Blast Analysis : gnl|CDD|197294

Analysis  rpsblast_cdd Start  229
End  413 Strand  +
Length  185 Note  Gaps:5
Hit Coverage  100.00 Hit Length  180
Hit Pident  68.89 E Val  2e-83
Hit Description  cd09198 PLDc_pPLDbeta_1 Catalytic domain repeat 1 of plant beta-type phospholipase D. Catalytic domain repeat 1 of plant beta-type phospholipase D (PLDbeta EC 3.1.4.4). Plant PLDbeta is a phosphatidylinositol 4 5-bisphosphate (PIP2)-dependent PLD that possesses a regulatory calcium-dependent phospholipid-binding C2 domain in the N-terminus and requires nanomolar calcium and cytosolic factors for optimal activity. The C2 domain is unique to plant PLDs and is not present in animal or fungal PLDs. Sequence analysis shows that plant PLDbeta is evolutionarily divergent from alpha-type plant PLD and plant PLDbeta is more closely related to mammalian and yeast PLDs than to plant PLDalpha. Like other PLD enzymes the monomer of plant PLDbeta consists of two catalytic domains each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. Plant PLDbeta may utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding a histidine residue from one HKD motif could function as the nucleophile attacking the phosphodiester bond to create a covalent phosphohistidine intermediate while the other histidine residue from the second HKD motif could serve as a general acid stabilizing the leaving group. Hit Pcons  13.33
Name  Qrob_P0173400.2
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1 Protein

Protein Identifier
Organism . Name 		Score Score Type Protein Description Alias (in v1) Code Enzyme Gene Prediction Quality
Qrob_P0173400.2 Quercus robur 0.0 egn (M=1) PF00168//PF00614//PF12357//PF13091 - C2 domain // Phospholipase D Active site motif // Phospholipase D C terminal // PLD-like domain   EC:3.1.4.4 validated