The domain within your query sequence starts at position 61 and ends at position 165; the E-value for the Rotamase domain shown below is 1.4e-25.
HLLVKHSQSRRPSSWRQEKITRSKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKA RGDLGPFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE
Rotamase |
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PFAM accession number: | PF00639 |
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Interpro abstract (IPR000297): | Peptidyl-prolyl cis-trans isomerase ( EC 5.2.1.8 ) (PPIase or rotamase) is an enzyme that accelerates protein folding by catalysing the cis-trans isomerisation of proline imidic peptide bonds in oligopeptides [ (PUBMED:2186809) ]. Most characterised PPiases belong to two families, the cyclophilin-type and the the FKBP-type. A third family has been discovered [ (PUBMED:7925971) ]. So far, the only biochemically characterised member of this family is the Escherichia coli protein parvulin (gene ppiC), a small (92 residues) cytoplasmic enzyme that prefers amino acid residues with hydrophobic side chains like leucine and phenylalanine in the P1 position of the peptides substrates. This entry represents a conserved region that contains a serine which could play a role in the catalytic mechanism of these enzymes. |
GO function: | peptidyl-prolyl cis-trans isomerase activity (GO:0003755) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Rotamase