ID   CUTI5_ASPTN             Reviewed;         220 AA.
AC   Q0CRP4;
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 5;
DE            EC=3.1.1.74 {ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-ProRule:PRU10109};
DE   AltName: Full=Cutin hydrolase 5;
DE   Flags: Precursor;
GN   ORFNames=ATEG_03640;
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; CH476598; EAU35442.1; -; Genomic_DNA.
DR   RefSeq; XP_001212818.1; XM_001212818.1.
DR   AlphaFoldDB; Q0CRP4; -.
DR   SMR; Q0CRP4; -.
DR   ESTHER; asptn-cuti5; Cutinase.
DR   PRIDE; Q0CRP4; -.
DR   EnsemblFungi; EAU35442; EAU35442; ATEG_03640.
DR   GeneID; 4318500; -.
DR   VEuPathDB; FungiDB:ATEG_03640; -.
DR   eggNOG; ENOG502SI38; Eukaryota.
DR   HOGENOM; CLU_040058_2_0_1; -.
DR   OMA; GHFNDAN; -.
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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..220
FT                   /note="Probable cutinase 5"
FT                   /id="PRO_0000395259"
FT   ACT_SITE        132
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   ACT_SITE        187
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   ACT_SITE        200
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   SITE            53
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   SITE            133
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00590"
FT   DISULFID        42..121
FT                   /evidence="ECO:0000250|UniProtKB:P52956"
FT   DISULFID        68..82
FT                   /evidence="ECO:0000250|UniProtKB:P52956"
FT   DISULFID        183..190
FT                   /evidence="ECO:0000250|UniProtKB:P52956"
SQ   SEQUENCE   220 AA;  23020 MW;  F7A49F85C11D85B0 CRC64;
     MVALHTLLLT AFAAVSLANP IPAPELEARQ IINANDLENG VCKPVVLIFA RGSTELGNMG
     AIAGMPTCNA LKLALGSQNV ACQGVGGAYT ASLIPNFLPA NTNQASIREA TGVFEMAHTR
     CPNSQIVAGG YSQGSAVMDN TIQDLPDVIK NKVKGVVLFG FTRNLQDLGR IPNYPKEQTK
     VICAVGDLVC VGTLIITPAH LTYTLNAPEA AQFLASMVSV