The domain within your query sequence starts at position 13 and ends at position 144; the E-value for the TPMT domain shown below is 4.6e-8.

SADYWEKFFQQRGKTAFEWYGTYLELCEVLHKYIKPKEKVLVIGCGNSELSEQLYDVGYQ
DIVNIDISEVVIKQMKERNGSRRPHMSFLKMDMTQLEFPDATFQVVLDKGTLDAVLTDEE
EVTLRQVDRMLA

TPMT

TPMT
PFAM accession number:PF05724
Interpro abstract (IPR008854):

This family consists of thiopurine S-methyltransferase ( EC 2.1.1.67 ), thiol S-methyltransferase ( EC 2.1.1.9 ) and thiocyanate methyltransferase ( EC 2.1.1.n4 ).

Thiopurine S-methyltransferase is a cytosolic enzyme that catalyses S-methylation of aromatic and heterocyclic sulphydryl compounds, including anticancer and immunosuppressive thiopurines [ (PUBMED:9780226) ]. Thiopurine is commonly used to suppress the immune system in the case of autoimmune disease, inflammatory bowel disease and to prevent transplanted organ rejection [ (PUBMED:16207256) ]. Thiopurine drugs can be toxic to cells but their effect can be mediated by the incorporation of thioguanine nucleotides into DNA [ (PUBMED:15570193) ].

Thiocyanate methyltransferase and thiol S-methyltransferase are involved in glucosinolate metabolism and defense against phytopathogens. Thiocyanate methyltransferase is highly reactive to thiocyanate (NCS-) derived from myrosinase-mediated hydrolysis of glucosinolates upon tissue damage [ (PUBMED:19419967) ].

GO function:S-adenosylmethionine-dependent methyltransferase activity (GO:0008757)

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