5B76,6VFO,5V9P,1F62,6J2P,1WE9,4L7X,5Z8L,5TDR,2YT5,5XFQ,5U2J,3O35,2KE1


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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PSSM-Id: 425785
Aligned: 71 rows
Threshold Bit Score: 39.7828
Created: 21-Mar-2022
Updated: 17-Oct-2022
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:
5B76_A         16 ICsFCLGtkeqnrekkPEELISCADCGNSGHPSCLKFSPEltVRVKAl------RWQCIECKTC 73   human
Q9ZUA9        637 DCkCGARdd------dGERMVACDACKVWHHTLCNSIEDDeaVPSV---------FLCNMCYGD 685  thale cress
O74508        120 YC-ICQKpd------dGSWMLGCDGCEDWFHGTCVNIPESynDLTV--------QYFCPKCTEE 168  Schizosaccharomyces pombe 972h-
6J2P_C         27 YC-ICKRpd------yGELMVGCDGCDDWFHFTCLHIPEQfkDLVF--------SFYCPYCQAG 75   Saccharomyces cerevisiae S288C
Q92576        719 QCgFCKKph------gNRFMVGCGRCDDWFHGDCVGLSLSqaQQMGEed----kEYVCVKCCAE 772  human
1WE9_A          8 QCgACGEsy-----aaDEFWICCDLCEMWFHGKCVKITPAraEHIK--------QYKCPSCSNK 58   thale cress
XP_015691563  175 LCgTCGTnd-----gkDEFWICCDNCEKWYHGKCVKITPAraEHIK--------QYKCPDCTNK 225 
4L7X_A          8 YC-ICRQph------nNRFMICCDRCEEWFHGDCVGISEArgRLLERng----eDYICPNCTIL 60   human
Q03214       1240 YC-FCRRve------eGTAMVECEICKEWYHVDCISNGELvpPDDPNv------LFVCSICTPP 1290 Saccharomyces cerevisiae S288C
P29375       1163 FC-ICRKt-------aSGFMLQCELCKDWFHNSCVPLPKSssQKKGSswqakevKFLCPLCMRS 1218 human
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