CUTI_PHYCP
ID CUTI_PHYCP Reviewed; 210 AA.
AC P41754; Q01764;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Putative cutinase;
DE EC=3.1.1.74;
DE AltName: Full=Cutin hydrolase;
OS Phytophthora capsici.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4784;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9508797; DOI=10.1007/s002940050330;
RA Munoz C.I., Bailey A.M.;
RT "A cutinase-encoding gene from Phytophthora capsici isolated by
RT differential-display RT-PCR.";
RL Curr. Genet. 33:225-230(1998).
RN [2]
RP SEQUENCE REVISION.
RA Munoz C.I., Bailey A.M.;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC -!- CAUTION: Does not belong to the cutinase family. We doubt this is
CC really a cutinase. {ECO:0000305}.
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DR EMBL; X89452; CAA61622.1; -; Genomic_DNA.
DR PIR; S57943; S57943.
DR AlphaFoldDB; P41754; -.
DR PRIDE; P41754; -.
DR GO; GO:0050525; F:cutinase activity; IEA:UniProtKB-EC.
PE 4: Predicted;
KW Hydrolase; Serine esterase.
FT CHAIN 1..210
FT /note="Putative cutinase"
FT /id="PRO_0000174188"
FT REGION 26..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 210 AA; 23175 MW; 2377F9B0C8575AB2 CRC64;
MALQSLPCRH GSPTIRLTAD TPIVPDSERL PLKRDEPGSR SMRSTFIPSS QCSNLSSATA
SSSRRRSCRR YQHGEAVASS STRWRTKWNL FIICLLLLCL PGLAVRYMHD MFSPCISGVA
NSQHSSSQSP RSHCRSLVPS FIAIYSASVV LCALISCFLD PYETTLPLTN VTNCLTLFRS
SGSLRSEHRC STSDSRRSRQ QLSITSRGSA