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Database: UniProt
Entry: A0A166DW70_9HOMO
LinkDB: A0A166DW70_9HOMO
Original site: A0A166DW70_9HOMO 
ID   A0A166DW70_9HOMO        Unreviewed;      1009 AA.
AC   A0A166DW70;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   16-JAN-2019, entry version 13.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PENSPDRAFT_754443 {ECO:0000313|EMBL:KZV68017.1};
OS   Peniophora sp. CONT.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Russulales; Peniophoraceae; Peniophora.
OX   NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV68017.1, ECO:0000313|Proteomes:UP000077086};
RN   [1] {ECO:0000313|EMBL:KZV68017.1, ECO:0000313|Proteomes:UP000077086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CONT {ECO:0000313|EMBL:KZV68017.1,
RC   ECO:0000313|Proteomes:UP000077086};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K.,
RA   Labutti K., Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T.,
RA   Yoshinaga Y., Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi
RT   Provides Insights into the Origins of Lignocellulose Decay
RT   Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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; KV424565; KZV68017.1; -; Genomic_DNA.
DR   EnsemblFungi; KZV68017; KZV68017; PENSPDRAFT_754443.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000077086; 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:UP000077086};
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:KZV68017.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077086};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24   1009       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007872408.
FT   DOMAIN      384    566       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1009 AA;  109289 MW;  56DCCD6096384648 CRC64;
     MRVSSFLAAL CGALYASLIP VSAQIKSTGL TTDVEWDSHS LYIFGQRVFV LSAEVHPWRV
     PNPDLWSDIF QKIKANGFNS VSFCVNWALH YPTPDAGGGE GDWQEGSYRD IQRFIDEAKA
     AGLWLIARPG PYINAETTGG GFPGWVGNIA GSLRTDNVNY TNAWLPYQTS ISKILAKNQI
     TNGGPIILVQ AENEFTEGAG RSDYMQAVID TLRANGIVVP LTFNDIHSGQ AGNFSPDKGG
     EGAVDIYCGD TYPQGKSKWA QTQLVYYDYH KAVAPSNPLC LAEFGDGKLM GWESNTIGGT
     GYEKYTTTLD NNEFEAIFYK DAYGQTATMF NIYMIFGGTN WGQTAEPTIY SSYDYGGALN
     ENRVVTLKMN EVRLQGAFLR VARELTGATL ISNGTNYTST PLIHTAELRN LESSSSFYIL
     RHNDSTSTEV TSTSLSVTTS EGNLEIPRSG NITLTGRDSK ILVTDFVFGT NDTSILYSTT
     EILTWSTIGD RDYLVLYAQP GENGETVLKF DGEPTVDLTE APAATSSYED GLLILNYALD
     GDQYIDIEGN STFTVVILDK TSAYNWHAPI LAGEGDFPNF FSIGSNSSVL VKGPYLVRNA
     SISEDTLRLT GDINGTTSIE FIAPPNVNSL IWNGAPYAAT PTTHRSYVAQ IKADEAVALP
     TFGTWKVSGS LPEADPNFDD SELVTADLTA TNYTNLPPLS DDVVLYSQQY DFFGGNLIFR
     GHFNASGTET GFNLTVIGGF AFAYSAFLNG QFLGSGQGDS TVAQVTNVWN VTVDMLKVGE
     DNILTVIQDH MGLAEASSNG GKEPRGLRGY EILGSNVTFS SWKIQGNQGG ARDAPDTFRG
     YLNEGGLYAE RIGAHLPGFD DSSWSSGSPL ASEGGGLSGA GVNFYRASFN WTPALNIDIP
     LRLSITPSDT GVHFRVQIYL NGWQLGKYVN NLGPQTLFVL PPGILRRQSE NTLALSLWSL
     DDEPVGLAGL EFTSDGQFSS ALNLLDHKLA LDYAPQASLR PVDIAVPPM
//
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