The domain within your query sequence starts at position 17 and ends at position 237; the E-value for the IMD domain shown below is 1.6e-98.
YKTIMEQFNPSLRNFIAMGKNYEKALAGVTFAAKGYFDALVKMGELASESQGSKELGDVL FQMAEVHRQIQNQLEETLKSFHNELLTQLEQKVELDSRYLSAALKKYQTEQRSKGDALDK CQAELKKLRKKSQGSKNPQKYSDKELQYIDAISNKQGELENYVSDGYKTALTEERRRFCF LVEKQCAVAKNSAAYHSKGKELLAQKLPLWQQACADPNKIP
IMD |
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PFAM accession number: | PF08397 |
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Interpro abstract (IPR013606): | The I-BAR domain (also known as IMD domain, IRSp53 and MIM homology domain) is a BAR-like domain of approximately 250 amino acids found at the N-terminal in the IRSp53 (insulin receptor tyrosine kinase substrate p53) and in the evolutionarily related IRSp53/MIM family. The BAR domain forms an anti-parallel all-helical dimer, with a curved (banana-like) shape, that promotes membrane tubulation. The BAR domain containing proteins can be classified into three types: BAR, F-BAR and I-BAR. BAR and F-BAR proteins generate positive membrane curvature, while I-BAR proteins induce negative curvature [ (PUBMED:21743456) (PUBMED:21093245) ]. The I-BAR domain containing proteins include:
The vertebrate I-BAR family is divided into two major groups: the IRSp53/IRTKS/Pinkbar subfamily and the MIM/ABBA subfamily. The putative invertebrate homologues are positioned between them. The IRSp53/IRTKS/Pinkbar subfamily members contain a SH3 domain, and the MIM/ABBA subfamily proteins contain a WH2 (WASP-homology 2) domain. The vertebrate SH3-containing subfamily is further divided into three groups according to the presence or absence of the WWB and the half-CRIB motif [ (PUBMED:14752106) (PUBMED:17497115) ]. The BAR domain binds phosphoinositide-rich vesicles with high affinity and does not display strong actin filament binding/bundling activity [ (PUBMED:21093245) (PUBMED:17371834) ]. |
GO process: | plasma membrane organization (GO:0007009) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry IMD