ID   CUTI1_ASPNC             Reviewed;         262 AA.
AC   A2R2W3;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Probable cutinase 1;
DE            EC=3.1.1.74 {ECO:0000255|PROSITE-ProRule:PRU10108};
DE   AltName: Full=Cutin hydrolase 1;
DE   Flags: Precursor;
GN   ORFNames=An14g02170;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11373}.
CC   -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR   EMBL; AM270317; CAK41954.1; -; Genomic_DNA.
DR   RefSeq; XP_001400843.1; XM_001400806.1.
DR   AlphaFoldDB; A2R2W3; -.
DR   SMR; A2R2W3; -.
DR   ESTHER; aspnc-cuti1; Cutinase.
DR   PaxDb; A2R2W3; -.
DR   EnsemblFungi; CAK41954; CAK41954; An14g02170.
DR   GeneID; 4987073; -.
DR   KEGG; ang:ANI_1_330124; -.
DR   VEuPathDB; FungiDB:An14g02170; -.
DR   HOGENOM; CLU_040058_2_0_1; -.
DR   Proteomes; UP000006706; Chromosome 1R.
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; 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.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Reference proteome; Secreted; Serine esterase;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..262
FT                   /note="Probable cutinase 1"
FT                   /id="PRO_5000220917"
FT   REGION          228..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        138
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10108"
FT   ACT_SITE        193
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10108"
FT   ACT_SITE        206
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10108"
FT   SITE            59
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   SITE            139
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        48..127
FT                   /evidence="ECO:0000250|UniProtKB:P52956"
FT   DISULFID        74..88
FT                   /evidence="ECO:0000250|UniProtKB:P52956"
FT   DISULFID        189..196
FT                   /evidence="ECO:0000250|UniProtKB:P52956"
SQ   SEQUENCE   262 AA;  26688 MW;  025B0F0C5E9D86B5 CRC64;
     MAPLKSLLLG ASLATLALST PLATDAENLY ARQFGTGSTA NELEQGSCKD VTLIFARGST
     ELGNMGTVIG PPLCDNLKSK LGSDKVACQG VGGQYSAGLV QNALPQNTDP GSISAAKQMF
     EEANSKCPNT KIVAGGYSQG SAVIDNAVQE LSTTVKDQVK GVVLFGFTRN VQDHGQIPNY
     PKDDVKVYCA VGDLVCDDTL VVTAMHLTYG MDAGDAASFL AEKVQSSSSS TTSSSSDAAS
     SSSAAGTSSS GLSGLSSFFG GL