ID   CUTI1_ASPFC             Reviewed;         211 AA.
AC   B0XRY3;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Probable cutinase 1;
DE            EC=3.1.1.74 {ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-ProRule:PRU10109};
DE   AltName: Full=Cutin hydrolase 1;
DE   Flags: Precursor;
GN   ORFNames=AFUB_025250;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
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   -!- FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters
CC       found in the cell wall of plants (By similarity). Degrades cutin, a
CC       macromolecule that forms the structure of the plant cuticle (By
CC       similarity). {ECO:0000250|UniProtKB:P00590}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-
CC         ProRule:PRU10109};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11373}.
CC   -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR   EMBL; DS499595; EDP54469.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0XRY3; -.
DR   SMR; B0XRY3; -.
DR   ESTHER; aspfu-q4x1n0; Cutinase.
DR   EnsemblFungi; EDP54469; EDP54469; AFUB_025250.
DR   VEuPathDB; FungiDB:AFUB_025250; -.
DR   HOGENOM; CLU_040058_2_0_1; -.
DR   PhylomeDB; B0XRY3; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0050525; F:cutinase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000675; Cutinase/axe.
DR   InterPro; IPR043580; CUTINASE_1.
DR   InterPro; IPR043579; CUTINASE_2.
DR   InterPro; IPR011150; Cutinase_monf.
DR   PANTHER; PTHR33630; PTHR33630; 1.
DR   Pfam; PF01083; Cutinase; 1.
DR   PRINTS; PR00129; CUTINASE.
DR   SMART; SM01110; Cutinase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00155; CUTINASE_1; 1.
DR   PROSITE; PS00931; CUTINASE_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Secreted; Serine esterase; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..211
FT                   /note="Probable cutinase 1"
FT                   /id="PRO_0000395251"
FT   ACT_SITE        125
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   ACT_SITE        193
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   SITE            47
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   SITE            126
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        36..114
FT                   /evidence="ECO:0000250|UniProtKB:P52956"
FT   DISULFID        62..75
FT                   /evidence="ECO:0000250|UniProtKB:P52956"
FT   DISULFID        176..183
FT                   /evidence="ECO:0000250|UniProtKB:P52956"
SQ   SEQUENCE   211 AA;  21856 MW;  43B8A1C7C8956014 CRC64;
     MKFALLSLAA MAVASPVAID VRQTAITGDE LRTGPCEPIT FIFARGSTEP GLLGITTGPG
     VCNALKLSRP GQVACQGVGP AYIADLASNF LPQGTSQVAI DEAAGLFKLA ASKCPDTKIV
     AGGYSQGAAV MHGAIRNLPS NVQNMIKGVV LFGDTRNKQD GGRIPNFPTD RTKIYCAFGD
     LVCDGTLIIT PAHLSYGDDV PSATSFLLSK V