ID A0A2W1H8L0_9PLEO Unreviewed; 149 AA. AC A0A2W1H8L0; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 11-DEC-2019, entry version 6. DE RecName: Full=Cutinase {ECO:0000256|RuleBase:RU361263}; DE EC=3.1.1.74 {ECO:0000256|RuleBase:RU361263}; GN ORFNames=A1F99_09670 {ECO:0000313|EMBL:PZD42011.1}; OS Pyrenophora tritici-repentis. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes; OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; OC Pyrenophora. OX NCBI_TaxID=45151 {ECO:0000313|EMBL:PZD42011.1, ECO:0000313|Proteomes:UP000248883}; RN [1] {ECO:0000313|EMBL:PZD42011.1, ECO:0000313|Proteomes:UP000248883} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=29685100; DOI=10.1186/s12864-018-4680-3; RA Moolhuijzen P., See P.T., Hane J.K., Shi G., Liu Z., Oliver R.P., RA Moffat C.S.; RT "Comparative genomics of the wheat fungal pathogen Pyrenophora tritici- RT repentis reveals chromosomal variations and genome plasticity."; RL BMC Genomics 19:279-279(2018). CC -!- FUNCTION: Catalyzes the hydrolysis of cutin, a polyester that forms the CC structure of plant cuticle. {ECO:0000256|RuleBase:RU361263}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Cutin + H(2)O = cutin monomers.; EC=3.1.1.74; CC Evidence={ECO:0000256|RuleBase:RU361263}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU361263}. CC -!- SIMILARITY: Belongs to the cutinase family. CC {ECO:0000256|RuleBase:RU361263}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PZD42011.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MUXC01000660; PZD42011.1; -; Genomic_DNA. DR Proteomes; UP000248883; 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 SMART; SM01110; Cutinase; 1. DR SUPFAM; SSF53474; SSF53474; 1. DR PROSITE; PS00155; CUTINASE_1; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|RuleBase:RU361263}; KW Secreted {ECO:0000256|RuleBase:RU361263}; KW Serine esterase {ECO:0000256|RuleBase:RU361263}. FT DOMAIN 1..146 FT /note="Cutinase" FT /evidence="ECO:0000259|SMART:SM01110" SQ SEQUENCE 149 AA; 15054 MW; 2070EF7B04877890 CRC64; MTVIFARGTG EMGNVGTVSG PPMFKAIRVK LGNDRVTVQG VDYAASAAGN INLGGDGGQK MADLVQLAKK QCPSTKIILS GYSQGAMVVH NAFSKGVSAG DVAGAVLFGD PLKRQAISGL AADKVKHHLS YGSSAEAAAT FAIQAAGFA //