CUTI1_VERDA
ID CUTI1_VERDA Reviewed; 295 AA.
AC A0A2J8C362;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Cutinase 11 {ECO:0000303|PubMed:29068240};
DE EC=3.1.1.74 {ECO:0000305|PubMed:29068240};
DE AltName: Full=VdCUT11 {ECO:0000303|PubMed:29068240};
DE Flags: Precursor;
GN ORFNames=VD0003_g7577 {ECO:0000312|EMBL:PNH49577.1},
GN VDGD_07784 {ECO:0000312|EMBL:RBQ90445.1},
GN VDGE_07784 {ECO:0000312|EMBL:RXG42413.1},
GN VEDA_01118 {ECO:0000303|PubMed:29068240};
OS Verticillium dahliae (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=27337 {ECO:0000312|Proteomes:UP000236507};
RN [1] {ECO:0000312|Proteomes:UP000236507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12251 {ECO:0000312|Proteomes:UP000236507};
RA Armitage A., Cockerton H., Fan R., Harrison R.;
RT "Vegetative compatibility groups explain variation in the virulence of
RT Verticillium dahliae on strawberry.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000252987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gwydir1A3 {ECO:0000312|Proteomes:UP000252987};
RA Gardiner D.M.;
RT "Genome of an Australian isolate of Verticillium dahliae pathogenic on
RT cotton.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|Proteomes:UP000288725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Getta Getta;
RA Gardiner D.M.;
RT "Genome of Verticillium dahliae isolate Getta Getta.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE, ACTIVE
RP SITE, AND MUTAGENESIS OF SER-113; ASP-198 AND HIS-210.
RC STRAIN=Vd991;
RX PubMed=29068240; DOI=10.1094/mpmi-06-17-0136-r;
RA Gui Y.J., Zhang W.Q., Zhang D.D., Zhou L., Short D.P.G., Wang J., Ma X.F.,
RA Li T.G., Kong Z.Q., Wang B.L., Wang D., Li N.Y., Subbarao K.V., Chen J.Y.,
RA Dai X.F.;
RT "A Verticillium dahliae Extracellular Cutinase Modulates Plant Immune
RT Responses.";
RL Mol. Plant Microbe Interact. 31:260-273(2018).
CC -!- FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters
CC found in the cell wall of plants (PubMed:29068240). May degrade cutin,
CC a macromolecule that forms the structure of the plant cuticle
CC (PubMed:29068240). May also degrade suberin, a specialized
CC macromolecule found in the cell wall of various plant tissues
CC (PubMed:29068240). Allows pathogenic fungi to penetrate through the
CC cuticular barrier into the host plant during the initial stage of
CC fungal infection (By similarity). Involved in pathogenesis
CC (PubMed:29068240). {ECO:0000250|UniProtKB:P00590,
CC ECO:0000269|PubMed:29068240}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC Evidence={ECO:0000305|PubMed:29068240};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29068240}.
CC -!- INDUCTION: Induced during infection of cotton.
CC {ECO:0000269|PubMed:29068240}.
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: Normal cell population growth and colony
CC morphology. {ECO:0000269|PubMed:29068240}.
CC -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR EMBL; PHNV01000284; PNH49577.1; -; Genomic_DNA.
DR EMBL; QEPA01000443; RBQ90445.1; -; Genomic_DNA.
DR EMBL; RSDZ01000132; RXG42413.1; -; Genomic_DNA.
DR OMA; CPNTREV; -.
DR Proteomes; UP000236507; Unassembled WGS sequence.
DR Proteomes; UP000252987; Chromosome 2.
DR Proteomes; UP000288725; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0044409; P:entry into host; IMP:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR000675; Cutinase/axe.
DR PANTHER; PTHR33630; PTHR33630; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF01083; Cutinase; 1.
DR SMART; SM01110; Cutinase; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Hydrolase; Secreted; Signal; Virulence.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..295
FT /note="Cutinase 11"
FT /evidence="ECO:0000255"
FT /id="PRO_5029353846"
FT DOMAIN 260..295
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 228..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..258
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 113
FT /evidence="ECO:0000269|PubMed:29068240"
FT ACT_SITE 198
FT /evidence="ECO:0000269|PubMed:29068240"
FT ACT_SITE 210
FT /evidence="ECO:0000269|PubMed:29068240"
FT DISULFID 25..102
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 184..202
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT MUTAGEN 113
FT /note="S->A: Loss of enzymatic activity and attenuates
FT virulence; when associated with A-198 and A-210."
FT /evidence="ECO:0000269|PubMed:29068240"
FT MUTAGEN 198
FT /note="D->A: Loss of enzymatic activity and attenuates
FT virulence; when associated with A-113 and A-210."
FT /evidence="ECO:0000269|PubMed:29068240"
FT MUTAGEN 210
FT /note="H->A: Loss of enzymatic activity and attenuates
FT virulence; when associated with A-113 and A-198."
FT /evidence="ECO:0000269|PubMed:29068240"
SQ SEQUENCE 295 AA; 29632 MW; 9A59F850985529AA CRC64;
MQTSALLLAA QALVASAGLI ERQSCPSIHV FGARETTVGP GYGSAGTVVN LILNAYPGST
AEAIVYPACG GQSSCGGISY GNSAMQGTNA VASAVNSFNQ RCPNTQIVLV GYSQGGQIMD
NALCGGGDPG SGITNTAVPL TASAVTAVKA AILMGSPRYR AGFPYNVGTC TAQGFAARPA
GFVCPSGSKI QNYCDSPDPY CCTGNNQAVH QGYGGVYGQA ALTFVRSKLN SGGSPPTTPP
TTPPTTPPTT PPTTPPPSGS CAALYGQCGG QGWNGATCCS QGTCRASNQW YSQCL
