Blast Analysis : gnl|CDD|189021

Analysis  rpsblast_cdd Start  67
End  119 Strand  +
Length  53 Note  none
Hit Coverage  44.17 Hit Length  120
Hit Pident  54.72 E Val  4e-17
Hit Description  cd08553 PIN_Fcf1-like PIN domain of rRNA-processing proteins Fcf1 (Utp24 YDR339C) Utp23 (YOR004W) and other eukaryotic homologs. Fcf1 (FAF1-copurifying factor 1 also known as Utp24) and Utp23 (U three-associated protein 23) are essential proteins involved in pre-rRNA processing and 40S ribosomal subunit assembly. Components of the small subunit (SSU) processome Fcf1 and Utp23 are essential nucleolar proteins that are required for processing of the 18S pre-rRNA at sites A0-A2. The Fcf1 protein was reported to interact with Pmc1p (vacuolar Ca2+ ATPase) and Cor1p (core subunit of the ubiquinol-cytochrome c reductase complex). The PIN (PilT N terminus) domains of these proteins are homologs of flap endonuclease-1 (FEN1)-like PIN domains but apparently lack the H3TH domain or extensive arch/clamp region seen in the latter. PIN domains typically contain three or four conserved acidic residues (putative metal-binding active site residues). The Fcf1 PIN domain subfamily has four of these putative active site residues. Point mutation studies showed that the conserved acidic residues in the putative active site of Saccharomyces cerevisiae Fcf1 are essential for pre-rRNA processing at sites A1 and A2 whereas the presence of the Fcf1 protein itself is also required for cleavage at site A0. S. cerevisiae Utp23 lacks several of these key residues and mutation of the conserved acidic residues seen in Utp23 did not interfere with rRNA maturation and cell viability. The subfamily of Fcf1- and Utp23-like homologs found in eukaryotes (except fungi) posses three of the four conserved residues seen in S. cerevisiae Fcf1. Hit Pcons  16.98
Name  Qrob_P0379590.2

1 Protein

Protein Identifier
Organism . Name
Score Score Type Protein Description Alias (in v1) Code Enzyme Gene Prediction Quality
Qrob_P0379590.2 Quercus robur 100.0 egn (M=1) K14566 - U3 small nucleolar RNA-associated protein 24     validated