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Conserved domains on  [gi|5901940|ref|NP_008823|]
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DNA (cytosine-5)-methyltransferase 3B isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PWWP_DNMT3B cd20155
PWWP domain found in DNA (cytosine-5)-methyltransferase 3B (DNMT3B); DNMT3B, also called DNA ...
224-340 7.08e-83

PWWP domain found in DNA (cytosine-5)-methyltransferase 3B (DNMT3B); DNMT3B, also called DNA methyltransferase HsaIIIB, DNA MTase HsaIIIB, or M.HsaIIIB, is required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. It may preferentially methylate nucleosomal DNA within the nucleosome core region. DNMT3B may function as a transcriptional co-repressor by associating with CBX4 and independently of DNA methylation. In tumorigenesis, DNA methylation by DNMT3B is known to play a role in the inactivation of tumor suppressor genes. In addition, a point mutation in the PWWP domain of DNMT3B has been identified in patients with ICF (immunodeficiency, centromeric instability, and facial anomalies) syndrome, a rare autosomal recessive disorder characterized by hypomethylation of classical satellite DNA.


:

Pssm-ID: 438983  Cd Length: 117  Bit Score: 260.96  E-value: 7.08e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  224 GIGDLVWGKIKGFSWWPAMVVSWKATSKRQAMSGMRWVQWFGDGKFSEVSADKLVALGLFSQHFNLATFNKLVSYRKAMY 303
Cdd:cd20155   1 GIGELVWGKIKGFSWWPAMVVSWRATGKRQASSGMRWLQWFGDGKFSEVSADKLVSLTAFSQHFNLSTYNKLVSYRKAMY 80
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 5901940  304 HALEKARVRAGKTFPSSPGDSLEDQLKPMLEWAHGGF 340
Cdd:cd20155  81 HALEVARVRAGKTFPSSPGESLEDQLKPMLDWAHGGF 117
ADDz_Dnmt3b cd11728
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3b (Dnmt3b); ADDz_Dnmt3b ...
431-550 5.62e-82

ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3b (Dnmt3b); ADDz_Dnmt3b is an active catalytic domain of Dnmt3b. Dnmt3b is a member of the Dnmt3 family and is a de novo DNA methyltransferases that has an N-terminal variable region followed by a conserved PWWP region and the cysteine-rich ADDz domain. DNA methylation is an important epigenetic mechanism involved in diverse biological processes such as embryonic development, gene expression, and genomic imprinting. The methyltransferase activity of Dnmt3a is not only responsible for the establishment of DNA methylation pattern, but is also essential for the inheritance of these patterns during mitosis. Dnmt3b is ubiquitously expressed in most adult tissues. The ADDz_Dnmt3 domain is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif. A knockout of Dnmt3b has been shown to be lethal in the mouse model.


:

Pssm-ID: 277254 [Multi-domain]  Cd Length: 120  Bit Score: 258.63  E-value: 5.62e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  431 LEDGCLSCGRKNPVSFHPLFEGGLCQTCRDRFLELFYMYDDDGYQSYCTVCCEGRELLLCSNTSCCRCFCVECLEVLVGT 510
Cdd:cd11728   1 IEDFCLSCGRSNPATFHPLFEGGLCITCKDRFLELFYMYDDDGYQSYCTVCCEGRELLLCGNASCCRCFCVDCLEVLVGP 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 5901940  511 GTAAEAKLQEPWSCYMCLPQRCHGVLRRRKDWNVRLQAFF 550
Cdd:cd11728  81 GTAAKAKEQDPWSCYMCLPQRCYGVLKRRTDWSVRLQEFF 120
Dcm super family cl43082
DNA-cytosine methylase [Replication, recombination and repair];
572-850 1.13e-15

DNA-cytosine methylase [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG0270:

Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 78.31  E-value: 1.13e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  572 RRPIRVLSLFDGI---ATGylvLKELGIKVGkyVASEVCEESIAVgtvkHEGNIKYVN----DVRNITKKNIEewGPFDL 644
Cdd:COG0270   1 SKKLTVIDLFAGAgglSLG---FEKAGFEVV--FAVEIDPDACET----YRANFPEAKviegDIRDIDPEELI--PDVDL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  645 VIGGSPCNDLSNVNPaRKGLYEGTGRLFFEFYHLLNYSRPKegddrpfFWMFENVVAMKVGDKRD-----ISRFLEC--- 716
Cdd:COG0270  70 LIGGPPCQPFSVAGK-RKGLEDPRGTLFFEFIRIVEELRPK-------AFVLENVPGLLSSDKGKtfeeiLKELEELgyr 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  717 -NPVMIDAIKVSAA-HRARYFwgnlpgmnrpVIASKNDKLELQ----DCLEYNR-----IAKLKKVQTITTKSNSIKQGk 785
Cdd:COG0270 142 vDYKVLNAADYGVPqNRERVF----------IVGFRKDLDLFEfpepTHLKPYVtvgdaLEDLPDAHEARYLSETITAG- 210
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5901940  786 nqlfpvvMNGKEDVL------WCT--ELERIFGFPVHYTDVSNMGRGARQklLGRSWSVPVIRHLFAPLKDYF 850
Cdd:COG0270 211 -------YGGGGRFLhpgeprRLTvrEAARLQGFPDDFKFPGSKTQAYRQ--IGNAVPPPLAEAIAKAILKAL 274
 
Name Accession Description Interval E-value
PWWP_DNMT3B cd20155
PWWP domain found in DNA (cytosine-5)-methyltransferase 3B (DNMT3B); DNMT3B, also called DNA ...
224-340 7.08e-83

PWWP domain found in DNA (cytosine-5)-methyltransferase 3B (DNMT3B); DNMT3B, also called DNA methyltransferase HsaIIIB, DNA MTase HsaIIIB, or M.HsaIIIB, is required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. It may preferentially methylate nucleosomal DNA within the nucleosome core region. DNMT3B may function as a transcriptional co-repressor by associating with CBX4 and independently of DNA methylation. In tumorigenesis, DNA methylation by DNMT3B is known to play a role in the inactivation of tumor suppressor genes. In addition, a point mutation in the PWWP domain of DNMT3B has been identified in patients with ICF (immunodeficiency, centromeric instability, and facial anomalies) syndrome, a rare autosomal recessive disorder characterized by hypomethylation of classical satellite DNA.


Pssm-ID: 438983  Cd Length: 117  Bit Score: 260.96  E-value: 7.08e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  224 GIGDLVWGKIKGFSWWPAMVVSWKATSKRQAMSGMRWVQWFGDGKFSEVSADKLVALGLFSQHFNLATFNKLVSYRKAMY 303
Cdd:cd20155   1 GIGELVWGKIKGFSWWPAMVVSWRATGKRQASSGMRWLQWFGDGKFSEVSADKLVSLTAFSQHFNLSTYNKLVSYRKAMY 80
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 5901940  304 HALEKARVRAGKTFPSSPGDSLEDQLKPMLEWAHGGF 340
Cdd:cd20155  81 HALEVARVRAGKTFPSSPGESLEDQLKPMLDWAHGGF 117
ADDz_Dnmt3b cd11728
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3b (Dnmt3b); ADDz_Dnmt3b ...
431-550 5.62e-82

ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3b (Dnmt3b); ADDz_Dnmt3b is an active catalytic domain of Dnmt3b. Dnmt3b is a member of the Dnmt3 family and is a de novo DNA methyltransferases that has an N-terminal variable region followed by a conserved PWWP region and the cysteine-rich ADDz domain. DNA methylation is an important epigenetic mechanism involved in diverse biological processes such as embryonic development, gene expression, and genomic imprinting. The methyltransferase activity of Dnmt3a is not only responsible for the establishment of DNA methylation pattern, but is also essential for the inheritance of these patterns during mitosis. Dnmt3b is ubiquitously expressed in most adult tissues. The ADDz_Dnmt3 domain is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif. A knockout of Dnmt3b has been shown to be lethal in the mouse model.


Pssm-ID: 277254 [Multi-domain]  Cd Length: 120  Bit Score: 258.63  E-value: 5.62e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  431 LEDGCLSCGRKNPVSFHPLFEGGLCQTCRDRFLELFYMYDDDGYQSYCTVCCEGRELLLCSNTSCCRCFCVECLEVLVGT 510
Cdd:cd11728   1 IEDFCLSCGRSNPATFHPLFEGGLCITCKDRFLELFYMYDDDGYQSYCTVCCEGRELLLCGNASCCRCFCVDCLEVLVGP 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 5901940  511 GTAAEAKLQEPWSCYMCLPQRCHGVLRRRKDWNVRLQAFF 550
Cdd:cd11728  81 GTAAKAKEQDPWSCYMCLPQRCYGVLKRRTDWSVRLQEFF 120
ADD_DNMT3 pfam17980
Cysteine rich ADD domain in DNMT3; This is a cysteine-rich domain termed ADD ...
416-471 1.66e-29

Cysteine rich ADD domain in DNMT3; This is a cysteine-rich domain termed ADD (ATRX-DNMT3-DNMT3L, AD-DATRX) found in DNMT3A proteins. The ADD domains of the DNMT3 family have a decisive role in blocking DNMT activity in the areas of the genome with chromatin containing methylated H3K4. Furthermore, the ADD domain of DNMMT3A (ADD-3A) competes with the chromodomain (CD) of heterochromatin protein 1 alpha (HP1alpha, CDHP1alpha) for binding to the H3 tail. The DNA methyltransferase (DNMT) 3 family members DNMT3A and DNMT3B and the DNMT3-like non-enzymatic regulatory factor DNMT3L, are involved in de-novo establishment of DNA methylation patterns in early mammalian development.


Pssm-ID: 465603  Cd Length: 56  Bit Score: 111.22  E-value: 1.66e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 5901940    416 SREQMASDVANNKSSLEDGCLSCGRKNPVSFHPLFEGGLCQTCRDRFLELFYMYDD 471
Cdd:pfam17980   1 SREQMVYEVRENKRNIEDFCLSCGSLNVHTFHPLFEGGLCQKCKDNFLETLYRYDE 56
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
223-281 7.85e-22

domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 89.33  E-value: 7.85e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5901940     223 FGIGDLVWGKIKGFSWWPAMVVSWKAT----SKRQAMSGMRWVQWFGDGKFSEVSADKLVALG 281
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVISPKMTpdniMKRKSDENLYPVLFFGDKDTAWIPSSKLFPLT 63
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
226-310 1.06e-17

PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain binds to Histone-4 methylated at lysine-20, H4K20me, suggesting that it is methyl-lysine recognition motif. Removal of two conserved aromatic residues in a hydrophobic cavity created by this domain within the full-length protein, Pdp1, abolishes the interaction o f the protein with H4K20me3. In fission yeast, Set9 is the sole enzyme that catalyzes all three states of H4K20me, and Set9-mediated H4K20me is required for efficient recruitment of checkpoint protein Crb2 to sites of DNA damage. The methylation of H4K20 is involved in a diverse array of cellular processes, such as organizing higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression.


Pssm-ID: 459964 [Multi-domain]  Cd Length: 92  Bit Score: 78.62  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940    226 GDLVWGKIKGFSWWPAMVVSW----KATSKRQAMSGMRWVQWFGDGKFSEVSADKLVALGLFSQHFNLATFNKLVS---Y 298
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVVDPeelpENVLKPKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEFEYLKKKKKKKKkkaF 80
                          90
                  ....*....|..
gi 5901940    299 RKAMYHALEKAR 310
Cdd:pfam00855  81 KKALEEAEEALK 92
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
572-850 1.13e-15

DNA-cytosine methylase [Replication, recombination and repair];


Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 78.31  E-value: 1.13e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  572 RRPIRVLSLFDGI---ATGylvLKELGIKVGkyVASEVCEESIAVgtvkHEGNIKYVN----DVRNITKKNIEewGPFDL 644
Cdd:COG0270   1 SKKLTVIDLFAGAgglSLG---FEKAGFEVV--FAVEIDPDACET----YRANFPEAKviegDIRDIDPEELI--PDVDL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  645 VIGGSPCNDLSNVNPaRKGLYEGTGRLFFEFYHLLNYSRPKegddrpfFWMFENVVAMKVGDKRD-----ISRFLEC--- 716
Cdd:COG0270  70 LIGGPPCQPFSVAGK-RKGLEDPRGTLFFEFIRIVEELRPK-------AFVLENVPGLLSSDKGKtfeeiLKELEELgyr 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  717 -NPVMIDAIKVSAA-HRARYFwgnlpgmnrpVIASKNDKLELQ----DCLEYNR-----IAKLKKVQTITTKSNSIKQGk 785
Cdd:COG0270 142 vDYKVLNAADYGVPqNRERVF----------IVGFRKDLDLFEfpepTHLKPYVtvgdaLEDLPDAHEARYLSETITAG- 210
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5901940  786 nqlfpvvMNGKEDVL------WCT--ELERIFGFPVHYTDVSNMGRGARQklLGRSWSVPVIRHLFAPLKDYF 850
Cdd:COG0270 211 -------YGGGGRFLhpgeprRLTvrEAARLQGFPDDFKFPGSKTQAYRQ--IGNAVPPPLAEAIAKAILKAL 274
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
575-843 2.46e-12

Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many aspects of biology. Cytosine-specific DNA methylases are found both in prokaryotes and eukaryotes. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the mammalian genome. These effects include transcriptional repression via inhibition of transcription factor binding or the recruitment of methyl-binding proteins and their associated chromatin remodeling factors, X chromosome inactivation, imprinting and the suppression of parasitic DNA sequences. DNA methylation is also essential for proper embryonic development and is an important player in both DNA repair and genome stability.


Pssm-ID: 238192 [Multi-domain]  Cd Length: 275  Bit Score: 68.03  E-value: 2.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  575 IRVLSLFDGIATGYLVLKELGIKVgkYVASEVCEESIAVGTVKHeGNIKYVNDVRNITKKniEEWGPFDLVIGGSPCNDL 654
Cdd:cd00315   1 LRVIDLFAGIGGFRLGLEKAGFEI--VAANEIDKSAAETYEANF-PNKLIEGDITKIDEK--DFIPDIDLLTGGFPCQPF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  655 SNVNpARKGLYEGTGRLFFEFYHLLNYSRPKegddrpfFWMFENVVAMKVGDKRD-----ISRFLECN----PVMIDAIK 725
Cdd:cd00315  76 SIAG-KRKGFEDTRGTLFFEIIRILKEKKPK-------YFLLENVKGLLTHDNGNtlkviLNTLEELGynvyWKLLNASD 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  726 VSAAH-RARYFW-GNLPGMN----RPVIASKNDKLELQDCLeynRIAKLKKVQTITTKSNSIKQGKNQLFPVVMNGKEDV 799
Cdd:cd00315 148 YGVPQnRERVFIiGIRKDLIlnffSPFPKPSEKKKTLKDIL---RIRDPDEPSPTLTASYGKGTGSVHPTAPDMIGKESN 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 5901940  800 ---LWCTELERIFGFPVHYtDVSNMGRGARQKLLGRSWSVPVIRHLF 843
Cdd:cd00315 225 irrLTPRECARLQGFPDDF-EFPGKSVTQAYRQIGNSVPVPVAEAIA 270
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
575-699 5.88e-09

C-5 cytosine-specific DNA methylase;


Pssm-ID: 395093 [Multi-domain]  Cd Length: 324  Bit Score: 58.48  E-value: 5.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940    575 IRVLSLFDGIATGYLVLKELGIKVgkYVASEVCEESIAV-GTVKHEGNIkyvNDVRNITKKNIEEwgpFDLVIGGSPCND 653
Cdd:pfam00145   1 FKFIDLFAGIGGFRLGLEQAGFEC--VAANEIDKSAAKTyEANFPKVPI---GDITLIDIKDIPD---IDILTGGFPCQD 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 5901940    654 LSNVNpARKGLYEGTGRLFFEFYHLLNYSRPKegddrpfFWMFENV 699
Cdd:pfam00145  73 FSIAG-KQKGFEDTRGTLFFEIIRIIKEKKPK-------AFLLENV 110
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
627-840 3.45e-08

DNA-methyltransferase (dcm); All proteins in this family for which functions are known are DNA-cytosine methyltransferases. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273211 [Multi-domain]  Cd Length: 315  Bit Score: 56.18  E-value: 3.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940    627 DVRNITKKNIEEwgpFDLVIGGSPCNDLSnVNPARKGLYEGTGRLFFEFYHLLNYSRPKegddrpfFWMFENVVAMKVGD 706
Cdd:TIGR00675  48 DITKISPSDIPD---FDILLGGFPCQPFS-IAGKRKGFEDTRGTLFFEIVRILKEKKPK-------FFLLENVKGLVSHD 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940    707 K-RDISrflecnpVMIDAI---------KVSAA-------HRAR-------YFWGNLPgMNRPVIASKNDKLELQDCLE- 761
Cdd:TIGR00675 117 KgRTFK-------VIIETLeelgykvyyKVLNAkdfgvpqNRERiyivgfrDFDDKLN-FEFPKPIYVAKKKRIGDLLDl 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940    762 --------------------------------------YNRIAKLKKVQTITTK-SNSIKQGKNqlFPVVMNGKEDV--- 799
Cdd:TIGR00675 189 svdleekyylseekknglllllenmrkkegtgeqigsfYNRESKSSIIRTLSARgYTFVKGGKS--VLIVPHKSTVVhpg 266
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 5901940    800 ----LWCTELERIFGFPVHYTDvsNMGRGARQKLLGRSWSVPVIR 840
Cdd:TIGR00675 267 rirrLTPRECARLQGFPDDFKF--PVSDSQLYKQAGNAVVVPVIE 309
 
Name Accession Description Interval E-value
PWWP_DNMT3B cd20155
PWWP domain found in DNA (cytosine-5)-methyltransferase 3B (DNMT3B); DNMT3B, also called DNA ...
224-340 7.08e-83

PWWP domain found in DNA (cytosine-5)-methyltransferase 3B (DNMT3B); DNMT3B, also called DNA methyltransferase HsaIIIB, DNA MTase HsaIIIB, or M.HsaIIIB, is required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. It may preferentially methylate nucleosomal DNA within the nucleosome core region. DNMT3B may function as a transcriptional co-repressor by associating with CBX4 and independently of DNA methylation. In tumorigenesis, DNA methylation by DNMT3B is known to play a role in the inactivation of tumor suppressor genes. In addition, a point mutation in the PWWP domain of DNMT3B has been identified in patients with ICF (immunodeficiency, centromeric instability, and facial anomalies) syndrome, a rare autosomal recessive disorder characterized by hypomethylation of classical satellite DNA.


Pssm-ID: 438983  Cd Length: 117  Bit Score: 260.96  E-value: 7.08e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  224 GIGDLVWGKIKGFSWWPAMVVSWKATSKRQAMSGMRWVQWFGDGKFSEVSADKLVALGLFSQHFNLATFNKLVSYRKAMY 303
Cdd:cd20155   1 GIGELVWGKIKGFSWWPAMVVSWRATGKRQASSGMRWLQWFGDGKFSEVSADKLVSLTAFSQHFNLSTYNKLVSYRKAMY 80
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 5901940  304 HALEKARVRAGKTFPSSPGDSLEDQLKPMLEWAHGGF 340
Cdd:cd20155  81 HALEVARVRAGKTFPSSPGESLEDQLKPMLDWAHGGF 117
ADDz_Dnmt3b cd11728
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3b (Dnmt3b); ADDz_Dnmt3b ...
431-550 5.62e-82

ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3b (Dnmt3b); ADDz_Dnmt3b is an active catalytic domain of Dnmt3b. Dnmt3b is a member of the Dnmt3 family and is a de novo DNA methyltransferases that has an N-terminal variable region followed by a conserved PWWP region and the cysteine-rich ADDz domain. DNA methylation is an important epigenetic mechanism involved in diverse biological processes such as embryonic development, gene expression, and genomic imprinting. The methyltransferase activity of Dnmt3a is not only responsible for the establishment of DNA methylation pattern, but is also essential for the inheritance of these patterns during mitosis. Dnmt3b is ubiquitously expressed in most adult tissues. The ADDz_Dnmt3 domain is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif. A knockout of Dnmt3b has been shown to be lethal in the mouse model.


Pssm-ID: 277254 [Multi-domain]  Cd Length: 120  Bit Score: 258.63  E-value: 5.62e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  431 LEDGCLSCGRKNPVSFHPLFEGGLCQTCRDRFLELFYMYDDDGYQSYCTVCCEGRELLLCSNTSCCRCFCVECLEVLVGT 510
Cdd:cd11728   1 IEDFCLSCGRSNPATFHPLFEGGLCITCKDRFLELFYMYDDDGYQSYCTVCCEGRELLLCGNASCCRCFCVDCLEVLVGP 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 5901940  511 GTAAEAKLQEPWSCYMCLPQRCHGVLRRRKDWNVRLQAFF 550
Cdd:cd11728  81 GTAAKAKEQDPWSCYMCLPQRCYGVLKRRTDWSVRLQEFF 120
ADDz_Dnmt3 cd11725
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 (Dnmt3); Dnmt3 is a de ...
431-536 4.45e-50

ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 (Dnmt3); Dnmt3 is a de novo DNA methyltransferase family that includes two active enzymes Dnmt3a and -3b and one regulatory factor Dnmt3l. The ADDz domain of Dnmt3 is located in the C-terminal region of Dnmt3, which is an active catalytic domain in Dnmt3a and -b, but lacks some residues for enzymatic activity in Dnmt3l. DNA methylation is an important epigenetic mechanism involved in diverse biological processes such as embryonic development, gene expression, and genomic imprinting. The ADDz_Dnmt3 domain is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif.


Pssm-ID: 277251 [Multi-domain]  Cd Length: 108  Bit Score: 171.42  E-value: 4.45e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  431 LEDGCLSCGRKNP--VSFHPLFEGGLCQTCRDRFLELFYMYDDDGYQSYCTVCCEGRELLLCSNTSCCRCFCVECLEVLV 508
Cdd:cd11725   1 IEDICLACGSLEVseTSDHPFFEGGLCKNCKERFLECIFLFDDDGYQMYCTICGGGGEVVLCDNPDCTRVYCTECLDLLL 80
                        90       100
                ....*....|....*....|....*...
gi 5901940  509 GTGTAAEAKLQEPWSCYMCLPQRCHGVL 536
Cdd:cd11725  81 GPGAVAKILESDPWFCFLCSPESNSLLG 108
PWWP_DNMT3A cd20154
PWWP domain found in DNA (cytosine-5)-methyltransferase 3A (DNMT3A); DNMT3A, also called DNA ...
218-344 1.04e-49

PWWP domain found in DNA (cytosine-5)-methyltransferase 3A (DNMT3A); DNMT3A, also called DNA methyltransferase HsaIIIA, DNA MTase HsaIIIA, or M.HsaIIIA, is required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. It modifies DNA in a non-processive manner and also methylates non-CpG sites. It may preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. DNMT3A is recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. It contains a PWWP domain that binds methylated histone.


Pssm-ID: 438982  Cd Length: 134  Bit Score: 171.30  E-value: 1.04e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  218 QDGKEFGIGDLVWGKIKGFSWWPAMVVSWKATSKRQAMSGMRWVQWFGDGKFSEVSADKLVALGLFSQHFNLATFNKLVS 297
Cdd:cd20154   1 EDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFSSAFHQATYNKQPM 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 5901940  298 YRKAMYHALEKARVRAGKTFPSSP-------GDSLEDQLKPMLEWAHGGFKPTG 344
Cdd:cd20154  81 YRKAIYEVLQVASSRAGKLFPVCPesdesdtSKAVEVQNKQMIEWALGGFQPSG 134
ADDz_Dnmt3l cd11727
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 like (Dnmt3l); Dnmt3l ...
430-550 2.13e-47

ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 like (Dnmt3l); Dnmt3l is a regulator of DNA methylation, which acts by recognizing unmethylated histone H3 tails and interacting with Dnmt3a to stimulate its de novo DNA methylation activity. The ADDz_Dnmt3l domain is located in the C-terminal region of Dnmt3l that otherwise lacks some residues required for DNA methyltransferase activity. DNA methylation is an important epigenetic mechanism involved in diverse biological processes such as embryonic development, gene expression, and genomic imprinting. Dnmt3l is also associating with HDAC1 and acts as a transcriptional repressor. The ADDz_Dnmt3l domain is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif.


Pssm-ID: 277253 [Multi-domain]  Cd Length: 123  Bit Score: 164.64  E-value: 2.13e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  430 SLEDGCLSCGRKNPVSFHPLFEGGLCQTCRDRFLELFYMYDDDGYQSYCTVCCEGRELLLCSNTSCCRCFCVECLEVLVG 509
Cdd:cd11727   2 SIEEICICCGSLQIHTQHPLFHGGICAPCTEKFLEAFFLYDEDGYQAYCTICCSGETLLMCDDPDCTRCYCFECVDSLVG 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 5901940  510 TGTAAEAKLQEPWSCYMCLPQRCHGVLRRRKDWNVRLQAFF 550
Cdd:cd11727  82 PGTSEKVKATNNWVCFLCLPSSRSGLLQRKRKWRSQLKAFY 122
ADDz_Dnmt3a cd11729
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3a (Dnmt3a); Dnmt3a is a ...
430-553 1.96e-46

ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3a (Dnmt3a); Dnmt3a is a member of the Dnmt3 family and is a protein with de novo DNA methyltransferase activity. Dnmt3 family members are Dnmt3a, Dnmt3b, and Dnmt3l the non-enzymatic regulatory factor. Dnmt3a is recruited by Dnmt3l to unmethylated histone H3 and methylates the target. Dnmt3a has a variable region at the N-terminus, followed by a conserved PWWP region and the cysteine-rich ADDz domain. ADDz_Dnmt3a is an active catalytic domain of Dnmt3a. DNA methylation is an important epigenetic mechanism involved in diverse biological processes such as embryonic development, gene expression, and genomic imprinting. The methyltransferase activity of Dnmt3a is not only responsible for the establishment of DNA methylation pattern, but is also essential for the inheritance of these patterns during mitosis. The ADDz_Dnmt3 domain is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif. A knockout of Dnmt3a has been shown to be lethal in the mouse model.


Pssm-ID: 277255 [Multi-domain]  Cd Length: 128  Bit Score: 162.10  E-value: 1.96e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  430 SLEDGCLSCGRKNPVSFHPLFEGGLCQTCRDRFLELFYMYDDDGYQSYCTVCCEGRELLLCSNTSCCRCFCVECLEVLVG 509
Cdd:cd11729   3 NIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLVG 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 5901940  510 TGTAAEAKLQEPWSCYMCLPQRCHGVLRRRKDWNVRLQAFFTSD 553
Cdd:cd11729  83 PGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANN 126
ADDz cd11672
ATRX, Dnmt3 and Dnmt3l PHD-like zinc finger domain (ADDz); The ADDz zinc finger domain is ...
432-529 5.34e-41

ATRX, Dnmt3 and Dnmt3l PHD-like zinc finger domain (ADDz); The ADDz zinc finger domain is present in the chromatin-associated proteins cytosine-5-methyltransferase 3 (Dnmt3) and ATRX, a SNF2 type transcription factor protein. The Dnmt3 family includes two active DNA methyltransferases, Dnmt3a and -3b, and one regulatory factor Dnmt3l. DNA methylation is an important epigenetic mechanism involved in diverse biological processes such as embryonic development, gene expression, and genomic imprinting. The ADDz domain is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif.


Pssm-ID: 277250 [Multi-domain]  Cd Length: 99  Bit Score: 145.40  E-value: 5.34e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  432 EDGCLSCGRKNPVSFHPLFEGGLCQTCRDRFLELFYMYDDDGYQSYCTVCCEGRELLLCSNTSCCRCFCVECLEVLVGTG 511
Cdd:cd11672   2 EDICIACGSLVVIYRHPLFQGGICKNCKKYFLSDDISYDDDGYQSYCRICCEGGNLLCCGNNFCHRCFCKECVDRLVGPG 81
                        90
                ....*....|....*...
gi 5901940  512 TAAEAKLQEPWSCYMCLP 529
Cdd:cd11672  82 ELSTMDENNQWYCYICHP 99
PWWP_DNMT3 cd05835
PWWP domain found in the DNA (cytosine-5)-methyltransferase 3 (DNMT3) family; The DNMT3 family ...
225-313 7.68e-36

PWWP domain found in the DNA (cytosine-5)-methyltransferase 3 (DNMT3) family; The DNMT3 family includes DNMT3A and DNMT3B, which are required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNMT3A, also called DNA methyltransferase HsaIIIA, DNA MTase HsaIIIA, or M.HsaIIIA, modifies DNA in a non-processive manner and also methylates non-CpG sites. It may preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. DNMT3A is recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. DNMT3B, also called DNA methyltransferase HsaIIIB, DNA MTase HsaIIIB, or M.HsaIIIB, may preferentially methylate nucleosomal DNA within the nucleosome core region. DNMT3B may function as a transcriptional co-repressor by associating with CBX4 and independently of DNA methylation. Members of this family contains a PWWP domain that is responsible for establishing DNA methylation patterns during embryogenesis and gametogenesis. In tumorigenesis, DNA methylation by DNMT3B is known to play a role in the inactivation of tumor suppressor genes. In addition, a point mutation in the PWWP domain of DNMT3B has been identified in patients with ICF (immunodeficiency, centromeric instability, and facial anomalie) syndrome , a rare autosomal recessive disorder characterized by hypomethylation of classical satellite DNA.


Pssm-ID: 438960 [Multi-domain]  Cd Length: 89  Bit Score: 130.46  E-value: 7.68e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  225 IGDLVWGKIKGFSWWPAMVVSWKATSKRQAMSGMRWVQWFGDGKFSEVSADKLVALGLFSQHFNLaTFNKLVSYRKAMYH 304
Cdd:cd05835   2 IGDLVWAKLKGSPWWPGIVVSHKDCGQKPPAEGSVWVFWFGDHKVSEVPLDKILPFAEFFNKFYI-SKNSSKLYKKAVYE 80

                ....*....
gi 5901940  305 ALEKARVRA 313
Cdd:cd05835  81 ALKEAAERS 89
ADD_DNMT3 pfam17980
Cysteine rich ADD domain in DNMT3; This is a cysteine-rich domain termed ADD ...
416-471 1.66e-29

Cysteine rich ADD domain in DNMT3; This is a cysteine-rich domain termed ADD (ATRX-DNMT3-DNMT3L, AD-DATRX) found in DNMT3A proteins. The ADD domains of the DNMT3 family have a decisive role in blocking DNMT activity in the areas of the genome with chromatin containing methylated H3K4. Furthermore, the ADD domain of DNMMT3A (ADD-3A) competes with the chromodomain (CD) of heterochromatin protein 1 alpha (HP1alpha, CDHP1alpha) for binding to the H3 tail. The DNA methyltransferase (DNMT) 3 family members DNMT3A and DNMT3B and the DNMT3-like non-enzymatic regulatory factor DNMT3L, are involved in de-novo establishment of DNA methylation patterns in early mammalian development.


Pssm-ID: 465603  Cd Length: 56  Bit Score: 111.22  E-value: 1.66e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 5901940    416 SREQMASDVANNKSSLEDGCLSCGRKNPVSFHPLFEGGLCQTCRDRFLELFYMYDD 471
Cdd:pfam17980   1 SREQMVYEVRENKRNIEDFCLSCGSLNVHTFHPLFEGGLCQKCKDNFLETLYRYDE 56
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
223-281 7.85e-22

domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 89.33  E-value: 7.85e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5901940     223 FGIGDLVWGKIKGFSWWPAMVVSWKAT----SKRQAMSGMRWVQWFGDGKFSEVSADKLVALG 281
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVISPKMTpdniMKRKSDENLYPVLFFGDKDTAWIPSSKLFPLT 63
PWWP cd05162
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
226-307 4.10e-18

PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, is a small domain consisting of 100-150 amino acids and is composed of a five-stranded antiparallel beta-barrel followed by a helical region. It is found in numerous proteins that are involved in cell division, growth, and differentiation. Most PWWP-domain proteins seem to be nuclear, often DNA-binding, proteins that function as transcription factors regulating a variety of developmental processes. PWWP domains specifically recognize DNA and histone methylated lysines at the level of the nucleosome. Based on the fact that other regions of PWWP-domain proteins are responsible for nuclear localization and DNA-binding, is likely that the PWWP domain acts as a site for protein-protein binding interactions, influencing chromatin remodeling and thereby regulating transcriptional processes. Some PWWP-domain proteins have been linked to cancer or other diseases; some are known to function as growth factors.


Pssm-ID: 438958 [Multi-domain]  Cd Length: 86  Bit Score: 79.85  E-value: 4.10e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  226 GDLVWGKIKGFSWWPAMVVSWKATSKRQAMS---GMRWVQWFGDGKFSEVSADKLVALGLFSQHFNLATFNKLVSYRKAM 302
Cdd:cd05162   1 GDLVWAKLKGYPWWPARVVDPEELPEEVGKKkkkGGVLVQFFGDNDYAWVKSKNIKPFEEGFKKEFKKKKKKSKKFKKAV 80

                ....*
gi 5901940  303 YHALE 307
Cdd:cd05162  81 EEAEE 85
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
226-310 1.06e-17

PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain binds to Histone-4 methylated at lysine-20, H4K20me, suggesting that it is methyl-lysine recognition motif. Removal of two conserved aromatic residues in a hydrophobic cavity created by this domain within the full-length protein, Pdp1, abolishes the interaction o f the protein with H4K20me3. In fission yeast, Set9 is the sole enzyme that catalyzes all three states of H4K20me, and Set9-mediated H4K20me is required for efficient recruitment of checkpoint protein Crb2 to sites of DNA damage. The methylation of H4K20 is involved in a diverse array of cellular processes, such as organizing higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression.


Pssm-ID: 459964 [Multi-domain]  Cd Length: 92  Bit Score: 78.62  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940    226 GDLVWGKIKGFSWWPAMVVSW----KATSKRQAMSGMRWVQWFGDGKFSEVSADKLVALGLFSQHFNLATFNKLVS---Y 298
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVVDPeelpENVLKPKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEFEYLKKKKKKKKkkaF 80
                          90
                  ....*....|..
gi 5901940    299 RKAMYHALEKAR 310
Cdd:pfam00855  81 KKALEEAEEALK 92
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
572-850 1.13e-15

DNA-cytosine methylase [Replication, recombination and repair];


Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 78.31  E-value: 1.13e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  572 RRPIRVLSLFDGI---ATGylvLKELGIKVGkyVASEVCEESIAVgtvkHEGNIKYVN----DVRNITKKNIEewGPFDL 644
Cdd:COG0270   1 SKKLTVIDLFAGAgglSLG---FEKAGFEVV--FAVEIDPDACET----YRANFPEAKviegDIRDIDPEELI--PDVDL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  645 VIGGSPCNDLSNVNPaRKGLYEGTGRLFFEFYHLLNYSRPKegddrpfFWMFENVVAMKVGDKRD-----ISRFLEC--- 716
Cdd:COG0270  70 LIGGPPCQPFSVAGK-RKGLEDPRGTLFFEFIRIVEELRPK-------AFVLENVPGLLSSDKGKtfeeiLKELEELgyr 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  717 -NPVMIDAIKVSAA-HRARYFwgnlpgmnrpVIASKNDKLELQ----DCLEYNR-----IAKLKKVQTITTKSNSIKQGk 785
Cdd:COG0270 142 vDYKVLNAADYGVPqNRERVF----------IVGFRKDLDLFEfpepTHLKPYVtvgdaLEDLPDAHEARYLSETITAG- 210
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5901940  786 nqlfpvvMNGKEDVL------WCT--ELERIFGFPVHYTDVSNMGRGARQklLGRSWSVPVIRHLFAPLKDYF 850
Cdd:COG0270 211 -------YGGGGRFLhpgeprRLTvrEAARLQGFPDDFKFPGSKTQAYRQ--IGNAVPPPLAEAIAKAILKAL 274
ADDz_ATRX cd11726
ADDz domain found in ATRX (alpha-thalassemia/mental retardation, X-linked); ADDz_ATRX is a ...
435-529 2.44e-13

ADDz domain found in ATRX (alpha-thalassemia/mental retardation, X-linked); ADDz_ATRX is a PHD-like zinc finger domain of ATRX, which belongs to the SNF2 family of chromatin remodeling proteins. ATRX is a large chromatin-associated nuclear protein with two domains, ADDz_ATRX at the N-terminus, followed by a C-terminal ATPase/helicase domain. The ADDz_ATRX domain recognizes a specific methylated histone, and this interaction is required for heterochromatin localization of the ATRX protein. Missense mutations in either of the two ATRX domains lead to the X-linked alpha-thalassemia and mental retardation syndrome; however the mutations in the ADDz_ATRX domain produce a more severe disease phenotype that may also relate to disturbing unknown functions or interaction sites of this domain. The ADDz domain is also present in chromatin-associated proteins cytosine-5-methyltransferase 3 (Dnmt3); it is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif.


Pssm-ID: 277252 [Multi-domain]  Cd Length: 102  Bit Score: 66.56  E-value: 2.44e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  435 CLSCGR-----KNPVSFHPLFEGGLCQTCRDRFLELFYMYDDDGYQSYCTVCCEGRELLLCSntSCCRCFCVECLEVLVG 509
Cdd:cd11726   5 CTACGEqlnhfSKEVHRHPVLKVLICKSCLKFYNSGEFSKDEDGSDEYCRWCGQGGDLICCD--FCPNVFCKKCIKRNLG 82
                        90       100
                ....*....|....*....|
gi 5901940  510 TGTAAEAKLQEPWSCYMCLP 529
Cdd:cd11726  83 RAELSRIEESDKWKCFVCDP 102
PWWP_MBD5 cd20141
PWWP domain found in methyl-CpG-binding domain protein 5 (MBD5) and similar proteins; MBD5, is ...
223-286 2.89e-13

PWWP domain found in methyl-CpG-binding domain protein 5 (MBD5) and similar proteins; MBD5, is a methyl-CpG-binding protein that binds to heterochromatin. It does not interact with either methylated or unmethylated DNA. MBD5 acts as a transcriptional regulator responsible for 2q23.1 deletion syndrome. It belongs to the MBD family proteins, which play central roles in transcriptional regulation and development. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438969  Cd Length: 92  Bit Score: 66.19  E-value: 2.89e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5901940  223 FGIGDLVWGKIKGFSWWPAMVVSWKATSKRQamSGMRWVQWFGDGKFSEVSADKLVAL--GLFSQH 286
Cdd:cd20141   1 FNVGDLVWGQIRGFPSWPGKLVSENDVGKTN--EGKVWVSWFGDHSFGQVEPDKLKTLseGLEAHH 64
PWWP_PWWP2B cd20153
PWWP domain found in PWWP domain-containing protein 2B (PWWP2B); PWWP2B is a paralog of PWWP2A, ...
218-310 1.43e-12

PWWP domain found in PWWP domain-containing protein 2B (PWWP2B); PWWP2B is a paralog of PWWP2A, a H2A.Z-specific chromatin binding protein which may play an important role in the neural crest stem cell migration and differentiation during early development. PWWP2A and PWWP2B form a stable complex with NuRD subunits MTA1/2/3:HDAC1/2:RBBP4/7, but not with MBD2/3, p66alpha/beta, and CHD3/4. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438981  Cd Length: 116  Bit Score: 64.98  E-value: 1.43e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  218 QDGKEFGIGDLVWGKIKGFSWWPAMVVSWKATSKRQAMSGMR--WVQWFGDGKFSEVSADKLVAlglFSQHFNLaTFN-- 293
Cdd:cd20153   9 EEGRTVSVGDIVWGKIHGFPWWPARVLSISLSQKEDGEPSWQeaKVSWFGSPTTSLLSVSKLSP---FSEFFKL-RFNrk 84
                        90
                ....*....|....*..
gi 5901940  294 KLVSYRKAMYHALEKAR 310
Cdd:cd20153  85 KKGMYRKAITEAAKAAE 101
PWWP_PWWP2 cd20140
PWWP domain found in the PWWP domain-containing protein 2 (PWWP2) family; The PWWP2 family ...
220-310 1.82e-12

PWWP domain found in the PWWP domain-containing protein 2 (PWWP2) family; The PWWP2 family includes PWWP2A and its paralog PWWP2B. PWWP2A is a H2A.Z-specific chromatin binding protein which may play an important role in the neural crest stem cell migration and differentiation during early development. It is also required for proper mitosis progression. PWWP2A and PWWP2B form a stable complex with NuRD subunits MTA1/2/3:HDAC1/2:RBBP4/7, but not with MBD2/3, p66alpha/beta, and CHD3/4. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438968  Cd Length: 92  Bit Score: 63.82  E-value: 1.82e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  220 GKEFGIGDLVWGKIKGFSWWPAMVVS-WKATSKRQAMSGMR-WVQWFGDGKFSEVSADKlvaLGLFSQHFNLATFNKLV- 296
Cdd:cd20140   1 GRTLRVGDIVWGKIHGFPWWPGRILSiTVSRDDNGELSTQEaHVSWFGSSTTSYMPCSQ---LYPFLEDFKLRYNKKKRg 77
                        90
                ....*....|....
gi 5901940  297 SYRKAMYHALEKAR 310
Cdd:cd20140  78 PYKEAVRQALEAAK 91
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
575-843 2.46e-12

Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many aspects of biology. Cytosine-specific DNA methylases are found both in prokaryotes and eukaryotes. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the mammalian genome. These effects include transcriptional repression via inhibition of transcription factor binding or the recruitment of methyl-binding proteins and their associated chromatin remodeling factors, X chromosome inactivation, imprinting and the suppression of parasitic DNA sequences. DNA methylation is also essential for proper embryonic development and is an important player in both DNA repair and genome stability.


Pssm-ID: 238192 [Multi-domain]  Cd Length: 275  Bit Score: 68.03  E-value: 2.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  575 IRVLSLFDGIATGYLVLKELGIKVgkYVASEVCEESIAVGTVKHeGNIKYVNDVRNITKKniEEWGPFDLVIGGSPCNDL 654
Cdd:cd00315   1 LRVIDLFAGIGGFRLGLEKAGFEI--VAANEIDKSAAETYEANF-PNKLIEGDITKIDEK--DFIPDIDLLTGGFPCQPF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  655 SNVNpARKGLYEGTGRLFFEFYHLLNYSRPKegddrpfFWMFENVVAMKVGDKRD-----ISRFLECN----PVMIDAIK 725
Cdd:cd00315  76 SIAG-KRKGFEDTRGTLFFEIIRILKEKKPK-------YFLLENVKGLLTHDNGNtlkviLNTLEELGynvyWKLLNASD 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  726 VSAAH-RARYFW-GNLPGMN----RPVIASKNDKLELQDCLeynRIAKLKKVQTITTKSNSIKQGKNQLFPVVMNGKEDV 799
Cdd:cd00315 148 YGVPQnRERVFIiGIRKDLIlnffSPFPKPSEKKKTLKDIL---RIRDPDEPSPTLTASYGKGTGSVHPTAPDMIGKESN 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 5901940  800 ---LWCTELERIFGFPVHYtDVSNMGRGARQKLLGRSWSVPVIRHLF 843
Cdd:cd00315 225 irrLTPRECARLQGFPDDF-EFPGKSVTQAYRQIGNSVPVPVAEAIA 270
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
575-699 5.88e-09

C-5 cytosine-specific DNA methylase;


Pssm-ID: 395093 [Multi-domain]  Cd Length: 324  Bit Score: 58.48  E-value: 5.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940    575 IRVLSLFDGIATGYLVLKELGIKVgkYVASEVCEESIAV-GTVKHEGNIkyvNDVRNITKKNIEEwgpFDLVIGGSPCND 653
Cdd:pfam00145   1 FKFIDLFAGIGGFRLGLEQAGFEC--VAANEIDKSAAKTyEANFPKVPI---GDITLIDIKDIPD---IDILTGGFPCQD 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 5901940    654 LSNVNpARKGLYEGTGRLFFEFYHLLNYSRPKegddrpfFWMFENV 699
Cdd:pfam00145  73 FSIAG-KQKGFEDTRGTLFFEIIRIIKEKKPK-------AFLLENV 110
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
223-265 5.94e-09

PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called 3-hydroxyisobutyrate dehydrogenase-like protein, cytokine-like nuclear factor N-PAC, nuclear protein NP60, or nuclear protein of 60 kDa, is a putative oxidoreductase that is recruited on chromatin and promotes KDM1B demethylase activity. It recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3). GLYR1 enhances the activity of MAP2K4 and MAP2K6 kinases to phosphorylate p38-alpha. In addition to the PWWP domain, GLYR1 also contains an AT-hook and a C-terminal NAD-binding domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438961 [Multi-domain]  Cd Length: 86  Bit Score: 53.76  E-value: 5.94e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 5901940  223 FGIGDLVWGKIKGFSWWPAMVVSWKATSKRQAMS-GMRWVQWFG 265
Cdd:cd05836   1 FKIGDLVWAKMKGFPPWPGKIVNPPPDLKKPPRKkKMHCVYFFG 44
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
627-840 3.45e-08

DNA-methyltransferase (dcm); All proteins in this family for which functions are known are DNA-cytosine methyltransferases. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273211 [Multi-domain]  Cd Length: 315  Bit Score: 56.18  E-value: 3.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940    627 DVRNITKKNIEEwgpFDLVIGGSPCNDLSnVNPARKGLYEGTGRLFFEFYHLLNYSRPKegddrpfFWMFENVVAMKVGD 706
Cdd:TIGR00675  48 DITKISPSDIPD---FDILLGGFPCQPFS-IAGKRKGFEDTRGTLFFEIVRILKEKKPK-------FFLLENVKGLVSHD 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940    707 K-RDISrflecnpVMIDAI---------KVSAA-------HRAR-------YFWGNLPgMNRPVIASKNDKLELQDCLE- 761
Cdd:TIGR00675 117 KgRTFK-------VIIETLeelgykvyyKVLNAkdfgvpqNRERiyivgfrDFDDKLN-FEFPKPIYVAKKKRIGDLLDl 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940    762 --------------------------------------YNRIAKLKKVQTITTK-SNSIKQGKNqlFPVVMNGKEDV--- 799
Cdd:TIGR00675 189 svdleekyylseekknglllllenmrkkegtgeqigsfYNRESKSSIIRTLSARgYTFVKGGKS--VLIVPHKSTVVhpg 266
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 5901940    800 ----LWCTELERIFGFPVHYTDvsNMGRGARQKLLGRSWSVPVIR 840
Cdd:TIGR00675 267 rirrLTPRECARLQGFPDDFKF--PVSDSQLYKQAGNAVVVPVIE 309
PWWP_ScIOC4-like cd05840
PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar ...
226-309 1.42e-07

PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar proteins; ScIOC4 functions as a component of the ISW1B complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW1B complex acts within coding regions to control the amount of RNA polymerase II released into productive elongation and to coordinate elongation with termination and pre-mRNA processing. The family also includes Schizosaccharomyces pombe PWWP domain-containing proteins 1 and 2 (SpPDP1 and SpPDP2). SpPDP1 associates with Set9 to regulate its chromatin localization and methyltransferase activity towards H4K20. Members of this family contain a PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438965  Cd Length: 94  Bit Score: 49.99  E-value: 1.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  226 GDLVWGKIKGFSWWPAMVVS---------WKATSKRQAMSGMRWVQWFGDGKFSEVSADKLVALglfSQHFnLATFNKLV 296
Cdd:cd05840   1 GDLVLAKVKGYPPWPAMVLPeellpknvlKAKKRKPKSKKTVYPVQFFPDNEYYWVSPSSLKPL---TKEE-IDKFLSKS 76
                        90
                ....*....|....
gi 5901940  297 SYR-KAMYHALEKA 309
Cdd:cd05840  77 KRKnKDLIEAYEVA 90
PWWP_PWWP2A cd20152
PWWP domain found in PWWP domain-containing protein 2A (PWWP2A); PWWP2A is a H2A.Z-specific ...
219-310 3.37e-07

PWWP domain found in PWWP domain-containing protein 2A (PWWP2A); PWWP2A is a H2A.Z-specific chromatin binding protein which may play an important role in the neural crest stem cell migration and differentiation during early development. It is also required for proper mitosis progression. PWWP2A and its paralog PWWP2B form a stable complex with NuRD subunits MTA1/2/3:HDAC1/2:RBBP4/7, but not with MBD2/3, p66alpha/beta, and CHD3/4. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438980  Cd Length: 122  Bit Score: 50.01  E-value: 3.37e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  219 DGKEFGIGDLVWGKIKGFSWWPAMVVSWKATSKRqamSGMR-----WVQWFGDGKFSEVSadkLVALGLFSQHFNlATFN 293
Cdd:cd20152  16 DGRTICVGDIVWAKIYGFPWWPARILAITVSRKD---NGLLvrqeaRISWFGSPTTSFLA---LSQLAPFLENFQ-SRFN 88
                        90
                ....*....|....*....
gi 5901940  294 KLVS--YRKAMYHALEKAR 310
Cdd:cd20152  89 KKRKglYRKAITEAAKAAK 107
PWWP_NSD_rpt1 cd20144
first PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
225-266 4.11e-06

first PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein family consists of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1 that are critical in maintaining the chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising in suppressing cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and play nonredundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, through mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (C5HCH). This model corresponds to the first PWWP domain. This family also includes Drosophila melanogaster maternal-effect sterile 4 (dMes4) that may act as a histone-lysine N-methyltransferase required for wing morphogenesis. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438972  Cd Length: 114  Bit Score: 46.54  E-value: 4.11e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 5901940  225 IGDLVWGKIKGFSWWPAMVVS---------WKATSKRQAMsgMRWVQWFGD 266
Cdd:cd20144   1 VGDLVWAKVSGHPWWPCMVTYdpesglytkIKGSGGRTYR--QYHVQFFGD 49
PWWP_NSD2_rpt1 cd20162
first PWWP domain found in nuclear SET domain-containing protein 2 (NSD2) and similar proteins; ...
223-266 5.97e-06

first PWWP domain found in nuclear SET domain-containing protein 2 (NSD2) and similar proteins; NSD2, also called histone-lysine N-methyltransferase NSD2, multiple myeloma SET domain-containing protein (MMSET), or protein trithorax-5 Wolf-Hirschhorn syndrome candidate 1 protein (WHSC1), is overexpressed frequently in the t(4;14) translocation in 15% to 20% of multiple myeloma. It plays important roles in cancer cell proliferation, survival, and tumor growth, through mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. It also enhances androgen receptor (AR)-mediated transcription. The principal chromatin-regulatory activity of NSD2 is dimethylation of histone H3 at lysine 36 (H3K36me2). NSD2 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, a high mobility group (HMG) box, five PHD (plant-homeodomain) zinc finger motifs, and an NSD-specific Cys-His rich domain (C5HCH). The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD domains mediate chromatin interaction and recognition of histone marks. This model corresponds to the first PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438990  Cd Length: 128  Bit Score: 46.44  E-value: 5.97e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 5901940  223 FGIGDLVWGKIKGFSWWPAMVVS-----WKATSKRQAMSGMRW-VQWFGD 266
Cdd:cd20162   1 YNVGDLVWSKVSGYPWWPCMVSAdpllhSHTKLKGQKKSARQYhVQFFGD 50
PWWP_MSH6 cd05837
PWWP domain found in DNA mismatch repair protein MSH6 and similar proteins; MSH6, also called ...
223-266 1.16e-05

PWWP domain found in DNA mismatch repair protein MSH6 and similar proteins; MSH6, also called G/T mismatch-binding protein (GTBP or GTMBP), MutS protein homolog 6, or MutS-alpha 160 kDa subunit (p160), is a mismatch repair protein homologous to bacterial MutS. It is a component of the post-replicative DNA mismatch repair system (MMR). It heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, it forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Mutations in MSH6 have been linked to increased cancer susceptibility, particularly in hereditary nonpolyposis colorectal cancer in humans. MSH6 contains a PWWP domain, but its role in MSH6 remains unclear. MSH6 orthologs found in Saccharomyces cerevisiae, Caenorhabditis elegans, and Arabidopsis thaliana lack the PWWP domain. PWWP domains typically recognize DNA and histone methylated lysines.


Pssm-ID: 438962  Cd Length: 103  Bit Score: 44.97  E-value: 1.16e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 5901940  223 FGIGDLVWGKIKGFSWWPAMVVSW-KATSKRQAMSGMRW-VQWFGD 266
Cdd:cd05837   1 FSPGDLVWAKLEGYPWWPSLVCNHpTTGFHKKFGKKGEVhVQFFDD 46
PWWP_AtATX1-like cd20142
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
226-280 1.34e-05

PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like proteins ATX1, ATX2, and similar proteins; This family includes A. thaliana ATX1 and ATX2, which are sister paralogs originating from a segmental chromosomal duplication. They are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1, also called protein SET domain group 27, or trithorax-homolog protein 1 (TRX-homolog protein 1), is a methyltransferase that trimethylates histone H3 at lysine 4 (H3K4me3). It also acts as a histone modifier and as a positive effector of gene expression. ATX1 regulates transcription from diverse classes of genes implicated in biotic and abiotic stress responses. It is involved in dehydration stress signaling in both abscisic acid (ABA)-dependent and ABA-independent pathways. ATX2, also called protein SET domain group 30, or trithorax-homolog protein 2 (TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). Both ATX1 and ATX2 are multi-domain containing proteins that consist of an N-terminal PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical plant homeodomain (PHD) domain, a non-canonical extended PHD (ePHD) domain, and a C-terminal SET domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438970 [Multi-domain]  Cd Length: 97  Bit Score: 44.65  E-value: 1.34e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5901940  226 GDLVWGKIKGFSWWPAMVVSWKATSKRQAM------SGMRWVQWFGDGKFSEVSADKLVAL 280
Cdd:cd20142   3 GDVVWAKVKGYPMWPALVIDEEHAERCGLEanrpgkKGTVPVQFFGTYEVARLNPKKVVGF 63
PWWP_HULK cd20147
PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family ...
226-280 2.92e-05

PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family includes HUA2-like proteins 1-3 (HULK1-3), which are probable transcription factors that act with partial redundancy with each other. They may play diverse and essential roles in the control of plant development, physiology and flowering time. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438975 [Multi-domain]  Cd Length: 92  Bit Score: 43.25  E-value: 2.92e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5901940  226 GDLVWGKIKGFSWWPAMVVSWKaTSKRQAMSGMRWVQWFGD--------GKFSEVSADKLVAL 280
Cdd:cd20147   1 GDLVLAKVKGFPAWPAQVSEPE-DWGSAPDPKKVFVHFFGTqqigfcnpGELSEFTEEIKQSL 62
PWWP_AtATX3-like cd20143
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
226-310 3.07e-05

PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like protein ATX3, ATX4, ATX5, and similar proteins; The family includes A. thaliana ATX3 (also called protein SET domain group 14, or trithorax-homolog protein 3), ATX4 (also called protein SET domain group 16, or trithorax-homolog protein 4) and ATX5 (also called protein SET domain group 29, or trithorax-homolog protein 5), which belong to the histone-lysine methyltransferase family. They show distinct phylogenetic origins from the family of ATX1 and ATX2. They are multi-domain containing protein that consists of an N-terminal PWWP domain, a canonical plant homeodomain (PHD) domain, a non-canonical extended PHD (ePHD) domain, and a C-terminal SET domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438971 [Multi-domain]  Cd Length: 100  Bit Score: 43.51  E-value: 3.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901940  226 GDLVWGKIKGFSWWPAMVV---SWKATSKRQAMSGMRWVQWFGDGK---FSEVSADKLValgLFSQhfNLATF---NKLV 296
Cdd:cd20143   3 GDLVWAKVGTHPFWPARVVepaEQAEEVRRRCVPGSLCVYFFGPGGsrdYGWVRRSMIF---PFTD--DLARFqtqKIKN 77
                        90
                ....*....|....*
gi 5901940  297 SYRKAMYH-ALEKAR 310
Cdd:cd20143  78 KKRPQEFQeALEEAK 92
PWWP_ZCWPW1 cd20145
PWWP domain found in zinc finger CW-type PWWP domain protein 1 (ZCWPW1) and similar proteins; ...
222-243 3.78e-05

PWWP domain found in zinc finger CW-type PWWP domain protein 1 (ZCWPW1) and similar proteins; ZCWPW1 is a histone H3K4me3 reader. It is associated with late-onset Alzheimer's disease (LOAD). In addition to the PWWP domain, ZCWPW1 contains a zinc finger CW (zf-CW) domain that is a histone modification reader for the histone H3 tail with trimethylated K4. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438973  Cd Length: 115  Bit Score: 43.69  E-value: 3.78e-05
                        10        20
                ....*....|....*....|..
gi 5901940  222 EFGIGDLVWGKIKGFSWWPAMV 243
Cdd:cd20145   5 KYTPGSLVWAKMPGYPWWPAMV 26
PWWP_HRP cd05834
PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The ...
223-243 4.05e-04

PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The HRP family includes hepatoma-derived growth factor (HDGF), and HDGF-related proteins (HRPs). HDGF, also called high mobility group protein 1-like 2 (HMG-1L2), is a heparin-binding protein that acts as a transcriptional repressor with mitogenic activity for fibroblasts. It is a prognostic factor in several types of cancer. HDGFL1 is also called PWWP domain-containing protein 1 (PWWP1). Its biological function remains unclear. HDGFL2, also called HDGF-related protein 2 (HRP-2), or hepatoma-derived growth factor 2 (HDGF-2), is involved in cellular growth control, through the regulation of cyclin D1 expression. HDGFL3, also called HDGF-related protein 3 (HRP-3), enhances DNA synthesis and may play a role in cell proliferation. The family also includes PC4 and SFRS1-interacting protein (PSIP) and similar proteins. PSIP, also called CLL-associated antigen KW-7, dense fine speckles 70 kDa protein (DFS 70), lens epithelium-derived growth factor (LEDGF), or transcriptional coactivator p75/p52, acts as a transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Members of the HRP family contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438959 [Multi-domain]  Cd Length: 82  Bit Score: 39.84  E-value: 4.05e-04
                        10        20
                ....*....|....*....|.
gi 5901940  223 FGIGDLVWGKIKGFSWWPAMV 243
Cdd:cd05834   1 FKPGDLVFAKVKGYPPWPARI 21
PWWP_NSD3_rpt1 cd20163
first PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar proteins; ...
223-245 7.11e-04

first PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar proteins; NSD3, also called histone-lysine N-methyltransferase NSD3, protein whistle, WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, or Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1-like protein 1, or WHSC1L1), is a lysine methyltransferase encoded by gene NSD3, which is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD3 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, five plant-homeodomain (PHD) zinc finger motifs, and an NSD-specific Cys-His rich domain (C5HCH). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD domains are involved in protein-protein interactions. This model corresponds to the first PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438991  Cd Length: 130  Bit Score: 40.30  E-value: 7.11e-04
                        10        20
                ....*....|....*....|...
gi 5901940  223 FGIGDLVWGKIKGFSWWPAMVVS 245
Cdd:cd20163   1 FQVGDLVWSKVGTYPWWPCMVSS 23
PWWP_BRPF cd05839
PWWP domain found in the bromodomain and PHD finger-containing (BRPF) protein family; The BRPF ...
223-249 2.88e-03

PWWP domain found in the bromodomain and PHD finger-containing (BRPF) protein family; The BRPF family of proteins includes BRPF1, BRD1/BRPF2, and BRPF3. They are scaffold proteins that form monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complexes with other regulatory subunits, such as inhibitor of growth 5 (ING5) and Esa1-associated factor 6 ortholog (EAF6). BRPF proteins have multiple domains, including a plant homeodomain (PHD) zinc finger followed by a non-canonical extended PHD (ePHD) finger, C2HC5HC2H, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. The PHD finger binds to lysine 4 of histone H3 (K4H3), the bromodomain interacts with acetylated lysines on N-terminal tails of histones and other proteins, and the PWWP domain shows histone-binding and chromatin association properties.


Pssm-ID: 438964  Cd Length: 106  Bit Score: 38.02  E-value: 2.88e-03
                        10        20
                ....*....|....*....|....*..
gi 5901940  223 FGIGDLVWGKIKGFSWWPAMVVSWKAT 249
Cdd:cd05839   1 LEPGDLVWAKCRGYPWYPAEIVDPKDP 27
PWWP_BS69 cd20159
PWWP domain found in protein BS69 and similar proteins; Protein BS69, also called zinc finger ...
227-246 6.50e-03

PWWP domain found in protein BS69 and similar proteins; Protein BS69, also called zinc finger MYND domain-containing protein 11 (ZMYND11 or ZMY11), is a ubiquitously expressed nuclear protein acting as a transcriptional co-repressor in association with various transcription factors. It was originally identified as an adenovirus 5 E1A-binding protein that inhibits E1A transactivation, as well as c-Myb transcription. It also mediates repression, at least in part, through interaction with the co-repressor N-CoR. Moreover, it interacts with Toll-interleukin 1 receptor domain (TIR)-containing adaptor molecule-1 (TICAM-1, also named TRIF) to facilitate NF-kappaB activation and type I IFN induction. It associates with PIAS1, a SUMO E3 enzyme, and Ubc9, a SUMO E2 enzyme, and plays an inhibitory role in muscle and neuronal differentiation. Moreover, BS69 regulates Epstein-Barr virus (EBV) latent membrane protein 1 (LMP1)/C-terminal activation region 2 (CTAR2)-mediated NF-kappaB activation by interfering with the complex formation between TNFR-associated death domain protein (TRADD) and LMP1/CTAR2. It also cooperates with tumor necrosis factor receptor (TNFR)-associated factor 3 (TRAF3) in the regulation of EBV-derived LMP1/CTAR1-induced NF-kappaB activation. Furthermore, BS69 is involved in the p53-p21Cip1-mediated senescence pathway. BS69 contains a plant homeodomain (PHD) finger, a bromodomain, a proline-tryptophan-tryptophan-proline (PWWP) domain, and a MYeloid translocation protein 8, Nervy and DEAF-1 (MYND) domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438987  Cd Length: 85  Bit Score: 36.42  E-value: 6.50e-03
                        10        20
                ....*....|....*....|
gi 5901940  227 DLVWGKIKGFSWWPAMVVSW 246
Cdd:cd20159   8 ELVWAKQKGFPYWPAKVIQK 27
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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