ID   CUTI2_FUSVN             Reviewed;         231 AA.
AC   Q96UT0;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=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   Name=CUT2;
OS   Fusarium vanettenii (Neocosmospora pisi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=2747968;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=T-8;
RX   PubMed=11756444; DOI=10.1074/jbc.m108799200;
RA   Li D., Sirakova T., Rogers L., Ettinger W.F., Kolattukudy P.E.;
RT   "Regulation of constitutively expressed and induced cutinase genes by
RT   different zinc finger transcription factors in Fusarium solani f. sp. pisi
RT   (Nectria haematococca).";
RL   J. Biol. Chem. 277:7905-7912(2002).
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). Allows pathogenic fungi to penetrate through the cuticular
CC       barrier into the host plant during the initial stage of fungal
CC       infection (By 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   -!- PTM: The 2 disulfide bonds play a critical role in holding the
CC       catalytic residues in juxta-position; reduction of the disulfide
CC       bridges results in the complete inactivation of the enzyme.
CC       {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; AF417004; AAL18696.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q96UT0; -.
DR   SMR; Q96UT0; -.
DR   ESTHER; fusso-CUT2; Cutinase.
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; Virulence.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..231
FT                   /note="Cutinase 2"
FT                   /id="PRO_0000006441"
FT   ACT_SITE        137
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   ACT_SITE        192
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   ACT_SITE        205
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   SITE            59
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   SITE            138
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        48..126
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        188..195
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
SQ   SEQUENCE   231 AA;  23932 MW;  8047714A249CB756 CRC64;
     MKFFALTTLL AATASALPTS HPVQELEARQ LGGGTTRNDL TNGNSASCAD VIFIYARGST
     ETGNLGTLGP SIASKLESAF GRDGVWIQGV GGAYRATLGD NSLPRGTSSA AIREMLGLFQ
     QANTKCPDAT LIAGGYSQGA ALGAASVEDL DSAIRDKIAG TVLFGYTKNL QNHGRIPNFP
     ADRTKVFCNT GDLVCTGSLI IAAPHLTYGP DARGPAPEFL IEKVRAVRGS A