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Conserved domains on  [gi|1034612227|ref|XP_016859015|]
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DNA (cytosine-5)-methyltransferase 3A isoform X1 [Homo sapiens]

Protein Classification

Dnmt3b_related and ADDz_Dnmt3a domain-containing protein (domain architecture ID 13564268)

protein containing domains Dnmt3b_related, ADDz_Dnmt3a, and Cyt_C5_DNA_methylase

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 ...
487-614 1.42e-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: 277.27  E-value: 1.42e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 487 CRNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 566
Cdd:cd11729     1 CRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1034612227 567 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 614
Cdd:cd11729    81 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 128
Dnmt3b_related cd05835
The PWWP domain is an essential component of DNA methyltransferase 3 B (Dnmt3b) which is ...
290-376 5.99e-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: 5.99e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 290 FGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPMYRKAI 369
Cdd:cd05835     1 FNVGDLVWGKIKGFPWWPGRVVSITVTSKRPPVVGMRWVTWFGSGTFSEVSVDKLSPFSEFFKAFSRYNRKKKGLYKKAI 80

                  ....*..
gi 1034612227 370 YEVLQVA 376
Cdd:cd05835    81 YEALEVA 87
Dcm COG0270
Site-specific DNA-cytosine methylase [Replication, recombination and repair];
632-795 2.64e-14

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


:

Pssm-ID: 223348 [Multi-domain]  Cd Length: 328  Bit Score: 74.78  E-value: 2.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 632 KPIRVLSLFDGIATGLLVLKDLGIQVdrYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEwGPFDLVIGGSPCN 711
Cdd:COG0270     2 EKMKVIDLFAGIGGLSLGFEEAGFEI--VFANEIDPPAVATYKANFPHGDIILGDIKELDGEALRK-SDVDVLIGGPPCQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 712 DLSIVNPaRKGLYEGTGRLFFEFYRLLHDARPKegddrpFFwLFENVVAM---GVSDKRDISRFLESN-----PVMIDAK 783
Cdd:COG0270    79 DFSIAGK-RRGYDDPRGSLFLEFIRLIEQLRPK------FF-VLENVKGLlssKGQTFDEIKKELEELgygveFNILNAA 150
                         170
                  ....*....|...
gi 1034612227 784 EVSAAH-RARYFW 795
Cdd:COG0270   151 DYGVPQsRERVFI 163
BASP1 super family cl37731
Brain acid soluble protein 1 (BASP1 protein); This family consists of several brain acid ...
11-156 4.87e-05

Brain acid soluble protein 1 (BASP1 protein); This family consists of several brain acid soluble protein 1 (BASP1) or neuronal axonal membrane protein NAP-22. The BASP1 is a neuron enriched Ca(2+)-dependent calmodulin-binding protein of unknown function.


The actual alignment was detected with superfamily member pfam05466:

Pssm-ID: 310221 [Multi-domain]  Cd Length: 238  Bit Score: 45.74  E-value: 4.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227  11 DTSSSAAEREEDRKDGEEQEEPRGKE---------ERQEPSTTARKVGRPgrKRKHPPVESGDTPKDpaviSKSPSMAQD 81
Cdd:pfam05466  64 VAANKTEEKEGEKDAAAAKEEAPKAEpekpeaaaeGKAEPPKSAEQEEEP--AAAPAPAAAGEAPKA----SEPSGEAKA 137
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034612227  82 SGASELLPNGdleKRSEPQPEEGSPAggqKGGAPAeGEGAAETLPEASRAVEngcctPKEGRGAPAEAGKEQKET 156
Cdd:pfam05466 138 SQPSEAPAAS---KVDEKSKEEGEAK---KTEAPA-APAAQETKSEAAPASD-----SKPSSSEAAPSSKETPAA 200
 
Name Accession Description Interval E-value
ADDz_Dnmt3a cd11729
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3a (Dnmt3a); Dnmt3a is a ...
487-614 1.42e-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: 277.27  E-value: 1.42e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 487 CRNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 566
Cdd:cd11729     1 CRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1034612227 567 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 614
Cdd:cd11729    81 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 128
Dnmt3b_related cd05835
The PWWP domain is an essential component of DNA methyltransferase 3 B (Dnmt3b) which is ...
290-376 5.99e-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: 5.99e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 290 FGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPMYRKAI 369
Cdd:cd05835     1 FNVGDLVWGKIKGFPWWPGRVVSITVTSKRPPVVGMRWVTWFGSGTFSEVSVDKLSPFSEFFKAFSRYNRKKKGLYKKAI 80

                  ....*..
gi 1034612227 370 YEVLQVA 376
Cdd:cd05835    81 YEALEVA 87
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
290-348 1.37e-20

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


Pssm-ID: 214603  Cd Length: 63  Bit Score: 85.86  E-value: 1.37e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034612227  290 FGIGELVWGKLRGFSWWPGRIVSWWMTG----RSRAAEGTRWVMWFGDGKFSVVCVEKLMPLS 348
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVISPKMTPdnimKRKSDENLYPVLFFGDKDTAWIPSSKLFPLT 63
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
290-377 2.36e-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: 83.62  E-value: 2.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 290 FGIGELVWGKLRGFSWWPGRIVSWWMTG----RSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNK---Q 362
Cdd:pfam00855   1 FKPGDLVWAKLKGYPWWPARVCDPEELPenilKKKPKPGLYLVRFFGDSEDAWVKPKDLKPFDEGDEFEYLKKKKKkkkK 80
                          90
                  ....*....|....*
gi 1034612227 363 PMYRKAIYEVLQVAS 377
Cdd:pfam00855  81 KKFKKAVEEAEEALK 95
Dcm COG0270
Site-specific DNA-cytosine methylase [Replication, recombination and repair];
632-795 2.64e-14

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


Pssm-ID: 223348 [Multi-domain]  Cd Length: 328  Bit Score: 74.78  E-value: 2.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 632 KPIRVLSLFDGIATGLLVLKDLGIQVdrYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEwGPFDLVIGGSPCN 711
Cdd:COG0270     2 EKMKVIDLFAGIGGLSLGFEEAGFEI--VFANEIDPPAVATYKANFPHGDIILGDIKELDGEALRK-SDVDVLIGGPPCQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 712 DLSIVNPaRKGLYEGTGRLFFEFYRLLHDARPKegddrpFFwLFENVVAM---GVSDKRDISRFLESN-----PVMIDAK 783
Cdd:COG0270    79 DFSIAGK-RRGYDDPRGSLFLEFIRLIEQLRPK------FF-VLENVKGLlssKGQTFDEIKKELEELgygveFNILNAA 150
                         170
                  ....*....|...
gi 1034612227 784 EVSAAH-RARYFW 795
Cdd:COG0270   151 DYGVPQsRERVFI 163
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
634-907 3.78e-13

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


Pssm-ID: 238192 [Multi-domain]  Cd Length: 275  Bit Score: 70.34  E-value: 3.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 634 IRVLSLFDGIATGLLVLKDLGIQVdrYIASEVCEDSITVGMVRHqGKIMYVGDVRSVTQKHIQEwgPFDLVIGGSPCNDL 713
Cdd:cd00315     1 LRVIDLFAGIGGFRLGLEKAGFEI--VAANEIDKSAAETYEANF-PNKLIEGDITKIDEKDFIP--DIDLLTGGFPCQPF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 714 SIVNpARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVSDKR----DISRFLESN-----PVMIDAKE 784
Cdd:cd00315    76 SIAG-KRKGFEDTRGTLFFEIIRILKEKKPK-------YFLLENVKGLLTHDNGntlkVILNTLEELgynvyWKLLNASD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 785 VSAAH-RARYFW-GNLPGMNRPLASTV----NDKLELQECLehgRIAKFSKV-RTITTRSNSIKQGKDQHFPVFMNEKED 857
Cdd:cd00315   148 YGVPQnRERVFIiGIRKDLILNFFSPFpkpsEKKKTLKDIL---RIRDPDEPsPTLTASYGKGTGSVHPTAPDMIGKESN 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034612227 858 ILWCT--EMERVFGFPVHYtDVSNMSRLARQRLLGRSWSVPVIRHLFAPLKE 907
Cdd:cd00315   225 IRRLTprECARLQGFPDDF-EFPGKSVTQAYRQIGNSVPVPVAEAIAKAIKE 275
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
685-899 6.46e-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: 6.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 685 GDVRSVTQKHIQEwgpFDLVIGGSPCNDLSIvNPARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVS 764
Cdd:TIGR00675  47 GDITKISPSDIPD---FDILLGGFPCQPFSI-AGKRKGFEDTRGTLFFEIVRILKEKKPK-------FFLLENVKGLVSH 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 765 DK-RDISRFLES--------NPVMIDAKEVSAA-HRAR-------YFWGNLPgMNRPLASTVNDKLELQECLEHG----- 822
Cdd:TIGR00675 116 DKgRTFKVIIETleelgykvYYKVLNAKDFGVPqNRERiyivgfrDFDDKLN-FEFPKPIYVAKKKRIGDLLDLSvdlee 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 823 ----------------------------------RIAKFSKVRTITTRSNSIKQGKDQ------HFPVFMNEKEDILWCT 862
Cdd:TIGR00675 195 kyylseekknglllllenmrkkegtgeqigsfynRESKSSIIRTLSARGYTFVKGGKSvlivphKSTVVHPGRIRRLTPR 274
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1034612227 863 EMERVFGFPVHYTDvsNMSRLARQRLLGRSWSVPVIR 899
Cdd:TIGR00675 275 ECARLQGFPDDFKF--PVSDSQLYKQAGNAVVVPVIE 309
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
634-907 2.01e-08

C-5 cytosine-specific DNA methylase;


Pssm-ID: 333875  Cd Length: 323  Bit Score: 56.94  E-value: 2.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 634 IRVLSLFDGIATGLLVLKDLGIQVdrYIASEVCEDSITVGMVRHQGKImyVGDVRSVTQKHIQEwgpFDLVIGGSPCNDL 713
Cdd:pfam00145   1 FKFIDLFAGIGGFRLGLEQAGFEC--VAANEIDKSAAKTYEANFPKVP--IGDITKIDIKDIPD---IDILTGGFPCQDF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 714 SIVNpARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVSDK-RDISRFLES--------NPVMIDAKE 784
Cdd:pfam00145  74 SIAG-KQKGFEDTRGTLFFEIIRIIKEKKPK-------AFLLENVKGLLSHDNgKTLNVILETleelgyhvHWKVLNASD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 785 VSAAH-RAR-YFWGNLPG--------------MNRPLASTVND------KLELQECLEHGRIAKFSKVRTITTRS----- 837
Cdd:pfam00145 146 YGVPQnRERvFIIGIRKDlilnlvpipdfdfpKPKDLTGTIRDlleesvLDENKYNLSDKFVENHERRKPTTKAPgggyp 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 838 -----NSIKQGKDQHFPVFMNEKED--------ILWCT-----------------EMERVFGFPVHYTDVSNMSRLARQr 887
Cdd:pfam00145 226 telsrNRVDKVEEGKGPSFTYRKSGrleppktgILIKNggrfrghpknirrltprECARLQGFPDDFIFPGSKTQLYKQ- 304
                         330       340
                  ....*....|....*....|
gi 1034612227 888 lLGRSWSVPVIRHLFAPLKE 907
Cdd:pfam00145 305 -IGNAVPVPVAEAIAKEIKK 323
BASP1 pfam05466
Brain acid soluble protein 1 (BASP1 protein); This family consists of several brain acid ...
11-156 4.87e-05

Brain acid soluble protein 1 (BASP1 protein); This family consists of several brain acid soluble protein 1 (BASP1) or neuronal axonal membrane protein NAP-22. The BASP1 is a neuron enriched Ca(2+)-dependent calmodulin-binding protein of unknown function.


Pssm-ID: 310221 [Multi-domain]  Cd Length: 238  Bit Score: 45.74  E-value: 4.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227  11 DTSSSAAEREEDRKDGEEQEEPRGKE---------ERQEPSTTARKVGRPgrKRKHPPVESGDTPKDpaviSKSPSMAQD 81
Cdd:pfam05466  64 VAANKTEEKEGEKDAAAAKEEAPKAEpekpeaaaeGKAEPPKSAEQEEEP--AAAPAPAAAGEAPKA----SEPSGEAKA 137
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034612227  82 SGASELLPNGdleKRSEPQPEEGSPAggqKGGAPAeGEGAAETLPEASRAVEngcctPKEGRGAPAEAGKEQKET 156
Cdd:pfam05466 138 SQPSEAPAAS---KVDEKSKEEGEAK---KTEAPA-APAAQETKSEAAPASD-----SKPSSSEAAPSSKETPAA 200
PHA03169 PHA03169
hypothetical protein; Provisional
15-188 1.26e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 41.88  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227  15 SAAEREEDRKDGEEQEEPRG------KEERQEPSTTARKVGRPGRKRKHPPVESGDTPKDPAVISKSPSM---------- 78
Cdd:PHA03169   71 SDTETAEESRHGEKEERGQGgpsgsgSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPpshpgphepa 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227  79 --AQDSGASELLPNGDLEKRSEPQPEEGSPAGGQ---KGGAPAEGEGAAETLPEASRAVENGCCTPKEGRGAP------- 146
Cdd:PHA03169  151 ppESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEpepDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPspntqqa 230
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034612227 147 AEAGKEQKETNIESMKMEGSRGRLRGGLGWESSLRQRPMPRL 188
Cdd:PHA03169  231 VEHEDEPTEPEREGPPFPGHRSHSYTVVGWKPSTRPGGVPKL 272
 
Name Accession Description Interval E-value
ADDz_Dnmt3a cd11729
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3a (Dnmt3a); Dnmt3a is a ...
487-614 1.42e-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: 277.27  E-value: 1.42e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 487 CRNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 566
Cdd:cd11729     1 CRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1034612227 567 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 614
Cdd:cd11729    81 VGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHD 128
ADDz cd11672
ATRX, Dnmt3 and Dnmt3l PHD-like zinc finger domain (ADDz); The ADDz zinc finger domain is ...
490-588 3.93e-61

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: 202.02  E-value: 3.93e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 490 IEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLVGP 569
Cdd:cd11672     1 IEDICIACGSLVVIYRHPLFQGGICKNCKKYFLSDDISYDDDGYQSYCRICCEGGNLLCCGNNFCHRCFCKECVDRLVGP 80
                          90
                  ....*....|....*....
gi 1034612227 570 GAAQAAIKEDPWNCYMCGH 588
Cdd:cd11672    81 GELSTMDENNQWYCYICHP 99
ADDz_Dnmt3b cd11728
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3b (Dnmt3b); ADDz_Dnmt3b ...
490-609 9.01e-58

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: 193.53  E-value: 9.01e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 490 IEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLVGP 569
Cdd:cd11728     1 IEDFCLSCGRSNPATFHPLFEGGLCITCKDRFLELFYMYDDDGYQSYCTVCCEGRELLLCGNASCCRCFCVDCLEVLVGP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034612227 570 GAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFF 609
Cdd:cd11728    81 GTAAKAKEQDPWSCYMCLPQRCYGVLKRRTDWSVRLQEFF 120
ADDz_Dnmt3 cd11725
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 (Dnmt3); Dnmt3 is a de ...
490-595 3.15e-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  Cd Length: 108  Bit Score: 182.97  E-value: 3.15e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 490 IEDICISCGSLNV--TLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLV 567
Cdd:cd11725     1 IEDICLACGSLEVseTSDHPFFEGGLCKNCKERFLECIFLFDDDGYQMYCTICGGGGEVVLCDNPDCTRVYCTECLDLLL 80
                          90       100
                  ....*....|....*....|....*...
gi 1034612227 568 GPGAAQAAIKEDPWNCYMCGHKGTYGLL 595
Cdd:cd11725    81 GPGAVAKILESDPWFCFLCSPESNSLLG 108
ADDz_Dnmt3l cd11727
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 like (Dnmt3l); Dnmt3l ...
488-609 2.05e-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  Cd Length: 123  Bit Score: 167.34  E-value: 2.05e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 488 RNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLV 567
Cdd:cd11727     1 RSIEEICICCGSLQIHTQHPLFHGGICAPCTEKFLEAFFLYDEDGYQAYCTICCSGETLLMCDDPDCTRCYCFECVDSLV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1034612227 568 GPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFF 609
Cdd:cd11727    81 GPGTSEKVKATNNWVCFLCLPSSRSGLLQRKRKWRSQLKAFY 122
Dnmt3b_related cd05835
The PWWP domain is an essential component of DNA methyltransferase 3 B (Dnmt3b) which is ...
290-376 5.99e-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: 5.99e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 290 FGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPMYRKAI 369
Cdd:cd05835     1 FNVGDLVWGKIKGFPWWPGRVVSITVTSKRPPVVGMRWVTWFGSGTFSEVSVDKLSPFSEFFKAFSRYNRKKKGLYKKAI 80

                  ....*..
gi 1034612227 370 YEVLQVA 376
Cdd:cd05835    81 YEALEVA 87
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
290-348 1.37e-20

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


Pssm-ID: 214603  Cd Length: 63  Bit Score: 85.86  E-value: 1.37e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034612227  290 FGIGELVWGKLRGFSWWPGRIVSWWMTG----RSRAAEGTRWVMWFGDGKFSVVCVEKLMPLS 348
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVISPKMTPdnimKRKSDENLYPVLFFGDKDTAWIPSSKLFPLT 63
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
290-377 2.36e-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: 83.62  E-value: 2.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 290 FGIGELVWGKLRGFSWWPGRIVSWWMTG----RSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNK---Q 362
Cdd:pfam00855   1 FKPGDLVWAKLKGYPWWPARVCDPEELPenilKKKPKPGLYLVRFFGDSEDAWVKPKDLKPFDEGDEFEYLKKKKKkkkK 80
                          90
                  ....*....|....*
gi 1034612227 363 PMYRKAIYEVLQVAS 377
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 ...
290-374 1.44e-17

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: 78.20  E-value: 1.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 290 FGIGELVWGKLRGFSWWPGRIVSW---WMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSsfCSAFHQATYNKQPMYR 366
Cdd:cd05162     1 FRPGDLVWAKMKGYPWWPALVVDPpkdSKKAKKKAKEGKVLVLFFGDKTFAWVGAERLKPFT--EHKESEAKQSKRKGFK 78

                  ....*...
gi 1034612227 367 KAIYEVLQ 374
Cdd:cd05162    79 KAYDEALE 86
Dcm COG0270
Site-specific DNA-cytosine methylase [Replication, recombination and repair];
632-795 2.64e-14

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


Pssm-ID: 223348 [Multi-domain]  Cd Length: 328  Bit Score: 74.78  E-value: 2.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 632 KPIRVLSLFDGIATGLLVLKDLGIQVdrYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEwGPFDLVIGGSPCN 711
Cdd:COG0270     2 EKMKVIDLFAGIGGLSLGFEEAGFEI--VFANEIDPPAVATYKANFPHGDIILGDIKELDGEALRK-SDVDVLIGGPPCQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 712 DLSIVNPaRKGLYEGTGRLFFEFYRLLHDARPKegddrpFFwLFENVVAM---GVSDKRDISRFLESN-----PVMIDAK 783
Cdd:COG0270    79 DFSIAGK-RRGYDDPRGSLFLEFIRLIEQLRPK------FF-VLENVKGLlssKGQTFDEIKKELEELgygveFNILNAA 150
                         170
                  ....*....|...
gi 1034612227 784 EVSAAH-RARYFW 795
Cdd:COG0270   151 DYGVPQsRERVFI 163
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
634-907 3.78e-13

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


Pssm-ID: 238192 [Multi-domain]  Cd Length: 275  Bit Score: 70.34  E-value: 3.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 634 IRVLSLFDGIATGLLVLKDLGIQVdrYIASEVCEDSITVGMVRHqGKIMYVGDVRSVTQKHIQEwgPFDLVIGGSPCNDL 713
Cdd:cd00315     1 LRVIDLFAGIGGFRLGLEKAGFEI--VAANEIDKSAAETYEANF-PNKLIEGDITKIDEKDFIP--DIDLLTGGFPCQPF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 714 SIVNpARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVSDKR----DISRFLESN-----PVMIDAKE 784
Cdd:cd00315    76 SIAG-KRKGFEDTRGTLFFEIIRILKEKKPK-------YFLLENVKGLLTHDNGntlkVILNTLEELgynvyWKLLNASD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 785 VSAAH-RARYFW-GNLPGMNRPLASTV----NDKLELQECLehgRIAKFSKV-RTITTRSNSIKQGKDQHFPVFMNEKED 857
Cdd:cd00315   148 YGVPQnRERVFIiGIRKDLILNFFSPFpkpsEKKKTLKDIL---RIRDPDEPsPTLTASYGKGTGSVHPTAPDMIGKESN 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034612227 858 ILWCT--EMERVFGFPVHYtDVSNMSRLARQRLLGRSWSVPVIRHLFAPLKE 907
Cdd:cd00315   225 IRRLTprECARLQGFPDDF-EFPGKSVTQAYRQIGNSVPVPVAEAIAKAIKE 275
ADDz_ATRX cd11726
ADDz domain found in ATRX (alpha-thalassemia/mental retardation, X-linked); ADDz_ATRX is a ...
494-586 2.45e-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  Cd Length: 102  Bit Score: 63.86  E-value: 2.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 494 CISCG-SLNVT----LEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCgnNNCCRCFCVECVDLLVG 568
Cdd:cd11726     5 CTACGeQLNHFskevHRHPVLKVLICKSCLKFYNSGEFSKDEDGSDEYCRWCGQGGDLICC--DFCPNVFCKKCIKRNLG 82
                          90
                  ....*....|....*...
gi 1034612227 569 PGAAQAAIKEDPWNCYMC 586
Cdd:cd11726    83 RAELSRIEESDKWKCFVC 100
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
685-899 6.46e-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: 6.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 685 GDVRSVTQKHIQEwgpFDLVIGGSPCNDLSIvNPARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVS 764
Cdd:TIGR00675  47 GDITKISPSDIPD---FDILLGGFPCQPFSI-AGKRKGFEDTRGTLFFEIVRILKEKKPK-------FFLLENVKGLVSH 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 765 DK-RDISRFLES--------NPVMIDAKEVSAA-HRAR-------YFWGNLPgMNRPLASTVNDKLELQECLEHG----- 822
Cdd:TIGR00675 116 DKgRTFKVIIETleelgykvYYKVLNAKDFGVPqNRERiyivgfrDFDDKLN-FEFPKPIYVAKKKRIGDLLDLSvdlee 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 823 ----------------------------------RIAKFSKVRTITTRSNSIKQGKDQ------HFPVFMNEKEDILWCT 862
Cdd:TIGR00675 195 kyylseekknglllllenmrkkegtgeqigsfynRESKSSIIRTLSARGYTFVKGGKSvlivphKSTVVHPGRIRRLTPR 274
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1034612227 863 EMERVFGFPVHYTDvsNMSRLARQRLLGRSWSVPVIR 899
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 ...
290-369 1.08e-08

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: 52.84  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 290 FGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEG-TRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQAtyNKQPMYRKA 368
Cdd:cd05836     1 LKLGDLVWAKMKGFPPWPGRIVKPPKDLKKPRGKAkCFFVFFFGSENHAWIKEENIKPYHEHKEEMIKL--NKGARFQQA 78

                  .
gi 1034612227 369 I 369
Cdd:cd05836    79 V 79
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
634-907 2.01e-08

C-5 cytosine-specific DNA methylase;


Pssm-ID: 333875  Cd Length: 323  Bit Score: 56.94  E-value: 2.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 634 IRVLSLFDGIATGLLVLKDLGIQVdrYIASEVCEDSITVGMVRHQGKImyVGDVRSVTQKHIQEwgpFDLVIGGSPCNDL 713
Cdd:pfam00145   1 FKFIDLFAGIGGFRLGLEQAGFEC--VAANEIDKSAAKTYEANFPKVP--IGDITKIDIKDIPD---IDILTGGFPCQDF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 714 SIVNpARKGLYEGTGRLFFEFYRLLHDARPKegddrpfFWLFENVVAMGVSDK-RDISRFLES--------NPVMIDAKE 784
Cdd:pfam00145  74 SIAG-KQKGFEDTRGTLFFEIIRIIKEKKPK-------AFLLENVKGLLSHDNgKTLNVILETleelgyhvHWKVLNASD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 785 VSAAH-RAR-YFWGNLPG--------------MNRPLASTVND------KLELQECLEHGRIAKFSKVRTITTRS----- 837
Cdd:pfam00145 146 YGVPQnRERvFIIGIRKDlilnlvpipdfdfpKPKDLTGTIRDlleesvLDENKYNLSDKFVENHERRKPTTKAPgggyp 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 838 -----NSIKQGKDQHFPVFMNEKED--------ILWCT-----------------EMERVFGFPVHYTDVSNMSRLARQr 887
Cdd:pfam00145 226 telsrNRVDKVEEGKGPSFTYRKSGrleppktgILIKNggrfrghpknirrltprECARLQGFPDDFIFPGSKTQLYKQ- 304
                         330       340
                  ....*....|....*....|
gi 1034612227 888 lLGRSWSVPVIRHLFAPLKE 907
Cdd:pfam00145 305 -IGNAVPVPVAEAIAKEIKK 323
BASP1 pfam05466
Brain acid soluble protein 1 (BASP1 protein); This family consists of several brain acid ...
11-156 4.87e-05

Brain acid soluble protein 1 (BASP1 protein); This family consists of several brain acid soluble protein 1 (BASP1) or neuronal axonal membrane protein NAP-22. The BASP1 is a neuron enriched Ca(2+)-dependent calmodulin-binding protein of unknown function.


Pssm-ID: 310221 [Multi-domain]  Cd Length: 238  Bit Score: 45.74  E-value: 4.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227  11 DTSSSAAEREEDRKDGEEQEEPRGKE---------ERQEPSTTARKVGRPgrKRKHPPVESGDTPKDpaviSKSPSMAQD 81
Cdd:pfam05466  64 VAANKTEEKEGEKDAAAAKEEAPKAEpekpeaaaeGKAEPPKSAEQEEEP--AAAPAPAAAGEAPKA----SEPSGEAKA 137
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034612227  82 SGASELLPNGdleKRSEPQPEEGSPAggqKGGAPAeGEGAAETLPEASRAVEngcctPKEGRGAPAEAGKEQKET 156
Cdd:pfam05466 138 SQPSEAPAAS---KVDEKSKEEGEAK---KTEAPA-APAAQETKSEAAPASD-----SKPSSSEAAPSSKETPAA 200
PHA03169 PHA03169
hypothetical protein; Provisional
15-188 1.26e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 41.88  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227  15 SAAEREEDRKDGEEQEEPRG------KEERQEPSTTARKVGRPGRKRKHPPVESGDTPKDPAVISKSPSM---------- 78
Cdd:PHA03169   71 SDTETAEESRHGEKEERGQGgpsgsgSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPpshpgphepa 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227  79 --AQDSGASELLPNGDLEKRSEPQPEEGSPAGGQ---KGGAPAEGEGAAETLPEASRAVENGCCTPKEGRGAP------- 146
Cdd:PHA03169  151 ppESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEpepDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPspntqqa 230
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034612227 147 AEAGKEQKETNIESMKMEGSRGRLRGGLGWESSLRQRPMPRL 188
Cdd:PHA03169  231 VEHEDEPTEPEREGPPFPGHRSHSYTVVGWKPSTRPGGVPKL 272
MARCKS pfam02063
MARCKS family;
10-152 1.41e-03

MARCKS family;


Pssm-ID: 307950 [Multi-domain]  Cd Length: 285  Bit Score: 41.61  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227  10 GDTSSSAAEREEDRKDGEEQEEPRGKEERQEPSTTARKVGRPGRKRKHPPVESGDTPKDpaviSKSPSMAQDSGASELLP 89
Cdd:pfam02063 146 AEAEGAAASAEGGKEEAAAGPEAAAAEEGKAAGEEAAAAPAAAASTEEAKEEAGGAPQE----AKAEEAAPEKPASEEAK 221
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034612227  90 NGDLEKRSEPQPEEGSPAGGQKGGAPAEGEGAAETLPEASRAVENGCCTPKegrgAPAEAGKE 152
Cdd:pfam02063 222 AAEEQKPAEEKKAEEAPASASACEAPSAAGEAASPEQEAPPAEEPAAASQE----AQSESSPE 280
MUM1_like cd06080
Mutated melanoma-associated antigen 1 (MUM-1) is a melanoma-associated antigen (MAA). MUM-1 ...
290-312 1.83e-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: 1.83e-03
                          10        20
                  ....*....|....*....|...
gi 1034612227 290 FGIGELVWGKLRGFSWWPGRIVS 312
Cdd:cd06080     1 FEKNDLVWAKIQGYPWWPAVIKS 23
MIP-T3 pfam10243
Microtubule-binding protein MIP-T3; This protein, which interacts with both microtubules and ...
14-249 1.91e-03

Microtubule-binding protein MIP-T3; This protein, which interacts with both microtubules and TRAF3 (tumor necrosis factor receptor-associated factor 3), is conserved from worms to humans. The N-terminal region is the microtubule binding domain and is well-conserved; the C-terminal 100 residues, also well-conserved, constitute the coiled-coil region which binds to TRAF3. The central region of the protein is rich in lysine and glutamic acid and carries KKE motifs which may also be necessary for tubulin-binding, but this region is the least well-conserved.


Pssm-ID: 313469 [Multi-domain]  Cd Length: 518  Bit Score: 41.77  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227  14 SSAAEREEDRKDGEEQEEPRGKEERQEpsTTARKVGRPGRKRKHP--------PVESGDTPKDPAVISKSPSMAQDSGAS 85
Cdd:pfam10243 122 EKPQSTPKDRKPKEELKEPRPPTEKEK--EKEKKVKAPRDREKEKrrdrekasSAEKKPKKKDSKNKKKDPEREKKKQAS 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227  86 -ELLPNGDLEKRSEPQPEEGSPAGGQKGGAPA-EGEGAAETLPEASRAVENGCCTPKEGRGAP-AEAGKEQKETNIESM- 161
Cdd:pfam10243 200 gKAVSGKEEERDHNEEREKEADDGPDPETNTSpPSEHESRRSSEKSRRSSKSEKKPQSNPGQStSQEQPTDVTSLPRPPt 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034612227 162 KMEGSRGRLRGGLGWESSLRQRPmPRLTFQ-----AGDPYYISKRKRDEWLARWKREAEKKAKVIagmnaVEENQGPGES 236
Cdd:pfam10243 280 EAKSGRTSLRPPSPRPASARPAP-PRVKRKnveivLQDAQGVGKIVSNVILEGKKSEDEDDENFV-----VEADEQAHDI 353
                         250
                  ....*....|...
gi 1034612227 237 QKVEEASPPAVQQ 249
Cdd:pfam10243 354 VAREEDLPGLLED 366
HDGF_related cd05834
The PWWP domain is an essential part of the Hepatoma Derived Growth Factor (HDGF) family of ...
290-357 2.08e-03

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: 37.65  E-value: 2.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034612227 290 FGIGELVWGKLRGFSWWPGRI--VSWWMTGRSRAAegtrwVMWFGDGKFSVVCVEKLMP---------LSSFCSAFHQA 357
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 ...
290-349 2.31e-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: 2.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034612227 290 FGIGELVWGKLRGFSWWPGRIVSWWMT------GRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSS 349
Cdd:cd05840     1 FQPGDRVLAKVKGFPAWPAIVVPEEMLpdsvlkGKKKKNKRTYPVMFFPDGDYYWVPNKDLKPLTE 66
 
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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