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Conserved domains on  [gi|51556225|ref|NP_001003958|]
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DNA (cytosine-5)-methyltransferase 3A isoform 1 [Rattus norvegicus]

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 ...
 281-414 1.22e-102

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: 314.60  E-value: 1.22e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 281 EDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPM 360
Cdd:cd20154   1 EDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFSSAFHQATYNKQPM 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 51556225 361 YRKAIYEVLQVASSRAGKLFPACHDSDESDTGKAVEVQNKQMIEWALGGFQPSG 414
Cdd:cd20154  81 YRKAIYEVLQVASSRAGKLFPVCPESDESDTSKAVEVQNKQMIEWALGGFQPSG 134
ADDz_Dnmt3a cd11729
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3a (Dnmt3a); Dnmt3a is a ...
 483-610 1.48e-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: 277.27  E-value: 1.48e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 483 CRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 562
Cdd:cd11729   1 CRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 51556225 563 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 610
Cdd:cd11729  81 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 128
Dcm super family cl43082
DNA-cytosine methylase [Replication, recombination and repair];
627-905 1.24e-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: 89.87  E-value: 1.24e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 627 RKPIRVLSLFDGI---ATGLlvlKDLGIQVdrYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQewGPFDLVIGG 703
Cdd:COG0270   1 SKKLTVIDLFAGAgglSLGF---EKAGFEV--VFAVEIDPDACETYRANFPEAKVIEGDIRDIDPEELI--PDVDLLIGG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 704 SPCNDLSIVNPaRKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVSDK----RDISRFLES-----NPV 774
Cdd:COG0270  74 PPCQPFSVAGK-RKGLEDPRGTLFFEFIRIVEELRPK-------AFVLENVPGLLSSDKgktfEEILKELEElgyrvDYK 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 775 MIDAKEVSAA-HRARYF----WGNLPGMNRPLASTVNDKLELQECLEH----GRIAKFSKvrTITTRSNsikqgkdqHFP 845
Cdd:COG0270 146 VLNAADYGVPqNRERVFivgfRKDLDLFEFPEPTHLKPYVTVGDALEDlpdaHEARYLSE--TITAGYG--------GGG 215

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51556225 846 VFMNEKEDIlWCT--EMERVFGFPVHYTDVSNMSRLARQrlLGRSWSVPVIRHLFAPLKEYF 905
Cdd:COG0270 216 RFLHPGEPR-RLTvrEAARLQGFPDDFKFPGSKTQAYRQ--IGNAVPPPLAEAIAKAILKAL 274
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
 1-121 1.01e-06

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 52.77  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225    1 MPSSGPGDTSISSLEREDDrKEGEEQEENRGKEERQEPSATArkvgRPGRKRKHPPV------------ESSDTPKDPAV 68
Cdd:PTZ00449 519 LPPKAPGDKEGEEGEHEDS-KESDEPKEGGKPGETKEGEVGK----KPGPAKEHKPSkiptlskkpefpKDPKHPKDPEE 593

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51556225   69 TTKSQ----PTAQDSGPSDLLPNGDLEKRSEPQPEEG----SPAAGQKGGAPAEGEGTETP 121
Cdd:PTZ00449 594 PKKPKrprsAQRPTRPKSPKLPELLDIPKSPKRPESPkspkRPPPPQRPSSPERPEGPKII 654
 
Name Accession Description Interval E-value
PWWP_DNMT3A cd20154
PWWP domain found in DNA (cytosine-5)-methyltransferase 3A (DNMT3A); DNMT3A, also called DNA ...
 281-414 1.22e-102

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: 314.60  E-value: 1.22e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 281 EDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPM 360
Cdd:cd20154   1 EDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFSSAFHQATYNKQPM 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 51556225 361 YRKAIYEVLQVASSRAGKLFPACHDSDESDTGKAVEVQNKQMIEWALGGFQPSG 414
Cdd:cd20154  81 YRKAIYEVLQVASSRAGKLFPVCPESDESDTSKAVEVQNKQMIEWALGGFQPSG 134
ADDz_Dnmt3a cd11729
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3a (Dnmt3a); Dnmt3a is a ...
 483-610 1.48e-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: 277.27  E-value: 1.48e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 483 CRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 562
Cdd:cd11729   1 CRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 51556225 563 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 610
Cdd:cd11729  81 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 128
ADD_DNMT3 pfam17980
Cysteine rich ADD domain in DNMT3; This is a cysteine-rich domain termed ADD ...
 471-526 7.06e-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: 115.08  E-value: 7.06e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 51556225   471 TRERLVYEVRQKCRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDD 526
Cdd:pfam17980   1 SREQMVYEVRENKRNIEDFCLSCGSLNVHTFHPLFEGGLCQKCKDNFLETLYRYDE 56
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 286-344 1.10e-20

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 86.24  E-value: 1.10e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51556225    286 FGIGELVWGKLRGFSWWPGRIVSWWMTG----RSRAAEGTRWVMWFGDGKFSVVCVEKLMPLS 344
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVISPKMTPdnimKRKSDENLYPVLFFGDKDTAWIPSSKLFPLT 63
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
627-905 1.24e-19

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


Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 89.87  E-value: 1.24e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 627 RKPIRVLSLFDGI---ATGLlvlKDLGIQVdrYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQewGPFDLVIGG 703
Cdd:COG0270   1 SKKLTVIDLFAGAgglSLGF---EKAGFEV--VFAVEIDPDACETYRANFPEAKVIEGDIRDIDPEELI--PDVDLLIGG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 704 SPCNDLSIVNPaRKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVSDK----RDISRFLES-----NPV 774
Cdd:COG0270  74 PPCQPFSVAGK-RKGLEDPRGTLFFEFIRIVEELRPK-------AFVLENVPGLLSSDKgktfEEILKELEElgyrvDYK 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 775 MIDAKEVSAA-HRARYF----WGNLPGMNRPLASTVNDKLELQECLEH----GRIAKFSKvrTITTRSNsikqgkdqHFP 845
Cdd:COG0270 146 VLNAADYGVPqNRERVFivgfRKDLDLFEFPEPTHLKPYVTVGDALEDlpdaHEARYLSE--TITAGYG--------GGG 215

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51556225 846 VFMNEKEDIlWCT--EMERVFGFPVHYTDVSNMSRLARQrlLGRSWSVPVIRHLFAPLKEYF 905
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 ...
 289-373 1.67e-17

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


Pssm-ID: 459964 [Multi-domain]  Cd Length: 92  Bit Score: 78.24  E-value: 1.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225   289 GELVWGKLRGFSWWPGRIVSWWMTGRS----RAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNK---QPMY 361
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVVDPEELPENvlkpKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEFEYLKKKKKkkkKKAF 80

                          90
                  ....*....|..
gi 51556225   362 RKAIYEVLQVAS 373
Cdd:pfam00855  81 KKALEEAEEALK 92
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
 630-903 4.40e-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: 4.40e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 630 IRVLSLFDGIATGLLVLKDLGIQVdrYIASEVCEDSITVGMVRHqGKIMYVGDVRSVTQKHIQEwgPFDLVIGGSPCNDL 709
Cdd:cd00315   1 LRVIDLFAGIGGFRLGLEKAGFEI--VAANEIDKSAAETYEANF-PNKLIEGDITKIDEKDFIP--DIDLLTGGFPCQPF 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 710 SIVNpARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVSDKR----DISRFLESN-----PVMIDAKE 780
Cdd:cd00315  76 SIAG-KRKGFEDTRGTLFFEIIRILKEKKPK-------YFLLENVKGLLTHDNGntlkVILNTLEELgynvyWKLLNASD 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 781 VSAAH-RARYFW-GNLPGMNRPLASTV----NDKLELQECLehgRIAKFSKV-RTITTRSNSIKQGKDQHFPVFMNEKED 853
Cdd:cd00315 148 YGVPQnRERVFIiGIRKDLILNFFSPFpkpsEKKKTLKDIL---RIRDPDEPsPTLTASYGKGTGSVHPTAPDMIGKESN 224

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 51556225 854 ILWCT--EMERVFGFPVHYtDVSNMSRLARQRLLGRSWSVPVIRHLFAPLKE 903
Cdd:cd00315 225 IRRLTprECARLQGFPDDF-EFPGKSVTQAYRQIGNSVPVPVAEAIAKAIKE 275
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
 681-895 7.53e-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: 7.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225   681 GDVRSVTQKHIQEwgpFDLVIGGSPCNDLSIvNPARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVS 760
Cdd:TIGR00675  47 GDITKISPSDIPD---FDILLGGFPCQPFSI-AGKRKGFEDTRGTLFFEIVRILKEKKPK-------FFLLENVKGLVSH 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225   761 DK-RDISRFLES--------NPVMIDAKEVSAA-HRAR-------YFWGNLPgMNRPLASTVNDKLELQECLEHG----- 818
Cdd:TIGR00675 116 DKgRTFKVIIETleelgykvYYKVLNAKDFGVPqNRERiyivgfrDFDDKLN-FEFPKPIYVAKKKRIGDLLDLSvdlee 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225   819 ----------------------------------RIAKFSKVRTITTRSNSIKQGKDQ------HFPVFMNEKEDILWCT 858
Cdd:TIGR00675 195 kyylseekknglllllenmrkkegtgeqigsfynRESKSSIIRTLSARGYTFVKGGKSvlivphKSTVVHPGRIRRLTPR 274

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 51556225   859 EMERVFGFPVHYTDvsNMSRLARQRLLGRSWSVPVIR 895
Cdd:TIGR00675 275 ECARLQGFPDDFKF--PVSDSQLYKQAGNAVVVPVIE 309
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
630-754 2.97e-08

C-5 cytosine-specific DNA methylase;


Pssm-ID: 395093 [Multi-domain]  Cd Length: 324  Bit Score: 56.55  E-value: 2.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225   630 IRVLSLFDGIATGLLVLKDLGIQVdrYIASEVCEDSITVGMVRHQGKImyVGDVRSVTQKHIQEwgpFDLVIGGSPCNDL 709
Cdd:pfam00145   1 FKFIDLFAGIGGFRLGLEQAGFEC--VAANEIDKSAAKTYEANFPKVP--IGDITLIDIKDIPD---IDILTGGFPCQDF 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 51556225   710 SIVNpARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENV 754
Cdd:pfam00145  74 SIAG-KQKGFEDTRGTLFFEIIRIIKEKKPK-------AFLLENV 110
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 1-121 1.01e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 52.77  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225    1 MPSSGPGDTSISSLEREDDrKEGEEQEENRGKEERQEPSATArkvgRPGRKRKHPPV------------ESSDTPKDPAV 68
Cdd:PTZ00449 519 LPPKAPGDKEGEEGEHEDS-KESDEPKEGGKPGETKEGEVGK----KPGPAKEHKPSkiptlskkpefpKDPKHPKDPEE 593

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51556225   69 TTKSQ----PTAQDSGPSDLLPNGDLEKRSEPQPEEG----SPAAGQKGGAPAEGEGTETP 121
Cdd:PTZ00449 594 PKKPKrprsAQRPTRPKSPKLPELLDIPKSPKRPESPkspkRPPPPQRPSSPERPEGPKII 654
 
Name Accession Description Interval E-value
PWWP_DNMT3A cd20154
PWWP domain found in DNA (cytosine-5)-methyltransferase 3A (DNMT3A); DNMT3A, also called DNA ...
 281-414 1.22e-102

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: 314.60  E-value: 1.22e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 281 EDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPM 360
Cdd:cd20154   1 EDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFSSAFHQATYNKQPM 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 51556225 361 YRKAIYEVLQVASSRAGKLFPACHDSDESDTGKAVEVQNKQMIEWALGGFQPSG 414
Cdd:cd20154  81 YRKAIYEVLQVASSRAGKLFPVCPESDESDTSKAVEVQNKQMIEWALGGFQPSG 134
ADDz_Dnmt3a cd11729
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3a (Dnmt3a); Dnmt3a is a ...
 483-610 1.48e-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: 277.27  E-value: 1.48e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 483 CRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 562
Cdd:cd11729   1 CRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 51556225 563 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 610
Cdd:cd11729  81 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 128
ADDz cd11672
ATRX, Dnmt3 and Dnmt3l PHD-like zinc finger domain (ADDz); The ADDz zinc finger domain is ...
 486-584 1.22e-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: 200.87  E-value: 1.22e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 486 IEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLVGP 565
Cdd:cd11672   1 IEDICIACGSLVVIYRHPLFQGGICKNCKKYFLSDDISYDDDGYQSYCRICCEGGNLLCCGNNFCHRCFCKECVDRLVGP 80

                        90
                ....*....|....*....
gi 51556225 566 GAAQAAIKEDPWNCYMCGH 584
Cdd:cd11672  81 GELSTMDENNQWYCYICHP 99
ADDz_Dnmt3b cd11728
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3b (Dnmt3b); ADDz_Dnmt3b ...
 486-605 1.35e-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: 193.15  E-value: 1.35e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 486 IEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLVGP 565
Cdd:cd11728   1 IEDFCLSCGRSNPATFHPLFEGGLCITCKDRFLELFYMYDDDGYQSYCTVCCEGRELLLCGNASCCRCFCVDCLEVLVGP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 51556225 566 GAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFF 605
Cdd:cd11728  81 GTAAKAKEQDPWSCYMCLPQRCYGVLKRRTDWSVRLQEFF 120
ADDz_Dnmt3 cd11725
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 (Dnmt3); Dnmt3 is a de ...
 486-591 4.08e-54

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: 182.97  E-value: 4.08e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 486 IEDICISCGSLNV--TLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLV 563
Cdd:cd11725   1 IEDICLACGSLEVseTSDHPFFEGGLCKNCKERFLECIFLFDDDGYQMYCTICGGGGEVVLCDNPDCTRVYCTECLDLLL 80

                        90       100
                ....*....|....*....|....*...
gi 51556225 564 GPGAAQAAIKEDPWNCYMCGHKGTYGLL 591
Cdd:cd11725  81 GPGAVAKILESDPWFCFLCSPESNSLLG 108
PWWP_DNMT3B cd20155
PWWP domain found in DNA (cytosine-5)-methyltransferase 3B (DNMT3B); DNMT3B, also called DNA ...
 287-410 5.13e-50

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: 171.98  E-value: 5.13e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 287 GIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPMYRKAIY 366
Cdd:cd20155   1 GIGELVWGKIKGFSWWPAMVVSWRATGKRQASSGMRWLQWFGDGKFSEVSADKLVSLTAFSQHFNLSTYNKLVSYRKAMY 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 51556225 367 EVLQVASSRAGKLFPachdsdeSDTGKAVEVQNKQMIEWALGGF 410
Cdd:cd20155  81 HALEVARVRAGKTFP-------SSPGESLEDQLKPMLDWAHGGF 117
ADDz_Dnmt3l cd11727
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 like (Dnmt3l); Dnmt3l ...
 484-605 2.95e-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: 166.95  E-value: 2.95e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 484 RNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLV 563
Cdd:cd11727   1 RSIEEICICCGSLQIHTQHPLFHGGICAPCTEKFLEAFFLYDEDGYQAYCTICCSGETLLMCDDPDCTRCYCFECVDSLV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 51556225 564 GPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFF 605
Cdd:cd11727  81 GPGTSEKVKATNNWVCFLCLPSSRSGLLQRKRKWRSQLKAFY 122
PWWP_DNMT3 cd05835
PWWP domain found in the DNA (cytosine-5)-methyltransferase 3 (DNMT3) family; The DNMT3 family ...
 288-376 6.04e-38

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: 136.62  E-value: 6.04e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 288 IGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQaTYNKQPMYRKAIYE 367
Cdd:cd05835   2 IGDLVWAKLKGSPWWPGIVVSHKDCGQKPPAEGSVWVFWFGDHKVSEVPLDKILPFAEFFNKFYI-SKNSSKLYKKAVYE 80


                ....*....
gi 51556225 368 VLQVASSRA 376
Cdd:cd05835  81 ALKEAAERS 89
ADD_DNMT3 pfam17980
Cysteine rich ADD domain in DNMT3; This is a cysteine-rich domain termed ADD ...
 471-526 7.06e-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: 115.08  E-value: 7.06e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 51556225   471 TRERLVYEVRQKCRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDD 526
Cdd:pfam17980   1 SREQMVYEVRENKRNIEDFCLSCGSLNVHTFHPLFEGGLCQKCKDNFLETLYRYDE 56
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 286-344 1.10e-20

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 86.24  E-value: 1.10e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51556225    286 FGIGELVWGKLRGFSWWPGRIVSWWMTG----RSRAAEGTRWVMWFGDGKFSVVCVEKLMPLS 344
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVISPKMTPdnimKRKSDENLYPVLFFGDKDTAWIPSSKLFPLT 63
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
627-905 1.24e-19

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


Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 89.87  E-value: 1.24e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 627 RKPIRVLSLFDGI---ATGLlvlKDLGIQVdrYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQewGPFDLVIGG 703
Cdd:COG0270   1 SKKLTVIDLFAGAgglSLGF---EKAGFEV--VFAVEIDPDACETYRANFPEAKVIEGDIRDIDPEELI--PDVDLLIGG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 704 SPCNDLSIVNPaRKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVSDK----RDISRFLES-----NPV 774
Cdd:COG0270  74 PPCQPFSVAGK-RKGLEDPRGTLFFEFIRIVEELRPK-------AFVLENVPGLLSSDKgktfEEILKELEElgyrvDYK 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 775 MIDAKEVSAA-HRARYF----WGNLPGMNRPLASTVNDKLELQECLEH----GRIAKFSKvrTITTRSNsikqgkdqHFP 845
Cdd:COG0270 146 VLNAADYGVPqNRERVFivgfRKDLDLFEFPEPTHLKPYVTVGDALEDlpdaHEARYLSE--TITAGYG--------GGG 215

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51556225 846 VFMNEKEDIlWCT--EMERVFGFPVHYTDVSNMSRLARQrlLGRSWSVPVIRHLFAPLKEYF 905
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 ...
 289-373 1.67e-17

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


Pssm-ID: 459964 [Multi-domain]  Cd Length: 92  Bit Score: 78.24  E-value: 1.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225   289 GELVWGKLRGFSWWPGRIVSWWMTGRS----RAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNK---QPMY 361
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVVDPEELPENvlkpKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEFEYLKKKKKkkkKKAF 80

                          90
                  ....*....|..
gi 51556225   362 RKAIYEVLQVAS 373
Cdd:pfam00855  81 KKALEEAEEALK 92
PWWP_PWWP2B cd20153
PWWP domain found in PWWP domain-containing protein 2B (PWWP2B); PWWP2B is a paralog of PWWP2A, ...
 281-372 6.71e-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: 68.83  E-value: 6.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 281 EDGRGFGIGELVWGKLRGFSWWPGRIVSwwmTGRSRAAEGT-RW----VMWFGDGKFSVVCVEKLMPLSSfcsaFHQATY 355
Cdd:cd20153   9 EEGRTVSVGDIVWGKIHGFPWWPARVLS---ISLSQKEDGEpSWqeakVSWFGSPTTSLLSVSKLSPFSE----FFKLRF 81

                        90
                ....*....|....*....
gi 51556225 356 N--KQPMYRKAIYEVLQVA 372
Cdd:cd20153  82 NrkKKGMYRKAITEAAKAA 100
PWWP_MBD5 cd20141
PWWP domain found in methyl-CpG-binding domain protein 5 (MBD5) and similar proteins; MBD5, is ...
 286-353 9.03e-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: 67.73  E-value: 9.03e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51556225 286 FGIGELVWGKLRGFSWWPGRIVSwwMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQA 353
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, ...
 289-367 1.57e-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: 66.75  E-value: 1.57e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 289 GELVWGKLRGFSWWPGRIVSWWMTG---RSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPMYRKAI 365
Cdd:cd05162   1 GDLVWAKLKGYPWWPARVVDPEELPeevGKKKKKGGVLVQFFGDNDYAWVKSKNIKPFEEGFKKEFKKKKKKSKKFKKAV 80


                ..
gi 51556225 366 YE 367
Cdd:cd05162  81 EE 82
PWWP_PWWP2 cd20140
PWWP domain found in the PWWP domain-containing protein 2 (PWWP2) family; The PWWP2 family ...
 283-374 4.00e-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: 65.75  E-value: 4.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 283 GRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRW--VMWFGDGKFSVVCVEKLMPlssFCSAFHQaTYNKQP- 359
Cdd:cd20140   1 GRTLRVGDIVWGKIHGFPWWPGRILSITVSRDDNGELSTQEahVSWFGSSTTSYMPCSQLYP---FLEDFKL-RYNKKKr 76

                        90
                ....*....|....*.
gi 51556225 360 -MYRKAIYEVLQVASS 374
Cdd:cd20140  77 gPYKEAVRQALEAAKQ 92
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
 630-903 4.40e-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: 4.40e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 630 IRVLSLFDGIATGLLVLKDLGIQVdrYIASEVCEDSITVGMVRHqGKIMYVGDVRSVTQKHIQEwgPFDLVIGGSPCNDL 709
Cdd:cd00315   1 LRVIDLFAGIGGFRLGLEKAGFEI--VAANEIDKSAAETYEANF-PNKLIEGDITKIDEKDFIP--DIDLLTGGFPCQPF 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 710 SIVNpARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVSDKR----DISRFLESN-----PVMIDAKE 780
Cdd:cd00315  76 SIAG-KRKGFEDTRGTLFFEIIRILKEKKPK-------YFLLENVKGLLTHDNGntlkVILNTLEELgynvyWKLLNASD 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 781 VSAAH-RARYFW-GNLPGMNRPLASTV----NDKLELQECLehgRIAKFSKV-RTITTRSNSIKQGKDQHFPVFMNEKED 853
Cdd:cd00315 148 YGVPQnRERVFIiGIRKDLILNFFSPFpkpsEKKKTLKDIL---RIRDPDEPsPTLTASYGKGTGSVHPTAPDMIGKESN 224

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 51556225 854 ILWCT--EMERVFGFPVHYtDVSNMSRLARQRLLGRSWSVPVIRHLFAPLKE 903
Cdd:cd00315 225 IRRLTprECARLQGFPDDF-EFPGKSVTQAYRQIGNSVPVPVAEAIAKAIKE 275
PWWP_PWWP2A cd20152
PWWP domain found in PWWP domain-containing protein 2A (PWWP2A); PWWP2A is a H2A.Z-specific ...
 282-373 1.71e-12

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: 65.03  E-value: 1.71e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 282 DGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAA--EGTRWVMWFGDGKFSVVCVEKLMP-LSSFCSAFHQatyNKQ 358
Cdd:cd20152  16 DGRTICVGDIVWAKIYGFPWWPARILAITVSRKDNGLlvRQEARISWFGSPTTSFLALSQLAPfLENFQSRFNK---KRK 92

                        90
                ....*....|....*
gi 51556225 359 PMYRKAIYEVLQVAS 373
Cdd:cd20152  93 GLYRKAITEAAKAAK 107
ADDz_ATRX cd11726
ADDz domain found in ATRX (alpha-thalassemia/mental retardation, X-linked); ADDz_ATRX is a ...
 490-582 3.64e-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: 63.48  E-value: 3.64e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 490 CISCG-SLNVT----LEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCgnNNCCRCFCVECVDLLVG 564
Cdd:cd11726   5 CTACGeQLNHFskevHRHPVLKVLICKSCLKFYNSGEFSKDEDGSDEYCRWCGQGGDLICC--DFCPNVFCKKCIKRNLG 82

                        90
                ....*....|....*...
gi 51556225 565 PGAAQAAIKEDPWNCYMC 582
Cdd:cd11726  83 RAELSRIEESDKWKCFVC 100
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
 681-895 7.53e-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: 7.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225   681 GDVRSVTQKHIQEwgpFDLVIGGSPCNDLSIvNPARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVS 760
Cdd:TIGR00675  47 GDITKISPSDIPD---FDILLGGFPCQPFSI-AGKRKGFEDTRGTLFFEIVRILKEKKPK-------FFLLENVKGLVSH 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225   761 DK-RDISRFLES--------NPVMIDAKEVSAA-HRAR-------YFWGNLPgMNRPLASTVNDKLELQECLEHG----- 818
Cdd:TIGR00675 116 DKgRTFKVIIETleelgykvYYKVLNAKDFGVPqNRERiyivgfrDFDDKLN-FEFPKPIYVAKKKRIGDLLDLSvdlee 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225   819 ----------------------------------RIAKFSKVRTITTRSNSIKQGKDQ------HFPVFMNEKEDILWCT 858
Cdd:TIGR00675 195 kyylseekknglllllenmrkkegtgeqigsfynRESKSSIIRTLSARGYTFVKGGKSvlivphKSTVVHPGRIRRLTPR 274

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 51556225   859 EMERVFGFPVHYTDvsNMSRLARQRLLGRSWSVPVIR 895
Cdd:TIGR00675 275 ECARLQGFPDDFKF--PVSDSQLYKQAGNAVVVPVIE 309
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
630-754 2.97e-08

C-5 cytosine-specific DNA methylase;


Pssm-ID: 395093 [Multi-domain]  Cd Length: 324  Bit Score: 56.55  E-value: 2.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225   630 IRVLSLFDGIATGLLVLKDLGIQVdrYIASEVCEDSITVGMVRHQGKImyVGDVRSVTQKHIQEwgpFDLVIGGSPCNDL 709
Cdd:pfam00145   1 FKFIDLFAGIGGFRLGLEQAGFEC--VAANEIDKSAAKTYEANFPKVP--IGDITLIDIKDIPD---IDILTGGFPCQDF 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 51556225   710 SIVNpARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENV 754
Cdd:pfam00145  74 SIAG-KQKGFEDTRGTLFFEIIRIIKEKKPK-------AFLLENV 110
PWWP_AtATX3-like cd20143
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
 289-373 3.14e-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: 49.29  E-value: 3.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 289 GELVWGKLRGFSWWPGRIV---SWWMTGRSRAAEGTRWVMWFGDGK---FSVVCVEKLMPLSSFCSAFHQATY--NKQP- 359
Cdd:cd20143   3 GDLVWAKVGTHPFWPARVVepaEQAEEVRRRCVPGSLCVYFFGPGGsrdYGWVRRSMIFPFTDDLARFQTQKIknKKRPq 82

                        90
                ....*....|....
gi 51556225 360 MYRKAIYEVLQVAS 373
Cdd:cd20143  83 EFQEALEEAKLADA 96
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 1-121 1.01e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 52.77  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225    1 MPSSGPGDTSISSLEREDDrKEGEEQEENRGKEERQEPSATArkvgRPGRKRKHPPV------------ESSDTPKDPAV 68
Cdd:PTZ00449 519 LPPKAPGDKEGEEGEHEDS-KESDEPKEGGKPGETKEGEVGK----KPGPAKEHKPSkiptlskkpefpKDPKHPKDPEE 593

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51556225   69 TTKSQ----PTAQDSGPSDLLPNGDLEKRSEPQPEEG----SPAAGQKGGAPAEGEGTETP 121
Cdd:PTZ00449 594 PKKPKrprsAQRPTRPKSPKLPELLDIPKSPKRPESPkspkRPPPPQRPSSPERPEGPKII 654
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
 286-368 9.74e-06

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: 44.52  E-value: 9.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 286 FGIGELVWGKLRGFSWWPGRIVS-WWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFhqATYNKQPMYRKA 364
Cdd:cd05836   1 FKIGDLVWAKMKGFPPWPGKIVNpPPDLKKPPRKKKMHCVYFFGSENYAWIEDENIKPYEEFKEEM--LKSKKSAGFKDA 78


                ....
gi 51556225 365 IYEV 368
Cdd:cd05836  79 VEAI 82
PWWP_HRP cd05834
PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The ...
 286-367 1.51e-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: 38.30  E-value: 1.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 286 FGIGELVWGKLRGFSWWPGRIvswwmtgrSRAAEGTRW------VMWFGDGKFSVVCVEKLMPLSSFcsAFHQATYNKQP 359
Cdd:cd05834   1 FKPGDLVFAKVKGYPPWPARI--------DEIPEGAKIpknkypVFFYGTHETAFLKPKDLFPYEEN--KEKYGKPRKRK 70


                ....*...
gi 51556225 360 MYRKAIYE 367
Cdd:cd05834  71 GFNEGLWE 78
PWWP_MSH6 cd05837
PWWP domain found in DNA mismatch repair protein MSH6 and similar proteins; MSH6, also called ...
 286-304 3.20e-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: 3.20e-03
                        10
                ....*....|....*....
gi 51556225 286 FGIGELVWGKLRGFSWWPG 304
Cdd:cd05837   1 FSPGDLVWAKLEGYPWWPS 19
PWWP_ScIOC4-like cd05840
PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar ...
 289-374 4.67e-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: 4.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51556225 289 GELVWGKLRGFSWWPGRIVS--------WWMTGRSRAAEGTRW-VMWFGDGKFSVVCVEKLMPLS-SFCSAFHQATYNKQ 358
Cdd:cd05840   1 GDLVLAKVKGYPPWPAMVLPeellpknvLKAKKRKPKSKKTVYpVQFFPDNEYYWVSPSSLKPLTkEEIDKFLSKSKRKN 80

                        90
                ....*....|....*.
gi 51556225 359 pmyrKAIYEVLQVASS 374
Cdd:cd05840  81 ----KDLIEAYEVALE 92
PWWP_ZCWPW2 cd20146
PWWP domain found in zinc finger CW-type PWWP domain protein 2 (ZCWPW2) and similar proteins; ...
 289-306 5.82e-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: 37.66  E-value: 5.82e-03
                        10
                ....*....|....*...
gi 51556225 289 GELVWGKLRGFSWWPGRI 306
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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