ID   CUTI2_ASPTN             Reviewed;         216 AA.
AC   Q0CES4;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 61.
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=ATEG_07810;
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; CH476604; EAU32072.1; -; Genomic_DNA.
DR   RefSeq; XP_001216431.1; XM_001216431.1.
DR   AlphaFoldDB; Q0CES4; -.
DR   SMR; Q0CES4; -.
DR   ESTHER; asptn-cuti2; Cutinase.
DR   EnsemblFungi; EAU32072; EAU32072; ATEG_07810.
DR   GeneID; 4322671; -.
DR   VEuPathDB; FungiDB:ATEG_07810; -.
DR   eggNOG; ENOG502SI38; Eukaryota.
DR   HOGENOM; CLU_040058_2_0_1; -.
DR   OMA; SCPKAIF; -.
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..216
FT                   /note="Probable cutinase 2"
FT                   /id="PRO_0000395256"
FT   ACT_SITE        129
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   ACT_SITE        184
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   ACT_SITE        197
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   SITE            52
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   SITE            130
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        41..118
FT                   /evidence="ECO:0000250|UniProtKB:P52956"
FT   DISULFID        67..79
FT                   /evidence="ECO:0000250|UniProtKB:P52956"
FT   DISULFID        180..187
FT                   /evidence="ECO:0000250|UniProtKB:P52956"
SQ   SEQUENCE   216 AA;  22680 MW;  343D6C65551FDE46 CRC64;
     MNYKLLTLAL ASLAAANPIE RQRKIHPAVL SGGDELRNGD CQPVTFIFAR ASTEQGLLGG
     STGPALCNRL KSALDGVACQ GVGPKYQATL AANALPKGTS DEAIEEAQSL FQLAAEKCPD
     TQIVAGGYSQ GTAVMHGAIP GLDDALKDKI KGVVLFGDTR NQQDNGQIPD FPKDKIKIYC
     AAGDMVCYGT LIVAAPHFSY IADVPDAADF LVSKLE