ID   CUTI2_ASPFC             Reviewed;         214 AA.
AC   B0Y537;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Probable cutinase 2;
DE            EC=3.1.1.74 {ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-ProRule:PRU10109};
DE   AltName: Full=Cutin hydrolase 2;
DE   Flags: Precursor;
GN   ORFNames=AFUB_071270;
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; DS499598; EDP50786.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y537; -.
DR   SMR; B0Y537; -.
DR   ESTHER; aspfu-q4wqv2; Cutinase.
DR   EnsemblFungi; EDP50786; EDP50786; AFUB_071270.
DR   VEuPathDB; FungiDB:AFUB_071270; -.
DR   HOGENOM; CLU_040058_2_0_1; -.
DR   PhylomeDB; B0Y537; -.
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; Glycoprotein; Hydrolase; Secreted; Serine esterase; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..214
FT                   /note="Probable cutinase 2"
FT                   /id="PRO_0000395252"
FT   ACT_SITE        126
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   ACT_SITE        181
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   ACT_SITE        194
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   SITE            48
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   SITE            127
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        37..115
FT                   /evidence="ECO:0000250|UniProtKB:P52956"
FT   DISULFID        63..76
FT                   /evidence="ECO:0000250|UniProtKB:P52956"
FT   DISULFID        177..184
FT                   /evidence="ECO:0000250|UniProtKB:P52956"
SQ   SEQUENCE   214 AA;  22326 MW;  C0B300C69C56CB63 CRC64;
     MNLRLLTLAL AGLAAASPVA IEERQLSSGN ELRNGACKPI TFIFARASTE PGLMGLSTGP
     AVCNSLKAAK PGQVACQGVG PAYTADLASN ALPENTSQAA INEAMELFKQ AASKCPDTQI
     VAGGYSQGTA VMDGSIKRLP EEVKERIKGV VLFGYTRNAQ ERGQIANFPK DKVKIYCAMG
     DLVCDGTLIV TAAHFTYGAN TGDAARFLLG KLTA