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 6e-101.

YKTIMEQFNPSLRNFIAMGKNYEKALAGVTFAAKGYFDALVKMGELASESQGSKELGDVL
FQMAEVHRQIQNQLEETLKSFHNELLTQLEQKVELDSRYLSAALKKYQTEQRSKGDALDK
CQAELKKLRKKSQGSKNPQKYSDKELQYIDAISNKQGELENYVSDGYKTALTEERRRFCF
LVEKQCAVAKNSAAYHSKGKELLAQKLPLWQQACADPNKIP

IMD

IMD
PFAM accession number:PF08397
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:

  • Vertebrate MIM (missing in metastasis), an actin-binding scaffold protein that may be involved in cancer metastasis.
  • Vertebrate ABBA, a MIM-related protein.
  • Vertebrate insulin receptor tyrosine kinase substrate p53 (IRSp53), a multifunctional adaptor protein that links Rac1 with a Wiskott-Aldrich syndrome family verprolin-homologous protein 2 (WAVE2) to induce lamellipodia or Cdc42 with Mena to induce filopodia [(PUBMED:14980512)].
  • Vertebrate IRTKS.
  • Vertebrate Pinkbar.
  • Drosophila melanogaster (Fruit fly) CG32082-PA.
  • Caenorhabditis elegans M04F3.5 protein.

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