ID   A0A2S5B2L6_9BASI        Unreviewed;       579 AA.
AC   A0A2S5B2L6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Putative Alpha-amylase {ECO:0000313|EMBL:POY70996.1};
DE            EC=3.2.1.1 {ECO:0000313|EMBL:POY70996.1};
DE   Flags: Fragment;
GN   ORFNames=BMF94_5921 {ECO:0000313|EMBL:POY70996.1};
OS   Rhodotorula taiwanensis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=741276 {ECO:0000313|EMBL:POY70996.1, ECO:0000313|Proteomes:UP000237144};
RN   [1] {ECO:0000313|EMBL:POY70996.1, ECO:0000313|Proteomes:UP000237144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD1149 {ECO:0000313|EMBL:POY70996.1,
RC   ECO:0000313|Proteomes:UP000237144};
RX   PubMed=29375494;
RA   Tkavc R., Matrosova V.Y., Grichenko O.E., Gostincar C., Volpe R.P.,
RA   Klimenkova P., Gaidamakova E.K., Zhou C.E., Stewart B.J., Lyman M.G.,
RA   Malfatti S.A., Rubinfeld B., Courtot M., Singh J., Dalgard C.L.,
RA   Hamilton T., Frey K.G., Gunde-Cimerman N., Dugan L., Daly M.J.;
RT   "Prospects for Fungal Bioremediation of Acidic Radioactive Waste Sites:
RT   Characterization and Genome Sequence of Rhodotorula taiwanensis MD1149.";
RL   Front. Microbiol. 8:2528-2528(2018).
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}.
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:POY70996.1}.
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DR   EMBL; PJQD01000088; POY70996.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S5B2L6; -.
DR   STRING; 741276.A0A2S5B2L6; -.
DR   OrthoDB; 2728918at2759; -.
DR   Proteomes; UP000237144; Unassembled WGS sequence.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005509; F:calcium ion binding; 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;
KW   Glycosidase {ECO:0000313|EMBL:POY70996.1};
KW   Hydrolase {ECO:0000313|EMBL:POY70996.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237144};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..579
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015527736"
FT   DOMAIN          93..483
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          43..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:POY70996.1"
SQ   SEQUENCE   579 AA;  65337 MW;  CE08D4EAB02F6B33 CRC64;
     AARERSALAL LAFPVSLSLS LSLLQFLTYT IDDMSTKPEI ARKSSINAPT GPPVDAVPFD
     PPKPADQPKR TQAWRANARG LGKGDEEAGT TNYTACQAFE WYTEGNGKHW NWLKEKAPEF
     AEMGITAVWI PPPYKCDTKD STGYSPYDLW DLGEFDQKGA VETKYGTKQE LLDMIKAMKE
     NDAVLNHKAG ADRPETFKVI EVDQEDRTKE ISEPFDIEGW TGFDFEGRGD KYSKLKWNFE
     HFNGVDYDNK TQKNGIFKIL GENKGWNKHV DRSEKGVFDY LMSANIDVSH PIVREDLINW
     GKWLIKETGA DGFRFDAVRH IDEVFLSEFV RAVRDDNDNC VGEFWMPDVD VINGYLDKFP
     EQFSCFDAPL HDNFYQASMQ NENYDLRQIF DNTLVKTRPM DAVTIVANHD TQPGQTCEAP
     VGAWFAPLAY SLILLRGDGY PSIFLGDLVG CKSDPPVEPV SQLADFARAR KWFAYGPTRD
     YWDHPNCVGW VREGDKEHDG CAVVMCNGTE DGSKRMQIQG NDEHKGEEWI DVLGWSGDKT
     ITIGDDGWAD FTCPAKSVSI WVKKGARGLD AFKNAPKQE
//