NCBI Conserved Domain Search

Conserved domains on [gi|1958681660|ref|XP_038949805|]

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histone-lysine N-methyltransferase SETDB2 isoform X2 [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, ...

158-635

6.61e-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: 339.89 E-value: 6.61e-110

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 158 FSFNTYVQLTRNHPKQNEVVSDVDISNGVesvsisfcnevdnsklpqfkyrttvwprayhlnvssmFSDSCDCSEGCIDI 237
Cdd:cd10523     1 FSFNTYVQLDRNPQDQQQLVDDFDISNGA-------------------------------------FVDSCDCTDGCIDI 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 238 KKCACLQLTAKNAKACPLSPDGECTGYKYKRLQRLIPSGIYECNLFCKCNRQMCQNRVIQHGPRVRLQVFKSEKKGWGVR 317
Cdd:cd10523    44 LKCACLQLTARAFSKSESSPSKGGRGYKYKRLQEPIPSGLYECNVSCKCNRMLCQNRVVQHGLQVRLQVFKTEKKGWGVR 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 318 CLDDIDKGTFVCIYSGRLLSRATPEktnigeseseqqhtvknsfskkrkievvcsdrqthcespkTEGCPPKFSSDLEep 397
Cdd:cd10523   124 CLDDIDKGTFVCIYAGRVLSRARSP----------------------------------------TEPLPPKLELPSE-- 161

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 398 vvemnnrnisrtqrhsvirrpksktdvfHYNEKNMgfvcsysaapeEKNGFkpaqehldSKARRAhedlsssqvgysedk 477
Cdd:cd10523   162 ----------------------------NEVEVVT-----------SWLIL--------SKKRKL--------------- 179

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 478 qltesdvidtttsredtspaygckhaailnskntkkvlevpvktsqeeepaasqsqqvscgeelasertkipsaslvqls 557
Cdd:cd10523       --------------------------------------------------------------------------------

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958681660 558 KESLFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRNFPLAAFFTNRYVKARTELTWDYGYEAGTMPEKEILCQC 635
Cdd:cd10523   180 RENVCFLDASKEGNVGRFLNHSCCPNLFVQNVFVDTHDKNFPWVAFFTNRVVKAGTELTWDYSYDAGTSPEQEIPCLC 257

PHD_SF super family

cl22851

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

648-761

1.19e-37

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: 136.57 E-value: 1.19e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 648 CVLCPEGHDWSVIYFSPSANIAAHENCLLYSSGLVECEAHDPFNIAKNFDVSSVLEKIWNGSTSKCSFCNNEGAIMGCDE 727
Cdd:cd15712     1 CAFCPKGEEYSIMYFAQEQNIAAHQNCLLYSSGFVESEEYNPLNLDRRFDVESVLNEIKRGKRLKCNFCRKKGATVGCEE 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958681660 728 TSCAKNYHLLCAKEDRAILQV-GVKRTYKIFCPEH 761
Cdd:cd15712    81 RACRRSYHYFCALCDDAAIETdEVRGIYRVFCQKH 115

HMT_MBD

cd01395

Methyl-CpG binding domains (MBD) present in putative histone methyltransferases (HMT) such as ...

100-160

2.16e-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: 96.68 E-value: 2.16e-24

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958681660 100 PLQLPLRCHFQRRHAKTNSPSAALHVNYRTPCGRSLRNMEEVFHYLLETeCNFLFTDNFSF 160
Cdd:cd01395     1 PLHTPLLCGFQRMKYRARVGKVKKHVIYKAPCGRSLRNMSEVHRYLRET-CSFLTVDNFSF 60

SET

pfam00856

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

313-373

3.53e-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: 3.53e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958681660 313 GWGVRCLDDIDKGTFVCIYSGR-LLSRATPEKTNIGESESEQQHTVKNSFSKKRKIEVVCSD 373
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) ...

158-635

6.61e-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: 339.89 E-value: 6.61e-110

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 158 FSFNTYVQLTRNHPKQNEVVSDVDISNGVesvsisfcnevdnsklpqfkyrttvwprayhlnvssmFSDSCDCSEGCIDI 237
Cdd:cd10523     1 FSFNTYVQLDRNPQDQQQLVDDFDISNGA-------------------------------------FVDSCDCTDGCIDI 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 238 KKCACLQLTAKNAKACPLSPDGECTGYKYKRLQRLIPSGIYECNLFCKCNRQMCQNRVIQHGPRVRLQVFKSEKKGWGVR 317
Cdd:cd10523    44 LKCACLQLTARAFSKSESSPSKGGRGYKYKRLQEPIPSGLYECNVSCKCNRMLCQNRVVQHGLQVRLQVFKTEKKGWGVR 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 318 CLDDIDKGTFVCIYSGRLLSRATPEktnigeseseqqhtvknsfskkrkievvcsdrqthcespkTEGCPPKFSSDLEep 397
Cdd:cd10523   124 CLDDIDKGTFVCIYAGRVLSRARSP----------------------------------------TEPLPPKLELPSE-- 161

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 398 vvemnnrnisrtqrhsvirrpksktdvfHYNEKNMgfvcsysaapeEKNGFkpaqehldSKARRAhedlsssqvgysedk 477
Cdd:cd10523   162 ----------------------------NEVEVVT-----------SWLIL--------SKKRKL--------------- 179

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 478 qltesdvidtttsredtspaygckhaailnskntkkvlevpvktsqeeepaasqsqqvscgeelasertkipsaslvqls 557
Cdd:cd10523       --------------------------------------------------------------------------------

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958681660 558 KESLFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRNFPLAAFFTNRYVKARTELTWDYGYEAGTMPEKEILCQC 635
Cdd:cd10523   180 RENVCFLDASKEGNVGRFLNHSCCPNLFVQNVFVDTHDKNFPWVAFFTNRVVKAGTELTWDYSYDAGTSPEQEIPCLC 257

ePHD_PHF11

cd15712

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

648-761

1.19e-37

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: 136.57 E-value: 1.19e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 648 CVLCPEGHDWSVIYFSPSANIAAHENCLLYSSGLVECEAHDPFNIAKNFDVSSVLEKIWNGSTSKCSFCNNEGAIMGCDE 727
Cdd:cd15712     1 CAFCPKGEEYSIMYFAQEQNIAAHQNCLLYSSGFVESEEYNPLNLDRRFDVESVLNEIKRGKRLKCNFCRKKGATVGCEE 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958681660 728 TSCAKNYHLLCAKEDRAILQV-GVKRTYKIFCPEH 761
Cdd:cd15712    81 RACRRSYHYFCALCDDAAIETdEVRGIYRVFCQKH 115

HMT_MBD

cd01395

Methyl-CpG binding domains (MBD) present in putative histone methyltransferases (HMT) such as ...

100-160

2.16e-24

Pssm-ID: 238689 Cd Length: 60 Bit Score: 96.68 E-value: 2.16e-24

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958681660 100 PLQLPLRCHFQRRHAKTNSPSAALHVNYRTPCGRSLRNMEEVFHYLLETeCNFLFTDNFSF 160
Cdd:cd01395     1 PLHTPLLCGFQRMKYRARVGKVKKHVIYKAPCGRSLRNMSEVHRYLRET-CSFLTVDNFSF 60

zf-HC5HC2H

pfam13771

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

671-761

1.08e-18

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: 81.61 E-value: 1.08e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 671 HENCLLYSSGLVECEAHDPfniakNFDVSSVLEKIWNGSTSKCSFCN-NEGAIMGCDETSCAKNYHLLCAKEDRAILQV- 748
Cdd:pfam13771   1 HVVCALWSPELVQRGNDSM-----GFPIEDIEKIPKRRWKLKCYLCKkKGGACIQCSKKNCRRAFHVTCALEAGLLMQFd 75

                          90
                  ....*....|...
gi 1958681660 749 GVKRTYKIFCPEH 761
Cdd:pfam13771  76 EDNGTFKSYCKKH 88

Pre-SET

pfam05033

Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ...

182-294

2.21e-18

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: 80.93 E-value: 2.21e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 182 ISNGVESVSISFCNEVDNSKLP-QFKYRTTVWpraYHLNVSSMFSDSCDCsEGCIDiKKCACLQLTaknakacplsPDGE 260
Cdd:pfam05033   1 ISKGKENVPIPVVNEVDDEPPPpDFTYITSYI---YPKEFLLIIPQGCDC-GDCSS-EKCSCAQLN----------GGEF 65

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958681660 261 CTGYKYKRLQRL-IPSGIYECNLFCKCnRQMCQNR 294
Cdd:pfam05033  66 RFPYDKDGLLVPeSKPPIYECNPLCGC-PPSCPNR 99

SET

smart00317

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

560-622

1.74e-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: 1.74e-14

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958681660  560 SLFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYE 622
Cdd:smart00317  62 SDLCIDARRKGNLARFINHSCEPNCELLFVEVNGDDR----IVIFALRDIKPGEELTIDYGSD 120

SET

COG2940

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

564-635

1.71e-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: 1.71e-11

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958681660 564 LDASKEGNVGRFLNHSCYPNLWvqnvFVETHDRNFplaaFFTNRYVKARTELTWDYGYEagtMPEKEILCQC 635
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, ...

98-164

4.49e-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: 56.61 E-value: 4.49e-10

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958681660   98 ENPLQLPLRCHFQRRHA--KTNSPSAALHVNYRTPCGRSLRNMEEVFHYLLETECNFLFTDNFSFNTYV 164
Cdd:smart00391   1 GDPLRLPLPCGWRRETKqrKSGRSAGKFDVYYISPCGKKLRSKSELARYLHKNGDLSLDLECFDFNATV 69

MBD

pfam01429

Methyl-CpG binding domain; The Methyl-CpG binding domain (MBD) binds to DNA that contains one ...

97-164

1.48e-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: 1.48e-07

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660  97 GENPLQLPLRCHFQR--RHAKTNSPSAALHVNYRTPCGRSLRNMEEVFHYLLETECNFLFTDNFSFNTYV 164
Cdd:pfam01429   3 RKREDRLPLPPGWRReeRQRKSGSKAGKVDVFYYSPTGKKLRSKSEVARYLEANGGTSPKLEDFSFTVRS 72

SET

pfam00856

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

313-373

3.53e-03

Pssm-ID: 459965 [Multi-domain] Cd Length: 115 Bit Score: 38.27 E-value: 3.53e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958681660 313 GWGVRCLDDIDKGTFVCIYSGR-LLSRATPEKTNIGESESEQQHTVKNSFSKKRKIEVVCSD 373
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) ...

158-635

6.61e-110

Pssm-ID: 380921 [Multi-domain] Cd Length: 266 Bit Score: 339.89 E-value: 6.61e-110

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 158 FSFNTYVQLTRNHPKQNEVVSDVDISNGVesvsisfcnevdnsklpqfkyrttvwprayhlnvssmFSDSCDCSEGCIDI 237
Cdd:cd10523     1 FSFNTYVQLDRNPQDQQQLVDDFDISNGA-------------------------------------FVDSCDCTDGCIDI 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 238 KKCACLQLTAKNAKACPLSPDGECTGYKYKRLQRLIPSGIYECNLFCKCNRQMCQNRVIQHGPRVRLQVFKSEKKGWGVR 317
Cdd:cd10523    44 LKCACLQLTARAFSKSESSPSKGGRGYKYKRLQEPIPSGLYECNVSCKCNRMLCQNRVVQHGLQVRLQVFKTEKKGWGVR 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 318 CLDDIDKGTFVCIYSGRLLSRATPEktnigeseseqqhtvknsfskkrkievvcsdrqthcespkTEGCPPKFSSDLEep 397
Cdd:cd10523   124 CLDDIDKGTFVCIYAGRVLSRARSP----------------------------------------TEPLPPKLELPSE-- 161

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 398 vvemnnrnisrtqrhsvirrpksktdvfHYNEKNMgfvcsysaapeEKNGFkpaqehldSKARRAhedlsssqvgysedk 477
Cdd:cd10523   162 ----------------------------NEVEVVT-----------SWLIL--------SKKRKL--------------- 179

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 478 qltesdvidtttsredtspaygckhaailnskntkkvlevpvktsqeeepaasqsqqvscgeelasertkipsaslvqls 557
Cdd:cd10523       --------------------------------------------------------------------------------

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958681660 558 KESLFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRNFPLAAFFTNRYVKARTELTWDYGYEAGTMPEKEILCQC 635
Cdd:cd10523   180 RENVCFLDASKEGNVGRFLNHSCCPNLFVQNVFVDTHDKNFPWVAFFTNRVVKAGTELTWDYSYDAGTSPEQEIPCLC 257

SET_SETDB

cd10541

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

213-635

4.21e-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: 265.18 E-value: 4.21e-82

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 213 PRAYHLNVS-SMFSDSCDCSEGCIDIKKCACLQLTAKNAKACPLSPDGECTGYKYKRLQRLIPSGIYECNLFCKCNRQMC 291
Cdd:cd10541     2 PFYYIPDISyGKFLVGCDCTDGCRDKSKCACHQLTIQATACTPGGQDNPTAGYQYKRLEECLPTGVYECNKLCKCDPNMC 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 292 QNRVIQHGPRVRLQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLSRATPEKtnigesesEQQHTVKNSFSKKRKIEVVC 371
Cdd:cd10541    82 QNRLVQHGLQVRLQLFKTQNKGWGIRCLDDIAKGTFVCIYAGKILTDDFADK--------EGLEMGDEYFANLDHIEESC 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 372 Sdrqthcespktegcppkfssdleepvvemnnrnisrtqrhsvirrpksktdvfhyneknmgfvcsysaapeekngfkpa 451
Cdd:cd10541   154 Y------------------------------------------------------------------------------- 154

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 452 qehldskarrahedlsssqvgysedkqltesdVIDTTtsredtspaygckhaailnskntkkvlevpvktsqeeepaasq 531
Cdd:cd10541   155 --------------------------------IIDAK------------------------------------------- 159

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 532 sqqvscgeelasertkipsaslvqlskeslflldasKEGNVGRFLNHSCYPNLWVQNVFVETHDRNFPLAAFFTNRYVKA 611
Cdd:cd10541   160 ------------------------------------LEGNLGRYLNHSCSPNLFVQNVFVDTHDLRFPWVAFFASKRIKA 203

                         410       420
                  ....*....|....*....|....
gi 1958681660 612 RTELTWDYGYEAGTMPEKEILCQC 635
Cdd:cd10541   204 GTELTWDYNYEVGSVEGKELLCCC 227

SET_SETDB1

cd10517

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

181-635

7.02e-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: 255.68 E-value: 7.02e-78

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 181 DISNGVESVSISFCNEVDNSKLPQFKYRTTVWPRA-YHLNVSSMFSDSCDCSEGCIDIKKCACLQLTAKNAKACPLSPDG 259
Cdd:cd10517     8 DISYGKEGVPIPCVNEIDNSSPPYVEYSKERIPGKgVNINLDPDFLVGCDCTDGCRDKSKCACQQLTIEATAATPGGQIN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 260 ECTGYKYKRLQRLIPSGIYECNLFCKCNRqMCQNRVIQHGPRVRLQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLsra 339
Cdd:cd10517    88 PSAGYQYRRLMEKLPTGVYECNSRCKCDK-RCYNRVVQNGLQVRLQVFKTEKKGWGIRCLDDIPKGSFVCIYAGQIL--- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 340 tpektnigeseSEQqhtvknsfskkrkievvcsdrqthcespktegcppkfssdleepvvEMNNRnisrtqrhsvirrpk 419
Cdd:cd10517   164 -----------TED----------------------------------------------EANEE--------------- 171

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 420 sktdvfhynEKNMGfvcsysaapeekngfkpaqehldskarrahedlsssqvgyseDKQLTESDVIDTttsredtspayg 499
Cdd:cd10517   172 ---------GLQYG------------------------------------------DEYFAELDYIEV------------ 188

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 500 ckhaaILNSKntkkvlevpvktsqeeepaasqsqqvsCGEELASErtkipsaslvqlskESLFLLDASKEGNVGRFLNHS 579
Cdd:cd10517   189 -----VEKLK---------------------------EGYESDVE--------------EHCYIIDAKSEGNLGRYLNHS 222

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958681660 580 CYPNLWVQNVFVETHDRNFPLAAFFTNRYVKARTELTWDYGYEAGTMPEKEILCQC 635
Cdd:cd10517   223 CSPNLFVQNVFVDTHDLRFPWVAFFASRYIRAGTELTWDYNYEVGSVPGKVLYCYC 278

ePHD_PHF11

cd15712

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

648-761

1.19e-37

Pssm-ID: 277182 [Multi-domain] Cd Length: 115 Bit Score: 136.57 E-value: 1.19e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 648 CVLCPEGHDWSVIYFSPSANIAAHENCLLYSSGLVECEAHDPFNIAKNFDVSSVLEKIWNGSTSKCSFCNNEGAIMGCDE 727
Cdd:cd15712     1 CAFCPKGEEYSIMYFAQEQNIAAHQNCLLYSSGFVESEEYNPLNLDRRFDVESVLNEIKRGKRLKCNFCRKKGATVGCEE 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958681660 728 TSCAKNYHLLCAKEDRAILQV-GVKRTYKIFCPEH 761
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) ...

204-620

6.91e-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: 132.49 E-value: 6.91e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 204 QFKYRTTVWPRAYHLNVSSmFSDSCDCSEGCIDiKKCACLQLTAKNakacplspdgecTGYKYKRLQRLIPSG--IYECN 281
Cdd:cd10538     4 TYIKDNIVGKNVQPFSNII-DSVGCKCKDDCLD-SKCACAAESDGI------------FAYTKNGLLRLNNSPppIFECN 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 282 LFCKCNRqMCQNRVIQHGPRVRLQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLSratpektnigeseseqqhtvkNSF 361
Cdd:cd10538    70 SKCSCDD-DCKNRVVQRGLQARLQVFRTSKKGWGVRSLEFIPKGSFVCEYVGEVIT---------------------TSE 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 362 SKKRkievvcsdrqthcespktegcppkfssdleepvvemnnRNISRTQRHsvirrpksktdvfhyneknmgfvcSYSAA 441
Cdd:cd10538   128 ADRR--------------------------------------GKIYDKSGG------------------------SYLFD 145

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 442 peekngfkpaqehLDSKarrahedlsssqvgysedkqltesdvidtttsredtspaygckhaailnskntkkvlevpvkt 521
Cdd:cd10538   146 -------------LDEF--------------------------------------------------------------- 149

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 522 sqeeepaasqsqqvscgeelasertkipsaSLVQLSKESLFlLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRNFPLA 601
Cdd:cd10538   150 ------------------------------SDSDGDGEELC-VDATFCGNVSRFINHSCDPNLFPFNVVIDHDDLRYPRI 198

                         410
                  ....*....|....*....
gi 1958681660 602 AFFTNRYVKARTELTWDYG 620
Cdd:cd10538   199 ALFATRDILPGEELTFDYG 217

SET_AtSUVH-like

cd10545

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

225-621

1.01e-30

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: 120.97 E-value: 1.01e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 225 SDSCDCSEGCIDI-KKCAClqlTAKNAKACPLSPDGectgykykRLQRLIPSgIYECNLFCKCNRQmCQNRVIQHGPRVR 303
Cdd:cd10545    21 STGCDCKNRCTDGaSDCAC---VKKNGGEIPYNFNG--------RLIRAKPA-IYECGPLCKCPPS-CYNRVTQKGLRYR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 304 LQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLSRATPEKtnigeseseqqhtvknsfskkrkievvcsdrqthcespkt 383
Cdd:cd10545    88 LEVFKTAERGWGVRSWDSIPAGSFICEYVGELLDTSEADT---------------------------------------- 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 384 egcppkfssdleepvvemnnrnisrtqrhsvirrpKSKTDVFHYNEKNmgfvcsysaapeekngfkpaqehldskarraH 463
Cdd:cd10545   128 -----------------------------------RSGNDDYLFDIDN-------------------------------R 141

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 464 EDLSSSQVGysedkqlTESDVIDTTTSREdtspaygckhaailnskntkkvlevpvktSQEEEPAASqsqqvscgeelas 543
Cdd:cd10545   142 QTNRGWDGG-------QRLDVGMSDGERS-----------------------------SAEDEESSE------------- 172

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958681660 544 ertkipsaslvqlskeslFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRNFPLAAFFTNRYVKARTELTWDYGY 621
Cdd:cd10545   173 ------------------FTIDAGSFGNVARFINHSCSPNLFVQCVLYDHNDLRLPRVMLFAADNIPPLQELTYDYGY 232

SET_EHMT

cd10543

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

219-337

2.08e-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: 102.80 E-value: 2.08e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 219 NVSSMfsDSCDCSEGCiDIKKCACLQLTAKNA--KACPLSPDgectgykykrLQRLIPSGIYECNLFCKCNRQmCQNRVI 296
Cdd:cd10543    20 NITSL--QTCSCRDDC-SSDNCVCGRLSVRCWydKEGRLLPD----------FNKLDPPLIFECNRACSCWRN-CRNRVV 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958681660 297 QHGPRVRLQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLS 337
Cdd:cd10543    86 QNGIRYRLQLFRTRGMGWGVRALQDIPKGTFVCEYIGELIS 126

HMT_MBD

cd01395

Methyl-CpG binding domains (MBD) present in putative histone methyltransferases (HMT) such as ...

100-160

2.16e-24

Pssm-ID: 238689 Cd Length: 60 Bit Score: 96.68 E-value: 2.16e-24

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958681660 100 PLQLPLRCHFQRRHAKTNSPSAALHVNYRTPCGRSLRNMEEVFHYLLETeCNFLFTDNFSF 160
Cdd:cd01395     1 PLHTPLLCGFQRMKYRARVGKVKKHVIYKAPCGRSLRNMSEVHRYLRET-CSFLTVDNFSF 60

SET_SUV39H

cd10542

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

228-343

3.25e-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: 102.76 E-value: 3.25e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 228 CDCSEGCIDIKKCACLQLTAknakacplspdgecTGYKYKRLQRL-IPSG--IYECNLFCKCNRQmCQNRVIQHGPRVRL 304
Cdd:cd10542    25 CECTEDCHNNNPTCCPAESG--------------VKFAYDKQGRLrLPPGtpIYECNSRCKCGPD-CPNRVVQRGRKVPL 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958681660 305 QVFK-SEKKGWGVRCLDDIDKGTFVCIYSGRLLSRATPEK 343
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); ...

648-761

6.23e-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: 97.46 E-value: 6.23e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 648 CVLCPEGHDWSVIYF--SPSANIAAHENCLLYSSGLVECEAHDPFNIAkNFDVSSVLEKIWNGSTSKCSFCNNEGAIMGC 725
Cdd:cd15673     1 CGFCKSGEENKETGGklASGEKIAAHHNCMLFSSGLVQYVSPNENDFG-GFDIEDVKKEIKRGRKLKCNLCKKTGATIGC 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958681660 726 DETSCAKNYHLLCAKEDRA-ILQVGVKRTYKIFCPEH 761
Cdd:cd15673    80 DVKQCKKTYHYHCAKKDDAkIIERNSQGIYRVYCKNH 116

SET_SETMAR

cd10544

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

221-337

1.10e-23

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: 101.22 E-value: 1.10e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 221 SSMFSDSCDCSEGCIDIKKCACLQ--LTAKNAKACPLSPDGECTGykykrlqrliPsgIYECNLFCKCNRQmCQNRVIQH 298
Cdd:cd10544    20 NEITFPGCDCKTSSCEPETCSCLRkyGPNYDDDGCLLDFDGKYSG----------P--VFECNSMCKCSES-CQNRVVQN 86

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958681660 299 GPRVRLQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLS 337
Cdd:cd10544    87 GLQFKLQVFKTPKKGWGLRTLEFIPKGRFVCEYAGEVIG 125

SET_EHMT1

cd10535

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

228-339

6.78e-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: 89.61 E-value: 6.78e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 228 CDCSEGCIDiKKCACLQLTAKnakaCPLSPDGECtgykYKRLQRLIPSGIYECNLFCKCNRQmCQNRVIQHGPRVRLQVF 307
Cdd:cd10535    27 CVCIDDCSS-SNCMCGQLSMR----CWYDKDGRL----LPEFNMAEPPLIFECNHACSCWRN-CRNRVVQNGLRARLQLY 96

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958681660 308 KSEKKGWGVRCLDDIDKGTFVCIYSGRLLSRA 339
Cdd:cd10535    97 RTRDMGWGVRSLQDIPPGTFVCEYVGELISDS 128

SET_EHMT2

cd10533

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

228-339

1.64e-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: 1.64e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 228 CDCSEGCIDiKKCACLQLTAKnakaCPLSPDGECtgykYKRLQRLIPSGIYECNLFCKCNRQmCQNRVIQHGPRVRLQVF 307
Cdd:cd10533    27 CTCVDDCSS-SNCLCGQLSIR----CWYDKDGRL----LQEFNKIEPPLIFECNQACSCWRN-CKNRVVQSGIKVRLQLY 96

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958681660 308 KSEKKGWGVRCLDDIDKGTFVCIYSGRLLSRA 339
Cdd:cd10533    97 RTAKMGWGVRALQTIPQGTFICEYVGELISDA 128

zf-HC5HC2H

pfam13771

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

671-761

1.08e-18

Pssm-ID: 463977 [Multi-domain] Cd Length: 88 Bit Score: 81.61 E-value: 1.08e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 671 HENCLLYSSGLVECEAHDPfniakNFDVSSVLEKIWNGSTSKCSFCN-NEGAIMGCDETSCAKNYHLLCAKEDRAILQV- 748
Cdd:pfam13771   1 HVVCALWSPELVQRGNDSM-----GFPIEDIEKIPKRRWKLKCYLCKkKGGACIQCSKKNCRRAFHVTCALEAGLLMQFd 75

                          90
                  ....*....|...
gi 1958681660 749 GVKRTYKIFCPEH 761
Cdd:pfam13771  76 EDNGTFKSYCKKH 88

Pre-SET

pfam05033

Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ...

182-294

2.21e-18

Pssm-ID: 461530 [Multi-domain] Cd Length: 99 Bit Score: 80.93 E-value: 2.21e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 182 ISNGVESVSISFCNEVDNSKLP-QFKYRTTVWpraYHLNVSSMFSDSCDCsEGCIDiKKCACLQLTaknakacplsPDGE 260
Cdd:pfam05033   1 ISKGKENVPIPVVNEVDDEPPPpDFTYITSYI---YPKEFLLIIPQGCDC-GDCSS-EKCSCAQLN----------GGEF 65

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958681660 261 CTGYKYKRLQRL-IPSGIYECNLFCKCnRQMCQNR 294
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 ...

204-343

2.26e-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: 83.00 E-value: 2.26e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 204 QFKYRTTVWPRayhlnvSSMFSDSCDCS--EGCI--DIKKCACLQLTAKNAKACPlspdgectgyKYKRLQRLIPSGIYE 279
Cdd:cd20073     8 SYRYGLGIEPP------DPLFISGCSCSklGGCDlnNPGSCQCLEDSNEKSFAYD----------EYGRVRANTGSIIYE 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958681660 280 CNLFCKCNRQmCQNRVIQHGPRVRLQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLSRATPEK 343
Cdd:cd20073    72 CNENCDCGIN-CPNRVVQRGRKLPLEIFKTKHKGWGLRCPRFIKAGTFIGVYLGEVITQSEAEI 134

MBD

cd00122

MeCP2, MBD1, MBD2, MBD3, MBD4, CLLD8-like, and BAZ2A-like proteins constitute a family of ...

100-160

3.14e-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: 3.14e-17

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958681660 100 PLQLPLRCHFQRRHAKTNSPSA-ALHVNYRTPCGRSLRNMEEVFHYLLETECNFLFTDNFSF 160
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; ...

222-345

1.33e-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: 1.33e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 222 SMFSDSCDCSEG--CIdIKKCACLQ-LTAKNAKACPLSPDG-ECTGYKYKRLQRLIPSG---IYECNLFCKCNrQMCQNR 294
Cdd:cd19473    20 EEFRSGCECTDDedCM-YSGCLCLQdVDPDDDRDPGKKKNAyHSSGAKKGCLRGHMLNSrlpIYECHEGCACS-DDCPNR 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958681660 295 VIQHGPRVRLQVFK-SEKKGWGVRCLDDIDKGTFVCIYSGRLLsraTPEKTN 345
Cdd:cd19473    98 VVERGRKVPLQIFRtSDGRGWGVRSTVDIKRGQFVDCYVGEII---TPEEAQ 146

SET

smart00317

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

560-622

1.74e-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: 1.74e-14

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958681660  560 SLFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYE 622
Cdd:smart00317  62 SDLCIDARRKGNLARFINHSCEPNCELLFVEVNGDDR----IVIFALRDIKPGEELTIDYGSD 120

ePHD2_PHF6

cd15711

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

668-761

3.71e-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: 3.71e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 668 IAAHENCLLYSSGLVECEAHDPFNIAkNFDVSSVLEKIWNGSTSKCSFCNNEGAIMGCDETSCAKNYHLLCAKEDRAILQ 747
Cdd:cd15711    25 AAAHYKCMLFSSGTVQLTTTSRAEFG-DFDIKTVIQEIKRGKRMKCTLCSQLGATIGCEIKACVKTYHYHCGVQDKAKYI 103

                          90
                  ....*....|....*
gi 1958681660 748 VGVKR-TYKIFCPEH 761
Cdd:cd15711   104 ENMSRgIYKLYCKNH 118

ePHD_PHF7_G2E3_like

cd15669

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

648-761

4.13e-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: 66.50 E-value: 4.13e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 648 CVLCPEGHDWSVIY--FSPSANIAAHENCLLYSSGLVEcEAHDPFNIAkNFDVSSVLEKIWNGSTSKCSFCNNEGAIMGC 725
Cdd:cd15669     1 CVLCGRSDDDPDKYgeKLQKDGICAHYFCLLFSSGLPQ-RGEDNEGIY-GFLPEDIRKEVRRASRLRCFYCKKKGASIGC 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958681660 726 DETSCAKNYHLLCAKEDRAILQvgVKRTYKIFCPEH 761
Cdd:cd15669    79 AVKGCRRSFHFPCGLENGCVTQ--FFGEYRSFCWEH 112

SET_SUV39H2

cd10532

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

562-619

1.19e-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: 68.76 E-value: 1.19e-12

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958681660 562 FLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRNFPLAAFFTNRYVKARTELTWDY 619
Cdd:cd10532   149 FTVDAARYGNVSHFVNHSCDPNLQVFNVFIDNLDTRLPRIALFSTRTIKAGEELTFDY 206

ePHD1_PHF6

cd15710

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

663-761

2.50e-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: 64.60 E-value: 2.50e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 663 SPSANIAAHENCLLYSSGLVECEAhDPFNIAkNFDVSSVLEKIWNGSTSKCSFCNNEGAIMGCDETSCAKNYHLLCAKED 742
Cdd:cd15710    18 SENQKVAAHHKCMLFSSALVSSHS-DSENLG-GFSIEDVQKEIKRGTKLMCSLCHCPGATIGCDVKTCHRTYHYYCALHD 95

                          90       100
                  ....*....|....*....|
gi 1958681660 743 RAILQVGVKR-TYKIFCPEH 761
Cdd:cd15710    96 KAQIRENPSQgIYMIYCRKH 115

ePHD

cd15571

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

648-761

3.31e-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: 64.14 E-value: 3.31e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 648 CVLCPEG---HDWSVIYFSPSANIAAHENCLLYSSGLVECEAHDPfniaKNFDVSSVLEKiwnGSTSKCSFCN-NEGAIM 723
Cdd:cd15571     1 CALCPRSggaLKGGGALKTTSDGLWVHVVCALWSPEVYFDDGTLL----EVEGVSKIPKR---RKKLKCSICGkRGGACI 73

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958681660 724 GCDETSCAKNYHLLCAKEDRAILQVGVKRT-YKIFCPEH 761
Cdd:cd15571    74 QCSYPGCPRSFHVSCAIRAGCLFEFEDGPGnFVVYCPKH 112

SET_SUV39H1

cd10525

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

559-619

4.05e-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: 67.23 E-value: 4.05e-12

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958681660 559 ESLFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRNFPLAAFFTNRYVKARTELTWDY 619
Cdd:cd10525   148 EDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIALFATRTIRAGEELTFDY 208

SET

pfam00856

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

553-620

6.02e-12

Pssm-ID: 459965 [Multi-domain] Cd Length: 115 Bit Score: 63.31 E-value: 6.02e-12

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 553 LVQLSKESLFLLDAS--KEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYG 620
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 ...

181-285

1.19e-11

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: 62.05 E-value: 1.19e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660  181 DISNGVESVSISFCNEVDNSKLP-QFKY-RTTVWPRAYHLNVSSMFSDSCDCSEGCIDIKKCACLQLTaknakacplspD 258
Cdd:smart00468   3 DISNGKENVPVPLVNEVDEDPPPpDFEYiSEYIYGQGVPIDRSPSPLVGCSCSGDCSSSNKCECARKN-----------G 71

                           90       100
                   ....*....|....*....|....*..
gi 1958681660  259 GECTGYKYKRLQRLIPSGIYECNLFCK 285
Cdd:smart00468  72 GEFAYELNGGLRLKRKPLIYECNSRCS 98

SET

COG2940

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

564-635

1.71e-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: 1.71e-11

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958681660 564 LDASKEGNVGRFLNHSCYPNLWvqnvFVETHDRNFplaaFFTNRYVKARTELTWDYGYEagtMPEKEILCQC 635
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 ...

218-343

4.15e-11

Pssm-ID: 380930 [Multi-domain] Cd Length: 243 Bit Score: 64.14 E-value: 4.15e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 218 LNVSSMFSDSCDCSEgcidikkcaCLQltaknAKACPLSPdGECTGYKyKRLQRLIPSG--IYECNLFCKCNRQmCQNRV 295
Cdd:cd10532    15 INLDNEATVGCDCSD---------CFF-----GKCCPAEA-GVLFAYN-EHGQLKIPPGtpIYECNSRCKCGPD-CPNRV 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958681660 296 IQHGPRVRLQVFK-SEKKGWGVRCLDDIDKGTFVCIYSGRLLSRATPEK 343
Cdd:cd10532    78 VQKGTQYSLCIFRtSNGRGWGVKTLQKIKKNSFVMEYVGEVITSEEAER 126

SET_SETD2

cd19172

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

564-637

6.31e-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: 6.31e-11

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958681660 564 LDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYEA-GTMPEKeilcqCFC 637
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), ...

564-637

1.94e-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: 59.58 E-value: 1.94e-10

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958681660 564 LDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYEAgtmpEKEILCQCFC 637
Cdd:cd10531    65 IDATRKGNLSRFINHSCEPNCETQKWIVNGEYR----IGIFALRDIPAGEELTFDYNFVN----YNEAKQVCLC 130

SET

cd08161

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

572-620

4.39e-10

Pssm-ID: 380914 [Multi-domain] Cd Length: 72 Bit Score: 56.49 E-value: 4.39e-10

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958681660 572 VGRFLNHSCYPNLWvqnvFVETHDRNFPLAAFFTNRYVKARTELTWDYG 620
Cdd:cd08161    28 LARFINHSCEPNCE----FEEVYVGGKPRVFIVALRDIKAGEELTVDYG 72

MBD

smart00391

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

98-164

4.49e-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: 56.61 E-value: 4.49e-10

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958681660   98 ENPLQLPLRCHFQRRHA--KTNSPSAALHVNYRTPCGRSLRNMEEVFHYLLETECNFLFTDNFSFNTYV 164
Cdd:smart00391   1 GDPLRLPLPCGWRRETKqrKSGRSAGKFDVYYISPCGKKLRSKSELARYLHKNGDLSLDLECFDFNATV 69

SET_SUV39H1

cd10525

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

240-343

5.97e-10

Pssm-ID: 380923 [Multi-domain] Cd Length: 255 Bit Score: 61.06 E-value: 5.97e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 240 CACLQLTAKNAKACPLSPDGECTGYKYKRLQRLIPS-GIYECNLFCKCNRQmCQNRVIQHGPRVRLQVFKSEK-KGWGVR 317
Cdd:cd10525    24 CECQDCLSQPVGGCCPGASKHRFAYNEQGQVKVRPGlPIYECNSRCRCGPD-CPNRVVQKGIQYDLCIFRTDNgRGWGVR 102

                          90       100
                  ....*....|....*....|....*.
gi 1958681660 318 CLDDIDKGTFVCIYSGRLLSRATPEK 343
Cdd:cd10525   103 TLEKIRKNSFVMEYVGEIITSEEAER 128

SET_ASH1L

cd19174

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

556-635

2.81e-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: 2.81e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 556 LSKESLFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYEAGTMPEKEIlCQC 635
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); ...

648-761

4.88e-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: 54.25 E-value: 4.88e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 648 CVLCPEGHDWsviyfspsaniaAHENCLLYSSGLVECEahdpfniakNFDVSSVLEKIWNGSTSKCSFCNNEGAIMGCDE 727
Cdd:cd15665     1 CALCNLGEVY------------AHHCCAAWSEGVCQTE---------DGALENVDKAVAKALSQKCSFCLRYGASISCRM 59

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958681660 728 TSCAKNYHLLCAKEDRAILqvgVKRTYKIFCPEH 761
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 ...

671-761

1.42e-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: 53.18 E-value: 1.42e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 671 HENCLLYSSGLVEcEAHDPFniaKNfdvssVLEKIWNGSTSKCSFCNNEGAIMGCDETSCAKNYHLLCAKEDRAILQvgv 750
Cdd:cd15664    28 HINCALWSAEVFE-EDDGSL---QN-----VHSAVSRGRMMKCELCGKPGATVGCCLKSCPANYHFMCARKAECVFQ--- 95

                          90
                  ....*....|.
gi 1958681660 751 kRTYKIFCPEH 761
Cdd:cd15664    96 -DDKKVFCPAH 105

SET

smart00317

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

302-343

1.75e-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: 53.49 E-value: 1.75e-08

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958681660  302 VRLQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLSRATPEK 343
Cdd:smart00317   1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEE 42

ePHD_RAI1_like

cd15668

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

648-761

3.79e-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: 51.92 E-value: 3.79e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 648 CVLCPEGHDWSVI--YFSPSANIAAHENCLLYSSGLVECEAHdpfniaknfdVSSVLEKIWNGSTSKCSFCNNEGAIMGC 725
Cdd:cd15668     1 CVFCKRGPHYKGLgdLFGPYYEVWVHEDCAVWAPGVYLVGGK----------LYGLEEAVWVAKQSVCSSCQQTGATIGC 70

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958681660 726 DETSCAKNYHLLCAKEDRAILQvgvKRTYKIFCPEH 761
Cdd:cd15668    71 LHKGCKAKYHYPCAVESGCQLD---EENFSLLCPKH 103

SET_LegAS4-like

cd10522

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

564-622

4.06e-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: 4.06e-08

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958681660 564 LDASKEGNVGRFLNHSCYPNLWvqnvFVETHDRNFPLAAFFTNRYVKARTELTWDYGYE 622
Cdd:cd10522    65 IDAGKKGNLTRFINHSDQPNLE----LIVRTLKGEQHIGFVAIRDIKPGEELFISYGPK 119

ePHD2_KMT2C_like

cd15666

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

648-761

5.35e-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: 51.53 E-value: 5.35e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 648 CVLCPEGHDWSVI----YFSPSANIAAHENCLLYSSGLVEceahdpfniAKNFDVSSVLEKIWNGSTSKCSFCNNEGAIM 723
Cdd:cd15666     1 CVLCGGEGDGDTDgpgrLLNLDVDKWVHLNCALWSYEVYE---------TQNGALMNVEEALRRALTTTCSHCGRTGATV 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958681660 724 GCDETSCAKNYHLLCAKEDRAILqvgvkrtYK---IFCPEH 761
Cdd:cd15666    72 PCFKPRCANVYHLPCAIKDGCMF-------FKdktMLCPSH 105

SET_SETD1-like

cd10518

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

565-635

6.98e-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: 6.98e-08

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958681660 565 DASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDY--GYEagtmPEKEILCQC 635
Cdd:cd10518    80 DATKKGNIARFINHSCDPNCYAKIITVDGEKH----IVIFAKRDIAPGEELTYDYkfPIE----DEEKIPCLC 144

SET_SET1

cd20072

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

533-635

7.94e-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: 7.94e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 533 QQVSCGEELASERTKIPSASLVQLSKESLflLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKAR 612
Cdd:cd20072    49 QQVADEREKRYLRQGIGSSYLFRIDDDTV--VDATKKGNIARFINHCCDPNCTAKIIKVEGEKR----IVIYAKRDIAAG 122

                          90       100
                  ....*....|....*....|...
gi 1958681660 613 TELTWDYGYEagtMPEKEILCQC 635
Cdd:cd20072   123 EELTYDYKFP---REEDKIPCLC 142

MBD

pfam01429

Methyl-CpG binding domain; The Methyl-CpG binding domain (MBD) binds to DNA that contains one ...

97-164

1.48e-07

Pssm-ID: 396147 [Multi-domain] Cd Length: 76 Bit Score: 49.67 E-value: 1.48e-07

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660  97 GENPLQLPLRCHFQR--RHAKTNSPSAALHVNYRTPCGRSLRNMEEVFHYLLETECNFLFTDNFSFNTYV 164
Cdd:pfam01429   3 RKREDRLPLPPGWRReeRQRKSGSKAGKVDVFYYSPTGKKLRSKSEVARYLEANGGTSPKLEDFSFTVRS 72

SET_SETD1

cd19169

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

544-636

2.52e-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: 51.18 E-value: 2.52e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 544 ERTKIPSASLVQLSKEslFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRNFplaaFFTNRYVKARTELTWDYGYea 623
Cdd:cd19169    60 EAIGIGSSYLFRVDDD--TIIDATKCGNLARFINHSCNPNCYAKIITVESQKKIV----IYSKRPIAVNEEITYDYKF-- 131

                          90
                  ....*....|...
gi 1958681660 624 gTMPEKEILCQCF 636
Cdd:cd19169   132 -PIEDEKIPCLCG 143

SET_KMT2A_2B

cd19170

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

564-638

3.74e-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: 50.47 E-value: 3.74e-07

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958681660 564 LDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYgyeagTMPEKEILCQCFCQ 638
Cdd:cd19170    78 VDATMHGNAARFINHSCEPNCYSRVVNIDGKKH----IVIFALRRILRGEELTYDY-----KFPIEDVKIPCTCG 143

ePHD_KMT2A

cd15693

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

670-761

1.70e-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: 47.69 E-value: 1.70e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 670 AHENCLLYSSGLVEceahDPFNIAKNFDVSSVlekiwNGSTSKCSFCNNEGAIMGCDETSCAKNYHLLCAKEDRAILQvg 749
Cdd:cd15693    29 THVNCALWSAEVFE----DDDGSLKNVHMAVI-----RGKQLRCEFCQKPGATVGCCLTSCTSNYHFMCSRAKNCVFL-- 97

                          90
                  ....*....|..
gi 1958681660 750 vkRTYKIFCPEH 761
Cdd:cd15693    98 --EDKKVYCQRH 107

SET_EZH

cd10519

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

562-621

2.06e-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: 2.06e-06

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 562 FLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGY 621
Cdd:cd10519    62 FVVDATRKGNKIRFANHSSNPNCYAKVMMVNGDHR----IGIFAKRDIEAGEELFFDYGY 117

SET_ASH1L

cd19174

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

304-355

3.38e-06

Pssm-ID: 380951 [Multi-domain] Cd Length: 141 Bit Score: 47.67 E-value: 3.38e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958681660 304 LQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLSRATPEKTNIGESESEQQH 355
Cdd:cd19174     2 LERFRTEDKGWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRMIEQYHNHSHH 53

SET_SETD2-like

cd10531

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

304-343

6.21e-06

Pssm-ID: 380929 Cd Length: 136 Bit Score: 46.48 E-value: 6.21e-06

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958681660 304 LQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLSRATPEK 343
Cdd:cd10531     2 LELFRTEKKGWGVKAKEDIQKGEFIIEYVGEVIDKKEFKE 41

SET_NSD

cd19173

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

556-635

6.27e-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: 6.27e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 556 LSKESLFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYEAgTMPEKEIlCQC 635
Cdd:cd19173    59 LTLDKDRIIDAGPKGNLSRFMNHSCQPNCETQKWTVNGDTR----VGLFAVRDIPAGEELTFNYNLDC-LGNEKKV-CRC 132

ePHD_KMT2B

cd15694

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

671-761

8.61e-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: 45.42 E-value: 8.61e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 671 HENCLLYSSGLVEceahdpfniAKNFDVSSVLEKIWNGSTSKCSFCNNEGAIMGCDETSCAKNYHLLCAKEDRAILQvgv 750
Cdd:cd15694    28 HVNCAIWSAEVFE---------ENDGSLKNVHAAVARGRQMRCEHCQKIGATVGCCLSACLSNFHFMCARASRCCFQ--- 95

                          90
                  ....*....|.
gi 1958681660 751 kRTYKIFCPEH 761
Cdd:cd15694    96 -DDKKVFCQKH 105

SET_SETD1A

cd19204

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

548-635

9.95e-06

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: 9.95e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 548 IPSASLVQLSKESLflLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYeagTMP 627
Cdd:cd19204    65 IGSSYLFRVDHDTI--IDATKCGNLARFINHCCTPNCYAKVITIESQKK----IVIYSKQPIGVNEEITYDYKF---PIE 135


                  ....*...
gi 1958681660 628 EKEILCQC 635
Cdd:cd19204   136 DNKIPCLC 143

SET_NSD2

cd19211

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

563-635

1.02e-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: 1.02e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958681660 563 LLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYEAgtMPEKEILCQC 635
Cdd:cd19211    66 IIDAGPKGNYSRFMNHSCQPNCETQKWTVNGDTR----VGLFAVCDIPAGTELTFNYNLDC--LGNEKTVCRC 132

ePHD1_KMT2D

cd15695

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

648-761

1.05e-05

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: 44.91 E-value: 1.05e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 648 CVLCPEGHDWsviyfspsaniaAHENCLLYSSGLVECEAHDPFNIAKnfdvssvleKIWNGSTSKCSFCNNEGAIMGCDE 727
Cdd:cd15695     1 CALCNCGECW------------VHHWCAAWSAGVKQHEGDGLIGVDK---------AVFSGISQKCEHCKRLGATIQCHA 59

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958681660 728 TSCAKNYHLLCAKEDRAILQVgvkRTYKIFCPEH 761
Cdd:cd15695    60 EGCPRFYHFPCAAASGSFQSM---KTLLLLCPEH 90

SET_ASHR3-like

cd19175

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

553-621

1.21e-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: 1.21e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958681660 553 LVQLSKEslFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGY 621
Cdd:cd19175    56 MCEIDKD--MVIDATFKGNLSRFINHSCDPNCELQKWQVDGETR----IGVFAIRDIKKGEELTYDYQF 118

SET_SETD1B

cd19205

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

563-635

1.95e-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: 1.95e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958681660 563 LLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYeagTMPEKEILCQC 635
Cdd:cd19205    78 IIDATKCGNFARFINHSCNPNCYAKVITVESQKK----IVIYSKQHINVNEEITYDYKF---PIEDVKIPCLC 143

ePHD1_KMT2C

cd15696

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

670-739

2.01e-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: 44.16 E-value: 2.01e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 670 AHENCLLYSSGLVECEAHDPFNIAKNFDvssvlekiwNGSTSKCSFCNNEGAIMGCDETSCAKNYHLLCA 739
Cdd:cd15696    11 AHLRCAEWSLGVCQGEEQLLVNVDKAVV---------SGSTERCAFCKHLGATIKCCEEKCTQMYHYPCA 71

ePHD_RAI1

cd15700

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

670-761

2.35e-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: 44.10 E-value: 2.35e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 670 AHENCLLYSSGLVeceahdpFNIAKNFDVSSVLEKiwnGSTSKCSFCNNEGAIMGCDETSCAKNYHLLCAKEDRAILqvg 749
Cdd:cd15700    26 VHEACAVWTTGVY-------LVAGKLFGLQEAVQK---AADAKCSSCQGAGATVGCCHKGCTQSYHYICAVEAGCLF--- 92

                          90
                  ....*....|..
gi 1958681660 750 VKRTYKIFCPEH 761
Cdd:cd15700    93 EEENFSLRCPKH 104

SET_EZH1

cd19217

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

537-621

3.02e-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: 3.02e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 537 CGEELASERT--------KIPSASLVQLSKEslFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRY 608
Cdd:cd19217    36 CGELISQDEAdrrgkvydKYMSSFLFNLNND--FVVDATRKGNKIRFANHSVNPNCYAKVVMVNGDHR----IGIFAKRA 109

                          90
                  ....*....|...
gi 1958681660 609 VKARTELTWDYGY 621
Cdd:cd19217   110 IQQGEELFFDYRY 122

ePHD_TCF20

cd15699

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

648-761

3.33e-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: 43.75 E-value: 3.33e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 648 CVLCPEGHDWSVI--YFSPSANIAAHENCLLYSSGLVeceahdpFNIAKNFDVSSVLEkiwNGSTSKCSFCNNEGAIMGC 725
Cdd:cd15699     1 CCLCGKWANYRNLgdLFGPFYEFWVHEGCILWANGIY-------LVCGRLYGLQEALD---IAREMKCSHCQEAGATLGC 70

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958681660 726 DETSCAKNYHLLCAKEDRAILQvgvKRTYKIFCPEH 761
Cdd:cd15699    71 YNKGCSFRYHYPCAIDADCLLN---EENFSVRCPKH 103

SET_NSD1

cd19210

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

563-635

4.10e-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: 4.10e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958681660 563 LLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYEAgtMPEKEILCQC 635
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; ...

574-637

5.26e-05

Pssm-ID: 380996 [Multi-domain] Cd Length: 274 Bit Score: 46.16 E-value: 5.26e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958681660 574 RFLNHSCYPNLWVQNVFVETHDRNFPLAAFFTNRYVKARTELTWDY-------GYEAGTMPEKEILCQCFC 637
Cdd:cd19473   195 RFINHSCDPNLRIFARVGDHADKHIHDLAFFAIKDIPRGTELTFDYvdgvtglDDDAGDEEKEKEMTKCLC 265

SET_SETD2

cd19172

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

303-337

6.54e-05

Pssm-ID: 380949 [Multi-domain] Cd Length: 142 Bit Score: 43.72 E-value: 6.54e-05

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1958681660 303 RLQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLS 337
Cdd:cd19172     3 KVEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLD 37

SET_KMT2C_2D

cd19171

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

562-635

7.49e-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: 7.49e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958681660 562 FLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYEAGTmPEKEILCQC 635
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) ...

562-621

1.17e-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: 1.17e-04

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 562 FLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGY 621
Cdd:cd19218    65 FVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHR----IGIFAKRAIQTGEELFFDYRY 120

SET_KMT2A

cd19206

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

563-635

2.89e-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: 2.89e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958681660 563 LLDASKEGNVGRFLNHSCYPNLW--VQNVFVETHdrnfplAAFFTNRYVKARTELTWDYGYEAGTmPEKEILCQC 635
Cdd:cd19206    77 VVDATMHGNAARFINHSCEPNCYsrVINIDGQKH------IVIFAMRKIYRGEELTYDYKFPIED-ASNKLPCNC 144

HAT_MBD

cd01397

Methyl-CpG binding domains (MBD) present in putative chromatin remodelling factor such as ...

101-162

3.69e-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: 39.70 E-value: 3.69e-04

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958681660 101 LQLPLRcHFQRRHAKTNSPSAALH--VNYRTPCGRSLRNMEEVFHYLLETECNFLFTDNFSFNT 162
Cdd:cd01397     2 LRVPLE-LGWRRETRIRGLGGRIQgeVAYYAPCGKKLRQYPEVIKYLSKNGISLLSRENFSFSA 64

SET_KMT2B

cd19207

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

563-635

1.09e-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: 1.09e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958681660 563 LLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDYGYEAGTMPEKeILCQC 635
Cdd:cd19207    77 VVDATMHGNAARFINHSCEPNCYSRVIHVEGQKH----IVIFALRKIYRGEELTYDYKFPIEDASNK-LPCNC 144

SET_NSD

cd19173

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

302-340

1.39e-03

Pssm-ID: 380950 [Multi-domain] Cd Length: 142 Bit Score: 39.99 E-value: 1.39e-03

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1958681660 302 VRLQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLSRAT 340
Cdd:cd19173     2 PPTEPFKTGDRGWGLRTKRDIKKGDFVIEYVGELIDEEE 40

SET_SETD8

cd10528

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

565-620

1.48e-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: 1.48e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958681660 565 DASKE-GNVGRFLNHSC-YPNLWVQNVFVETHDRNFplaaFFTNRYVKARTELTWDYG 620
Cdd:cd10528    86 DATKEsGRLGRLINHSKkKPNLKTKLLVIDGVPHLI----LVAKRDIKPGEELLYDYG 139

SET_NSD3

cd19212

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

563-619

2.45e-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: 2.45e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958681660 563 LLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELTWDY 619
Cdd:cd19212    66 IIDAGPKGNYSRFMNHSCNPNCETQKWTVNGDVR----VGLFALCDIPAGMELTFNY 118

ePHD2_KMT2C

cd15697

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

667-761

2.65e-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: 2.65e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 667 NIAAHENCLLYSSGLVECEAHDPFNIAKnfdvssvleKIWNGSTSKCSFCNNEGAIMGCDETSCAKNYHLLCAKEdraiL 746
Cdd:cd15697    24 DLWVHLNCALWSTEVYETQAGALINVEL---------ALRRGLQMKCVFCHKTGATSGCHRLRCTNVYHFTCAIK----A 90

                          90
                  ....*....|....*
gi 1958681660 747 QVGVKRTYKIFCPEH 761
Cdd:cd15697    91 QCMFFKDKTMLCPMH 105

SET_KMT2D

cd19209

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

540-635

2.89e-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: 2.89e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 540 ELASERTKI---PSASLVQLSKESLFLLDASKEGNVGRFLNHSCYPNLWVQNVFVETHDRnfplAAFFTNRYVKARTELT 616
Cdd:cd19209    53 EVANRREKIyeeQNRGIYMFRINNEHVIDATLTGGPARYINHSCAPNCVAEVVTFDKEDK----IIIISSRRIPKGEELT 128

                          90
                  ....*....|....*....
gi 1958681660 617 WDYGYEAGTmPEKEILCQC 635
Cdd:cd19209   129 YDYQFDFED-DQHKIPCHC 146

ePHD2_KMT2D

cd15698

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

671-761

3.51e-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: 38.11 E-value: 3.51e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958681660 671 HENCLLYSSGLVECEAHDPFNiaknfdVSSVLEKiwnGSTSKCSFCNNEGAIMGCDETSCAKNYHLLCAKEDRAILqvgv 750
Cdd:cd15698    28 HLNCALWSTEVYETQGGALMN------VEVALHR---GLLTKCSLCQKTGATNSCNRLRCPNVYHFACAIRAKCMF---- 94

                          90
                  ....*....|.
gi 1958681660 751 KRTYKIFCPEH 761
Cdd:cd15698    95 FKDKTMLCPMH 105

SET

pfam00856

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

313-373

3.53e-03

Pssm-ID: 459965 [Multi-domain] Cd Length: 115 Bit Score: 38.27 E-value: 3.53e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958681660 313 GWGVRCLDDIDKGTFVCIYSGR-LLSRATPEKTNIGESESEQQHTVKNSFSKKRKIEVVCSD 373
Cdd:pfam00856   1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLELRLWGPYLFTLDEDSEYCID 62

SET_ASHR3-like

cd19175

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

303-343

4.57e-03

Pssm-ID: 380952 [Multi-domain] Cd Length: 139 Bit Score: 38.55 E-value: 4.57e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958681660 303 RLQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLSRATPEK 343
Cdd:cd19175     1 KMKLVKTEKCGWGLVADEDINAGEFIIEYVGEVIDDKTCEE 41

PHD5_NSD

cd15568

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

713-761

5.31e-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: 35.77 E-value: 5.31e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958681660 713 CSFCNNEGAIMGCDETSCAKNYHLLCAKEDrailqVGVKRTYkiFCPEH 761
Cdd:cd15568     2 CFRCGDGGDLVLCDFKGCPKVYHLSCLGLE-----KPPGGKW--ICPWH 43

SET_SETD8

cd10528

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

294-343

9.57e-03

Pssm-ID: 380926 [Multi-domain] Cd Length: 141 Bit Score: 37.56 E-value: 9.57e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958681660 294 RVIQHGPRVRLQVFKSEKKGWGVRCLDDIDKGTFVCIYSGRLLSRATPEK 343
Cdd:cd10528     9 ELILSGKEEGLKVIEIDGKGRGVIATRPFEKGDFVVEYHGDLITITEAKK 58

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