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Database: UniProt
Entry: G2XY18_BOTF4
LinkDB: G2XY18_BOTF4
Original site: G2XY18_BOTF4 
ID   G2XY18_BOTF4            Unreviewed;      1012 AA.
AC   G2XY18;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   16-JAN-2019, entry version 45.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=BofuT4P379000005001 {ECO:0000313|EMBL:CCD45355.1};
OS   Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD45355.1, ECO:0000313|Proteomes:UP000008177};
RN   [1] {ECO:0000313|Proteomes:UP000008177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P.,
RA   Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S.,
RA   Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M.,
RA   Pradier J.M., Quevillon E., Sharon A., Simon A., ten Have A.,
RA   Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V.,
RA   Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z.,
RA   Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C.,
RA   Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S.,
RA   Guldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M.,
RA   Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C.,
RA   Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H.,
RA   Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C.,
RA   Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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; FQ790277; CCD45355.1; -; Genomic_DNA.
DR   ProteinModelPortal; G2XY18; -.
DR   STRING; 40559.EDN20177; -.
DR   EnsemblFungi; CCD45355; CCD45355; BofuT4P379000005001.
DR   InParanoid; G2XY18; -.
DR   Proteomes; UP000008177; Unplaced contigs.
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:UP000008177};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869, ECO:0000313|EMBL:CCD45355.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008177};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19   1012       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5003440409.
FT   DOMAIN      396    573       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1012 AA;  109826 MW;  10F2B3DA6038B3C4 CRC64;
     MRFLHAFTAV ACAAQAAALS INIGGEKLVV ERDAGLQDIV TYDEHSLKVY GERIFVFAGE
     FHPYRLPVPD LWLDIFQKVK SLGLNTISFY VDWALVEGNP GHYTADGVFA FEPFFDAAKE
     AGIYLIARPG PYINAEVAGG GFPGWLQRVS GVLRSRAPDY LEATDNYMAN IASLIAKYEI
     TKGGPIILYQ PENEYSGYQG YVPGGWPDPI YFEYVKKQAR DAGVTVPFIS NDAYAGGLFA
     PGDVVNGTTV GDVDIYGHDS YPLGFDCAHP TTWPAGNLPT YFAATHEEQS PSTFYSINEF
     QGGAFDPWGG LGFQACAQLL NEQFERVFYK NDFASGVALL SLYMIYGGTN WGNLGHSGGY
     TSYDYGAAIT ENREVTREKY SELKIEANFL KVSPAYLTTT VGAAANGTYT NSNSITTTPL
     IGNGTVTNFY IVRHSDYQSL ASTAYKLTVT TSQGALTIPQ LNGSLTLSGR DSKWHVTDYD
     IGGTTLLYSS AEIFTWKKFD DKTVLVVYGG PGESHELAVI TKSSAQVIEG SGVTSKSTNG
     STILNWQTST TRRVVKVGSV FVYILDRNSA YNYWVPDFAR TDKWGAFASS IENTASVIVE
     AGYLVRSVST KGSDLRIYGD LNATVPFKVI GAPKGTKNLY FNSQKVSYKT DSTTGELSST
     LTYTAPKISL PKLSGLSWKY LDNLPEIKST YDDSAWTVAN KTSTSNPYLT PLLTPTVLNG
     PDYGYSTGVL IFRGHFTATG NESSLYIATQ GGSAFGSSVW LNSTYIGSWA GADYAEGKNS
     TYTLPNLKAG SKYTFTVLID NNGLDENWVV GVEEMKSPRG ILNYALSGHA QDSITWKLTG
     NLGGEQYIDQ VRGPLNEGGL YAERQGYTQP SPPSSSWTSG SPFKGIKSAG VGFWTSTFKL
     DLPKGYDVPL AFNFGNSTST NGTSDYRVQL WVNGWQFGKY VNNVGPQTSF PVPQGILNYN
     GQNTLAIELW AQQPSGAAVT DFTLTAGTPV LTSLKAPSLV DSPAWSKRKG AY
//
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