Conserved Protein Domain Family
PHD1_MORF

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cd15689: PHD1_MORF 
PHD finger 1 found in monocytic leukemia zinc finger protein-related factor (MORF)
MORF, also termed MOZ2, or histone acetyltransferase KAT6B, or MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4 (MYST4), is a ubiquitously expressed transcriptional regulator with intrinsic histone acetyltransferase (HAT) activity. It can interact with the Runt-domain transcription factor Runx2 and form a tetrameric complex with BRPFs, ING5, and EAF6. MORF and monocytic leukemia zinc-finger protein (MOZ) are catalytic subunits of HAT complexes that are required for normal developmental programs, such as hematopoiesis, neurogenesis, and skeletogenesis, and are also implicated in human leukemias. MORF contains an N-terminal region containing two plant homeodomain (PHD) fingers, a putative HAT domain, an acidic region, and a C-terminal Ser/Met-rich domain. The model corresponds to the first PHD finger.
Statistics
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PSSM-Id: 277159
Aligned: 3 rows
Threshold Bit Score: 122.84
Created: 21-Mar-2014
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
Feature 1: Zn binding site [ion binding site], 8 residue positions
Conserved feature residue pattern:C C C C H C C CClick to see conserved feature residue pattern help
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1          #  #                 #  #    #  #                 #  # 
Q8WYB5     212 PIPICSFCLGTKESNREKKPEELLSCADCGSSGHPSCLKFCPELTTNVKALRWQCIECK 270  human
XP_421609  212 PIPICSFCLGTKESNREKKPEELLSCADCGSSGHPSCLKFCPELTSNVKALRWQCIECK 270  chicken
XP_697383  212 PIPICSFCLGTKESNRDKRPEELLSCADCGSSGHPSCLKFSADLTANVKALRWQCIECK 270  zebrafish

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