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Conserved domains on  [gi|2217326180|ref|XP_047299550|]
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DNA (cytosine-5)-methyltransferase 3A isoform X7 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PWWP_DNMT3A cd20154
PWWP domain found in DNA (cytosine-5)-methyltransferase 3A (DNMT3A); DNMT3A, also called DNA ...
125-258 1.30e-103

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: 313.44  E-value: 1.30e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 125 EDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPM 204
Cdd:cd20154     1 EDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFSSAFHQATYNKQPM 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217326180 205 YRKAIYEVLQVASSRAGKLFPVCHDSDESDTAKAVEVQNKPMIEWALGGFQPSG 258
Cdd:cd20154    81 YRKAIYEVLQVASSRAGKLFPVCPESDESDTSKAVEVQNKQMIEWALGGFQPSG 134
ADDz_Dnmt3a cd11729
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3a (Dnmt3a); Dnmt3a is a ...
327-454 2.70e-88

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: 273.42  E-value: 2.70e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 327 CRNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 406
Cdd:cd11729     1 CRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2217326180 407 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 454
Cdd:cd11729    81 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 128
Dcm super family cl43082
DNA-cytosine methylase [Replication, recombination and repair];
471-749 1.61e-19

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: 89.48  E-value: 1.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 471 RKPIRVLSLFDGI---ATGLlvlKDLGIQVdrYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQewGPFDLVIGG 547
Cdd:COG0270     1 SKKLTVIDLFAGAgglSLGF---EKAGFEV--VFAVEIDPDACETYRANFPEAKVIEGDIRDIDPEELI--PDVDLLIGG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 548 SPCNDLSIVNPaRKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVSDK----RDISRFLES-----NPV 618
Cdd:COG0270    74 PPCQPFSVAGK-RKGLEDPRGTLFFEFIRIVEELRPK-------AFVLENVPGLLSSDKgktfEEILKELEElgyrvDYK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 619 MIDAKEVSAA-HRARYF----WGNLPGMNRPLASTVNDKLELQECLEH----GRIAKFSKvrTITTRSNsikqgkdqHFP 689
Cdd:COG0270   146 VLNAADYGVPqNRERVFivgfRKDLDLFEFPEPTHLKPYVTVGDALEDlpdaHEARYLSE--TITAGYG--------GGG 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217326180 690 VFMNEKEDIlWCT--EMERVFGFPVHYTDVSNMSRLARQrlLGRSWSVPVIRHLFAPLKEYF 749
Cdd:COG0270   216 RFLHPGEPR-RLTvrEAARLQGFPDDFKFPGSKTQAYRQ--IGNAVPPPLAEAIAKAILKAL 274
 
Name Accession Description Interval E-value
PWWP_DNMT3A cd20154
PWWP domain found in DNA (cytosine-5)-methyltransferase 3A (DNMT3A); DNMT3A, also called DNA ...
125-258 1.30e-103

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: 313.44  E-value: 1.30e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 125 EDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPM 204
Cdd:cd20154     1 EDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFSSAFHQATYNKQPM 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217326180 205 YRKAIYEVLQVASSRAGKLFPVCHDSDESDTAKAVEVQNKPMIEWALGGFQPSG 258
Cdd:cd20154    81 YRKAIYEVLQVASSRAGKLFPVCPESDESDTSKAVEVQNKQMIEWALGGFQPSG 134
ADDz_Dnmt3a cd11729
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3a (Dnmt3a); Dnmt3a is a ...
327-454 2.70e-88

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: 273.42  E-value: 2.70e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 327 CRNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 406
Cdd:cd11729     1 CRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2217326180 407 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 454
Cdd:cd11729    81 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 128
ADD_DNMT3 pfam17980
Cysteine rich ADD domain in DNMT3; This is a cysteine-rich domain termed ADD ...
315-370 4.00e-31

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: 115.46  E-value: 4.00e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217326180 315 TRERLVYEVRQKCRNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDD 370
Cdd:pfam17980   1 SREQMVYEVRENKRNIEDFCLSCGSLNVHTFHPLFEGGLCQKCKDNFLETLYRYDE 56
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
130-188 3.67e-20

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 84.70  E-value: 3.67e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217326180  130 FGIGELVWGKLRGFSWWPGRIVSWWMTG----RSRAAEGTRWVMWFGDGKFSVVCVEKLMPLS 188
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVISPKMTPdnimKRKSDENLYPVLFFGDKDTAWIPSSKLFPLT 63
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
471-749 1.61e-19

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


Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 89.48  E-value: 1.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 471 RKPIRVLSLFDGI---ATGLlvlKDLGIQVdrYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQewGPFDLVIGG 547
Cdd:COG0270     1 SKKLTVIDLFAGAgglSLGF---EKAGFEV--VFAVEIDPDACETYRANFPEAKVIEGDIRDIDPEELI--PDVDLLIGG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 548 SPCNDLSIVNPaRKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVSDK----RDISRFLES-----NPV 618
Cdd:COG0270    74 PPCQPFSVAGK-RKGLEDPRGTLFFEFIRIVEELRPK-------AFVLENVPGLLSSDKgktfEEILKELEElgyrvDYK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 619 MIDAKEVSAA-HRARYF----WGNLPGMNRPLASTVNDKLELQECLEH----GRIAKFSKvrTITTRSNsikqgkdqHFP 689
Cdd:COG0270   146 VLNAADYGVPqNRERVFivgfRKDLDLFEFPEPTHLKPYVTVGDALEDlpdaHEARYLSE--TITAGYG--------GGG 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217326180 690 VFMNEKEDIlWCT--EMERVFGFPVHYTDVSNMSRLARQrlLGRSWSVPVIRHLFAPLKEYF 749
Cdd:COG0270   216 RFLHPGEPR-RLTvrEAARLQGFPDDFKFPGSKTQAYRQ--IGNAVPPPLAEAIAKAILKAL 274
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
133-217 2.98e-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: 77.47  E-value: 2.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 133 GELVWGKLRGFSWWPGRIVSWWMTGRS----RAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNK---QPMY 205
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVVDPEELPENvlkpKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEFEYLKKKKKkkkKKAF 80
                          90
                  ....*....|..
gi 2217326180 206 RKAIYEVLQVAS 217
Cdd:pfam00855  81 KKALEEAEEALK 92
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
474-747 3.45e-13

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: 70.34  E-value: 3.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 474 IRVLSLFDGIATGLLVLKDLGIQVdrYIASEVCEDSITVGMVRHqGKIMYVGDVRSVTQKHIQEwgPFDLVIGGSPCNDL 553
Cdd:cd00315     1 LRVIDLFAGIGGFRLGLEKAGFEI--VAANEIDKSAAETYEANF-PNKLIEGDITKIDEKDFIP--DIDLLTGGFPCQPF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 554 SIVNpARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVSDKR----DISRFLESN-----PVMIDAKE 624
Cdd:cd00315    76 SIAG-KRKGFEDTRGTLFFEIIRILKEKKPK-------YFLLENVKGLLTHDNGntlkVILNTLEELgynvyWKLLNASD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 625 VSAAH-RARYFW-GNLPGMNRPLASTV----NDKLELQECLehgRIAKFSKV-RTITTRSNSIKQGKDQHFPVFMNEKED 697
Cdd:cd00315   148 YGVPQnRERVFIiGIRKDLILNFFSPFpkpsEKKKTLKDIL---RIRDPDEPsPTLTASYGKGTGSVHPTAPDMIGKESN 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217326180 698 ILWCT--EMERVFGFPVHYtDVSNMSRLARQRLLGRSWSVPVIRHLFAPLKE 747
Cdd:cd00315   225 IRRLTprECARLQGFPDDF-EFPGKSVTQAYRQIGNSVPVPVAEAIAKAIKE 275
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
525-739 5.89e-10

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: 61.19  E-value: 5.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 525 GDVRSVTQKHIQEwgpFDLVIGGSPCNDLSIvNPARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVS 604
Cdd:TIGR00675  47 GDITKISPSDIPD---FDILLGGFPCQPFSI-AGKRKGFEDTRGTLFFEIVRILKEKKPK-------FFLLENVKGLVSH 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 605 DK-RDISRFLES--------NPVMIDAKEVSAA-HRAR-------YFWGNLPgMNRPLASTVNDKLELQECLEHG----- 662
Cdd:TIGR00675 116 DKgRTFKVIIETleelgykvYYKVLNAKDFGVPqNRERiyivgfrDFDDKLN-FEFPKPIYVAKKKRIGDLLDLSvdlee 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 663 ----------------------------------RIAKFSKVRTITTRSNSIKQGKDQ------HFPVFMNEKEDILWCT 702
Cdd:TIGR00675 195 kyylseekknglllllenmrkkegtgeqigsfynRESKSSIIRTLSARGYTFVKGGKSvlivphKSTVVHPGRIRRLTPR 274
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2217326180 703 EMERVFGFPVHYTDvsNMSRLARQRLLGRSWSVPVIR 739
Cdd:TIGR00675 275 ECARLQGFPDDFKF--PVSDSQLYKQAGNAVVVPVIE 309
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
474-598 2.88e-08

C-5 cytosine-specific DNA methylase;


Pssm-ID: 395093 [Multi-domain]  Cd Length: 324  Bit Score: 56.17  E-value: 2.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 474 IRVLSLFDGIATGLLVLKDLGIQVdrYIASEVCEDSITVGMVRHQGKImyVGDVRSVTQKHIQEwgpFDLVIGGSPCNDL 553
Cdd:pfam00145   1 FKFIDLFAGIGGFRLGLEQAGFEC--VAANEIDKSAAKTYEANFPKVP--IGDITLIDIKDIPD---IDILTGGFPCQDF 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2217326180 554 SIVNpARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENV 598
Cdd:pfam00145  74 SIAG-KQKGFEDTRGTLFFEIIRIIKEKKPK-------AFLLENV 110
 
Name Accession Description Interval E-value
PWWP_DNMT3A cd20154
PWWP domain found in DNA (cytosine-5)-methyltransferase 3A (DNMT3A); DNMT3A, also called DNA ...
125-258 1.30e-103

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: 313.44  E-value: 1.30e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 125 EDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPM 204
Cdd:cd20154     1 EDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFSSAFHQATYNKQPM 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217326180 205 YRKAIYEVLQVASSRAGKLFPVCHDSDESDTAKAVEVQNKPMIEWALGGFQPSG 258
Cdd:cd20154    81 YRKAIYEVLQVASSRAGKLFPVCPESDESDTSKAVEVQNKQMIEWALGGFQPSG 134
ADDz_Dnmt3a cd11729
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3a (Dnmt3a); Dnmt3a is a ...
327-454 2.70e-88

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: 273.42  E-value: 2.70e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 327 CRNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 406
Cdd:cd11729     1 CRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2217326180 407 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 454
Cdd:cd11729    81 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 128
ADDz cd11672
ATRX, Dnmt3 and Dnmt3l PHD-like zinc finger domain (ADDz); The ADDz zinc finger domain is ...
330-428 4.00e-60

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: 197.78  E-value: 4.00e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 330 IEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLVGP 409
Cdd:cd11672     1 IEDICIACGSLVVIYRHPLFQGGICKNCKKYFLSDDISYDDDGYQSYCRICCEGGNLLCCGNNFCHRCFCKECVDRLVGP 80
                          90
                  ....*....|....*....
gi 2217326180 410 GAAQAAIKEDPWNCYMCGH 428
Cdd:cd11672    81 GELSTMDENNQWYCYICHP 99
ADDz_Dnmt3b cd11728
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3b (Dnmt3b); ADDz_Dnmt3b ...
330-449 3.75e-57

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: 190.45  E-value: 3.75e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 330 IEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLVGP 409
Cdd:cd11728     1 IEDFCLSCGRSNPATFHPLFEGGLCITCKDRFLELFYMYDDDGYQSYCTVCCEGRELLLCGNASCCRCFCVDCLEVLVGP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217326180 410 GAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFF 449
Cdd:cd11728    81 GTAAKAKEQDPWSCYMCLPQRCYGVLKRRTDWSVRLQEFF 120
ADDz_Dnmt3 cd11725
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 (Dnmt3); Dnmt3 is a de ...
330-435 3.59e-53

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: 179.12  E-value: 3.59e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 330 IEDICISCGSLNV--TLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLV 407
Cdd:cd11725     1 IEDICLACGSLEVseTSDHPFFEGGLCKNCKERFLECIFLFDDDGYQMYCTICGGGGEVVLCDNPDCTRVYCTECLDLLL 80
                          90       100
                  ....*....|....*....|....*...
gi 2217326180 408 GPGAAQAAIKEDPWNCYMCGHKGTYGLL 435
Cdd:cd11725    81 GPGAVAKILESDPWFCFLCSPESNSLLG 108
PWWP_DNMT3B cd20155
PWWP domain found in DNA (cytosine-5)-methyltransferase 3B (DNMT3B); DNMT3B, also called DNA ...
131-254 4.71e-51

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: 173.52  E-value: 4.71e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 131 GIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPMYRKAIY 210
Cdd:cd20155     1 GIGELVWGKIKGFSWWPAMVVSWRATGKRQASSGMRWLQWFGDGKFSEVSADKLVSLTAFSQHFNLSTYNKLVSYRKAMY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2217326180 211 EVLQVASSRAGKLFPvchdsdeSDTAKAVEVQNKPMIEWALGGF 254
Cdd:cd20155    81 HALEVARVRAGKTFP-------SSPGESLEDQLKPMLDWAHGGF 117
ADDz_Dnmt3l cd11727
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 like (Dnmt3l); Dnmt3l ...
328-449 7.66e-48

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: 165.03  E-value: 7.66e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 328 RNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLV 407
Cdd:cd11727     1 RSIEEICICCGSLQIHTQHPLFHGGICAPCTEKFLEAFFLYDEDGYQAYCTICCSGETLLMCDDPDCTRCYCFECVDSLV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2217326180 408 GPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFF 449
Cdd:cd11727    81 GPGTSEKVKATNNWVCFLCLPSSRSGLLQRKRKWRSQLKAFY 122
PWWP_DNMT3 cd05835
PWWP domain found in the DNA (cytosine-5)-methyltransferase 3 (DNMT3) family; The DNMT3 family ...
132-220 4.47e-37

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: 133.54  E-value: 4.47e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 132 IGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQaTYNKQPMYRKAIYE 211
Cdd:cd05835     2 IGDLVWAKLKGSPWWPGIVVSHKDCGQKPPAEGSVWVFWFGDHKVSEVPLDKILPFAEFFNKFYI-SKNSSKLYKKAVYE 80

                  ....*....
gi 2217326180 212 VLQVASSRA 220
Cdd:cd05835    81 ALKEAAERS 89
ADD_DNMT3 pfam17980
Cysteine rich ADD domain in DNMT3; This is a cysteine-rich domain termed ADD ...
315-370 4.00e-31

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: 115.46  E-value: 4.00e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217326180 315 TRERLVYEVRQKCRNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDD 370
Cdd:pfam17980   1 SREQMVYEVRENKRNIEDFCLSCGSLNVHTFHPLFEGGLCQKCKDNFLETLYRYDE 56
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
130-188 3.67e-20

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 84.70  E-value: 3.67e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217326180  130 FGIGELVWGKLRGFSWWPGRIVSWWMTG----RSRAAEGTRWVMWFGDGKFSVVCVEKLMPLS 188
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVISPKMTPdnimKRKSDENLYPVLFFGDKDTAWIPSSKLFPLT 63
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
471-749 1.61e-19

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


Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 89.48  E-value: 1.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 471 RKPIRVLSLFDGI---ATGLlvlKDLGIQVdrYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQewGPFDLVIGG 547
Cdd:COG0270     1 SKKLTVIDLFAGAgglSLGF---EKAGFEV--VFAVEIDPDACETYRANFPEAKVIEGDIRDIDPEELI--PDVDLLIGG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 548 SPCNDLSIVNPaRKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVSDK----RDISRFLES-----NPV 618
Cdd:COG0270    74 PPCQPFSVAGK-RKGLEDPRGTLFFEFIRIVEELRPK-------AFVLENVPGLLSSDKgktfEEILKELEElgyrvDYK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 619 MIDAKEVSAA-HRARYF----WGNLPGMNRPLASTVNDKLELQECLEH----GRIAKFSKvrTITTRSNsikqgkdqHFP 689
Cdd:COG0270   146 VLNAADYGVPqNRERVFivgfRKDLDLFEFPEPTHLKPYVTVGDALEDlpdaHEARYLSE--TITAGYG--------GGG 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217326180 690 VFMNEKEDIlWCT--EMERVFGFPVHYTDVSNMSRLARQrlLGRSWSVPVIRHLFAPLKEYF 749
Cdd:COG0270   216 RFLHPGEPR-RLTvrEAARLQGFPDDFKFPGSKTQAYRQ--IGNAVPPPLAEAIAKAILKAL 274
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
133-217 2.98e-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: 77.47  E-value: 2.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 133 GELVWGKLRGFSWWPGRIVSWWMTGRS----RAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNK---QPMY 205
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVVDPEELPENvlkpKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEFEYLKKKKKkkkKKAF 80
                          90
                  ....*....|..
gi 2217326180 206 RKAIYEVLQVAS 217
Cdd:pfam00855  81 KKALEEAEEALK 92
PWWP_PWWP2B cd20153
PWWP domain found in PWWP domain-containing protein 2B (PWWP2B); PWWP2B is a paralog of PWWP2A, ...
125-216 3.18e-14

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: 69.60  E-value: 3.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 125 EDGRGFGIGELVWGKLRGFSWWPGRIVSwwmTGRSRAAEGT-RW----VMWFGDGKFSVVCVEKLMPLSSfcsaFHQATY 199
Cdd:cd20153     9 EEGRTVSVGDIVWGKIHGFPWWPARVLS---ISLSQKEDGEpSWqeakVSWFGSPTTSLLSVSKLSPFSE----FFKLRF 81
                          90
                  ....*....|....*....
gi 2217326180 200 N--KQPMYRKAIYEVLQVA 216
Cdd:cd20153    82 NrkKKGMYRKAITEAAKAA 100
PWWP_MBD5 cd20141
PWWP domain found in methyl-CpG-binding domain protein 5 (MBD5) and similar proteins; MBD5, is ...
130-197 5.86e-14

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: 68.11  E-value: 5.86e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217326180 130 FGIGELVWGKLRGFSWWPGRIVSwwMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQA 197
Cdd:cd20141     1 FNVGDLVWGQIRGFPSWPGKLVS--ENDVGKTNEGKVWVSWFGDHSFGQVEPDKLKTLSEGLEAHHRA 66
PWWP cd05162
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
133-211 2.96e-13

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: 65.60  E-value: 2.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 133 GELVWGKLRGFSWWPGRIVSWWMTG---RSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPMYRKAI 209
Cdd:cd05162     1 GDLVWAKLKGYPWWPARVVDPEELPeevGKKKKKGGVLVQFFGDNDYAWVKSKNIKPFEEGFKKEFKKKKKKSKKFKKAV 80

                  ..
gi 2217326180 210 YE 211
Cdd:cd05162    81 EE 82
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
474-747 3.45e-13

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: 70.34  E-value: 3.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 474 IRVLSLFDGIATGLLVLKDLGIQVdrYIASEVCEDSITVGMVRHqGKIMYVGDVRSVTQKHIQEwgPFDLVIGGSPCNDL 553
Cdd:cd00315     1 LRVIDLFAGIGGFRLGLEKAGFEI--VAANEIDKSAAETYEANF-PNKLIEGDITKIDEKDFIP--DIDLLTGGFPCQPF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 554 SIVNpARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVSDKR----DISRFLESN-----PVMIDAKE 624
Cdd:cd00315    76 SIAG-KRKGFEDTRGTLFFEIIRILKEKKPK-------YFLLENVKGLLTHDNGntlkVILNTLEELgynvyWKLLNASD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 625 VSAAH-RARYFW-GNLPGMNRPLASTV----NDKLELQECLehgRIAKFSKV-RTITTRSNSIKQGKDQHFPVFMNEKED 697
Cdd:cd00315   148 YGVPQnRERVFIiGIRKDLILNFFSPFpkpsEKKKTLKDIL---RIRDPDEPsPTLTASYGKGTGSVHPTAPDMIGKESN 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217326180 698 ILWCT--EMERVFGFPVHYtDVSNMSRLARQRLLGRSWSVPVIRHLFAPLKE 747
Cdd:cd00315   225 IRRLTprECARLQGFPDDF-EFPGKSVTQAYRQIGNSVPVPVAEAIAKAIKE 275
PWWP_PWWP2 cd20140
PWWP domain found in the PWWP domain-containing protein 2 (PWWP2) family; The PWWP2 family ...
127-218 4.85e-13

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: 65.36  E-value: 4.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 127 GRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRW--VMWFGDGKFSVVCVEKLMPlssFCSAFHQaTYNKQP- 203
Cdd:cd20140     1 GRTLRVGDIVWGKIHGFPWWPGRILSITVSRDDNGELSTQEahVSWFGSSTTSYMPCSQLYP---FLEDFKL-RYNKKKr 76
                          90
                  ....*....|....*.
gi 2217326180 204 -MYRKAIYEVLQVASS 218
Cdd:cd20140    77 gPYKEAVRQALEAAKQ 92
PWWP_PWWP2A cd20152
PWWP domain found in PWWP domain-containing protein 2A (PWWP2A); PWWP2A is a H2A.Z-specific ...
126-217 8.00e-13

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: 65.80  E-value: 8.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 126 DGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAA--EGTRWVMWFGDGKFSVVCVEKLMP-LSSFCSAFHQatyNKQ 202
Cdd:cd20152    16 DGRTICVGDIVWAKIYGFPWWPARILAITVSRKDNGLlvRQEARISWFGSPTTSFLALSQLAPfLENFQSRFNK---KRK 92
                          90
                  ....*....|....*
gi 2217326180 203 PMYRKAIYEVLQVAS 217
Cdd:cd20152    93 GLYRKAITEAAKAAK 107
ADDz_ATRX cd11726
ADDz domain found in ATRX (alpha-thalassemia/mental retardation, X-linked); ADDz_ATRX is a ...
334-426 8.79e-12

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: 61.94  E-value: 8.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 334 CISCG-SLNVT----LEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCgnNNCCRCFCVECVDLLVG 408
Cdd:cd11726     5 CTACGeQLNHFskevHRHPVLKVLICKSCLKFYNSGEFSKDEDGSDEYCRWCGQGGDLICC--DFCPNVFCKKCIKRNLG 82
                          90
                  ....*....|....*...
gi 2217326180 409 PGAAQAAIKEDPWNCYMC 426
Cdd:cd11726    83 RAELSRIEESDKWKCFVC 100
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
525-739 5.89e-10

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: 61.19  E-value: 5.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 525 GDVRSVTQKHIQEwgpFDLVIGGSPCNDLSIvNPARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVS 604
Cdd:TIGR00675  47 GDITKISPSDIPD---FDILLGGFPCQPFSI-AGKRKGFEDTRGTLFFEIVRILKEKKPK-------FFLLENVKGLVSH 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 605 DK-RDISRFLES--------NPVMIDAKEVSAA-HRAR-------YFWGNLPgMNRPLASTVNDKLELQECLEHG----- 662
Cdd:TIGR00675 116 DKgRTFKVIIETleelgykvYYKVLNAKDFGVPqNRERiyivgfrDFDDKLN-FEFPKPIYVAKKKRIGDLLDLSvdlee 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 663 ----------------------------------RIAKFSKVRTITTRSNSIKQGKDQ------HFPVFMNEKEDILWCT 702
Cdd:TIGR00675 195 kyylseekknglllllenmrkkegtgeqigsfynRESKSSIIRTLSARGYTFVKGGKSvlivphKSTVVHPGRIRRLTPR 274
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2217326180 703 EMERVFGFPVHYTDvsNMSRLARQRLLGRSWSVPVIR 739
Cdd:TIGR00675 275 ECARLQGFPDDFKF--PVSDSQLYKQAGNAVVVPVIE 309
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
474-598 2.88e-08

C-5 cytosine-specific DNA methylase;


Pssm-ID: 395093 [Multi-domain]  Cd Length: 324  Bit Score: 56.17  E-value: 2.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 474 IRVLSLFDGIATGLLVLKDLGIQVdrYIASEVCEDSITVGMVRHQGKImyVGDVRSVTQKHIQEwgpFDLVIGGSPCNDL 553
Cdd:pfam00145   1 FKFIDLFAGIGGFRLGLEQAGFEC--VAANEIDKSAAKTYEANFPKVP--IGDITLIDIKDIPD---IDILTGGFPCQDF 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2217326180 554 SIVNpARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENV 598
Cdd:pfam00145  74 SIAG-KQKGFEDTRGTLFFEIIRIIKEKKPK-------AFLLENV 110
PWWP_AtATX3-like cd20143
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
133-217 3.28e-07

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: 48.90  E-value: 3.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 133 GELVWGKLRGFSWWPGRIV---SWWMTGRSRAAEGTRWVMWFGDGK---FSVVCVEKLMPLSSFCSAFHQATY--NKQP- 203
Cdd:cd20143     3 GDLVWAKVGTHPFWPARVVepaEQAEEVRRRCVPGSLCVYFFGPGGsrdYGWVRRSMIFPFTDDLARFQTQKIknKKRPq 82
                          90
                  ....*....|....
gi 2217326180 204 MYRKAIYEVLQVAS 217
Cdd:cd20143    83 EFQEALEEAKLADA 96
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
130-212 1.03e-05

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: 44.13  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 130 FGIGELVWGKLRGFSWWPGRIVS-WWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFhqATYNKQPMYRKA 208
Cdd:cd05836     1 FKIGDLVWAKMKGFPPWPGKIVNpPPDLKKPPRKKKMHCVYFFGSENYAWIEDENIKPYEEFKEEM--LKSKKSAGFKDA 78

                  ....
gi 2217326180 209 IYEV 212
Cdd:cd05836    79 VEAI 82
PWWP_HRP cd05834
PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The ...
130-211 1.56e-03

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: 37.92  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 130 FGIGELVWGKLRGFSWWPGRIvswwmtgrSRAAEGTRW------VMWFGDGKFSVVCVEKLMPLSSFcsAFHQATYNKQP 203
Cdd:cd05834     1 FKPGDLVFAKVKGYPPWPARI--------DEIPEGAKIpknkypVFFYGTHETAFLKPKDLFPYEEN--KEKYGKPRKRK 70

                  ....*...
gi 2217326180 204 MYRKAIYE 211
Cdd:cd05834    71 GFNEGLWE 78
PWWP_MSH6 cd05837
PWWP domain found in DNA mismatch repair protein MSH6 and similar proteins; MSH6, also called ...
130-148 2.89e-03

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: 38.04  E-value: 2.89e-03
                          10
                  ....*....|....*....
gi 2217326180 130 FGIGELVWGKLRGFSWWPG 148
Cdd:cd05837     1 FSPGDLVWAKLEGYPWWPS 19
PWWP_ScIOC4-like cd05840
PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar ...
133-218 4.39e-03

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: 37.28  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326180 133 GELVWGKLRGFSWWPGRIVS--------WWMTGRSRAAEGTRW-VMWFGDGKFSVVCVEKLMPLS-SFCSAFHQATYNKQ 202
Cdd:cd05840     1 GDLVLAKVKGYPPWPAMVLPeellpknvLKAKKRKPKSKKTVYpVQFFPDNEYYWVSPSSLKPLTkEEIDKFLSKSKRKN 80
                          90
                  ....*....|....*.
gi 2217326180 203 pmyrKAIYEVLQVASS 218
Cdd:cd05840    81 ----KDLIEAYEVALE 92
PWWP_ZCWPW2 cd20146
PWWP domain found in zinc finger CW-type PWWP domain protein 2 (ZCWPW2) and similar proteins; ...
133-150 5.04e-03

PWWP domain found in zinc finger CW-type PWWP domain protein 2 (ZCWPW2) and similar proteins; ZCWPW2 is a histone H3K4me3 reader. In addition to the PWWP domain, ZCWPW2 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: 438974  Cd Length: 113  Bit Score: 37.28  E-value: 5.04e-03
                          10
                  ....*....|....*...
gi 2217326180 133 GELVWGKLRGFSWWPGRI 150
Cdd:cd20146    12 GSLVWAKMTGYPRWPAIL 29
 
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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