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Conserved domains on  [gi|15236295|ref|NP_193082|]
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SU(VAR)3-9 homolog 9 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
 409-638 9.51e-131

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: 384.06  E-value: 9.51e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 409 LYYEYLAQTSFPPGLFvqQSGNASGCDCVNGCGSG---CLCEAKNSGEIAYDYNGTLIRQKPLIHECGSACQCPPSCRNR 485
Cdd:cd10545   1 SGFTYTVKLIIPPGVS--LPVPSTGCDCKNRCTDGasdCACVKKNGGEIPYNFNGRLIRAKPAIYECGPLCKCPPSCYNR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 486 VTQKGLRNRLEVFRSLETGWGVRSLDVLHAGAFICEYAGVALTREQANILTMNGDTLVYPARFSSARWEDWGDLSQVL-A 564
Cdd:cd10545  79 VTQKGLRYRLEVFKTAERGWGVRSWDSIPAGSFICEYVGELLDTSEADTRSGNDDYLFDIDNRQTNRGWDGGQRLDVGmS 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15236295 565 DFERPSYPDIPPVDFAMDVSKMRNVACYISHSTDPNVIVQFVLHDHNSLMFPRVMLFAAENIPPMTELSLDYGV 638
Cdd:cd10545 159 DGERSSAEDEESSEFTIDAGSFGNVARFINHSCSPNLFVQCVLYDHNDLRLPRVMLFAADNIPPLQELTYDYGY 232
SRA smart00466
SET and RING finger associated domain; Domain of unknown function in SET domain containing ...
 200-356 2.88e-87

SET and RING finger associated domain; Domain of unknown function in SET domain containing proteins and in Deinococcus radiodurans DRA1533.


:

Pssm-ID: 197742  Cd Length: 155  Bit Score: 269.24  E-value: 2.88e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295    200 DKRIVGSIPGVQVGDIFFFRFELCVMGLHGHPQSGIDFLTgslSSNGEPIATSVIVSGGYEDDDDQGDVIMYTGQGGQDR 279
Cdd:smart00466   1 MKRIFGPVPGVEVGDIFFYRVELCLVGLHRPTQAGIDGLE---SDEGEPGATSVVSSGGYEDDTDDGDVLIYTGQGGRDM 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15236295    280 LGRQAEHQRLEGGNLAMERSMYYGIEVRVIRGLK-YENEVSSRVYVYDGLFRIVDSWFDVGKSGFGVFKYRLERIEGQ 356
Cdd:smart00466  78 THGQPEDQKLERGNLALEASCRKGIPVRVVRGMKgYSKYAPGKGYIYDGLYRIVDYWREVGKSGFLVFKFKLVRIPGQ 155
 
Name Accession Description Interval E-value
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
 409-638 9.51e-131

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: 384.06  E-value: 9.51e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 409 LYYEYLAQTSFPPGLFvqQSGNASGCDCVNGCGSG---CLCEAKNSGEIAYDYNGTLIRQKPLIHECGSACQCPPSCRNR 485
Cdd:cd10545   1 SGFTYTVKLIIPPGVS--LPVPSTGCDCKNRCTDGasdCACVKKNGGEIPYNFNGRLIRAKPAIYECGPLCKCPPSCYNR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 486 VTQKGLRNRLEVFRSLETGWGVRSLDVLHAGAFICEYAGVALTREQANILTMNGDTLVYPARFSSARWEDWGDLSQVL-A 564
Cdd:cd10545  79 VTQKGLRYRLEVFKTAERGWGVRSWDSIPAGSFICEYVGELLDTSEADTRSGNDDYLFDIDNRQTNRGWDGGQRLDVGmS 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15236295 565 DFERPSYPDIPPVDFAMDVSKMRNVACYISHSTDPNVIVQFVLHDHNSLMFPRVMLFAAENIPPMTELSLDYGV 638
Cdd:cd10545 159 DGERSSAEDEESSEFTIDAGSFGNVARFINHSCSPNLFVQCVLYDHNDLRLPRVMLFAADNIPPLQELTYDYGY 232
SRA smart00466
SET and RING finger associated domain; Domain of unknown function in SET domain containing ...
 200-356 2.88e-87

SET and RING finger associated domain; Domain of unknown function in SET domain containing proteins and in Deinococcus radiodurans DRA1533.


Pssm-ID: 197742  Cd Length: 155  Bit Score: 269.24  E-value: 2.88e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295    200 DKRIVGSIPGVQVGDIFFFRFELCVMGLHGHPQSGIDFLTgslSSNGEPIATSVIVSGGYEDDDDQGDVIMYTGQGGQDR 279
Cdd:smart00466   1 MKRIFGPVPGVEVGDIFFYRVELCLVGLHRPTQAGIDGLE---SDEGEPGATSVVSSGGYEDDTDDGDVLIYTGQGGRDM 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15236295    280 LGRQAEHQRLEGGNLAMERSMYYGIEVRVIRGLK-YENEVSSRVYVYDGLFRIVDSWFDVGKSGFGVFKYRLERIEGQ 356
Cdd:smart00466  78 THGQPEDQKLERGNLALEASCRKGIPVRVVRGMKgYSKYAPGKGYIYDGLYRIVDYWREVGKSGFLVFKFKLVRIPGQ 155
SAD_SRA pfam02182
SAD/SRA domain; The domain goes by several names including SAD, SRA and YDG. It adopts a beta ...
 203-353 4.70e-68

SAD/SRA domain; The domain goes by several names including SAD, SRA and YDG. It adopts a beta barrel, modified PUA-like, fold that is widely present in eukaryotic chromatin proteins and in bacteria. Versions of this domain are known to bind hemi-methylated CpG dinucleotides and also other 5mC containing dinucleotides. The domain binds DNA by flipping out the methylated cytosine base from the DNA double helix.The conserved tyrosine and aspartate residues and a glycine rich patch are critical for recognition of the flipped out base. Mammalian UHRF1 that contains this domain plays an important role in maintenance of methylation at CpG dinucleotides by recruiting DNMT1 to hemimethylated sites associated with replication forks. The SAD/SRA domain has been combined with other domains involved in the ubiquitin pathway on multiple occasions and such proteins link recognition of DNA methylation to chromatin-protein ubiquitination. The domain is also found in species that lack DNA methylation, such as certain apicomplexans, suggestive of other DNA-binding modes or functions. A highly derived and distinct version of the domain is also found in fungi where it is fused to AlkB-type 2OGFeDO domains. In bacteria, the domain is usually fused or associated with restriction endonucleases, many of which target methylated or hemi-methylated DNA.


Pssm-ID: 460476  Cd Length: 146  Bit Score: 218.57  E-value: 4.70e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295   203 IVGSIPGVQVGDIFFFRFELCVMGLHGHPQSGIDFLtgslSSNGepiATSVIVSGGYEDDDDQGDVIMYTGQGGQD-RLG 281
Cdd:pfam02182   1 RFGHVPGVEVGDIFSSRAELCVVGLHRPTQAGIDGM----KSEG---AYSIVLSGGYEDDEDNGDVLIYTGSGGRDnTKK 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15236295   282 RQAEHQRLEGGNLAMERSMYYGIEVRVIRGLKYENEVSSRVYVYDGLFRIVDSWFDVGKSGFGVFKYRLERI 353
Cdd:pfam02182  74 KQSADQKLERGNLALANSCETGNPVRVIRGSKRDSYPPKKGYRYDGLYKVEKYWEEKGKSGFLVFKFKLRRL 145
PreSET smart00468
N-terminal to some SET domains; A Cys-rich putative Zn2+-binding domain that occurs N-terminal ...
 384-477 3.05e-31

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: 117.13  E-value: 3.05e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295    384 NFDISNGKENVPVYLFNDIDSDQEPLYYEYLAQTSFPPG-LFVQQSGNASGCDCVNGCGSG--CLCEAKNSGEIAY-DYN 459
Cdd:smart00468   1 CLDISNGKENVPVPLVNEVDEDPPPPDFEYISEYIYGQGvPIDRSPSPLVGCSCSGDCSSSnkCECARKNGGEFAYeLNG 80

                           90
                   ....*....|....*...
gi 15236295    460 GTLIRQKPLIHECGSACQ 477
Cdd:smart00468  81 GLRLKRKPLIYECNSRCS 98
Pre-SET pfam05033
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ...
 387-485 1.80e-29

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: 112.13  E-value: 1.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295   387 ISNGKENVPVYLFNDIDSDQEPLYYEYLAQTSFPPGLFVQqsgNASGCDCVNgCGS-GCLCEAKNSGE--IAYDYNGTLI 463
Cdd:pfam05033   1 ISKGKENVPIPVVNEVDDEPPPPDFTYITSYIYPKEFLLI---IPQGCDCGD-CSSeKCSCAQLNGGEfrFPYDKDGLLV 76

                          90       100
                  ....*....|....*....|...
gi 15236295   464 -RQKPLIHECGSACQCPPSCRNR 485
Cdd:pfam05033  77 pESKPPIYECNPLCGCPPSCPNR 99
 
Name Accession Description Interval E-value
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
 409-638 9.51e-131

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: 384.06  E-value: 9.51e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 409 LYYEYLAQTSFPPGLFvqQSGNASGCDCVNGCGSG---CLCEAKNSGEIAYDYNGTLIRQKPLIHECGSACQCPPSCRNR 485
Cdd:cd10545   1 SGFTYTVKLIIPPGVS--LPVPSTGCDCKNRCTDGasdCACVKKNGGEIPYNFNGRLIRAKPAIYECGPLCKCPPSCYNR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 486 VTQKGLRNRLEVFRSLETGWGVRSLDVLHAGAFICEYAGVALTREQANILTMNGDTLVYPARFSSARWEDWGDLSQVL-A 564
Cdd:cd10545  79 VTQKGLRYRLEVFKTAERGWGVRSWDSIPAGSFICEYVGELLDTSEADTRSGNDDYLFDIDNRQTNRGWDGGQRLDVGmS 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15236295 565 DFERPSYPDIPPVDFAMDVSKMRNVACYISHSTDPNVIVQFVLHDHNSLMFPRVMLFAAENIPPMTELSLDYGV 638
Cdd:cd10545 159 DGERSSAEDEESSEFTIDAGSFGNVARFINHSCSPNLFVQCVLYDHNDLRLPRVMLFAADNIPPLQELTYDYGY 232
SRA smart00466
SET and RING finger associated domain; Domain of unknown function in SET domain containing ...
 200-356 2.88e-87

SET and RING finger associated domain; Domain of unknown function in SET domain containing proteins and in Deinococcus radiodurans DRA1533.


Pssm-ID: 197742  Cd Length: 155  Bit Score: 269.24  E-value: 2.88e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295    200 DKRIVGSIPGVQVGDIFFFRFELCVMGLHGHPQSGIDFLTgslSSNGEPIATSVIVSGGYEDDDDQGDVIMYTGQGGQDR 279
Cdd:smart00466   1 MKRIFGPVPGVEVGDIFFYRVELCLVGLHRPTQAGIDGLE---SDEGEPGATSVVSSGGYEDDTDDGDVLIYTGQGGRDM 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15236295    280 LGRQAEHQRLEGGNLAMERSMYYGIEVRVIRGLK-YENEVSSRVYVYDGLFRIVDSWFDVGKSGFGVFKYRLERIEGQ 356
Cdd:smart00466  78 THGQPEDQKLERGNLALEASCRKGIPVRVVRGMKgYSKYAPGKGYIYDGLYRIVDYWREVGKSGFLVFKFKLVRIPGQ 155
SAD_SRA pfam02182
SAD/SRA domain; The domain goes by several names including SAD, SRA and YDG. It adopts a beta ...
 203-353 4.70e-68

SAD/SRA domain; The domain goes by several names including SAD, SRA and YDG. It adopts a beta barrel, modified PUA-like, fold that is widely present in eukaryotic chromatin proteins and in bacteria. Versions of this domain are known to bind hemi-methylated CpG dinucleotides and also other 5mC containing dinucleotides. The domain binds DNA by flipping out the methylated cytosine base from the DNA double helix.The conserved tyrosine and aspartate residues and a glycine rich patch are critical for recognition of the flipped out base. Mammalian UHRF1 that contains this domain plays an important role in maintenance of methylation at CpG dinucleotides by recruiting DNMT1 to hemimethylated sites associated with replication forks. The SAD/SRA domain has been combined with other domains involved in the ubiquitin pathway on multiple occasions and such proteins link recognition of DNA methylation to chromatin-protein ubiquitination. The domain is also found in species that lack DNA methylation, such as certain apicomplexans, suggestive of other DNA-binding modes or functions. A highly derived and distinct version of the domain is also found in fungi where it is fused to AlkB-type 2OGFeDO domains. In bacteria, the domain is usually fused or associated with restriction endonucleases, many of which target methylated or hemi-methylated DNA.


Pssm-ID: 460476  Cd Length: 146  Bit Score: 218.57  E-value: 4.70e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295   203 IVGSIPGVQVGDIFFFRFELCVMGLHGHPQSGIDFLtgslSSNGepiATSVIVSGGYEDDDDQGDVIMYTGQGGQD-RLG 281
Cdd:pfam02182   1 RFGHVPGVEVGDIFSSRAELCVVGLHRPTQAGIDGM----KSEG---AYSIVLSGGYEDDEDNGDVLIYTGSGGRDnTKK 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15236295   282 RQAEHQRLEGGNLAMERSMYYGIEVRVIRGLKYENEVSSRVYVYDGLFRIVDSWFDVGKSGFGVFKYRLERI 353
Cdd:pfam02182  74 KQSADQKLERGNLALANSCETGNPVRVIRGSKRDSYPPKKGYRYDGLYKVEKYWEEKGKSGFLVFKFKLRRL 145
SET_SETDB-like cd10538
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
 433-637 1.17e-55

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: 188.35  E-value: 1.17e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 433 GCDCVNGC-GSGCLCEAKNSGEIAYDYNG--TLIRQKPLIHECGSACQCPPSCRNRVTQKGLRNRLEVFRSLETGWGVRS 509
Cdd:cd10538  26 GCKCKDDClDSKCACAAESDGIFAYTKNGllRLNNSPPPIFECNSKCSCDDDCKNRVVQRGLQARLQVFRTSKKGWGVRS 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 510 LDVLHAGAFICEYAGVALTREQAN----ILTMNGDTlvYparfssarwedwgdlsqvLADFERPSYPDIPPVDFAMDVSK 585
Cdd:cd10538 106 LEFIPKGSFVCEYVGEVITTSEADrrgkIYDKSGGS--Y------------------LFDLDEFSDSDGDGEELCVDATF 165

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15236295 586 MRNVACYISHSTDPNVIVQFVLHDHNSLMFPRVMLFAAENIPPMTELSLDYG 637
Cdd:cd10538 166 CGNVSRFINHSCDPNLFPFNVVIDHDDLRYPRIALFATRDILPGEELTFDYG 217
SET_SETDB1 cd10517
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
 378-637 2.85e-43

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: 157.07  E-value: 2.85e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 378 RPRGYINfDISNGKENVPVYLFNDIDSDQEPlYYEYLAQTSFPPGLFVQQSGN-ASGCDCVNGC--------------GS 442
Cdd:cd10517   1 KPYYYIC-DISYGKEGVPIPCVNEIDNSSPP-YVEYSKERIPGKGVNINLDPDfLVGCDCTDGCrdkskcacqqltieAT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 443 GCLCEAKNSGEIAYDYNgtliR-QKPL---IHECGSACQCPPSCRNRVTQKGLRNRLEVFRSLETGWGVRSLDVLHAGAF 518
Cdd:cd10517  79 AATPGGQINPSAGYQYR----RlMEKLptgVYECNSRCKCDKRCYNRVVQNGLQVRLQVFKTEKKGWGIRCLDDIPKGSF 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 519 ICEYAGVALTREQANI-LTMNGDTlvYPARF---SSARWEDWGDLSQVladfERPSYpdippvdfAMDVSKMRNVACYIS 594
Cdd:cd10517 155 VCIYAGQILTEDEANEeGLQYGDE--YFAELdyiEVVEKLKEGYESDV----EEHCY--------IIDAKSEGNLGRYLN 220

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15236295 595 HSTDPNVIVQFVLHDHNSLMFPRVMLFAAENIPPMTELSLDYG 637
Cdd:cd10517 221 HSCSPNLFVQNVFVDTHDLRFPWVAFFASRYIRAGTELTWDYN 263
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 432-636 1.29e-37

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: 140.12  E-value: 1.29e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 432 SGCDCVNGC---GSGClCEAKNSGEIAYDYNGTLI--RQKPlIHECGSACQCPPSCRNRVTQKGLRNRLEVFR-SLETGW 505
Cdd:cd10542  23 VGCECTEDChnnNPTC-CPAESGVKFAYDKQGRLRlpPGTP-IYECNSRCKCGPDCPNRVVQRGRKVPLCIFRtSNGRGW 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 506 GVRSLDVLHAGAFICEYAGVALTREQAN----ILTMNGDTLVYparfssarwedwgDLsqvlaDFERpsypDIPPvdFAM 581
Cdd:cd10542 101 GVKTLEDIKKGTFVMEYVGEIITSEEAErrgkIYDANGRTYLF-------------DL-----DYND----DDCE--YTV 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15236295 582 DVSKMRNVACYISHSTDPNVIVQFVLHDHNSLMFPRVMLFAAENIPPMTELSLDY 636
Cdd:cd10542 157 DAAYYGNISHFINHSCDPNLAVYAVWINHLDPRLPRIAFFAKRDIKAGEELTFDY 211
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 411-637 1.08e-35

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: 134.39  E-value: 1.08e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 411 YEYLAQTSFPPGLFVQQS-GNASGCDCVNGCGS-GCLCeAKNSGEIAYDYNGTLIR-----QKPLIHECGSACQCPPSCR 483
Cdd:cd10543   3 FLYVTENCETSPLNIDRNiTSLQTCSCRDDCSSdNCVC-GRLSVRCWYDKEGRLLPdfnklDPPLIFECNRACSCWRNCR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 484 NRVTQKGLRNRLEVFRSLETGWGVRSLDVLHAGAFICEYAGVALTREQANiltmngdtlvyparfssARWEDwgdlsQVL 563
Cdd:cd10543  82 NRVVQNGIRYRLQLFRTRGMGWGVRALQDIPKGTFVCEYIGELISDSEAD-----------------SREDD-----SYL 139

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15236295 564 ADFERPSYPdippvDFAMDVSKMRNVACYISHSTDPNVIVQFVLHDHNSLMFPRVMLFAAENIPPMTELSLDYG 637
Cdd:cd10543 140 FDLDNKDGE-----TYCIDARRYGNISRFINHLCEPNLIPVRVFVEHQDLRFPRIAFFASRDIKAGEELGFDYG 208
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
 432-637 1.42e-31

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: 123.56  E-value: 1.42e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 432 SGCDCVNG-CGS-GCLCEAKNSGEiaYDYNGTLI-----RQKPLIhECGSACQCPPSCRNRVTQKGLRNRLEVFRSLETG 504
Cdd:cd10544  25 PGCDCKTSsCEPeTCSCLRKYGPN--YDDDGCLLdfdgkYSGPVF-ECNSMCKCSESCQNRVVQNGLQFKLQVFKTPKKG 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 505 WGVRSLDVLHAGAFICEYAGVALTREQA-------NILTMNGdTLVYPARFSSarwedwgdlSQVLADFERPSYpdippv 577
Cdd:cd10544 102 WGLRTLEFIPKGRFVCEYAGEVIGFEEArrrtksqTKGDMNY-IIVLREHLSS---------GKVLETFVDPTY------ 165

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 578 dfamdvskMRNVACYISHSTDPNVIVQFVLHDHnslMFPRVMLFAAENIPPMTELSLDYG 637
Cdd:cd10544 166 --------IGNIGRFLNHSCEPNLFMVPVRVDS---MVPKLALFAARDIVAGEELSFDYS 214
PreSET smart00468
N-terminal to some SET domains; A Cys-rich putative Zn2+-binding domain that occurs N-terminal ...
 384-477 3.05e-31

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: 117.13  E-value: 3.05e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295    384 NFDISNGKENVPVYLFNDIDSDQEPLYYEYLAQTSFPPG-LFVQQSGNASGCDCVNGCGSG--CLCEAKNSGEIAY-DYN 459
Cdd:smart00468   1 CLDISNGKENVPVPLVNEVDEDPPPPDFEYISEYIYGQGvPIDRSPSPLVGCSCSGDCSSSnkCECARKNGGEFAYeLNG 80

                           90
                   ....*....|....*...
gi 15236295    460 GTLIRQKPLIHECGSACQ 477
Cdd:smart00468  81 GLRLKRKPLIYECNSRCS 98
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 411-637 1.25e-30

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: 120.12  E-value: 1.25e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 411 YEYLAQTSFPPGLFVQQS-GNASGCDCVNGCGSG-CLCeAKNSGEIAYDYNGTLIRQ-----KPLIHECGSACQCPPSCR 483
Cdd:cd10533   3 YKYISENCETSTMNIDRNiTHLQHCTCVDDCSSSnCLC-GQLSIRCWYDKDGRLLQEfnkiePPLIFECNQACSCWRNCK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 484 NRVTQKGLRNRLEVFRSLETGWGVRSLDVLHAGAFICEYAGVALTREQANIltMNGDTLVYparfssarwedwgDLSQVL 563
Cdd:cd10533  82 NRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADV--REDDSYLF-------------DLDNKD 146

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15236295 564 ADFerpsypdippvdFAMDVSKMRNVACYISHSTDPNVIVQFVLHDHNSLMFPRVMLFAAENIPPMTELSLDYG 637
Cdd:cd10533 147 GEV------------YCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYG 208
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
 434-637 4.76e-30

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: 118.50  E-value: 4.76e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 434 CDCVNGCGSG-CLCeAKNSGEIAYDYNGTLI-----RQKPLIHECGSACQCPPSCRNRVTQKGLRNRLEVFRSLETGWGV 507
Cdd:cd10535  27 CVCIDDCSSSnCMC-GQLSMRCWYDKDGRLLpefnmAEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTRDMGWGV 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 508 RSLDVLHAGAFICEYAGVALTREQANIltmngdtlvyparfssaRWEDwgdlsQVLADFERPSYPdippvDFAMDVSKMR 587
Cdd:cd10535 106 RSLQDIPPGTFVCEYVGELISDSEADV-----------------REED-----SYLFDLDNKDGE-----VYCIDARFYG 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15236295 588 NVACYISHSTDPNVIVQFVLHDHNSLMFPRVMLFAAENIPPMTELSLDYG 637
Cdd:cd10535 159 NVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYG 208
Pre-SET pfam05033
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ...
 387-485 1.80e-29

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: 112.13  E-value: 1.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295   387 ISNGKENVPVYLFNDIDSDQEPLYYEYLAQTSFPPGLFVQqsgNASGCDCVNgCGS-GCLCEAKNSGE--IAYDYNGTLI 463
Cdd:pfam05033   1 ISKGKENVPIPVVNEVDDEPPPPDFTYITSYIYPKEFLLI---IPQGCDCGD-CSSeKCSCAQLNGGEfrFPYDKDGLLV 76

                          90       100
                  ....*....|....*....|...
gi 15236295   464 -RQKPLIHECGSACQCPPSCRNR 485
Cdd:pfam05033  77 pESKPPIYECNPLCGCPPSCPNR 99
SET_SETDB cd10541
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...
 433-637 5.12e-27

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: 109.94  E-value: 5.12e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 433 GCDCVNGC--GSGCLCE------------AKNSGEIAYDYNgTLIRQKPL-IHECGSACQCPPS-CRNRVTQKGLRNRLE 496
Cdd:cd10541  17 GCDCTDGCrdKSKCACHqltiqatactpgGQDNPTAGYQYK-RLEECLPTgVYECNKLCKCDPNmCQNRLVQHGLQVRLQ 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 497 VFRSLETGWGVRSLDVLHAGAFICEYAGVALTREQANIltmngdtlvyparfssarwEDWGDLSQVLADFERpsypdIPP 576
Cdd:cd10541  96 LFKTQNKGWGIRCLDDIAKGTFVCIYAGKILTDDFADK-------------------EGLEMGDEYFANLDH-----IEE 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15236295 577 VDFAMDVSKMRNVACYISHSTDPNVIVQFVLHDHNSLMFPRVMLFAAENIPPMTELSLDYG 637
Cdd:cd10541 152 SCYIIDAKLEGNLGRYLNHSCSPNLFVQNVFVDTHDLRFPWVAFFASKRIKAGTELTWDYN 212
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 411-636 4.92e-26

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: 107.28  E-value: 4.92e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 411 YEYLAQTSFPPGLFVQQsGNASGCDCVNgCGSGCLCEAKNSGEIAYDYNGTL-IRQKPLIHECGSACQCPPSCRNRVTQK 489
Cdd:cd10532   3 FYYINEYKPAPGINLDN-EATVGCDCSD-CFFGKCCPAEAGVLFAYNEHGQLkIPPGTPIYECNSRCKCGPDCPNRVVQK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 490 GLRNRLEVFRSLE-TGWGVRSLDVLHAGAFICEYAGVALTREQAN----ILTMNGDTLVYparfssarwedwgDLsqvla 564
Cdd:cd10532  81 GTQYSLCIFRTSNgRGWGVKTLQKIKKNSFVMEYVGEVITSEEAErrgqFYDSKGITYLF-------------DL----- 142

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15236295 565 DFERPsypdippvDFAMDVSKMRNVACYISHSTDPNVIVQFVLHDHNSLMFPRVMLFAAENIPPMTELSLDY 636
Cdd:cd10532 143 DYESD--------EFTVDAARYGNVSHFVNHSCDPNLQVFNVFIDNLDTRLPRIALFSTRTIKAGEELTFDY 206
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
 434-637 9.86e-26

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: 106.84  E-value: 9.86e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 434 CDCVNGCGSGCLC--------------EAKNSGEIAYDYNgTLIRQKPL-IHECGSACQCPPS-CRNRVTQKGLRNRLEV 497
Cdd:cd10523  34 CDCTDGCIDILKCaclqltarafskseSSPSKGGRGYKYK-RLQEPIPSgLYECNVSCKCNRMlCQNRVVQHGLQVRLQV 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 498 FRSLETGWGVRSLDVLHAGAFICEYAGVALTReqanilTMNGDTLVYPARFSSARWEDwgdlsqvladfERPSYPDIPPV 577
Cdd:cd10523 113 FKTEKKGWGVRCLDDIDKGTFVCIYAGRVLSR------ARSPTEPLPPKLELPSENEV-----------EVVTSWLILSK 175

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15236295 578 D-------FAMDVSKMRNVACYISHSTDPNVIVQFVLHDHNSLMFPRVMLFAAENIPPMTELSLDYG 637
Cdd:cd10523 176 KrklrenvCFLDASKEGNVGRFLNHSCCPNLFVQNVFVDTHDKNFPWVAFFTNRVVKAGTELTWDYS 242
SET_SUV39H_Clr4-like cd20073
SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 ...
 411-636 1.00e-25

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: 106.89  E-value: 1.00e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 411 YEYLAQTSFPPGLFVQQSGNASGCDC--VNGCG----SGCLC-EAKNSGEIAYDYNGTL-IRQKPLIHECGSACQCPPSC 482
Cdd:cd20073   3 FEFITSYRYGLGIEPPDPLFISGCSCskLGGCDlnnpGSCQClEDSNEKSFAYDEYGRVrANTGSIIYECNENCDCGINC 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 483 RNRVTQKGLRNRLEVFRSLETGWGVRSLDVLHAGAFICEYAGVALTREQANILTMNgdtlvyparfssarWEDWGdlsqV 562
Cdd:cd20073  83 PNRVVQRGRKLPLEIFKTKHKGWGLRCPRFIKAGTFIGVYLGEVITQSEAEIRGKK--------------YDNVG----V 144

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15236295 563 LADFERPSYPDIPPVDFAMDVSKMRNVACYISHSTDPNVIVQFVLHDHNSLMFPRVMLFAAENIPPMTELSLDY 636
Cdd:cd20073 145 TYLFDLDLFEDQVDEYYTVDAQYCGDVTRFINHSCDPNLAIYSVLRDKSDSKIYDLAFFAIKDIPALEELTFDY 218
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 493-644 1.52e-23

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: 96.25  E-value: 1.52e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295    493 NRLEVFRSLETGWGVRSLDVLHAGAFICEYAGVALTREQANILTMNGDTlvyparfssarwedWGDLSQVLadFErpsyp 572
Cdd:smart00317   1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDT--------------DGAKAFYL--FD----- 59

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15236295    573 diPPVDFAMDVSKMRNVACYISHSTDPNVIVQFVLHDHNSlmfpRVMLFAAENIPPMTELSLDYGvVDDWNA 644
Cdd:smart00317  60 --IDSDLCIDARRKGNLARFINHSCEPNCELLFVEVNGDD----RIVIFALRDIKPGEELTIDYG-SDYANE 124
SET_SUV39H_DIM5-like cd19473
SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...
 432-641 2.08e-23

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: 100.47  E-value: 2.08e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 432 SGCDCVNG--C-GSGCLC-------EAKNSGEIAYDYNGT-----LIRQKPL-----IHECGSACQCPPSCRNRVTQKGL 491
Cdd:cd19473  24 SGCECTDDedCmYSGCLClqdvdpdDDRDPGKKKNAYHSSgakkgCLRGHMLnsrlpIYECHEGCACSDDCPNRVVERGR 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 492 RNRLEVFR-SLETGWGVRSLDVLHAGAFICEYAGVALTREQANiltmngdtlvyparfssaRWEDWGDLSQ-------VL 563
Cdd:cd19473 104 KVPLQIFRtSDGRGWGVRSTVDIKRGQFVDCYVGEIITPEEAQ------------------RRRDAATIAQrkdvylfAL 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 564 ADFERPSYPDI----PPvdFAMDVSKMRNVACYISHSTDPNVIVQFVLHDHNSLMFPRVMLFAAENIPPMTELSLDY--G 637
Cdd:cd19473 166 DKFSDPDSLDPrlrgDP--YEIDGEFMSGPTRFINHSCDPNLRIFARVGDHADKHIHDLAFFAIKDIPRGTELTFDYvdG 243


                ....
gi 15236295 638 VVDD 641
Cdd:cd19473 244 VTGL 247
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 431-641 1.49e-22

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: 97.27  E-value: 1.49e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 431 ASGC---DCVNGCGSGClCEAKNSGEIAYDYNGTL-IRQKPLIHECGSACQCPPSCRNRVTQKGLRNRLEVFRSLE-TGW 505
Cdd:cd10525  21 AVGCecqDCLSQPVGGC-CPGASKHRFAYNEQGQVkVRPGLPIYECNSRCRCGPDCPNRVVQKGIQYDLCIFRTDNgRGW 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 506 GVRSLDVLHAGAFICEYAGVALTREQAN----ILTMNGDTLVYparfssarwedwgDLSQVladferpsyPDIppvdFAM 581
Cdd:cd10525 100 GVRTLEKIRKNSFVMEYVGEIITSEEAErrgqIYDRQGATYLF-------------DLDYV---------EDV----YTV 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 582 DVSKMRNVACYISHSTDPNVIVQFVLHDHNSLMFPRVMLFAAENIPPMTELSLDYGVVDD 641
Cdd:cd10525 154 DAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIALFATRTIRAGEELTFDYNMQVD 213
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
 495-649 3.02e-15

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: 72.67  E-value: 3.02e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 495 LEVFRSLETGWGVRSLDVLHAGAFICEYAGvaltrEqaniltmngdtlVYPARFSSARwedwgdLSQVLADFERPSYPDI 574
Cdd:cd10531   2 LELFRTEKKGWGVKAKEDIQKGEFIIEYVG-----E------------VIDKKEFKER------LDEYEELGKSNFYILS 58

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15236295 575 PPVDFAMDVSKMRNVACYISHSTDPNVIVQFVlhdhNSLMFPRVMLFAAENIPPMTELSLDYGVVdDWNAKLAIC 649
Cdd:cd10531  59 LSDDVVIDATRKGNLSRFINHSCEPNCETQKW----IVNGEYRIGIFALRDIPAGEELTFDYNFV-NYNEAKQVC 128
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 504-637 5.21e-14

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: 68.70  E-value: 5.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295   504 GWGVRSLDVLHAGAFICEYAGVALTREQANILTMNGDTLVYPARFSSARWEDWGDLSQVLADferpsypdippvdfaMDV 583
Cdd:pfam00856   1 GRGLFATEDIPKGEFIGEYVEVLLITKEEADKRELLYYDKLELRLWGPYLFTLDEDSEYCID---------------ARA 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15236295   584 SKMRNVACYISHSTDPNVIVQFVLHDHNslmfPRVMLFAAENIPPMTELSLDYG 637
Cdd:pfam00856  66 LYYGNWARFINHSCDPNCEVRVVYVNGG----PRIVIFALRDIKPGEELTIDYG 115
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
 495-636 6.82e-11

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: 60.38  E-value: 6.82e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 495 LEVFRSLETGWGVRSLDVLHAGAFICEYAGVALTREQaniltmngdtlvyparFSSARWEDW-GDLSQVLADFERpsypd 573
Cdd:cd19174   2 LERFRTEDKGWGVRTKEPIKAGQFIIEYVGEVVSEQE----------------FRRRMIEQYhNHSHHYCLNLDS----- 60

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15236295 574 ippvDFAMDVSKMRNVACYISHSTDPNVIVQfvLHDHNSLmfPRVMLFAAENIPPMTELSLDY 636
Cdd:cd19174  61 ----GMVIDGYRMGNEARFVNHSCDPNCEMQ--KWSVNGV--YRIGLFALKDIPAGEELTYDY 115
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
 504-637 1.51e-07

SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar proteins; The family includes EZH1 and EZH2. EZH1 (EC 2.1.1.43; also termed ENX-2, or histone-lysine N-methyltransferase EZH1) is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. EZH2 (EC 2.1.1.43; also termed lysine N-methyltransferase 6, ENX-1, or histone-lysine N-methyltransferase EZH2) is a catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Both, EZH1 and EZH2, can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively.


Pssm-ID: 380917  Cd Length: 117  Bit Score: 50.32  E-value: 1.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 504 GWGVRSLDVLHAGAFICEYAGVALTREQANiltMNGdtLVYPARFSSarwedwgdlsqVLADFERpsypdippvDFAMDV 583
Cdd:cd10519  12 GWGLFLKEPIKKDEFIGEYTGELISQDEAD---RRG--KIYDKYNSS-----------YLFNLND---------QFVVDA 66

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15236295 584 SKMRNVACYISHSTDPNVI--VQFVLHDHnslmfpRVMLFAAENIPPMTELSLDYG 637
Cdd:cd10519  67 TRKGNKIRFANHSSNPNCYakVMMVNGDH------RIGIFAKRDIEAGEELFFDYG 116
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
 495-636 1.13e-06

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: 48.38  E-value: 1.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 495 LEVFRSLETGWGVRSLDVLHAGAFICEYAGVALTREQANiltmngdtlvypARFSSARWEDWGDLSQVLADFERpsypdi 574
Cdd:cd19210   4 VEIFRTLGRGWGLRCKTDIKKGEFVNEYVGELIDEEECR------------ARIRYAQEHDITNFYMLTLDKDR------ 65

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15236295 575 ppvdfAMDVSKMRNVACYISHSTDPNVIVQFVLHDHNSlmfpRVMLFAAENIPPMTELSLDY 636
Cdd:cd19210  66 -----IIDAGPKGNYARFMNHCCQPNCETQKWTVNGDT----RVGLFALCDIKAGTELTFNY 118
SET_SETD1-like cd10518
SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...
 483-636 2.56e-06

SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), histone-lysine N-methyltransferases (KMT2A/KMT2B/KMT2C/KMT2D) and similar proteins; This family includes SET domain-containing protein 1A (SETD1A), 1B (SETD1B), as well as histone-lysine N-methyltransferase 2A (KMT2A), 2B (KMT2B), 2C (KMT2C), 2D (KMT2D). These proteins are histone-lysine N-methyltransferases (EC 2.1.1.43) that specifically methylate 'Lys-4' of histone H3 (H3K4me).


Pssm-ID: 380916  Cd Length: 150  Bit Score: 47.59  E-value: 2.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 483 RNRVTQKGLRNRLEVFRSLETGWGVRSLDVLHAGAFICEYAGVaLTReqaniltmngdtlvyparfssarwedwgdlsQV 562
Cdd:cd10518   4 RFRQLRSRLKERLRVGKSGIHGWGLFAKRPIAAGEMVIEYVGE-VIR-------------------------------PI 51

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 563 LADFERPSYPDIPPVDFAM---------DVSKMRNVACYISHSTDPNVIVQFVLHDHNSlmfpRVMLFAAENIPPMTELS 633
Cdd:cd10518  52 VADKREKRYDEEGGGGTYMfridedlviDATKKGNIARFINHSCDPNCYAKIITVDGEK----HIVIFAKRDIAPGEELT 127


                ...
gi 15236295 634 LDY 636
Cdd:cd10518 128 YDY 130
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
 506-636 2.91e-06

SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar proteins; SETD5 is a probable transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. KMT2E (also termed inactive lysine N-methyltransferase 2E or myeloid/lymphoid or mixed-lineage leukemia protein 5 (MLL5)) associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription. The family also includes Saccharomyces cerevisiae SET domain-containing proteins, SET3 and SET4, and Schizosaccharomyces pombe SET3. Most of these family members contain a post-SET domain which harbors a zinc-binding site.


Pssm-ID: 380927  Cd Length: 127  Bit Score: 46.88  E-value: 2.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 506 GVRSLDVLHAGAFICEYAGVALTREQaniltmngdtlvYPARFSSarwedwgdlsqvladFERPS-----YPDIPPVDFA 580
Cdd:cd10529  18 GLVATEDISPGEPILEYKGEVSLRSE------------FKEDNGF---------------FKRPSpfvffYDGFEGLPLC 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15236295 581 MDVSKMRNVACYISHSTDPNVIVQFVLHDHNSLmfpRVMLFAAENIPPMTELSLDY 636
Cdd:cd10529  71 VDARKYGNEARFIRRSCRPNAELRHVVVSNGEL---RLFIFALKDIRKGTEITIPF 123
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 589-637 2.92e-06

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, Enhancer-of-zeste, Trithorax (SET) domain superfamily corresponds to SET domain-containing lysine methyltransferases, which catalyze site and state-specific methylation of lysine residues in histones that are fundamental in epigenetic regulation of gene activation and silencing in eukaryotic organisms. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains has been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as N-SET and C-SET. C-SET forms an unusual and conserved knot-like structure of probable functional importance. In addition to N-SET and C-SET, an insert region (I-SET) and flanking regions of high structural variability form part of the overall structure. Some family members contain a pre-SET domain, which is found in a number of histone methyltransferases (HMTase), and a post-SET domain, which harbors a zinc-binding site.


Pssm-ID: 380914 [Multi-domain]  Cd Length: 72  Bit Score: 45.32  E-value: 2.92e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 15236295 589 VACYISHSTDPNVIVQFVLHDHNslmfPRVMLFAAENIPPMTELSLDYG 637
Cdd:cd08161  28 LARFINHSCEPNCEFEEVYVGGK----PRVFIVALRDIKAGEELTVDYG 72
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
 504-637 6.26e-06

SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and similar proteins; LegAS4 is a type IV secretion system effector of Legionella pneumophila. It contains a SET domain that is involved in the modification of Lys4 of histone H3 (H3K4) in the nucleolus of the host cell, thereby enhancing heterochromatic rDNA transcription. It also contains an ankyrin repeat domain of unknown function at its C-terminal region.


Pssm-ID: 380920 [Multi-domain]  Cd Length: 122  Bit Score: 45.80  E-value: 6.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 504 GWGVRSLDVLHAGAFICEYAGVALTREQaniltmngdtlvyparfssarwEDwgdlsQVLADFERPSYP-DIPPVDFAMD 582
Cdd:cd10522  14 GLGLFAAETIAKGEFVGEYTGEVLDRWE----------------------ED-----RDSVYHYDPLYPfDLNGDILVID 66

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15236295 583 VSKMRNVACYISHSTDPNVIVQFVLHDHNslmfPRVMLFAAENIPPMTELSLDYG 637
Cdd:cd10522  67 AGKKGNLTRFINHSDQPNLELIVRTLKGE----QHIGFVAIRDIKPGEELFISYG 117
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
 494-636 1.07e-05

SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and similar proteins; SETD2 (also termed HIF-1, huntingtin yeast partner B, huntingtin-interacting protein 1 (HIP-1), huntingtin-interacting protein B, lysine N-methyltransferase 3A or protein-lysine N-methyltransferase SETD2) acts as histone-lysine N-methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using demethylated 'Lys-36' (H3K36me2) as substrate. It has been shown that methylation is a posttranslational modification of dynamic microtubules and that SETD2 methylates alpha-tubulin at lysine 40, the same lysine that is marked by acetylation on microtubules. Methylation of microtubules occurs during mitosis and cytokinesis and can be ablated by SETD2 deletion, which causes mitotic spindle and cytokinesis defects, micronuclei, and polyploidy.


Pssm-ID: 380949 [Multi-domain]  Cd Length: 142  Bit Score: 45.65  E-value: 1.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 494 RLEVFRSLETGWGVRSLDVLHAGAFICEYAGVALTREQaniltmngdtlvyparFSSaRWEDWGDLSQvladfeRPSYpd 573
Cdd:cd19172   3 KVEVFRTEKKGWGLRAAEDLPKGTFVIEYVGEVLDEKE----------------FKR-RMKEYAREGN------RHYY-- 57

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15236295 574 ippvdFAM-------DVSKMRNVACYISHSTDPNVIVQ-FVLHDHnslmfPRVMLFAAENIPPMTELSLDY 636
Cdd:cd19172  58 -----FMAlksdeiiDATKKGNLSRFINHSCEPNCETQkWTVNGE-----LRVGFFAKRDIPAGEELTFDY 118
AWS smart00570
associated with SET domains; subdomain of PRESET
 431-490 5.55e-05

associated with SET domains; subdomain of PRESET


Pssm-ID: 197795  Cd Length: 50  Bit Score: 40.85  E-value: 5.55e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15236295    431 ASGCDCVN------GCGSGCLCEAKNSgeiaydyngtlirqkplihECGSACQCPPSCRNRVTQKG 490
Cdd:smart00570   2 IMTCECKPtdddetACGSDCLNRMLFI-------------------ECSSSCPCGSYCSNQRFQKR 48
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
 496-638 3.26e-04

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


Pssm-ID: 380988 [Multi-domain]  Cd Length: 142  Bit Score: 41.51  E-value: 3.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236295 496 EVFRSLETGWGVRSLDVLHAGAFICEYAGVALTREQANiltmngdtlvypARFSSARWEDWGDLSQVLADFERpsypdip 575
Cdd:cd19211   5 KIIKTEGKGWGLIAKRDIKKGEFVNEYVGELIDEEECM------------ARIKHAHENDITHFYMLTIDKDR------- 65

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15236295 576 pvdfAMDVSKMRNVACYISHSTDPNVIVQFVLHDHNSlmfpRVMLFAAENIPPMTELSLDYGV 638
Cdd:cd19211  66 ----IIDAGPKGNYSRFMNHSCQPNCETQKWTVNGDT----RVGLFAVCDIPAGTELTFNYNL 120
SET_SETD8 cd10528
SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2. ...
 592-638 4.84e-03

SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2.1.1.43; also termed N-lysine methyltransferase KMT5A, H4-K20-HMTase KMT5A, lysine N-methyltransferase 5A, lysine-specific methylase 5A, PR/SET domain-containing protein 07, PR-Set7 or PR/SET07) is a nucleosomal histone-lysine N-methyltransferase that specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). It plays a central role in the silencing of euchromatic genes.


Pssm-ID: 380926 [Multi-domain]  Cd Length: 141  Bit Score: 37.94  E-value: 4.84e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 15236295 592 YISHS-TDPNVI-VQFVLHDHnslmfPRVMLFAAENIPPMTELSLDYGV 638
Cdd:cd10528  97 LINHSkKKPNLKtKLLVIDGV-----PHLILVAKRDIKPGEELLYDYGD 140
 
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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