKH 113
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 912-1017 4.31e-24

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: 97.98  E-value: 4.31e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333    912 GWGLFARRNIQEGEMVLEYRGEQV-RGIIADLREARYRREGKD----CYLFKISEEV--VVDATE--KGNIARLINHSCM 982
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVLLiTKEEADKRELLYYDKLELrlwgPYLFTLDEDSeyCIDARAlyYGNWARFINHSCD 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 30696333    983 PNCYARIMSVGDDEsRIVLIAKTTVASCEELTYDY 1017
Cdd:pfam00856   81 PNCEVRVVYVNGGP-RIVIFALRDIKPGEELTIDY 114
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 912-1042 7.31e-24

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


Pssm-ID: 380940 [Multi-domain]  Cd Length: 245  Bit Score: 101.60  E-value: 7.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  912 GWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREGkDCYLF-----KISEEVVVDATEKGNIARLINHSCMPN-- 984
Cdd:cd10542   99 GWGVKTLEDIKKGTFVMEYVGEIITSEEAERRGKIYDANG-RTYLFdldynDDDCEYTVDAAYYGNISHFINHSCDPNla 177

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30696333  985 CYARIMSVGD-DESRIVLIAKTTVASCEELTYDYLFDPDE---------PDEFKVPCLCKSPNCRKFM 1042
Cdd:cd10542  178 VYAVWINHLDpRLPRIAFFAKRDIKAGEELTFDYLMTGTGgssestipkPKDVRVPCLCGSKNCRKYL 245
ePHD_BRPF cd15670
Extended PHD finger found in BRPF proteins; The extended plant homeodomain (ePHD) zinc finger ...
 664-775 3.81e-23

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: 95.48  E-value: 3.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  664 CCLCPVKGGALKPTDvETLWVHVTCAWFQPEVCFASEEKMEPALGILSIPSSNFVKICVICKQIHGSCTQCCK--CSTYY 741
Cdd:cd15670    1 CVLCPNKGGAFKQTD-DGRWAHVVCALWIPEVSFANTVFLEPIDGIQNIPKARWKLTCYICKKRMGACIQCHKknCYTAF 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 30696333  742 HAMCASRAGYRMEL-HCLEKNGRQI--TKMVSYCSYH 775
Cdd:cd15670   80 HVTCAQQAGLYMKIePVKDPGNGTSdsVRKEAYCDKH 116
SET_NSD cd19173
SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...
 912-1042 1.38e-22

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: 94.69  E-value: 1.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  912 GWGLFARRNIQEGEMVLEYRGEqvrgiIADLREARYRREGK------DCYLFKISEEVVVDATEKGNIARLINHSCMPNC 985
Cdd:cd19173   13 GWGLRTKRDIKKGDFVIEYVGE-----LIDEEECRRRLKKAhennitNFYMLTLDKDRIIDAGPKGNLSRFMNHSCQPNC 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 30696333  986 YARIMSVGDDeSRIVLIAKTTVASCEELTYDYLFDpDEPDEfKVPCLCKSPNCRKFM 1042
Cdd:cd19173   88 ETQKWTVNGD-TRVGLFAVRDIPAGEELTFNYNLD-CLGNE-KKVCRCGAPNCSGFL 141
ePHD_ATX1_2_like cd15662
Extended PHD finger found in Arabidopsis thaliana ATX1, -2, and similar proteins; The extended ...
 664-775 2.39e-22

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: 92.92  E-value: 2.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  664 CCLCPVKGGALKPTdVETLWVHVTCAWFQPEVCFASEEKMEPALGILSIPSSNFVKICVICKQIHGSCTQCCK--CSTYY 741
Cdd:cd15662    1 CCLCPVVGGALKPT-TDGRWAHLACAIWIPETCLLDVKTMEPVDGINAISKERWELSCTICKQRYGACIQCSNnsCRVAY 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 30696333  742 HAMCASRAGYRMEL--HCLEKNGRQITKMVSYCSYH 775
Cdd:cd15662   80 HPLCARAAGLCMEVadEGGEDPGDQGLRLLSYCPRH 115
ePHD_JADE2 cd15705
Extended PHD finger found in protein Jade-2 and similar proteins; The extended plant ...
 664-775 3.38e-22

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: 92.47  E-value: 3.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  664 CCLCPVKGGALKPTDVETLWVHVTCAWFQPEVCFASEEKMEPALGILSIPSSNFVKICVICKQIHGSCTQCC--KCSTYY 741
Cdd:cd15705    1 CLLCPKRGGALKPTRSGTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKECTGTCIQCSmpSCITAF 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 30696333  742 HAMCASRAGyrMELHCLEKNGRQItKMVSYCSYH 775
Cdd:cd15705   81 HVTCAFDHG--LEMRTTLADNDEV-KFKSFCLEH 111
ePHD_BRPF1 cd15701
Extended PHD finger found in bromodomain and PHD finger-containing protein 1 (BRPF1) and ...
 664-778 7.71e-22

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: 92.06  E-value: 7.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  664 CCLCPVKGGALKPTDvETLWVHVTCAWFQPEVCFASEEKMEPALGILSIPSSNFVKICVICKQI-HGSCTQCCK--CSTY 740
Cdd:cd15701    1 CALCPNKGGAFKQTD-DGRWAHVVCALWIPEVCFANTVFLEPIDSIEHIPPARWKLTCYICKQRgSGACIQCHKanCYTA 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 30696333  741 YHAMCASRAGYRMELHCLEKNGRQIT----KMVSYCSYHRAP 778
Cdd:cd15701   80 FHVTCAQQAGLYMKMEPVRETGANGTsfsvRKTAYCDIHTPP 121
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
 912-1017 1.79e-21

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: 90.86  E-value: 1.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  912 GWGLFARRNIQEGEMVLEYRGEQVRGiiaDLREARYRREGKDCYLFKIS-EEVVVDATEKGNIARLINHSCMPNCYARIM 990
Cdd:cd10522   14 GLGLFAAETIAKGEFVGEYTGEVLDR---WEEDRDSVYHYDPLYPFDLNgDILVIDAGKKGNLTRFINHSDQPNLELIVR 90

                         90       100
                 ....*....|....*....|....*..
gi 30696333  991 SVGDDEsRIVLIAKTTVASCEELTYDY 1017
Cdd:cd10522   91 TLKGEQ-HIGFVAIRDIKPGEELFISY 116
SET_EZH2 cd19218
SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...
 908-1017 3.21e-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: 89.97  E-value: 3.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  908 SGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREGkdC-YLFKISEEVVVDATEKGNIARLINHSCMPNCY 986
Cdd:cd19218   11 SDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYM--CsFLFNLNNDFVVDATRKGNKIRFANHSVNPNCY 88

                         90       100       110
                 ....*....|....*....|....*....|.
gi 30696333  987 ARIMSVGDDEsRIVLIAKTTVASCEELTYDY 1017
Cdd:cd19218   89 AKVMMVNGDH-RIGIFAKRAIQTGEELFFDY 118
ePHD_BRPF3 cd15703
Extended PHD finger found in bromodomain and PHD finger-containing protein 3 (BRPF3) and ...
 664-775 4.96e-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: 4.96e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  664 CCLCPVKGGALKPTDvETLWVHVTCAWFQPEVCFASEEKMEPALGILSIPSSNFVKICVICKQI-HGSCTQCCK--CSTY 740
Cdd:cd15703    1 CVLCPNKGGAFKQTS-DGRWAHVVCAIWIPEVCFANTVFLEPVEGVNNIPPARWKLTCYLCKQKgRGAAIQCHKvnCYTA 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 30696333  741 YHAMCASRAGYRMELHCLEKNGRQIT----KMVSYCSYH 775
Cdd:cd15703   80 FHVTCAQRAGLFMKIEPVRETGLNGTtftvRKTAYCENH 118
ePHD_JADE1 cd15704
Extended PHD finger found in protein Jade-1 and similar proteins; The extended plant ...
 663-775 6.89e-21

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: 88.97  E-value: 6.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  663 ECCLCPVKGGALKPTDVETLWVHVTCAWFQPEVCFASEEKMEPALGILSIPSSNFVKICVICKQIHGSCTQCC--KCSTY 740
Cdd:cd15704    3 KCLLCPKKGGAMKPTRSGTKWVHVSCALWIPEVSIGSPEKMEPITKVSHIPSSRWALVCSLCNEKVGASIQCSvkNCRTA 82

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 30696333  741 YHAMCASRAGYRMELHCLEKNGrqiTKMVSYCSYH 775
Cdd:cd15704   83 FHVTCAFDRGLEMKTILAENDE---VKFKSYCPKH 114
ePHD_JADE3 cd15706
Extended PHD finger found in protein Jade-3 and similar proteins; The extended plant ...
 664-775 7.42e-21

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: 88.63  E-value: 7.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  664 CCLCPVKGGALKPTDVETLWVHVTCAWFQPEVCFASEEKMEPALGILSIPSSNFVKICVICKQIHGSCTQCC--KCSTYY 741
Cdd:cd15706    1 CLLCPKTGGAMKATRTGTKWAHVSCALWIPEVSIACPERMEPITKVSHIPPSRWALVCSLCKLKTGACIQCSvkSCITAF 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 30696333  742 HAMCASRAGyrMELHCLEKNGRQItKMVSYCSYH 775
Cdd:cd15706   81 HVTCAFEHS--LEMKTILDEGDEV-KFKSYCLKH 111
PHD_ATX3_4_5_like cd15495
PHD finger found in Arabidopsis thaliana histone-lysine N-methyltransferase arabidopsis ...
 609-655 2.09e-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: 85.12  E-value: 2.09e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 30696333  609 RCAVCRWVEDWDYNKIIICNRCQIAVHQECYGTRNVRDFTSWVCKAC 655
Cdd:cd15495    1 RCAVCNEGEDDDNNPLITCNRCQISVHQKCYGIREVDPDGSWVCRAC 47
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
 912-1042 2.31e-20

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: 88.51  E-value: 2.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  912 GWGLFARRNIQEGEMVLEYRGEqvrgiIADLREARYR-REGKD-----CYLFKISEEVVVDATEKGNIARLINHSCMPNC 985
Cdd:cd19211   13 GWGLIAKRDIKKGEFVNEYVGE-----LIDEEECMARiKHAHEndithFYMLTIDKDRIIDAGPKGNYSRFMNHSCQPNC 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 30696333  986 YARIMSVGDDeSRIVLIAKTTVASCEELTYDYLFD--PDEpdefKVPCLCKSPNCRKFM 1042
Cdd:cd19211   88 ETQKWTVNGD-TRVGLFAVCDIPAGTELTFNYNLDclGNE----KTVCRCGAPNCSGFL 141
SET_EZH1 cd19217
SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...
 896-1019 4.47e-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: 87.43  E-value: 4.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  896 QRTEMERVCFGRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREgKDCYLFKISEEVVVDATEKGNIAR 975
Cdd:cd19217    1 QRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYDKY-MSSFLFNLNNDFVVDATRKGNKIR 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 30696333  976 LINHSCMPNCYARIMSVGDDEsRIVLIAKTTVASCEELTYDYLF 1019
Cdd:cd19217   80 FANHSVNPNCYAKVVMVNGDH-RIGIFAKRAIQQGEELFFDYRY 122
SET_SETD8 cd10528
SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2. ...
 912-1017 7.91e-20

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: 86.86  E-value: 7.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  912 GWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRR-EGKDCYL--FKISEEVV-VDAT-EKGNIARLINHSCM-PNC 985
Cdd:cd10528   28 GRGVIATRPFEKGDFVVEYHGDLITITEAKKREALYAKdPSTGCYMyyFQYKGKTYcVDATkESGRLGRLINHSKKkPNL 107

                         90       100       110
                 ....*....|....*....|....*....|..
gi 30696333  986 YARIMSVgDDESRIVLIAKTTVASCEELTYDY 1017
Cdd:cd10528  108 KTKLLVI-DGVPHLILVAKRDIKPGEELLYDY 138
ePHD_AF10_like cd15672
Extended PHD finger found in protein AF-10 and AF-17; The extended plant homeodomain (ePHD) ...
 664-775 9.53e-19

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: 82.89  E-value: 9.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  664 CCLCPVKGGALKPTDvETLWVHVTCAWFQPEVCFASEEKMEPALgILSIPSSNFVKICVIC-------KQIHGSCTQCCK 736
Cdd:cd15672    1 CELCPHKDGALKRTD-NGGWAHVVCALYIPEVRFGNVATMEPII-LQDVPQDRFNKTCYICeeqgresKASTGACMQCNK 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 30696333  737 --CSTYYHAMCASRAGyrmeLHCLEK-NGRQITKMVSYCSYH 775
Cdd:cd15672   79 sgCKQSFHVTCAQMAG----LLCEEAgNYSDNVKYCGYCSYH 116
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 224-320 2.42e-18

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: 80.93  E-value: 2.42e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333    224 GDLVWGKsGRNEPFWPAIVIDPMTQAPELVLRSCIPDAACVMFFGHSgtenerDYAWVRRGMIFPFVDYVERLQEQSELR 303
Cdd:pfam00855    1 GDLVWAK-LKGYPWWPARVVDPEELPENVLKPKKKDGEYLVRFFGDS------EFAWVKPKDLKPFDEGDEFEYLKKKKK 73

                           90
                   ....*....|....*..
gi 30696333    304 GCNPRDFQMALEEALLA 320
Cdd:pfam00855   74 KKKKKAFKKALEEAEEA 90
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
 912-1042 2.74e-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: 85.81  E-value: 2.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  912 GWGLFARRNIQEGEMVLEYRGEqvrgiIADLREARYR----REGKDCYLFKISE--------EVVVDATEKGNIARLINH 979
Cdd:cd10544  101 GWGLRTLEFIPKGRFVCEYAGE-----VIGFEEARRRtksqTKGDMNYIIVLREhlssgkvlETFVDPTYIGNIGRFLNH 175

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30696333  980 SCMPNCYARIMSVGDDESRIVLIAKTTVASCEELTYDY------------LFDPDEPDEFKvPCLCKSPNCRKFM 1042
Cdd:cd10544  176 SCEPNLFMVPVRVDSMVPKLALFAARDIVAGEELSFDYsgefsnsvesvtLARQDESKSRK-PCLCGAENCRGFL 249
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
 912-1042 3.66e-18

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: 82.28  E-value: 3.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  912 GWGLFARRNIQEGEMVLEYRGEQVrgiiaDLREAR----YRREGKDC--YLFKISEEVVVDATEKGNIARLINHSCMPNC 985
Cdd:cd19210   13 GWGLRCKTDIKKGEFVNEYVGELI-----DEEECRarirYAQEHDITnfYMLTLDKDRIIDAGPKGNYARFMNHCCQPNC 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 30696333  986 YARIMSVGDDeSRIVLIAKTTVASCEELTYDYlfDPDEPDEFKVPCLCKSPNCRKFM 1042
Cdd:cd19210   88 ETQKWTVNGD-TRVGLFALCDIKAGTELTFNY--NLECLGNGKTVCKCGAPNCSGFL 141
ePHD_BRPF2 cd15702
Extended PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and ...
 664-775 4.05e-18

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: 81.25  E-value: 4.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  664 CCLCPVKGGALKPTDVETlWVHVTCAWFQPEVCFASEEKMEPALGILSIPSSNFVKICVICKQIH-GSCTQCCK--CSTY 740
Cdd:cd15702    1 CVLCPNKGGAFKKTDDDR-WGHVVCALWIPEVGFANTVFIEPIDGVRNIPPARWKLTCYLCKQKGvGACIQCHKanCYTA 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 30696333  741 YHAMCASRAGYRMELHCL-EKNGRQIT---KMVSYCSYH 775
Cdd:cd15702   80 FHVTCAQKAGLYMKMEPVkEVTGGGTTfsvRKTAYCDAH 118
SET_NSD3 cd19212
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
 912-1042 4.95e-18

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


Pssm-ID: 380989 [Multi-domain]  Cd Length: 142  Bit Score: 81.90  E-value: 4.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  912 GWGLFARRNIQEGEMVLEYRGEQVrgiiaDLREARYR------REGKDCYLFKISEEVVVDATEKGNIARLINHSCMPNC 985
Cdd:cd19212   13 GWGLRTKRSIKKGEFVNEYVGELI-----DEEECRLRikraheNSVTNFYMLTVTKDRIIDAGPKGNYSRFMNHSCNPNC 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 30696333  986 YARIMSVGDDeSRIVLIAKTTVASCEELTYDYlfDPDEPDEFKVPCLCKSPNCRKFM 1042
Cdd:cd19212   88 ETQKWTVNGD-VRVGLFALCDIPAGMELTFNY--NLDCLGNGRTECHCGADNCSGFL 141
SET_SETDB-like cd10538
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
 894-1017 3.22e-17

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


Pssm-ID: 380936 [Multi-domain]  Cd Length: 217  Bit Score: 81.65  E-value: 3.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  894 HLQRTEMERVCFGRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREGkDCYLFKIS---------EEVV 964
Cdd:cd10538   82 VVQRGLQARLQVFRTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRGKIYDKSG-GSYLFDLDefsdsdgdgEELC 160

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 30696333  965 VDATEKGNIARLINHSCMPNCYA-RIMSVGDDES--RIVLIAKTTVASCEELTYDY 1017
Cdd:cd10538  161 VDATFCGNVSRFINHSCDPNLFPfNVVIDHDDLRypRIALFATRDILPGEELTFDY 216
PWWP cd05162
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
 224-320 2.29e-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: 74.84  E-value: 2.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  224 GDLVWGKSgRNEPFWPAIVIDPmTQAPELVLRSCIPDAACVMFFGhsgtenERDYAWVRRGMIFPFVDYVErlqEQSELR 303
Cdd:cd05162    1 GDLVWAKL-KGYPWWPARVVDP-EELPEEVGKKKKKGGVLVQFFG------DNDYAWVKSKNIKPFEEGFK---KEFKKK 69

                         90
                 ....*....|....*..
gi 30696333  304 GCNPRDFQMALEEALLA 320
Cdd:cd05162   70 KKKSKKFKKAVEEAEEA 86
SET_EZH-like cd19168
SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb ...
 901-1017 2.50e-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: 76.07  E-value: 2.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  901 ERVCFGRSGIH-GWGLFARRNIQEGEMVLEYRGEqvrgIIADLREAryRREGKD-----CYLFKISEEVVVDATEKGNIA 974
Cdd:cd19168    1 KAVVLGKSQLEcGLGLFAAEDIKEGEFVIEYTGE----LISHDEGV--RREHRRgdvsyLYLFEEQEGIWVDAAIYGNLS 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 30696333  975 RLINH----SCMPNCYARIMSVgDDESRIVLIAKTTVASCEELTYDY 1017
Cdd:cd19168   75 RYINHatdkVKTGNCMPKIMYV-NHEWRIKFTAIKDIKIGEELFFNY 120
ePHD_JMJD2 cd15675
Extended PHD finger found in Jumonji domain-containing protein 2 (JMJD2) family of histone ...
 664-754 7.66e-16

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: 74.32  E-value: 7.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  664 CCLCPVKGGALKPTdVETLWVHVTCAWFQPEVCFASEEKMEPaLGILSIPSSNFVKICVICKQI------HGSCTQCC-- 735
Cdd:cd15675    1 CCLCCLRGGALKPT-TDGRWAHVVCAIAIPEVRFSNVPERGP-IDISKIPPARLKLKCIYCSKItksmshMGACIQCStg 78

                         90
                 ....*....|....*....
gi 30696333  736 KCSTYYHAMCASRAGYRME 754
Cdd:cd15675   79 KCTTSFHVTCAHAAGVQME 97
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
 685-775 1.56e-15

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: 72.75  E-value: 1.56e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333    685 HVTCAWFQPEVCFASEEK-MEPALGILSIPSSNFVKICVICKQIHGSCTQCCK--CSTYYHAMCASRAGYRMELHclEKN 761
Cdd:pfam13771    1 HVVCALWSPELVQRGNDSmGFPIEDIEKIPKRRWKLKCYLCKKKGGACIQCSKknCRRAFHVTCALEAGLLMQFD--EDN 78

                           90
                   ....*....|....
gi 30696333    762 GrqitKMVSYCSYH 775
Cdd:pfam13771   79 G----TFKSYCKKH 88
ePHD_AF10 cd15708
Extended PHD finger found in protein AF-10 and similar proteins; The extended plant ...
 664-775 4.36e-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: 72.80  E-value: 4.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  664 CCLCPVKGGALKPTDvETLWVHVTCAWFQPEVCFASEEKMEPALgILSIPSSNFVKICVIC-------KQIHGSCTQCCK 736
Cdd:cd15708    5 CELCPHKDGALKRTD-NGGWAHVVCALYIPEVQFANVSTMEPIV-LQSVPHERYNKTCYICdeqgresKAATGACMTCNK 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 30696333  737 --CSTYYHAMCASRAGYRMElhcLEKNGRQITKMVSYCSYH 775
Cdd:cd15708   83 hgCRQAFHVTCAQLAGLLCE---EEGNGADNVQYCGYCKYH 120
ePHD_JMJD2B cd15714
Extended PHD finger found in Jumonji domain-containing protein 2B (JMJD2B); The extended plant ...
 664-754 7.38e-15

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: 71.51  E-value: 7.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  664 CCLCPVKGGALKPTdVETLWVHVTCAWFQPEVCFASEEKMEPaLGILSIPSSNFVKICVIC----KQIHGSCTQCC--KC 737
Cdd:cd15714    1 CCLCNLRGGALQMT-TDERWVHVICAIAVPEARFLNVIERHP-VDVSAIPEQRWKLKCVYCrkrmKKVSGACIQCSydHC 78

                         90
                 ....*....|....*..
gi 30696333  738 STYYHAMCASRAGYRME 754
Cdd:cd15714   79 STSFHVTCAHAAGVVME 95
SET_SUV39H_DIM5-like cd19473
SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...
 912-1042 2.83e-14

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


Pssm-ID: 380996 [Multi-domain]  Cd Length: 274  Bit Score: 74.28  E-value: 2.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  912 GWGLFARRNIQEGEMVLEYRGEqvrgIIADLrEARYRREG------KDCYLFKI--------------SEEVVVDATEKG 971
Cdd:cd19473  117 GWGVRSTVDIKRGQFVDCYVGE----IITPE-EAQRRRDAatiaqrKDVYLFALdkfsdpdsldprlrGDPYEIDGEFMS 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  972 NIARLINHSCMPNCyaRIMS-VGDDESR----IVLIAKTTVASCEELTYDYL---------FDPDEPDEFKVPCLCKSPN 1037
Cdd:cd19473  192 GPTRFINHSCDPNL--RIFArVGDHADKhihdLAFFAIKDIPRGTELTFDYVdgvtgldddAGDEEKEKEMTKCLCGSPK 269


                 ....*
gi 30696333 1038 CRKFM 1042
Cdd:cd19473  270 CRGYL 274
ePHD_Snt2p_like cd15667
Extended PHD finger found in Saccharomyces cerevisiae SANT domain-containing protein 2 (Snt2p) ...
 651-746 7.51e-14

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: 69.72  E-value: 7.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  651 VCKACETPEIKRECCLCPVKGGALKPTDVETlWVHVTCAWFQPEVCFASEEKMEPALGILSIPSSNFVKICVICKQIHGS 730
Cdd:cd15667    3 LCNAKESNYELAKKQSPRTRPDALKCTSNGT-WCHVLCALFNEDIKFGNSKSLQPILNTESVLLKGSRQKCEICKVSGGG 81

                         90
                 ....*....|....*.
gi 30696333  731 CTQCCKCSTYYHAMCA 746
Cdd:cd15667   82 LVKCEVCDDRFHVSCA 97
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
 914-1020 9.25e-14

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: 68.84  E-value: 9.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  914 GLFARRNIQEGEMVLEYRGEQVrgIIADLREARYRREGKDCYLFKIS----EEVVVDATEKGNIARLINHSCMPNCYARI 989
Cdd:cd10529   18 GLVATEDISPGEPILEYKGEVS--LRSEFKEDNGFFKRPSPFVFFYDgfegLPLCVDARKYGNEARFIRRSCRPNAELRH 95

                         90       100       110
                 ....*....|....*....|....*....|.
gi 30696333  990 MSVGDDESRIVLIAKTTVASCEELTYDYLFD 1020
Cdd:cd10529   96 VVVSNGELRLFIFALKDIRKGTEITIPFDYD 126
SET_SUV39H_Clr4-like cd20073
SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 ...
 912-1042 1.40e-13

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: 71.83  E-value: 1.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  912 GWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREGKdCYLF-------KISEEVVVDATEKGNIARLINHSCMPN 984
Cdd:cd20073  104 GWGLRCPRFIKAGTFIGVYLGEVITQSEAEIRGKKYDNVGV-TYLFdldlfedQVDEYYTVDAQYCGDVTRFINHSCDPN 182

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30696333  985 CYARIMSVGDDESRI---VLIAKTTVASCEELTYDYLFDPDEPD---------------EFKVPCLCKSPNCRKFM 1042
Cdd:cd20073  183 LAIYSVLRDKSDSKIydlAFFAIKDIPALEELTFDYSGRNNFDQlgfignrsnskyinlKNKRPCYCGSANCRGWL 258
ePHD_JMJD2C cd15715
Extended PHD finger found in Jumonji domain-containing protein 2C (JMJD2C); The extended plant ...
 664-754 4.11e-13

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: 66.52  E-value: 4.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  664 CCLCPVKGGALKPTDvETLWVHVTCAWFQPEVCFASEEKMEPaLGILSIPSSNFVKICVIC----KQIHGSCTQCC--KC 737
Cdd:cd15715    1 CCLCNLRGGALKQTS-DDKWAHVMCAVALPEVRFINVVERTP-IDISRIPLQRLKLKCIFCrnriKRVSGACIQCSygRC 78

                         90
                 ....*....|....*..
gi 30696333  738 STYYHAMCASRAGYRME 754
Cdd:cd15715   79 PASFHVTCAHAAGVLME 95
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 912-1042 4.74e-13

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


Pssm-ID: 380923 [Multi-domain]  Cd Length: 255  Bit Score: 70.31  E-value: 4.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  912 GWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREGKdCYLFKIS--EEV-VVDATEKGNIARLINHSCMPNCYAR 988
Cdd:cd10525   98 GWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGA-TYLFDLDyvEDVyTVDAAYYGNISHFVNHSCDPNLQVY 176

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30696333  989 ---IMSVGDDESRIVLIAKTTVASCEELTYDYLFDPDEPD---------------------EFKVPCLCKSPNCRKFM 1042
Cdd:cd10525  177 nvfIDNLDERLPRIALFATRTIRAGEELTFDYNMQVDPVDaestkmdsnfglaglpgspkkRVRIECKCGVRSCRKYL 254
ePHD_AF17 cd15709
Extended PHD finger found in protein AF-17 and similar proteins; The extended plant ...
 664-775 2.08e-12

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: 65.08  E-value: 2.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  664 CCLCPVKGGALKPTDvETLWVHVTCAWFQPEVCFASEEKMEPALgILSIPSSNFVKICVIC-------KQIHGSCTQCCK 736
Cdd:cd15709    5 CELCPHKDGALKRTD-NGGWAHVVCALYIPEVQFANVLTMEPIV-LQYVPHDRFNKTCYICeeqgresKAASGACMTCNR 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 30696333  737 --CSTYYHAMCASRAGYRMELHCLEKNGrqiTKMVSYCSYH 775
Cdd:cd15709   83 hgCRQAFHVTCAQMAGLLCEEEVLEVDN---VKYCGYCKYH 120
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 912-1042 3.62e-12

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


Pssm-ID: 380930 [Multi-domain]  Cd Length: 243  Bit Score: 67.61  E-value: 3.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  912 GWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREGkDCYLFKI---SEEVVVDATEKGNIARLINHSCMPNCyaR 988
Cdd:cd10532   96 GWGVKTLQKIKKNSFVMEYVGEVITSEEAERRGQFYDSKG-ITYLFDLdyeSDEFTVDAARYGNVSHFVNHSCDPNL--Q 172

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30696333  989 IMSVGDDE-----SRIVLIAKTTVASCEELTYDYLF------DPDEPD------EFKVPCLCKSPNCRKFM 1042
Cdd:cd10532  173 VFNVFIDNldtrlPRIALFSTRTIKAGEELTFDYQMkgsgdlSSDSIDnspakkRVRTVCKCGAVTCRGYL 243
ePHD_PHF14 cd15674
Extended PHD finger found in PHD finger protein 14 (PHF14) and similar proteins; The extended ...
 664-750 1.29e-11

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: 62.40  E-value: 1.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  664 CCLCPVKGGALKPTDVETlWVHVTCAWFQPEVCFASEEKMEPAlgILS-IPSSNF-VKICVICKQIH----GSCTQC--C 735
Cdd:cd15674    1 CELCPNRGGIFKETDTGR-WVHLVCALYTPGVAFGDVDKLSPV--TLTeMNYSKWgARECSLCEDPRfartGVCISCdaG 77

                         90
                 ....*....|....*
gi 30696333  736 KCSTYYHAMCASRAG 750
Cdd:cd15674   78 MCKSYFHVTCAQREG 92
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 902-1017 1.31e-11

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: 61.11  E-value: 1.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  902 RVCFGRSGIHGWGLFARRNIQEGEMVLeyrgeqvrgiiadlrearyrregkdcylfkiseevvvdatekgnIARLINHSC 981
Cdd:cd08161    1 EIRPSTIPGAGFGLFATRDIPKGEVIG--------------------------------------------LARFINHSC 36

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 30696333  982 MPNCYARIMSVgDDESRIVLIAKTTVASCEELTYDY 1017
Cdd:cd08161   37 EPNCEFEEVYV-GGKPRVFIVALRDIKAGEELTVDY 71
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
 912-1040 1.59e-11

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: 66.01  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  912 GWGLFARRNIQEGEMVLEYRG--------EQVRGIIADLREARYRREGKDCYLF-----KISEEV-VVDATEKGNIARLI 977
Cdd:cd10523  119 GWGVRCLDDIDKGTFVCIYAGrvlsrarsPTEPLPPKLELPSENEVEVVTSWLIlskkrKLRENVcFLDASKEGNVGRFL 198

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30696333  978 NHSCMPNCYARIMSVGDDESRIVLIAKTT---VASCEELTYDYLFDPDEPDEFKVPCLCKSPNCRK 1040
Cdd:cd10523  199 NHSCCPNLFVQNVFVDTHDKNFPWVAFFTnrvVKAGTELTWDYSYDAGTSPEQEIPCLCGVNKCQK 264
PWWP_NSD_rpt2 cd05838
second PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
 224-320 3.02e-11

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: 60.72  E-value: 3.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  224 GDLVWGKSGrNEPFWPAIVIDPmTQAPELVL-RSCIPDAACVMFFGhsgtenERDYAWVRRGMIFPFVDYVERLQEQSel 302
Cdd:cd05838    3 GDIVWVKLG-NYRWWPAEILHP-REVPDNIQsLPHPPGEFPVRFFG------SHDYYWVHRGRVFLFEEGDKGSKEKS-- 72

                         90
                 ....*....|....*...
gi 30696333  303 RGCNPRDFQMALEEALLA 320
Cdd:cd05838   73 KKSLDKSFKRALKEANEA 90
ePHD_JMJD2A cd15713
Extended PHD finger (ePHD) found in Jumonji domain-containing protein 2A (JMJD2A); The ...
 664-754 3.14e-11

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: 61.14  E-value: 3.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  664 CCLCPVKGGALKPTDvETLWVHVTCAWFQPEVCFASEEKMEPaLGILSIPSSNFVKICVIC----KQIHGSCTQCC--KC 737
Cdd:cd15713    1 CCLCSLRGGALQRAN-DDKWVHVMCAVAVLEARFVNIAERSP-VDVSKIPLQRFKLKCIFCkkrrKRTAGCCVQCShgRC 78

                         90
                 ....*....|....*..
gi 30696333  738 STYYHAMCASRAGYRME 754
Cdd:cd15713   79 PTSFHASCAQAAGVMMQ 95
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
 907-1017 3.43e-11

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: 64.35  E-value: 3.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  907 RSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADlrearyRREGKDCYLFKI--------------------------- 959
Cdd:cd10545   92 KTAERGWGVRSWDSIPAGSFICEYVGELLDTSEAD------TRSGNDDYLFDIdnrqtnrgwdggqrldvgmsdgerssa 165

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30696333  960 ----SEEVVVDATEKGNIARLINHSCMPNCYARIMSVGDDESRI---VLIAKTTVASCEELTYDY 1017
Cdd:cd10545  166 edeeSSEFTIDAGSFGNVARFINHSCSPNLFVQCVLYDHNDLRLprvMLFAADNIPPLQELTYDY 230
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 912-1039 7.20e-11

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: 63.51  E-value: 7.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  912 GWGLFARRNIQEGEMVLEYRGEQVRGIIADLREaryrregKDCYLF----KISEEVVVDATEKGNIARLINHSCMPNCYA 987
Cdd:cd10543  102 GWGVRALQDIPKGTFVCEYIGELISDSEADSRE-------DDSYLFdldnKDGETYCIDARRYGNISRFINHLCEPNLIP 174

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30696333  988 RIMSVGDDE---SRIVLIAKTTVASCEELTYDYlfdpdePDEF------KVPCLCKSPNCR 1039
Cdd:cd10543  175 VRVFVEHQDlrfPRIAFFASRDIKAGEELGFDY------GEKFwrikgkYFTCRCGSPKCK 229
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 902-1039 1.55e-10

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: 62.26  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  902 RVCFGRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREaryrregKDCYLF----KISEEVVVDATEKGNIARLI 977
Cdd:cd10535   92 RLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVRE-------EDSYLFdldnKDGEVYCIDARFYGNVSRFI 164

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30696333  978 NHSCMPNCY-ARIMSVGDDES--RIVLIAKTTVASCEELTYDYlfdpdePDEF------KVPCLCKSPNCR 1039
Cdd:cd10535  165 NHHCEPNLVpVRVFMAHQDLRfpRIAFFSTRLIEAGEQLGFDY------GERFwdikgkLFSCRCGSPKCR 229
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 902-1039 4.45e-10

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


Pssm-ID: 380931 [Multi-domain]  Cd Length: 239  Bit Score: 61.19  E-value: 4.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  902 RVCFGRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREaryrregKDCYLF----KISEEVVVDATEKGNIARLI 977
Cdd:cd10533   92 RLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVRE-------DDSYLFdldnKDGEVYCIDARYYGNISRFI 164

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30696333  978 NHSCMPNCY-ARIMSVGDDES--RIVLIAKTTVASCEELTYDYLFDPDEPDEFKVPCLCKSPNCR 1039
Cdd:cd10533  165 NHLCDPNIIpVRVFMLHQDLRfpRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCK 229
SET_SpSET3-like cd19183
SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...
 914-1024 4.53e-09

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: 56.64  E-value: 4.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  914 GLFARRNIQEGEMVLEYRGEQVRG--IIADlREARYRREG--KDCYLFKISEEVVVDATEKGNIARLINHSCMPNCYARI 989
Cdd:cd19183   15 GLFADRPIPAGDPIQELLGEIGLQseYIAD-PENQYQILGapKPHVFFHPQSPLYIDTRRSGSVARFIRRSCRPNAELVT 93

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 30696333  990 MSVGDD-ESRIVLIAKTTVASCEELTYDYLFDPDEP 1024
Cdd:cd19183   94 VASDSGsVLKFVLYASRDISPGEEITIGWDWDNPHP 129
SET_SETDB1 cd10517
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
 912-1040 5.55e-09

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: 58.45  E-value: 5.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  912 GWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYR----------------REGKD------CYlfkiseevVVDATE 969
Cdd:cd10517  140 GWGIRCLDDIPKGSFVCIYAGQILTEDEANEEGLQYGdeyfaeldyievveklKEGYEsdveehCY--------IIDAKS 211

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30696333  970 KGNIARLINHSCMPNCYARIMSVGDDESR---IVLIAKTTVASCEELTYDYLFDPDePDEFKV-PCLCKSPNCRK 1040
Cdd:cd10517  212 EGNLGRYLNHSCSPNLFVQNVFVDTHDLRfpwVAFFASRYIRAGTELTWDYNYEVG-SVPGKVlYCYCGSSNCRG 285
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
 221-317 6.83e-09

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: 53.76  E-value: 6.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  221 FYSGDLVWGKSGRNePFWPAIVIDPMTQAPELVLRScipDAACVMFFghsGTENerdYAWVRRGMIFPFVDYVERLqeqs 300
Cdd:cd05836    1 FKIGDLVWAKMKGF-PPWPGKIVNPPPDLKKPPRKK---KMHCVYFF---GSEN---YAWIEDENIKPYEEFKEEM---- 66

                         90
                 ....*....|....*..
gi 30696333  301 eLRGCNPRDFQMALEEA 317
Cdd:cd05836   67 -LKSKKSAGFKDAVEAI 82
PHD_BRPF_JADE_like cd15492
PHD finger found in BRPF proteins, Jade proteins, protein AF-10, AF-17, and similar proteins; ...
 609-655 1.25e-08

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: 51.85  E-value: 1.25e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 30696333  609 RCAVCRWVEDWDYNKIIICNRCQIAVHQECYGTRNVRDfTSWVCKAC 655
Cdd:cd15492    1 VCDVCLDGESEDDNEIVFCDGCNVAVHQSCYGIPLIPE-GDWFCRKC 46
SET_SETDB cd10541
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...
 912-1040 2.29e-08

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: 56.01  E-value: 2.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  912 GWGLFARRNIQEGEMVLEYRGeqvRGIIADLREARYRREGKDCY--LFKISEEV-VVDATEKGNIARLINHSCMPNCYAR 988
Cdd:cd10541  103 GWGIRCLDDIAKGTFVCIYAG---KILTDDFADKEGLEMGDEYFanLDHIEESCyIIDAKLEGNLGRYLNHSCSPNLFVQ 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30696333  989 IMSVGDDESRIVLIAKTT---VASCEELTYDYLFDPDEPDEFKVPCLCKSPNCRK 1040
Cdd:cd10541  180 NVFVDTHDLRFPWVAFFAskrIKAGTELTWDYNYEVGSVEGKELLCCCGSNECRG 234
PHD_TCF19_like cd15517
PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ...
 415-466 6.58e-08

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: 49.85  E-value: 6.58e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30696333  415 VCGICkRIWNHLDSQSWVRCDGCKVWIHSACDQISHKHFKDlgETDYYCPTC 466
Cdd:cd15517    1 VCGIC-NLETAAVDELWVQCDGCDKWFHQFCLGLSNERYAD--EDKFKCPNC 49
PHD_2 pfam13831
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 622-655 7.83e-07

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: 46.18  E-value: 7.83e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 30696333    622 NKIIICNRCQIAVHQECYGTRNVRDFTSWVCKAC 655
Cdd:pfam13831    2 SPLVYCSKCSVQVHASCYGVPPIPDGDGWKCRRC 35
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 224-288 1.74e-06

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 46.18  E-value: 1.74e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30696333     224 GDLVWGKSGRNePFWPAIVIDPMTQAPELVLRSCIPDAACVMFFGHsgteneRDYAWVRRGMIFP 288
Cdd:smart00293    4 GDLVWAKMKGF-PWWPALVISPKMTPDNIMKRKSDENLYPVLFFGD------KDTAWIPSSKLFP 61
PHD_JADE2 cd15680
PHD finger found in protein Jade-2 and similar proteins; Jade-2, also termed PHD finger ...
 610-655 1.97e-06

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: 45.38  E-value: 1.97e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 30696333  610 CAVCRWVEDWDYNKIIICNRCQIAVHQECYGTRNVrDFTSWVCKAC 655
Cdd:cd15680    2 CDVCRSPEGEDGNEMVFCDKCNVCVHQACYGILKV-PTGSWLCRTC 46
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
 908-1018 2.41e-06

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: 47.76  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  908 SGIHGWGLFARRNIQEGEMVLeyRGEQVRGIIADLREARYRREGKDCYLFKIseevvvdatekgniARLINHSCMPNCYA 987
Cdd:cd20071    6 EGSKGRGLVATRDIEPGELIL--VEKPLVSVPSNSFSLTDGLNEIGVGLFPL--------------ASLLNHSCDPNAVV 69

                         90       100       110
                 ....*....|....*....|....*....|.
gi 30696333  988 RImsvgDDESRIVLIAKTTVASCEELTYDYL 1018
Cdd:cd20071   70 VF----DGNGTLRVRALRDIKAGEELTISYI 96
PHD_JADE cd15573
PHD finger found in proteins Jade-1, Jade-2, Jade-3, and similar proteins; This family ...
 610-655 2.49e-06

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: 45.09  E-value: 2.49e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 30696333  610 CAVCRWVEDWDYNKIIICNRCQIAVHQECYGTRNVRDfTSWVCKAC 655
Cdd:cd15573    2 CDVCRSPDSEEGNEMVFCDKCNICVHQACYGIQKIPE-GSWLCRTC 46
PHD_JADE1 cd15679
PHD finger found in protein Jade-1 and similar proteins; Jade-1, also termed PHD finger ...
 610-655 3.50e-06

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: 45.06  E-value: 3.50e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 30696333  610 CAVCRWVEDWDYNKIIICNRCQIAVHQECYGTRNVRDfTSWVCKAC 655
Cdd:cd15679    2 CDVCQSPDGEDGNEMVFCDKCNICVHQACYGILKVPE-GSWLCRTC 46
PHD_JADE3 cd15681
PHD finger found in protein Jade-3 and similar proteins; Jade-3, also termed PHD finger ...
 610-655 4.99e-06

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: 44.58  E-value: 4.99e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 30696333  610 CAVCRWVEDWDYNKIIICNRCQIAVHQECYGTRNVRDfTSWVCKAC 655
Cdd:cd15681    2 CDVCRSPDSEEGNDMVFCDKCNICVHQACYGILKVPE-GSWLCRTC 46
PHD_ARID4_like cd15615
PHD finger found in Arabidopsis thaliana AT-rich interactive domain-containing protein 4 ...
 416-466 5.09e-06

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: 44.78  E-value: 5.09e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 30696333  416 CGICKRIW--NHLDSQSWVRCDGCKVWIHSACDQISHKHFKDLGETD---YYCPTC 466
Cdd:cd15615    2 CILCGQVYeeNEGDEKEWVQCDSCSEWVHFECDGRTGLGAFKYAKSDglqYVCPRC 57
PWWP_NSD3_rpt2 cd20166
second PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar ...
 225-317 1.73e-05

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: 44.58  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  225 DLVWGKSGrNEPFWPAIVIDPMTQAPEL-VLRSCIPDAAcVMFFGhsgtenERDYAWVRRGMIFPfvdYVERLQEQSELR 303
Cdd:cd20166    4 QIVWVKLG-NYRWWPAEICNPRSVPLNIqGLKHDIGDFP-VFFFG------SHDYYWVHQGRVFP---YVEGDKSFAEGQ 72

                         90
                 ....*....|....
gi 30696333  304 GCNPRDFQMALEEA 317
Cdd:cd20166   73 TSINKTFKKALEEA 86
PHD_BRPF2 cd15677
PHD finger found in bromodomain and PHD finger-containing protein 2 (BRPF2) and similar ...
 610-655 2.51e-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: 42.69  E-value: 2.51e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 30696333  610 CAVCRWVEDWDYNKIIICNRCQIAVHQECYGTRNVRDfTSWVCKAC 655
Cdd:cd15677    4 CCICMDGECQNSNVILFCDMCNLAVHQECYGVPYIPE-GQWLCRHC 48
PHD_BRPF cd15572
PHD finger found in bromodomain and PHD finger-containing (BRPF) proteins; The family of BRPF ...
 610-655 4.76e-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: 41.83  E-value: 4.76e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 30696333  610 CAVCRWVEDWDYNKIIICNRCQIAVHQECYGTRNVRDfTSWVCKAC 655
Cdd:cd15572    4 CCICLDGECQNSNVILFCDMCNLAVHQECYGVPYIPE-GQWLCRRC 48
PHD1_PHF14 cd15561
PHD finger 1 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...
 610-655 2.79e-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: 39.73  E-value: 2.79e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30696333  610 CAVCRWVEDWDYNKIIICNRCQIAVHQECYGTRNVRDFTS---------WVCKAC 655
Cdd:cd15561    2 CCVCLGDRSNDADEIIECDKCGISVHEGCYGVIDESDSSSsasssstepWFCEPC 56
PHD3_KDM5A_like cd15610
PHD finger 3 found in Lysine-specific demethylase 5A (KDM5A), 5B (KDM5B), and similar proteins; ...
 427-466 4.15e-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: 39.23  E-value: 4.15e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 30696333  427 DSQSWVRCDGCKVWIHSACDQISHKHFKDlgETDYYCPTC 466
Cdd:cd15610   13 DEVNWVQCDGCEEWFHLLCVGLSPEEVAE--DEDYICPSC 50
SET_SETD5 cd19181
SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...
 915-1037 4.48e-04

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: 41.92  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  915 LFARRNIQEGEMVLEYRGEQVrgiiadLREaRYRREG---KDCYLF-----KISE-EVVVDATEKGNIARLINHSCMPNC 985
Cdd:cd19181   21 LRAARDLALDTLIIEYRGKVM------LRQ-QFEVNGhffKRPYPFvlfysKFNGvEMCVDARTFGNDARFIRRSCTPNA 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30696333  986 YARIMsVGDDESRIVLIAKTTVASCEELTYDYLFDPDEPDeFKVPCLCKSPN 1037
Cdd:cd19181   94 EVRHM-IADGMIHLCIYAVAAIAKDAEVTIAFDYEYSNCN-YKVDCACHKGN 143
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
 609-655 5.03e-04

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: 38.84  E-value: 5.03e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 30696333  609 RCAVCRWVEDWDyNKIIICNRCQIAVHQECYG--TRNVRDFTSWVCKAC 655
Cdd:cd15489    1 SCIVCGKGGDLG-GELLQCDGCGKWFHADCLGppLSSFVPNGKWICPVC 48
PWWP_BRPF cd05839
PWWP domain found in the bromodomain and PHD finger-containing (BRPF) protein family; The BRPF ...
 224-283 5.11e-04

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: 40.33  E-value: 5.11e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  224 GDLVWGKSgRNEPFWPAIVIDPMTQ----------APELVLRSCIPDAACVMFFghsgtENERDYAWVRR 283
Cdd:cd05839    4 GDLVWAKC-RGYPWYPAEIVDPKDPkegngvpipvPPDRVLKKSNEKLYLVLFF-----DAKRTWGWLPR 67
PHD_BRPF1 cd15676
PHD finger found in bromodomain and PHD finger-containing protein 1 (BRPF1) and similar ...
 610-655 6.29e-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: 38.88  E-value: 6.29e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 30696333  610 CAVCRWVEDWDYNKIIICNRCQIAVHQECYGTRNVRDfTSWVCKAC 655
Cdd:cd15676   10 CCICNDGECQNSNVILFCDMCNLAVHQECYGVPYIPE-GQWLCRRC 54
PHD_ATX1_2_like cd15494
PHD finger found in Arabidopsis thaliana histone-lysine N-methyltransferase arabidopsis ...
 609-655 7.49e-04

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: 38.20  E-value: 7.49e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 30696333  609 RCAVCRWVEDWDYNKIIICNRCQIAVHQECYGTRNVRDFTSWVCKAC 655
Cdd:cd15494    1 KCSVCGEDEEYEDNLLLQCDKCRMMVHMRCYGVLEPPPGALWLCNLC 47
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 415-469 9.67e-04

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: 38.24  E-value: 9.67e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 30696333    415 VCGICKRIWNHLDsqsWVRCDGCKVWIHSACDQIShKHFKDLGETDYYCPTCRTK 469
Cdd:pfam00628    1 YCAVCGKSDDGGE---LVQCDGCDDWFHLACLGPP-LDPAEIPSGEWLCPECKPK 51
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 609-655 1.08e-03

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: 37.86  E-value: 1.08e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 30696333    609 RCAVCRwvEDWDYNKIIICNRCQIAVHQECYG---TRNVRDFTSWVCKAC 655
Cdd:pfam00628    1 YCAVCG--KSDDGGELVQCDGCDDWFHLACLGpplDPAEIPSGEWLCPEC 48
PWWP_NSD2_rpt2 cd20165
second PWWP domain found in nuclear SET domain-containing protein 2 (NSD2) and similar ...
 225-317 1.27e-03

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: 39.17  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  225 DLVWGKSGrNEPFWPAIVIDPMTQAPELV-LRSCIPDAAcVMFFGhsgtenERDYAWVRRGMIFPFVDYvERLQEQSELR 303
Cdd:cd20165    4 DIIWVKLG-NYRWWPAEVCHPKNVPPNIQkMKHEIGEFP-VFFFG------SKDYYWTHQARVFPYMEG-DRGSKYQGGK 74

                         90
                 ....*....|....
gi 30696333  304 GCNpRDFQMALEEA 317
Cdd:cd20165   75 GIG-KVFKNALQEA 87
PWWP_DNMT3 cd05835
PWWP domain found in the DNA (cytosine-5)-methyltransferase 3 (DNMT3) family; The DNMT3 family ...
 224-269 1.40e-03

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: 38.78  E-value: 1.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 30696333  224 GDLVWGKSGRnEPFWPAIVIDP-MTQAPElvlrsCIPDAACVMFFGH 269
Cdd:cd05835    3 GDLVWAKLKG-SPWWPGIVVSHkDCGQKP-----PAEGSVWVFWFGD 43
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
 415-466 1.43e-03

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: 37.68  E-value: 1.43e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30696333  415 VCGICKRiwNHLDSQSWVRCDGCKVWIHSACDQISHKHFKDLGetDYYCPTC 466
Cdd:cd15489    1 SCIVCGK--GGDLGGELLQCDGCGKWFHADCLGPPLSSFVPNG--KWICPVC 48
PHD_BRPF3 cd15678
PHD finger found in bromodomain and PHD finger-containing protein 3 (BRPF3) and similar ...
 610-655 1.46e-03

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: 37.69  E-value: 1.46e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 30696333  610 CAVCRWVEDWDYNKIIICNRCQIAVHQECYGTRNVRDfTSWVCKAC 655
Cdd:cd15678    4 CCVCLDDECHNSNVILFCDICNLAVHQECYGVPYIPE-GQWLCRCC 48
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
 902-1023 1.50e-03

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: 39.16  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  902 RVCFGRSGIHGWGLFARRNIQEGEM-----VLEYRGEQVRGIIADLREARYRREGKDCYLFKISeevvvdatekgnIARL 976
Cdd:cd10540    1 RLEVKPSTLKGRGVFATRPIKKGEVieeapVIVLPKEEYQHLCKTVLDHYVFSWGDGCLALALG------------YGSM 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 30696333  977 INHSCMPNCYARImsvgDDES-RIVLIAKTTVASCEELTYDYLFDPDE 1023
Cdd:cd10540   69 FNHSYTPNAEYEI----DFENqTIVFYALRDIEAGEELTINYGDDLWD 112
PHD_OBE1_like cd15612
PHD finger found in Arabidopsis thaliana protein OBERON 1, OBERON 2, and similar proteins ...
 416-466 2.24e-03

PHD finger found in Arabidopsis thaliana protein OBERON 1, OBERON 2, and similar proteins mainly found in plants; Included in this family are OBERON 1 (OBE1, or potyvirus VPg-interacting protein 2) and OBERON 2 (OBE2, or potyvirus VPg-interacting protein 1), which have been involved in the maintenance and/or establishment of the meristems in Arabidopsis. They interact with potyvirus VPg-interacting proteins (PVIP1 and 2) and act as central regulators in auxin-mediated control of development. Both OBE1and OBE2 contain a plant homeodomain (PHD) finger. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins.


Pssm-ID: 277084  Cd Length: 60  Bit Score: 37.21  E-value: 2.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 30696333  416 CGICKRIWNHLDSQSWVRCDGCKVWIHSAC----DQISHKHFKD----LGETDYYCPTC 466
Cdd:cd15612    2 CPICSKFDFAVNTCSWIGCDVCSHWTHTDCairsGEISMGVSLKgvegSTEMEFHCRAC 60
PHD_AF10_AF17 cd15574
PHD finger found in protein AF-10 and AF-17; This family includes protein AF-10 and AF-17. ...
 610-655 2.57e-03

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: 36.72  E-value: 2.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 30696333  610 CAVCRWVEDWDYNKIIICN--RCQIAVHQECYGTRNVRDfTSWVCKAC 655
Cdd:cd15574    2 CCVCSDERGWAENPLVYCDghGCNVAVHQACYGIVQVPT-GPWFCRKC 48
PWWP_ZCWPW1 cd20145
PWWP domain found in zinc finger CW-type PWWP domain protein 1 (ZCWPW1) and similar proteins; ...
 224-318 2.58e-03

PWWP domain found in zinc finger CW-type PWWP domain protein 1 (ZCWPW1) and similar proteins; ZCWPW1 is a histone H3K4me3 reader. It is associated with late-onset Alzheimer's disease (LOAD). In addition to the PWWP domain, ZCWPW1 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: 438973  Cd Length: 115  Bit Score: 38.68  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30696333  224 GDLVWGKSGRNePFWPAIV-IDPMT-QAPELVLRSCIPDAACVMFFGhsgteNERDYAWVRRGMIFPFvdyvERLQEQSE 301
Cdd:cd20145    9 GSLVWAKMPGY-PWWPAMVeDDPDTeEFFWLDEESDIPTKYHVTFFD-----KPVSRAWVRASSIKPF----TDNSNEPN 78

                         90
                 ....*....|....*..
gi 30696333  302 LRGCNPRDFQMALEEAL 318
Cdd:cd20145   79 LTKKKGKKYKKRLNEAV 95
PHD_KDM7 cd15640
PHD finger found in lysine-specific demethylase 7 (KDM7); KDM7, also termed JmjC ...
 432-466 3.26e-03

PHD finger found in lysine-specific demethylase 7 (KDM7); KDM7, also termed JmjC domain-containing histone demethylation protein 1D (JHDM1D), or KIAA1718, is a dual histone demethylase that catalyzes demethylation of monomethylated and dimethylated H3K9 (H3K9me2/me1) and H3K27 (H3K27me2/me1), which functions as an eraser of silencing marks on chromatin during brain development. It also plays a tumor-suppressive role by regulating angiogenesis. KDM7 contains a plant homeodomain (PHD) that binds Lys4-trimethylated histone 3 (H3K4me3) and a jumonji domain that demethylates either H3K9me2 or H3K27me2.


Pssm-ID: 277110  Cd Length: 50  Bit Score: 36.50  E-value: 3.26e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 30696333  432 VRCDGCKVWIHSACDQISHKHFKDLGEtdYYCPTC 466
Cdd:cd15640   15 IECDICKDWFHGSCVQVEEHHAADIDL--YHCPNC 47
PHD_HAC_like cd15614
PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar ...
 430-466 3.35e-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: 37.33  E-value: 3.35e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 30696333  430 SWVRCDGCKVWIHSACDQISHKHFKDlGETDYYCPTC 466
Cdd:cd15614   38 AWVQCDKCERWQHQICGLYNGRRNAD-ETAEYVCPLC 73
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 415-466 4.31e-03

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 36.04  E-value: 4.31e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 30696333     415 VCGICKRiwnHLDSQSWVRCDGCKVWIHSACDQISHKhfKDLGETDYYCPTC 466
Cdd:smart00249    1 YCSVCGK---PDDGGELLQCDGCDRWYHQTCLGPPLL--EEEPDGKWYCPKC 47
PHD1_MTF2_PHF19_like cd15499
PHD finger 1 found in polycomb repressive complex 2 (PRC2)-associated polycomb-like (PCL) ...
 610-656 4.80e-03

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


Pssm-ID: 276974  Cd Length: 53  Bit Score: 36.32  E-value: 4.80e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30696333  610 CAVCRWVEDWDYNKIIICNRCQIAVHQECY----GTRNVRDFTSWVCKACE 656
Cdd:cd15499    2 CSICGGAEARDGNEILICDKCDKGYHQLCHspkvRTSPLEGDEKWFCSRCV 52
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 609-655 5.68e-03

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


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 35.65  E-value: 5.68e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 30696333     609 RCAVCRwvEDWDYNKIIICNRCQIAVHQECYG--TRNVRDFTSWVCKAC 655
Cdd:smart00249    1 YCSVCG--KPDDGGELLQCDGCDRWYHQTCLGppLLEEEPDGKWYCPKC 47
PHD_TCF19 cd15609
PHD finger found in Transcription factor 19 (TCF-19) and similar proteins; TCF-19, also termed ...
 427-464 6.77e-03

PHD finger found in Transcription factor 19 (TCF-19) and similar proteins; TCF-19, also termed transcription factor SC1, was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It also 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. TCF-19 contains an N-terminal fork head association domain (FHA), a proline rich region, and a C-terminal plant homeodomain (PHD) finger. The FHA domain may serve as a nuclear signaling domain or as a phosphoprotein binding domain. The proline rich region is a common characteristic of trans-activating factors. The PHD finger may allow TCF-19 to interact with chromatin via methylated histone H3.


Pssm-ID: 277082  Cd Length: 50  Bit Score: 35.52  E-value: 6.77e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 30696333  427 DSQSWVRCDGCKVWIHSACDQISHKHFKDLgETDYYCP 464
Cdd:cd15609   13 ETVSWVQCDDCDQWYHVACVGCDYNAVKDP-DADFHCG 49
 
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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