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Database: UniProt
Entry: A0A0W0G465_9AGAR
LinkDB: A0A0W0G465_9AGAR
Original site: A0A0W0G465_9AGAR 
ID   A0A0W0G465_9AGAR        Unreviewed;      1019 AA.
AC   A0A0W0G465;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   16-JAN-2019, entry version 14.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=WG66_4068 {ECO:0000313|EMBL:KTB43355.1};
OS   Moniliophthora roreri.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Marasmiaceae;
OC   Moniliophthora.
OX   NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB43355.1, ECO:0000313|Proteomes:UP000054988};
RN   [1] {ECO:0000313|EMBL:KTB43355.1, ECO:0000313|Proteomes:UP000054988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB43355.1,
RC   ECO:0000313|Proteomes:UP000054988};
RA   Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT   "Draft genome sequence of Moniliophthora roreri, the causal agent of
RT   frosty pod rot of cacao.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KTB43355.1}.
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DR   EMBL; LATX01001184; KTB43355.1; -; Genomic_DNA.
DR   EnsemblFungi; KTB43355; KTB43355; WG66_4068.
DR   Proteomes; UP000054988; 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:UP000054988};
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:KTB43355.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054988};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     16       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        17   1019       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5006902360.
FT   DOMAIN      380    583       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1019 AA;  112860 MW;  A50378AEF21F2E50 CRC64;
     MLCSWLVFAL FMVVLAQPPS RKASRTRFPR QTPDKTIQDI VTWDQYSLIV NGKRLAIYGG
     EVHPYRMPVH SLYLDVLQKM KSAGFNAVSI YVFWGIVEPK RGEVAFEGIR DLQPFFDAAK
     EAGLYLIARP GPYINAETSG GGFPGWGTYT PGLWRTSNTS YVEAYQNYMK TVGSLVAKNE
     ITKGGPVILF QAENEYTGWQ EPYTEDFAYE QRLMEDIRAS GVTVPITTND AYPGGHFTSV
     DIYGYDSYPN GFNCFEPYTW AAEAVPEWFW NAHMEFSPDV PNSVFEFQGG AIDGWGGAGF
     DRLDEITELS IVFYKNQLAM STTLFNIYMT YGGTNWGGIG YPGVYSSYDY GAAIAEDRTL
     REKYYEIKLQ ANFIHASPAY LTTRPMNIYA SQGSFTGNSA LKVTQVLDVV GNKTGFYVVR
     QTDASTNAVQ NYQLTVPTSL GGIKIPQIGG LLTLSGKDSK IHVVDYYAGT THLLYSSAEI
     FTWATMDEKD ILIVYGNSGE LHETAFAFNT TTLPKINIAF GSGKVESKVI LNNTLVLQYR
     TVGQTVIQVG EKILLYLLGK DLFRSQGASI NPSTLDRENA YQFWTLYPPS SGALPRFSTE
     NPVLIKGGYL MRTVSVDEGT LAITGDLNVT SSLEIIAPRA STKAITFNGK KLAVESSAYG
     TLLAKITVQL PEVKIPNLQS LQWKTADSLP EVQRTYSDTL WTTADRTQTV NPNQPNGTDV
     VLYAGEYGYH TGNILWRAHF NATGSESGFK VDVWGGTAFG YSIWLDDRFL GSWVGDASHG
     NYDQAFAFPQ PLRKGSTHVL TILQDHMGYN ENWAAAGEDF KTPRGIRSYS FIGSNSTSVS
     VWKVTGNLGG EDHIDRTRGP LNEGGLFAER QGWHLPDFDD SQWASGRPSE GLPRAGVSFY
     RTNFELNIPK GIDYPLALVV SNSTIDSHHR VQFYVNGYQF GKYVNHLGPQ TSFPIRMDHV
     AQGIFNYQGP NTLAVSLWAL DSSGAKLSFD LKLKAKIESG MAPVVNAPLT RWAPRKGAY
//
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