4NW2,2B2U,2B2U,4O9I,5O9G


Conserved Protein Domain Family
CD1_tandem

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cd18660: CD1_tandem 
Click on image for an interactive view with Cn3D
repeat 1 of paired tandem chromodomains
Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 to CHD9, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.
Statistics
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PSSM-Id: 349307
Aligned: 36 rows
Threshold Bit Score: 61.6078
Created: 3-Oct-2017
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
peptide bindingDNA binding
Conserved site includes 5 residues -Click on image for an interactive view with Cn3D
Feature 1:peptide binding site [polypeptide binding site]
Evidence:
  • Structure:2B2U; human CHD1 tandem chromodomains complexed with histone H3 tail containing trimethyllysine 4 and dimethylarginine 2, contacts at 4A
  • Comment:human CHD1 uses 2 aromatic residues (tryptophans) for methyllysine recognition

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1        #                                                 # ##   #                    
4NW2_A      21 EFETIERFMDCRIgrkgatgatttiyaveadgdpnagfeknkepgEIQYLIKWKGWsHIHNTWETEETLKqqn---vrGM 97   human
2B2U_A      12 EFETIERFMDCRIgrkgatgatttiyaveadgdpnagfeknkepgEIQYLIKWKGWsHIHNTWETEETLKqqn---vrGM 88   human
ETO15326   233 VQLEIDKIIWRKSlkdav-----------------------tgldDYEYYVLWKGLsHLHCEWVSQKTIEqd----pnGA 285  Reticulomyxa filosa
6318930     96 PLNEIDKILDCEMrptksseqgs-------------sdaepkpifVKQYLVKWKGLsYLHCSWVPEKEFQkayksnhrLK 162  thale cress
EKX50105   198 CKYNIDKILGMEMkkqlse--------------------nneeieVALFLVKWREKsYLHTSWVTENDILae-----gGK 252  Guillardia theta...
GAQ80045   233 RLANMEKIIDWRVvtdrlgadnq-------------lgsprstkkRKEYLLKWKGQsHLHASWVPIEEVEeaaqyllgLR 299  Klebsormidium ni...
KZL76196   662 VSDKIQTLVAWRPsekksldsg--------------ktysdlnedEKEYLIKWQGKsYFHCTWMPGAWVFhi-----aAG 722  Colletotrichum t...
EFA77978   271 EEFTVEKVLDTRMqgdd------------------------aanqMEQVLVKWKGLsYLHCSWVDSNQLIqt----rsGK 322  Polysphondylium ...
CDS03286   442 FNKKVEKIVTWRIagepadkrld-------------itfndaskeTKEYLVKWVDTsYCHLTWVPEEWIMr------tSK 502  Lichtheimia ramosa
Q8TD26     290 DANIIEKILASKTvqevhp--------------------geppfdLELFYVKYRNFsYLHCKWATMEELEkd----prIA 345  human
Feature 1              
4NW2_A      98 KKLDNYKK 105  human
2B2U_A      89 KKLDNYKK 96   human
ETO15326   286 KKLKNFLK 293  Reticulomyxa filosa
6318930    163 TRVNNFHR 170  thale cress
EKX50105   253 VRLNNFMS 260  Guillardia theta CCMP2712
GAQ80045   300 AKLRNFQN 307  Klebsormidium nitens
KZL76196   723 NMRTSFAK 730  Colletotrichum tofieldiae
EFA77978   323 ARLQRYQQ 330  Polysphondylium pallidum PN500
CDS03286   503 QLYSKYCE 510  Lichtheimia ramosa
Q8TD26     346 QKIKRFRN 353  human

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