Summary: Putative snoRNA binding domain
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Putative snoRNA binding domain Provide feedback
This family consists of various Pre RNA processing ribonucleoproteins. The function of the aligned region is unknown however it may be a common RNA or snoRNA or Nop1p binding domain. Nop5p (Nop58p) Q12499 from yeast is the protein component of a ribonucleoprotein protein required for pre-18s rRNA processing and is suggested to function with Nop1p in a snoRNA complex . Nop56p O00567 and Nop5p interact with Nop1p and are required for ribosome biogenesis . Prp31p p49704 is required for pre-mRNA splicing in S. cerevisiae .
Wu P, Brockenbrough JS, Metcalfe AC, Chen S, Aris JP; , J Biol Chem 1998;273:16453-16463.: Nop5p is a small nucleolar ribonucleoprotein component required for pre- 18 S rRNA processing in yeast. PUBMED:9632712 EPMC:9632712
Gautier T, Berges T, Tollervey D, Hurt E; , Mol Cell Biol 1997;17:7088-7098.: Nucleolar KKE/D repeat proteins Nop56p and Nop58p interact with Nop1p and are required for ribosome biogenesis. PUBMED:9372940 EPMC:9372940
Weidenhammer EM, Singh M, Ruiz-Noriega M, Woolford JL Jr; , Nucleic Acids Res. 1996;24:1164-1170.: The PRP31 gene encodes a novel protein required for pre-mRNA splicing in Saccharomyces cerevisiae. PUBMED:8604353 EPMC:8604353
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002687This domain is present in various pre-mRNA processing ribonucleoproteins. The function of the domain is unknown however it may be a common RNA or snoRNA or Nop1p binding domain.
Proteins have been implicated in an expanding variety of functions during pre-mRNA splicing. Molecular cloning has identified genes encoding spliceosomal proteins that potentially act as novel RNA helicases, GTPases, or protein isomerases. Novel protein-protein and protein-RNA interactions that are required for functional spliceosome formation have also been described. Finally, growing evidence suggests that proteins may contribute directly to the spliceosome's active sites [PUBMED:9159080].
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We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_1362 (release 4.2)|
|Author:||Bashton M, Bateman A|
|Number in seed:||16|
|Number in full:||1302|
|Average length of the domain:||145.10 aa|
|Average identity of full alignment:||41 %|
|Average coverage of the sequence by the domain:||29.75 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Nop domain has been found. There are 30 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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