(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 68.
DE   RecName: Full=Probable cutinase 3;
DE            EC=3.1.1.74;
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.
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 cutin, a polyester that forms the
CC       structure of plant cuticle. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cutin + H(2)O = cutin monomers.; EC=3.1.1.74;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10108};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
DR   EMBL; AAHF01000016; EAL84469.1; -; Genomic_DNA.
DR   RefSeq; XP_746507.1; XM_741414.1.
DR   SMR; Q4W9Z4; -.
DR   ESTHER; aspfu-q4w9z4; Cutinase.
DR   EnsemblFungi; EAL84469; EAL84469; AFUA_4G03210.
DR   GeneID; 3504036; -.
DR   KEGG; afm:AFUA_4G03210; -.
DR   EuPathDB; FungiDB:Afu4g03210; -.
DR   HOGENOM; HOG000171425; -.
DR   InParanoid; Q4W9Z4; -.
DR   KO; K08095; -.
DR   OMA; NALPQNT; -.
DR   OrthoDB; 1227171at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   Proteomes; UP000002530; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR011150; Cutinase_monf.
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;
DR   PRODOM; Q4W9Z4.
DR   SWISS-2DPAGE; Q4W9Z4.
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10108"
FT   ACT_SITE        184
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10108"
FT   ACT_SITE        197
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10108"
FT   DISULFID        39..187
FT                   /evidence="ECO:0000250"
FT   DISULFID        118..180
FT                   /evidence="ECO:0000250"
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
//

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