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Database: UniProt
Entry: M7U6V2_BOTF1
LinkDB: M7U6V2_BOTF1
Original site: M7U6V2_BOTF1 
ID   M7U6V2_BOTF1            Unreviewed;       624 AA.
AC   M7U6V2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Putative ser thr protein phosphatase family protein {ECO:0000313|EMBL:EMR89335.1};
GN   ORFNames=BcDW1_1995 {ECO:0000313|EMBL:EMR89335.1};
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:EMR89335.1, 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; KB707749; EMR89335.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7U6V2; -.
DR   STRING; 1290391.M7U6V2; -.
DR   HOGENOM; CLU_019028_0_0_1; -.
DR   Proteomes; UP000012045; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR   CDD; cd07407; MPP_YHR202W_N; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 2.
DR   InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR   InterPro; IPR006179; 5_nucleotidase/apyrase.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR014485; Pesterase_C1039.
DR   InterPro; IPR041823; YHR202W_N.
DR   PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR   PANTHER; PTHR11575:SF43; SER_THR PROTEIN PHOSPHATASE FAMILY (AFU_ORTHOLOGUE AFUA_3G04160); 1.
DR   PIRSF; PIRSF017316; Pesterase_C1039; 1.
DR   SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..624
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004086346"
FT   REGION          296..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          507..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..525
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   624 AA;  70026 MW;  CCE18513D9797E84 CRC64;
     MAKHLLTLTG LLTSLAAGAQ PSAPAAIAAP MRPLQWGQLN FLQTTDTHGW HAGHLQEAQY
     SADWGDYISF AEQMKKQADD KGVDLLLVDT GDRIEGNGLY DASDPKGQYT YDIFREQQID
     IICTGNHELY KADAAAREYD RTVPNFNGNY LASNLDYINP KTGEQIPMAK RYRKFTTKNQ
     GIKVVAFGFL FDFNRNANNT VVQEVEKTIK EEWFQQAIRE DADLFVVIGH VTLDGPEYKA
     IYKALRDQNW DTPIQFFGGH SHIRSYAKYD SKAYGIQSGR YMETVGWMSI EGIKKNEKEK
     TPQEEHTASA QGTEVAERAS MSFQRRYIDN NLFGYHFHTG LNETTFPTEH GKNVSRSIAK
     ARKALNLDHN FGCAPKDLWM SRAKYPSKDS LFSWLSDEVM PDVVSRLDRK DVPTIAITNT
     GAMRFDIFKG AFTRDTTFII SPFVSKFVYI KDVPIAAAEQ VLPLLNSGGN IFSSSNLDIN
     NLAPPEHLSY KTDILAPSIP ISDLPPPSNA QSPLFSSSSN HKPDLIPGYT TKDDNGSDGD
     DTIHSPITFH RVPNCIESRI NIPSTSSNPE TVDLVFIDFI KPWVLVALRF SGADYTDEDV
     NSYRNETLTE LMAGWIKENW GQDC
//
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