The domain within your query sequence starts at position 1061 and ends at position 1182; the E-value for the FABD domain shown below is 5.24e-65.

GTAGTKVALRKTKQAAEKISADKISKEALLECADLLSSAITEPVPNSQLVDTGHQLLDYC
SGYVDSIPQTRNKFAFREAVSKLELSLQELQVSSTAAGVPGTNPVLNNLLSCVQEISDVV
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FABD

F-actin binding domain (FABD)

• SMART accession number: SM00808
• Description: FABD is the F-actin binding domain of Bcr-Abl and its cellular counterpart c-Abl. The Bcr-Abl tyrosine kinase causes different forms of leukemia in humans. Depending on its position within the cell, Bcr-Abl differentially affects cellular growth. The FABD forms a compact left-handed four-helix bundle in solution.
• Interpro abstract (IPR015015):

  The F-actin binding domain forms a compact bundle of four antiparallel alpha-helices, which are arranged in a left-handed topology. Binding of F-actin to the F-actin binding domain may result in cytoplasmic retention and subcellular distribution of the protein, as well as possible inhibition of protein function [ (PUBMED:16109371) ]. Proteins containing this domain include tyrosine-protein kinases Abl1, which is a non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis [ (PUBMED:9037071) (PUBMED:11971963) ]. Abl1 is linked to different forms of leukemia in humans.

• GO process: protein phosphorylation (GO:0006468)
• GO function: ATP binding (GO:0005524), non-membrane spanning protein tyrosine kinase activity (GO:0004715)

There are 876 FABD domains in 876 proteins in SMART's nrdb database.

Cellular role (predicted cellular role)

Cellular role: interaction
Binding / catalysis: F-actin binding

Literature (relevant references for this domain)

Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

• Hantschel O et al.
• Structural basis for the cytoskeletal association of Bcr-Abl/c-Abl.
• Mol Cell. 2005; 19: 461-73

The Bcr-Abl tyrosine kinase causes different forms of leukemia in humans. Depending on its position within the cell, Bcr-Abl differentially affects cellular growth. However, no structural and molecular details for the anticipated localization determinants are available. We present the NMR structure of the F-actin binding domain (FABD) of Bcr-Abl and its cellular counterpart c-Abl. The FABD forms a compact left-handed four-helix bundle in solution. We show that the nuclear export signal (NES) previously reported in this region is part of the hydrophobic core and nonfunctional in the intact protein. In contrast, we could identify the critical residues of helix alphaIII that are responsible for F-actin binding and cytoskeletal association. We propose that these interactions represent a major determinant for both Bcr-Abl and c-Abl localization.

Metabolism (metabolic pathways involving proteins which contain this domain)

% proteins involved	KEGG pathway ID	Description
36.17	map04012	ErbB signaling pathway
21.28	map05220	Chronic myeloid leukemia
21.28	map04360	Axon guidance
21.28	map04110	Cell cycle

This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with FABD domain which could be assigned to a KEGG orthologous group, and not all proteins containing FABD domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.

Structure (3D structures containing this domain)

3D Structures of FABD domains in PDB

PDB code	Title
1zzp	Solution structure of the F-actin binding domain of Bcr-Abl/c-Abl
2kk1	Solution structure of C-terminal Domain of Tyrosine-protein kinase ABL2 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) target HR5537A

Links (links to other resources describing this domain)

• INTERPRO: IPR015015