ID   F2TUD5_AJEDA            Unreviewed;       538 AA.
AC   F2TUD5;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Alpha-amylase {ECO:0000313|EMBL:EGE86848.1};
GN   ORFNames=BDDG_09798 {ECO:0000313|EMBL:EGE86848.1};
OS   Ajellomyces dermatitidis (strain ATCC 18188 / CBS 674.68) (Blastomyces
OS   dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=653446 {ECO:0000313|EMBL:EGE86848.1};
RN   [1] {ECO:0000313|EMBL:EGE86848.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18188 {ECO:0000313|EMBL:EGE86848.1};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Genome Sequencing Center for Infectious Disease.;
RA   Cuomo C., Klein B., Sullivan T., Heitman J., Young S., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A.M., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "Annotation of Blastomyces dermatitidis strain ATCC 18188.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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; GG749789; EGE86848.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2TUD5; -.
DR   HOGENOM; CLU_024572_2_0_1; -.
DR   Proteomes; UP000007802; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          36..425
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   538 AA;  61736 MW;  6E40144B9C88DEBF CRC64;
     MGSLISSAYQ YIFRKRETQW LDIDDFNPDE SGEQNQLMLQ AFEWYVPDDQ KHWRRLLAAL
     PSLKAIGVTS IWLPPGCKAM SPSGNGYDIY DLYDLGEFDQ KGSRATKWGT KEELVALVKR
     AHEMEIAVIW DTVLNHKAAA DHTERCVAVR VNPKDRRKII SEPEEIEAWL GFSFPGRGTR
     YSKMKYHWYH FTGVDYNARN KKTGIYKIMG PDTKDWARDV SKENGNYDYL MFANLDYSHP
     EVREDVLKWI QWIGDQLPIA GLRLDAVKHY SAGFLKEFIG HVQRTVGPGW FLVAEYWKVE
     VRELLEYLGR MDYLVSLFDA PLVHRFSQIS RTAGADLRRV FEGTLVKHEQ KHAVTFVMNH
     DTQPSQSLEE PIEDFFKPLA YALILLRKEG HPCLFYGDLY GMCGGCQGIL KPSCNDRLAD
     LALARKLYAY GRQRDYFDKR NCIGFVRLGD SAHPDGLACV LSNGPADTKR MYVGKAHAGS
     VWTEVYGYCR SRVKIDSRGY GVFGVVSRNV SVWVREDAMG RESFGKFDSD IYSYLVTD
//