CUTI3_ASPTN
ID CUTI3_ASPTN Reviewed; 218 AA.
AC Q0CNE3;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Probable cutinase 3;
DE EC=3.1.1.74 {ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-ProRule:PRU10109};
DE AltName: Full=Cutin hydrolase 3;
DE Flags: Precursor;
GN ORFNames=ATEG_04791;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU35238.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CH476599; EAU35238.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001213969.1; XM_001213969.1.
DR AlphaFoldDB; Q0CNE3; -.
DR SMR; Q0CNE3; -.
DR ESTHER; asptn-cuti3; Cutinase.
DR EnsemblFungi; EAU35238; EAU35238; ATEG_04791.
DR GeneID; 4320440; -.
DR eggNOG; ENOG502SI38; Eukaryota.
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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..218
FT /note="Probable cutinase 3"
FT /id="PRO_0000395257"
FT ACT_SITE 131
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 186
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 199
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 132
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 41..120
FT /evidence="ECO:0000250|UniProtKB:P52956"
FT DISULFID 67..81
FT /evidence="ECO:0000250|UniProtKB:P52956"
FT DISULFID 182..189
FT /evidence="ECO:0000250|UniProtKB:P52956"
SQ SEQUENCE 218 AA; 22667 MW; CF830CACA534FDE7 CRC64;
MSLRSVLVAA LAALAVATPV PENSLQERQL MSSNDVEDGV CRDVTFIFAR GSTEQGNMGF
VVGPEVCTSL KADLGSGKVA CQGVGGAYTA SLAPNFLSAN TDPQSIQAAT DLFEKAVANC
PNTQIVAGGY SQGSAVMDNS IQALPADIQE KVKGVVLFGF TRNLQDNGQI PNYPKEDVKV
YCALGDLVCS GTLIITPAHM TYGVNAGDAA QFLASKVQ
