ID M5BY25_THACB Unreviewed; 260 AA.
AC M5BY25;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:CCO32543.1};
DE EC=3.2.1.1 {ECO:0000313|EMBL:CCO32543.1};
GN Name=amy {ECO:0000313|EMBL:CCO32543.1};
GN ORFNames=BN14_06604 {ECO:0000313|EMBL:CCO32543.1};
OS Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS rot fungus) (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=1108050 {ECO:0000313|EMBL:CCO32543.1, ECO:0000313|Proteomes:UP000012065};
RN [1] {ECO:0000313|EMBL:CCO32543.1, ECO:0000313|Proteomes:UP000012065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG1-IB / isolate 7/3/14 {ECO:0000313|Proteomes:UP000012065};
RX PubMed=23280342; DOI=10.1016/j.jbiotec.2012.12.010;
RA Wibberg D.W., Jelonek L.J., Rupp O.R., Hennig M.H., Eikmeyer F.E.,
RA Goesmann A.G., Hartmann A.H., Borriss R.B., Grosch R.G., Puehler A.P.,
RA Schlueter A.S.;
RT "Establishment and interpretation of the genome sequence of the
RT phytopathogenic fungus Rhizoctonia solani AG1-IB isolate 7/3/14.";
RL J. Biotechnol. 0:0-0(2013).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCO32543.1}.
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DR EMBL; CAOJ01010011; CCO32543.1; -; Genomic_DNA.
DR AlphaFoldDB; M5BY25; -.
DR HOGENOM; CLU_082761_0_0_1; -.
DR Proteomes; UP000012065; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR15048; STARCH-BINDING DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR15048:SF0; STARCH-BINDING DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR Pfam; PF00686; CBM_20; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000313|EMBL:CCO32543.1};
KW Hydrolase {ECO:0000313|EMBL:CCO32543.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326}.
FT DOMAIN 160..260
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT REGION 238..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 260 AA; 27110 MW; F3AC112B8F3E910F CRC64;
MLAHPYGTPT VLSSYSFADH DTGSPSSGAG SCSGAGGSNG WICQHRWAAI AGMVQWRNGV
TGGINHWVSG TQQQIAFGRG ASGFVAINNE GVAWTMTFET NLPDNSYCDM VSGVAGAEGT
CTGASYIVSR KKLTAKIPPR SAIALFPGAV GIGSSGGDGG SSVVDIPVSF RASVETNADE
NLFVVGSIPQ LGNWAPSNAI AMSSSSLPTW NVNVTILAET EFYYKYIRKT SNGSVIWESD
PNRSAVTPPS GSLTLDDTWR
//
