methyl-CpG-binding domain protein 1 isoform X3 [Homo sapiens]
Protein Classification
MeCP2_MBD and zf-CXXC domain-containing protein( domain architecture ID 11267665)
MeCP2_MBD and zf-CXXC domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| MBD | smart00391 | Methyl-CpG binding domain; Methyl-CpG binding domain, also known as the TAM (TTF-IIP5, ARBP, ... |
3-76 | 6.79e-24 | ||
Methyl-CpG binding domain; Methyl-CpG binding domain, also known as the TAM (TTF-IIP5, ARBP, MeCP1) domain : Pssm-ID: 128673 Cd Length: 77 Bit Score: 95.52 E-value: 6.79e-24
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| zf-CXXC | pfam02008 | CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ... |
356-402 | 5.25e-15 | ||
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases. : Pssm-ID: 366873 Cd Length: 48 Bit Score: 69.31 E-value: 5.25e-15
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| zf-CXXC | pfam02008 | CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ... |
168-215 | 4.17e-10 | ||
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases. : Pssm-ID: 366873 Cd Length: 48 Bit Score: 55.44 E-value: 4.17e-10
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| zf-CXXC | pfam02008 | CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ... |
217-262 | 2.73e-08 | ||
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases. : Pssm-ID: 366873 Cd Length: 48 Bit Score: 50.05 E-value: 2.73e-08
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| Name | Accession | Description | Interval | E-value | ||
| MBD | smart00391 | Methyl-CpG binding domain; Methyl-CpG binding domain, also known as the TAM (TTF-IIP5, ARBP, ... |
3-76 | 6.79e-24 | ||
Methyl-CpG binding domain; Methyl-CpG binding domain, also known as the TAM (TTF-IIP5, ARBP, MeCP1) domain Pssm-ID: 128673 Cd Length: 77 Bit Score: 95.52 E-value: 6.79e-24
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| MeCP2_MBD | cd01396 | MeCP2, MBD1, MBD2, MBD3, and MBD4 are members of a protein family that share the ... |
5-75 | 6.89e-22 | ||
MeCP2, MBD1, MBD2, MBD3, and MBD4 are members of a protein family that share the methyl-CpG-binding domain (MBD). The MBD, consists of about 70 residues and is defined as the minimal region required for binding to methylated DNA by a methyl-CpG-binding protein which binds specifically to methylated DNA. The MBD can recognize a single symmetrically methylated CpG either as naked DNA or within chromatin. MeCP2, MBD1 and MBD2 (and likely MBD3) form complexes with histone deacetylase and are involved in histone deacetylase-dependent repression of transcription. MBD4 is an endonuclease that forms a complex with the DNA mismatch-repair protein MLH1. Pssm-ID: 238690 Cd Length: 77 Bit Score: 89.74 E-value: 6.89e-22
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| MBD | pfam01429 | Methyl-CpG binding domain; The Methyl-CpG binding domain (MBD) binds to DNA that contains one ... |
1-70 | 3.68e-18 | ||
Methyl-CpG binding domain; The Methyl-CpG binding domain (MBD) binds to DNA that contains one or more symmetrically methylated CpGs. DNA methylation in animals is associated with alterations in chromatin structure and silencing of gene expression. MBD has negligible non-specific affinity for DNA. In vitro foot-printing with MeCP2 showed the MBD can protect a 12 nucleotide region surrounding a methyl CpG pair. MBDs are found in several Methyl-CpG binding proteins and also DNA demethylase. Pssm-ID: 396147 [Multi-domain] Cd Length: 76 Bit Score: 78.94 E-value: 3.68e-18
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| zf-CXXC | pfam02008 | CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ... |
356-402 | 5.25e-15 | ||
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases. Pssm-ID: 366873 Cd Length: 48 Bit Score: 69.31 E-value: 5.25e-15
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| zf-CXXC | pfam02008 | CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ... |
168-215 | 4.17e-10 | ||
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases. Pssm-ID: 366873 Cd Length: 48 Bit Score: 55.44 E-value: 4.17e-10
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| zf-CXXC | pfam02008 | CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ... |
217-262 | 2.73e-08 | ||
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases. Pssm-ID: 366873 Cd Length: 48 Bit Score: 50.05 E-value: 2.73e-08
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| Name | Accession | Description | Interval | E-value | ||
| MBD | smart00391 | Methyl-CpG binding domain; Methyl-CpG binding domain, also known as the TAM (TTF-IIP5, ARBP, ... |
3-76 | 6.79e-24 | ||
Methyl-CpG binding domain; Methyl-CpG binding domain, also known as the TAM (TTF-IIP5, ARBP, MeCP1) domain Pssm-ID: 128673 Cd Length: 77 Bit Score: 95.52 E-value: 6.79e-24
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| MeCP2_MBD | cd01396 | MeCP2, MBD1, MBD2, MBD3, and MBD4 are members of a protein family that share the ... |
5-75 | 6.89e-22 | ||
MeCP2, MBD1, MBD2, MBD3, and MBD4 are members of a protein family that share the methyl-CpG-binding domain (MBD). The MBD, consists of about 70 residues and is defined as the minimal region required for binding to methylated DNA by a methyl-CpG-binding protein which binds specifically to methylated DNA. The MBD can recognize a single symmetrically methylated CpG either as naked DNA or within chromatin. MeCP2, MBD1 and MBD2 (and likely MBD3) form complexes with histone deacetylase and are involved in histone deacetylase-dependent repression of transcription. MBD4 is an endonuclease that forms a complex with the DNA mismatch-repair protein MLH1. Pssm-ID: 238690 Cd Length: 77 Bit Score: 89.74 E-value: 6.89e-22
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| MBD | pfam01429 | Methyl-CpG binding domain; The Methyl-CpG binding domain (MBD) binds to DNA that contains one ... |
1-70 | 3.68e-18 | ||
Methyl-CpG binding domain; The Methyl-CpG binding domain (MBD) binds to DNA that contains one or more symmetrically methylated CpGs. DNA methylation in animals is associated with alterations in chromatin structure and silencing of gene expression. MBD has negligible non-specific affinity for DNA. In vitro foot-printing with MeCP2 showed the MBD can protect a 12 nucleotide region surrounding a methyl CpG pair. MBDs are found in several Methyl-CpG binding proteins and also DNA demethylase. Pssm-ID: 396147 [Multi-domain] Cd Length: 76 Bit Score: 78.94 E-value: 3.68e-18
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| MBD | cd00122 | MeCP2, MBD1, MBD2, MBD3, MBD4, CLLD8-like, and BAZ2A-like proteins constitute a family of ... |
5-64 | 3.96e-16 | ||
MeCP2, MBD1, MBD2, MBD3, MBD4, CLLD8-like, and BAZ2A-like proteins constitute a family of proteins that share the methyl-CpG-binding domain (MBD). The MBD consists of about 70 residues and is defined as the minimal region required for binding to methylated DNA by a methyl-CpG-binding protein which binds specifically to methylated DNA. The MBD can recognize a single symmetrically methylated CpG either as naked DNA or within chromatin. MeCP2, MBD1 and MBD2 (and likely MBD3) form complexes with histone deacetylase and are involved in histone deacetylase-dependent repression of transcription. MBD4 is an endonuclease that forms a complex with the DNA mismatch-repair protein MLH1. The MBDs present in putative chromatin remodelling subunit, BAZ2A, and putative histone methyltransferase, CLLD8, represent two phylogenetically distinct groups within the MBD protein family. Pssm-ID: 238069 Cd Length: 62 Bit Score: 72.74 E-value: 3.96e-16
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| zf-CXXC | pfam02008 | CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ... |
356-402 | 5.25e-15 | ||
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases. Pssm-ID: 366873 Cd Length: 48 Bit Score: 69.31 E-value: 5.25e-15
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| zf-CXXC | pfam02008 | CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ... |
168-215 | 4.17e-10 | ||
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases. Pssm-ID: 366873 Cd Length: 48 Bit Score: 55.44 E-value: 4.17e-10
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| zf-CXXC | pfam02008 | CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ... |
217-262 | 2.73e-08 | ||
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterized by two repeats, and shows a peculiar internal duplication in which the second unit is inserted into the first one. Each of these units is characterized by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases. Pssm-ID: 366873 Cd Length: 48 Bit Score: 50.05 E-value: 2.73e-08
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| Blast search parameters | ||||
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