ID   CUTI1_ASPTN             Reviewed;         209 AA.
AC   Q0CD01;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=ATEG_08433;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476605; EAU31606.1; -; Genomic_DNA.
DR   RefSeq; XP_001217054.1; XM_001217054.1.
DR   AlphaFoldDB; Q0CD01; -.
DR   SMR; Q0CD01; -.
DR   ESTHER; asptn-cuti1; Cutinase.
DR   PRIDE; Q0CD01; -.
DR   EnsemblFungi; EAU31606; EAU31606; ATEG_08433.
DR   GeneID; 4353579; -.
DR   VEuPathDB; FungiDB:ATEG_08433; -.
DR   eggNOG; ENOG502SI38; Eukaryota.
DR   HOGENOM; CLU_040058_2_0_1; -.
DR   OMA; KIFCLPT; -.
DR   OrthoDB; 1227171at2759; -.
DR   Proteomes; UP000007963; 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; Reference proteome; Secreted; Serine esterase;
KW   Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..209
FT                   /note="Probable cutinase 1"
FT                   /id="PRO_0000395255"
FT   ACT_SITE        123
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   ACT_SITE        178
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   ACT_SITE        191
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   SITE            45
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   SITE            124
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        34..112
FT                   /evidence="ECO:0000250|UniProtKB:P52956"
FT   DISULFID        60..73
FT                   /evidence="ECO:0000250|UniProtKB:P52956"
FT   DISULFID        174..181
FT                   /evidence="ECO:0000250|UniProtKB:P52956"
SQ   SEQUENCE   209 AA;  22035 MW;  E550242F2EFA2F39 CRC64;
     MKLLTVLTLL TGLVAASPID LEKRQRNELR VGACEEITFI FARASTETGY LGGSTGPGVC
     NGLKLARVGQ VACQGVAPRY TADLASNFLP QGTSQAAIDE AVELFQLAAS KCPNTKIVAG
     GYSQGTAVMH NAIPALPDNI KNMIKGVVLF GDTRNQQDGG RIPNFPTDKT KIYCAVGDLV
     CEGTLVITAA HFTYMANVAD AVSFLLARV