CUTI3_ASPFU
ID CUTI3_ASPFU Reviewed; 217 AA.
AC Q4W9Z4;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Probable cutinase 3;
DE EC=3.1.1.74 {ECO:0000255|PROSITE-ProRule:PRU10108};
DE AltName: Full=Cutin hydrolase 3;
DE Flags: Precursor;
GN ORFNames=AFUA_4G03210;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11373}.
CC -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR EMBL; AAHF01000016; EAL84469.1; -; Genomic_DNA.
DR RefSeq; XP_746507.1; XM_741414.1.
DR AlphaFoldDB; Q4W9Z4; -.
DR SMR; Q4W9Z4; -.
DR ESTHER; aspfu-q4w9z4; Cutinase.
DR EnsemblFungi; EAL84469; EAL84469; AFUA_4G03210.
DR GeneID; 3504036; -.
DR KEGG; afm:AFUA_4G03210; -.
DR VEuPathDB; FungiDB:Afu4g03210; -.
DR eggNOG; ENOG502SI38; Eukaryota.
DR HOGENOM; CLU_040058_2_0_1; -.
DR InParanoid; Q4W9Z4; -.
DR OMA; VIGPPLC; -.
DR OrthoDB; 1227171at2759; -.
DR Proteomes; UP000002530; Chromosome 4.
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; 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.
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..217
FT /note="Probable cutinase 3"
FT /id="PRO_0000395250"
FT ACT_SITE 129
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10108"
FT ACT_SITE 184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10108"
FT ACT_SITE 197
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10108"
FT SITE 50
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 39..118
FT /evidence="ECO:0000250|UniProtKB:P52956"
FT DISULFID 65..79
FT /evidence="ECO:0000250|UniProtKB:P52956"
FT DISULFID 180..187
FT /evidence="ECO:0000250|UniProtKB:P52956"
SQ SEQUENCE 217 AA; 22483 MW; 10735C585B7690FA CRC64;
MSLRSLFVAG LATLALAVPA PQIQARQGMS SNELESGPCR DVTFIFARGS TEQGNMGLIV
GPGVCSSLKK DLGSDKVACQ GVGGAYTAQL APNFLSQNTN QASINAATDM FDLANTKCPN
TKIVAGGYSQ GSAVIDNTIQ ALGSDLKAKV KGVVLFGFTR NVADKGQIPG YPKDQTKIYC
AVGDMVCVNT LIITPAHLTY GADAGDAAKF LASKVQE
