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Conserved domains on  [gi|767914097|ref|XP_011530969|]
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DNA (cytosine-5)-methyltransferase 3A isoform X6 [Homo sapiens]

Protein Classification

Dnmt3b_related and ADDz_Dnmt3a domain-containing protein (domain architecture ID 10146849)

protein containing domains Dnmt3b_related, ADDz_Dnmt3a, and Dcm

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ADDz_Dnmt3a cd11729
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3a (Dnmt3a); Dnmt3a is a ...
264-391 6.08e-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  Cd Length: 128  Bit Score: 270.72  E-value: 6.08e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097 264 CRNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 343
Cdd:cd11729    1 CRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767914097 344 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 391
Cdd:cd11729   81 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 128
Dnmt3b_related cd05835
The PWWP domain is an essential component of DNA methyltransferase 3 B (Dnmt3b) which is ...
67-153 2.88e-39

The PWWP domain is an essential component of DNA methyltransferase 3 B (Dnmt3b) which 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 syndrome (immunodeficiency, centromeric instability, and facial anomalies), a rare autosomal recessive disorder characterized by hypomethylation of classical satellite DNA. The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, is a small domain consisting of 100-150 amino acids. The PWWP domain 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.


:

Pssm-ID: 99896  Cd Length: 87  Bit Score: 139.04  E-value: 2.88e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097  67 FGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPMYRKAI 146
Cdd:cd05835    1 FNVGDLVWGKIKGFPWWPGRVVSITVTSKRPPVVGMRWVTWFGSGTFSEVSVDKLSPFSEFFKAFSRYNRKKKGLYKKAI 80

                 ....*..
gi 767914097 147 YEVLQVA 153
Cdd:cd05835   81 YEALEVA 87
Dcm COG0270
Site-specific DNA-cytosine methylase [Replication, recombination and repair];
409-572 1.79e-14

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


:

Pssm-ID: 223348 [Multi-domain]  Cd Length: 328  Bit Score: 74.78  E-value: 1.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097 409 KPIRVLSLFDGIATGLLVLKDLGIQVdrYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEwGPFDLVIGGSPCN 488
Cdd:COG0270    2 EKMKVIDLFAGIGGLSLGFEEAGFEI--VFANEIDPPAVATYKANFPHGDIILGDIKELDGEALRK-SDVDVLIGGPPCQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097 489 DLSIVNPaRKGLYEGTGRLFFEFYRLLHDARPKegddrpFFwLFENVVAM---GVSDKRDISRFLESN-----PVMIDAK 560
Cdd:COG0270   79 DFSIAGK-RRGYDDPRGSLFLEFIRLIEQLRPK------FF-VLENVKGLlssKGQTFDEIKKELEELgygveFNILNAA 150
                        170
                 ....*....|...
gi 767914097 561 EVSAAH-RARYFW 572
Cdd:COG0270  151 DYGVPQsRERVFI 163
 
Name Accession Description Interval E-value
ADDz_Dnmt3a cd11729
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3a (Dnmt3a); Dnmt3a is a ...
264-391 6.08e-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  Cd Length: 128  Bit Score: 270.72  E-value: 6.08e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097 264 CRNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 343
Cdd:cd11729    1 CRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767914097 344 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 391
Cdd:cd11729   81 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 128
Dnmt3b_related cd05835
The PWWP domain is an essential component of DNA methyltransferase 3 B (Dnmt3b) which is ...
67-153 2.88e-39

The PWWP domain is an essential component of DNA methyltransferase 3 B (Dnmt3b) which 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 syndrome (immunodeficiency, centromeric instability, and facial anomalies), a rare autosomal recessive disorder characterized by hypomethylation of classical satellite DNA. The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, is a small domain consisting of 100-150 amino acids. The PWWP domain 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.


Pssm-ID: 99896  Cd Length: 87  Bit Score: 139.04  E-value: 2.88e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097  67 FGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPMYRKAI 146
Cdd:cd05835    1 FNVGDLVWGKIKGFPWWPGRVVSITVTSKRPPVVGMRWVTWFGSGTFSEVSVDKLSPFSEFFKAFSRYNRKKKGLYKKAI 80

                 ....*..
gi 767914097 147 YEVLQVA 153
Cdd:cd05835   81 YEALEVA 87
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
67-125 1.85e-20

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


Pssm-ID: 214603  Cd Length: 63  Bit Score: 85.09  E-value: 1.85e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767914097    67 FGIGELVWGKLRGFSWWPGRIVSWWMTG----RSRAAEGTRWVMWFGDGKFSVVCVEKLMPLS 125
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVISPKMTPdnimKRKSDENLYPVLFFGDKDTAWIPSSKLFPLT 63
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
67-154 2.16e-19

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 organising higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression.


Pssm-ID: 334286  Cd Length: 95  Bit Score: 83.24  E-value: 2.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097   67 FGIGELVWGKLRGFSWWPGRIVSWWMTG----RSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNK---Q 139
Cdd:pfam00855   1 FKPGDLVWAKLKGYPWWPARVCDPEELPenilKKKPKPGLYLVRFFGDSEDAWVKPKDLKPFDEGDEFEYLKKKKKkkkK 80
                          90
                  ....*....|....*
gi 767914097  140 PMYRKAIYEVLQVAS 154
Cdd:pfam00855  81 KKFKKAVEEAEEALK 95
Dcm COG0270
Site-specific DNA-cytosine methylase [Replication, recombination and repair];
409-572 1.79e-14

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


Pssm-ID: 223348 [Multi-domain]  Cd Length: 328  Bit Score: 74.78  E-value: 1.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097 409 KPIRVLSLFDGIATGLLVLKDLGIQVdrYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEwGPFDLVIGGSPCN 488
Cdd:COG0270    2 EKMKVIDLFAGIGGLSLGFEEAGFEI--VFANEIDPPAVATYKANFPHGDIILGDIKELDGEALRK-SDVDVLIGGPPCQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097 489 DLSIVNPaRKGLYEGTGRLFFEFYRLLHDARPKegddrpFFwLFENVVAM---GVSDKRDISRFLESN-----PVMIDAK 560
Cdd:COG0270   79 DFSIAGK-RRGYDDPRGSLFLEFIRLIEQLRPK------FF-VLENVKGLlssKGQTFDEIKKELEELgygveFNILNAA 150
                        170
                 ....*....|...
gi 767914097 561 EVSAAH-RARYFW 572
Cdd:COG0270  151 DYGVPQsRERVFI 163
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
411-684 2.62e-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: 2.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097 411 IRVLSLFDGIATGLLVLKDLGIQVdrYIASEVCEDSITVGMVRHqGKIMYVGDVRSVTQKHIQEwgPFDLVIGGSPCNDL 490
Cdd:cd00315    1 LRVIDLFAGIGGFRLGLEKAGFEI--VAANEIDKSAAETYEANF-PNKLIEGDITKIDEKDFIP--DIDLLTGGFPCQPF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097 491 SIVNpARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVSDKR----DISRFLESN-----PVMIDAKE 561
Cdd:cd00315   76 SIAG-KRKGFEDTRGTLFFEIIRILKEKKPK-------YFLLENVKGLLTHDNGntlkVILNTLEELgynvyWKLLNASD 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097 562 VSAAH-RARYFW-GNLPGMNRPLASTV----NDKLELQECLehgRIAKFSKV-RTITTRSNSIKQGKDQHFPVFMNEKED 634
Cdd:cd00315  148 YGVPQnRERVFIiGIRKDLILNFFSPFpkpsEKKKTLKDIL---RIRDPDEPsPTLTASYGKGTGSVHPTAPDMIGKESN 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767914097 635 ILWCT--EMERVFGFPVHYtDVSNMSRLARQRLLGRSWSVPVIRHLFAPLKE 684
Cdd:cd00315  225 IRRLTprECARLQGFPDDF-EFPGKSVTQAYRQIGNSVPVPVAEAIAKAIKE 275
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
462-676 4.46e-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  Cd Length: 315  Bit Score: 61.19  E-value: 4.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097  462 GDVRSVTQKHIQEwgpFDLVIGGSPCNDLSIvNPARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVS 541
Cdd:TIGR00675  47 GDITKISPSDIPD---FDILLGGFPCQPFSI-AGKRKGFEDTRGTLFFEIVRILKEKKPK-------FFLLENVKGLVSH 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097  542 DK-RDISRFLES--------NPVMIDAKEVSAA-HRAR-------YFWGNLPgMNRPLASTVNDKLELQECLEHG----- 599
Cdd:TIGR00675 116 DKgRTFKVIIETleelgykvYYKVLNAKDFGVPqNRERiyivgfrDFDDKLN-FEFPKPIYVAKKKRIGDLLDLSvdlee 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097  600 ----------------------------------RIAKFSKVRTITTRSNSIKQGKDQ------HFPVFMNEKEDILWCT 639
Cdd:TIGR00675 195 kyylseekknglllllenmrkkegtgeqigsfynRESKSSIIRTLSARGYTFVKGGKSvlivphKSTVVHPGRIRRLTPR 274
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767914097  640 EMERVFGFPVHYTDvsNMSRLARQRLLGRSWSVPVIR 676
Cdd:TIGR00675 275 ECARLQGFPDDFKF--PVSDSQLYKQAGNAVVVPVIE 309
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
411-684 1.97e-08

C-5 cytosine-specific DNA methylase;


Pssm-ID: 333875  Cd Length: 323  Bit Score: 56.16  E-value: 1.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097  411 IRVLSLFDGIATGLLVLKDLGIQVdrYIASEVCEDSITVGMVRHQGKImyVGDVRSVTQKHIQEwgpFDLVIGGSPCNDL 490
Cdd:pfam00145   1 FKFIDLFAGIGGFRLGLEQAGFEC--VAANEIDKSAAKTYEANFPKVP--IGDITKIDIKDIPD---IDILTGGFPCQDF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097  491 SIVNpARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVSDK-RDISRFLES--------NPVMIDAKE 561
Cdd:pfam00145  74 SIAG-KQKGFEDTRGTLFFEIIRIIKEKKPK-------AFLLENVKGLLSHDNgKTLNVILETleelgyhvHWKVLNASD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097  562 VSAAH-RAR-YFWGNLPG--------------MNRPLASTVND------KLELQECLEHGRIAKFSKVRTITTRS----- 614
Cdd:pfam00145 146 YGVPQnRERvFIIGIRKDlilnlvpipdfdfpKPKDLTGTIRDlleesvLDENKYNLSDKFVENHERRKPTTKAPgggyp 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097  615 -----NSIKQGKDQHFPVFMNEKED--------ILWCT-----------------EMERVFGFPVHYTDVSNMSRLARQr 664
Cdd:pfam00145 226 telsrNRVDKVEEGKGPSFTYRKSGrleppktgILIKNggrfrghpknirrltprECARLQGFPDDFIFPGSKTQLYKQ- 304
                         330       340
                  ....*....|....*....|
gi 767914097  665 lLGRSWSVPVIRHLFAPLKE 684
Cdd:pfam00145 305 -IGNAVPVPVAEAIAKEIKK 323
 
Name Accession Description Interval E-value
ADDz_Dnmt3a cd11729
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3a (Dnmt3a); Dnmt3a is a ...
264-391 6.08e-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  Cd Length: 128  Bit Score: 270.72  E-value: 6.08e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097 264 CRNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 343
Cdd:cd11729    1 CRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767914097 344 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 391
Cdd:cd11729   81 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 128
ADDz cd11672
ATRX, Dnmt3 and Dnmt3l PHD-like zinc finger domain (ADDz); The ADDz zinc finger domain is ...
267-365 1.89e-59

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  Cd Length: 99  Bit Score: 194.70  E-value: 1.89e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097 267 IEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLVGP 346
Cdd:cd11672    1 IEDICIACGSLVVIYRHPLFQGGICKNCKKYFLSDDISYDDDGYQSYCRICCEGGNLLCCGNNFCHRCFCKECVDRLVGP 80
                         90
                 ....*....|....*....
gi 767914097 347 GAAQAAIKEDPWNCYMCGH 365
Cdd:cd11672   81 GELSTMDENNQWYCYICHP 99
ADDz_Dnmt3b cd11728
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3b (Dnmt3b); ADDz_Dnmt3b ...
267-386 5.46e-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  Cd Length: 120  Bit Score: 188.91  E-value: 5.46e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097 267 IEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLVGP 346
Cdd:cd11728    1 IEDFCLSCGRSNPATFHPLFEGGLCITCKDRFLELFYMYDDDGYQSYCTVCCEGRELLLCGNASCCRCFCVDCLEVLVGP 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767914097 347 GAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFF 386
Cdd:cd11728   81 GTAAKAKEQDPWSCYMCLPQRCYGVLKRRTDWSVRLQEFF 120
ADDz_Dnmt3 cd11725
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 (Dnmt3); Dnmt3 is a de ...
267-372 1.66e-52

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  Cd Length: 108  Bit Score: 176.43  E-value: 1.66e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097 267 IEDICISCGSLNV--TLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLV 344
Cdd:cd11725    1 IEDICLACGSLEVseTSDHPFFEGGLCKNCKERFLECIFLFDDDGYQMYCTICGGGGEVVLCDNPDCTRVYCTECLDLLL 80
                         90       100
                 ....*....|....*....|....*...
gi 767914097 345 GPGAAQAAIKEDPWNCYMCGHKGTYGLL 372
Cdd:cd11725   81 GPGAVAKILESDPWFCFLCSPESNSLLG 108
ADDz_Dnmt3l cd11727
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 like (Dnmt3l); Dnmt3l ...
265-386 1.44e-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  Cd Length: 123  Bit Score: 163.48  E-value: 1.44e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097 265 RNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLV 344
Cdd:cd11727    1 RSIEEICICCGSLQIHTQHPLFHGGICAPCTEKFLEAFFLYDEDGYQAYCTICCSGETLLMCDDPDCTRCYCFECVDSLV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767914097 345 GPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFF 386
Cdd:cd11727   81 GPGTSEKVKATNNWVCFLCLPSSRSGLLQRKRKWRSQLKAFY 122
Dnmt3b_related cd05835
The PWWP domain is an essential component of DNA methyltransferase 3 B (Dnmt3b) which is ...
67-153 2.88e-39

The PWWP domain is an essential component of DNA methyltransferase 3 B (Dnmt3b) which 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 syndrome (immunodeficiency, centromeric instability, and facial anomalies), a rare autosomal recessive disorder characterized by hypomethylation of classical satellite DNA. The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, is a small domain consisting of 100-150 amino acids. The PWWP domain 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.


Pssm-ID: 99896  Cd Length: 87  Bit Score: 139.04  E-value: 2.88e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097  67 FGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPMYRKAI 146
Cdd:cd05835    1 FNVGDLVWGKIKGFPWWPGRVVSITVTSKRPPVVGMRWVTWFGSGTFSEVSVDKLSPFSEFFKAFSRYNRKKKGLYKKAI 80

                 ....*..
gi 767914097 147 YEVLQVA 153
Cdd:cd05835   81 YEALEVA 87
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
67-125 1.85e-20

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


Pssm-ID: 214603  Cd Length: 63  Bit Score: 85.09  E-value: 1.85e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767914097    67 FGIGELVWGKLRGFSWWPGRIVSWWMTG----RSRAAEGTRWVMWFGDGKFSVVCVEKLMPLS 125
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVISPKMTPdnimKRKSDENLYPVLFFGDKDTAWIPSSKLFPLT 63
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
67-154 2.16e-19

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 organising higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression.


Pssm-ID: 334286  Cd Length: 95  Bit Score: 83.24  E-value: 2.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097   67 FGIGELVWGKLRGFSWWPGRIVSWWMTG----RSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNK---Q 139
Cdd:pfam00855   1 FKPGDLVWAKLKGYPWWPARVCDPEELPenilKKKPKPGLYLVRFFGDSEDAWVKPKDLKPFDEGDEFEYLKKKKKkkkK 80
                          90
                  ....*....|....*
gi 767914097  140 PMYRKAIYEVLQVAS 154
Cdd:pfam00855  81 KKFKKAVEEAEEALK 95
PWWP cd05162
The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, is a small domain consisting of ...
67-151 7.87e-18

The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, is a small domain consisting of 100-150 amino acids. The PWWP domain 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. The function of the PWWP domain is still not known precisely; however, 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: 99894  Cd Length: 87  Bit Score: 78.59  E-value: 7.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097  67 FGIGELVWGKLRGFSWWPGRIVSW---WMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSsfCSAFHQATYNKQPMYR 143
Cdd:cd05162    1 FRPGDLVWAKMKGYPWWPALVVDPpkdSKKAKKKAKEGKVLVLFFGDKTFAWVGAERLKPFT--EHKESEAKQSKRKGFK 78

                 ....*...
gi 767914097 144 KAIYEVLQ 151
Cdd:cd05162   79 KAYDEALE 86
Dcm COG0270
Site-specific DNA-cytosine methylase [Replication, recombination and repair];
409-572 1.79e-14

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


Pssm-ID: 223348 [Multi-domain]  Cd Length: 328  Bit Score: 74.78  E-value: 1.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097 409 KPIRVLSLFDGIATGLLVLKDLGIQVdrYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEwGPFDLVIGGSPCN 488
Cdd:COG0270    2 EKMKVIDLFAGIGGLSLGFEEAGFEI--VFANEIDPPAVATYKANFPHGDIILGDIKELDGEALRK-SDVDVLIGGPPCQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097 489 DLSIVNPaRKGLYEGTGRLFFEFYRLLHDARPKegddrpFFwLFENVVAM---GVSDKRDISRFLESN-----PVMIDAK 560
Cdd:COG0270   79 DFSIAGK-RRGYDDPRGSLFLEFIRLIEQLRPK------FF-VLENVKGLlssKGQTFDEIKKELEELgygveFNILNAA 150
                        170
                 ....*....|...
gi 767914097 561 EVSAAH-RARYFW 572
Cdd:COG0270  151 DYGVPQsRERVFI 163
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
411-684 2.62e-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: 2.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097 411 IRVLSLFDGIATGLLVLKDLGIQVdrYIASEVCEDSITVGMVRHqGKIMYVGDVRSVTQKHIQEwgPFDLVIGGSPCNDL 490
Cdd:cd00315    1 LRVIDLFAGIGGFRLGLEKAGFEI--VAANEIDKSAAETYEANF-PNKLIEGDITKIDEKDFIP--DIDLLTGGFPCQPF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097 491 SIVNpARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVSDKR----DISRFLESN-----PVMIDAKE 561
Cdd:cd00315   76 SIAG-KRKGFEDTRGTLFFEIIRILKEKKPK-------YFLLENVKGLLTHDNGntlkVILNTLEELgynvyWKLLNASD 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097 562 VSAAH-RARYFW-GNLPGMNRPLASTV----NDKLELQECLehgRIAKFSKV-RTITTRSNSIKQGKDQHFPVFMNEKED 634
Cdd:cd00315  148 YGVPQnRERVFIiGIRKDLILNFFSPFpkpsEKKKTLKDIL---RIRDPDEPsPTLTASYGKGTGSVHPTAPDMIGKESN 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767914097 635 ILWCT--EMERVFGFPVHYtDVSNMSRLARQRLLGRSWSVPVIRHLFAPLKE 684
Cdd:cd00315  225 IRRLTprECARLQGFPDDF-EFPGKSVTQAYRQIGNSVPVPVAEAIAKAIKE 275
ADDz_ATRX cd11726
ADDz domain found in ATRX (alpha-thalassemia/mental retardation, X-linked); ADDz_ATRX is a ...
271-363 1.29e-11

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  Cd Length: 102  Bit Score: 61.17  E-value: 1.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097 271 CISCG-SLNVT----LEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCgnNNCCRCFCVECVDLLVG 345
Cdd:cd11726    5 CTACGeQLNHFskevHRHPVLKVLICKSCLKFYNSGEFSKDEDGSDEYCRWCGQGGDLICC--DFCPNVFCKKCIKRNLG 82
                         90
                 ....*....|....*...
gi 767914097 346 PGAAQAAIKEDPWNCYMC 363
Cdd:cd11726   83 RAELSRIEESDKWKCFVC 100
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
462-676 4.46e-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  Cd Length: 315  Bit Score: 61.19  E-value: 4.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097  462 GDVRSVTQKHIQEwgpFDLVIGGSPCNDLSIvNPARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVS 541
Cdd:TIGR00675  47 GDITKISPSDIPD---FDILLGGFPCQPFSI-AGKRKGFEDTRGTLFFEIVRILKEKKPK-------FFLLENVKGLVSH 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097  542 DK-RDISRFLES--------NPVMIDAKEVSAA-HRAR-------YFWGNLPgMNRPLASTVNDKLELQECLEHG----- 599
Cdd:TIGR00675 116 DKgRTFKVIIETleelgykvYYKVLNAKDFGVPqNRERiyivgfrDFDDKLN-FEFPKPIYVAKKKRIGDLLDLSvdlee 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097  600 ----------------------------------RIAKFSKVRTITTRSNSIKQGKDQ------HFPVFMNEKEDILWCT 639
Cdd:TIGR00675 195 kyylseekknglllllenmrkkegtgeqigsfynRESKSSIIRTLSARGYTFVKGGKSvlivphKSTVVHPGRIRRLTPR 274
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 767914097  640 EMERVFGFPVHYTDvsNMSRLARQRLLGRSWSVPVIR 676
Cdd:TIGR00675 275 ECARLQGFPDDFKF--PVSDSQLYKQAGNAVVVPVIE 309
N_Pac_NP60 cd05836
The PWWP domain is an essential part of the cytokine-like nuclear factor n-pac protein, or ...
67-146 4.70e-09

The PWWP domain is an essential part of the cytokine-like nuclear factor n-pac protein, or NP60, which enhances the activity of MAP2K4 and MAP2K6 kinases to phosphorylate p38-alpha. In a variety of cell lines, NP60 has been shown to localize to the nucleus. In addition to the PWWP domain, NP60 also contains an AT-hook and a C-terminal NAD-binding domain. The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, is a small domain consisting of 100-150 amino acids. The PWWP domain 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.


Pssm-ID: 99897  Cd Length: 86  Bit Score: 53.61  E-value: 4.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097  67 FGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEG-TRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQAtyNKQPMYRKA 145
Cdd:cd05836    1 LKLGDLVWAKMKGFPPWPGRIVKPPKDLKKPRGKAkCFFVFFFGSENHAWIKEENIKPYHEHKEEMIKL--NKGARFQQA 78

                 .
gi 767914097 146 I 146
Cdd:cd05836   79 V 79
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
411-684 1.97e-08

C-5 cytosine-specific DNA methylase;


Pssm-ID: 333875  Cd Length: 323  Bit Score: 56.16  E-value: 1.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097  411 IRVLSLFDGIATGLLVLKDLGIQVdrYIASEVCEDSITVGMVRHQGKImyVGDVRSVTQKHIQEwgpFDLVIGGSPCNDL 490
Cdd:pfam00145   1 FKFIDLFAGIGGFRLGLEQAGFEC--VAANEIDKSAAKTYEANFPKVP--IGDITKIDIKDIPD---IDILTGGFPCQDF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097  491 SIVNpARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVSDK-RDISRFLES--------NPVMIDAKE 561
Cdd:pfam00145  74 SIAG-KQKGFEDTRGTLFFEIIRIIKEKKPK-------AFLLENVKGLLSHDNgKTLNVILETleelgyhvHWKVLNASD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097  562 VSAAH-RAR-YFWGNLPG--------------MNRPLASTVND------KLELQECLEHGRIAKFSKVRTITTRS----- 614
Cdd:pfam00145 146 YGVPQnRERvFIIGIRKDlilnlvpipdfdfpKPKDLTGTIRDlleesvLDENKYNLSDKFVENHERRKPTTKAPgggyp 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914097  615 -----NSIKQGKDQHFPVFMNEKED--------ILWCT-----------------EMERVFGFPVHYTDVSNMSRLARQr 664
Cdd:pfam00145 226 telsrNRVDKVEEGKGPSFTYRKSGrleppktgILIKNggrfrghpknirrltprECARLQGFPDDFIFPGSKTQLYKQ- 304
                         330       340
                  ....*....|....*....|
gi 767914097  665 lLGRSWSVPVIRHLFAPLKE 684
Cdd:pfam00145 305 -IGNAVPVPVAEAIAKEIKK 323
HDGF_related cd05834
The PWWP domain is an essential part of the Hepatoma Derived Growth Factor (HDGF) family of ...
67-134 9.99e-04

The PWWP domain is an essential part of the Hepatoma Derived Growth Factor (HDGF) family of proteins, and is necessary for DNA binding by HDGF. This family of endogenous nuclear-targeted mitogens includes HRP (HDGF-related proteins 1, 2, 3, 4, or HPR1, HPR2, HPR3, HPR4, respectively) and lens epithelium-derived growth factor, LEDGF. Members of the HDGF family have been linked to human diseases, and HDGF is a prognostic factor in several types of cancer. The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, is a small domain consisting of 100-150 amino acids. The PWWP domain 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.


Pssm-ID: 99895  Cd Length: 83  Bit Score: 38.42  E-value: 9.99e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767914097  67 FGIGELVWGKLRGFSWWPGRI--VSWWMTGRSRAAegtrwVMWFGDGKFSVVCVEKLMP---------LSSFCSAFHQA 134
Cdd:cd05834    3 FKAGDLVFAKVKGYPAWPARVdePEDWKPPGKKYP-----VYFFGTHETAFLKPEDLFPytenkkkfgKPKKRKGFNEA 76
SPBC215_ISWI_like cd05840
The PWWP domain is a component of the S. pombe hypothetical protein SPBC215, as well as ISWI ...
67-126 1.41e-03

The PWWP domain is a component of the S. pombe hypothetical protein SPBC215, as well as ISWI complex protein 4. The ISWI (imitation switch) proteins are ATPases responsible for chromatin remodeling in eukaryotes, and SPBC215 is proposed to also bind chromatin. The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, is a small domain consisting of 100-150 amino acids. The PWWP domain 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.


Pssm-ID: 99901  Cd Length: 93  Bit Score: 38.07  E-value: 1.41e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767914097  67 FGIGELVWGKLRGFSWWPGRIVSWWMT------GRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSS 126
Cdd:cd05840    1 FQPGDRVLAKVKGFPAWPAIVVPEEMLpdsvlkGKKKKNKRTYPVMFFPDGDYYWVPNKDLKPLTE 66
MUM1_like cd06080
Mutated melanoma-associated antigen 1 (MUM-1) is a melanoma-associated antigen (MAA). MUM-1 ...
67-89 1.51e-03

Mutated melanoma-associated antigen 1 (MUM-1) is a melanoma-associated antigen (MAA). MUM-1 belongs to the mutated or aberrantly expressed type of MAAs, along with antigens such as CDK4, beta-catenin, gp100-in4, p15, and N-acetylglucosaminyltransferase V. It is highly expressed in several types of human cancers. The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, is a small domain consisting of 100-150 amino acids. The PWWP domain 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.


Pssm-ID: 99903  Cd Length: 80  Bit Score: 37.80  E-value: 1.51e-03
                         10        20
                 ....*....|....*....|...
gi 767914097  67 FGIGELVWGKLRGFSWWPGRIVS 89
Cdd:cd06080    1 FEKNDLVWAKIQGYPWWPAVIKS 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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