NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|755564482|ref|XP_011245754|]
View 

histone-lysine N-methyltransferase SUV39H1 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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, ...
159-372 2.02e-157

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 cd10525:

Pssm-ID: 394802 [Multi-domain]  Cd Length: 255  Bit Score: 444.72  E-value: 2.02e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 159 RSFVYINEYRVGEGITLNQVAVGCECQDCLLAPTGGCCPGASLHKFAYNDQGQVRLKAGQPIYECNSRCCCGYDCPNRVV 238
Cdd:cd10525    1 RDFVYINEYKVGEGVTLNQVAVGCECQDCLSQPVGGCCPGASKHRFAYNEQGQVKVRPGLPIYECNSRCRCGPDCPNRVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 239 QKGIRYDLCIFRTNDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGN 318
Cdd:cd10525   81 QKGIQYDLCIFRTDNGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGN 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755564482 319 ISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDYNMQVDP 372
Cdd:cd10525  161 ISHFVNHSCDPNLQVYNVFIDNLDERLPRIALFATRTIRAGEELTFDYNMQVDP 214
CD_SUV39H1_like cd18639
chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin ...
44-92 1.23e-29

chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin Organization Modifier (chromo) domain of human SUV39H1, a histone lysine methyltransferase (HMT) which catalyzes di- and tri-methylation of lysine 9 of histone H3 (H3K9me2/3), leading to heterochromatin formation and gene silencing. H3K9me2/3 represents a specific mark for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3, and/or CBX5) proteins to methylated histones. SUV39H1 mainly functions in heterochromatin regions. The human SUV39H1/2, histone H3K9 methyltransferases, are the mammalian homologs of Drosophila Su(var)3-9 and Schizosaccharomyces pombe Clr4. SUV39H1 contains a chromodomain at its N-terminus and a SET domain at its C-terminus. Although the SET domain performs the catalytic activity, the chromodomain of SUV39H1 is essential for the catalytic activity of SUV39H1. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


:

Pssm-ID: 349289  Cd Length: 49  Bit Score: 109.14  E-value: 1.23e-29
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 755564482  44 FEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCIRVLKQFHK 92
Cdd:cd18639    1 YEVEYLCDYKKIREQEYYLVKWKGYPDSENTWEPRQNLKCSRLLKQFHK 49
 
Name Accession Description Interval E-value
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
159-372 2.02e-157

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: 444.72  E-value: 2.02e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 159 RSFVYINEYRVGEGITLNQVAVGCECQDCLLAPTGGCCPGASLHKFAYNDQGQVRLKAGQPIYECNSRCCCGYDCPNRVV 238
Cdd:cd10525    1 RDFVYINEYKVGEGVTLNQVAVGCECQDCLSQPVGGCCPGASKHRFAYNEQGQVKVRPGLPIYECNSRCRCGPDCPNRVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 239 QKGIRYDLCIFRTNDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGN 318
Cdd:cd10525   81 QKGIQYDLCIFRTDNGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGN 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755564482 319 ISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDYNMQVDP 372
Cdd:cd10525  161 ISHFVNHSCDPNLQVYNVFIDNLDERLPRIALFATRTIRAGEELTFDYNMQVDP 214
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
244-367 2.55e-42

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: 145.56  E-value: 2.55e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482   244 YDLCIFRTnDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGA--TYLFDLDyveDVYTVDAAYYGNISH 321
Cdd:smart00317   1 NKLEVFKS-PGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkaFYLFDID---SDLCIDARRKGNLAR 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 755564482   322 FVNHSCDPNLQVYNVFIDNLDerlpRIAFFATRTIWAGEELTFDYN 367
Cdd:smart00317  77 FINHSCEPNCELLFVEVNGDD----RIVIFALRDIKPGEELTIDYG 118
CD_SUV39H1_like cd18639
chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin ...
44-92 1.23e-29

chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin Organization Modifier (chromo) domain of human SUV39H1, a histone lysine methyltransferase (HMT) which catalyzes di- and tri-methylation of lysine 9 of histone H3 (H3K9me2/3), leading to heterochromatin formation and gene silencing. H3K9me2/3 represents a specific mark for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3, and/or CBX5) proteins to methylated histones. SUV39H1 mainly functions in heterochromatin regions. The human SUV39H1/2, histone H3K9 methyltransferases, are the mammalian homologs of Drosophila Su(var)3-9 and Schizosaccharomyces pombe Clr4. SUV39H1 contains a chromodomain at its N-terminus and a SET domain at its C-terminus. Although the SET domain performs the catalytic activity, the chromodomain of SUV39H1 is essential for the catalytic activity of SUV39H1. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349289  Cd Length: 49  Bit Score: 109.14  E-value: 1.23e-29
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 755564482  44 FEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCIRVLKQFHK 92
Cdd:cd18639    1 YEVEYLCDYKKIREQEYYLVKWKGYPDSENTWEPRQNLKCSRLLKQFHK 49
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
256-367 1.26e-29

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: 111.46  E-value: 1.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482  256 GWGVRTLEKIRKNSFVMEYVGE-IITSEEAERRGQIY-----DRQGATYLFDLDyVEDVYTVD--AAYYGNISHFVNHSC 327
Cdd:pfam00856   1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYydkleLRLWGPYLFTLD-EDSEYCIDarALYYGNWARFINHSC 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 755564482  328 DPNLQVYNVFIDnldeRLPRIAFFATRTIWAGEELTFDYN 367
Cdd:pfam00856  80 DPNCEVRVVYVN----GGPRIVIFALRDIKPGEELTIDYG 115
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
250-367 1.62e-27

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 106.20  E-value: 1.62e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 250 RTNDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIyDRQGATYLFDLDyveDVYTVDAAYYGNISHFVNHSCDP 329
Cdd:COG2940   11 RPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPH-KEPLHTYLFELD---DDGVIDGALGGNPARFINHSCDP 86
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 755564482 330 NLQvynvfidnLDERLPRIAFFATRTIWAGEELTFDYN 367
Cdd:COG2940   87 NCE--------ADEEDGRIFIVALRDIAAGEELTYDYG 116
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
44-92 3.53e-14

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 66.45  E-value: 3.53e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755564482   44 FEVEYLCDYKKIREQ-EYYLVKWRGYPDSENTWEPRQNL-KCIRVLKQFHK 92
Cdd:pfam00385   1 YEVERILDHRKDKGGkEEYLVKWKGYPYDENTWEPEENLsKCPELIEEFKD 51
CHROMO smart00298
Chromatin organization modifier domain;
43-93 2.79e-11

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 58.38  E-value: 2.79e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 755564482    43 DFEVEYLCDYKKIREQEY-YLVKWRGYPDSENTWEPRQNLK-CIRVLKQFHKD 93
Cdd:smart00298   1 EYEVEKILDHRWKKKGELeYLVKWKGYSYSEDTWEPEENLLnCSKKLDNYKKK 53
 
Name Accession Description Interval E-value
SET_SUV39H1 cd10525
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
159-372 2.02e-157

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: 444.72  E-value: 2.02e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 159 RSFVYINEYRVGEGITLNQVAVGCECQDCLLAPTGGCCPGASLHKFAYNDQGQVRLKAGQPIYECNSRCCCGYDCPNRVV 238
Cdd:cd10525    1 RDFVYINEYKVGEGVTLNQVAVGCECQDCLSQPVGGCCPGASKHRFAYNEQGQVKVRPGLPIYECNSRCRCGPDCPNRVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 239 QKGIRYDLCIFRTNDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGN 318
Cdd:cd10525   81 QKGIQYDLCIFRTDNGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGN 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755564482 319 ISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDYNMQVDP 372
Cdd:cd10525  161 ISHFVNHSCDPNLQVYNVFIDNLDERLPRIALFATRTIRAGEELTFDYNMQVDP 214
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
161-373 3.67e-132

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: 380.10  E-value: 3.67e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 161 FVYINEYRVGEGITLNQ-VAVGCECQ-DCLLAPTGgCCPGASLHKFAYNDQGQVRLKAGQPIYECNSRCCCGYDCPNRVV 238
Cdd:cd10542    3 FQYINDYIPGDGVKIPEdFLVGCECTeDCHNNNPT-CCPAESGVKFAYDKQGRLRLPPGTPIYECNSRCKCGPDCPNRVV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 239 QKGIRYDLCIFRTNDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVED--VYTVDAAYY 316
Cdd:cd10542   82 QRGRKVPLCIFRTSNGRGWGVKTLEDIKKGTFVMEYVGEIITSEEAERRGKIYDANGRTYLFDLDYNDDdcEYTVDAAYY 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755564482 317 GNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDYNMQVDPA 373
Cdd:cd10542  162 GNISHFINHSCDPNLAVYAVWINHLDPRLPRIAFFAKRDIKAGEELTFDYLMTGTGG 218
SET_SUV39H2 cd10532
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
161-369 5.68e-122

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: 354.20  E-value: 5.68e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 161 FVYINEYRVGEGITL-NQVAVGCECQDCllaPTGGCCPGASLHKFAYNDQGQVRLKAGQPIYECNSRCCCGYDCPNRVVQ 239
Cdd:cd10532    3 FYYINEYKPAPGINLdNEATVGCDCSDC---FFGKCCPAEAGVLFAYNEHGQLKIPPGTPIYECNSRCKCGPDCPNRVVQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 240 KGIRYDLCIFRTNDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNI 319
Cdd:cd10532   80 KGTQYSLCIFRTSNGRGWGVKTLQKIKKNSFVMEYVGEVITSEEAERRGQFYDSKGITYLFDLDYESDEFTVDAARYGNV 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 755564482 320 SHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDYNMQ 369
Cdd:cd10532  160 SHFVNHSCDPNLQVFNVFIDNLDTRLPRIALFSTRTIKAGEELTFDYQMK 209
SET_SETDB-like cd10538
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
160-367 1.61e-84

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: 257.68  E-value: 1.61e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 160 SFVYINEYRVGEGITLNQ---VAVGCECQD-CLLAPtggC-CPGASLHKFAYNDQGQVRL-KAGQPIYECNSRCCCGYDC 233
Cdd:cd10538    2 SFTYIKDNIVGKNVQPFSniiDSVGCKCKDdCLDSK---CaCAAESDGIFAYTKNGLLRLnNSPPPIFECNSKCSCDDDC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 234 PNRVVQKGIRYDLCIFRTNDgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDV----- 308
Cdd:cd10538   79 KNRVVQRGLQARLQVFRTSK-KGWGVRSLEFIPKGSFVCEYVGEVITTSEADRRGKIYDKSGGSYLFDLDEFSDSdgdge 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 309 -YTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDYN 367
Cdd:cd10538  158 eLCVDATFCGNVSRFINHSCDPNLFPFNVVIDHDDLRYPRIALFATRDILPGEELTFDYG 217
SET_SUV39H_Clr4-like cd20073
SET domain (including pre-SET and post-SET domains) found in of Schizosaccharomyces pombe H3K9 ...
161-366 2.44e-65

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: 210.12  E-value: 2.44e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 161 FVYINEYRVGEGITLNQ--VAVGCECQD---CLLAPTGGC-CPGASLHK-FAYNDQGQVRLKAGQPIYECNSRCCCGYDC 233
Cdd:cd20073    3 FEFITSYRYGLGIEPPDplFISGCSCSKlggCDLNNPGSCqCLEDSNEKsFAYDEYGRVRANTGSIIYECNENCDCGINC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 234 PNRVVQKGIRYDLCIFRTNDgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVED----VY 309
Cdd:cd20073   83 PNRVVQRGRKLPLEIFKTKH-KGWGLRCPRFIKAGTFIGVYLGEVITQSEAEIRGKKYDNVGVTYLFDLDLFEDqvdeYY 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755564482 310 TVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDY 366
Cdd:cd20073  162 TVDAQYCGDVTRFINHSCDPNLAIYSVLRDKSDSKIYDLAFFAIKDIPALEELTFDY 218
SET_SETDB1 cd10517
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
146-375 4.70e-61

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: 199.82  E-value: 4.70e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 146 ITVENEVDLDGPPrSFVYINEYRVGEGITLN---QVAVGCECQD---------C--LLAPTGGCCPGASLHKFAYNDQGq 211
Cdd:cd10517   18 IPCVNEIDNSSPP-YVEYSKERIPGKGVNINldpDFLVGCDCTDgcrdkskcaCqqLTIEATAATPGGQINPSAGYQYR- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 212 vRLKAGQP--IYECNSRCCCGYDCPNRVVQKGIRYDLCIFRTNDgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQ 289
Cdd:cd10517   96 -RLMEKLPtgVYECNSRCKCDKRCYNRVVQNGLQVRLQVFKTEK-KGWGIRCLDDIPKGSFVCIYAGQILTEDEANEEGL 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 290 IYDRQgatYLFDLDYVEDV---------------YTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATR 354
Cdd:cd10517  174 QYGDE---YFAELDYIEVVeklkegyesdveehcYIIDAKSEGNLGRYLNHSCSPNLFVQNVFVDTHDLRFPWVAFFASR 250
                        250       260
                 ....*....|....*....|.
gi 755564482 355 TIWAGEELTFDYNMQVDPAHG 375
Cdd:cd10517  251 YIRAGTELTWDYNYEVGSVPG 271
SET_SUV39H_DIM5-like cd19473
SET domain (including pre-SET domain) found in Neurospora crassa (DIM-5) and similar proteins; ...
160-366 4.76e-61

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: 199.47  E-value: 4.76e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 160 SFVYINEYRVGEGITLNQVA--VGCECQDCLLAPTGGC-C---------PGASLHKFAYNDQGQvrlKAG---------- 217
Cdd:cd19473    2 DFRFIEKSILGEGVELADEEfrSGCECTDDEDCMYSGClClqdvdpdddRDPGKKKNAYHSSGA---KKGclrghmlnsr 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 218 QPIYECNSRCCCGYDCPNRVVQKGIRYDLCIFRTNDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRgqiydRQGAT 297
Cdd:cd19473   79 LPIYECHEGCACSDDCPNRVVERGRKVPLQIFRTSDGRGWGVRSTVDIKRGQFVDCYVGEIITPEEAQRR-----RDAAT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 298 -------YLFDLDYVEDV-----------YTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAG 359
Cdd:cd19473  154 iaqrkdvYLFALDKFSDPdsldprlrgdpYEIDGEFMSGPTRFINHSCDPNLRIFARVGDHADKHIHDLAFFAIKDIPRG 233

                 ....*..
gi 755564482 360 EELTFDY 366
Cdd:cd19473  234 TELTFDY 240
SET_EHMT cd10543
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
161-366 4.05e-60

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: 195.64  E-value: 4.05e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 161 FVYINEYRVGEGITLNQVA---VGCECQD-CLlapTGGCCPGASLHKFAYNDQGqvRLKAG----QP--IYECNSRCCCG 230
Cdd:cd10543    3 FLYVTENCETSPLNIDRNItslQTCSCRDdCS---SDNCVCGRLSVRCWYDKEG--RLLPDfnklDPplIFECNRACSCW 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 231 YDCPNRVVQKGIRYDLCIFRTNdGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRgqiydrQGATYLFDLDYVE-DVY 309
Cdd:cd10543   78 RNCRNRVVQNGIRYRLQLFRTR-GMGWGVRALQDIPKGTFVCEYIGELISDSEADSR------EDDSYLFDLDNKDgETY 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755564482 310 TVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDY 366
Cdd:cd10543  151 CIDARRYGNISRFINHLCEPNLIPVRVFVEHQDLRFPRIAFFASRDIKAGEELGFDY 207
SET_AtSUVH-like cd10545
SET domain found in Arabidopsis thaliana histone H3-K9 methyltransferases (SUVHs) and similar ...
160-367 2.11e-52

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: 175.67  E-value: 2.11e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 160 SFVYINEYRVGEGITLNQVAVGCECQD-CLLAPTGGCCPGASLHKFAYNDQGqvRLKAGQP-IYECNSRCCCGYDCPNRV 237
Cdd:cd10545    2 GFTYTVKLIIPPGVSLPVPSTGCDCKNrCTDGASDCACVKKNGGEIPYNFNG--RLIRAKPaIYECGPLCKCPPSCYNRV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 238 VQKGIRYDLCIFRTNDgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDrqgatYLFDLDYVEDV--------- 308
Cdd:cd10545   80 TQKGLRYRLEVFKTAE-RGWGVRSWDSIPAGSFICEYVGELLDTSEADTRSGNDD-----YLFDIDNRQTNrgwdggqrl 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755564482 309 -------------------YTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDYN 367
Cdd:cd10545  154 dvgmsdgerssaedeesseFTIDAGSFGNVARFINHSCSPNLFVQCVLYDHNDLRLPRVMLFAADNIPPLQELTYDYG 231
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
181-366 8.18e-51

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: 172.10  E-value: 8.18e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 181 GCECQDCLLAPTGGCCpgasLHKF--AYNDQGQVRL---KAGQPIYECNSRCCCGYDCPNRVVQKGIRYDLCIFRTnDGR 255
Cdd:cd10544   26 GCDCKTSSCEPETCSC----LRKYgpNYDDDGCLLDfdgKYSGPVFECNSMCKCSESCQNRVVQNGLQFKLQVFKT-PKK 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 256 GWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDyvEDVYT-------VDAAYYGNISHFVNHSCD 328
Cdd:cd10544  101 GWGLRTLEFIPKGRFVCEYAGEVIGFEEARRRTKSQTKGDMNYIIVLR--EHLSSgkvletfVDPTYIGNIGRFLNHSCE 178
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 755564482 329 PNLQVYNVFIDNLderLPRIAFFATRTIWAGEELTFDY 366
Cdd:cd10544  179 PNLFMVPVRVDSM---VPKLALFAARDIVAGEELSFDY 213
SET_EHMT1 cd10535
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
220-366 1.91e-47

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: 162.41  E-value: 1.91e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 220 IYECNSRCCCGYDCPNRVVQKGIRYDLCIFRTNDgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRgqiydrQGATYL 299
Cdd:cd10535   67 IFECNHACSCWRNCRNRVVQNGLRARLQLYRTRD-MGWGVRSLQDIPPGTFVCEYVGELISDSEADVR------EEDSYL 139
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755564482 300 FDLDYVE-DVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDY 366
Cdd:cd10535  140 FDLDNKDgEVYCIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDY 207
SET_EHMT2 cd10533
SET domain (including pre-SET and post-SET domains) found in euchromatic histone-lysine ...
220-366 2.85e-44

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: 154.40  E-value: 2.85e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 220 IYECNSRCCCGYDCPNRVVQKGIRYDLCIFRTNDgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRgqiydrQGATYL 299
Cdd:cd10533   67 IFECNQACSCWRNCKNRVVQSGIKVRLQLYRTAK-MGWGVRALQTIPQGTFICEYVGELISDAEADVR------EDDSYL 139
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755564482 300 FDLDYVE-DVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDY 366
Cdd:cd10533  140 FDLDNKDgEVYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDY 207
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
244-367 2.55e-42

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: 145.56  E-value: 2.55e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482   244 YDLCIFRTnDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGA--TYLFDLDyveDVYTVDAAYYGNISH 321
Cdd:smart00317   1 NKLEVFKS-PGKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkaFYLFDID---SDLCIDARRKGNLAR 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 755564482   322 FVNHSCDPNLQVYNVFIDNLDerlpRIAFFATRTIWAGEELTFDYN 367
Cdd:smart00317  77 FINHSCEPNCELLFVEVNGDD----RIVIFALRDIKPGEELTIDYG 118
SET_SETDB cd10541
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1), ...
173-375 3.60e-40

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: 143.45  E-value: 3.60e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 173 ITLNQVAVGCECQD---------C--LLAPTGGCCPGASLHKFAYNDQGQVRLKAGQPIYECNSRCCCGYD-CPNRVVQK 240
Cdd:cd10541    9 ISYGKFLVGCDCTDgcrdkskcaChqLTIQATACTPGGQDNPTAGYQYKRLEECLPTGVYECNKLCKCDPNmCQNRLVQH 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 241 GIRYDLCIFRTNDgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIydrQGATYLFDLDYVED-VYTVDAAYYGNI 319
Cdd:cd10541   89 GLQVRLQLFKTQN-KGWGIRCLDDIAKGTFVCIYAGKILTDDFADKEGLE---MGDEYFANLDHIEEsCYIIDAKLEGNL 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755564482 320 SHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDYNMQVDPAHG 375
Cdd:cd10541  165 GRYLNHSCSPNLFVQNVFVDTHDLRFPWVAFFASKRIKAGTELTWDYNYEVGSVEG 220
SET_EZH cd10519
SET domain found in enhancer of zeste homolog 1 (EZH1), zeste homolog 2 (EZH2) and similar ...
256-366 2.20e-36

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: 129.29  E-value: 2.20e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 256 GWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDyveDVYTVDAAYYGNISHFVNHSCDPNLQVyN 335
Cdd:cd10519   12 GWGLFLKEPIKKDEFIGEYTGELISQDEADRRGKIYDKYNSSYLFNLN---DQFVVDATRKGNKIRFANHSSNPNCYA-K 87
                         90       100       110
                 ....*....|....*....|....*....|.
gi 755564482 336 VFIDNLDErlpRIAFFATRTIWAGEELTFDY 366
Cdd:cd10519   88 VMMVNGDH---RIGIFAKRDIEAGEELFFDY 115
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
245-369 3.73e-34

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: 124.29  E-value: 3.73e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 245 DLCIFRTNDgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRgQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISHFVN 324
Cdd:cd10531    1 KLELFRTEK-KGWGVKAKEDIQKGEFIIEYVGEVIDKKEFKER-LDEYEELGKSNFYILSLSDDVVIDATRKGNLSRFIN 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 755564482 325 HSCDPNL--QVYNVFIDnlderlPRIAFFATRTIWAGEELTFDYNMQ 369
Cdd:cd10531   79 HSCEPNCetQKWIVNGE------YRIGIFALRDIPAGEELTFDYNFV 119
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
248-370 2.25e-33

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: 122.30  E-value: 2.25e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 248 IFRTnDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGAT--YLFDLDYVEdvyTVDAAYYGNISHFVNH 325
Cdd:cd19172    6 VFRT-EKKGWGLRAAEDLPKGTFVIEYVGEVLDEKEFKRRMKEYAREGNRhyYFMALKSDE---IIDATKKGNLSRFINH 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 755564482 326 SCDPN--LQVYNVfidnldERLPRIAFFATRTIWAGEELTFDYNMQV 370
Cdd:cd19172   82 SCEPNceTQKWTV------NGELRVGFFAKRDIPAGEELTFDYQFER 122
SET_ASH1L cd19174
SET domain (including post-SET domain) found in ASH1-like protein (ASH1L) and similar proteins; ...
249-367 3.71e-31

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: 116.24  E-value: 3.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 249 FRTNDgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRG-QIYDRQGATYLFDLDYVEdvyTVDAAYYGNISHFVNHSC 327
Cdd:cd19174    5 FRTED-KGWGVRTKEPIKAGQFIIEYVGEVVSEQEFRRRMiEQYHNHSHHYCLNLDSGM---VIDGYRMGNEARFVNHSC 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 755564482 328 DPN--LQVYNVfidnldERLPRIAFFATRTIWAGEELTFDYN 367
Cdd:cd19174   81 DPNceMQKWSV------NGVYRIGLFALKDIPAGEELTYDYN 116
SET_SETD1-like cd10518
SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...
256-374 7.76e-31

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: 115.77  E-value: 7.76e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 256 GWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGA--TYLFDLDyveDVYTVDAAYYGNISHFVNHSCDPNLQV 333
Cdd:cd10518   25 GWGLFAKRPIAAGEMVIEYVGEVIRPIVADKREKRYDEEGGggTYMFRID---EDLVIDATKKGNIARFINHSCDPNCYA 101
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 755564482 334 YNVFIDNLDerlpRIAFFATRTIWAGEELTFDYNMQVDPAH 374
Cdd:cd10518  102 KIITVDGEK----HIVIFAKRDIAPGEELTYDYKFPIEDEE 138
SET_SETDB2 cd10523
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 2 (SETDB2) ...
220-367 8.92e-31

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: 119.17  E-value: 8.92e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 220 IYECNSRCCCGYD-CPNRVVQKGIRYDLCIFRTNDgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQG--- 295
Cdd:cd10523   83 LYECNVSCKCNRMlCQNRVVQHGLQVRLQVFKTEK-KGWGVRCLDDIDKGTFVCIYAGRVLSRARSPTEPLPPKLELpse 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 296 --------ATYLFDLDYVED-VYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDY 366
Cdd:cd10523  162 nevevvtsWLILSKKRKLREnVCFLDASKEGNVGRFLNHSCCPNLFVQNVFVDTHDKNFPWVAFFTNRVVKAGTELTWDY 241

                 .
gi 755564482 367 N 367
Cdd:cd10523  242 S 242
CD_SUV39H1_like cd18639
chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin ...
44-92 1.23e-29

chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin Organization Modifier (chromo) domain of human SUV39H1, a histone lysine methyltransferase (HMT) which catalyzes di- and tri-methylation of lysine 9 of histone H3 (H3K9me2/3), leading to heterochromatin formation and gene silencing. H3K9me2/3 represents a specific mark for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3, and/or CBX5) proteins to methylated histones. SUV39H1 mainly functions in heterochromatin regions. The human SUV39H1/2, histone H3K9 methyltransferases, are the mammalian homologs of Drosophila Su(var)3-9 and Schizosaccharomyces pombe Clr4. SUV39H1 contains a chromodomain at its N-terminus and a SET domain at its C-terminus. Although the SET domain performs the catalytic activity, the chromodomain of SUV39H1 is essential for the catalytic activity of SUV39H1. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349289  Cd Length: 49  Bit Score: 109.14  E-value: 1.23e-29
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 755564482  44 FEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCIRVLKQFHK 92
Cdd:cd18639    1 YEVEYLCDYKKIREQEYYLVKWKGYPDSENTWEPRQNLKCSRLLKQFHK 49
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
256-367 1.26e-29

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: 111.46  E-value: 1.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482  256 GWGVRTLEKIRKNSFVMEYVGE-IITSEEAERRGQIY-----DRQGATYLFDLDyVEDVYTVD--AAYYGNISHFVNHSC 327
Cdd:pfam00856   1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYydkleLRLWGPYLFTLD-EDSEYCIDarALYYGNWARFINHSC 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 755564482  328 DPNLQVYNVFIDnldeRLPRIAFFATRTIWAGEELTFDYN 367
Cdd:pfam00856  80 DPNCEVRVVYVN----GGPRIVIFALRDIKPGEELTIDYG 115
SET_NSD cd19173
SET domain (including post-SET domain) found in nuclear SET domain-containing proteins, NSD1, ...
248-368 2.55e-28

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: 108.56  E-value: 2.55e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 248 IFRTNDgRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGAT--YLFDLDyvEDVYtVDAAYYGNISHFVNH 325
Cdd:cd19173    6 PFKTGD-RGWGLRTKRDIKKGDFVIEYVGELIDEEECRRRLKKAHENNITnfYMLTLD--KDRI-IDAGPKGNLSRFMNH 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 755564482 326 SCDPNL--QVYNVFIDnlderlPRIAFFATRTIWAGEELTFDYNM 368
Cdd:cd19173   82 SCQPNCetQKWTVNGD------TRVGLFAVRDIPAGEELTFNYNL 120
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
250-367 1.62e-27

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 106.20  E-value: 1.62e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 250 RTNDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIyDRQGATYLFDLDyveDVYTVDAAYYGNISHFVNHSCDP 329
Cdd:COG2940   11 RPSPIHGRGVFATRDIPKGTLIGEYPGEVITWAEAERREPH-KEPLHTYLFELD---DDGVIDGALGGNPARFINHSCDP 86
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 755564482 330 NLQvynvfidnLDERLPRIAFFATRTIWAGEELTFDYN 367
Cdd:COG2940   87 NCE--------ADEEDGRIFIVALRDIAAGEELTYDYG 116
SET_EZH2 cd19218
SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43) ...
252-366 5.16e-26

SET domain found in enhancer of zeste homolog 2 (EZH2) and similar proteins; EZH2 (EC 2.1.1.43), also termed lysine N-methyltransferase 6, or ENX-1, or histone-lysine N-methyltransferase EZH2, is a catalytic subunit of the polycomb repressive complex 2 (PRC2)/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. It can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. PRC2 is involved in several cancers; EZH2 is overexpressed in breast, liver and prostate cancer, while point mutations in EZH2 alter the substrate preference and product specificity of PRC2 in Non-Hodgkin lymphomas (NHLs). Thus, PRC2 is a popular target for cancer therapeutics.


Pssm-ID: 380995  Cd Length: 120  Bit Score: 101.91  E-value: 5.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 252 NDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDyveDVYTVDAAYYGNISHFVNHSCDPNL 331
Cdd:cd19218   11 SDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLN---NDFVVDATRKGNKIRFANHSVNPNC 87
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 755564482 332 QVyNVFIDNLDErlpRIAFFATRTIWAGEELTFDY 366
Cdd:cd19218   88 YA-KVMMVNGDH---RIGIFAKRAIQTGEELFFDY 118
SET_EZH1 cd19217
SET domain found in enhancer of zeste homolog 1 (EZH1) and similar proteins; EZH1 (EC 2.1.1.43) ...
239-366 8.19e-25

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


Pssm-ID: 380994  Cd Length: 136  Bit Score: 98.99  E-value: 8.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 239 QKGIRYDLcIFRTNDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDyveDVYTVDAAYYGN 318
Cdd:cd19217    1 QRGLKKHL-LLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYDKYMSSFLFNLN---NDFVVDATRKGN 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 755564482 319 ISHFVNHSCDPNLQVYNVFIdNLDErlpRIAFFATRTIWAGEELTFDY 366
Cdd:cd19217   77 KIRFANHSVNPNCYAKVVMV-NGDH---RIGIFAKRAIQQGEELFFDY 120
SET_ASHR3-like cd19175
SET domain (including post-SET domain) found in Arabidopsis thaliana ASH1-related protein 3 ...
256-367 8.50e-25

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: 99.03  E-value: 8.50e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 256 GWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVyTVDAAYYGNISHFVNHSCDPNLQVYN 335
Cdd:cd19175   11 GWGLVADEDINAGEFIIEYVGEVIDDKTCEERLWDMKHKGEKNFYMCEIDKDM-VIDATFKGNLSRFINHSCDPNCELQK 89
                         90       100       110
                 ....*....|....*....|....*....|..
gi 755564482 336 VFIDNLDerlpRIAFFATRTIWAGEELTFDYN 367
Cdd:cd19175   90 WQVDGET----RIGVFAIRDIKKGEELTYDYQ 117
PreSET smart00468
N-terminal to some SET domains; A Cys-rich putative Zn2+-binding domain that occurs N-terminal ...
133-228 1.67e-24

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: 96.72  E-value: 1.67e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482   133 EQELNAKRSHLGRITVeNEVDLDGPPRSFVYINEYRVGEGIT---LNQVAVGCECQ-DCLLAPTGgCCPGASLHKFAYND 208
Cdd:smart00468   1 CLDISNGKENVPVPLV-NEVDEDPPPPDFEYISEYIYGQGVPidrSPSPLVGCSCSgDCSSSNKC-ECARKNGGEFAYEL 78
                           90       100
                   ....*....|....*....|
gi 755564482   209 QGQVRLKAGQPIYECNSRCC 228
Cdd:smart00468  79 NGGLRLKRKPLIYECNSRCS 98
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
256-367 2.49e-24

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: 97.03  E-value: 2.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 256 GWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQiyDRQGATYLFDLDYveDVYTVDAAYYGNISHFVNHSCDPNLQVYN 335
Cdd:cd10522   14 GLGLFAAETIAKGEFVGEYTGEVLDRWEEDRDSV--YHYDPLYPFDLNG--DILVIDAGKKGNLTRFINHSDQPNLELIV 89
                         90       100       110
                 ....*....|....*....|....*....|..
gi 755564482 336 VFidnlDERLPRIAFFATRTIWAGEELTFDYN 367
Cdd:cd10522   90 RT----LKGEQHIGFVAIRDIKPGEELFISYG 117
Pre-SET pfam05033
Pre-SET motif; This protein motif is a zinc binding motif. It contains 9 conserved cysteines ...
137-236 4.20e-23

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: 92.87  E-value: 4.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482  137 NAKRSHLGRITVENEVDLDGPPRSFVYINEYRVGEGITLNQvAVGCECQDCLlapTGGC-CPGASLH--KFAYNDQGQVR 213
Cdd:pfam05033   1 ISKGKENVPIPVVNEVDDEPPPPDFTYITSYIYPKEFLLII-PQGCDCGDCS---SEKCsCAQLNGGefRFPYDKDGLLV 76
                          90       100
                  ....*....|....*....|...
gi 755564482  214 LKAGQPIYECNSRCCCGYDCPNR 236
Cdd:pfam05033  77 PESKPPIYECNPLCGCPPSCPNR 99
SET_SET1 cd20072
SET domain (including post-SET domain) found in catalytic component of the Saccharomyces ...
257-371 6.63e-23

SET domain (including post-SET domain) found in catalytic component of the Saccharomyces cerevisiae COMPASS complex and similar proteins; The family contains mostly fungal SET domains, including SET1 found in the catalytic component of the Saccharomyces cerevisiae COMPASS (complex of proteins associated with Set1). SET1 is a histone-lysine N-methyltransferase that specifically methylates 'Lys-4' of histone H3 (H3K4me), when part of the SET1 histone methyltransferase (HMT) complex. The activity of this catalytic domain is established through forming a complex with a set of core proteins; it is extensively contacted by Cps60 (Bre2), Cps50 (Swd1), and Cps30 (Swd3).


Pssm-ID: 380998  Cd Length: 148  Bit Score: 94.03  E-value: 6.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 257 WGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQG--ATYLFDLDyvEDVyTVDAAYYGNISHFVNHSCDPNLQVY 334
Cdd:cd20072   25 WGLYAMENISAKDMVIEYVGEVIRQQVADEREKRYLRQGigSSYLFRID--DDT-VVDATKKGNIARFINHCCDPNCTAK 101
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 755564482 335 NVFIDNldERlpRIAFFATRTIWAGEELTFDYNMQVD 371
Cdd:cd20072  102 IIKVEG--EK--RIVIYAKRDIAAGEELTYDYKFPRE 134
SET_EZH-like cd19168
SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb ...
256-366 6.55e-22

SET domain found in enhancer of zeste homolog 1 (EZH1) and zeste homolog 2 (EZH2) of polycomb repressive complex 2 (PRC2), and similar proteins; The family includes EZH1 and EZH2. EZH1 (EC 2.1.1.43; also termed ENX-2, or histone-lysine N-methyltransferase EZH1) is a catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. EZH2 (EC 2.1.1.43; also termed lysine N-methyltransferase 6, ENX-1, or histone-lysine N-methyltransferase EZH2) is a catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Both EZH1 and EZH2 can mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. PRC2 is involved in several cancers; EZH2 is overexpressed in breast, liver and prostate cancer, while point mutations in EZH2 alter the substrate preference and product specificity of PRC2 in Non-Hodgkin lymphomas (NHLs). Thus, PRC2 is a popular target for cancer therapeutics.


Pssm-ID: 380945  Cd Length: 124  Bit Score: 90.71  E-value: 6.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 256 GWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDyveDVYTVDAAYYGNISHFVNHSCDP----NL 331
Cdd:cd19168   13 GLGLFAAEDIKEGEFVIEYTGELISHDEGVRREHRRGDVSYLYLFEEQ---EGIWVDAAIYGNLSRYINHATDKvktgNC 89
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 755564482 332 QVYNVFidnlDERLPRIAFFATRTIWAGEELTFDY 366
Cdd:cd19168   90 MPKIMY----VNHEWRIKFTAIKDIKIGEELFFNY 120
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
256-366 8.64e-22

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), 2D (KMT2D) and similar proteins; This family includes KMT2C and KMT2D. Both, KMT2C (also termed HALR or MLL3) and KMT2D (also termed ALR or MLL2), act as histone methyltransferases that methylate 'Lys-4' of histone H3 (H3K4me). They are subunits of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation.


Pssm-ID: 380948 [Multi-domain]  Cd Length: 153  Bit Score: 91.34  E-value: 8.64e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 256 GWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQG-ATYLFDLDyveDVYTVDAAYYGNISHFVNHSCDPNL--Q 332
Cdd:cd19171   25 GLGLYAARDIEKHTMVIEYIGEIIRNEVANRREKIYESQNrGIYMFRID---NDWVIDATMTGGPARYINHSCNPNCvaE 101
                         90       100       110
                 ....*....|....*....|....*....|....
gi 755564482 333 VYNVfidnldERLPRIAFFATRTIWAGEELTFDY 366
Cdd:cd19171  102 VVTF------DKEKKIIIISNRRIAKGEELTYDY 129
SET_SETD1 cd19169
SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...
256-366 8.67e-22

SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and similar proteins; This family includes SET domain-containing protein 1A (SETD1A) and SET domain-containing protein 1B (SETD1B). These proteins are histone-lysine N-methyltransferases that specifically methylate 'Lys-4' of histone H3 (H3K4me) when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated.


Pssm-ID: 380946  Cd Length: 148  Bit Score: 90.86  E-value: 8.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 256 GWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQ--GATYLFDLDyveDVYTVDAAYYGNISHFVNHSCDPNL-- 331
Cdd:cd19169   24 DWGLFALEPIAADEMVIEYVGQVIRQSVADEREKRYEAIgiGSSYLFRVD---DDTIIDATKCGNLARFINHSCNPNCya 100
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 755564482 332 QVYNVfidnldERLPRIAFFATRTIWAGEELTFDY 366
Cdd:cd19169  101 KIITV------ESQKKIVIYSKRPIAVNEEITYDY 129
SET_NSD3 cd19212
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
248-368 1.88e-21

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


Pssm-ID: 380989 [Multi-domain]  Cd Length: 142  Bit Score: 89.98  E-value: 1.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 248 IFRTnDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDvYTVDAAYYGNISHFVNHSC 327
Cdd:cd19212    6 IIKT-ERRGWGLRTKRSIKKGEFVNEYVGELIDEEECRLRIKRAHENSVTNFYMLTVTKD-RIIDAGPKGNYSRFMNHSC 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 755564482 328 DPN--LQVYNVFIDNlderlpRIAFFATRTIWAGEELTFDYNM 368
Cdd:cd19212   84 NPNceTQKWTVNGDV------RVGLFALCDIPAGMELTFNYNL 120
SET_SETD8 cd10528
SET domain found in SET domain-containing protein 8 (SETD8) and similar proteins; SETD8 (EC 2. ...
253-366 1.52e-20

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


Pssm-ID: 380926 [Multi-domain]  Cd Length: 141  Bit Score: 87.25  E-value: 1.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 253 DGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIY--DRQGATYLFDLDYVEDVYTVDAA----YYGNIshfVNHS 326
Cdd:cd10528   25 DGKGRGVIATRPFEKGDFVVEYHGDLITITEAKKREALYakDPSTGCYMYYFQYKGKTYCVDATkesgRLGRL---INHS 101
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 755564482 327 C-DPNLQVYNVFIDNlderLPRIAFFATRTIWAGEELTFDY 366
Cdd:cd10528  102 KkKPNLKTKLLVIDG----VPHLILVAKRDIKPGEELLYDY 138
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
248-368 5.18e-20

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


Pssm-ID: 380988 [Multi-domain]  Cd Length: 142  Bit Score: 85.81  E-value: 5.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 248 IFRTnDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDvYTVDAAYYGNISHFVNHSC 327
Cdd:cd19211    6 IIKT-EGKGWGLIAKRDIKKGEFVNEYVGELIDEEECMARIKHAHENDITHFYMLTIDKD-RIIDAGPKGNYSRFMNHSC 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 755564482 328 DPN--LQVYNVFIDNlderlpRIAFFATRTIWAGEELTFDYNM 368
Cdd:cd19211   84 QPNceTQKWTVNGDT------RVGLFAVCDIPAGTELTFNYNL 120
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
256-368 1.09e-19

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


Pssm-ID: 380947 [Multi-domain]  Cd Length: 152  Bit Score: 85.14  E-value: 1.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 256 GWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQG-ATYLFDLDyveDVYTVDAAYYGNISHFVNHSCDPNLQVY 334
Cdd:cd19170   25 GRGLFCKRNIDAGEMVIEYAGEVIRSVLTDKREKYYESKGiGCYMFRID---DDEVVDATMHGNAARFINHSCEPNCYSR 101
                         90       100       110
                 ....*....|....*....|....*....|....
gi 755564482 335 NVFIDNLDerlpRIAFFATRTIWAGEELTFDYNM 368
Cdd:cd19170  102 VVNIDGKK----HIVIFALRRILRGEELTYDYKF 131
SET_NSD1 cd19210
SET domain (including post-SET domain) found in nuclear receptor-binding SET domain-containing ...
248-369 2.10e-19

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: 84.21  E-value: 2.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 248 IFRTNdGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDvYTVDAAYYGNISHFVNHSC 327
Cdd:cd19210    6 IFRTL-GRGWGLRCKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKD-RIIDAGPKGNYARFMNHCC 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 755564482 328 DPN--LQVYNVFIDNlderlpRIAFFATRTIWAGEELTFDYNMQ 369
Cdd:cd19210   84 QPNceTQKWTVNGDT------RVGLFALCDIKAGTELTFNYNLE 121
SET_KMT2A cd19206
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) ...
236-373 1.42e-17

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A) and similar proteins; KMT2A (EC2.1.1.43; also termed lysine N-methyltransferase 2A, ALL-1, CXXC-type zinc finger protein 7 (CXXC7), myeloid/lymphoid or mixed-lineage leukemia (MLL), myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), trithorax-like protein (TRX1), or zinc finger protein HRX) acts as a histone methyltransferase that plays an essential role in early development and hematopoiesis. It is a catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac).


Pssm-ID: 380983 [Multi-domain]  Cd Length: 154  Bit Score: 79.30  E-value: 1.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 236 RVVQKGIRYDLCIFRTN-DGRGWGVRtlEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQG-ATYLFDLDyveDVYTVDA 313
Cdd:cd19206    6 RHLKKTSKEAVGVYRSPiHGRGLFCK--RNIDAGEMVIEYSGNVIRSILTDKREKYYDSKGiGCYMFRID---DSEVVDA 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 314 AYYGNISHFVNHSCDPNLQVYNVFIDNLDErlprIAFFATRTIWAGEELTFDYNMQVDPA 373
Cdd:cd19206   81 TMHGNAARFINHSCEPNCYSRVINIDGQKH----IVIFAMRKIYRGEELTYDYKFPIEDA 136
SET_SETD5-like cd10529
SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine ...
258-368 1.13e-15

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: 73.08  E-value: 1.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 258 GVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDR-QGATYLFDLDYVEDVYtVDAAYYGNISHFVNHSCDPNLQVYNV 336
Cdd:cd10529   18 GLVATEDISPGEPILEYKGEVSLRSEFKEDNGFFKRpSPFVFFYDGFEGLPLC-VDARKYGNEARFIRRSCRPNAELRHV 96
                         90       100       110
                 ....*....|....*....|....*....|....
gi 755564482 337 FIDNldERLpRIAFFATRTIWAGEELT--FDYNM 368
Cdd:cd10529   97 VVSN--GEL-RLFIFALKDIRKGTEITipFDYDY 127
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
44-92 2.82e-15

CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this group are chromodomains or chromo shadow domains; these are SH3-fold-beta-barrel domains of the chromo-like superfamily. Chromodomains lack the first strand of the SH3-fold-beta-barrel, this first strand is altered by insertion in the chromo shadow domains. The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. Chromodomain-containing proteins include: i) those having an N-terminal chromodomain followed by a related chromo shadow domain, such as Drosophila and human heterochromatin protein Su(var)205 (HP1), and mammalian modifier 1 and 2; ii) those having a single chromodomain, such as Drosophila protein Polycomb (Pc), mammalian modifier 3, human Mi-2 autoantigen, and several yeast and Caenorhabditis elegans proteins of unknown function; iii) those having paired tandem chromodomains, such as mammalian DNA-binding/helicase proteins CHD-1 to CHD-4 and yeast protein CHD1; (iv) and elongation factor eEF3, a member of the ATP-binding cassette (ABC) family of proteins, that serves an essential function in the translation cycle of fungi. eEF3 is a soluble factor lacking a transmembrane domain and having two ABC domains arranged in tandem, with a unique chromodomain inserted within the ABC2 domain.


Pssm-ID: 349274 [Multi-domain]  Cd Length: 50  Bit Score: 69.43  E-value: 2.82e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 755564482  44 FEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLK-CIRVLKQFHK 92
Cdd:cd00024    1 YEVEKILDHRVRKGKLEYLVKWKGYPPEENTWEPEENLTnAPELIKEYEK 50
SET_KMT2D cd19209
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) ...
255-377 2.63e-14

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2D (KMT2D) and similar proteins; KMT2D (EC2.1.1.43; also termed lysine N-methyltransferase 2D, ALL1-related protein (ALR), or myeloid/lymphoid or mixed-lineage leukemia protein 2 (MLL2)), acts as histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me). It is a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription. KMT2D is a subunit of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation.


Pssm-ID: 380986 [Multi-domain]  Cd Length: 155  Bit Score: 70.11  E-value: 2.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 255 RGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQG-ATYLFDLDyveDVYTVDAAYYGNISHFVNHSCDPNLQV 333
Cdd:cd19209   26 QGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNrGIYMFRIN---NEHVIDATLTGGPARYINHSCAPNCVA 102
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755564482 334 YNVFIDNLDerlpRIAFFATRTIWAGEELTFDYNMQVD------PAH-GLW 377
Cdd:cd19209  103 EVVTFDKED----KIIIISSRRIPKGEELTYDYQFDFEddqhkiPCHcGAW 149
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
44-92 3.53e-14

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 66.45  E-value: 3.53e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755564482   44 FEVEYLCDYKKIREQ-EYYLVKWRGYPDSENTWEPRQNL-KCIRVLKQFHK 92
Cdd:pfam00385   1 YEVERILDHRKDKGGkEEYLVKWKGYPYDENTWEPEENLsKCPELIEEFKD 51
SET_SETD1A cd19204
SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and ...
257-371 1.15e-13

SET domain (including post-SET domain) found in SET domain-containing protein 1A (SETD1A) and similar proteins; SETD1A (EC2.1.1.43), also termed lysine N-methyltransferase 2F, or Set1/Ash2 histone methyltransferase complex subunit SET1, is a histone-lysine N-methyltransferase that specifically methylates 'Lys-4' of histone H3 (H3K4me), when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. Human SET domain containing protein 1A (hSETD1A) expression occurs at a high rate in hepatocellular carcinoma patients and controls tumor metastasis in breast cancer by activating MMP expression.


Pssm-ID: 380981 [Multi-domain]  Cd Length: 153  Bit Score: 68.13  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 257 WGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQ--GATYLFDLDYVEdvyTVDAAYYGNISHFVNHSCDPNLQVY 334
Cdd:cd19204   26 WGLFAMEPIAADEMVIEYVGQNIRQVVADMREKRYVQEgiGSSYLFRVDHDT---IIDATKCGNLARFINHCCTPNCYAK 102
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 755564482 335 NVFIdnldERLPRIAFFATRTIWAGEELTFDYNMQVD 371
Cdd:cd19204  103 VITI----ESQKKIVIYSKQPIGVNEEITYDYKFPIE 135
SET_KMT2C cd19208
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) ...
255-371 1.69e-13

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C) and similar proteins; KMT2C (EC2.1.1.43; also termed lysine N-methyltransferase 2C, homologous to ALR protein (HALR) myeloid/lymphoid, or mixed-lineage leukemia protein 3 (MLL3)), acts as a histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me) and may be involved in leukemogenesis and developmental disorder. KMT2C is a catalytic subunit of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation. Overexpression of KMT2C is associated with estrogen receptor-positive breast cancer; KMT2C mediates the estrogen dependence of breast cancer through regulation of estrogen receptor alpha (ERalpha) enhancer function. KMT2C is frequently mutated in certain populations with diffuse-type gastric adenocarcinomas (DGA); its loss promotes epithelial-to-mesenchymal transition (EMT) and is associated with worse overall survival.


Pssm-ID: 380985 [Multi-domain]  Cd Length: 154  Bit Score: 67.73  E-value: 1.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 255 RGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQG-ATYLFDLDyveDVYTVDAAYYGNISHFVNHSCDPNLQV 333
Cdd:cd19208   25 QGLGLYAARDIEKHTMVIEYIGTIIRNEVANRKEKLYESQNrGVYMFRID---NDHVIDATLTGGPARYINHSCAPNCVA 101
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 755564482 334 YNVFIdnldERLPRIAFFATRTIWAGEELTFDYNMQVD 371
Cdd:cd19208  102 EVVTF----EKGHKIIISSSRRIQKGEELCYDYKFDFE 135
SET_KMT2B cd19207
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) ...
256-373 2.96e-13

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2B (KMT2B) and similar proteins; KMT2B (EC2.1.1.43; also termed lysine N-methyltransferase 2B, myeloid/lymphoid or mixed-lineage leukemia protein 4 (MLL2/MLL4), trithorax homolog 2 (TRX2), or WW domain-binding protein 7 (WBP-7)), acts as a histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me). It is required during the transcriptionally active period of oocyte growth for the establishment and/or maintenance of bulk H3K4 trimethylation (H3K4me3), global transcriptional silencing that precedes resumption of meiosis, oocyte survival and normal zygotic genome activation.


Pssm-ID: 380984 [Multi-domain]  Cd Length: 154  Bit Score: 66.97  E-value: 2.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 256 GWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQG-ATYLFDLDyveDVYTVDAAYYGNISHFVNHSCDPNLQVY 334
Cdd:cd19207   25 GRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDSKGiGCYMFRID---DFDVVDATMHGNAARFINHSCEPNCYSR 101
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 755564482 335 NVFIdnldERLPRIAFFATRTIWAGEELTFDYNMQVDPA 373
Cdd:cd19207  102 VIHV----EGQKHIVIFALRKIYRGEELTYDYKFPIEDA 136
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
319-367 7.60e-13

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: 63.42  E-value: 7.60e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 755564482 319 ISHFVNHSCDPNLQVYNVFIDnldeRLPRIAFFATRTIWAGEELTFDYN 367
Cdd:cd08161   28 LARFINHSCEPNCEFEEVYVG----GKPRVFIVALRDIKAGEELTVDYG 72
SET_SETD1B cd19205
SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...
257-371 3.33e-12

SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and similar proteins; SETD1B (EC2.1.1.43), also termed lysine N-methyltransferase 2G, is a histone-lysine N-methyltransferase that specifically methylates 'Lys-4' of histone H3 (H3K4me) when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. Loss of SETD1B occurs in up to half the gastric and colorectal cancers, most commonly via SETD1B mutations, while de novo variants in SETD1B are associated with intellectual disability, epilepsy and autism.


Pssm-ID: 380982 [Multi-domain]  Cd Length: 153  Bit Score: 63.92  E-value: 3.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 257 WGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQG--ATYLFDLDYVEdvyTVDAAYYGNISHFVNHSCDPNLQVY 334
Cdd:cd19205   26 WGLFAMEPIAADEMVIEYVGQNIRQVIADMREKRYEDEGigSSYMFRVDHDT---IIDATKCGNFARFINHSCNPNCYAK 102
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 755564482 335 NVFIdnldERLPRIAFFATRTIWAGEELTFDYNMQVD 371
Cdd:cd19205  103 VITV----ESQKKIVIYSKQHINVNEEITYDYKFPIE 135
chromodomain cd18968
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
43-90 8.11e-12

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349324  Cd Length: 57  Bit Score: 60.05  E-value: 8.11e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755564482  43 DFEVEYLC-----DYKKIREQEY-YLVKWRGYPDSENTWEPRQNLK-CIRVLKQF 90
Cdd:cd18968    1 EYEVEVILaarvvKDAESRKKGWkYLVKWAGYPDEENTWEPEESFDgCDDLLERF 55
CHROMO smart00298
Chromatin organization modifier domain;
43-93 2.79e-11

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 58.38  E-value: 2.79e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 755564482    43 DFEVEYLCDYKKIREQEY-YLVKWRGYPDSENTWEPRQNLK-CIRVLKQFHKD 93
Cdd:smart00298   1 EYEVEKILDHRWKKKGELeYLVKWKGYSYSEDTWEPEENLLnCSKKLDNYKKK 53
CD_HP1a_insect cd18653
chromodomain of insect HP1a; CHRomatin Organization Modifier (chromo) domain of insect HP1a. ...
43-90 3.62e-11

chromodomain of insect HP1a; CHRomatin Organization Modifier (chromo) domain of insect HP1a. HP1a is a member of the heterochromatin protein family, and is enriched in the heterochromatin and associated with centromeres. HP1 has diverse functions in heterochromatin formation and impacts both gene expression and gene silencing. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. In Drosophila, there are at least five HP1 family proteins, this subgroup includes the CD of Drosophila melanogaster HP1a.


Pssm-ID: 349300  Cd Length: 50  Bit Score: 58.12  E-value: 3.62e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 755564482  43 DFEVEYLCDyKKIREQ--EYYLvKWRGYPDSENTWEPRQNLKCIRVLKQF 90
Cdd:cd18653    1 EYAVEKICD-RRVRKGkvEYYL-KWKGYPETENTWEPEENLDCQDLIQQY 48
CD_MarY1_POL_like cd18975
chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes ...
44-92 4.21e-11

chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in the polyprotein from the MarY1 Ty3/Gypsy long terminal repeat (LTR) retroelement from the from the Ectomycorrhizal Basidiomycete Tricholoma matsutake. The pol gene in TY3/gypsy elements generally encodes domains in the following order: prt-reverse transcriptase-RNase H-integrase, in marY1 POL the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349331  Cd Length: 49  Bit Score: 57.94  E-value: 4.21e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 755564482  44 FEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCIRVLKQFHK 92
Cdd:cd18975    1 YEVESILNSRLHRGKLQYLIQWKGYPLEEASWELEDNIKNPRLIEEFHK 49
CD_POL_like cd18974
chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the ...
44-92 1.79e-10

chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Penicillium solitum protein PENSOL_c198G03123 a putative polyprotein from a Ty3/Gypsy long terminal repeat (LTR) retroelement. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349330  Cd Length: 50  Bit Score: 55.95  E-value: 1.79e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 755564482  44 FEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLK-CIRVLKQFHK 92
Cdd:cd18974    1 WEVEEIVDEKMIDDELHYLVKWKGWPAEYNQWEPEDDMEnAPKAIQSYEK 50
CD_HP1_like cd18960
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
44-92 2.72e-10

chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; uncharacterized subgroup; CHRomatin Organization Modifier (chromo) domain of mammalian HP1alpha (Cbx5), HP1beta (Cbx1), HP1gamma (Cbx5), and similar proteins. HP1 has diverse functions in heterochromatin formation and impacts both gene expression and gene silencing. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3).


Pssm-ID: 349316  Cd Length: 51  Bit Score: 55.64  E-value: 2.72e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 755564482  44 FEVEYLCDYKKIRE-QEYYLVKWRGYPDSENTWEPRQNLKCIRVLKQFHK 92
Cdd:cd18960    2 FVVERILDKRLGRNgGEEFLIKWQGFPESDSSWEPRENLQCDEMLEEFEK 51
CD_Tf2-1_POL_like cd18973
chromodomain of Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type ...
44-92 3.56e-10

chromodomain of Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type 1, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type 1 (Tf2-1), and similar proteins. It belongs to the Ty3/gypsy family of long terminal repeat (LTR) retrotransposons. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349329  Cd Length: 50  Bit Score: 55.33  E-value: 3.56e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 755564482  44 FEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLK-CIRVLKQFHK 92
Cdd:cd18973    1 YVVEAILDNKRRKGKWLYLVKWKGYGPEHNTWEPRENLEhAQKLLKKYYQ 50
CD_HP1_like cd18631
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
43-92 4.45e-10

chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; CHRomatin Organization Modifier (chromo) domain of mammalian HP1alpha (Cbx5), HP1beta (Cbx1), HP1gamma (Cbx5), and similar proteins. HP1 has diverse functions in heterochromatin formation and impacts both gene expression and gene silencing. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3).


Pssm-ID: 349281  Cd Length: 50  Bit Score: 54.75  E-value: 4.45e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 755564482  43 DFEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCIRVLKQFHK 92
Cdd:cd18631    1 EYVVEKVLDRRVVKGKVEYLLKWKGYPDEDNTWEPEENLDCPDLIAEFEE 50
CD_POL_like cd18976
chromodomain of uncharacterized putative retroelement polyprotein proteins; This subgroup ...
46-90 1.09e-09

chromodomain of uncharacterized putative retroelement polyprotein proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in uncharacterized putative retrotransposon proteins, and similar proteins. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349332  Cd Length: 51  Bit Score: 53.72  E-value: 1.09e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 755564482  46 VEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNL--KCIRVLKQF 90
Cdd:cd18976    3 VESLLDRRKVRGQVQYLVKWRGFPRSEATWEPREELmrRCAELVAAY 49
CD_HP1alpha_Cbx5 cd18651
chromodomain of heterochromatin protein 1 homolog alpha; CHRomatin Organization Modifier ...
43-92 3.42e-09

chromodomain of heterochromatin protein 1 homolog alpha; CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 homolog alpha (also known as HP1alpha, Cbx5, and Chromobox 5), and related proteins. HP1alpha has diverse functions in heterochromatin formation, gene regulation, and mitotic progression, and forms complex networks of gene, RNA, and protein interactions. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha, HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3).


Pssm-ID: 349298  Cd Length: 50  Bit Score: 52.30  E-value: 3.42e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 755564482  43 DFEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCIRVLKQFHK 92
Cdd:cd18651    1 EYVVEKVLDRRVVKGQVEYLLKWKGFSEEHNTWEPEKNLDCPELISEFMK 50
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
44-81 3.93e-09

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349322  Cd Length: 49  Bit Score: 52.28  E-value: 3.93e-09
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 755564482  44 FEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNL 81
Cdd:cd18966    1 YEVERILAERRDDGGKRYLVKWEGYPLEEATWEPEENI 38
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
248-367 3.97e-09

SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces pombe Set7 is a novel histone-lysine N-methyltransferase. The family also includes a viral histone H3 lysine 27 methyltransferase from Paramecium bursaria Chlorella virus 1 (PBCV-1).


Pssm-ID: 380938  Cd Length: 112  Bit Score: 54.18  E-value: 3.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 248 IFRTNDGRGWGVRTLEKIRKNSFVmEYVGEIITSEEaERRGQIYdrqgaTYLFDLDYV-EDVYTVDAAYYGniSHFvNHS 326
Cdd:cd10540    3 EVKPSTLKGRGVFATRPIKKGEVI-EEAPVIVLPKE-EYQHLCK-----TVLDHYVFSwGDGCLALALGYG--SMF-NHS 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 755564482 327 CDPNLQVYnvfidnLDERLPRIAFFATRTIWAGEELTFDYN 367
Cdd:cd10540   73 YTPNAEYE------IDFENQTIVFYALRDIEAGEELTINYG 107
chromodomain cd18965
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
46-96 7.64e-09

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349321  Cd Length: 53  Bit Score: 51.32  E-value: 7.64e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755564482  46 VEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCIRVLKQFHKDLER 96
Cdd:cd18965    3 IEALLKKRQFNRKLEYLVKWHGLPESENTWEREKDIKHVSHWKQLLKDLRA 53
CD_HP1gamma_Cbx3 cd18652
chromodomain of heterochromatin protein 1 homolog gamma; CHRomatin Organization Modifier ...
43-90 1.03e-08

chromodomain of heterochromatin protein 1 homolog gamma; CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 homolog gamma (also known as HP1gamma, Cbx3, and Chromobox 3), and related proteins. HP1gamma is a highly conserved non-histone protein, which is a member of the heterochromatin protein family, and is enriched in the heterochromatin and associated with centromeres. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. In addition to being involved in transcriptional silencing in heterochromatin-like complexes, HP1gamma also binds lamin B receptor, an integral membrane protein found in the inner nuclear membrane. The dual binding functions of the protein may explain the association of heterochromatin with the inner nuclear membrane. HP1gamma is also recruited to sites of ultraviolet-induced DNA damage and double-strand breaks. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma.


Pssm-ID: 349299  Cd Length: 50  Bit Score: 51.16  E-value: 1.03e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 755564482  43 DFEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCIRVLKQF 90
Cdd:cd18652    1 EFVVEKVLDRRVVNGKVEYFLKWKGFTDADNTWEPEENLDCPELIEAF 48
CD_HP1beta_Cbx1 cd18650
chromodomain of heterochromatin protein 1 homolog beta; CHRomatin Organization Modifier ...
43-90 1.19e-08

chromodomain of heterochromatin protein 1 homolog beta; CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 homolog beta (also known as HP1beta, CBX1, and chromobox 1), and related proteins. HP1beta is a highly conserved non-histone protein, which is a member of the heterochromatin protein family, and is enriched in the heterochromatin and associated with centromeres. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta, and HP1gamma (also known as Cbx3).


Pssm-ID: 349297  Cd Length: 50  Bit Score: 50.71  E-value: 1.19e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 755564482  43 DFEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCIRVLKQF 90
Cdd:cd18650    1 EYVVEKVLDRRVVKGKVEYLLKWKGFSDEDNTWEPEENLDCPDLIAEF 48
CD_EhHp1_like cd18638
chromodomain of Entamoeba histolytica heterochromatin protein 1, and similar proteins; This ...
44-92 2.86e-08

chromodomain of Entamoeba histolytica heterochromatin protein 1, and similar proteins; This subgroup includes the N-terminal CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 (HP1)-like protein from Entamoeba histolytica, and similar proteins. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349288  Cd Length: 52  Bit Score: 49.95  E-value: 2.86e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755564482  44 FEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLK--CIRVLKQFHK 92
Cdd:cd18638    2 FEVEKIVKKKTVKGGTEYFVKWKGYSAKENTWETEDNLEksYKEMIDEFEK 52
CD_DDE_transposase_like cd18978
chromodomain of Rhizopus microsporus putative DDE transposases, and similar proteins; This ...
43-92 3.07e-08

chromodomain of Rhizopus microsporus putative DDE transposases, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Rhizopus microsporus putative DDE transposases, and similar proteins. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349334  Cd Length: 52  Bit Score: 49.62  E-value: 3.07e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 755564482  43 DFEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCIRVLKQFHK 92
Cdd:cd18978    3 SYEVEKIINHRGEKNRRKYLVKWKGYDDTDNSWVTQEDFNDKDMIDEYEN 52
CD_NC-like cd18980
chromodomain of a Tasahii var. asahii CBS 8904 retrotransposon nucleocapsid protein, and ...
43-91 4.11e-08

chromodomain of a Tasahii var. asahii CBS 8904 retrotransposon nucleocapsid protein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Trichosporon asahii var. asahii CBS 8904 retrotransposon nucleocapsid protein, and similar proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349336  Cd Length: 56  Bit Score: 49.49  E-value: 4.11e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755564482  43 DFEVEYLCDYK---KIREQEYYLVKWRGYPDSENTWEPRQNLK-CIRVLKQFH 91
Cdd:cd18980    3 EYEVEAILDHKvdrRYRDPNFYLVRWRGYGPSHDSWEPTSALEnAQDLLREFW 55
CD_POL_like cd18972
chromodomain of a Moniliophthora perniciosa FA553 putative retrotransposon polyprotein, and ...
44-92 4.37e-08

chromodomain of a Moniliophthora perniciosa FA553 putative retrotransposon polyprotein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in a Moniliophthora perniciosa FA553 putative retrotelement polyprotein, which includes domains in the following order: a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related "chromo shadow" domain


Pssm-ID: 349328  Cd Length: 50  Bit Score: 49.43  E-value: 4.37e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 755564482  44 FEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLK-CIRVLKQFHK 92
Cdd:cd18972    1 YEVEAIVGHKPKKKPRQFLVSWLGYDSSHNEWKQKEELEnARELLQDYLK 50
SET_SpSET3-like cd19183
SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET ...
265-380 1.47e-07

SET domain (including post-SET domain) found in Schizosaccharomyces pombe SET domain-containing protein 3 (SETD3) and similar proteins; Schizosaccharomyces pombe SETD3 functions as a transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. It is required for both, gene activation and repression.


Pssm-ID: 380960  Cd Length: 173  Bit Score: 51.25  E-value: 1.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 265 IRKNSFVMEYVGEIITSEE--AERRGQiYDRQGATYLFDLDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLd 342
Cdd:cd19183   22 IPAGDPIQELLGEIGLQSEyiADPENQ-YQILGAPKPHVFFHPQSPLYIDTRRSGSVARFIRRSCRPNAELVTVASDSG- 99
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 755564482 343 eRLPRIAFFATRTIWAGEELTFDYnmQVDPAHGLWVPI 380
Cdd:cd19183  100 -SVLKFVLYASRDISPGEEITIGW--DWDNPHPFRRFA 134
SET_SETD5 cd19181
SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and ...
259-373 4.10e-07

SET domain (including post-SET domain) found in SET domain-containing protein 5 (SETD5) and similar proteins; SETD5 is a probable transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. SETD5 loss-of-function mutations are a likely cause of a familial syndromic intellectual disability with variable phenotypic expression.


Pssm-ID: 380958  Cd Length: 150  Bit Score: 49.24  E-value: 4.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 259 VRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFI 338
Cdd:cd19181   21 LRAARDLALDTLIIEYRGKVMLRQQFEVNGHFFKRPYPFVLFYSKFNGVEMCVDARTFGNDARFIRRSCTPNAEVRHMIA 100
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 755564482 339 DNlderLPRIAFFATRTIWAGEELT--FDY-----NMQVDPA 373
Cdd:cd19181  101 DG----MIHLCIYAVAAIAKDAEVTiaFDYeysncNYKVDCA 138
CD_MMP8 cd18633
chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), ...
44-92 9.53e-07

chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), a component of the RanBPM-containing large protein complex, binds methylated H3K9. This may in turn recruit the H3K9 methyltransferases GLP and ESET, and DNA methyltransferase 3A to the promoter of the E-cadherin gene, mediating the E-cadherin gene silencing and promoting tumor cell motility and invasion. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349283  Cd Length: 51  Bit Score: 45.35  E-value: 9.53e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 755564482  44 FEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLK-CIRVLKQFHK 92
Cdd:cd18633    2 FEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEVHLEdCKEVLLEFRK 51
CD_Rhino cd18630
chromodomain of Drosophila melanogaster Rhino, and similar proteins; N-terminal CHRomatin ...
61-90 1.09e-06

chromodomain of Drosophila melanogaster Rhino, and similar proteins; N-terminal CHRomatin Organization Modifier (chromo) domain of Drosophila melanogaster Rhino (also known as heterochromatin protein 1-like), and similar proteins. Rhino is a female-specific protein that affects chromosome structure and egg polarity that is required for germline PIWI-interacting RNA (piRNA) production. In Drosophila the RDC (rhino, deadlock, and cutoff) complex, composed of rhino, the protein deadlock (Del) and the Rai1-like transcription termination cofactor cutoff (Cuff) binds to chromatin of dual-strand piRNA clusters, special genomic regions, which encode piRNA precursors. The RDC complex is anchored to H3K9me3-marked chromatin in part via the H3K9me3-binding activity of Rhino, and is required for transcription of piRNA precursors. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349280  Cd Length: 51  Bit Score: 45.20  E-value: 1.09e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 755564482  61 YLVKWRGYPDSENTWEPRQNL-KCIRVLKQF 90
Cdd:cd18630   19 VLVKWSGFPNENNTWEPLENLgNCMKLVADY 49
CD_Clr4_like cd18632
N-terminal chromodomain of the fission yeast histone methyltransferase Clr4, and similar ...
43-90 1.32e-06

N-terminal chromodomain of the fission yeast histone methyltransferase Clr4, and similar proteins; N-terminal CHRomatin Organization Modifier (chromo) domain of cryptic loci regulator 4 (Clr4), a histone H3 lysine methyltransferase which targets H3K9. Clr4 regulates silencing and switching at the mating-type loci and affects chromatin structure at centromeres. Clr4 is a catalytic component of the rik1-associated E3 ubiquitin ligase complex that shows ubiquitin ligase activity and is required for histone H3K9 methylation. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349282  Cd Length: 55  Bit Score: 45.19  E-value: 1.32e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755564482  43 DFEVEYLCDYKKIRE--QEYYLVKWRGYPDSENTWEPRQNLK-CIRVLKQF 90
Cdd:cd18632    1 EYEVEKIVDEKTDRNtaEPLYLVRWKNYSKNHDTWEPAENLSgCQAVLEKW 51
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
248-374 1.77e-06

SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing protein, and similar proteins; The family includes SET and MYND domain-containing proteins, SMYD1-SYMD5. SMYD1 (EC 2.1.1.43; also termed BOP) is a heart and muscle specific SET-MYND domain containing protein, which functions as a histone methyltransferase and regulates downstream gene transcription. It methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. SMYD2 (also termed HSKM-B, or lysine N-methyltransferase 3C (KMT3C)) functions as a histone methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. It specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). SMYD3 (also termed zinc finger MYND domain-containing protein 1) functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex. SMYD4 functions as a potential tumor suppressor that plays a critical role in breast carcinogenesis at least partly through inhibiting the expression of PDGFR-alpha. SMYD5 (also termed protein NN8-4AG, or retinoic acid-induced protein 15) functions as histone lysine methyltransferase that mediates H4K20me3 at heterochromatin regions.


Pssm-ID: 380997 [Multi-domain]  Cd Length: 122  Bit Score: 46.60  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 248 IFRTNDGRGWGVRTLEKIRKnsfvmeyvGEIITSEEAErrgqIYDRQGATYLFDLDYVEDVytvdaAYYGNISHFvNHSC 327
Cdd:cd20071    2 VRESEGSKGRGLVATRDIEP--------GELILVEKPL----VSVPSNSFSLTDGLNEIGV-----GLFPLASLL-NHSC 63
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 755564482 328 DPNLQVynVFIDNlderlPRIAFFATRTIWAGEELTFDYNMQVDPAH 374
Cdd:cd20071   64 DPNAVV--VFDGN-----GTLRVRALRDIKAGEELTISYIDPLLPRT 103
SET_KMT2E cd19182
SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar ...
268-367 2.34e-06

SET domain found in inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar proteins; KMT2E (also termed inactive lysine N-methyltransferase 2E, myeloid/lymphoid or mixed-lineage leukemia protein 5 (MLL5)) plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. It associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription. Lack of key residues in the SET domain as well as the presence of an unusually large loop in the SET-I subdomain preclude the interaction of MLL5 SET with its cofactor and substrate thus making MLL5 devoid of any in vitro methyltransferase activity on full-length histones and histone H3 peptide.


Pssm-ID: 380959  Cd Length: 129  Bit Score: 46.81  E-value: 2.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 268 NSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVfidnLDERLPR 347
Cdd:cd19182   30 DTLIIEYRGKFMLREQFEANGYFFKRPYPFVLFYSKFHGLEMCVDARTFGNEARFIRRSCTPNAEVRHV----IEDGTIH 105
                         90       100
                 ....*....|....*....|..
gi 755564482 348 IAFFATRTIWAGEELT--FDYN 367
Cdd:cd19182  106 LYIYSIRSIPKGTEITiaFDFD 127
CD_Cbx2 cd18647
chromodomain of chromobox homolog 2; CHRomatin Organization Modifier (chromo) domain of ...
44-92 2.36e-06

chromodomain of chromobox homolog 2; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 2 (CBX2), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells.


Pssm-ID: 349294  Cd Length: 53  Bit Score: 44.66  E-value: 2.36e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 755564482  44 FEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCIRVLKQFHK 92
Cdd:cd18647    4 FAAECILSKRLRKGKLEYLVKWRGWSSKHNSWEPEENILDPRLLLAFQK 52
CD_polycomb_like cd18627
chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier ...
53-92 2.40e-06

chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier (chromo) domain of Polycomb and Polycomb-group (PcG) chromobox (CBX) family proteins such as CBX2, CBX4, CBX6, CBX7, and CBX8. These CBX proteins are components of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells.


Pssm-ID: 349277  Cd Length: 49  Bit Score: 44.30  E-value: 2.40e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 755564482  53 KKIRE-QEYYLVKWRGYPDSENTWEPRQNLKCIRVLKQFHK 92
Cdd:cd18627    9 KRIRKgKVEYLVKWKGWSQKYNTWEPEENILDPRLLAAFES 49
CD_CDY cd18634
chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain ...
44-92 3.16e-06

chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain found in the mammalian chromodomain Y-like (CDY) protein family, and similar proteins. The human CDY family includes 6 proteins: the genes encoding four of these: two copies of CDY1 (CDY1a, CDY1a) and two copies of CDY2(CDY2a and CDY2b), are located on chromosome Y, and the genes encoding the other two members (CDYL and CDYL2) are located on autosomes. The chromosomal genes are only present in primates, whereas the CDYL and CDYL2 genes exist in most mammalian species. The CDY family proteins contain two functional domains: a chromodomain involved in chromatin binding and a catalytic domain found in many coenzyme A (CoA)- dependent acylation enzymes. CDYL is ubiquitously expressed, whereas CDYL2 shows selective expression in tissues of testis, prostate, spleen, and leukocyte. The CDYL genes are ubiquitously expressed, the CDY genes are only expressed in the testis. Deletion of the CDY1b gene has been shown to be a risk factor for male infertility. Impairments in CDY2 expression could be implicated in the pathogenesis of maturation arrest (a failure of germ cell development).


Pssm-ID: 349284  Cd Length: 52  Bit Score: 43.97  E-value: 3.16e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755564482  44 FEVEYLCDYKKIREQEY-YLVKWRGYPDSENTWEPRQNLK-CIRVLKQFHK 92
Cdd:cd18634    2 YEVERIVDKRKNKKGKTeYLVRWKGYDSEDDTWEPEQHLLnCEEFIHDFNR 52
CD_CMT3_like cd18635
chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier ...
44-90 4.63e-06

chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier (chromo) domain of DNA (cytosine-5)-methyltransferase chromomethylase 3 (CMT3, EC:2.1.1.37), and similar proteins. CMT3 is primarily a CHG (where H is either A, T or C) methyltransferase and is predominantly expressed in actively replicating cells. The protein is involved in preferentially methylating transposon-related sequences, reducing their mobility. Studies suggest that in order to target DNA methylation, CMT3 associates with H3K9me2-containing nucleosomes through binding of its BAH- and chromo-domains to H3K9me2. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349285  Cd Length: 57  Bit Score: 43.84  E-value: 4.63e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755564482  44 FEVEYLCDYKKIREQE------YYLVKWRGYPDSENTWEPRQNL-KCIRVLKQF 90
Cdd:cd18635    2 FEVEKLVGICYGDPKKtgerglYFKVRWKGYGPEEDTWEPIEGLsNCPEKIKEF 55
CD_polycomb cd18644
chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG ...
44-92 7.48e-06

chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG (polycomb-group) chromodomain protein Polycomb (Pc) from Drosophila melanogaster, anthropod, worm, and sea cucumber, and similar proteins. Pc is a component of the Polycomb-group (PcG) multiprotein PRC1 complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. The core subunits of PRC1 are polycomb (Pc), polyhomeotic (Ph), posterior sex combs (Psc), and sex comb extra (Sce, also known as dRing). Polycomb (Pc) plays a role in modulating life span in flies, it negatively regulates longevity.


Pssm-ID: 349291  Cd Length: 54  Bit Score: 43.22  E-value: 7.48e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 755564482  44 FEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCIRVLKQFHK 92
Cdd:cd18644    4 YAAEKILKKRVRKGKVEYLVKWKGWSNKHNTWEPEENILDRRLIEIFER 52
CD_POL_like cd18971
chromodomain of a Magnaporthe grisea putative retrotransposon polyprotein, and similar ...
44-90 1.58e-05

chromodomain of a Magnaporthe grisea putative retrotransposon polyprotein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in a Magnaporthe grisea putative retrotransposon polyprotein which includes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349327  Cd Length: 50  Bit Score: 42.00  E-value: 1.58e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 755564482  44 FEVEYLCDYKKIREQEY---YLVKWRGYpdSENTWEPRQNLKCIRVLKQF 90
Cdd:cd18971    1 YEVEEILAARRRRIRGKgreVLVKWVGY--AEPTWEPLDNLADTAALDRF 48
chromodomain cd18964
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
52-92 3.00e-05

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349320  Cd Length: 54  Bit Score: 41.16  E-value: 3.00e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 755564482  52 YKKIREQEY-YLVKWRGYPDSENTWEPRQNL-KCIRVLKQFHK 92
Cdd:cd18964   12 SARDGPGKFlWLVKWDGYPIEDATWEPPENLgEHAKLIEDFEK 54
CD_MT_like cd18962
chromodomain of a putative Coemansia reversa NRRL 1564 methyltransferase, and similar proteins; ...
46-92 4.17e-05

chromodomain of a putative Coemansia reversa NRRL 1564 methyltransferase, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in a Coemansia reversa NRRL 1564 SET (Su(var)3-9, enhancer-of-zeste, trithorax) domain-containing protein, and similar proteins. The SU(VAR)3-9 protein is the main chromocenter-specific histone H3-K9 methyltransferase (HMTase) in Drosophila where it plays a role in heterochromatic gene silencing. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349318  Cd Length: 52  Bit Score: 41.01  E-value: 4.17e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 755564482  46 VEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCIRVLKQFHK 92
Cdd:cd18962    6 VEAIVNDVLIDGKHMYEVKWEGYPSDHNNWVAEWDLNDKEILRKYNK 52
chromodomain cd18969
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; for most members ...
43-75 4.33e-05

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; for most members of this subgroup, the chromodomain is followed by a chromo shadow domain; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain. For the majority of members of this subgroup, the chromodomain is followed by a chromo shadow domain (CSD).


Pssm-ID: 349325  Cd Length: 56  Bit Score: 40.97  E-value: 4.33e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 755564482  43 DFEVEYL--CDYKKIREQEY-YLVKWRGYPDSENTW 75
Cdd:cd18969    3 EYEIEEIldVKKGGFEDGKLaYFVKWKGYPSSENSW 38
CD_Cbx4 cd18645
chromodomain of chromobox homolog 4; CHRomatin Organization Modifier (chromo) domain of ...
44-91 6.78e-05

chromodomain of chromobox homolog 4; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 4 (CBX4), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells. In addition to a chromodomain with H3K27me3-binding activity, Cbx4 contains two SUMO-interacting motifs responsible for its small ubiquitin-related modifier (SUMO) E3 ligase activity. CBX proteins may act as an oncogene or tumor suppressor in a cell-type-dependent manner, for example CBX8 promotes proliferation while suppressing metastasis, in colorectal carcinoma progression. CBX4 may serve as a tumor suppressor in colorectal carcinoma, and has been shown to be an oncogene in osteosarcoma and breast cancer.


Pssm-ID: 349292  Cd Length: 55  Bit Score: 40.43  E-value: 6.78e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 755564482  44 FEVEYLcDYKKIREQEY-YLVKWRGYPDSENTWEPRQNLKCIRVLKQFH 91
Cdd:cd18645    4 FAVESI-EKKRIRKGRVeYLVKWRGWSPKYNTWEPEENILDPRLLIAFQ 51
CD_Chro-like cd18640
chromodomain of Drosophila melanogaster chromator chromodomain protein, and similar proteins; ...
61-92 9.45e-05

chromodomain of Drosophila melanogaster chromator chromodomain protein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in chromodomain of Drosophila melanogaster chromator (also known as Chriz/Chro) chromodomain protein, and similar proteins. Chromator is a nuclear protein that plays a role in proper spindle dynamics during mitosis. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349290  Cd Length: 52  Bit Score: 39.97  E-value: 9.45e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 755564482  61 YLVKWRGYPDSENTWEPRQNL-KCIRVLKQFHK 92
Cdd:cd18640   20 YLVKWENRSHHENTWEPMANLeRCKYLLQMFEK 52
SET_SMYD4 cd10536
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
313-366 2.67e-04

SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing protein 4 (SMYD4) and similar proteins; SMYD4 functions as a potential tumor suppressor that plays a critical role in breast carcinogenesis at least partly through inhibiting the expression of PDGFR-alpha. In zebrafish, SMYD4 is ubiquitously expressed in early embryos and becomes enriched in the developing heart; mutants show a strong defect in cardiomyocyte proliferation, which lead to a severe cardiac malformation.


Pssm-ID: 380934 [Multi-domain]  Cd Length: 218  Bit Score: 41.90  E-value: 2.67e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755564482 313 AAYYGNIShFVNHSCDPNlqVYNVFIDNLderlprIAFFATRTIWAGEELTFDY 366
Cdd:cd10536  145 TAIYPTLS-LLNHSCDPN--TIRSFYGNT------IVVRATRPIKKGEEITICY 189
CD_Cbx6 cd18648
chromodomain of chromobox homolog 6; CHRomatin Organization Modifier (chromo) domain of ...
53-97 4.55e-04

chromodomain of chromobox homolog 6; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 6 (CBX6), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells.


Pssm-ID: 349295  Cd Length: 58  Bit Score: 38.11  E-value: 4.55e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 755564482  53 KKIREQEY-YLVKWRGYPDSENTWEPRQNLKCIRVLKQF-HKDLERE 97
Cdd:cd18648   12 RRIRKGRIeYLVKWKGWAIKYSTWEPEENILDSRLIAAFeQKERERE 58
CD_Cbx8 cd18649
chromodomain of chromobox homolog 8; CHRomatin Organization Modifier (chromo) domain of ...
44-90 4.93e-04

chromodomain of chromobox homolog 8; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 8 (CBX8), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells. CBX proteins may act as an oncogene or tumor suppressor in a cell-type-dependent manner, CBX8 for example promotes proliferation while suppressing metastasis, in colorectal carcinoma progression.


Pssm-ID: 349296  Cd Length: 55  Bit Score: 38.16  E-value: 4.93e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 755564482  44 FEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCIRVLKQF 90
Cdd:cd18649    5 FAAEALLKRRIRKGRMEYLVKWKGWSQKYSTWEPEENILDARLLAAF 51
CD_POL_like cd18970
chromodomain of Hypsizygus marmoreus TY3B-I_0 protein, and similar proteins; This subgroup ...
44-81 8.21e-04

chromodomain of Hypsizygus marmoreus TY3B-I_0 protein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Hypsizygus marmoreus TY3B-I_0 protein, a putative TY3/gypsy retrotransposon polyprotein, and similar proteins. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349326  Cd Length: 49  Bit Score: 37.03  E-value: 8.21e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 755564482  44 FEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNL 81
Cdd:cd18970    1 FFVERILDERRRGRGWQYLVRWLGYGPSDDSWLPRREL 38
CD_Chp1_like cd18636
chromodomain of chromodomain-containing protein 1, and similar proteins; CHRomatin ...
44-81 1.17e-03

chromodomain of chromodomain-containing protein 1, and similar proteins; CHRomatin Organization Modifier (chromo) domain of chromodomain-containing protein 1 (CHp1), and similar proteins. Chp1 is needed for RNA interference-dependent heterochromatin formation in fission yeast. Chp1 is a member of the RNA-induced transcriptional silencing (RITS) complex which maintains the heterochromatin regions. The chromodomain of the Chp1 component binds the histone H3 lysine 9 methylated tail (H3K9me) and the core of the nucleosome. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349286  Cd Length: 52  Bit Score: 37.04  E-value: 1.17e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 755564482  44 FEVE-YLCD-YKKIREQEYYlVKWRGYPDSENTWEPRQNL 81
Cdd:cd18636    2 YEVEdILADrVNKNGINEYY-IKWAGYDWYDNTWEPEQNL 40
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
59-92 1.51e-03

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD5, CHD6, CHD7, CHD8, and CHD9. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. CHD6, CHD7, and CHD8 enzymes have been demonstrated to have different substrate specificities and remodeling activities. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 36.50  E-value: 1.51e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 755564482  59 EYYLVKWRGYPDSENTWEPRQNLKCIRVlKQFHK 92
Cdd:cd18663   25 THYLVKWCSLPYEDSTWELEEDVDPAKI-EEFEK 57
chromodomain cd18967
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
61-92 1.62e-03

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349323  Cd Length: 55  Bit Score: 36.46  E-value: 1.62e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 755564482  61 YLVKWRGYPDSenTWEPRQNLKCIRVLKQFHK 92
Cdd:cd18967   26 YLTKWEGFPDE--TWEPAESFDDRKILHDYRR 55
SET_SETD7 cd10530
SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins; SETD7 (EC 2. ...
274-366 1.85e-03

SET domain found in SET domain-containing protein 7 (SETD7) and similar proteins; SETD7 (EC 2.1.1.43; also termed histone H3-K4 methyltransferase SETD7, H3-K4-HMTase SETD7, lysine N-methyltransferase 7 (KMT7) or SET7/9) is a histone-lysine N-methyltransferase that specifically monomethylates 'Lys-4' of histone H3. It plays a central role in the transcriptional activation of genes such as collagenase or insulin. Set7/9 also methylates non-histone proteins, including estrogen receptor alpha (ERa), suggesting it has a role in diverse biological processes. ERa methylation by Set7/9 stabilizes ERa and activates its transcriptional activities, which are involved in the carcinogenesis of breast cancer. In a high-throughput screen, treatment of human breast cancer cells (MCF7 cells) with cyproheptadine, a Set7/9 inhibitor, decreased the expression and transcriptional activity of ERa, thereby inhibiting estrogen-dependent cell growth.


Pssm-ID: 380928  Cd Length: 130  Bit Score: 38.43  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755564482 274 YVGEIITSEEAERRGqiYDRQGATYLFDLDYVEDV---YTVDAAYYGNISHFVNHSCDPNLQvYNVFIDnlderlPRIAF 350
Cdd:cd10530   38 YNGVRITHQEVDSRD--WSLNGNTISLDEETVIDVpepYNSVSKYCASLGHKANHSFTPNCI-YDPFVH------PRFGP 108
                         90       100
                 ....*....|....*....|
gi 755564482 351 F----ATRTIWAGEELTFDY 366
Cdd:cd10530  109 IkcirTLRAVEAGEELTVAY 128
CD1_tandem_CHD1_yeast_like cd18665
repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
54-88 3.45e-03

repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein 1, and similar proteins; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349312  Cd Length: 65  Bit Score: 35.82  E-value: 3.45e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 755564482  54 KIREQEYYLVKWRGYPDSENTWEPRQNLKCIRVLK 88
Cdd:cd18665   24 DPKENYEFLIKWTDESHLHNTWETYESLKQVRGLK 58
CD_Cbx7 cd18646
chromodomain of chromobox homolog 7; CHRomatin Organization Modifier (chromo) domain of ...
44-81 3.89e-03

chromodomain of chromobox homolog 7; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 7 (CBX7), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells. CBX proteins may act as an oncogene or tumor suppressor in a cell-type-dependent manner, for example CBX8 promotes proliferation while suppressing metastasis, in colorectal carcinoma progression. CBX7 has been shown to function as a tumor suppressor in lung carcinoma and an oncogene in gastric cancer and lymphoma.


Pssm-ID: 349293  Cd Length: 56  Bit Score: 35.45  E-value: 3.89e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 755564482  44 FEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNL 81
Cdd:cd18646    5 FAVESIRKKRVRKGKVEYLVKWKGWPPKYSTWEPEEHI 42
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
57-82 3.99e-03

repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 to CHD9, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349306 [Multi-domain]  Cd Length: 54  Bit Score: 35.24  E-value: 3.99e-03
                         10        20
                 ....*....|....*....|....*.
gi 755564482  57 EQEYYLVKWRGYPDSENTWEPRQNLK 82
Cdd:cd18659   17 GVTEYLVKWKGLPYDECTWESEEDIS 42
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH