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Conserved domains on  [gi|2180230694|ref|NP_001386891|]
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methyl-CpG-binding domain protein 1 isoform 110 [Homo sapiens]

Protein Classification

CXXC-type zinc finger protein( domain architecture ID 10488070)

CXXC-type zinc finger protein, such as human CXXC4 and CXXC5, contains eight conserved cysteine residues that bind to two zinc ions and plays important roles in epigenetic regulation by targeting various activities to CpG islands

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 162-208 2.21e-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: 70.08  E-value: 2.21e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2180230694 162 NRRQNRKCGACAACLRRMDCGRCDFCCDKPKFGGSNQKRQKCRWRQC 208
Cdd:pfam02008   2 NRRKRRRCGVCEGCQRPEDCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 1-46 3.81e-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: 55.05  E-value: 3.81e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2180230694   1 MFKRVGCGECAACQVTEDCGACSTCLLQLPHDVASGLFCKCERRRC 46
Cdd:pfam02008   3 RRKRRRCGVCEGCQRPEDCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 48-93 1.33e-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: 50.82  E-value: 1.33e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2180230694  48 RIVERSRGCGVCRGCQTQEDCGHCPICLRPPRPGL--RRQWKCVQRRC 93
Cdd:pfam02008   1 RNRRKRRRCGVCEGCQRPEDCGQCSFCLDMPKFGGpgKKKQKCRLRRC 48
 
Name Accession Description Interval E-value
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 162-208 2.21e-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: 70.08  E-value: 2.21e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2180230694 162 NRRQNRKCGACAACLRRMDCGRCDFCCDKPKFGGSNQKRQKCRWRQC 208
Cdd:pfam02008   2 NRRKRRRCGVCEGCQRPEDCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 1-46 3.81e-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: 55.05  E-value: 3.81e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2180230694   1 MFKRVGCGECAACQVTEDCGACSTCLLQLPHDVASGLFCKCERRRC 46
Cdd:pfam02008   3 RRKRRRCGVCEGCQRPEDCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 48-93 1.33e-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: 50.82  E-value: 1.33e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2180230694  48 RIVERSRGCGVCRGCQTQEDCGHCPICLRPPRPGL--RRQWKCVQRRC 93
Cdd:pfam02008   1 RNRRKRRRCGVCEGCQRPEDCGQCSFCLDMPKFGGpgKKKQKCRLRRC 48
 
Name Accession Description Interval E-value
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 162-208 2.21e-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: 70.08  E-value: 2.21e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2180230694 162 NRRQNRKCGACAACLRRMDCGRCDFCCDKPKFGGSNQKRQKCRWRQC 208
Cdd:pfam02008   2 NRRKRRRCGVCEGCQRPEDCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 1-46 3.81e-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: 55.05  E-value: 3.81e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2180230694   1 MFKRVGCGECAACQVTEDCGACSTCLLQLPHDVASGLFCKCERRRC 46
Cdd:pfam02008   3 RRKRRRCGVCEGCQRPEDCGQCSFCLDMPKFGGPGKKKQKCRLRRC 48
zf-CXXC pfam02008
CXXC zinc finger domain; This domain contains eight conserved cysteine residues that bind to ...
 48-93 1.33e-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: 50.82  E-value: 1.33e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2180230694  48 RIVERSRGCGVCRGCQTQEDCGHCPICLRPPRPGL--RRQWKCVQRRC 93
Cdd:pfam02008   1 RNRRKRRRCGVCEGCQRPEDCGQCSFCLDMPKFGGpgKKKQKCRLRRC 48
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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