ID   AMYA1_ASPOR             Reviewed;         499 AA.
AC   P0C1B3; P10529; P11763; Q00250; Q2U6K7;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Alpha-amylase A type-1/2;
DE            EC=3.2.1.1 {ECO:0000305};
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE   AltName: Full=Taka-amylase A;
DE            Short=TAA;
DE   Flags: Precursor;
GN   Name=amy1; Synonyms=amyI, Taa-G1; ORFNames=AO090023000944;
GN   and
GN   Name=amy2; Synonyms=amyII, Taa-G2; ORFNames=AO090120000196;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (AMY1 AND AMY2).
RC   STRAIN=DSM 63303;
RX   PubMed=2785629; DOI=10.1111/j.1365-2958.1989.tb00097.x;
RA   Wirsel S., Lachmund A., Wildhardt G., Ruttkowski E.;
RT   "Three alpha-amylase genes of Aspergillus oryzae exhibit identical intron-
RT   exon organization.";
RL   Mol. Microbiol. 3:3-14(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2789162; DOI=10.1016/0378-1119(89)90096-6;
RA   Genes M.J., Dove M.J., Seligy V.L.;
RT   "Aspergillus oryzae has two nearly identical Taka-amylase genes, each
RT   containing eight introns.";
RL   Gene 79:107-117(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Tada S., Iimura Y., Gomi K., Takahashi K., Hara S., Yoshizawa K.;
RT   "Cloning and nucleotide sequence of the genomic Taka-amylase A gene of
RT   Aspergillus oryzae.";
RL   Agric. Biol. Chem. 53:593-599(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (AMY1 AND AMY2).
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
RN   [5]
RP   PROTEIN SEQUENCE OF 22-499.
RX   DOI=10.2183/pjab.58.208;
RA   Toda H., Kondo K., Narita K.;
RT   "The complete amino acid sequence of Taka-amylase A.";
RL   Proc. Jpn. Acad., B, Phys. Biol. Sci. 58:208-212(1982).
RN   [6]
RP   PROTEIN SEQUENCE OF 206-225.
RX   PubMed=4733850; DOI=10.1093/oxfordjournals.jbchem.a130210;
RA   Isemura S., Ikenaka T.;
RT   "The amino acid sequences of glycopeptides obtained from Taka-amylase A
RT   with trypsin and chymotrypsin.";
RL   J. Biochem. 74:1-10(1973).
RN   [7]
RP   PROTEIN SEQUENCE OF 434-499.
RA   Narita K.;
RT   "Amino acid sequence of the C-terminal sixty-six residues of Taka-amylase
RT   A.";
RL   Proc. Jpn. Acad. 51:285-290(1975).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 22-499 IN COMPLEX WITH CALCIUM,
RP   COFACTOR, AND DISULFIDE BONDS.
RX   PubMed=6156152; DOI=10.1093/oxfordjournals.jbchem.a132896;
RA   Matsuura Y., Kusunoki M., Harada W., Tanaka N., Iga Y., Yasuoka N.,
RA   Toda H., Narita K., Kakudo M.;
RT   "Molecular structure of taka-amylase A. I. Backbone chain folding at 3-A
RT   resolution.";
RL   J. Biochem. 87:1555-1558(1980).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
RX   PubMed=6609921; DOI=10.1093/oxfordjournals.jbchem.a134659;
RA   Matsuura Y., Kusunoki M., Harada W., Kakudo M.;
RT   "Structure and possible catalytic residues of Taka-amylase A.";
RL   J. Biochem. 95:697-702(1984).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH CALCIUM AND
RP   ACARBOSE, COFACTOR, DISULFIDE BONDS, AND ACTIVE SITE.
RX   PubMed=9283074; DOI=10.1021/bi970539i;
RA   Brzozowski A.M., Davies G.J.;
RT   "Structure of the Aspergillus oryzae alpha-amylase complexed with the
RT   inhibitor acarbose at 2.0-A resolution.";
RL   Biochemistry 36:10837-10845(1997).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 22-499 IN COMPLEX WITH MALTOSE
RP   AND CALCIUM IONS, GLYCOSYLATION AT ASN-218, AND DISULFIDE BONDS.
RX   PubMed=16880540; DOI=10.1107/s1744309106024729;
RA   Vujicic-Zagar A., Dijkstra B.W.;
RT   "Monoclinic crystal form of Aspergillus niger alpha-amylase in complex with
RT   maltose at 1.8 angstroms resolution.";
RL   Acta Crystallogr. F 62:716-721(2006).
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:0000305};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:16880540, ECO:0000269|PubMed:6609921,
CC         ECO:0000269|PubMed:9283074};
CC       Note=Binds 2 calcium ions per subunit (PubMed:6609921, PubMed:9283074,
CC       PubMed:16880540). Calcium is inhibitory at high concentrations.
CC       {ECO:0000269|PubMed:16880540, ECO:0000269|PubMed:6609921,
CC       ECO:0000269|PubMed:9283074, ECO:0000305};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16880540,
CC       ECO:0000269|PubMed:9283074}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- BIOTECHNOLOGY: Used in the brewing industry to increase the
CC       fermentability of beer worts (including those made from unmalted
CC       cereals), in the starch industry to make high maltose and high DE
CC       syrups (starch saccharification), in the alcohol industry to reduce
CC       fermentation time, in the cereal food industry for flour
CC       supplementation and improvement of chilled and frozen dough, and in the
CC       forestry industry for low-temperature modification of starch. Sold
CC       under the name Fungamyl by Novozymes.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; X12725; CAA31218.1; -; Genomic_DNA.
DR   EMBL; X12726; CAA31219.1; -; Genomic_DNA.
DR   EMBL; D00434; BAA00336.1; -; Genomic_DNA.
DR   EMBL; AP007157; BAE59434.1; -; Genomic_DNA.
DR   EMBL; AP007166; BAE62808.1; -; Genomic_DNA.
DR   PIR; JK0201; JK0201.
DR   PIR; JT0466; JT0466.
DR   PIR; S04548; ALAS1.
DR   RefSeq; XP_001821436.1; XM_001821384.2.
DR   RefSeq; XP_001823941.1; XM_001823889.2.
DR   PDB; 2GUY; X-ray; 1.59 A; A=22-499.
DR   PDB; 2GVY; X-ray; 1.80 A; A/B=22-499.
DR   PDB; 2TAA; X-ray; 3.00 A; A/B/C=22-499.
DR   PDB; 3KWX; X-ray; 2.40 A; A=22-499.
DR   PDB; 3VX0; X-ray; 1.50 A; A=22-499.
DR   PDB; 3VX1; X-ray; 2.20 A; A=22-499.
DR   PDB; 6TAA; X-ray; 2.10 A; A=22-499.
DR   PDB; 6XSJ; X-ray; 1.40 A; A/B=1-499.
DR   PDB; 6XSV; X-ray; 1.65 A; A=1-499.
DR   PDB; 6YQ7; X-ray; 1.58 A; A/B=1-499.
DR   PDB; 7P4W; X-ray; 2.28 A; A=22-497.
DR   PDB; 7TAA; X-ray; 1.98 A; A=22-499.
DR   PDBsum; 2GUY; -.
DR   PDBsum; 2GVY; -.
DR   PDBsum; 2TAA; -.
DR   PDBsum; 3KWX; -.
DR   PDBsum; 3VX0; -.
DR   PDBsum; 3VX1; -.
DR   PDBsum; 6TAA; -.
DR   PDBsum; 6XSJ; -.
DR   PDBsum; 6XSV; -.
DR   PDBsum; 6YQ7; -.
DR   PDBsum; 7P4W; -.
DR   PDBsum; 7TAA; -.
DR   AlphaFoldDB; P0C1B3; -.
DR   SMR; P0C1B3; -.
DR   STRING; 510516.P0C1B3; -.
DR   Allergome; 86; Asp o 21.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GlyConnect; 25; 1 N-Linked glycan (1 site).
DR   GlyCosmos; P0C1B3; 1 site, 1 glycan.
DR   EnsemblFungi; BAE59434; BAE59434; AO090023000944.
DR   EnsemblFungi; BAE62808; BAE62808; AO090120000196.
DR   GeneID; 5993438; -.
DR   GeneID; 5996200; -.
DR   KEGG; aor:AO090023000944; -.
DR   KEGG; aor:AO090120000196; -.
DR   VEuPathDB; FungiDB:AO090023000944; -.
DR   VEuPathDB; FungiDB:AO090120000196; -.
DR   HOGENOM; CLU_006462_7_2_1; -.
DR   OMA; YWIYEAN; -.
DR   OrthoDB; 3249969at2759; -.
DR   EvolutionaryTrace; P0C1B3; -.
DR   Proteomes; UP000006564; Chromosome 3.
DR   Proteomes; UP000006564; Chromosome 5.
DR   GO; GO:0030428; C:cell septum; IDA:AspGD.
DR   GO; GO:0030287; C:cell wall-bounded periplasmic space; IDA:AspGD.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0009277; C:fungal-type cell wall; IDA:AspGD.
DR   GO; GO:0032163; C:hyphal septin band; IDA:AspGD.
DR   GO; GO:0031521; C:spitzenkorper; IDA:AspGD.
DR   GO; GO:0004556; F:alpha-amylase activity; IGI:AspGD.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IGI:AspGD.
DR   CDD; cd11319; AmyAc_euk_AmyA; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR013777; A-amylase-like.
DR   InterPro; IPR015340; A_amylase_C_dom.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10357:SF212; 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   PIRSF; PIRSF001024; Alph-amyl_fung; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Carbohydrate metabolism; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Metal-binding;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|Ref.5"
FT   CHAIN           22..499
FT                   /note="Alpha-amylase A type-1/2"
FT                   /id="PRO_0000001349"
FT   ACT_SITE        227
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305|PubMed:9283074"
FT   ACT_SITE        251
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000305|PubMed:9283074"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:9283074"
FT   BINDING         104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:9283074"
FT   BINDING         142
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:16880540,
FT                   ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:9283074"
FT   BINDING         183
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:16880540,
FT                   ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074"
FT   BINDING         196
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:16880540,
FT                   ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074"
FT   BINDING         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:9283074"
FT   BINDING         227
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:9283074"
FT   BINDING         230..231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:9283074"
FT   BINDING         231
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:16880540,
FT                   ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074"
FT   BINDING         251
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:9283074"
FT   BINDING         255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:9283074"
FT   BINDING         318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:9283074"
FT   BINDING         365
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:9283074"
FT   SITE            318
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000305|PubMed:9283074"
FT   CARBOHYD        218
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16880540"
FT                   /id="CAR_000125"
FT   DISULFID        51..59
FT                   /evidence="ECO:0000269|PubMed:16880540,
FT                   ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074,
FT                   ECO:0007744|PDB:7TAA"
FT   DISULFID        171..185
FT                   /evidence="ECO:0000269|PubMed:16880540,
FT                   ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074,
FT                   ECO:0007744|PDB:7TAA"
FT   DISULFID        261..304
FT                   /evidence="ECO:0000269|PubMed:16880540,
FT                   ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074,
FT                   ECO:0007744|PDB:7TAA"
FT   DISULFID        461..496
FT                   /evidence="ECO:0000269|PubMed:16880540,
FT                   ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074,
FT                   ECO:0007744|PDB:7TAA"
FT   CONFLICT        93..94
FT                   /note="TT -> DC (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        101
FT                   /note="H -> T (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        106
FT                   /note="Q -> T (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        184
FT                   /note="D -> Y (in Ref. 3; BAA00336)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        195
FT                   /note="P -> L (in Ref. 3; BAA00336)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        255
FT                   /note="G -> V (in Ref. 3; BAA00336)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        345
FT                   /note="I -> L (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        406..409
FT                   /note="WPIY -> PYI (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        443..444
FT                   /note="Missing (in Ref. 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        448
FT                   /note="G -> Q (in Ref. 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        448
FT                   /note="G -> S (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        458
FT                   /note="V -> VGTTV (in Ref. 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        465..466
FT                   /note="Missing (in Ref. 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        469..471
FT                   /note="DGN -> BGB (in Ref. 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        497
FT                   /note="S -> SD (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           24..27
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          32..35
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           37..40
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:6YQ7"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           63..68
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           70..74
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   TURN            75..77
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          80..83
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          87..89
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          104..111
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           113..115
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           118..130
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          134..139
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          146..148
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           150..152
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           155..157
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          158..160
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           164..166
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           176..178
FT                   /evidence="ECO:0007829|PDB:2TAA"
FT   HELIX           179..184
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          185..188
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          190..194
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           202..219
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          223..227
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           229..231
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           234..236
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           237..244
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          246..250
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           257..260
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           261..265
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          267..271
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           273..283
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           290..303
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           307..309
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          310..312
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           322..325
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           329..341
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          342..349
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           352..354
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   TURN            361..364
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           368..371
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          375..377
FT                   /evidence="ECO:0007829|PDB:6YQ7"
FT   HELIX           378..396
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           400..402
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          406..411
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          414..421
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   TURN            422..424
FT                   /evidence="ECO:0007829|PDB:3VX0"
FT   STRAND          426..431
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          440..444
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          454..457
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   TURN            458..461
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          462..465
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          468..470
FT                   /evidence="ECO:0007829|PDB:6TAA"
FT   STRAND          472..476
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          482..486
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   HELIX           487..490
FT                   /evidence="ECO:0007829|PDB:6XSJ"
FT   STRAND          493..495
FT                   /evidence="ECO:0007829|PDB:3KWX"
SQ   SEQUENCE   499 AA;  54810 MW;  E407AE50DD071B52 CRC64;
     MMVAWWSLFL YGLQVAAPAL AATPADWRSQ SIYFLLTDRF ARTDGSTTAT CNTADQKYCG
     GTWQGIIDKL DYIQGMGFTA IWITPVTAQL PQTTAYGDAY HGYWQQDIYS LNENYGTADD
     LKALSSALHE RGMYLMVDVV ANHMGYDGAG SSVDYSVFKP FSSQDYFHPF CFIQNYEDQT
     QVEDCWLGDN TVSLPDLDTT KDVVKNEWYD WVGSLVSNYS IDGLRIDTVK HVQKDFWPGY
     NKAAGVYCIG EVLDGDPAYT CPYQNVMDGV LNYPIYYPLL NAFKSTSGSM DDLYNMINTV
     KSDCPDSTLL GTFVENHDNP RFASYTNDIA LAKNVAAFII LNDGIPIIYA GQEQHYAGGN
     DPANREATWL SGYPTDSELY KLIASANAIR NYAISKDTGF VTYKNWPIYK DDTTIAMRKG
     TDGSQIVTIL SNKGASGDSY TLSLSGAGYT AGQQLTEVIG CTTVTVGSDG NVPVPMAGGL
     PRVLYPTEKL AGSKICSSS
//