The domain within your query sequence starts at position 250 and ends at position 349; the E-value for the RVP domain shown below is 2.5e-8.
LYINCKVNGHPLKAFVDSGAQMTIMSQACAERCNIMRLVDRRWGGVAKGVGTQRIMGRVH LAQIQIEGDFLQCSFSILEEQPMDILLGLDMLRRHQCSID
RVP |
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PFAM accession number: | PF00077 |
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Interpro abstract (IPR018061): | Aspartic peptidases, also known as aspartyl proteases ([intenz:3.4.23.-]), are widely distributed proteolytic enzymes [ (PUBMED:6795036) (PUBMED:2194475) (PUBMED:1851433) ] known to exist in vertebrates, fungi, plants, protozoa, bacteria, archaea, retroviruses and some plant viruses. All known aspartic peptidases are endopeptidases. A water molecule, activated by two aspartic acid residues, acts as the nucleophile in catalysis. Aspartic peptidases can be grouped into five clans, each of which shows a unique structural fold [ (PUBMED:8439290) ].
This group of aspartic peptidases belong to the peptidase clan AA. The clan includes the single domain aspartic proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses) which are active as homodimers. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin [ (PUBMED:1851433) (PUBMED:8841139) ]. Family A2 includes the peptidase (retropepsin, EC 3.4.23.16) from the human immunodeficiency virus and other retroviruses. In most retroviruses, the peptidase is encoded as a segment of a polyprotein (usually the pol polyprotein, which includes the peptidase, a reverse transcriptase, RNase H and an integrase, but occassionally the gag polyprotein) which it cleaves during viral maturation to release individual proteins. Some retrotransposon polyproteins also contain a homologous, retropepsin-like peptidase which is also a member of family A2. Family A3 includes peptidases from the double-stranded DNA plant viruses known as badnaviruses or pararetroviruses. The viral genome includes genes (ORFs IV and V) that encodes polyproteins. The ORF V polyprotein contains the peptidase and a reverse transcriptase. The peptidase processes the ORF IV polyprotein, which includes the viral coat protein [ (PUBMED:15831103) ]. Family A9 includes peptidases from spumaretroviruses, and the peptidase is a component of either the gag and pol polyprotein, which is processes [ (PUBMED:9311808) ]. The structure has been solved for the peptidase from simian foamy virus and shows a retropepsin-like fold [ (PUBMED:18597783) ]. Family A11 includes polyprotein-processing peptidases from retrotransposons such as the copia transposon from Drosophila melanogaster . No tertiary structure has been solved for any member of the family, and family A11 is included in clan AA on the basis of the similar motif around the active site Asp. Family A28 includes the yeast DNA-damage inducible protein 1 which is a component of the DNA repair pathway. The tertiary structure shows a retropepsin-like fold [ (PUBMED:17010377) ]. This peptidase is not a component of a polyprotein. Family A32 includes the bacterial PerP peptidase which converts the transmembrane factor PodJ from a form that recruits proteins for pilus formation, to a truncated form that recruits proteins for stalk formation. This converts the bacterium from a motile form to the sessile form found in biofilms [ (PUBMED:16395329) ]. |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry RVP