1F62,4BXZ,4QF3,5XFR,1XWH,2RO1,5XFQ,1WEM,5TDR,4LJN


Conserved Protein Domain Family
PHD

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pfam00628: PHD 
Click on image for an interactive view with Cn3D
PHD-finger
PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains. Several PHD fingers have been identified as binding modules of methylated histone H3.
Statistics
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Aligned: 82 rows
Threshold Bit Score: 44.7913
Threshold Setting Gi: 119611838
Created: 23-Apr-2019
Updated: 18-Jul-2019
Structure
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Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
1F62_A          2 RCkVCRKkg-eDDKLILCDECNKAFHLFCLRPALy--EVPD---G-------EWQCPACQPA 50   human
P29375       1163 FC-ICRKt--aSGFMLQCELCKDWFHNSCVPLPKsssQKKG---SswqakevKFLCPLCMRS 1218 human
EAW91432     1020 IC-LCQKa--pAAPMIQCELCRDAFHTSCVAVPSisqGLRI------------WLCPHCRRs 1066 human
O74508        120 YC-ICQKpd-dGSWMLGCDGCEDWFHGTCVNIPEsynDLTV-----------QYFCPKCTEE 168  Schizosaccharomyces pombe 972h-
Q03012         24 YC-ICKRpd-yGELMVGCDGCDDWFHFTCLHIPEqfkDLVF-----------SFYCPYCQAG 72   Saccharomyces cerevisiae S288C
Q92576        719 QCgFCKKph-gNRFMVGCGRCDDWFHGDCVGLSLsqaQQMG---Eed----kEYVCVKCCAE 772  human
O81488        201 QCgACGEsyaaDEFWICCDLCEMWFHGKCVKITParaEHIK-----------QYKCPSCSNK 251  thale cress
XP_015691563  175 lCgTCGTndgkDEFWICCDNCEKWYHGKCVKITParaEHIK-----------QYKCPDCTNK 225  malo sina
Q9BTC0        270 YC-ICRQph-nNRFMICCDRCEEWFHGDCVGISEargRLLE---Rng----eDYICPNCTIL 322  human
1WEM_A         17 lycICRQph-nNRFMICCDRCEEWFHGDCVGISEargRLLErngE-------DYICPNCTil 70   house mouse
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