Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyGlycosyl hydrolase domain-like 8034942 3001528 SCOP2B (2022-06-29)
ASCOP2B Superfamily(Trans)glycosidases 8034943 3000313 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ADUF1939e1ud3A1 A: beta sandwichesX: Glycosyl hydrolase domain-likeH: Glycosyl hydrolase domain (From Topology)T: Glycosyl hydrolase domainF: DUF1939ECOD (1.6)
AAlpha-amylasee1ud3A2 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: Alpha-amylaseECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.20.20.80 Alpha Beta Alpha-Beta Barrel TIM Barrel GlycosidasesCATH (4.3.0)
A2.40.30.140 Mainly Beta Beta Barrel Elongation Factor Tu (Ef-tu) domain 3CATH (4.3.0)
A2.60.40.1180 Mainly Beta Sandwich Immunoglobulin-like Golgi alpha-mannosidase IICATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF00128Alpha amylase, catalytic domain (Alpha-amylase)Alpha amylase, catalytic domainAlpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, a ...Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.
Domain
PF09154Alpha-amylase C-terminal (Alpha-amy_C_pro)Alpha-amylase C-terminalThis entry represents a C-terminal domain associated with prokaryotic alpha-amylases, which adopt a secondary structure consisting of an eight-stranded antiparallel beta-sheet containing a Greek key motif. Their exact function has not, as yet, been d ...This entry represents a C-terminal domain associated with prokaryotic alpha-amylases, which adopt a secondary structure consisting of an eight-stranded antiparallel beta-sheet containing a Greek key motif. Their exact function has not, as yet, been determined [1].
Domain