ID B8M0E6_TALSN Unreviewed; 567 AA.
AC B8M0E6;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Alpha-amylase, putative {ECO:0000313|EMBL:EED21243.1};
DE EC=3.2.1.98 {ECO:0000313|EMBL:EED21243.1};
GN ORFNames=TSTA_084740 {ECO:0000313|EMBL:EED21243.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED21243.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061}.
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DR EMBL; EQ962653; EED21243.1; -; Genomic_DNA.
DR RefSeq; XP_002478206.1; XM_002478161.1.
DR AlphaFoldDB; B8M0E6; -.
DR STRING; 441959.B8M0E6; -.
DR GeneID; 8106080; -.
DR VEuPathDB; FungiDB:TSTA_084740; -.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_024572_2_0_1; -.
DR InParanoid; B8M0E6; -.
DR OMA; CVVIMSN; -.
DR OrthoDB; 2728918at2759; -.
DR PhylomeDB; B8M0E6; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0033927; F:glucan 1,4-alpha-maltohexaosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11318; AmyAc_bac_fung_AmyA; 1.
DR Gene3D; 2.40.30.140; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013776; A-amylase_thermo.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PIRSF; PIRSF001021; Alph-amls_thrmst; 2.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000313|EMBL:EED21243.1};
KW Hydrolase {ECO:0000313|EMBL:EED21243.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT DOMAIN 44..424
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 567 AA; 64843 MW; 8947E290ACDC0D15 CRC64;
MDALLNCFLA FSKQKQNDWK ETEEQAQNIE KEPSWNSPED NICMLEAFEW YTPHDGRHWK
RLQQALPELK DIGIDNILLP PGCKAMNPSG NGYDIHDLYD LGEFDQKGTV ATKWGTKQDL
VTLAQLAEQL GIGIYWDAVL NHKAGADRKE RCLAVTVDPE DRNIDLTKPQ EIEAWVGFDF
SNRGETYSKM KYNWQHFNGT DYNDIDHKSA IYKIFAPGKD WAKDVSTENG NYDYLMFANL
DHSHPEVRED ILNWTNWIGA QLPLRGMRLD AVKHYSAEFQ KLLVDHVRRT RKEWFFVSEF
WSGDVLEIQE YLKRFDYKVY AFDAPLCQRL SAVSQTRGAD LRLVFEKTLV KCEPENAVTF
VMNHDTQPKQ ALEAPIPPSF KPLAYALILL RKDGYPCIFY GDLYGICSSV PAKMAKQKPM
TQSRIPKELQ GLPAMILARK LYAYGEQQDY FLQRNCVGFV RYGNARHPAG LACVMNNGLT
AINLRMHVGK RHAGERWSDV LLDNNQALGV EDLKNGKDNE KTGKIGKRRV VQISSKGYAD
FPVASMSVGV WVNEAAEGRE RFVGMNL
//
