ID   A1CIW4_ASPCL            Unreviewed;       636 AA.
AC   A1CIW4;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   02-SEP-2026, entry version 95.
DE   RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE            EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN   ORFNames=ACLA_052920 {ECO:0000313|EMBL:EAW10819.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW10819.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW10819.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276
RC   / 107 {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC         polysaccharides containing three or more (1->4)-alpha-linked D-
CC         glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|ARBA:ARBA00000548};
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; DS027054; EAW10819.1; -; Genomic_DNA.
DR   RefSeq; XP_001272245.1; XM_001272244.1.
DR   AlphaFoldDB; A1CIW4; -.
DR   STRING; 344612.A1CIW4; -.
DR   GeneID; 4704010; -.
DR   KEGG; act:ACLA_052920; -.
DR   VEuPathDB; FungiDB:ACLA_052920; -.
DR   eggNOG; KOG0471; Eukaryota.
DR   HOGENOM; CLU_006462_7_2_1; -.
DR   OMA; VTNHMAW; -.
DR   OrthoDB; 204980at2759; -.
DR   Proteomes; UP000006701; 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:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR   CDD; cd11319; AmyAc_euk_AmyA; 1.
DR   CDD; cd05811; CBM20_glucoamylase; 1.
DR   FunFam; 2.60.40.1180:FF:000037; Alpha-amylase A; 1.
DR   FunFam; 3.20.20.80:FF:000120; Alpha-amylase A; 1.
DR   FunFam; 2.60.40.10:FF:000552; Related to glucoamylase; 1.
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; IPR015340; A_amylase_C_dom.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR002044; CBM20.
DR   InterPro; IPR034836; CBM20_glucoamylase.
DR   InterPro; IPR006047; GH13_cat_dom.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR10357:SF231; ALPHA-AMYLASE; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   Pfam; PF09260; A_amylase_dom_C; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF00686; CBM_20; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM01065; CBM_2; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 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   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..636
FT                   /note="alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002633484"
FT   DOMAIN          529..636
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
FT   REGION          606..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..636
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   636 AA;  68945 MW;  D26D7D66BA69675F CRC64;
     MKLLALTTAF ALLGKGVFGL TPAEWRGQSI YFLITDRFAR TDGSTTAPCD LSQRAYCGGS
     WQGIIKQLDY IQGMGFTAIW ITPITEQIPQ DTAEGSAFHG YWQKDIYNVN SHFGTADDIR
     ALSKALHDRG MYLMIDVVAN HMGYNGPGAS TDFSTFTPFN SASYFHSYCP INNYNDQSQV
     ENCWLGDNTV ALADLYTQHS DVRNIWYSWI KEIVGNYSAD GLRIDTVKHV EKDFWTGYTQ
     AAGVYTVGEV LDGDPAYTCP YQGYVDGVLN YPIYYPLLRA FESSSGSMGD LYNMINSVAS
     DCKDPTVLGS FIENHDNPRF ASYTKDMSQA KAVISYVILS DGIPIIYSGQ EQHYSGGNDP
     YNREAIWLSG YSTTSELYKF IATTNKIRQL AISKDSSYLT SRNNPFYTDS NTIAMRKGSG
     GSQVITVLSN SGSNGGSYTL NLGNSGYSSG ANLVEVYTCS SVTVGSDGKI PVPMASGLPR
     VLVPASWMSG SGLCGSSSTT TLVTATTTPT GSSSSTTLAT AVTTPTGSCK TATTVPVVLE
     ESVRTSYGEN IFISGSIPQL GSWNPDKAVA LSSSQYTSSN PLWAVTLDLP VGTSFEYKFL
     KKEQNGGVAW ENDPNRSYTV PEACAGTSQK VDSSWR
//