The domain within your query sequence starts at position 5 and ends at position 127; the E-value for the Tropomodulin domain shown below is 1e-19.
AKYRRQVSEDPDIDSLLSTLSPEEMEELEKELDVVDPDGSIPVGLRQRNQTDKQPSGSFN REAMLNFCEKESKKLIQREMSVDESKQVGRKTDAKNGEEKDSDASRKAPGPRQDSDLGKE PKK
Tropomodulin |
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PFAM accession number: | PF03250 |
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Interpro abstract (IPR004934): | Actin filaments have an intrinsic polarity, each with a fast-growing (barbed) end and a slow-growing (pointed) end. The slow-growing end is regulated by tropomodulins, a family of capping proteins that require tropomyosins for optimal function [ (PUBMED:19216712) ]. Tropomyosins contains two domains: an N-terminal unstructured tropomyosin-binding region which has an actin pointed-end-capping activity, an C-terminal region that contains one compact domain represented by alternating alpha-helices and beta-structures [ (PUBMED:19216712) ]. The tropomyosin-independent actin-capping site is located at the C terminus [ (PUBMED:19216712) ]. The structure of tropomyosin-1 has been solved [ (PUBMED:25061212) ]. Proteins in this entry include Tropomodulin (TMOD)-1/2/3/4 and Leiomodin (LMOD)-1/2/3. |
GO process: | pointed-end actin filament capping (GO:0051694) |
GO function: | tropomyosin binding (GO:0005523) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Tropomodulin