Summary: PepSY-associated TM helix
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PepSY-associated TM helix Provide feedback
This alignment represents a conserved TM helix found in family of bacterial proteins. The previous DUF337 alignment covered the whole (or most) of the protein. Analysis with dotter (E Sonnhammer) indicated that the same region was represented multiple times within the old alignment.
Internal database links
|Similarity to PfamA using HHSearch:||PepSY_TM_1 PepSY_TM_2 PepSY_TM_3|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR005625
This domain represents a conserved transmembrane (TM) helix that is found in bacterial proteins. Coil residues are significantly more conserved than other residues and are frequently found within channels and transporters, where they introduce the flexibility and polarity required for transport across the membrane [PUBMED:18511074].
This TM helix associates with PepSY (peptidase (M4) and YpeB of subtilis). PepSY is a repeated region first identified in Thermoanaerobacter tengcongensis. The PepSY domain functions in the control of M4 peptidases through their propeptide and in the germination of spores. It may also play a part in regulating protease activity [PUBMED:15124630].
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This example describes an architecture with one
Gladomain, followed by two consecutive
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Curation and family details
|Seed source:||Yeats C|
|Author:||Bateman A, Yeats C|
|Number in seed:||216|
|Number in full:||157|
|Average length of the domain:||35.30 aa|
|Average identity of full alignment:||47 %|
|Average coverage of the sequence by the domain:||13.52 %|
|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:||11|
|Download:||download the raw HMM for this family|
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