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Conserved domains on  [gi|1281027836|ref|XP_022998335|]
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methyl-CpG-binding domain-containing protein 5-like isoform X1 [Cucurbita maxima]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MBD super family cl00110
MeCP2, MBD1, MBD2, MBD3, MBD4, CLLD8-like, and BAZ2A-like proteins constitute a family of ...
127-172 1.34e-11

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.


The actual alignment was detected with superfamily member cd01396:

Pssm-ID: 469618  Cd Length: 77  Bit Score: 58.92  E-value: 1.34e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1281027836 127 WLPPGWVVEDRVRASGaTAGTVDKYYFDPnSGRRFRSKIEVLYFLE 172
Cdd:cd01396     6 RLPPGWKRELVPRKSG-SAGKFDVYYISP-TGKKFRSKVELARYLE 49
 
Name Accession Description Interval E-value
MeCP2_MBD cd01396
MeCP2, MBD1, MBD2, MBD3, and MBD4 are members of a protein family that share the ...
127-172 1.34e-11

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: 58.92  E-value: 1.34e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1281027836 127 WLPPGWVVEDRVRASGaTAGTVDKYYFDPnSGRRFRSKIEVLYFLE 172
Cdd:cd01396     6 RLPPGWKRELVPRKSG-SAGKFDVYYISP-TGKKFRSKVELARYLE 49
MBD pfam01429
Methyl-CpG binding domain; The Methyl-CpG binding domain (MBD) binds to DNA that contains one ...
126-172 8.28e-10

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: 53.90  E-value: 8.28e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1281027836 126 NWLPPGWVVEDRVRASGATAGTVDKYYFDPNsGRRFRSKIEVLYFLE 172
Cdd:pfam01429   9 LPLPPGWRREERQRKSGSKAGKVDVFYYSPT-GKKLRSKSEVARYLE 54
MBD smart00391
Methyl-CpG binding domain; Methyl-CpG binding domain, also known as the TAM (TTF-IIP5, ARBP, ...
128-176 3.22e-06

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: 43.90  E-value: 3.22e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1281027836  128 LPPGWVVEDRVRASGATAGTVDKYYFDPnSGRRFRSKIEVL-YFLETGTL 176
Cdd:smart00391   8 LPCGWRRETKQRKSGRSAGKFDVYYISP-CGKKLRSKSELArYLHKNGDL 56
 
Name Accession Description Interval E-value
MeCP2_MBD cd01396
MeCP2, MBD1, MBD2, MBD3, and MBD4 are members of a protein family that share the ...
127-172 1.34e-11

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: 58.92  E-value: 1.34e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1281027836 127 WLPPGWVVEDRVRASGaTAGTVDKYYFDPnSGRRFRSKIEVLYFLE 172
Cdd:cd01396     6 RLPPGWKRELVPRKSG-SAGKFDVYYISP-TGKKFRSKVELARYLE 49
MBD cd00122
MeCP2, MBD1, MBD2, MBD3, MBD4, CLLD8-like, and BAZ2A-like proteins constitute a family of ...
127-172 2.36e-10

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: 55.02  E-value: 2.36e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1281027836 127 WLPPGWVVEDRVRASGaTAGTVDKYYFDPnSGRRFRSKIEVLYFLE 172
Cdd:cd00122     5 PLPPGWKRELVIRKSG-SAGKGDVYYYSP-CGKKLRSKPEVARYLE 48
MBD pfam01429
Methyl-CpG binding domain; The Methyl-CpG binding domain (MBD) binds to DNA that contains one ...
126-172 8.28e-10

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: 53.90  E-value: 8.28e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1281027836 126 NWLPPGWVVEDRVRASGATAGTVDKYYFDPNsGRRFRSKIEVLYFLE 172
Cdd:pfam01429   9 LPLPPGWRREERQRKSGSKAGKVDVFYYSPT-GKKLRSKSEVARYLE 54
MBD smart00391
Methyl-CpG binding domain; Methyl-CpG binding domain, also known as the TAM (TTF-IIP5, ARBP, ...
128-176 3.22e-06

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: 43.90  E-value: 3.22e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1281027836  128 LPPGWVVEDRVRASGATAGTVDKYYFDPnSGRRFRSKIEVL-YFLETGTL 176
Cdd:smart00391   8 LPCGWRRETKQRKSGRSAGKFDVYYISP-CGKKLRSKSELArYLHKNGDL 56
 
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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