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Database: UniProt
Entry: G2Y4X8_BOTF4
LinkDB: G2Y4X8_BOTF4
Original site: G2Y4X8_BOTF4 
ID   G2Y4X8_BOTF4            Unreviewed;      1010 AA.
AC   G2Y4X8;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   16-JAN-2019, entry version 42.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=BofuT4P29000018001 {ECO:0000313|EMBL:CCD47718.1};
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:CCD47718.1, 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; FQ790287; CCD47718.1; -; Genomic_DNA.
DR   STRING; 40559.EDN23908; -.
DR   EnsemblFungi; CCD47718; CCD47718; BofuT4P29000018001.
DR   InParanoid; G2Y4X8; -.
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:CCD47718.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008177};
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_5003440225.
FT   DOMAIN      395    580       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1010 AA;  111784 MW;  C6DE61DDEF247AE3 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 GHGENGTFGV PAEIAVTPLF
     GAINKGTNGT RTNFYVVRHA DFTSLARTSY KFTINTSHGN ITIPQLGGSL VMNGRDSKIH
     VTDYDIGGIN MIYSSAEVFS WAKNHNNERV LILYGGDRDN NEAAFPVSLG LPNVIEGHGV
     DIRRIGEAWV LQWTVNQERR IVQIGKLRVY LLWRNEAYNY WSLELEAPAP IGNHTSPSKP
     SIIVNGGYLL RTASIEGKQL KLTGDINATT NFEVISTPTE VTSLLLNDKL LHTEKSRNGN
     IQAHISYSPP 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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