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Conserved domains on  [gi|21355905|ref|NP_649907|]
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Methyl-CpG binding domain protein-like, isoform B [Drosophila melanogaster]

Protein Classification

MBDa and MBD_C domain-containing protein( domain architecture ID 11244108)

MBDa and MBD_C domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MBD_C pfam14048
C-terminal domain of methyl-CpG binding protein 2 and 3; CpG-methylation is a frequently ...
131-224 3.41e-33

C-terminal domain of methyl-CpG binding protein 2 and 3; CpG-methylation is a frequently occurring epigenetic modification of vertebrate genomes resulting in transcriptional repression. This domain was found at the C-terminus of the methyl-CpG-binding domain (MBD) containing proteins MBD2 and MBD3, the latter was shown to not bind directly to methyl-CpG DNA but rather interact with components of the NuRD/Mi2 complex, an abundant deacetylase complex. The domain is subject to structure determination by the Joint Center of Structural Genomics.


:

Pssm-ID: 464072  Cd Length: 94  Bit Score: 115.03  E-value: 3.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355905   131 SGEELDDISLPKTIRTVGPNVNEQTVLQSVATALHMLNAGVHGQSSTKADLTKNAMAFMNPEQPLMHAVIISEDDIRKQE 210
Cdd:pfam14048   1 DGELLSTLDLPKSLKPIGPGITDETLLQSLATALHSSPQPITGQTASSDALEKNPGVGLNPDQPLCKQFVITEEDIRRQE 80
                          90
                  ....*....|....
gi 21355905   211 DRVGVARRKLQDAL 224
Cdd:pfam14048  81 ERVKKARKRLAEAL 94
MBDa pfam16564
p55-binding region of Methyl-CpG-binding domain proteins MBD; MBDa is a second MBD domain of ...
57-127 3.75e-26

p55-binding region of Methyl-CpG-binding domain proteins MBD; MBDa is a second MBD domain of Methyl-CpG-binding domain proteins. region implicated in binding the RbAp46/48 (retinoblastoma protein-associated protein) homolog p55, which is one of the components of the MBD2-NuRD complex. The MBD2-NuRD complex is a nucleosome remodelling and deacetylation complex.


:

Pssm-ID: 465179  Cd Length: 68  Bit Score: 96.17  E-value: 3.75e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21355905    57 KVDVFYYSRaLRTDVSLVPPIRQTASIFKQPVTVIRNHkqDPAKAKNEPKHGTREKPKQLFWEKRLERLRA 127
Cdd:pfam16564   1 RQDQLDKAK-RRPDLSTALPIRLTSCIFKQPVTRITSH--PGNKVRYRPKEGTLEKPQQLCWEKRLQGLQA 68
 
Name Accession Description Interval E-value
MBD_C pfam14048
C-terminal domain of methyl-CpG binding protein 2 and 3; CpG-methylation is a frequently ...
131-224 3.41e-33

C-terminal domain of methyl-CpG binding protein 2 and 3; CpG-methylation is a frequently occurring epigenetic modification of vertebrate genomes resulting in transcriptional repression. This domain was found at the C-terminus of the methyl-CpG-binding domain (MBD) containing proteins MBD2 and MBD3, the latter was shown to not bind directly to methyl-CpG DNA but rather interact with components of the NuRD/Mi2 complex, an abundant deacetylase complex. The domain is subject to structure determination by the Joint Center of Structural Genomics.


Pssm-ID: 464072  Cd Length: 94  Bit Score: 115.03  E-value: 3.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355905   131 SGEELDDISLPKTIRTVGPNVNEQTVLQSVATALHMLNAGVHGQSSTKADLTKNAMAFMNPEQPLMHAVIISEDDIRKQE 210
Cdd:pfam14048   1 DGELLSTLDLPKSLKPIGPGITDETLLQSLATALHSSPQPITGQTASSDALEKNPGVGLNPDQPLCKQFVITEEDIRRQE 80
                          90
                  ....*....|....
gi 21355905   211 DRVGVARRKLQDAL 224
Cdd:pfam14048  81 ERVKKARKRLAEAL 94
MBDa pfam16564
p55-binding region of Methyl-CpG-binding domain proteins MBD; MBDa is a second MBD domain of ...
57-127 3.75e-26

p55-binding region of Methyl-CpG-binding domain proteins MBD; MBDa is a second MBD domain of Methyl-CpG-binding domain proteins. region implicated in binding the RbAp46/48 (retinoblastoma protein-associated protein) homolog p55, which is one of the components of the MBD2-NuRD complex. The MBD2-NuRD complex is a nucleosome remodelling and deacetylation complex.


Pssm-ID: 465179  Cd Length: 68  Bit Score: 96.17  E-value: 3.75e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21355905    57 KVDVFYYSRaLRTDVSLVPPIRQTASIFKQPVTVIRNHkqDPAKAKNEPKHGTREKPKQLFWEKRLERLRA 127
Cdd:pfam16564   1 RQDQLDKAK-RRPDLSTALPIRLTSCIFKQPVTRITSH--PGNKVRYRPKEGTLEKPQQLCWEKRLQGLQA 68
 
Name Accession Description Interval E-value
MBD_C pfam14048
C-terminal domain of methyl-CpG binding protein 2 and 3; CpG-methylation is a frequently ...
131-224 3.41e-33

C-terminal domain of methyl-CpG binding protein 2 and 3; CpG-methylation is a frequently occurring epigenetic modification of vertebrate genomes resulting in transcriptional repression. This domain was found at the C-terminus of the methyl-CpG-binding domain (MBD) containing proteins MBD2 and MBD3, the latter was shown to not bind directly to methyl-CpG DNA but rather interact with components of the NuRD/Mi2 complex, an abundant deacetylase complex. The domain is subject to structure determination by the Joint Center of Structural Genomics.


Pssm-ID: 464072  Cd Length: 94  Bit Score: 115.03  E-value: 3.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355905   131 SGEELDDISLPKTIRTVGPNVNEQTVLQSVATALHMLNAGVHGQSSTKADLTKNAMAFMNPEQPLMHAVIISEDDIRKQE 210
Cdd:pfam14048   1 DGELLSTLDLPKSLKPIGPGITDETLLQSLATALHSSPQPITGQTASSDALEKNPGVGLNPDQPLCKQFVITEEDIRRQE 80
                          90
                  ....*....|....
gi 21355905   211 DRVGVARRKLQDAL 224
Cdd:pfam14048  81 ERVKKARKRLAEAL 94
MBDa pfam16564
p55-binding region of Methyl-CpG-binding domain proteins MBD; MBDa is a second MBD domain of ...
57-127 3.75e-26

p55-binding region of Methyl-CpG-binding domain proteins MBD; MBDa is a second MBD domain of Methyl-CpG-binding domain proteins. region implicated in binding the RbAp46/48 (retinoblastoma protein-associated protein) homolog p55, which is one of the components of the MBD2-NuRD complex. The MBD2-NuRD complex is a nucleosome remodelling and deacetylation complex.


Pssm-ID: 465179  Cd Length: 68  Bit Score: 96.17  E-value: 3.75e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21355905    57 KVDVFYYSRaLRTDVSLVPPIRQTASIFKQPVTVIRNHkqDPAKAKNEPKHGTREKPKQLFWEKRLERLRA 127
Cdd:pfam16564   1 RQDQLDKAK-RRPDLSTALPIRLTSCIFKQPVTRITSH--PGNKVRYRPKEGTLEKPQQLCWEKRLQGLQA 68
MBD pfam01429
Methyl-CpG binding domain; The Methyl-CpG binding domain (MBD) binds to DNA that contains one ...
9-126 5.66e-12

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: 59.30  E-value: 5.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355905     9 IERKRVDCSVLPKGWQRDEV-RKSGssannnassnnnssatassnNNNNKVDVFYYSralrtdvslvpPIRQTASIFKQP 87
Cdd:pfam01429   1 IERKREDRLPLPPGWRREERqRKSG--------------------SKAGKVDVFYYS-----------PTGKKLRSKSEV 49
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 21355905    88 VTVIRNHKqdpakaknepkhGTREKPKQLFWEKRLERLR 126
Cdd:pfam01429  50 ARYLEANG------------GTSPKLEDFSFTVRSEVGR 76
 
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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