CUTI2_MAGO7
ID CUTI2_MAGO7 Reviewed; 214 AA.
AC G4MZV6;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Cutinase CUT2 {ECO:0000303|PubMed:17704215};
DE EC=3.1.1.74 {ECO:0000255|RuleBase:RU361263, ECO:0000305|PubMed:17704215};
DE Flags: Precursor;
GN Name=CUT2 {ECO:0000303|PubMed:17704215};
GN ORFNames=MGG_09100 {ECO:0000312|EMBL:EHA51400.1};
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507 {ECO:0000312|EMBL:EHA51400.1, ECO:0000312|Proteomes:UP000009058};
RN [1] {ECO:0000312|Proteomes:UP000009058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=Guy11 {ECO:0000303|PubMed:17704215};
RX PubMed=17704215; DOI=10.1105/tpc.107.051219;
RA Skamnioti P., Gurr S.J.;
RT "Magnaporthe grisea cutinase2 mediates appressorium differentiation and
RT host penetration and is required for full virulence.";
RL Plant Cell 19:2674-2689(2007).
CC -!- FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters
CC found in the cell wall of plants (PubMed:17704215). Degrades cutin, a
CC macromolecule that forms the structure of the plant cuticle
CC (PubMed:17704215). Required for efficient penetration of the host plant
CC cuticle by the appressorium during the initial stage of fungal
CC infection (PubMed:17704215). {ECO:0000269|PubMed:17704215}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC Evidence={ECO:0000255|RuleBase:RU361263,
CC ECO:0000305|PubMed:17704215};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17704215}.
CC -!- INDUCTION: Induced during infection; levels are increased during germ
CC tube and appressorium differentiation, and during penetration.
CC {ECO:0000269|PubMed:17704215}.
CC -!- PTM: The 2 disulfide bonds play a critical role in holding the
CC catalytic residues in juxta-position; reduction of the disulfide
CC bridges results in the complete inactivation of the enzyme.
CC {ECO:0000250|UniProtKB:P11373}.
CC -!- DISRUPTION PHENOTYPE: Decreases secreted carboxylic ester hydrolase
CC activity during growth on cutin carbon source (PubMed:17704215).
CC Decreases conidiation and results in abnormal germling morphology
CC (PubMed:17704215). Impairs penetration of the host epidermis and
CC decreases virulence in rice and wheat (PubMed:17704215).
CC {ECO:0000269|PubMed:17704215}.
CC -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR EMBL; CM001233; EHA51400.1; -; Genomic_DNA.
DR RefSeq; XP_003711207.1; XM_003711159.1.
DR ESTHER; mago7-g4mzv6; Cutinase.
DR EnsemblFungi; MGG_09100T0; MGG_09100T0; MGG_09100.
DR GeneID; 2680019; -.
DR KEGG; mgr:MGG_09100; -.
DR VEuPathDB; FungiDB:MGG_09100; -.
DR eggNOG; ENOG502SI38; Eukaryota.
DR HOGENOM; CLU_040058_2_0_1; -.
DR InParanoid; G4MZV6; -.
DR OMA; IFVWARG; -.
DR OrthoDB; 1227171at2759; -.
DR Proteomes; UP000009058; Chromosome 3.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IMP:UniProtKB.
DR GO; GO:0050525; F:cutinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0120326; P:appressorium-mediated entry into host; IMP:UniProtKB.
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 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 1: Evidence at protein level;
KW Disulfide bond; Hydrolase; Reference proteome; Secreted; Serine esterase;
KW Signal; Virulence.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|RuleBase:RU361263"
FT CHAIN 19..214
FT /note="Cutinase CUT2"
FT /evidence="ECO:0000255|RuleBase:RU361263"
FT /id="PRO_5005132179"
FT ACT_SITE 128
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 183
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 196
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 129
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 40..117
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 179..186
FT /evidence="ECO:0000250|UniProtKB:P00590"
SQ SEQUENCE 214 AA; 21602 MW; 5BDF1C705C99407C CRC64;
MQFSLSIATA ILAATASAMP VLETRQTVGT TANEFTSGGC KDVVLLYARG TTQAGNMGQE
PGPELGNALK ARLGAARVAV QGVAYSASLL GNLNPGGAPA NEATSFRTLI GQVASQCPNA
RIVVSGYSQG AALVHRAVEG ATAAVRARIA AGVTFGDTQK QQDGGRIPGL DASKTLIICN
TGDRVCEGTL IITAAHSGYG ARAGEAVDFI AARV
