Conserved Protein Domain Family
ePHD_ATX1_2_like
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cd15662: ePHD_ATX1_2_like 
Extended PHD finger found in Arabidopsis thaliana ATX1, -2, and similar proteins
The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This subfamily includes the ePHD finger of A. thaliana histone-lysine N-methyltransferase arabidopsis trithorax-like proteins ATX1, -2, and similar proteins. ATX1 and -2 are sister paralogs originating from a segmental chromosomal duplication; they are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1 (also known as protein SET domain group 27, or trithorax-homolog protein 1/TRX-homolog protein 1), is a methyltransferase that trimethylates histone H3 at lysine 4 (H3K4me3). It also acts as a histone modifier and as a positive effector of gene expression. ATX1 regulates transcription from diverse classes of genes implicated in biotic and abiotic stress responses. It is involved in dehydration stress signaling in both abscisic acid (ABA)-dependent and ABA-independent pathways. ATX2 (also known as protein SET domain group 30, or trithorax-homolog protein 2/TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). ATX1 and ATX2 are multi-domain proteins that consist of an N-terminal PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical PHD finger, this non-canonical ePHD finger, and a C-terminal SET domain.
Links
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Statistics
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PSSM-Id: 277132
Aligned: 6 rows
Threshold Bit Score: 178.437
Created: 23-Jul-2014
Updated: 2-Oct-2020
Structure
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Aligned Rows:
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Zn binding siteputative
Feature 1: Zn binding site [ion binding site], 12 residue positions
Conserved feature residue pattern:C C H C C C C C H C C HClick to see conserved feature residue pattern help
Evidence:
  • Comment:based on the structure evidence that human Borjeson-Forssman-Lehmann syndrome-associated protein PHF6 (PDB 4NN2) binds three Zn2+ ions through its ePHD finger
  • Comment:The extended PHD finger is characterized by Cys2HisCys5HisCys2His.
Scroll to Sequence Alignment Display
Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1         #  #                  #  #                                  #  #         #     #
Q9C5X4        668 CCLCPVVGGAMKPtt--dGRWAHLACAIWIPEtclsdvkkMEPIDgvnk--vskdRWKLMCTICGVsYGACIQCsn-nsC 742  thale cress
XP_001780587  501 CCLCPVTSGALKKtt--dGRWAHLMCAMWIPEtclvdvkrMEPVDgina--iskeRWRLTCSICNVpYGACIRCsv-nsC 575  Physcomitrell...
EIE26040      453 CALCPVEGGLLKRtt--cGRWVHSACTLWVPEtai--dcdVGLVDglqyipkachRLPLSCAVCSQaYGACIQCaghrsC 528  Coccomyxa sp....
CCO17344      853 CCLCPVIGGALKPtt-vdGVWAHSACCQWIPEttvldietMEPIDniaa--iqreRWELLCTICKQrCGTKVQCch-pgC 928  Bathycoccus p...
XP_001703016  857 CCLCPVAGGALKPttlgpGTWAHMVCLNWLPEltcgdpitGEPVDnipg--iqreRWELSCCICKQrMGAKIQCa---lC 931  Chlamydomonas...
P0CB22        685 CCLCPVVGGAMKPtt--dGRWAHLACAIWIPEtclldvkkMEPIDgvkk--vskdRWKLLCSICGVsYGACIQCsn-ntC 759  thale cress

Feature 1             #  #                                   #  #
Q9C5X4        743 RVAYHPLCARAAGLCVelendmsv-----egeeadqcIRMLSFCKRH 784  thale cress
XP_001780587  576 KTAFHPLCARSAGLYMevleekl-------qvngetdLRLLSYCRKH 615  Physcomitrella patens subsp. patens
EIE26040      529 CASFHPLCARAAGLCMrvwreg---------talsagLRLMCYCPRH 566  Coccomyxa sp. C-169
CCO17344      929 FLAYHPLCARGAGLFMdqgdeygna----dedpeddtMHLISYCHRH 971  Bathycoccus prasinos
XP_001703016  932 YQAYHPLCGRMAGLHMevava-----------pggkgLKRTNFCPRH 967  Chlamydomonas reinhardtii
P0CB22        760 RVAYHPLCARAAGLCVeladedrlfllsmdddeadqcIRLLSFCKRH 806  thale cress

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