CUTI1_ASPCL
ID CUTI1_ASPCL Reviewed; 211 AA.
AC A1CSZ4;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Probable cutinase 1;
DE EC=3.1.1.74 {ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-ProRule:PRU10109};
DE AltName: Full=Cutin hydrolase 1;
DE Flags: Precursor;
GN ORFNames=ACLA_081180;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027060; EAW06431.1; -; Genomic_DNA.
DR RefSeq; XP_001267857.1; XM_001267856.1.
DR AlphaFoldDB; A1CSZ4; -.
DR SMR; A1CSZ4; -.
DR ESTHER; aspcl-cuti1; Cutinase.
DR EnsemblFungi; EAW06431; EAW06431; ACLA_081180.
DR GeneID; 4700176; -.
DR KEGG; act:ACLA_081180; -.
DR VEuPathDB; FungiDB:ACLA_081180; -.
DR eggNOG; ENOG502SI38; Eukaryota.
DR HOGENOM; CLU_040058_2_0_1; -.
DR OMA; SCPKAIF; -.
DR OrthoDB; 1227171at2759; -.
DR Proteomes; UP000006701; 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..14
FT /evidence="ECO:0000255"
FT CHAIN 15..211
FT /note="Probable cutinase 1"
FT /id="PRO_0000395245"
FT ACT_SITE 125
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 180
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 193
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 47
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 126
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 36..114
FT /evidence="ECO:0000250|UniProtKB:P52956"
FT DISULFID 62..75
FT /evidence="ECO:0000250|UniProtKB:P52956"
FT DISULFID 176..183
FT /evidence="ECO:0000250|UniProtKB:P52956"
SQ SEQUENCE 211 AA; 22161 MW; 6C5269ABBAFC4C9E CRC64;
MKFALLALAA VALASPVTLD ERQIAIPENE LRTGPCEPIT FIFARASTEP GLLGISTGPG
VCNGLKLARP FKVACQGVGP AYTADLASNF LPQGTTQVAI DEATDLFKLA ASKCPDTQIV
AGGYSQGTAV MHGAIRNLPD NVKNLIRGVV LFGDTRNKQD GGRIPNFPTD RTKIYCALGD
LVCEGTLVIT AAHFTYTVNV PGAVAFLLSK L
