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Conserved domains on  [gi|1958681658|ref|XP_038949804|]
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histone-lysine N-methyltransferase SETDB2 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SET super family cl40432
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 210-687 2.89e-110

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.


The actual alignment was detected with superfamily member cd10523:

Pssm-ID: 394802 [Multi-domain]  Cd Length: 266  Bit Score: 342.20  E-value: 2.89e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  210 FSFNTYVQLTRNHPKQNEVVSDVDISNGVesvsisfcnevdnsklpqfkyrttvwprayhlnvssmFSDSCDCSEGCIDI 289
Cdd:cd10523      1 FSFNTYVQLDRNPQDQQQLVDDFDISNGA-------------------------------------FVDSCDCTDGCIDI 43

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  290 KKCACLQLTAKNAKACPLSPDGECTGYKYKRLQRLIPSGIYECNLFCKCNRQMCQNRVIQHGPRVRLQVFKSEKKGWGVR 369
Cdd:cd10523     44 LKCACLQLTARAFSKSESSPSKGGRGYKYKRLQEPIPSGLYECNVSCKCNRMLCQNRVVQHGLQVRLQVFKTEKKGWGVR 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  370 CLDDIDKGTFVCIYSGRLLSRATPEktnigeseseqqhtvknsfskkrkievvcsdrqthcespkTEGCPPKFSSDLEep 449
Cdd:cd10523    124 CLDDIDKGTFVCIYAGRVLSRARSP----------------------------------------TEPLPPKLELPSE-- 161

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  450 vvemnnrnisrtqrhsvirrpksktdvfHYNEKNMgfvcsysaapeEKNGFkpaqehldSKARRAhedlsssqvgysedk 529
Cdd:cd10523    162 ----------------------------NEVEVVT-----------SWLIL--------SKKRKL--------------- 179

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  530 qltesdvidtttsredtspaygckhaailnskntkkvlevpvktsqeeepaasqsqqvscgeelasertkipsaslvqls 609
Cdd:cd10523        --------------------------------------------------------------------------------

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958681658  610 KESLFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRNFPLAAFFTNRYVKARTELTWDYGYEAGTMPEKEILCQC 687
Cdd:cd10523    180 RENVCFLDASKEGNVGRFLNHSCCPNLFVQNVFVDTHDKNFPWVAFFTNRVVKAGTELTWDYSYDAGTSPEQEIPCLC 257
PHD_SF super family cl22851
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
 700-813 7.50e-38

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.


The actual alignment was detected with superfamily member cd15712:

Pssm-ID: 473978 [Multi-domain]  Cd Length: 115  Bit Score: 137.34  E-value: 7.50e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  700 CVLCPEGHDWSVIYFSPSANIAAHENCLLYSSGLVECEAHDPFNIAKNFDVSSVLEKIWNGSTSKCSFCNNEGAIMGCDE 779
Cdd:cd15712      1 CAFCPKGEEYSIMYFAQEQNIAAHQNCLLYSSGFVESEEYNPLNLDRRFDVESVLNEIKRGKRLKCNFCRKKGATVGCEE 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1958681658  780 TSCAKNYHLLCAKEDRAILQV-GVKRTYKIFCPEH 813
Cdd:cd15712     81 RACRRSYHYFCALCDDAAIETdEVRGIYRVFCQKH 115
HMT_MBD cd01395
Methyl-CpG binding domains (MBD) present in putative histone methyltransferases (HMT) such as ...
 152-212 1.22e-24

Methyl-CpG binding domains (MBD) present in putative histone methyltransferases (HMT) such as CLLD8 and SETDB1 proteins; CLLD8 contains a MBD, a PreSET and a bifurcated SET domain, suggesting that CLLD8 might be associated with methylation-mediated transcriptional repression. SETDB1 and other proteins in this group have a similar domain architecture. SETDB1 is a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins.


:

Pssm-ID: 238689  Cd Length: 60  Bit Score: 97.45  E-value: 1.22e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958681658  152 PLQLPLRCHFQRRHAKTNSPSAALHVNYRTPCGRSLRNMEEVFHYLLETeCNFLFTDNFSF 212
Cdd:cd01395      1 PLHTPLLCGFQRMKYRARVGKVKKHVIYKAPCGRSLRNMSEVHRYLRET-CSFLTVDNFSF 60
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 365-425 3.56e-03

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: 38.27  E-value: 3.56e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958681658  365 GWGVRCLDDIDKGTFVCIYSGR-LLSRATPEKTNIGESESEQQHTVKNSFSKKRKIEVVCSD 425
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLELRLWGPYLFTLDEDSEYCID 62
 
Name Accession Description Interval E-value
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
 210-687 2.89e-110

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: 342.20  E-value: 2.89e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  210 FSFNTYVQLTRNHPKQNEVVSDVDISNGVesvsisfcnevdnsklpqfkyrttvwprayhlnvssmFSDSCDCSEGCIDI 289
Cdd:cd10523      1 FSFNTYVQLDRNPQDQQQLVDDFDISNGA-------------------------------------FVDSCDCTDGCIDI 43

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  290 KKCACLQLTAKNAKACPLSPDGECTGYKYKRLQRLIPSGIYECNLFCKCNRQMCQNRVIQHGPRVRLQVFKSEKKGWGVR 369
Cdd:cd10523     44 LKCACLQLTARAFSKSESSPSKGGRGYKYKRLQEPIPSGLYECNVSCKCNRMLCQNRVVQHGLQVRLQVFKTEKKGWGVR 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  370 CLDDIDKGTFVCIYSGRLLSRATPEktnigeseseqqhtvknsfskkrkievvcsdrqthcespkTEGCPPKFSSDLEep 449
Cdd:cd10523    124 CLDDIDKGTFVCIYAGRVLSRARSP----------------------------------------TEPLPPKLELPSE-- 161

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  450 vvemnnrnisrtqrhsvirrpksktdvfHYNEKNMgfvcsysaapeEKNGFkpaqehldSKARRAhedlsssqvgysedk 529
Cdd:cd10523    162 ----------------------------NEVEVVT-----------SWLIL--------SKKRKL--------------- 179

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  530 qltesdvidtttsredtspaygckhaailnskntkkvlevpvktsqeeepaasqsqqvscgeelasertkipsaslvqls 609
Cdd:cd10523        --------------------------------------------------------------------------------

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958681658  610 KESLFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRNFPLAAFFTNRYVKARTELTWDYGYEAGTMPEKEILCQC 687
Cdd:cd10523    180 RENVCFLDASKEGNVGRFLNHSCCPNLFVQNVFVDTHDKNFPWVAFFTNRVVKAGTELTWDYSYDAGTSPEQEIPCLC 257
ePHD_PHF11 cd15712
Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain ...
 700-813 7.50e-38

Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of PHF11. PHF11, also termed BRCA1 C-terminus-associated protein, or renal carcinoma antigen NY-REN-34, is a transcriptional co-activator of the Th1 effector cytokine genes, interleukin-2 (IL2) and interferon-gamma (IFNG), co-operating with nuclear factor kappa B (NF-kappaB). It is involved in T-cell activation and viability. Polymorphisms within PHF11 are associated with total IgE, allergic asthma and eczema.


Pssm-ID: 277182 [Multi-domain]  Cd Length: 115  Bit Score: 137.34  E-value: 7.50e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  700 CVLCPEGHDWSVIYFSPSANIAAHENCLLYSSGLVECEAHDPFNIAKNFDVSSVLEKIWNGSTSKCSFCNNEGAIMGCDE 779
Cdd:cd15712      1 CAFCPKGEEYSIMYFAQEQNIAAHQNCLLYSSGFVESEEYNPLNLDRRFDVESVLNEIKRGKRLKCNFCRKKGATVGCEE 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1958681658  780 TSCAKNYHLLCAKEDRAILQV-GVKRTYKIFCPEH 813
Cdd:cd15712     81 RACRRSYHYFCALCDDAAIETdEVRGIYRVFCQKH 115
HMT_MBD cd01395
Methyl-CpG binding domains (MBD) present in putative histone methyltransferases (HMT) such as ...
 152-212 1.22e-24

Methyl-CpG binding domains (MBD) present in putative histone methyltransferases (HMT) such as CLLD8 and SETDB1 proteins; CLLD8 contains a MBD, a PreSET and a bifurcated SET domain, suggesting that CLLD8 might be associated with methylation-mediated transcriptional repression. SETDB1 and other proteins in this group have a similar domain architecture. SETDB1 is a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins.


Pssm-ID: 238689  Cd Length: 60  Bit Score: 97.45  E-value: 1.22e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958681658  152 PLQLPLRCHFQRRHAKTNSPSAALHVNYRTPCGRSLRNMEEVFHYLLETeCNFLFTDNFSF 212
Cdd:cd01395      1 PLHTPLLCGFQRMKYRARVGKVKKHVIYKAPCGRSLRNMSEVHRYLRET-CSFLTVDNFSF 60
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
 723-813 6.74e-19

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: 82.38  E-value: 6.74e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  723 HENCLLYSSGLVECEAHDPfniakNFDVSSVLEKIWNGSTSKCSFCN-NEGAIMGCDETSCAKNYHLLCAKEDRAILQV- 800
Cdd:pfam13771    1 HVVCALWSPELVQRGNDSM-----GFPIEDIEKIPKRRWKLKCYLCKkKGGACIQCSKKNCRRAFHVTCALEAGLLMQFd 75

                           90
                   ....*....|...
gi 1958681658  801 GVKRTYKIFCPEH 813
Cdd:pfam13771   76 EDNGTFKSYCKKH 88
Pre-SET pfam05033
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ...
 234-346 8.35e-19

Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines that coordinate three zinc ions. It is thought that this region plays a structural role in stabilising SET domains.


Pssm-ID: 461530 [Multi-domain]  Cd Length: 99  Bit Score: 82.47  E-value: 8.35e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  234 ISNGVESVSISFCNEVDNSKLP-QFKYRTTVWpraYHLNVSSMFSDSCDCsEGCIDiKKCACLQLTaknakacplsPDGE 312
Cdd:pfam05033    1 ISKGKENVPIPVVNEVDDEPPPpDFTYITSYI---YPKEFLLIIPQGCDC-GDCSS-EKCSCAQLN----------GGEF 65

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1958681658  313 CTGYKYKRLQRL-IPSGIYECNLFCKCnRQMCQNR 346
Cdd:pfam05033   66 RFPYDKDGLLVPeSKPPIYECNPLCGC-PPSCPNR 99
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 612-674 1.71e-14

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: 70.83  E-value: 1.71e-14
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958681658   612 SLFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYE 674
Cdd:smart00317   62 SDLCIDARRKGNLARFINHSCEPNCELLFVEVNGDDR----IVIFALRDIKPGEELTIDYGSD 120
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
616-687 1.64e-11

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 62.67  E-value: 1.64e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958681658  616 LDASKEGNVGRFLNHSCYPNLWvqnvFVETHDRNFplaaFFTNRYVKARTELTWDYGYEagtMPEKEILCQC 687
Cdd:COG2940     68 IDGALGGNPARFINHSCDPNCE----ADEEDGRIF----IVALRDIAAGEELTYDYGLD---YDEEEYPCRC 128
MBD smart00391
Methyl-CpG binding domain; Methyl-CpG binding domain, also known as the TAM (TTF-IIP5, ARBP, ...
 150-216 4.02e-10

Methyl-CpG binding domain; Methyl-CpG binding domain, also known as the TAM (TTF-IIP5, ARBP, MeCP1) domain


Pssm-ID: 128673  Cd Length: 77  Bit Score: 57.00  E-value: 4.02e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958681658   150 ENPLQLPLRCHFQRRHA--KTNSPSAALHVNYRTPCGRSLRNMEEVFHYLLETECNFLFTDNFSFNTYV 216
Cdd:smart00391    1 GDPLRLPLPCGWRRETKqrKSGRSAGKFDVYYISPCGKKLRSKSELARYLHKNGDLSLDLECFDFNATV 69
MBD pfam01429
Methyl-CpG binding domain; The Methyl-CpG binding domain (MBD) binds to DNA that contains one ...
 149-216 1.30e-07

Methyl-CpG binding domain; The Methyl-CpG binding domain (MBD) binds to DNA that contains one or more symmetrically methylated CpGs. DNA methylation in animals is associated with alterations in chromatin structure and silencing of gene expression. MBD has negligible non-specific affinity for DNA. In vitro foot-printing with MeCP2 showed the MBD can protect a 12 nucleotide region surrounding a methyl CpG pair. MBDs are found in several Methyl-CpG binding proteins and also DNA demethylase.


Pssm-ID: 396147 [Multi-domain]  Cd Length: 76  Bit Score: 49.67  E-value: 1.30e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  149 GENPLQLPLRCHFQR--RHAKTNSPSAALHVNYRTPCGRSLRNMEEVFHYLLETECNFLFTDNFSFNTYV 216
Cdd:pfam01429    3 RKREDRLPLPPGWRReeRQRKSGSKAGKVDVFYYSPTGKKLRSKSEVARYLEANGGTSPKLEDFSFTVRS 72
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 365-425 3.56e-03

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: 38.27  E-value: 3.56e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958681658  365 GWGVRCLDDIDKGTFVCIYSGR-LLSRATPEKTNIGESESEQQHTVKNSFSKKRKIEVVCSD 425
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLELRLWGPYLFTLDEDSEYCID 62
 
Name Accession Description Interval E-value
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
 210-687 2.89e-110

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: 342.20  E-value: 2.89e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  210 FSFNTYVQLTRNHPKQNEVVSDVDISNGVesvsisfcnevdnsklpqfkyrttvwprayhlnvssmFSDSCDCSEGCIDI 289
Cdd:cd10523      1 FSFNTYVQLDRNPQDQQQLVDDFDISNGA-------------------------------------FVDSCDCTDGCIDI 43

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  290 KKCACLQLTAKNAKACPLSPDGECTGYKYKRLQRLIPSGIYECNLFCKCNRQMCQNRVIQHGPRVRLQVFKSEKKGWGVR 369
Cdd:cd10523     44 LKCACLQLTARAFSKSESSPSKGGRGYKYKRLQEPIPSGLYECNVSCKCNRMLCQNRVVQHGLQVRLQVFKTEKKGWGVR 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  370 CLDDIDKGTFVCIYSGRLLSRATPEktnigeseseqqhtvknsfskkrkievvcsdrqthcespkTEGCPPKFSSDLEep 449
Cdd:cd10523    124 CLDDIDKGTFVCIYAGRVLSRARSP----------------------------------------TEPLPPKLELPSE-- 161

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  450 vvemnnrnisrtqrhsvirrpksktdvfHYNEKNMgfvcsysaapeEKNGFkpaqehldSKARRAhedlsssqvgysedk 529
Cdd:cd10523    162 ----------------------------NEVEVVT-----------SWLIL--------SKKRKL--------------- 179

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  530 qltesdvidtttsredtspaygckhaailnskntkkvlevpvktsqeeepaasqsqqvscgeelasertkipsaslvqls 609
Cdd:cd10523        --------------------------------------------------------------------------------

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958681658  610 KESLFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRNFPLAAFFTNRYVKARTELTWDYGYEAGTMPEKEILCQC 687
Cdd:cd10523    180 RENVCFLDASKEGNVGRFLNHSCCPNLFVQNVFVDTHDKNFPWVAFFTNRVVKAGTELTWDYSYDAGTSPEQEIPCLC 257
SET_SETDB cd10541
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...
 265-687 2.68e-82

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: 266.33  E-value: 2.68e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  265 PRAYHLNVS-SMFSDSCDCSEGCIDIKKCACLQLTAKNAKACPLSPDGECTGYKYKRLQRLIPSGIYECNLFCKCNRQMC 343
Cdd:cd10541      2 PFYYIPDISyGKFLVGCDCTDGCRDKSKCACHQLTIQATACTPGGQDNPTAGYQYKRLEECLPTGVYECNKLCKCDPNMC 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  344 QNRVIQHGPRVRLQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLSRATPEKtnigesesEQQHTVKNSFSKKRKIEVVC 423
Cdd:cd10541     82 QNRLVQHGLQVRLQLFKTQNKGWGIRCLDDIAKGTFVCIYAGKILTDDFADK--------EGLEMGDEYFANLDHIEESC 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  424 Sdrqthcespktegcppkfssdleepvvemnnrnisrtqrhsvirrpksktdvfhyneknmgfvcsysaapeekngfkpa 503
Cdd:cd10541    154 Y------------------------------------------------------------------------------- 154

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  504 qehldskarrahedlsssqvgysedkqltesdVIDTTtsredtspaygckhaailnskntkkvlevpvktsqeeepaasq 583
Cdd:cd10541    155 --------------------------------IIDAK------------------------------------------- 159

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  584 sqqvscgeelasertkipsaslvqlskeslflldasKEGNVGRFLNHSCYPNLWVQNVFVETHDRNFPLAAFFTNRYVKA 663
Cdd:cd10541    160 ------------------------------------LEGNLGRYLNHSCSPNLFVQNVFVDTHDLRFPWVAFFASKRIKA 203

                          410       420
                   ....*....|....*....|....
gi 1958681658  664 RTELTWDYGYEAGTMPEKEILCQC 687
Cdd:cd10541    204 GTELTWDYNYEVGSVEGKELLCCC 227
SET_SETDB1 cd10517
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
 233-687 4.23e-78

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: 256.83  E-value: 4.23e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  233 DISNGVESVSISFCNEVDNSKLPQFKYRTTVWPRA-YHLNVSSMFSDSCDCSEGCIDIKKCACLQLTAKNAKACPLSPDG 311
Cdd:cd10517      8 DISYGKEGVPIPCVNEIDNSSPPYVEYSKERIPGKgVNINLDPDFLVGCDCTDGCRDKSKCACQQLTIEATAATPGGQIN 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  312 ECTGYKYKRLQRLIPSGIYECNLFCKCNRqMCQNRVIQHGPRVRLQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLsra 391
Cdd:cd10517     88 PSAGYQYRRLMEKLPTGVYECNSRCKCDK-RCYNRVVQNGLQVRLQVFKTEKKGWGIRCLDDIPKGSFVCIYAGQIL--- 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  392 tpektnigeseSEQqhtvknsfskkrkievvcsdrqthcespktegcppkfssdleepvvEMNNRnisrtqrhsvirrpk 471
Cdd:cd10517    164 -----------TED----------------------------------------------EANEE--------------- 171

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  472 sktdvfhynEKNMGfvcsysaapeekngfkpaqehldskarrahedlsssqvgyseDKQLTESDVIDTttsredtspayg 551
Cdd:cd10517    172 ---------GLQYG------------------------------------------DEYFAELDYIEV------------ 188

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  552 ckhaaILNSKntkkvlevpvktsqeeepaasqsqqvsCGEELASErtkipsaslvqlskESLFLLDASKEGNVGRFLNHS 631
Cdd:cd10517    189 -----VEKLK---------------------------EGYESDVE--------------EHCYIIDAKSEGNLGRYLNHS 222

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958681658  632 CYPNLWVQNVFVETHDRNFPLAAFFTNRYVKARTELTWDYGYEAGTMPEKEILCQC 687
Cdd:cd10517    223 CSPNLFVQNVFVDTHDLRFPWVAFFASRYIRAGTELTWDYNYEVGSVPGKVLYCYC 278
ePHD_PHF11 cd15712
Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain ...
 700-813 7.50e-38

Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of PHF11. PHF11, also termed BRCA1 C-terminus-associated protein, or renal carcinoma antigen NY-REN-34, is a transcriptional co-activator of the Th1 effector cytokine genes, interleukin-2 (IL2) and interferon-gamma (IFNG), co-operating with nuclear factor kappa B (NF-kappaB). It is involved in T-cell activation and viability. Polymorphisms within PHF11 are associated with total IgE, allergic asthma and eczema.


Pssm-ID: 277182 [Multi-domain]  Cd Length: 115  Bit Score: 137.34  E-value: 7.50e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  700 CVLCPEGHDWSVIYFSPSANIAAHENCLLYSSGLVECEAHDPFNIAKNFDVSSVLEKIWNGSTSKCSFCNNEGAIMGCDE 779
Cdd:cd15712      1 CAFCPKGEEYSIMYFAQEQNIAAHQNCLLYSSGFVESEEYNPLNLDRRFDVESVLNEIKRGKRLKCNFCRKKGATVGCEE 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1958681658  780 TSCAKNYHLLCAKEDRAILQV-GVKRTYKIFCPEH 813
Cdd:cd15712     81 RACRRSYHYFCALCDDAAIETdEVRGIYRVFCQKH 115
SET_SETDB-like cd10538
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
 256-672 2.89e-35

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: 133.65  E-value: 2.89e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  256 QFKYRTTVWPRAYHLNVSSmFSDSCDCSEGCIDiKKCACLQLTAKNakacplspdgecTGYKYKRLQRLIPSG--IYECN 333
Cdd:cd10538      4 TYIKDNIVGKNVQPFSNII-DSVGCKCKDDCLD-SKCACAAESDGI------------FAYTKNGLLRLNNSPppIFECN 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  334 LFCKCNRqMCQNRVIQHGPRVRLQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLSratpektnigeseseqqhtvkNSF 413
Cdd:cd10538     70 SKCSCDD-DCKNRVVQRGLQARLQVFRTSKKGWGVRSLEFIPKGSFVCEYVGEVIT---------------------TSE 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  414 SKKRkievvcsdrqthcespktegcppkfssdleepvvemnnRNISRTQRHsvirrpksktdvfhyneknmgfvcSYSAA 493
Cdd:cd10538    128 ADRR--------------------------------------GKIYDKSGG------------------------SYLFD 145

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  494 peekngfkpaqehLDSKarrahedlsssqvgysedkqltesdvidtttsredtspaygckhaailnskntkkvlevpvkt 573
Cdd:cd10538    146 -------------LDEF--------------------------------------------------------------- 149

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  574 sqeeepaasqsqqvscgeelasertkipsaSLVQLSKESLFlLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRNFPLA 653
Cdd:cd10538    150 ------------------------------SDSDGDGEELC-VDATFCGNVSRFINHSCDPNLFPFNVVIDHDDLRYPRI 198

                          410
                   ....*....|....*....
gi 1958681658  654 AFFTNRYVKARTELTWDYG 672
Cdd:cd10538    199 ALFATRDILPGEELTFDYG 217
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
 277-673 4.43e-31

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: 122.13  E-value: 4.43e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  277 SDSCDCSEGCIDI-KKCAClqlTAKNAKACPLSPDGectgykykRLQRLIPSgIYECNLFCKCNRQmCQNRVIQHGPRVR 355
Cdd:cd10545     21 STGCDCKNRCTDGaSDCAC---VKKNGGEIPYNFNG--------RLIRAKPA-IYECGPLCKCPPS-CYNRVTQKGLRYR 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  356 LQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLSRATPEKtnigeseseqqhtvknsfskkrkievvcsdrqthcespkt 435
Cdd:cd10545     88 LEVFKTAERGWGVRSWDSIPAGSFICEYVGELLDTSEADT---------------------------------------- 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  436 egcppkfssdleepvvemnnrnisrtqrhsvirrpKSKTDVFHYNEKNmgfvcsysaapeekngfkpaqehldskarraH 515
Cdd:cd10545    128 -----------------------------------RSGNDDYLFDIDN-------------------------------R 141

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  516 EDLSSSQVGysedkqlTESDVIDTTTSREdtspaygckhaailnskntkkvlevpvktSQEEEPAASqsqqvscgeelas 595
Cdd:cd10545    142 QTNRGWDGG-------QRLDVGMSDGERS-----------------------------SAEDEESSE------------- 172

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958681658  596 ertkipsaslvqlskeslFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRNFPLAAFFTNRYVKARTELTWDYGY 673
Cdd:cd10545    173 ------------------FTIDAGSFGNVARFINHSCSPNLFVQCVLYDHNDLRLPRVMLFAADNIPPLQELTYDYGY 232
HMT_MBD cd01395
Methyl-CpG binding domains (MBD) present in putative histone methyltransferases (HMT) such as ...
 152-212 1.22e-24

Methyl-CpG binding domains (MBD) present in putative histone methyltransferases (HMT) such as CLLD8 and SETDB1 proteins; CLLD8 contains a MBD, a PreSET and a bifurcated SET domain, suggesting that CLLD8 might be associated with methylation-mediated transcriptional repression. SETDB1 and other proteins in this group have a similar domain architecture. SETDB1 is a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins.


Pssm-ID: 238689  Cd Length: 60  Bit Score: 97.45  E-value: 1.22e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958681658  152 PLQLPLRCHFQRRHAKTNSPSAALHVNYRTPCGRSLRNMEEVFHYLLETeCNFLFTDNFSF 212
Cdd:cd01395      1 PLHTPLLCGFQRMKYRARVGKVKKHVIYKAPCGRSLRNMSEVHRYLRET-CSFLTVDNFSF 60
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 271-389 1.35e-24

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: 103.57  E-value: 1.35e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  271 NVSSMfsDSCDCSEGCiDIKKCACLQLTAKNA--KACPLSPDgectgykykrLQRLIPSGIYECNLFCKCNRQmCQNRVI 348
Cdd:cd10543     20 NITSL--QTCSCRDDC-SSDNCVCGRLSVRCWydKEGRLLPD----------FNKLDPPLIFECNRACSCWRN-CRNRVV 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1958681658  349 QHGPRVRLQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLS 389
Cdd:cd10543     86 QNGIRYRLQLFRTRGMGWGVRALQDIPKGTFVCEYIGELIS 126
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 280-395 1.95e-24

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


Pssm-ID: 380940 [Multi-domain]  Cd Length: 245  Bit Score: 103.14  E-value: 1.95e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  280 CDCSEGCIDIKKCACLQLTAknakacplspdgecTGYKYKRLQRL-IPSG--IYECNLFCKCNRQmCQNRVIQHGPRVRL 356
Cdd:cd10542     25 CECTEDCHNNNPTCCPAESG--------------VKFAYDKQGRLrLPPGtpIYECNSRCKCGPD-CPNRVVQRGRKVPL 89

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958681658  357 QVFK-SEKKGWGVRCLDDIDKGTFVCIYSGRLLSRATPEK 395
Cdd:cd10542     90 CIFRtSNGRGWGVKTLEDIKKGTFVMEYVGEIITSEEAER 129
ePHD_PHF6_like cd15673
Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11); ...
 700-813 3.90e-24

Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the two ePHD fingers of PFH6 and the single ePHD finger of PFH11. PHF6, also termed the X-linked mental retardation disorder Borjeson-Forssman-Lehmann syndrome-associated protein, is a nucleolus, ribosomal RNA promoter-associated protein that regulates cell cycle progression by suppressing ribosomal RNA synthesis. It has been implicated in cell cycle control, genomic maintenance, and tumor suppression. PHF6 shows transcriptional repression activity through directly interacting with the nucleosome remodeling and deacetylation complex component RBBP4. PHF6 contains two non-canonical ePHD fingers. PHF11, also termed BRCA1 C-terminus-associated protein, or renal carcinoma antigen NY-REN-34, is a transcriptional co-activator of the Th1 effector cytokine genes, interleukin-2 (IL2) and interferon-gamma (IFNG), co-operating with nuclear factor kappa B (NF-kappaB). It is involved in T-cell activation and viability. Polymorphisms within PHF11 are associated with total IgE, allergic asthma and eczema.


Pssm-ID: 277143  Cd Length: 116  Bit Score: 98.23  E-value: 3.90e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  700 CVLCPEGHDWSVIYF--SPSANIAAHENCLLYSSGLVECEAHDPFNIAkNFDVSSVLEKIWNGSTSKCSFCNNEGAIMGC 777
Cdd:cd15673      1 CGFCKSGEENKETGGklASGEKIAAHHNCMLFSSGLVQYVSPNENDFG-GFDIEDVKKEIKRGRKLKCNLCKKTGATIGC 79

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1958681658  778 DETSCAKNYHLLCAKEDRA-ILQVGVKRTYKIFCPEH 813
Cdd:cd15673     80 DVKQCKKTYHYHCAKKDDAkIIERNSQGIYRVYCKNH 116
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
 273-389 5.79e-24

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: 102.38  E-value: 5.79e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  273 SSMFSDSCDCSEGCIDIKKCACLQ--LTAKNAKACPLSPDGECTGykykrlqrliPsgIYECNLFCKCNRQmCQNRVIQH 350
Cdd:cd10544     20 NEITFPGCDCKTSSCEPETCSCLRkyGPNYDDDGCLLDFDGKYSG----------P--VFECNSMCKCSES-CQNRVVQN 86

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1958681658  351 GPRVRLQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLS 389
Cdd:cd10544     87 GLQFKLQVFKTPKKGWGLRTLEFIPKGRFVCEYAGEVIG 125
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 280-391 5.03e-20

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: 89.99  E-value: 5.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  280 CDCSEGCIDiKKCACLQLTAKnakaCPLSPDGECtgykYKRLQRLIPSGIYECNLFCKCNRQmCQNRVIQHGPRVRLQVF 359
Cdd:cd10535     27 CVCIDDCSS-SNCMCGQLSMR----CWYDKDGRL----LPEFNMAEPPLIFECNHACSCWRN-CRNRVVQNGLRARLQLY 96

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958681658  360 KSEKKGWGVRCLDDIDKGTFVCIYSGRLLSRA 391
Cdd:cd10535     97 RTRDMGWGVRSLQDIPPGTFVCEYVGELISDS 128
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 280-391 1.38e-19

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: 88.92  E-value: 1.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  280 CDCSEGCIDiKKCACLQLTAKnakaCPLSPDGECtgykYKRLQRLIPSGIYECNLFCKCNRQmCQNRVIQHGPRVRLQVF 359
Cdd:cd10533     27 CTCVDDCSS-SNCLCGQLSIR----CWYDKDGRL----LQEFNKIEPPLIFECNQACSCWRN-CKNRVVQSGIKVRLQLY 96

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958681658  360 KSEKKGWGVRCLDDIDKGTFVCIYSGRLLSRA 391
Cdd:cd10533     97 RTAKMGWGVRALQTIPQGTFICEYVGELISDA 128
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
 723-813 6.74e-19

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: 82.38  E-value: 6.74e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  723 HENCLLYSSGLVECEAHDPfniakNFDVSSVLEKIWNGSTSKCSFCN-NEGAIMGCDETSCAKNYHLLCAKEDRAILQV- 800
Cdd:pfam13771    1 HVVCALWSPELVQRGNDSM-----GFPIEDIEKIPKRRWKLKCYLCKkKGGACIQCSKKNCRRAFHVTCALEAGLLMQFd 75

                           90
                   ....*....|...
gi 1958681658  801 GVKRTYKIFCPEH 813
Cdd:pfam13771   76 EDNGTFKSYCKKH 88
Pre-SET pfam05033
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ...
 234-346 8.35e-19

Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines that coordinate three zinc ions. It is thought that this region plays a structural role in stabilising SET domains.


Pssm-ID: 461530 [Multi-domain]  Cd Length: 99  Bit Score: 82.47  E-value: 8.35e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  234 ISNGVESVSISFCNEVDNSKLP-QFKYRTTVWpraYHLNVSSMFSDSCDCsEGCIDiKKCACLQLTaknakacplsPDGE 312
Cdd:pfam05033    1 ISKGKENVPIPVVNEVDDEPPPpDFTYITSYI---YPKEFLLIIPQGCDC-GDCSS-EKCSCAQLN----------GGEF 65

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1958681658  313 CTGYKYKRLQRL-IPSGIYECNLFCKCnRQMCQNR 346
Cdd:pfam05033   66 RFPYDKDGLLVPeSKPPIYECNPLCGC-PPSCPNR 99
SET_SUV39H_Clr4-like cd20073
SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 ...
 256-395 1.87e-17

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: 83.39  E-value: 1.87e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  256 QFKYRTTVWPRayhlnvSSMFSDSCDCS--EGCI--DIKKCACLQLTAKNAKACPlspdgectgyKYKRLQRLIPSGIYE 331
Cdd:cd20073      8 SYRYGLGIEPP------DPLFISGCSCSklGGCDlnNPGSCQCLEDSNEKSFAYD----------EYGRVRANTGSIIYE 71

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958681658  332 CNLFCKCNRQmCQNRVIQHGPRVRLQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLSRATPEK 395
Cdd:cd20073     72 CNENCDCGIN-CPNRVVQRGRKLPLEIFKTKHKGWGLRCPRFIKAGTFIGVYLGEVITQSEAEI 134
MBD cd00122
MeCP2, MBD1, MBD2, MBD3, MBD4, CLLD8-like, and BAZ2A-like proteins constitute a family of ...
 152-212 3.31e-17

MeCP2, MBD1, MBD2, MBD3, MBD4, CLLD8-like, and BAZ2A-like proteins constitute a family of proteins that share the methyl-CpG-binding domain (MBD). The MBD consists of about 70 residues and is defined as the minimal region required for binding to methylated DNA by a methyl-CpG-binding protein which binds specifically to methylated DNA. The MBD can recognize a single symmetrically methylated CpG either as naked DNA or within chromatin. MeCP2, MBD1 and MBD2 (and likely MBD3) form complexes with histone deacetylase and are involved in histone deacetylase-dependent repression of transcription. MBD4 is an endonuclease that forms a complex with the DNA mismatch-repair protein MLH1. The MBDs present in putative chromatin remodelling subunit, BAZ2A, and putative histone methyltransferase, CLLD8, represent two phylogenetically distinct groups within the MBD protein family.


Pssm-ID: 238069  Cd Length: 62  Bit Score: 76.59  E-value: 3.31e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958681658  152 PLQLPLRCHFQRRHAKTNSPSA-ALHVNYRTPCGRSLRNMEEVFHYLLETECNFLFTDNFSF 212
Cdd:cd00122      1 PLRDPLPPGWKRELVIRKSGSAgKGDVYYYSPCGKKLRSKPEVARYLEKTGPSSLDLENFSF 62
SET_SUV39H_DIM5-like cd19473
SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...
 274-397 1.40e-14

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


Pssm-ID: 380996 [Multi-domain]  Cd Length: 274  Bit Score: 75.05  E-value: 1.40e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  274 SMFSDSCDCSEG--CIdIKKCACLQ-LTAKNAKACPLSPDG-ECTGYKYKRLQRLIPSG---IYECNLFCKCNrQMCQNR 346
Cdd:cd19473     20 EEFRSGCECTDDedCM-YSGCLCLQdVDPDDDRDPGKKKNAyHSSGAKKGCLRGHMLNSrlpIYECHEGCACS-DDCPNR 97

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958681658  347 VIQHGPRVRLQVFK-SEKKGWGVRCLDDIDKGTFVCIYSGRLLsraTPEKTN 397
Cdd:cd19473     98 VVERGRKVPLQIFRtSDGRGWGVRSTVDIKRGQFVDCYVGEII---TPEEAQ 146
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 612-674 1.71e-14

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: 70.83  E-value: 1.71e-14
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958681658   612 SLFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYE 674
Cdd:smart00317   62 SDLCIDARRKGNLARFINHSCEPNCELLFVEVNGDDR----IVIFALRDIKPGEELTIDYGSD 120
ePHD_PHF7_G2E3_like cd15669
Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ...
 700-813 2.56e-13

Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ubiquitin-protein ligase (G2E3); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of PHF7 and G2E3. PHF7, also termed testis development protein NYD-SP6, is a testis-specific PHD finger-containing protein that associates with chromatin and binds histone H3 N-terminal tails with a preference for dimethyl lysine 4 (H3K4me2). It may play an important role in stimulating transcription involved in testicular development and/or spermatogenesis. PHF7 contains a PHD finger and a non-canonical ePHD finger, both of which may be involved in activating transcriptional regulation. G2E3 is a dual function ubiquitin ligase (E3) that may play a possible role in cell cycle regulation and the cellular response to DNA damage. It is essential for prevention of apoptosis in early embryogenesis. It is also a nucleo-cytoplasmic shuttling protein with DNA damage responsive localization. G2E3 contains two distinct RING-like ubiquitin ligase domains that catalyze lysine 48-linked polyubiquitination, and a C-terminal catalytic HECT domain that plays an important role in ubiquitin ligase activity and in the dynamic subcellular localization of the protein. The RING-like ubiquitin ligase domains consist of a PHD finger and an ePHD finger.


Pssm-ID: 277139 [Multi-domain]  Cd Length: 112  Bit Score: 67.28  E-value: 2.56e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  700 CVLCPEGHDWSVIY--FSPSANIAAHENCLLYSSGLVEcEAHDPFNIAkNFDVSSVLEKIWNGSTSKCSFCNNEGAIMGC 777
Cdd:cd15669      1 CVLCGRSDDDPDKYgeKLQKDGICAHYFCLLFSSGLPQ-RGEDNEGIY-GFLPEDIRKEVRRASRLRCFYCKKKGASIGC 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958681658  778 DETSCAKNYHLLCAKEDRAILQvgVKRTYKIFCPEH 813
Cdd:cd15669     79 AVKGCRRSFHFPCGLENGCVTQ--FFGEYRSFCWEH 112
ePHD2_PHF6 cd15711
Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
 720-813 3.17e-13

Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. PHF6 contains two non-canonical ePHD fingers, this model corresponds to the second ePHD finger. PHF6, also termed the X-linked mental retardation disorder Borjeson-Forssman-Lehmann syndrome-associated protein, is a nucleolus, ribosomal RNA promoter-associated protein that regulates cell cycle progression by suppressing ribosomal RNA synthesis. It has been implicated in cell cycle control, genomic maintenance, and tumor suppression. PHF6 shows transcriptional repression activity through directly interacting with the nucleosome remodeling and deacetylation complex component RBBP4.


Pssm-ID: 277181  Cd Length: 118  Bit Score: 67.03  E-value: 3.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  720 IAAHENCLLYSSGLVECEAHDPFNIAkNFDVSSVLEKIWNGSTSKCSFCNNEGAIMGCDETSCAKNYHLLCAKEDRAILQ 799
Cdd:cd15711     25 AAAHYKCMLFSSGTVQLTTTSRAEFG-DFDIKTVIQEIKRGKRMKCTLCSQLGATIGCEIKACVKTYHYHCGVQDKAKYI 103

                           90
                   ....*....|....*
gi 1958681658  800 VGVKR-TYKIFCPEH 813
Cdd:cd15711    104 ENMSRgIYKLYCKNH 118
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 614-671 1.06e-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: 69.15  E-value: 1.06e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958681658  614 FLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRNFPLAAFFTNRYVKARTELTWDY 671
Cdd:cd10532    149 FTVDAARYGNVSHFVNHSCDPNLQVFNVFIDNLDTRLPRIALFSTRTIKAGEELTFDY 206
ePHD cd15571
Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is ...
 700-813 1.64e-12

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: 64.91  E-value: 1.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  700 CVLCPEG---HDWSVIYFSPSANIAAHENCLLYSSGLVECEAHDPfniaKNFDVSSVLEKiwnGSTSKCSFCN-NEGAIM 775
Cdd:cd15571      1 CALCPRSggaLKGGGALKTTSDGLWVHVVCALWSPEVYFDDGTLL----EVEGVSKIPKR---RKKLKCSICGkRGGACI 73

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1958681658  776 GCDETSCAKNYHLLCAKEDRAILQVGVKRT-YKIFCPEH 813
Cdd:cd15571     74 QCSYPGCPRSFHVSCAIRAGCLFEFEDGPGnFVVYCPKH 112
ePHD1_PHF6 cd15710
Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
 715-813 1.87e-12

Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. PHF6 contains two non-canonical ePHD fingers, this model corresponds to the first ePHD finger. PHF6, also termed the X-linked mental retardation disorder Borjeson-Forssman-Lehmann syndrome-associated protein, is a nucleolus, ribosomal RNA promoter-associated protein that regulates cell cycle progression by suppressing ribosomal RNA synthesis. It has been implicated in cell cycle control, genomic maintenance, and tumor suppression. PHF6 shows transcriptional repression activity through directly interacting with the nucleosome remodeling and deacetylation complex component RBBP4. .


Pssm-ID: 277180  Cd Length: 115  Bit Score: 64.98  E-value: 1.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  715 SPSANIAAHENCLLYSSGLVECEAhDPFNIAkNFDVSSVLEKIWNGSTSKCSFCNNEGAIMGCDETSCAKNYHLLCAKED 794
Cdd:cd15710     18 SENQKVAAHHKCMLFSSALVSSHS-DSENLG-GFSIEDVQKEIKRGTKLMCSLCHCPGATIGCDVKTCHRTYHYYCALHD 95

                           90       100
                   ....*....|....*....|
gi 1958681658  795 RAILQVGVKR-TYKIFCPEH 813
Cdd:cd15710     96 KAQIRENPSQgIYMIYCRKH 115
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 611-671 3.79e-12

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: 67.61  E-value: 3.79e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958681658  611 ESLFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRNFPLAAFFTNRYVKARTELTWDY 671
Cdd:cd10525    148 EDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIALFATRTIRAGEELTFDY 208
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 605-672 6.00e-12

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: 63.31  E-value: 6.00e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  605 LVQLSKESLFLLDAS--KEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYG 672
Cdd:pfam00856   50 LFTLDEDSEYCIDARalYYGNWARFINHSCDPNCEVRVVYVNGGPR----IVIFALRDIKPGEELTIDYG 115
PreSET smart00468
N-terminal to some SET domains; A Cys-rich putative Zn2+-binding domain that occurs N-terminal ...
 233-337 7.44e-12

N-terminal to some SET domains; A Cys-rich putative Zn2+-binding domain that occurs N-terminal to some SET domains. Function is unknown. Unpublished.


Pssm-ID: 128744 [Multi-domain]  Cd Length: 98  Bit Score: 62.43  E-value: 7.44e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658   233 DISNGVESVSISFCNEVDNSKLP-QFKY-RTTVWPRAYHLNVSSMFSDSCDCSEGCIDIKKCACLQLTaknakacplspD 310
Cdd:smart00468    3 DISNGKENVPVPLVNEVDEDPPPpDFEYiSEYIYGQGVPIDRSPSPLVGCSCSGDCSSSNKCECARKN-----------G 71

                            90       100
                    ....*....|....*....|....*..
gi 1958681658   311 GECTGYKYKRLQRLIPSGIYECNLFCK 337
Cdd:smart00468   72 GEFAYELNGGLRLKRKPLIYECNSRCS 98
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
616-687 1.64e-11

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 62.67  E-value: 1.64e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958681658  616 LDASKEGNVGRFLNHSCYPNLWvqnvFVETHDRNFplaaFFTNRYVKARTELTWDYGYEagtMPEKEILCQC 687
Cdd:COG2940     68 IDGALGGNPARFINHSCDPNCE----ADEEDGRIF----IVALRDIAAGEELTYDYGLD---YDEEEYPCRC 128
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 270-395 3.25e-11

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: 64.53  E-value: 3.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  270 LNVSSMFSDSCDCSEgcidikkcaCLQltaknAKACPLSPdGECTGYKyKRLQRLIPSG--IYECNLFCKCNRQmCQNRV 347
Cdd:cd10532     15 INLDNEATVGCDCSD---------CFF-----GKCCPAEA-GVLFAYN-EHGQLKIPPGtpIYECNSRCKCGPD-CPNRV 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958681658  348 IQHGPRVRLQVFK-SEKKGWGVRCLDDIDKGTFVCIYSGRLLSRATPEK 395
Cdd:cd10532     78 VQKGTQYSLCIFRtSNGRGWGVKTLQKIKKNSFVMEYVGEVITSEEAER 126
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
 616-689 6.75e-11

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: 61.06  E-value: 6.75e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958681658  616 LDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYEA-GTMPEKeilcqCFC 689
Cdd:cd19172     67 IDATKKGNLSRFINHSCEPNCETQKWTVNGELR----VGFFAKRDIPAGEELTFDYQFERyGKEAQK-----CYC 132
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
 616-689 1.72e-10

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: 59.96  E-value: 1.72e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958681658  616 LDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYEAgtmpEKEILCQCFC 689
Cdd:cd10531     65 IDATRKGNLSRFINHSCEPNCETQKWIVNGEYR----IGIFALRDIPAGEELTFDYNFVN----YNEAKQVCLC 130
MBD smart00391
Methyl-CpG binding domain; Methyl-CpG binding domain, also known as the TAM (TTF-IIP5, ARBP, ...
 150-216 4.02e-10

Methyl-CpG binding domain; Methyl-CpG binding domain, also known as the TAM (TTF-IIP5, ARBP, MeCP1) domain


Pssm-ID: 128673  Cd Length: 77  Bit Score: 57.00  E-value: 4.02e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958681658   150 ENPLQLPLRCHFQRRHA--KTNSPSAALHVNYRTPCGRSLRNMEEVFHYLLETECNFLFTDNFSFNTYV 216
Cdd:smart00391    1 GDPLRLPLPCGWRRETKqrKSGRSAGKFDVYYISPCGKKLRSKSELARYLHKNGDLSLDLECFDFNATV 69
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 624-672 4.64e-10

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: 56.49  E-value: 4.64e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958681658  624 VGRFLNHSCYPNLWvqnvFVETHDRNFPLAAFFTNRYVKARTELTWDYG 672
Cdd:cd08161     28 LARFINHSCEPNCE----FEEVYVGGKPRVFIVALRDIKAGEELTVDYG 72
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 305-395 5.64e-10

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: 61.06  E-value: 5.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  305 CPLSPDGECT--------GYKYKRLQRLIPS-GIYECNLFCKCNRQmCQNRVIQHGPRVRLQVFKSEK-KGWGVRCLDDI 374
Cdd:cd10525     29 CLSQPVGGCCpgaskhrfAYNEQGQVKVRPGlPIYECNSRCRCGPD-CPNRVVQKGIQYDLCIFRTDNgRGWGVRTLEKI 107

                           90       100
                   ....*....|....*....|.
gi 1958681658  375 DKGTFVCIYSGRLLSRATPEK 395
Cdd:cd10525    108 RKNSFVMEYVGEIITSEEAER 128
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
 608-687 2.60e-09

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: 56.53  E-value: 2.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  608 LSKESLFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYEAGTMPEKEIlCQC 687
Cdd:cd19174     56 LNLDSGMVIDGYRMGNEARFVNHSCDPNCEMQKWSVNGVYR----IGLFALKDIPAGEELTYDYNFHSFNVEKQQP-CKC 130
ePHD1_KMT2C_like cd15665
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
 700-813 2.93e-09

Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the first ePHD finger of KMTC2C and KMTC2D. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named MLL4, a fourth human homolog of Drosophila trithorax, located on chromosome 12. It enzymatically generates trimethylated histone H3 Lysine 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. KMT2D is also a part of ASCOM. Both KMT2C and KMT2D contain the catalytic domain SET, five plant PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobilitygroup)-binding motif, and two FY-rich regions.


Pssm-ID: 277135  Cd Length: 90  Bit Score: 55.02  E-value: 2.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  700 CVLCPEGHDWsviyfspsaniaAHENCLLYSSGLVeceahdpfnIAKNFDVSSVLEKIWNGSTSKCSFCNNEGAIMGCDE 779
Cdd:cd15665      1 CALCNLGEVY------------AHHCCAAWSEGVC---------QTEDGALENVDKAVAKALSQKCSFCLRYGASISCRM 59

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1958681658  780 TSCAKNYHLLCAKEDRAILqvgVKRTYKIFCPEH 813
Cdd:cd15665     60 PSCSKSFHFPCAAAAGCFQ---DIKTLTLFCPEH 90
ePHD_KMT2A_like cd15664
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The ...
 723-813 1.13e-08

Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of histone-lysine N-methyltransferase trithorax (Trx) like proteins, KMT2A/MLL1 and KMT2B/MLL2. KMT2A and KMT2B comprise the mammalian Trx branch of COMPASS family, and are both essential for mammalian embryonic development. KMT2A regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in the MLL1 complex. KMT2B is a second human homolog of Drosophila trithorax, located on chromosome 19 and functions as the catalytic subunit in the MLL2 complex. It plays a critical role in memory formation by mediating hippocampal H3K4 di- and trimethylation. It is also required for RNA polymerase II association and protection from DNA methylation at the MagohB CpG island promoter. Both KMT2A and KMT2B contain a CxxC (x for any residue) zinc finger domain, three PHD fingers, this extended PHD (ePHD) finger, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain.


Pssm-ID: 277134  Cd Length: 105  Bit Score: 53.56  E-value: 1.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  723 HENCLLYSSGLVEcEAHDPFniaKNfdvssVLEKIWNGSTSKCSFCNNEGAIMGCDETSCAKNYHLLCAKEDRAILQvgv 802
Cdd:cd15664     28 HINCALWSAEVFE-EDDGSL---QN-----VHSAVSRGRMMKCELCGKPGATVGCCLKSCPANYHFMCARKAECVFQ--- 95

                           90
                   ....*....|.
gi 1958681658  803 kRTYKIFCPEH 813
Cdd:cd15664     96 -DDKKVFCPAH 105
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 354-395 1.74e-08

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: 53.88  E-value: 1.74e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1958681658   354 VRLQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLSRATPEK 395
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEE 42
ePHD_RAI1_like cd15668
Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 ...
 700-813 3.08e-08

Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 (TCF-20) and similar proteins; The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the C-terminal ePHD/ADD (ATRX-DNMT3-DNMT3L) domain of RAI1 and TCF-20. RAI1, a homolog of stromelysin-1 PDGF (platelet-derived growth factor)-responsive element-binding protein (SPBP, also termed TCF-20), is a chromatin-binding protein implicated in the regulation of gene expression. TCF-20 is involved in transcriptional activation of the MMP3 (matrix metalloprotease 3) promoter. It also functions as a transcriptional co-regulator that enhances or represses the transcriptional activity of certain transcription factors/cofactors, such as specificity protein 1 (Sp1), E twenty-six 1 (Ets1), paired box protein 6 (Pax6), small nuclear RING-finger (SNURF)/RNF4, c-Jun, androgen receptor (AR) and estrogen receptor alpha (ERalpha). Both RAI1 and TCF-20 are strongly enriched in chromatin in interphase HeLa cells, and display low nuclear mobility, and have been implicated in Smith-Magenis syndrome and Potocki-Lupski syndrome.


Pssm-ID: 277138  Cd Length: 103  Bit Score: 52.31  E-value: 3.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  700 CVLCPEGHDWSVI--YFSPSANIAAHENCLLYSSGLVECEAHdpfniaknfdVSSVLEKIWNGSTSKCSFCNNEGAIMGC 777
Cdd:cd15668      1 CVFCKRGPHYKGLgdLFGPYYEVWVHEDCAVWAPGVYLVGGK----------LYGLEEAVWVAKQSVCSSCQQTGATIGC 70

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958681658  778 DETSCAKNYHLLCAKEDRAILQvgvKRTYKIFCPEH 813
Cdd:cd15668     71 LHKGCKAKYHYPCAVESGCQLD---EENFSLLCPKH 103
ePHD2_KMT2C_like cd15666
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
 700-813 3.80e-08

Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the second ePHD finger of KMT2C, and KMT2D. KMT2C, also termed myeloid/lymphoid or mixed-lineage leukemia protein 3 (MLL3), or homologous to ALR protein, is a histone H3 lysine 4 (H3K4) lysine methyltransferase that functions as a circadian factor contributing to genome-scale circadian transcription. It is a component of a large complex that acts as a coactivator of multiple transcription factors, including the bile acid (BA)-activated nuclear receptor, farnesoid X receptor (FXR), a critical player in BA homeostasis. The MLL3 complex is essential for p53 transactivation of small heterodimer partner (SHP). KMT2C is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and its paralog MLL4. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named MLL4, a fourth human homolog of Drosophila trithorax, located on chromosome 12. It enzymatically generates trimethylated histone H3 Lysine 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such as HOXA1-3 and NESTIN. KMT2D is also a part of ASCOM. Both KMT2C and KMT2D contain the catalytic domain SET, five PHD fingers, two ePHD fingers, a RING finger, an HMG (high-mobilitygroup)-binding motif, and two FY-rich regions.


Pssm-ID: 277136  Cd Length: 105  Bit Score: 52.30  E-value: 3.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  700 CVLCPEGHDWSVI----YFSPSANIAAHENCLLYSSGLVEceahdpfniAKNFDVSSVLEKIWNGSTSKCSFCNNEGAIM 775
Cdd:cd15666      1 CVLCGGEGDGDTDgpgrLLNLDVDKWVHLNCALWSYEVYE---------TQNGALMNVEEALRRALTTTCSHCGRTGATV 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1958681658  776 GCDETSCAKNYHLLCAKEDRAILqvgvkrtYK---IFCPEH 813
Cdd:cd15666     72 PCFKPRCANVYHLPCAIKDGCMF-------FKdktMLCPSH 105
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
 616-674 4.30e-08

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: 52.73  E-value: 4.30e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958681658  616 LDASKEGNVGRFLNHSCYPNLWvqnvFVETHDRNFPLAAFFTNRYVKARTELTWDYGYE 674
Cdd:cd10522     65 IDAGKKGNLTRFINHSDQPNLE----LIVRTLKGEQHIGFVAIRDIKPGEELFISYGPK 119
SET_SETD1-like cd10518
SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...
 617-687 6.66e-08

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: 52.60  E-value: 6.66e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958681658  617 DASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDY--GYEagtmPEKEILCQC 687
Cdd:cd10518     80 DATKKGNIARFINHSCDPNCYAKIITVDGEKH----IVIFAKRDIAPGEELTYDYkfPIE----DEEKIPCLC 144
SET_SET1 cd20072
SET domain (including post-SET domain) found in catalytic component of the Saccharomyces ...
 585-687 8.33e-08

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: 52.43  E-value: 8.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  585 QQVSCGEELASERTKIPSASLVQLSKESLflLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKAR 664
Cdd:cd20072     49 QQVADEREKRYLRQGIGSSYLFRIDDDTV--VDATKKGNIARFINHCCDPNCTAKIIKVEGEKR----IVIYAKRDIAAG 122

                           90       100
                   ....*....|....*....|...
gi 1958681658  665 TELTWDYGYEagtMPEKEILCQC 687
Cdd:cd20072    123 EELTYDYKFP---REEDKIPCLC 142
MBD pfam01429
Methyl-CpG binding domain; The Methyl-CpG binding domain (MBD) binds to DNA that contains one ...
 149-216 1.30e-07

Methyl-CpG binding domain; The Methyl-CpG binding domain (MBD) binds to DNA that contains one or more symmetrically methylated CpGs. DNA methylation in animals is associated with alterations in chromatin structure and silencing of gene expression. MBD has negligible non-specific affinity for DNA. In vitro foot-printing with MeCP2 showed the MBD can protect a 12 nucleotide region surrounding a methyl CpG pair. MBDs are found in several Methyl-CpG binding proteins and also DNA demethylase.


Pssm-ID: 396147 [Multi-domain]  Cd Length: 76  Bit Score: 49.67  E-value: 1.30e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  149 GENPLQLPLRCHFQR--RHAKTNSPSAALHVNYRTPCGRSLRNMEEVFHYLLETECNFLFTDNFSFNTYV 216
Cdd:pfam01429    3 RKREDRLPLPPGWRReeRQRKSGSKAGKVDVFYYSPTGKKLRSKSEVARYLEANGGTSPKLEDFSFTVRS 72
SET_SETD1 cd19169
SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...
 596-688 2.72e-07

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: 50.80  E-value: 2.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  596 ERTKIPSASLVQLSKEslFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRNFplaaFFTNRYVKARTELTWDYGYea 675
Cdd:cd19169     60 EAIGIGSSYLFRVDDD--TIIDATKCGNLARFINHSCNPNCYAKIITVESQKKIV----IYSKRPIAVNEEITYDYKF-- 131

                           90
                   ....*....|...
gi 1958681658  676 gTMPEKEILCQCF 688
Cdd:cd19169    132 -PIEDEKIPCLCG 143
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
 616-690 3.67e-07

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: 50.85  E-value: 3.67e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958681658  616 LDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYgyeagTMPEKEILCQCFCQ 690
Cdd:cd19170     78 VDATMHGNAARFINHSCEPNCYSRVVNIDGKKH----IVIFALRRILRGEELTYDY-----KFPIEDVKIPCTCG 143
ePHD_KMT2A cd15693
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant ...
 698-813 1.42e-06

Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of KMT2A. KMT2A also termed ALL-1, or CXXC-type zinc finger protein 7, or myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), or trithorax-like protein (Htrx), or zinc finger protein HRX, is a histone methyltransferase that belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2). It regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in the MLL1 complex, which also contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL1 complex is highly active and specific for H3K4methylation. KMT2A contains a CxxC (x for any residue) zinc finger domain, three PHD fingers, a Bromodomain domain, this extended PHD finger, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain.


Pssm-ID: 277163  Cd Length: 113  Bit Score: 48.07  E-value: 1.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  698 RTCVLCpeghdwsVIYFSPSANIA-----------AHENCLLYSSGLVEceahDPFNIAKNFDVSSVlekiwNGSTSKCS 766
Cdd:cd15693      1 RQCALC-------LKYGDDSANDAgrllyigqnewTHVNCALWSAEVFE----DDDGSLKNVHMAVI-----RGKQLRCE 64

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1958681658  767 FCNNEGAIMGCDETSCAKNYHLLCAKEDRAILQvgvkRTYKIFCPEH 813
Cdd:cd15693     65 FCQKPGATVGCCLTSCTSNYHFMCSRAKNCVFL----EDKKVYCQRH 107
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
 614-673 2.17e-06

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: 47.62  E-value: 2.17e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  614 FLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGY 673
Cdd:cd10519     62 FVVDATRKGNKIRFANHSSNPNCYAKVMMVNGDHR----IGIFAKRDIEAGEELFFDYGY 117
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
 356-407 3.32e-06

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: 47.67  E-value: 3.32e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958681658  356 LQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLSRATPEKTNIGESESEQQH 407
Cdd:cd19174      2 LERFRTEDKGWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRMIEQYHNHSHH 53
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
 356-395 6.09e-06

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: 46.86  E-value: 6.09e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958681658  356 LQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLSRATPEK 395
Cdd:cd10531      2 LELFRTEKKGWGVKAKEDIQKGEFIIEYVGEVIDKKEFKE 41
SET_NSD cd19173
SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...
 608-687 6.64e-06

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: 46.92  E-value: 6.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  608 LSKESLFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYEAgTMPEKEIlCQC 687
Cdd:cd19173     59 LTLDKDRIIDAGPKGNLSRFMNHSCQPNCETQKWTVNGDTR----VGLFAVRDIPAGEELTFNYNLDC-LGNEKKV-CRC 132
ePHD1_KMT2D cd15695
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...
 700-813 6.90e-06

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


Pssm-ID: 277165  Cd Length: 90  Bit Score: 45.29  E-value: 6.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  700 CVLCPEGHDWsviyfspsaniaAHENCLLYSSGLVECEAHDPFNIAKnfdvssvleKIWNGSTSKCSFCNNEGAIMGCDE 779
Cdd:cd15695      1 CALCNCGECW------------VHHWCAAWSAGVKQHEGDGLIGVDK---------AVFSGISQKCEHCKRLGATIQCHA 59

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1958681658  780 TSCAKNYHLLCAKEDRAILQVgvkRTYKIFCPEH 813
Cdd:cd15695     60 EGCPRFYHFPCAAASGSFQSM---KTLLLLCPEH 90
ePHD_KMT2B cd15694
Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant ...
 723-813 7.79e-06

Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of KMT2B. KMT2B is also called trithorax homolog 2 or WW domain-binding protein 7 (WBP-7). KMT2B is encoded by the gene that was first named myeloid/lymphoid or mixed-lineage leukemia 2 (MLL2), a second human homolog of Drosophila trithorax, located on chromosome 19. It belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2) and is vital for normal mammalian embryonic development. KMT2B functions as the catalytic subunit in the MLL2 complex, which contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL2 complex is highly active and specific for histone 3 lysine 4 (H3K4) methylation, which stimulates chromatin transcription in a SAM- and H3K4-dependent manner. Moreover, KMT2B plays a critical role in memory formation by mediating hippocampal H3K4 di- and trimethylation. It is also required for RNA polymerase II association and protection from DNA methylation at the MagohB CpG island promoter. KMT2B contains a CxxC (x for any residue) zinc finger domain, three PHD fingers, this ePHD finger, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain.


Pssm-ID: 277164  Cd Length: 105  Bit Score: 45.80  E-value: 7.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  723 HENCLLYSSGLVEceahdpfniAKNFDVSSVLEKIWNGSTSKCSFCNNEGAIMGCDETSCAKNYHLLCAKEDRAILQvgv 802
Cdd:cd15694     28 HVNCAIWSAEVFE---------ENDGSLKNVHAAVARGRQMRCEHCQKIGATVGCCLSACLSNFHFMCARASRCCFQ--- 95

                           90
                   ....*....|.
gi 1958681658  803 kRTYKIFCPEH 813
Cdd:cd15694     96 -DDKKVFCQKH 105
SET_SETD1A cd19204
SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...
 600-687 1.01e-05

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: 46.56  E-value: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  600 IPSASLVQLSKESLflLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYeagTMP 679
Cdd:cd19204     65 IGSSYLFRVDHDTI--IDATKCGNLARFINHCCTPNCYAKVITIESQKK----IVIYSKQPIGVNEEITYDYKF---PIE 135


                   ....*...
gi 1958681658  680 EKEILCQC 687
Cdd:cd19204    136 DNKIPCLC 143
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
 615-687 1.03e-05

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: 46.14  E-value: 1.03e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958681658  615 LLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYEAgtMPEKEILCQC 687
Cdd:cd19211     66 IIDAGPKGNYSRFMNHSCQPNCETQKWTVNGDTR----VGLFAVCDIPAGTELTFNYNLDC--LGNEKTVCRC 132
SET_ASHR3-like cd19175
SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...
 605-673 1.33e-05

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: 45.87  E-value: 1.33e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958681658  605 LVQLSKEslFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGY 673
Cdd:cd19175     56 MCEIDKD--MVIDATFKGNLSRFINHSCDPNCELQKWQVDGETR----IGVFAIRDIKKGEELTYDYQF 118
ePHD1_KMT2C cd15696
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
 722-791 1.48e-05

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


Pssm-ID: 277166  Cd Length: 90  Bit Score: 44.55  E-value: 1.48e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  722 AHENCLLYSSGLVECEAHDPFNIAKNFDvssvlekiwNGSTSKCSFCNNEGAIMGCDETSCAKNYHLLCA 791
Cdd:cd15696     11 AHLRCAEWSLGVCQGEEQLLVNVDKAVV---------SGSTERCAFCKHLGATIKCCEEKCTQMYHYPCA 71
ePHD_RAI1 cd15700
Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant ...
 722-813 1.54e-05

Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model corresponds to the C-terminal ePHD/ADD (ATRX-DNMT3-DNMT3L) domain of RAI1. RAI1, a homolog of stromelysin-1 PDGF (platelet-derived growth factor)-responsive element-binding protein (SPBP, also termed TCF-20), is a chromatin-binding protein implicated in the regulation of gene expression. It is strongly enriched on chromatin in interphase HeLa cells, and displays low nuclear mobility, and has been implicated in Smith-Magenis syndrome, Potocki-Lupski syndrome, and non-syndromic autism. RAI1 contains a region with homology to the novel nucleosome-binding region SPBP and an ePHD/ADD domain with ability to bind nucleosomes.


Pssm-ID: 277170  Cd Length: 104  Bit Score: 44.87  E-value: 1.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  722 AHENCLLYSSGLVeceahdpFNIAKNFDVSSVLEKiwnGSTSKCSFCNNEGAIMGCDETSCAKNYHLLCAKEDRAILqvg 801
Cdd:cd15700     26 VHEACAVWTTGVY-------LVAGKLFGLQEAVQK---AADAKCSSCQGAGATVGCCHKGCTQSYHYICAVEAGCLF--- 92

                           90
                   ....*....|..
gi 1958681658  802 VKRTYKIFCPEH 813
Cdd:cd15700     93 EEENFSLRCPKH 104
SET_SETD1B cd19205
SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...
 615-687 1.90e-05

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: 45.82  E-value: 1.90e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958681658  615 LLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYeagTMPEKEILCQC 687
Cdd:cd19205     78 IIDATKCGNFARFINHSCNPNCYAKVITVESQKK----IVIYSKQHINVNEEITYDYKF---PIEDVKIPCLC 143
ePHD_TCF20 cd15699
Extended PHD finger (ePHD) found in transcription factor 20 (TCF-20); The extended plant ...
 700-813 2.66e-05

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


Pssm-ID: 277169  Cd Length: 103  Bit Score: 44.14  E-value: 2.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  700 CVLCPEGHDWSVI--YFSPSANIAAHENCLLYSSGLVeceahdpFNIAKNFDVSSVLEkiwNGSTSKCSFCNNEGAIMGC 777
Cdd:cd15699      1 CCLCGKWANYRNLgdLFGPFYEFWVHEGCILWANGIY-------LVCGRLYGLQEALD---IAREMKCSHCQEAGATLGC 70

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958681658  778 DETSCAKNYHLLCAKEDRAILQvgvKRTYKIFCPEH 813
Cdd:cd15699     71 YNKGCSFRYHYPCAIDADCLLN---EENFSVRCPKH 103
SET_EZH1 cd19217
SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...
 589-673 3.95e-05

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: 44.67  E-value: 3.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  589 CGEELASERT--------KIPSASLVQLSKEslFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRY 660
Cdd:cd19217     36 CGELISQDEAdrrgkvydKYMSSFLFNLNND--FVVDATRKGNKIRFANHSVNPNCYAKVVMVNGDHR----IGIFAKRA 109

                           90
                   ....*....|...
gi 1958681658  661 VKARTELTWDYGY 673
Cdd:cd19217    110 IQQGEELFFDYRY 122
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
 615-687 4.02e-05

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: 44.53  E-value: 4.02e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958681658  615 LLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYEAgtMPEKEILCQC 687
Cdd:cd19210     66 IIDAGPKGNYARFMNHCCQPNCETQKWTVNGDTR----VGLFALCDIKAGTELTFNYNLEC--LGNGKTVCKC 132
SET_SUV39H_DIM5-like cd19473
SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...
 626-689 5.54e-05

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: 46.16  E-value: 5.54e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958681658  626 RFLNHSCYPNLWVQNVFVETHDRNFPLAAFFTNRYVKARTELTWDY-------GYEAGTMPEKEILCQCFC 689
Cdd:cd19473    195 RFINHSCDPNLRIFARVGDHADKHIHDLAFFAIKDIPRGTELTFDYvdgvtglDDDAGDEEKEKEMTKCLC 265
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
 355-389 6.86e-05

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: 43.72  E-value: 6.86e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1958681658  355 RLQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLS 389
Cdd:cd19172      3 KVEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLD 37
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
 614-687 7.64e-05

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: 43.96  E-value: 7.64e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958681658  614 FLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYEAGTmPEKEILCQC 687
Cdd:cd19171     76 WVIDATMTGGPARYINHSCNPNCVAEVVTFDKEKK----IIIISNRRIAKGEELTYDYKFDFED-DQHKIPCLC 144
SET_EZH2 cd19218
SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...
 614-673 1.24e-04

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: 42.59  E-value: 1.24e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  614 FLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGY 673
Cdd:cd19218     65 FVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHR----IGIFAKRAIQTGEELFFDYRY 120
SET_KMT2A cd19206
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...
 615-687 2.95e-04

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: 42.32  E-value: 2.95e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958681658  615 LLDASKEGNVGRFLNHSCYPNLW--VQNVFVETHdrnfplAAFFTNRYVKARTELTWDYGYEAGTmPEKEILCQC 687
Cdd:cd19206     77 VVDATMHGNAARFINHSCEPNCYsrVINIDGQKH------IVIFAMRKIYRGEELTYDYKFPIED-ASNKLPCNC 144
HAT_MBD cd01397
Methyl-CpG binding domains (MBD) present in putative chromatin remodelling factor such as ...
 153-214 3.49e-04

Methyl-CpG binding domains (MBD) present in putative chromatin remodelling factor such as BAZ2A; BAZ2A contains a MBD, DDT, PHD-type zinc finger and Bromo domain suggesting that BAZ2A might be associated with histone acetyltransferase (HAT) activity. The Drosophila melanogaster toutatis protein, a putative subunit of the chromatin-remodeling complex, and other such proteins in this group share a similar domain architecture with BAZ2A, as does the Caenorhabditis elegans flectin homolog.


Pssm-ID: 238691 [Multi-domain]  Cd Length: 73  Bit Score: 40.08  E-value: 3.49e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958681658  153 LQLPLRcHFQRRHAKTNSPSAALH--VNYRTPCGRSLRNMEEVFHYLLETECNFLFTDNFSFNT 214
Cdd:cd01397      2 LRVPLE-LGWRRETRIRGLGGRIQgeVAYYAPCGKKLRQYPEVIKYLSKNGISLLSRENFSFSA 64
SET_KMT2B cd19207
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...
 615-687 1.16e-03

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: 40.78  E-value: 1.16e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958681658  615 LLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYEAGTMPEKeILCQC 687
Cdd:cd19207     77 VVDATMHGNAARFINHSCEPNCYSRVIHVEGQKH----IVIFALRKIYRGEELTYDYKFPIEDASNK-LPCNC 144
SET_NSD cd19173
SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...
 354-392 1.48e-03

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: 39.99  E-value: 1.48e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1958681658  354 VRLQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLSRAT 392
Cdd:cd19173      2 PPTEPFKTGDRGWGLRTKRDIKKGDFVIEYVGELIDEEE 40
SET_SETD8 cd10528
SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2. ...
 617-672 1.66e-03

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: 39.87  E-value: 1.66e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958681658  617 DASKE-GNVGRFLNHSC-YPNLWVQNVFVETHDRNFplaaFFTNRYVKARTELTWDYG 672
Cdd:cd10528     86 DATKEsGRLGRLINHSKkKPNLKTKLLVIDGVPHLI----LVAKRDIKPGEELLYDYG 139
SET_NSD3 cd19212
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
 615-671 2.29e-03

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: 39.52  E-value: 2.29e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958681658  615 LLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDY 671
Cdd:cd19212     66 IIDAGPKGNYSRFMNHSCNPNCETQKWTVNGDVR----VGLFALCDIPAGMELTFNY 118
ePHD2_KMT2C cd15697
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
 719-813 2.31e-03

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


Pssm-ID: 277167  Cd Length: 105  Bit Score: 38.49  E-value: 2.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  719 NIAAHENCLLYSSGLVECEAHDPFNiaknfdVSSVLEKiwnGSTSKCSFCNNEGAIMGCDETSCAKNYHLLCAKEdraiL 798
Cdd:cd15697     24 DLWVHLNCALWSTEVYETQAGALIN------VELALRR---GLQMKCVFCHKTGATSGCHRLRCTNVYHFTCAIK----A 90

                           90
                   ....*....|....*
gi 1958681658  799 QVGVKRTYKIFCPEH 813
Cdd:cd15697     91 QCMFFKDKTMLCPMH 105
ePHD2_KMT2D cd15698
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...
 723-813 2.72e-03

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


Pssm-ID: 277168  Cd Length: 107  Bit Score: 38.49  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  723 HENCLLYSSGLVECEAHDPFNiaknfdVSSVLEKiwnGSTSKCSFCNNEGAIMGCDETSCAKNYHLLCAKEDRAILqvgv 802
Cdd:cd15698     28 HLNCALWSTEVYETQGGALMN------VEVALHR---GLLTKCSLCQKTGATNSCNRLRCPNVYHFACAIRAKCMF---- 94

                           90
                   ....*....|.
gi 1958681658  803 KRTYKIFCPEH 813
Cdd:cd15698     95 FKDKTMLCPMH 105
SET_KMT2D cd19209
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...
 592-687 2.95e-03

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: 39.29  E-value: 2.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  592 ELASERTKI---PSASLVQLSKESLFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELT 668
Cdd:cd19209     53 EVANRREKIyeeQNRGIYMFRINNEHVIDATLTGGPARYINHSCAPNCVAEVVTFDKEDK----IIIISSRRIPKGEELT 128

                           90
                   ....*....|....*....
gi 1958681658  669 WDYGYEAGTmPEKEILCQC 687
Cdd:cd19209    129 YDYQFDFED-DQHKIPCHC 146
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 365-425 3.56e-03

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: 38.27  E-value: 3.56e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958681658  365 GWGVRCLDDIDKGTFVCIYSGR-LLSRATPEKTNIGESESEQQHTVKNSFSKKRKIEVVCSD 425
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLELRLWGPYLFTLDEDSEYCID 62
PHD5_NSD cd15568
PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
 765-813 4.21e-03

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


Pssm-ID: 277043 [Multi-domain]  Cd Length: 43  Bit Score: 36.15  E-value: 4.21e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958681658  765 CSFCNNEGAIMGCDETSCAKNYHLLCAKEDrailqVGVKRTYkiFCPEH 813
Cdd:cd15568      2 CFRCGDGGDLVLCDFKGCPKVYHLSCLGLE-----KPPGGKW--ICPWH 43
SET_ASHR3-like cd19175
SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...
 355-395 5.32e-03

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: 38.17  E-value: 5.32e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958681658  355 RLQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLSRATPEK 395
Cdd:cd19175      1 KMKLVKTEKCGWGLVADEDINAGEFIIEYVGEVIDDKTCEE 41
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
 584-690 8.27e-03

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: 37.36  E-value: 8.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681658  584 SQQVSCGEELASERtkiPsasLVQLSKESLFLLDASKEGNVG-----RFLNHSCYPNlwvqnvfVETHDRNFPLAAFFTN 658
Cdd:cd20071     16 TRDIEPGELILVEK---P---LVSVPSNSFSLTDGLNEIGVGlfplaSLLNHSCDPN-------AVVVFDGNGTLRVRAL 82

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1958681658  659 RYVKARTELTWDYGYEAGTMPE--KEILCQ----CFCQ 690
Cdd:cd20071     83 RDIKAGEELTISYIDPLLPRTErrRELLEKygftCSCP 120
 
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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