2DIQ,2DIG,2EQU,2FHD,2GF7,2GF7,2MAM,2MAM,4GY5,4GY5,4II1,4RG2,5XFR,6BHH,2FHD,3MEU,3MEU,3KUF,3KUF,6IE4,6IE4,6BHH,2LTO,2IG0


Conserved Protein Domain Family
Tudor_SF

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cd04508: Tudor_SF 
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Tudor domain superfamily
The Tudor domain is a conserved structural domain, originally identified in the Tudor protein of Drosophila, that adopts a beta-barrel-like core structure containing four short beta-strands followed by an alpha-helical region. It binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Tudor domain-containing proteins may mediate protein-protein interactions required for various DNA-templated biological processes, such as RNA metabolism, as well as histone modification and the DNA damage response. Members of this superfamily contain one or more copies of the Tudor domain.
Statistics
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PSSM-Id: 410449
View PSSM: cd04508
Aligned: 81 rows
Threshold Bit Score: 27.1654
Threshold Setting Gi: 283135389
Created: 12-Dec-2003
Updated: 17-Aug-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
putative
Conserved site includes 6 residues -Click on image for an interactive view with Cn3D
Feature 1:putative peptide binding site [polypeptide binding site]
Evidence:
  • Comment:In general, the Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
  • Structure:4GY5; Homo sapiens UHRF1 in complex with Histone H3k9me3, contacts at 4A
    View structure with Cn3D
  • Structure:2LTO; Homo sapiens TDRD3 in complex with DNA-directed RNA polymerase II subunit Rpb1 asymmetrically dimethylated CTD peptide, contacts at 4A
    View structure with Cn3D
  • Structure:2IG0; Homo sapiens 53BP1 in complex with dimethylated histone H4-k20 peptide, contacts at 4A
    View structure with Cn3D
  • Structure:3MEU: Human Saga-associated factor 29 homolog in complex with histone H3 peptide; contacts at 4A
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                #         # #                                   #     # #             
2DIQ_A         36 GDIVAAPLpt-----ngSWYRARVLGtle-------------------ngNLDLYFv---dFGDNGDCpl--kDLRA 83   human
2FHD_A         67 GDVVQSTRl--------GKIKHTVVKtfrstneqls----liavdalnndXVILAH-----GEIEVTVpi--sTIYV 124  fission yeast
4GY5_A         95 GQVVMLNYnpdnpkergFWYDAEISRkret----------------rtarELYANVvlgddSLNDCRIif-vdEVFK 154  human
4GY5_A         13 NEYVDARDtn-----mgAWFEAQVVRvtrkapsrdepcsstsrpaleedvIYHVKYdd-ypENGVVQMns--rDVRA 81   human
3MEU_A         46 GDKVAARVkavd--gdeQWILAEVVSysh------------------atnKYEVDDid-eeGKERHTLsr--rRVIP 99   human
OAO13180      219 GDSVMGFYgv-----dlMWYPARVLRvls-------------------pnSYYLVYd---gYNNKEVRtr--gHVLM 266  Blastocystis sp....
XP_010069758  100 DDSVEAKWr-------nGWRHGIVKMvme-------------------gsRYCVCI-----DGEGEDAvyegsDLRE 145  Eucalyptus grandis
GBF88129      195 GTCVEVFWpd-----dgQWWPATVLGada------------------atrRLQLLYd----TLQEEEItgpdfDSLI 244  Raphidocelis sub...
XP_002505857   23 NAQIELFWpd-----dgMWYKAEVVSlnt------------------rnrSAKVLYa----TGDVETLsi-deIAQE 71   Micromonas commoda
F4JYC8         46 GCYMLKDFdd------nEVFLGKIVSyd--------------------tgLYRVIYe----DGDCEELes--gDLRR 90   thale cress

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