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Database: UniProt
Entry: M7TS86_BOTF1
LinkDB: M7TS86_BOTF1
Original site: M7TS86_BOTF1 
ID   M7TS86_BOTF1            Unreviewed;      1010 AA.
AC   M7TS86;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   16-JAN-2019, entry version 27.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=BcDW1_4870 {ECO:0000313|EMBL:EMR86471.1};
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:EMR86471.1, 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
RT   rot of grape berries.";
RL   Genome Announc. 1:E0025213-E0025213(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000256|RuleBase:RU000675,
CC         ECO:0000256|SAAS:SAAS01116863};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
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DR   EMBL; KB707857; EMR86471.1; -; Genomic_DNA.
DR   EnsemblFungi; EMR86471; EMR86471; BcDW1_4870.
DR   Proteomes; UP000012045; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.102.20.10; -; 1.
DR   Gene3D; 2.60.120.260; -; 2.
DR   Gene3D; 2.60.390.10; -; 1.
DR   InterPro; IPR018954; Betagal_dom2.
DR   InterPro; IPR037110; Betagal_dom2_sf.
DR   InterPro; IPR025972; BetaGal_dom3.
DR   InterPro; IPR036833; BetaGal_dom3_sf.
DR   InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421; PTHR23421; 1.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF13364; BetaGal_dom4_5; 2.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF117100; SSF117100; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000012045};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012045};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21   1010       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5004085908.
FT   DOMAIN      395    580       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1010 AA;  111714 MW;  4B3BA514306984FC CRC64;
     MLIYFNLLLI SAWWIQGLFA LKVGSIQNAR IKVHKREVLQ DLVSWDEHSI IVRGERIMIY
     SGEVHPFRIP SPGLWLDIFQ KIKAMGFTGV SFYTYWGLNE GNPGQVITDG VFSLDEFFDA
     ATQAGIYLIA RPGPYINAET AAGGIPGWVL RIKGVIRSTD QDYLDSTQNY ASTIGKIIAK
     AQITNGGPVI MVQPENEYAS WPGVTNFPSQ MNKDYMAFVE QQLLDAGVVV PFVVNDNLNI
     GNFAPGSGLG EVDLYGIDAY PMRYDCGDPY IWPTYRFPKT WEVSHANYSP STPFTIGEFQ
     GGGGDGWGGV GEDRCAILTN NDAIKVQFKN TYSFRVAIFN VYMIYGGTNW GNLGYHGGYT
     SYDYGASITE DRQVWREKYS EMKLEANFLK ASAAYLTATA GHGENGTYGV PAEIAVTPLF
     GAINKGTNGT RTNFYVVRHA DFTSLARTSY KFTINTSHGN ITIPQLGGSL VMNGRDSKIH
     VTDYDIGGIN MIYSSAEVFS WAKNHNNERV LILYGGDRDN NEAAFPVSLG LPNVIEGHGV
     DIRRIGEAWV LQWTVNQERR IVQIGKLRVY LLWQNEAYNY WSLELEAPAP IGNHTSPSKP
     SIIVNGGYLL RTASIEGKQL KLTGDINATT NFEVISTPTE VTSLLLNGKL LHTEKSRNGN
     LQAHISYSPP SIDLPNFTTQ QWHYIDSLPE LHPHYDDSLW TPLDHITTNN TLNLTTPTSM
     YASDYGYHTG SLIYRGHFLS TGNETTFFAN TTGGAGFGHS IWLNSTFLGS WVGSGGNQTY
     AQTFSLPSLK SGSPYVFTVL IDHMGQDEEA PGTDAIKFPR GFLDYSLSSH PQADVIWKMT
     GNLGGEQFID RKRGPRNEGA MFAERQGYHL PNPPSDAWEI RNPVSDGIDN AGVGFFTTRF
     NLSIPEGWDV PLGFVFNGTG TAGNYRTQLF VNGWQFGKYV NNLGPQTRFP IPEGILNHQG
     TNTVALTLWS LDSEGANIGG FELAPNATIW SGYRKPTLVE GSGWSRREGY
//
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