ID   CUTI2_ASPNC             Reviewed;         271 AA.
AC   A5ABE6;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Probable cutinase 2;
DE            EC=3.1.1.74 {ECO:0000255|PROSITE-ProRule:PRU10109};
DE   AltName: Full=Cutin hydrolase 2;
DE   Flags: Precursor;
GN   ORFNames=An11g00110;
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:PRU10109};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11373}.
CC   -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM270218; CAK48244.1; -; Genomic_DNA.
DR   RefSeq; XP_001394015.1; XM_001393978.1.
DR   AlphaFoldDB; A5ABE6; -.
DR   SMR; A5ABE6; -.
DR   ESTHER; aspnc-cuti2; Cutinase.
DR   PaxDb; A5ABE6; -.
DR   EnsemblFungi; CAK48244; CAK48244; An11g00110.
DR   GeneID; 4984242; -.
DR   KEGG; ang:ANI_1_1504094; -.
DR   VEuPathDB; FungiDB:An11g00110; -.
DR   HOGENOM; CLU_040058_2_0_1; -.
DR   Proteomes; UP000006706; Chromosome 7R.
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; 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; 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..271
FT                   /note="Probable cutinase 2"
FT                   /id="PRO_5000242393"
FT   REGION          216..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        126
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10109"
FT   ACT_SITE        181
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10109"
FT   ACT_SITE        194
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10109"
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   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   271 AA;  27628 MW;  90A73A60C15B1E5B CRC64;
     MKLPYFLLGL AGLAAASPMG LAERQLSDGN ELRDGSCKPI IFIFARASTE PGLLGISTGP
     AVCNDLKMAK AGQVLCQGVG PAYTADLMSN ALPDNTSPAA ISESESLFKL AASKCPNSQI
     LAGGYSQGTA VMDDSIKQLP DDVKDKIKGV VLFGYTRNAQ EGGQIGNFPK DKVKIYCAMG
     DLVCDGTLIV TAAHFTYVMN TGEASQWLES KLSDTTTSSL TGSSSSDTSS STSTGDSSSE
     SSSAAGLGGL SGLTGLGSST SGGFPSLASL F