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Database: UniProt
Entry: M7THI5_BOTF1
LinkDB: M7THI5_BOTF1
Original site: M7THI5_BOTF1 
ID   M7THI5_BOTF1            Unreviewed;       725 AA.
AC   M7THI5;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Putative sterol esterase protein {ECO:0000313|EMBL:EMR80604.1};
GN   ORFNames=BcDW1_10764 {ECO:0000313|EMBL:EMR80604.1};
OS   Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR80604.1, ECO:0000313|Proteomes:UP000012045};
RN   [1] {ECO:0000313|Proteomes:UP000012045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX   PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA   Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT   "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT   grape berries.";
RL   Genome Announc. 1:E0025213-E0025213(2013).
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DR   EMBL; KB708114; EMR80604.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7THI5; -.
DR   STRING; 1290391.M7THI5; -.
DR   HOGENOM; CLU_024238_0_0_1; -.
DR   Proteomes; UP000012045; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR006693; AB_hydrolase_lipase.
DR   PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR   PANTHER; PTHR11005:SF160; STEROL ESTERASE 1-RELATED; 1.
DR   Pfam; PF04083; Abhydro_lipase; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        176..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          275..362
FT                   /note="Partial AB-hydrolase lipase"
FT                   /evidence="ECO:0000259|Pfam:PF04083"
FT   REGION          17..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          228..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   725 AA;  82237 MW;  6F0B171E868D0960 CRC64;
     MTSRFNSKKF EYVRYSAMPN EPEPESAYAD QAAKLSHVDP EDDHDGAGTA MRADYLTARD
     TVVVTEGGGR LPGPPLEESE RLNGLRRQAR GVGGNMISEV ERSEEIVGEE NRLAAGEKAK
     DSHDVGGNDG QTTGQGSLQK TMPPSQTHPL FPPLPLYGPS SFTRNLQCWT FRTTSFFITC
     AVLVTIMMGA GVMTVPAIFS YLWCKATFRD PWQGRVFYEE EKLRKRKRQE EENRWKKKNR
     QKLSKEKVND IEDDAGQGDF VPTEGGKDPL VCDVGYYARR VGLDVEELKV QTEDGFVIVL
     WHVYDPSEYT PMTAEQRAAR GPELFTGRGP SRPLSSDHNR QSKYPVLMIH GLLQSSGAYC
     TNDDHSLAFY LCKQGYDVWL GNNRCGFTPE HTLLDYADPR MWSWNIRQMG VLDLPALTSR
     VLSETGFPKL ALIGHSQGTT QTFVALAKEQ RPELGEKISV FCALAPAAYA GPLIDKGYFK
     FVRLISPSFF RIIFGIHAFL PYMMVFHKII PGKIFGTLGY HVFHLLFRWS DARWDKGTRD
     RCFQFAPVYV SAESMRWWLG MDGFAKHGCI LSTKEESMQE DEEDRLETLE NEGKREPKRS
     RAWYNEQVPP FALWVSGSDD LVDGRKLLQR FEKGREPCLK VVHQKVIEEY EHLDVIWAVD
     VLQKVGREVK EVVWKTCSAP DRSNCRVPLG CERVGVWDGV ERSGIFESRD FAESCQNQSD
     SDLTL
//
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