NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|528487581|ref|XP_005167053|]
View 

DNA (cytosine-5-)-methyltransferase 3 beta, duplicate a isoform X3 [Danio rerio]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FYVE_like_SF super family cl28890
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
 1011-1130 9.77e-75

FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger motif-containing module named after the four proteins, Fab1, YOTB, Vac1, and EEA1. The canonical FYVE domains are distinguished from other zinc fingers by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P, also termed PI3P)-binding site. They are found in many membrane trafficking regulators, including EEA1, Hrs, Vac1p, Vps27p, and FENS-1, which locate to early endosomes, specifically bind PtdIns3P, and play important roles in vesicular traffic and in signal transduction. Some proteins, such as rabphilin-3A and alpha-Rab3-interacting molecules (RIMs), are also involved in membrane trafficking and bind to members of the Rab subfamily of GTP hydrolases. However, they contain FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences. At this point, they may not bind to phosphoinositides. In addition, this superfamily also contains the third group of proteins, caspase-associated ring proteins CARP1 and CARP2. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains. The FYVE domain is structurally similar to the RING domain and the PHD finger. This superfamily also includes ADDz zinc finger domain, which is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger.


The actual alignment was detected with superfamily member cd11728:

Pssm-ID: 333710 [Multi-domain]  Cd Length: 120  Bit Score: 243.61  E-value: 9.77e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1011 IEDFCLSCGSSNTEIFHPLFKGSLCIKCKENFTETLYRYDDDGYQSYCTVCCAGLEVILCGNASCCRCFCKDCLNVLVGP 1090
Cdd:cd11728     1 IEDFCLSCGRSNPATFHPLFEGGLCITCKDRFLELFYMYDDDGYQSYCTVCCEGRELLLCGNASCCRCFCVDCLEVLVGP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 528487581 1091 GTFDKLKEVDPWSCYVCLPSKCYGVLKLRTDWSVRVQEFF 1130
Cdd:cd11728    81 GTAAKAKEQDPWSCYMCLPQRCYGVLKRRTDWSVRLQEFF 120
PWWP super family cl02554
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
 837-947 7.93e-41

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.


The actual alignment was detected with superfamily member cd20155:

Pssm-ID: 470613  Cd Length: 117  Bit Score: 146.55  E-value: 7.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581  837 VGELVWGKVKDFSLWPGLVVPWKG---RIVPVSMRRVEWFGDGMFSEIHTDGLLPFGAFSKNFCSKSYEGLPTYKNAIYQ 913
Cdd:cd20155     2 IGELVWGKIKGFSWWPAMVVSWRAtgkRQASSGMRWLQWFGDGKFSEVSADKLVSLTAFSQHFNLSTYNKLVSYRKAMYH 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 528487581  914 ILELAAERSGKLFPPSEKKG--EEVKAMMDWAFGGF 947
Cdd:cd20155    82 ALEVARVRAGKTFPSSPGESleDQLKPMLDWAHGGF 117
Dcm super family cl43082
DNA-cytosine methylase [Replication, recombination and repair];
1152-1430 6.08e-20

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: 91.41  E-value: 6.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1152 RRPIRVLSLFDGIatGYLvlkDLGFKLERY---IASEICEDSIAVGMVKHEGKIEYVKDVRTITRKHLAewGPFDLLIGG 1228
Cdd:COG0270     1 SKKLTVIDLFAGA--GGL---SLGFEKAGFevvFAVEIDPDACETYRANFPEAKVIEGDIRDIDPEELI--PDVDLLIGG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1229 SPCNDLSMVNPaRKGlFEGT-GRLFFEYYRMLTMMRPKedddrpfFWLFENVVAMSAHDK----ADICRFLE-----CNP 1298
Cdd:COG0270    74 PPCQPFSVAGK-RKG-LEDPrGTLFFEFIRIVEELRPK-------AFVLENVPGLLSSDKgktfEEILKELEelgyrVDY 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1299 VMIDA----VkvsPAHRARYF----WGNLPGMNRPVATSLTDNVDLQDCLESGRTAMFSKV--RTITTksnsikqgktgp 1368
Cdd:COG0270   145 KVLNAadygV---PQNRERVFivgfRKDLDLFEFPEPTHLKPYVTVGDALEDLPDAHEARYlsETITA------------ 209

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1369 lpvTMNGKEDYL------WCT--EMEKIFGFPKHYTDVNNmgRGQRQKVLGRSWSVPVIRHLFAPLKDYF 1430
Cdd:COG0270   210 ---GYGGGGRFLhpgeprRLTvrEAARLQGFPDDFKFPGS--KTQAYRQIGNAVPPPLAEAIAKAILKAL 274
BIM1 super family cl34944
Microtubule-binding protein involved in cell cycle control [Cell division and chromosome ...
 17-174 1.09e-13

Microtubule-binding protein involved in cell cycle control [Cell division and chromosome partitioning / Cytoskeleton];


The actual alignment was detected with superfamily member COG5217:

Pssm-ID: 227542 [Multi-domain]  Cd Length: 342  Bit Score: 74.26  E-value: 1.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581   17 SRYEVLGWINETLQTNFTQVEQCRSGACFCQLIDLLFpGTINLKKVKFESQKRSDFMQNYGLLQAAFRDLEVTEPVPVNE 96
Cdd:COG5217     8 SREELLFWENVVVRLDLQRIEDCGEGFAMQQIHDSIY-VDLPDSLVRFPWIAEYKHPGNGKILQLLFSDYGIDKAVLVLV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581   97 LLSGKFRPNFTYLKWFKKFFYANvKQERVYNAFEARDGQEIVPVDDVMKSPKAL------KSSYESGRAG------EESD 164
Cdd:COG5217    87 LVRCKLQDNLEFLQWLKDHWVRN-LGHISYDRNARRLGRTPKSTRELIEWIRSLgipisaIRELSKGVASckslstIHSS 165

                         170
                  ....*....|
gi 528487581  165 MEINGGRRSA 174
Cdd:COG5217   166 FPQNFVKNTA 175
 
Name Accession Description Interval E-value
ADDz_Dnmt3b cd11728
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3b (Dnmt3b); ADDz_Dnmt3b ...
 1011-1130 9.77e-75

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: 243.61  E-value: 9.77e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1011 IEDFCLSCGSSNTEIFHPLFKGSLCIKCKENFTETLYRYDDDGYQSYCTVCCAGLEVILCGNASCCRCFCKDCLNVLVGP 1090
Cdd:cd11728     1 IEDFCLSCGRSNPATFHPLFEGGLCITCKDRFLELFYMYDDDGYQSYCTVCCEGRELLLCGNASCCRCFCVDCLEVLVGP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 528487581 1091 GTFDKLKEVDPWSCYVCLPSKCYGVLKLRTDWSVRVQEFF 1130
Cdd:cd11728    81 GTAAKAKEQDPWSCYMCLPQRCYGVLKRRTDWSVRLQEFF 120
PWWP_DNMT3B cd20155
PWWP domain found in DNA (cytosine-5)-methyltransferase 3B (DNMT3B); DNMT3B, also called DNA ...
 837-947 7.93e-41

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: 146.55  E-value: 7.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581  837 VGELVWGKVKDFSLWPGLVVPWKG---RIVPVSMRRVEWFGDGMFSEIHTDGLLPFGAFSKNFCSKSYEGLPTYKNAIYQ 913
Cdd:cd20155     2 IGELVWGKIKGFSWWPAMVVSWRAtgkRQASSGMRWLQWFGDGKFSEVSADKLVSLTAFSQHFNLSTYNKLVSYRKAMYH 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 528487581  914 ILELAAERSGKLFPPSEKKG--EEVKAMMDWAFGGF 947
Cdd:cd20155    82 ALEVARVRAGKTFPSSPGESleDQLKPMLDWAHGGF 117
ADD_DNMT3 pfam17980
Cysteine rich ADD domain in DNMT3; This is a cysteine-rich domain termed ADD ...
 996-1051 7.70e-31

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


Pssm-ID: 465603  Cd Length: 56  Bit Score: 115.46  E-value: 7.70e-31
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 528487581   996 NRDQMVQEVTSKGRKIEDFCLSCGSSNTEIFHPLFKGSLCIKCKENFTETLYRYDD 1051
Cdd:pfam17980    1 SREQMVYEVRENKRNIEDFCLSCGSLNVHTFHPLFEGGLCQKCKDNFLETLYRYDE 56
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
1152-1430 6.08e-20

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


Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 91.41  E-value: 6.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1152 RRPIRVLSLFDGIatGYLvlkDLGFKLERY---IASEICEDSIAVGMVKHEGKIEYVKDVRTITRKHLAewGPFDLLIGG 1228
Cdd:COG0270     1 SKKLTVIDLFAGA--GGL---SLGFEKAGFevvFAVEIDPDACETYRANFPEAKVIEGDIRDIDPEELI--PDVDLLIGG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1229 SPCNDLSMVNPaRKGlFEGT-GRLFFEYYRMLTMMRPKedddrpfFWLFENVVAMSAHDK----ADICRFLE-----CNP 1298
Cdd:COG0270    74 PPCQPFSVAGK-RKG-LEDPrGTLFFEFIRIVEELRPK-------AFVLENVPGLLSSDKgktfEEILKELEelgyrVDY 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1299 VMIDA----VkvsPAHRARYF----WGNLPGMNRPVATSLTDNVDLQDCLESGRTAMFSKV--RTITTksnsikqgktgp 1368
Cdd:COG0270   145 KVLNAadygV---PQNRERVFivgfRKDLDLFEFPEPTHLKPYVTVGDALEDLPDAHEARYlsETITA------------ 209

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1369 lpvTMNGKEDYL------WCT--EMEKIFGFPKHYTDVNNmgRGQRQKVLGRSWSVPVIRHLFAPLKDYF 1430
Cdd:COG0270   210 ---GYGGGGRFLhpgeprRLTvrEAARLQGFPDDFKFPGS--KTQAYRQIGNAVPPPLAEAIAKAILKAL 274
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
 1155-1423 5.37e-15

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: 76.89  E-value: 5.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1155 IRVLSLFDGIATGYLVLKDLGFKLerYIASEICEDSIAVGMVKHEGKIeYVKDVRTITRKHLAEwgPFDLLIGGSPCNDL 1234
Cdd:cd00315     1 LRVIDLFAGIGGFRLGLEKAGFEI--VAANEIDKSAAETYEANFPNKL-IEGDITKIDEKDFIP--DIDLLTGGFPCQPF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1235 SmVNPARKGlFEGT-GRLFFEYYRMLTMMRPKedddrpfFWLFENVVAMSAHDK----ADICRFLE-----CNPVMIDA- 1303
Cdd:cd00315    76 S-IAGKRKG-FEDTrGTLFFEIIRILKEKKPK-------YFLLENVKGLLTHDNgntlKVILNTLEelgynVYWKLLNAs 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1304 ---VkvsPAHRARYFW-GNLPGMN----RPVATSLTDNVDLQDCLESGRTAmfSKVRTITTkSNSIKQGKTGPLPVTMNG 1375
Cdd:cd00315   147 dygV---PQNRERVFIiGIRKDLIlnffSPFPKPSEKKKTLKDILRIRDPD--EPSPTLTA-SYGKGTGSVHPTAPDMIG 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528487581 1376 KED---YLWCTEMEKIFGFPKHYtDVNNMGRGQRQKVLGRSWSVPVIRHLF 1423
Cdd:cd00315   221 KESnirRLTPRECARLQGFPDDF-EFPGKSVTQAYRQIGNSVPVPVAEAIA 270
BIM1 COG5217
Microtubule-binding protein involved in cell cycle control [Cell division and chromosome ...
 17-174 1.09e-13

Microtubule-binding protein involved in cell cycle control [Cell division and chromosome partitioning / Cytoskeleton];


Pssm-ID: 227542 [Multi-domain]  Cd Length: 342  Bit Score: 74.26  E-value: 1.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581   17 SRYEVLGWINETLQTNFTQVEQCRSGACFCQLIDLLFpGTINLKKVKFESQKRSDFMQNYGLLQAAFRDLEVTEPVPVNE 96
Cdd:COG5217     8 SREELLFWENVVVRLDLQRIEDCGEGFAMQQIHDSIY-VDLPDSLVRFPWIAEYKHPGNGKILQLLFSDYGIDKAVLVLV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581   97 LLSGKFRPNFTYLKWFKKFFYANvKQERVYNAFEARDGQEIVPVDDVMKSPKAL------KSSYESGRAG------EESD 164
Cdd:COG5217    87 LVRCKLQDNLEFLQWLKDHWVRN-LGHISYDRNARRLGRTPKSTRELIEWIRSLgipisaIRELSKGVASckslstIHSS 165

                         170
                  ....*....|
gi 528487581  165 MEINGGRRSA 174
Cdd:COG5217   166 FPQNFVKNTA 175
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
 1157-1420 8.50e-13

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: 71.20  E-value: 8.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581  1157 VLSLFDGIATGYLVLKDLGFKLerYIASEIceDSIAVGMVK--HEGKIEYvKDVRTITRKHLAEwgpFDLLIGGSPCNDL 1234
Cdd:TIGR00675    1 FIDLFAGIGGIRLGFEQAGFKC--VFASEI--DKYAQKTYEanFGNKVPF-GDITKISPSDIPD---FDILLGGFPCQPF 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581  1235 SMvnpARKGL-FEGT-GRLFFEYYRMLTMMRPKedddrpfFWLFENVVAMSAHDKAdicRFLecnPVMIDAV-----KVS 1307
Cdd:TIGR00675   73 SI---AGKRKgFEDTrGTLFFEIVRILKEKKPK-------FFLLENVKGLVSHDKG---RTF---KVIIETLeelgyKVY 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581  1308 -----------PAHRAR-YFWG----------NLP-GMNRPVATSLTDNVDLQDCLESG-----------------RTAM 1347
Cdd:TIGR00675  137 ykvlnakdfgvPQNRERiYIVGfrdfddklnfEFPkPIYVAKKKRIGDLLDLSVDLEEKyylseekknglllllenMRKK 216

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581  1348 FSKVRTITTKSNS-----------------IKQGKTgpLPVTMNGKEDY-------LWCTEMEKIFGFPKHYTDvnNMGR 1403
Cdd:TIGR00675  217 EGTGEQIGSFYNReskssiirtlsargytfVKGGKS--VLIVPHKSTVVhpgrirrLTPRECARLQGFPDDFKF--PVSD 292

                          330
                   ....*....|....*..
gi 528487581  1404 GQRQKVLGRSWSVPVIR 1420
Cdd:TIGR00675  293 SQLYKQAGNAVVVPVIE 309
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 838-918 8.69e-12

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: 62.44  E-value: 8.69e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581   838 GELVWGKVKDFSLWPGLVVPWKgrIVPVSMRR---------VEWFGDGMFSEIHTDGLLPFGAFSKNFCSKSYEG---LP 905
Cdd:pfam00855    1 GDLVWAKLKGYPWWPARVVDPE--ELPENVLKpkkkdgeylVRFFGDSEFAWVKPKDLKPFDEGDEFEYLKKKKKkkkKK 78

                           90
                   ....*....|...
gi 528487581   906 TYKNAIYQILELA 918
Cdd:pfam00855   79 AFKKALEEAEEAL 91
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
1155-1287 2.02e-11

C-5 cytosine-specific DNA methylase;


Pssm-ID: 395093 [Multi-domain]  Cd Length: 324  Bit Score: 66.95  E-value: 2.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581  1155 IRVLSLFDGIATGYLVLKDLGFKLerYIASEICEDSIAVGMVKHEGKIEyvKDVRTITRKHLAEwgpFDLLIGGSPCNDL 1234
Cdd:pfam00145    1 FKFIDLFAGIGGFRLGLEQAGFEC--VAANEIDKSAAKTYEANFPKVPI--GDITLIDIKDIPD---IDILTGGFPCQDF 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 528487581  1235 SmVNPARKGLFEGTGRLFFEYYRMLTMMRPKedddrpfFWLFENVVAMSAHDK 1287
Cdd:pfam00145   74 S-IAGKQKGFEDTRGTLFFEIIRIIKEKKPK-------AFLLENVKGLLSHDN 118
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 15-118 1.27e-10

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 59.99  E-value: 1.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581    15 KCSRYEVLGWINETLQ--------TNFTqvEQCRSGACFCQLIDLLFPGTINLKKVKfesQKRSDFMQNYGL-LQAAFRD 85
Cdd:pfam00307    1 LELEKELLRWINSHLAeygpgvrvTNFT--TDLRDGLALCALLNKLAPGLVDKKKLN---KSEFDKLENINLaLDVAEKK 75

                           90       100       110
                   ....*....|....*....|....*....|....
gi 528487581    86 LEVTEPVP-VNELLSGKFRPNFTYLKWFKKFFYA 118
Cdd:pfam00307   76 LGVPKVLIePEDLVEGDNKSVLTYLASLFRRFQA 109
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 835-890 4.27e-08

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 51.19  E-value: 4.27e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528487581    835 FAVGELVWGKVKDFSLWPGLVVPWKgrIVPVSMRR---------VEWFGDGMFSEIHTDGLLPFG 890
Cdd:smart00293    1 FKPGDLVWAKMKGFPWWPALVISPK--MTPDNIMKrksdenlypVLFFGDKDTAWIPSSKLFPLT 63
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 19-95 1.47e-04

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 42.30  E-value: 1.47e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581     19 YEVLGWINETLQ-------TNFTQVeqCRSGACFCQLIDLLFPGTINLKKVKfESQKRSDFMQNyglLQAAFRDLEVTEP 91
Cdd:smart00033    1 KTLLRWVNSLLAeydkppvTNFSSD--LKDGVALCALLNSLSPGLVDKKKVA-ASLSRFKKIEN---INLALSFAEKLGG 74


                    ....
gi 528487581     92 VPVN 95
Cdd:smart00033   75 KVVL 78
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 20-92 1.05e-03

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 40.01  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581   20 EVLGWINETLQ-------TNFTqvEQCRSGACFCQLIDLLFPGTInlKKVKFESQKRSDFMQNYGLLQAAFRDLEVTEPV 92
Cdd:cd00014     3 ELLKWINEVLGeelpvsiTDLF--ESLRDGVLLCKLINKLSPGSI--PKINKKPKSPFKKRENINLFLNACKKLGLPELD 78
 
Name Accession Description Interval E-value
ADDz_Dnmt3b cd11728
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3b (Dnmt3b); ADDz_Dnmt3b ...
 1011-1130 9.77e-75

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: 243.61  E-value: 9.77e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1011 IEDFCLSCGSSNTEIFHPLFKGSLCIKCKENFTETLYRYDDDGYQSYCTVCCAGLEVILCGNASCCRCFCKDCLNVLVGP 1090
Cdd:cd11728     1 IEDFCLSCGRSNPATFHPLFEGGLCITCKDRFLELFYMYDDDGYQSYCTVCCEGRELLLCGNASCCRCFCVDCLEVLVGP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 528487581 1091 GTFDKLKEVDPWSCYVCLPSKCYGVLKLRTDWSVRVQEFF 1130
Cdd:cd11728    81 GTAAKAKEQDPWSCYMCLPQRCYGVLKRRTDWSVRLQEFF 120
ADDz_Dnmt3a cd11729
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3a (Dnmt3a); Dnmt3a is a ...
 1009-1133 2.12e-45

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: 159.79  E-value: 2.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1009 RKIEDFCLSCGSSNTEIFHPLFKGSLCIKCKENFTETLYRYDDDGYQSYCTVCCAGLEVILCGNASCCRCFCKDCLNVLV 1088
Cdd:cd11729     2 RNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 528487581 1089 GPGTFDKLKEVDPWSCYVCLPSKCYGVLKLRTDWSVRVQEFFANN 1133
Cdd:cd11729    82 GPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANN 126
ADDz_Dnmt3l cd11727
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 like (Dnmt3l); Dnmt3l ...
 1009-1130 1.64e-44

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: 157.32  E-value: 1.64e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1009 RKIEDFCLSCGSSNTEIFHPLFKGSLCIKCKENFTETLYRYDDDGYQSYCTVCCAGLEVILCGNASCCRCFCKDCLNVLV 1088
Cdd:cd11727     1 RSIEEICICCGSLQIHTQHPLFHGGICAPCTEKFLEAFFLYDEDGYQAYCTICCSGETLLMCDDPDCTRCYCFECVDSLV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 528487581 1089 GPGTFDKLKEVDPWSCYVCLPSKCYGVLKLRTDWSVRVQEFF 1130
Cdd:cd11727    81 GPGTSEKVKATNNWVCFLCLPSSRSGLLQRKRKWRSQLKAFY 122
ADDz_Dnmt3 cd11725
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 (Dnmt3); Dnmt3 is a de ...
 1011-1116 2.76e-44

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: 156.01  E-value: 2.76e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1011 IEDFCLSCGSSNTEI--FHPLFKGSLCIKCKENFTETLYRYDDDGYQSYCTVCCAGLEVILCGNASCCRCFCKDCLNVLV 1088
Cdd:cd11725     1 IEDICLACGSLEVSEtsDHPFFEGGLCKNCKERFLECIFLFDDDGYQMYCTICGGGGEVVLCDNPDCTRVYCTECLDLLL 80

                          90       100
                  ....*....|....*....|....*...
gi 528487581 1089 GPGTFDKLKEVDPWSCYVCLPSKCYGVL 1116
Cdd:cd11725    81 GPGAVAKILESDPWFCFLCSPESNSLLG 108
PWWP_DNMT3B cd20155
PWWP domain found in DNA (cytosine-5)-methyltransferase 3B (DNMT3B); DNMT3B, also called DNA ...
 837-947 7.93e-41

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: 146.55  E-value: 7.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581  837 VGELVWGKVKDFSLWPGLVVPWKG---RIVPVSMRRVEWFGDGMFSEIHTDGLLPFGAFSKNFCSKSYEGLPTYKNAIYQ 913
Cdd:cd20155     2 IGELVWGKIKGFSWWPAMVVSWRAtgkRQASSGMRWLQWFGDGKFSEVSADKLVSLTAFSQHFNLSTYNKLVSYRKAMYH 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 528487581  914 ILELAAERSGKLFPPSEKKG--EEVKAMMDWAFGGF 947
Cdd:cd20155    82 ALEVARVRAGKTFPSSPGESleDQLKPMLDWAHGGF 117
ADDz cd11672
ATRX, Dnmt3 and Dnmt3l PHD-like zinc finger domain (ADDz); The ADDz zinc finger domain is ...
 1011-1109 1.19e-38

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: 139.62  E-value: 1.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1011 IEDFCLSCGSSNTEIFHPLFKGSLCIKCKENFTETLYRYDDDGYQSYCTVCCAGLEVILCGNASCCRCFCKDCLNVLVGP 1090
Cdd:cd11672     1 IEDICIACGSLVVIYRHPLFQGGICKNCKKYFLSDDISYDDDGYQSYCRICCEGGNLLCCGNNFCHRCFCKECVDRLVGP 80

                          90
                  ....*....|....*....
gi 528487581 1091 GTFDKLKEVDPWSCYVCLP 1109
Cdd:cd11672    81 GELSTMDENNQWYCYICHP 99
PWWP_DNMT3A cd20154
PWWP domain found in DNA (cytosine-5)-methyltransferase 3A (DNMT3A); DNMT3A, also called DNA ...
 831-951 2.01e-35

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: 131.63  E-value: 2.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581  831 DGKGFAVGELVWGKVKDFSLWPGLVVPW--KGRIVPVS-MRRVEWFGDGMFSEIHTDGLLPFGAFSKNFCSKSYEGLPTY 907
Cdd:cd20154     2 DGRGFGIGELVWGKLRGFSWWPGRIVSWwmTGRSRAAEgTRWVMWFGDGKFSVVCVEKLMPLSSFSSAFHQATYNKQPMY 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 528487581  908 KNAIYQILELAAERSGKLFPPSEKKGE---------EVKAMMDWAFGGFQPMG 951
Cdd:cd20154    82 RKAIYEVLQVASSRAGKLFPVCPESDEsdtskavevQNKQMIEWALGGFQPSG 134
ADD_DNMT3 pfam17980
Cysteine rich ADD domain in DNMT3; This is a cysteine-rich domain termed ADD ...
 996-1051 7.70e-31

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


Pssm-ID: 465603  Cd Length: 56  Bit Score: 115.46  E-value: 7.70e-31
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 528487581   996 NRDQMVQEVTSKGRKIEDFCLSCGSSNTEIFHPLFKGSLCIKCKENFTETLYRYDD 1051
Cdd:pfam17980    1 SREQMVYEVRENKRNIEDFCLSCGSLNVHTFHPLFEGGLCQKCKDNFLETLYRYDE 56
PWWP_DNMT3 cd05835
PWWP domain found in the DNA (cytosine-5)-methyltransferase 3 (DNMT3) family; The DNMT3 family ...
 837-922 9.37e-30

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: 113.51  E-value: 9.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581  837 VGELVWGKVKDFSLWPGLVVPWKGRIV---PVSMRRVEWFGDGMFSEIHTDGLLPFGAFSKNFCsKSYEGLPTYKNAIYQ 913
Cdd:cd05835     2 IGDLVWAKLKGSPWWPGIVVSHKDCGQkppAEGSVWVFWFGDHKVSEVPLDKILPFAEFFNKFY-ISKNSSKLYKKAVYE 80


                  ....*....
gi 528487581  914 ILELAAERS 922
Cdd:cd05835    81 ALKEAAERS 89
Dcm COG0270
DNA-cytosine methylase [Replication, recombination and repair];
1152-1430 6.08e-20

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


Pssm-ID: 440040 [Multi-domain]  Cd Length: 277  Bit Score: 91.41  E-value: 6.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1152 RRPIRVLSLFDGIatGYLvlkDLGFKLERY---IASEICEDSIAVGMVKHEGKIEYVKDVRTITRKHLAewGPFDLLIGG 1228
Cdd:COG0270     1 SKKLTVIDLFAGA--GGL---SLGFEKAGFevvFAVEIDPDACETYRANFPEAKVIEGDIRDIDPEELI--PDVDLLIGG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1229 SPCNDLSMVNPaRKGlFEGT-GRLFFEYYRMLTMMRPKedddrpfFWLFENVVAMSAHDK----ADICRFLE-----CNP 1298
Cdd:COG0270    74 PPCQPFSVAGK-RKG-LEDPrGTLFFEFIRIVEELRPK-------AFVLENVPGLLSSDKgktfEEILKELEelgyrVDY 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1299 VMIDA----VkvsPAHRARYF----WGNLPGMNRPVATSLTDNVDLQDCLESGRTAMFSKV--RTITTksnsikqgktgp 1368
Cdd:COG0270   145 KVLNAadygV---PQNRERVFivgfRKDLDLFEFPEPTHLKPYVTVGDALEDLPDAHEARYlsETITA------------ 209

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1369 lpvTMNGKEDYL------WCT--EMEKIFGFPKHYTDVNNmgRGQRQKVLGRSWSVPVIRHLFAPLKDYF 1430
Cdd:COG0270   210 ---GYGGGGRFLhpgeprRLTvrEAARLQGFPDDFKFPGS--KTQAYRQIGNAVPPPLAEAIAKAILKAL 274
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
 1155-1423 5.37e-15

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: 76.89  E-value: 5.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1155 IRVLSLFDGIATGYLVLKDLGFKLerYIASEICEDSIAVGMVKHEGKIeYVKDVRTITRKHLAEwgPFDLLIGGSPCNDL 1234
Cdd:cd00315     1 LRVIDLFAGIGGFRLGLEKAGFEI--VAANEIDKSAAETYEANFPNKL-IEGDITKIDEKDFIP--DIDLLTGGFPCQPF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1235 SmVNPARKGlFEGT-GRLFFEYYRMLTMMRPKedddrpfFWLFENVVAMSAHDK----ADICRFLE-----CNPVMIDA- 1303
Cdd:cd00315    76 S-IAGKRKG-FEDTrGTLFFEIIRILKEKKPK-------YFLLENVKGLLTHDNgntlKVILNTLEelgynVYWKLLNAs 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1304 ---VkvsPAHRARYFW-GNLPGMN----RPVATSLTDNVDLQDCLESGRTAmfSKVRTITTkSNSIKQGKTGPLPVTMNG 1375
Cdd:cd00315   147 dygV---PQNRERVFIiGIRKDLIlnffSPFPKPSEKKKTLKDILRIRDPD--EPSPTLTA-SYGKGTGSVHPTAPDMIG 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528487581 1376 KED---YLWCTEMEKIFGFPKHYtDVNNMGRGQRQKVLGRSWSVPVIRHLF 1423
Cdd:cd00315   221 KESnirRLTPRECARLQGFPDDF-EFPGKSVTQAYRQIGNSVPVPVAEAIA 270
BIM1 COG5217
Microtubule-binding protein involved in cell cycle control [Cell division and chromosome ...
 17-174 1.09e-13

Microtubule-binding protein involved in cell cycle control [Cell division and chromosome partitioning / Cytoskeleton];


Pssm-ID: 227542 [Multi-domain]  Cd Length: 342  Bit Score: 74.26  E-value: 1.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581   17 SRYEVLGWINETLQTNFTQVEQCRSGACFCQLIDLLFpGTINLKKVKFESQKRSDFMQNYGLLQAAFRDLEVTEPVPVNE 96
Cdd:COG5217     8 SREELLFWENVVVRLDLQRIEDCGEGFAMQQIHDSIY-VDLPDSLVRFPWIAEYKHPGNGKILQLLFSDYGIDKAVLVLV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581   97 LLSGKFRPNFTYLKWFKKFFYANvKQERVYNAFEARDGQEIVPVDDVMKSPKAL------KSSYESGRAG------EESD 164
Cdd:COG5217    87 LVRCKLQDNLEFLQWLKDHWVRN-LGHISYDRNARRLGRTPKSTRELIEWIRSLgipisaIRELSKGVASckslstIHSS 165

                         170
                  ....*....|
gi 528487581  165 MEINGGRRSA 174
Cdd:COG5217   166 FPQNFVKNTA 175
PWWP cd05162
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
 838-917 4.06e-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: 66.37  E-value: 4.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581  838 GELVWGKVKDFSLWPGLVV------PWKGRIVPVSMRRVEWFGDGMFSEIHTDGLLPFGAFSKNFCSKSYEGLPTYKNAI 911
Cdd:cd05162     1 GDLVWAKLKGYPWWPARVVdpeelpEEVGKKKKKGGVLVQFFGDNDYAWVKSKNIKPFEEGFKKEFKKKKKKSKKFKKAV 80


                  ....*.
gi 528487581  912 YQILEL 917
Cdd:cd05162    81 EEAEEA 86
ADDz_ATRX cd11726
ADDz domain found in ATRX (alpha-thalassemia/mental retardation, X-linked); ADDz_ATRX is a ...
 1014-1109 8.30e-13

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


Pssm-ID: 277252 [Multi-domain]  Cd Length: 102  Bit Score: 65.79  E-value: 8.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581 1014 FCLSCGSS-NT---EIF-HPLFKGSLCIKCKENFTETLYRYDDDGYQSYCTVCCAGLEVILCGnaSCCRCFCKDCLNVLV 1088
Cdd:cd11726     4 RCTACGEQlNHfskEVHrHPVLKVLICKSCLKFYNSGEFSKDEDGSDEYCRWCGQGGDLICCD--FCPNVFCKKCIKRNL 81

                          90       100
                  ....*....|....*....|.
gi 528487581 1089 GPGTFDKLKEVDPWSCYVCLP 1109
Cdd:cd11726    82 GRAELSRIEESDKWKCFVCDP 102
dcm TIGR00675
DNA-methyltransferase (dcm); All proteins in this family for which functions are known are ...
 1157-1420 8.50e-13

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: 71.20  E-value: 8.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581  1157 VLSLFDGIATGYLVLKDLGFKLerYIASEIceDSIAVGMVK--HEGKIEYvKDVRTITRKHLAEwgpFDLLIGGSPCNDL 1234
Cdd:TIGR00675    1 FIDLFAGIGGIRLGFEQAGFKC--VFASEI--DKYAQKTYEanFGNKVPF-GDITKISPSDIPD---FDILLGGFPCQPF 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581  1235 SMvnpARKGL-FEGT-GRLFFEYYRMLTMMRPKedddrpfFWLFENVVAMSAHDKAdicRFLecnPVMIDAV-----KVS 1307
Cdd:TIGR00675   73 SI---AGKRKgFEDTrGTLFFEIVRILKEKKPK-------FFLLENVKGLVSHDKG---RTF---KVIIETLeelgyKVY 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581  1308 -----------PAHRAR-YFWG----------NLP-GMNRPVATSLTDNVDLQDCLESG-----------------RTAM 1347
Cdd:TIGR00675  137 ykvlnakdfgvPQNRERiYIVGfrdfddklnfEFPkPIYVAKKKRIGDLLDLSVDLEEKyylseekknglllllenMRKK 216

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581  1348 FSKVRTITTKSNS-----------------IKQGKTgpLPVTMNGKEDY-------LWCTEMEKIFGFPKHYTDvnNMGR 1403
Cdd:TIGR00675  217 EGTGEQIGSFYNReskssiirtlsargytfVKGGKS--VLIVPHKSTVVhpgrirrLTPRECARLQGFPDDFKF--PVSD 292

                          330
                   ....*....|....*..
gi 528487581  1404 GQRQKVLGRSWSVPVIR 1420
Cdd:TIGR00675  293 SQLYKQAGNAVVVPVIE 309
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 838-918 8.69e-12

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: 62.44  E-value: 8.69e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581   838 GELVWGKVKDFSLWPGLVVPWKgrIVPVSMRR---------VEWFGDGMFSEIHTDGLLPFGAFSKNFCSKSYEG---LP 905
Cdd:pfam00855    1 GDLVWAKLKGYPWWPARVVDPE--ELPENVLKpkkkdgeylVRFFGDSEFAWVKPKDLKPFDEGDEFEYLKKKKKkkkKK 78

                           90
                   ....*....|...
gi 528487581   906 TYKNAIYQILELA 918
Cdd:pfam00855   79 AFKKALEEAEEAL 91
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
1155-1287 2.02e-11

C-5 cytosine-specific DNA methylase;


Pssm-ID: 395093 [Multi-domain]  Cd Length: 324  Bit Score: 66.95  E-value: 2.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581  1155 IRVLSLFDGIATGYLVLKDLGFKLerYIASEICEDSIAVGMVKHEGKIEyvKDVRTITRKHLAEwgpFDLLIGGSPCNDL 1234
Cdd:pfam00145    1 FKFIDLFAGIGGFRLGLEQAGFEC--VAANEIDKSAAKTYEANFPKVPI--GDITLIDIKDIPD---IDILTGGFPCQDF 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 528487581  1235 SmVNPARKGLFEGTGRLFFEYYRMLTMMRPKedddrpfFWLFENVVAMSAHDK 1287
Cdd:pfam00145   74 S-IAGKQKGFEDTRGTLFFEIIRIIKEKKPK-------AFLLENVKGLLSHDN 118
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 15-118 1.27e-10

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 59.99  E-value: 1.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581    15 KCSRYEVLGWINETLQ--------TNFTqvEQCRSGACFCQLIDLLFPGTINLKKVKfesQKRSDFMQNYGL-LQAAFRD 85
Cdd:pfam00307    1 LELEKELLRWINSHLAeygpgvrvTNFT--TDLRDGLALCALLNKLAPGLVDKKKLN---KSEFDKLENINLaLDVAEKK 75

                           90       100       110
                   ....*....|....*....|....*....|....
gi 528487581    86 LEVTEPVP-VNELLSGKFRPNFTYLKWFKKFFYA 118
Cdd:pfam00307   76 LGVPKVLIePEDLVEGDNKSVLTYLASLFRRFQA 109
PWWP_PWWP2 cd20140
PWWP domain found in the PWWP domain-containing protein 2 (PWWP2) family; The PWWP2 family ...
 832-918 1.34e-08

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: 53.42  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581  832 GKGFAVGELVWGKVKDFSLWPGLVVP-WKGRIVPVSMR----RVEWFGDGMFSEIHTDGLLPFGAFSKNFCSKSYEGLpt 906
Cdd:cd20140     1 GRTLRVGDIVWGKIHGFPWWPGRILSiTVSRDDNGELStqeaHVSWFGSSTTSYMPCSQLYPFLEDFKLRYNKKKRGP-- 78

                          90
                  ....*....|..
gi 528487581  907 YKNAIYQILELA 918
Cdd:cd20140    79 YKEAVRQALEAA 90
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
 835-916 3.90e-08

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: 51.84  E-value: 3.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581  835 FAVGELVWGKVKDFSLWPGLVV-PWKGRIVPVSMRRVEW---FGDGMFSEIHTDGLLPFGAFSKNFCSKSyeGLPTYKNA 910
Cdd:cd05836     1 FKIGDLVWAKMKGFPPWPGKIVnPPPDLKKPPRKKKMHCvyfFGSENYAWIEDENIKPYEEFKEEMLKSK--KSAGFKDA 78


                  ....*.
gi 528487581  911 IYQILE 916
Cdd:cd05836    79 VEAIEE 84
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 835-890 4.27e-08

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 51.19  E-value: 4.27e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528487581    835 FAVGELVWGKVKDFSLWPGLVVPWKgrIVPVSMRR---------VEWFGDGMFSEIHTDGLLPFG 890
Cdd:smart00293    1 FKPGDLVWAKMKGFPWWPALVISPK--MTPDNIMKrksdenlypVLFFGDKDTAWIPSSKLFPLT 63
PWWP_MBD5 cd20141
PWWP domain found in methyl-CpG-binding domain protein 5 (MBD5) and similar proteins; MBD5, is ...
 835-886 1.07e-06

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: 48.08  E-value: 1.07e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 528487581  835 FAVGELVWGKVKDFSLWPG-LVVPWKGRIVPVSMRRVEWFGDGMFSEIHTDGL 886
Cdd:cd20141     1 FNVGDLVWGQIRGFPSWPGkLVSENDVGKTNEGKVWVSWFGDHSFGQVEPDKL 53
PWWP_PWWP2A cd20152
PWWP domain found in PWWP domain-containing protein 2A (PWWP2A); PWWP2A is a H2A.Z-specific ...
 831-940 7.16e-06

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: 46.54  E-value: 7.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581  831 DGKGFAVGELVWGKVKDFSLWPG----LVVPWKGRIVPVSMR-RVEWFGDGMFSEIHTDGLLPF-GAFSKNFcSKSYEGL 904
Cdd:cd20152    16 DGRTICVGDIVWAKIYGFPWWPArilaITVSRKDNGLLVRQEaRISWFGSPTTSFLALSQLAPFlENFQSRF-NKKRKGL 94

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 528487581  905 ptYKNAIYQilelaAERSGKLFPPsekkgeEVKAMM 940
Cdd:cd20152    95 --YRKAITE-----AAKAAKQLTP------EVRALL 117
PWWP_PWWP2B cd20153
PWWP domain found in PWWP domain-containing protein 2B (PWWP2B); PWWP2B is a paralog of PWWP2A, ...
 831-911 1.30e-05

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: 45.72  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581  831 DGKGFAVGELVWGKVKDFSLWPglvvpwkGRIVPVSMR------------RVEWFGDGMFSEIHTDGLLPFGAFSKNFCS 898
Cdd:cd20153    10 EGRTVSVGDIVWGKIHGFPWWP-------ARVLSISLSqkedgepswqeaKVSWFGSPTTSLLSVSKLSPFSEFFKLRFN 82

                          90
                  ....*....|...
gi 528487581  899 KSYEGLptYKNAI 911
Cdd:cd20153    83 RKKKGM--YRKAI 93
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 19-95 1.47e-04

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 42.30  E-value: 1.47e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581     19 YEVLGWINETLQ-------TNFTQVeqCRSGACFCQLIDLLFPGTINLKKVKfESQKRSDFMQNyglLQAAFRDLEVTEP 91
Cdd:smart00033    1 KTLLRWVNSLLAeydkppvTNFSSD--LKDGVALCALLNSLSPGLVDKKKVA-ASLSRFKKIEN---INLALSFAEKLGG 74


                    ....
gi 528487581     92 VPVN 95
Cdd:smart00033   75 KVVL 78
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 20-92 1.05e-03

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 40.01  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528487581   20 EVLGWINETLQ-------TNFTqvEQCRSGACFCQLIDLLFPGTInlKKVKFESQKRSDFMQNYGLLQAAFRDLEVTEPV 92
Cdd:cd00014     3 ELLKWINEVLGeelpvsiTDLF--ESLRDGVLLCKLINKLSPGSI--PKINKKPKSPFKKRENINLFLNACKKLGLPELD 78
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 24-68 8.93e-03

first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 37.55  E-value: 8.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 528487581   24 WINETLQ-TNFTQV------------EQCRSGACFCQLIDLLFPGTINLKKVKFESQK 68
Cdd:cd21217     9 HINSLLAdDPDLKHllpidpdgddlfEALRDGVLLCKLINKIVPGTIDERKLNKKKPK 66
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH