The domain within your query sequence starts at position 36 and ends at position 271; the E-value for the Alpha-amylase domain shown below is 1.4e-21.

WVDIAKECERYLAPNGFAGVQVSPPNENIVVHSPSRPWWERYQPISYKICSRSGNEDEFR
DMVNRCNNVGVRIYVDAVINHMCGVGAQAGQSSTCGSYFNPNNRDFPGVPYSGFDFNDGK
CRTASGGIENYQDAAQVRDCRLSGLLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDASK
HMWPGDIKAILDKLHNLNTKWFSQGSRPFIFQEVIDLGGEAVSSNEYFGNGRVTEF

Alpha-amylase

Alpha-amylase
PFAM accession number:PF00128
Interpro abstract (IPR006047):

O-Glycosyl hydrolases (EC 3.2.1.) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [(PUBMED:7624375), (PUBMED:8535779)]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site.

Enzymes containing this domain, such as alpha-amylase, belong to family 13 of the glycosyl hydrolases. The maltogenic alpha-amylase is an enzyme which catalyses hydrolysis of (1-4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains in the conversion of starch to maltose. Other enzymes include neopullulanase, which hydrolyses pullulan to panose, and cyclomaltodextrinase, which hydrolyses cyclodextrins.

This entry represents the catalytic domain found in several protein members of this family. It has a structure consisting of an 8 stranded alpha/beta barrel that contains the active site, interrupted by a ~70 amino acid calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain [(PUBMED:16302977)].

GO process:carbohydrate metabolic process (GO:0005975)
GO function:catalytic activity (GO:0003824)

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