The domain within your query sequence starts at position 35 and ends at position 152; the E-value for the PTB domain shown below is 5e-44.

QYHVNHLVTFCLGEEDGVHTVEDASRKLAVMDSQGRVWAQEMLLRVSPSQVTLLDPVSKE
ELESYPLDAIVRCDAVMPRGRSRSLLLLVCQEPERAQPDVHFFQGLLLGAELIREDIQ

PTB

PTB
PFAM accession number:PF08416
Interpro abstract (IPR013625):

The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) of tensin tends to be found at the C terminus. Tensin is a multi-domain protein that binds to actin filaments and functions as a focal-adhesion molecule (focal adhesions are regions of plasma membrane through which cells attach to the extracellular matrix). Human tensin has actin-binding sites, an SH2 (IPR000980) domain and a region similar to the tumour suppressor PTEN [(PUBMED:11023826)]. The PTB domain interacts with the cytoplasmic tails of beta integrin by binding to an NPXY motif [(PUBMED:14592531)]. The PTB domain is also found in the epidermal growth factor receptor kinase substrate 8 (EPS8).

PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules [(PUBMED:10610414)]. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether [(PUBMED:11911882)]. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine [(PUBMED:11994738)]. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains [(PUBMED:15567406)].

GO function:protein binding (GO:0005515)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry PTB