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Conserved domains on  [gi|1002819318|ref|NP_001307656|]
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SETDB2-PHF11 protein [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SET super family cl40432
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 210-421 2.29e-94

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: 296.36  E-value: 2.29e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 210 FSFNTYVQLARNYPKQKEVVSDVDISNGVesvpisfcneidsrklpqfkyrktvwpraynltnfssmFTDSCDCSEGCID 289
Cdd:cd10523     1 FSFNTYVQLDRNPQDQQQLVDDFDISNGA--------------------------------------FVDSCDCTDGCID 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 290 ITKCACLQLTARNAKTSPLSSDKITTGYKYKRLQRQIPTGIYECSLLCKCNRQLCQNRVVQHGPQVRLQVFKTEQKGWGV 369
Cdd:cd10523    43 ILKCACLQLTARAFSKSESSPSKGGRGYKYKRLQEPIPSGLYECNVSCKCNRMLCQNRVVQHGLQVRLQVFKTEKKGWGV 122

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002819318 370 RCLDDIDRGTFVCIYSGRLLSRANTEKSYGI------DENGRDENTMKNIFSKKRKLE 421
Cdd:cd10523   123 RCLDDIDKGTFVCIYAGRVLSRARSPTEPLPpklelpSENEVEVVTSWLILSKKRKLR 180
ePHD_PHF11 cd15712
Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain ...
 539-653 2.34e-67

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: 218.61  E-value: 2.34e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 539 CALCPKDVEYNVLYFAQSENIAAHENCLLYSSGLVECEDQDPLNPDRSFDVESVKKEIQRGRKLKCKFCHKRGATVGCDL 618
Cdd:cd15712     1 CAFCPKGEEYSIMYFAQEQNIAAHQNCLLYSSGFVESEEYNPLNLDRRFDVESVLNEIKRGKRLKCNFCRKKGATVGCEE 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1002819318 619 KNCNKNYHFFCAKKDDAVPQSDGVRGIYKLLCQQH 653
Cdd:cd15712    81 RACRRSYHYFCALCDDAAIETDEVRGIYRVFCQKH 115
HMT_MBD cd01395
Methyl-CpG binding domains (MBD) present in putative histone methyltransferases (HMT) such as ...
 152-212 1.63e-25

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: 99.76  E-value: 1.63e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002819318 152 PLQLPIKCHFQRRHAKTNSHSSALHVSYKTPCGRSLRNVEEVFRYLLETeCNFLFTDNFSF 212
Cdd:cd01395     1 PLHTPLLCGFQRMKYRARVGKVKKHVIYKAPCGRSLRNMSEVHRYLRET-CSFLTVDNFSF 60
 
Name Accession Description Interval E-value
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
 210-421 2.29e-94

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: 296.36  E-value: 2.29e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 210 FSFNTYVQLARNYPKQKEVVSDVDISNGVesvpisfcneidsrklpqfkyrktvwpraynltnfssmFTDSCDCSEGCID 289
Cdd:cd10523     1 FSFNTYVQLDRNPQDQQQLVDDFDISNGA--------------------------------------FVDSCDCTDGCID 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 290 ITKCACLQLTARNAKTSPLSSDKITTGYKYKRLQRQIPTGIYECSLLCKCNRQLCQNRVVQHGPQVRLQVFKTEQKGWGV 369
Cdd:cd10523    43 ILKCACLQLTARAFSKSESSPSKGGRGYKYKRLQEPIPSGLYECNVSCKCNRMLCQNRVVQHGLQVRLQVFKTEKKGWGV 122

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002819318 370 RCLDDIDRGTFVCIYSGRLLSRANTEKSYGI------DENGRDENTMKNIFSKKRKLE 421
Cdd:cd10523   123 RCLDDIDKGTFVCIYAGRVLSRARSPTEPLPpklelpSENEVEVVTSWLILSKKRKLR 180
ePHD_PHF11 cd15712
Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain ...
 539-653 2.34e-67

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: 218.61  E-value: 2.34e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 539 CALCPKDVEYNVLYFAQSENIAAHENCLLYSSGLVECEDQDPLNPDRSFDVESVKKEIQRGRKLKCKFCHKRGATVGCDL 618
Cdd:cd15712     1 CAFCPKGEEYSIMYFAQEQNIAAHQNCLLYSSGFVESEEYNPLNLDRRFDVESVLNEIKRGKRLKCNFCRKKGATVGCEE 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1002819318 619 KNCNKNYHFFCAKKDDAVPQSDGVRGIYKLLCQQH 653
Cdd:cd15712    81 RACRRSYHYFCALCDDAAIETDEVRGIYRVFCQKH 115
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
 562-653 7.77e-26

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: 101.64  E-value: 7.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 562 HENCLLYSSGLVECEdqdplNPDRSFDVESVKKEIQRGRKLKCKFCHKR-GATVGCDLKNCNKNYHFFCAKKDDAVPQSD 640
Cdd:pfam13771   1 HVVCALWSPELVQRG-----NDSMGFPIEDIEKIPKRRWKLKCYLCKKKgGACIQCSKKNCRRAFHVTCALEAGLLMQFD 75

                          90
                  ....*....|...
gi 1002819318 641 GVRGIYKLLCQQH 653
Cdd:pfam13771  76 EDNGTFKSYCKKH 88
HMT_MBD cd01395
Methyl-CpG binding domains (MBD) present in putative histone methyltransferases (HMT) such as ...
 152-212 1.63e-25

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: 99.76  E-value: 1.63e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002819318 152 PLQLPIKCHFQRRHAKTNSHSSALHVSYKTPCGRSLRNVEEVFRYLLETeCNFLFTDNFSF 212
Cdd:cd01395     1 PLHTPLLCGFQRMKYRARVGKVKKHVIYKAPCGRSLRNMSEVHRYLRET-CSFLTVDNFSF 60
Pre-SET pfam05033
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ...
 234-347 6.38e-19

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


Pssm-ID: 461530 [Multi-domain]  Cd Length: 99  Bit Score: 82.47  E-value: 6.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 234 ISNGVESVPISFCNEIDS-RKLPQFKYRKTVWPraynLTNFSSMFTDSCDCsEGCIDiTKCACLQLTarnaktsplsSDK 312
Cdd:pfam05033   1 ISKGKENVPIPVVNEVDDePPPPDFTYITSYIY----PKEFLLIIPQGCDC-GDCSS-EKCSCAQLN----------GGE 64

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1002819318 313 ITTGYKYKRLQR-QIPTGIYECSLLCKCNRQlCQNR 347
Cdd:pfam05033  65 FRFPYDKDGLLVpESKPPIYECNPLCGCPPS-CPNR 99
MBD smart00391
Methyl-CpG binding domain; Methyl-CpG binding domain, also known as the TAM (TTF-IIP5, ARBP, ...
 150-227 8.39e-12

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: 61.62  E-value: 8.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318  150 ENPLQLPIKCHFQRRHA--KTNSHSSALHVSYKTPCGRSLRNVEEVFRYLLETECNFLFTDNFSFNTYVqlaRNYPKQKE 227
Cdd:smart00391   1 GDPLRLPLPCGWRRETKqrKSGRSAGKFDVYYISPCGKKLRSKSELARYLHKNGDLSLDLECFDFNATV---PVGPKFTP 77
PreSET smart00468
N-terminal to some SET domains; A Cys-rich putative Zn2+-binding domain that occurs N-terminal ...
 233-338 7.06e-10

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: 56.66  E-value: 7.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318  233 DISNGVESVPISFCNEIDSRKLP-QFKYRKTVWPRAYNLTNFSSMFTDSCDCSEGCIDITKCACLQLTARNAKTSplssd 311
Cdd:smart00468   3 DISNGKENVPVPLVNEVDEDPPPpDFEYISEYIYGQGVPIDRSPSPLVGCSCSGDCSSSNKCECARKNGGEFAYE----- 77

                           90       100
                   ....*....|....*....|....*..
gi 1002819318  312 kittgyKYKRLQRQIPTGIYECSLLCK 338
Cdd:smart00468  78 ------LNGGLRLKRKPLIYECNSRCS 98
MBD pfam01429
Methyl-CpG binding domain; The Methyl-CpG binding domain (MBD) binds to DNA that contains one ...
 149-216 2.44e-08

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: 51.59  E-value: 2.44e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 149 GENPLQLPIKCHFQR--RHAKTNSHSSALHVSYKTPCGRSLRNVEEVFRYLLETECNFLFTDNFSFNTYV 216
Cdd:pfam01429   3 RKREDRLPLPPGWRReeRQRKSGSKAGKVDVFYYSPTGKKLRSKSEVARYLEANGGTSPKLEDFSFTVRS 72
 
Name Accession Description Interval E-value
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
 210-421 2.29e-94

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: 296.36  E-value: 2.29e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 210 FSFNTYVQLARNYPKQKEVVSDVDISNGVesvpisfcneidsrklpqfkyrktvwpraynltnfssmFTDSCDCSEGCID 289
Cdd:cd10523     1 FSFNTYVQLDRNPQDQQQLVDDFDISNGA--------------------------------------FVDSCDCTDGCID 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 290 ITKCACLQLTARNAKTSPLSSDKITTGYKYKRLQRQIPTGIYECSLLCKCNRQLCQNRVVQHGPQVRLQVFKTEQKGWGV 369
Cdd:cd10523    43 ILKCACLQLTARAFSKSESSPSKGGRGYKYKRLQEPIPSGLYECNVSCKCNRMLCQNRVVQHGLQVRLQVFKTEKKGWGV 122

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002819318 370 RCLDDIDRGTFVCIYSGRLLSRANTEKSYGI------DENGRDENTMKNIFSKKRKLE 421
Cdd:cd10523   123 RCLDDIDKGTFVCIYAGRVLSRARSPTEPLPpklelpSENEVEVVTSWLILSKKRKLR 180
SET_SETDB cd10541
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...
 277-424 1.18e-75

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: 245.53  E-value: 1.18e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 277 FTDSCDCSEGCIDITKCACLQLTARNAKTSPLSSDKITTGYKYKRLQRQIPTGIYECSLLCKCNRQLCQNRVVQHGPQVR 356
Cdd:cd10541    14 FLVGCDCTDGCRDKSKCACHQLTIQATACTPGGQDNPTAGYQYKRLEECLPTGVYECNKLCKCDPNMCQNRLVQHGLQVR 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002819318 357 LQVFKTEQKGWGVRCLDDIDRGTFVCIYSGRLLSRANTEKSYGIDengrdentMKNIFSKKRKLEVAC 424
Cdd:cd10541    94 LQLFKTQNKGWGIRCLDDIAKGTFVCIYAGKILTDDFADKEGLEM--------GDEYFANLDHIEESC 153
ePHD_PHF11 cd15712
Extended PHD finger found in PHD finger protein 11 (PHF11); The extended plant homeodomain ...
 539-653 2.34e-67

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: 218.61  E-value: 2.34e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 539 CALCPKDVEYNVLYFAQSENIAAHENCLLYSSGLVECEDQDPLNPDRSFDVESVKKEIQRGRKLKCKFCHKRGATVGCDL 618
Cdd:cd15712     1 CAFCPKGEEYSIMYFAQEQNIAAHQNCLLYSSGFVESEEYNPLNLDRRFDVESVLNEIKRGKRLKCNFCRKKGATVGCEE 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1002819318 619 KNCNKNYHFFCAKKDDAVPQSDGVRGIYKLLCQQH 653
Cdd:cd15712    81 RACRRSYHYFCALCDDAAIETDEVRGIYRVFCQKH 115
SET_SETDB1 cd10517
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
 233-402 1.57e-58

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: 201.36  E-value: 1.57e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 233 DISNGVESVPISFCNEIDSRKLPQFKYRKTVWPRAYNLTNFSSMFTDSCDCSEGCIDITKCACLQLTARNAKTSPLSSDK 312
Cdd:cd10517     8 DISYGKEGVPIPCVNEIDNSSPPYVEYSKERIPGKGVNINLDPDFLVGCDCTDGCRDKSKCACQQLTIEATAATPGGQIN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 313 ITTGYKYKRLQRQIPTGIYECSLLCKCNRQlCQNRVVQHGPQVRLQVFKTEQKGWGVRCLDDIDRGTFVCIYSGRLLSR- 391
Cdd:cd10517    88 PSAGYQYRRLMEKLPTGVYECNSRCKCDKR-CYNRVVQNGLQVRLQVFKTEKKGWGIRCLDDIPKGSFVCIYAGQILTEd 166

                         170
                  ....*....|..
gi 1002819318 392 -ANTEKSYGIDE 402
Cdd:cd10517   167 eANEEGLQYGDE 178
ePHD_PHF6_like cd15673
Extended PHD finger found in PHD finger protein 6 (PHF6) and PHD finger protein 11 (PHF11); ...
 539-653 1.02e-51

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: 176.04  E-value: 1.02e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 539 CALCPKDVEYNVLYF--AQSENIAAHENCLLYSSGLVECEDQDPlNPDRSFDVESVKKEIQRGRKLKCKFCHKRGATVGC 616
Cdd:cd15673     1 CGFCKSGEENKETGGklASGEKIAAHHNCMLFSSGLVQYVSPNE-NDFGGFDIEDVKKEIKRGRKLKCNLCKKTGATIGC 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1002819318 617 DLKNCNKNYHFFCAKKDDAVPQSDGVRGIYKLLCQQH 653
Cdd:cd15673    80 DVKQCKKTYHYHCAKKDDAKIIERNSQGIYRVYCKNH 116
SET_SETDB-like cd10538
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
 256-407 7.65e-33

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: 126.33  E-value: 7.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 256 QFKYRKTVWPRAYNLTNFSsmFTDSCDCSEGCIDiTKCACLQLTARNaktsplssdkitTGYKYKRLQR--QIPTGIYEC 333
Cdd:cd10538     4 TYIKDNIVGKNVQPFSNII--DSVGCKCKDDCLD-SKCACAAESDGI------------FAYTKNGLLRlnNSPPPIFEC 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002819318 334 SLLCKCNRQlCQNRVVQHGPQVRLQVFKTEQKGWGVRCLDDIDRGTFVCIYSGRLLSRANTEKSYGIDENGRDE 407
Cdd:cd10538    69 NSKCSCDDD-CKNRVVQRGLQARLQVFRTSKKGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRGKIYDKSGGS 141
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
 280-402 5.25e-28

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: 112.88  E-value: 5.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 280 SCDCSEGCIDITK-CAClqlTARNAKTSPLSsdkittgyKYKRLQRQIPTgIYECSLLCKCNRQlCQNRVVQHGPQVRLQ 358
Cdd:cd10545    23 GCDCKNRCTDGASdCAC---VKKNGGEIPYN--------FNGRLIRAKPA-IYECGPLCKCPPS-CYNRVTQKGLRYRLE 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1002819318 359 VFKTEQKGWGVRCLDDIDRGTFVCIYSGRLLSRANTEKSYGIDE 402
Cdd:cd10545    90 VFKTAERGWGVRSWDSIPAGSFICEYVGELLDTSEADTRSGNDD 133
ePHD1_PHF6 cd15710
Extended PHD finger 1 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
 539-653 4.17e-27

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: 106.58  E-value: 4.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 539 CALCP--KDVEYNVLYFAQSENIAAHENCLLYSSGLVECE-DQDPLNpdrSFDVESVKKEIQRGRKLKCKFCHKRGATVG 615
Cdd:cd15710     1 CGFCRsnREKECGQLLISENQKVAAHHKCMLFSSALVSSHsDSENLG---GFSIEDVQKEIKRGTKLMCSLCHCPGATIG 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1002819318 616 CDLKNCNKNYHFFCAKKDDAVPQSDGVRGIYKLLCQQH 653
Cdd:cd15710    78 CDVKTCHRTYHYYCALHDKAQIRENPSQGIYMIYCRKH 115
zf-HC5HC2H pfam13771
PHD-like zinc-binding domain; The members of this family are annotated as containing PHD ...
 562-653 7.77e-26

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: 101.64  E-value: 7.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 562 HENCLLYSSGLVECEdqdplNPDRSFDVESVKKEIQRGRKLKCKFCHKR-GATVGCDLKNCNKNYHFFCAKKDDAVPQSD 640
Cdd:pfam13771   1 HVVCALWSPELVQRG-----NDSMGFPIEDIEKIPKRRWKLKCYLCKKKgGACIQCSKKNCRRAFHVTCALEAGLLMQFD 75

                          90
                  ....*....|...
gi 1002819318 641 GVRGIYKLLCQQH 653
Cdd:pfam13771  76 EDNGTFKSYCKKH 88
HMT_MBD cd01395
Methyl-CpG binding domains (MBD) present in putative histone methyltransferases (HMT) such as ...
 152-212 1.63e-25

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: 99.76  E-value: 1.63e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002819318 152 PLQLPIKCHFQRRHAKTNSHSSALHVSYKTPCGRSLRNVEEVFRYLLETeCNFLFTDNFSF 212
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 ...
 281-405 1.79e-24

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


Pssm-ID: 380940 [Multi-domain]  Cd Length: 245  Bit Score: 103.14  E-value: 1.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 281 CDCSEGCIDITKCACLQLtarnaktsplsSDKITTGYKYKRLQRQIPTGIYECSLLCKCNrQLCQNRVVQHGPQVRLQVF 360
Cdd:cd10542    25 CECTEDCHNNNPTCCPAE-----------SGVKFAYDKQGRLRLPPGTPIYECNSRCKCG-PDCPNRVVQRGRKVPLCIF 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1002819318 361 KTEQ-KGWGVRCLDDIDRGTFVCIYSGRLLSRANTE---KSYgiDENGR 405
Cdd:cd10542    93 RTSNgRGWGVKTLEDIKKGTFVMEYVGEIITSEEAErrgKIY--DANGR 139
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
 255-390 3.11e-24

SET domain (including pre-SET and post-SET domains) found in SET domain and mariner transposase fusion protein (SETMAR) and similar proteins; SETMAR (also termed metnase) is a DNA-binding protein that is indirectly recruited to sites of DNA damage through protein-protein interactions. It has a sequence-specific DNA-binding activity recognizing the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element and displays a DNA nicking and end joining activity. SETMAR also acts as a histone-lysine N-methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3. It specifically mediates dimethylation of H3 'Lys-36' at sites of DNA double-strand break and may recruit proteins required for efficient DSB repair through non-homologous end-joining.


Pssm-ID: 380942 [Multi-domain]  Cd Length: 254  Bit Score: 102.76  E-value: 3.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 255 PQFKYRKTVWPRAYNLTNFSSMFTDSCDCSEGCIDITKCACLQLTARNAKTSPLSSDKITtgyKYKRLqrqiptgIYECS 334
Cdd:cd10544     1 PDFQYTPENVPGPGADTDPNEITFPGCDCKTSSCEPETCSCLRKYGPNYDDDGCLLDFDG---KYSGP-------VFECN 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002819318 335 LLCKCNRQlCQNRVVQHGPQVRLQVFKTEQKGWGVRCLDDIDRGTFVCIYSGRLLS 390
Cdd:cd10544    71 SMCKCSES-CQNRVVQNGLQFKLQVFKTPKKGWGLRTLEFIPKGRFVCEYAGEVIG 125
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 280-390 5.98e-23

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: 98.18  E-value: 5.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 280 SCDCSEGCiDITKCACLQLTARNA--KTSPLSSDkittgykykrLQRQIPTGIYECSLLCKCNRQlCQNRVVQHGPQVRL 357
Cdd:cd10543    26 TCSCRDDC-SSDNCVCGRLSVRCWydKEGRLLPD----------FNKLDPPLIFECNRACSCWRN-CRNRVVQNGIRYRL 93

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1002819318 358 QVFKTEQKGWGVRCLDDIDRGTFVCIYSGRLLS 390
Cdd:cd10543    94 QLFRTRGMGWGVRALQDIPKGTFVCEYIGELIS 126
ePHD_PHF7_G2E3_like cd15669
Extended PHD finger found in PHD finger protein 7 (PHF7) and G2/M phase-specific E3 ...
 539-653 6.26e-21

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: 88.46  E-value: 6.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 539 CALCPKDVEYNVLY--FAQSENIAAHENCLLYSSGLVECEDQDPLNpdRSFDVESVKKEIQRGRKLKCKFCHKRGATVGC 616
Cdd:cd15669     1 CVLCGRSDDDPDKYgeKLQKDGICAHYFCLLFSSGLPQRGEDNEGI--YGFLPEDIRKEVRRASRLRCFYCKKKGASIGC 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1002819318 617 DLKNCNKNYHFFCAKKDDAVPQsdgVRGIYKLLCQQH 653
Cdd:cd15669    79 AVKGCRRSFHFPCGLENGCVTQ---FFGEYRSFCWEH 112
ePHD2_PHF6 cd15711
Extended PHD finger 2 found in PHD finger protein 6 (PHF6); The extended plant homeodomain ...
 539-653 1.06e-20

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: 88.22  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 539 CALCPKDVEYN----VLYFAQSENIAAHENCLLYSSGLVECEDQDPLNPDrSFDVESVKKEIQRGRKLKCKFCHKRGATV 614
Cdd:cd15711     1 CGFCHAGEEENetrgKLHIFNAKKAAAHYKCMLFSSGTVQLTTTSRAEFG-DFDIKTVIQEIKRGKRMKCTLCSQLGATI 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1002819318 615 GCDLKNCNKNYHFFCAKKDDAVPQSDGVRGIYKLLCQQH 653
Cdd:cd15711    80 GCEIKACVKTYHYHCGVQDKAKYIENMSRGIYKLYCKNH 118
ePHD_KMT2A_like cd15664
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A) and 2B (KMT2B); The ...
 539-653 1.07e-20

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: 87.85  E-value: 1.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 539 CALC-------PKDvEYNVLYFAQSENIaaHENCLLYSSGLVECEDQDPLNpdrsfdvesVKKEIQRGRKLKCKFCHKRG 611
Cdd:cd15664     1 CALCgvygddePND-AGRLLYCGQDEWV--HINCALWSAEVFEEDDGSLQN---------VHSAVSRGRMMKCELCGKPG 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1002819318 612 ATVGCDLKNCNKNYHFFCAKKDDAVPQSDGvrgiyKLLCQQH 653
Cdd:cd15664    69 ATVGCCLKSCPANYHFMCARKAECVFQDDK-----KVFCPAH 105
ePHD cd15571
Extended plant homeodomain (PHD) finger, characterized by Cys2HisCys5HisCys2His; PHD finger is ...
 539-653 1.66e-19

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: 84.56  E-value: 1.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 539 CALCPKDVEYNVLYFAQ---SENIAAHENCLLYSSGLVECEDQDPlnpdrsfDVESVKKEIQRGRKLKCKFCHKR-GATV 614
Cdd:cd15571     1 CALCPRSGGALKGGGALkttSDGLWVHVVCALWSPEVYFDDGTLL-------EVEGVSKIPKRRKKLKCSICGKRgGACI 73

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1002819318 615 GCDLKNCNKNYHFFCAKKDDAVPQSDGVRGIYKLLCQQH 653
Cdd:cd15571    74 QCSYPGCPRSFHVSCAIRAGCLFEFEDGPGNFVVYCPKH 112
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 281-406 4.39e-19

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: 87.30  E-value: 4.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 281 CDCSEGCIDiTKCACLQLTAR-----NAKTSPlssdkittgyKYKRLQrqiPTGIYECSLLCKCNRQlCQNRVVQHGPQV 355
Cdd:cd10535    27 CVCIDDCSS-SNCMCGQLSMRcwydkDGRLLP----------EFNMAE---PPLIFECNHACSCWRN-CRNRVVQNGLRA 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002819318 356 RLQVFKTEQKGWGVRCLDDIDRGTFVCIYSGRLLSRANT----EKSYGIDENGRD 406
Cdd:cd10535    92 RLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEAdvreEDSYLFDLDNKD 146
Pre-SET pfam05033
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ...
 234-347 6.38e-19

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


Pssm-ID: 461530 [Multi-domain]  Cd Length: 99  Bit Score: 82.47  E-value: 6.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 234 ISNGVESVPISFCNEIDS-RKLPQFKYRKTVWPraynLTNFSSMFTDSCDCsEGCIDiTKCACLQLTarnaktsplsSDK 312
Cdd:pfam05033   1 ISKGKENVPIPVVNEVDDePPPPDFTYITSYIY----PKEFLLIIPQGCDC-GDCSS-EKCSCAQLN----------GGE 64

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1002819318 313 ITTGYKYKRLQR-QIPTGIYECSLLCKCNRQlCQNR 347
Cdd:pfam05033  65 FRFPYDKDGLLVpESKPPIYECNPLCGCPPS-CPNR 99
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 281-406 2.30e-18

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: 85.07  E-value: 2.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 281 CDCSEGCIDiTKCACLQLTARnaktspLSSDKitTGYKYKRLQRQIPTGIYECSLLCKCNRQlCQNRVVQHGPQVRLQVF 360
Cdd:cd10533    27 CTCVDDCSS-SNCLCGQLSIR------CWYDK--DGRLLQEFNKIEPPLIFECNQACSCWRN-CKNRVVQSGIKVRLQLY 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002819318 361 KTEQKGWGVRCLDDIDRGTFVCIYSGRLLSRANT----EKSYGIDENGRD 406
Cdd:cd10533    97 RTAKMGWGVRALQTIPQGTFICEYVGELISDAEAdvreDDSYLFDLDNKD 146
MBD cd00122
MeCP2, MBD1, MBD2, MBD3, MBD4, CLLD8-like, and BAZ2A-like proteins constitute a family of ...
 152-212 6.77e-18

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: 78.13  E-value: 6.77e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002819318 152 PLQLPIKCHFQRRHAKTNSHS-SALHVSYKTPCGRSLRNVEEVFRYLLETECNFLFTDNFSF 212
Cdd:cd00122     1 PLRDPLPPGWKRELVIRKSGSaGKGDVYYYSPCGKKLRSKPEVARYLEKTGPSSLDLENFSF 62
SET_SUV39H_Clr4-like cd20073
SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 ...
 249-403 9.99e-18

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: 83.78  E-value: 9.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 249 IDSRKLPQFKYRKTVWPRaynltnfSSMFTDSCDCS--EGCI--DITKCACLQltarnaktsplSSDKITTGY-KYKRLQ 323
Cdd:cd20073     1 IDFEFITSYRYGLGIEPP-------DPLFISGCSCSklGGCDlnNPGSCQCLE-----------DSNEKSFAYdEYGRVR 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 324 RQIPTGIYECSLLCKCNRQlCQNRVVQHGPQVRLQVFKTEQKGWGVRCLDDIDRGTFVCIYSGRLLSRANTEKSYGIDEN 403
Cdd:cd20073    63 ANTGSIIYECNENCDCGIN-CPNRVVQRGRKLPLEIFKTKHKGWGLRCPRFIKAGTFIGVYLGEVITQSEAEIRGKKYDN 141
ePHD_KMT2A cd15693
Extended PHD finger found in histone-lysine N-methyltransferase 2A (KMT2A); The extended plant ...
 537-653 1.20e-17

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: 79.27  E-value: 1.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 537 RTCALCPK--DVEYN----VLYFAQSEniAAHENCLLYSSGLVECEDQDplnpdrsfdVESVKKEIQRGRKLKCKFCHKR 610
Cdd:cd15693     1 RQCALCLKygDDSANdagrLLYIGQNE--WTHVNCALWSAEVFEDDDGS---------LKNVHMAVIRGKQLRCEFCQKP 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1002819318 611 GATVGCDLKNCNKNYHFFCAKKDDAVPQSDGvrgiyKLLCQQH 653
Cdd:cd15693    70 GATVGCCLTSCTSNYHFMCSRAKNCVFLEDK-----KVYCQRH 107
SET_SUV39H_DIM5-like cd19473
SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...
 275-397 4.41e-16

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: 79.28  E-value: 4.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 275 SMFTDSCDCSEG--CIDITkCACLQLTARnaKTSPLSSDKI----TTGYKYKRLQRQIPTG---IYECSLLCKCNrQLCQ 345
Cdd:cd19473    20 EEFRSGCECTDDedCMYSG-CLCLQDVDP--DDDRDPGKKKnayhSSGAKKGCLRGHMLNSrlpIYECHEGCACS-DDCP 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 346 NRVVQHGPQVRLQVFKTEQ-KGWGVRCLDDIDRGTFVCIYSGRLLS-------RANTEKS 397
Cdd:cd19473    96 NRVVERGRKVPLQIFRTSDgRGWGVRSTVDIKRGQFVDCYVGEIITpeeaqrrRDAATIA 155
ePHD_KMT2B cd15694
Extended PHD finger found in histone-lysine N-methyltransferase 2B (KMT2B); The extended plant ...
 539-653 1.61e-14

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: 70.07  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 539 CALC-------PKDVEyNVLYFAQSEniAAHENCLLYSSGLVECEDQDplnpdrsfdVESVKKEIQRGRKLKCKFCHKRG 611
Cdd:cd15694     1 CALClkygdadSKDAG-RLLYIGQNE--WTHVNCAIWSAEVFEENDGS---------LKNVHAAVARGRQMRCEHCQKIG 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1002819318 612 ATVGCDLKNCNKNYHFFCAKKDDAVPQSDGvrgiyKLLCQQH 653
Cdd:cd15694    69 ATVGCCLSACLSNFHFMCARASRCCFQDDK-----KVFCQKH 105
ePHD2_KMT2C_like cd15666
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
 562-653 5.71e-12

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: 62.70  E-value: 5.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 562 HENCLLYSSGLVECEDQDPLNPDRSfdvesvkkeIQRGRKLKCKFCHKRGATVGCDLKNCNKNYHFFCAKKDDAVPQSDg 641
Cdd:cd15666    28 HLNCALWSYEVYETQNGALMNVEEA---------LRRALTTTCSHCGRTGATVPCFKPRCANVYHLPCAIKDGCMFFKD- 97

                          90
                  ....*....|..
gi 1002819318 642 vRGIYkllCQQH 653
Cdd:cd15666    98 -KTML---CPSH 105
MBD smart00391
Methyl-CpG binding domain; Methyl-CpG binding domain, also known as the TAM (TTF-IIP5, ARBP, ...
 150-227 8.39e-12

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: 61.62  E-value: 8.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318  150 ENPLQLPIKCHFQRRHA--KTNSHSSALHVSYKTPCGRSLRNVEEVFRYLLETECNFLFTDNFSFNTYVqlaRNYPKQKE 227
Cdd:smart00391   1 GDPLRLPLPCGWRRETKqrKSGRSAGKFDVYYISPCGKKLRSKSELARYLHKNGDLSLDLECFDFNATV---PVGPKFTP 77
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 320-396 8.03e-11

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


Pssm-ID: 380930 [Multi-domain]  Cd Length: 243  Bit Score: 62.99  E-value: 8.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 320 KRLQRQIPTG--IYECSLLCKCNRQlCQNRVVQHGPQVRLQVFKTEQ-KGWGVRCLDDIDRGTFVCIYSGRLLSRANTEK 396
Cdd:cd10532    48 EHGQLKIPPGtpIYECNSRCKCGPD-CPNRVVQKGTQYSLCIFRTSNgRGWGVKTLQKIKKNSFVMEYVGEVITSEEAER 126
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 330-396 6.29e-10

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


Pssm-ID: 380923 [Multi-domain]  Cd Length: 255  Bit Score: 60.68  E-value: 6.29e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002819318 330 IYECSLLCKCNRQlCQNRVVQHGPQVRLQVFKTEQ-KGWGVRCLDDIDRGTFVCIYSGRLLSRANTEK 396
Cdd:cd10525    62 IYECNSRCRCGPD-CPNRVVQKGIQYDLCIFRTDNgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAER 128
PreSET smart00468
N-terminal to some SET domains; A Cys-rich putative Zn2+-binding domain that occurs N-terminal ...
 233-338 7.06e-10

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: 56.66  E-value: 7.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318  233 DISNGVESVPISFCNEIDSRKLP-QFKYRKTVWPRAYNLTNFSSMFTDSCDCSEGCIDITKCACLQLTARNAKTSplssd 311
Cdd:smart00468   3 DISNGKENVPVPLVNEVDEDPPPpDFEYISEYIYGQGVPIDRSPSPLVGCSCSGDCSSSNKCECARKNGGEFAYE----- 77

                           90       100
                   ....*....|....*....|....*..
gi 1002819318  312 kittgyKYKRLQRQIPTGIYECSLLCK 338
Cdd:smart00468  78 ------LNGGLRLKRKPLIYECNSRCS 98
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 355-416 2.38e-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: 53.11  E-value: 2.38e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002819318  355 VRLQVFKTEQKGWGVRCLDDIDRGTFVCIYSGRLLSRANTEKSYGI-DENGRDENTMKNIFSK 416
Cdd:smart00317   1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAyDTDGAKAFYLFDIDSD 63
MBD pfam01429
Methyl-CpG binding domain; The Methyl-CpG binding domain (MBD) binds to DNA that contains one ...
 149-216 2.44e-08

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: 51.59  E-value: 2.44e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 149 GENPLQLPIKCHFQR--RHAKTNSHSSALHVSYKTPCGRSLRNVEEVFRYLLETECNFLFTDNFSFNTYV 216
Cdd:pfam01429   3 RKREDRLPLPPGWRReeRQRKSGSKAGKVDVFYYSPTGKKLRSKSEVARYLEANGGTSPKLEDFSFTVRS 72
ePHD2_KMT2C cd15697
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
 558-632 1.32e-07

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: 50.43  E-value: 1.32e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002819318 558 NIAAHENCLLYSSGLVECEDQDPLNPDRSfdvesvkkeIQRGRKLKCKFCHKRGATVGCDLKNCNKNYHFFCAKK 632
Cdd:cd15697    24 DLWVHLNCALWSTEVYETQAGALINVELA---------LRRGLQMKCVFCHKTGATSGCHRLRCTNVYHFTCAIK 89
ePHD1_KMT2C_like cd15665
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C) and 2D (KMT2D); ...
 561-630 1.42e-07

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: 50.01  E-value: 1.42e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 561 AHENCLLYSSGLVECEDQDplnpdrsfdVESVKKEIQRGRKLKCKFCHKRGATVGCDLKNCNKNYHFFCA 630
Cdd:cd15665    11 AHHCCAAWSEGVCQTEDGA---------LENVDKAVAKALSQKCSFCLRYGASISCRMPSCSKSFHFPCA 71
ePHD_TCF20 cd15699
Extended PHD finger (ePHD) found in transcription factor 20 (TCF-20); The extended plant ...
 539-653 3.44e-07

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: 49.14  E-value: 3.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 539 CALCPKDVEYNVL--YFAQSENIAAHENCLLYSSGLVecedqdpLNPDRSFdveSVKKEIQRGRKLKCKFCHKRGATVGC 616
Cdd:cd15699     1 CCLCGKWANYRNLgdLFGPFYEFWVHEGCILWANGIY-------LVCGRLY---GLQEALDIAREMKCSHCQEAGATLGC 70

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1002819318 617 DLKNCNKNYHFFCAKKDDAVPQSDGvrgiYKLLCQQH 653
Cdd:cd15699    71 YNKGCSFRYHYPCAIDADCLLNEEN----FSVRCPKH 103
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
 357-398 1.13e-06

SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ASH1L (EC 2.1.1.43; also termed absent small and homeotic disks protein 1 homolog, KMT2H, or lysine N-methyltransferase 2H) acts as histone-lysine N-methyltransferase that specifically methylates 'Lys-36' of histone H3 (H3K36me). It plays important roles in development; heterozygous mutation of ASH1L is associated with severe intellectual disability (ID) and multiple congenital anomaly (MCA).


Pssm-ID: 380951 [Multi-domain]  Cd Length: 141  Bit Score: 48.83  E-value: 1.13e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1002819318 357 LQVFKTEQKGWGVRCLDDIDRGTFVCIYSGRLLS----RANTEKSY 398
Cdd:cd19174     2 LERFRTEDKGWGVRTKEPIKAGQFIIEYVGEVVSeqefRRRMIEQY 47
ePHD_RAI1_like cd15668
Extended PHD finger found in retinoic acid-induced protein 1 (RAI1), transcription factor 20 ...
 600-653 1.32e-06

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: 47.30  E-value: 1.32e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002819318 600 RKLKCKFCHKRGATVGCDLKNCNKNYHFFCAKKDDAVPQSDGvrgiYKLLCQQH 653
Cdd:cd15668    54 KQSVCSSCQQTGATIGCLHKGCKAKYHYPCAVESGCQLDEEN----FSLLCPKH 103
ePHD2_KMT2D cd15698
Extended PHD finger 2 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...
 562-653 5.24e-06

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: 45.81  E-value: 5.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 562 HENCLLYSSGLVECEDQDPLNpdrsfdvesVKKEIQRGRKLKCKFCHKRGATVGCDLKNCNKNYHFFCAKKDDAVPQSDG 641
Cdd:cd15698    28 HLNCALWSTEVYETQGGALMN---------VEVALHRGLLTKCSLCQKTGATNSCNRLRCPNVYHFACAIRAKCMFFKDK 98

                          90
                  ....*....|..
gi 1002819318 642 VrgiykLLCQQH 653
Cdd:cd15698    99 T-----MLCPMH 105
ePHD1_KMT2C cd15696
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2C (KMT2C); The extended ...
 561-630 6.23e-06

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: 45.32  E-value: 6.23e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 561 AHENCLLYSSGLVECEDQDPLNpdrsfdvesVKKEIQRGRKLKCKFCHKRGATVGCDLKNCNKNYHFFCA 630
Cdd:cd15696    11 AHLRCAEWSLGVCQGEEQLLVN---------VDKAVVSGSTERCAFCKHLGATIKCCEEKCTQMYHYPCA 71
ePHD_RAI1 cd15700
Extended PHD finger (ePHD) found in retinoic acid-induced protein 1 (RAI1); The extended plant ...
 539-631 6.83e-06

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: 45.64  E-value: 6.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 539 CALCPKDVEYNVL------YFAQSeniAAHENCLLYSSGLVecedqdpLNPDRSFdveSVKKEIQRGRKLKCKFCHKRGA 612
Cdd:cd15700     1 CCLCRNPANYKDLgdlcgpYYPEH---WVHEACAVWTTGVY-------LVAGKLF---GLQEAVQKAADAKCSSCQGAGA 67

                          90
                  ....*....|....*....
gi 1002819318 613 TVGCDLKNCNKNYHFFCAK 631
Cdd:cd15700    68 TVGCCHKGCTQSYHYICAV 86
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
 357-390 1.55e-05

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: 45.32  E-value: 1.55e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1002819318 357 LQVFKTEQKGWGVRCLDDIDRGTFVCIYSGRLLS 390
Cdd:cd10531     2 LELFRTEKKGWGVKAKEDIQKGEFIIEYVGEVID 35
HAT_MBD cd01397
Methyl-CpG binding domains (MBD) present in putative chromatin remodelling factor such as ...
 153-214 1.14e-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: 41.24  E-value: 1.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002819318 153 LQLPIKcHFQRRHAKTNSHSSALH--VSYKTPCGRSLRNVEEVFRYLLETECNFLFTDNFSFNT 214
Cdd:cd01397     2 LRVPLE-LGWRRETRIRGLGGRIQgeVAYYAPCGKKLRQYPEVIKYLSKNGISLLSRENFSFSA 64
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
 356-390 1.66e-04

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: 42.57  E-value: 1.66e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1002819318 356 RLQVFKTEQKGWGVRCLDDIDRGTFVCIYSGRLLS 390
Cdd:cd19172     3 KVEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLD 37
ePHD1_KMT2D cd15695
Extended PHD finger 1 found in histone-lysine N-methyltransferase 2D (KMT2D); The extended ...
 561-653 4.59e-04

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: 39.90  E-value: 4.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 561 AHENCLLYSSGLVECEDQDPLNPDRSfdvesvkkeIQRGRKLKCKFCHKRGATVGCDLKNCNKNYHFFCAkkddAVPQSD 640
Cdd:cd15695    11 VHHWCAAWSAGVKQHEGDGLIGVDKA---------VFSGISQKCEHCKRLGATIQCHAEGCPRFYHFPCA----AASGSF 77

                          90
                  ....*....|...
gi 1002819318 641 GVRGIYKLLCQQH 653
Cdd:cd15695    78 QSMKTLLLLCPEH 90
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
 353-389 4.79e-04

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: 41.07  E-value: 4.79e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1002819318 353 PQVrlQVFKTEQKGWGVRCLDDIDRGTFVCIYSGRLL 389
Cdd:cd19210     2 PEV--EIFRTLGRGWGLRCKTDIKKGEFVNEYVGELI 36
SET_SETD8 cd10528
SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2. ...
 347-449 8.12e-04

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: 40.64  E-value: 8.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002819318 347 RVVQHGPQVRLQVFKTEQKGWGVRCLDDIDRGTFVCIYSGRLLSRANT---EKSYgidenGRDENTMKNIFSKKRKLEVA 423
Cdd:cd10528     9 ELILSGKEEGLKVIEIDGKGRGVIATRPFEKGDFVVEYHGDLITITEAkkrEALY-----AKDPSTGCYMYYFQYKGKTY 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 1002819318 424 CSDCEVEVLPLG-LETHPRTA---KTEKCP 449
Cdd:cd10528    84 CVDATKESGRLGrLINHSKKKpnlKTKLLV 113
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 366-426 9.11e-04

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: 39.81  E-value: 9.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002819318 366 GWGVRCLDDIDRGTFVCIYSGR-LLSRANTEKSYGIDENGRDENTMKNIFSKKRKLEVACSD 426
Cdd:pfam00856   1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLELRLWGPYLFTLDEDSEYCID 62
SET_NSD cd19173
SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...
 355-392 9.18e-04

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: 40.38  E-value: 9.18e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1002819318 355 VRLQVFKTEQKGWGVRCLDDIDRGTFVCIYSGRLLSRA 392
Cdd:cd19173     2 PPTEPFKTGDRGWGLRTKRDIKKGDFVIEYVGELIDEE 39
ePHD_JMJD2B cd15714
Extended PHD finger found in Jumonji domain-containing protein 2B (JMJD2B); The extended plant ...
 601-653 2.49e-03

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


Pssm-ID: 277184  Cd Length: 110  Bit Score: 38.38  E-value: 2.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002819318 601 KLKCKFCHKR-----GATVGCDLKNCNKNYHFFCAKKDDAVPQSDGVRGIYKLLCQQH 653
Cdd:cd15714    53 KLKCVYCRKRmkkvsGACIQCSYDHCSTSFHVTCAHAAGVVMEPDDWPYVVSITCFKH 110
SET_ASHR3-like cd19175
SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...
 356-396 6.89e-03

SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 (ASHR3) and similar proteins; This family includes Arabidopsis thaliana ASH1-related protein 3 (ASHR3, also termed protein SET DOMAIN GROUP 4 or protein stamen loss), ASH1 homolog 3 (ASHH3, also termed protein SET DOMAIN GROUP 7) and homolog 4 (ASHH4, also termed protein SET DOMAIN GROUP 24). They all function as histone-lysine N-methyltransferases (EC 2.1.1.43).


Pssm-ID: 380952 [Multi-domain]  Cd Length: 139  Bit Score: 37.78  E-value: 6.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1002819318 356 RLQVFKTEQKGWGVRCLDDIDRGTFVCIYSGRLLSRANTEK 396
Cdd:cd19175     1 KMKLVKTEKCGWGLVADEDINAGEFIIEYVGEVIDDKTCEE 41
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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