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Database: UniProt
Entry: F8PWB9_SERL3
LinkDB: F8PWB9_SERL3
Original site: F8PWB9_SERL3 
ID   F8PWB9_SERL3            Unreviewed;       997 AA.
AC   F8PWB9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   16-JAN-2019, entry version 41.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=SERLA73DRAFT_167797 {ECO:0000313|EMBL:EGN99924.1};
OS   Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Boletales; Coniophorineae;
OC   Serpulaceae; Serpula.
OX   NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN   [1] {ECO:0000313|Proteomes:UP000008063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX   PubMed=21764756; DOI=10.1126/science.1205411;
RA   Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA   Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M.,
RA   Blumentritt M., Coutinho P.M., Cullen D., de Vries R.P., Gathman A.,
RA   Goodell B., Henrissat B., Ihrmark K., Kauserud H., Kohler A.,
RA   LaButti K., Lapidus A., Lavin J.L., Lee Y.-H., Lindquist E., Lilly W.,
RA   Lucas S., Morin E., Murat C., Oguiza J.A., Park J., Pisabarro A.G.,
RA   Riley R., Rosling A., Salamov A., Schmidt O., Schmutz J., Skrede I.,
RA   Stenlid J., Wiebenga A., Xie X., Kuees U., Hibbett D.S.,
RA   Hoffmeister D., Hoegberg N., Martin F., Grigoriev I.V.,
RA   Watkinson S.C.;
RT   "The plant cell wall-decomposing machinery underlies the functional
RT   diversity of forest fungi.";
RL   Science 333:762-765(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; GL945479; EGN99924.1; -; Genomic_DNA.
DR   ProteinModelPortal; F8PWB9; -.
DR   EnsemblFungi; EGN99924; EGN99924; SERLA73DRAFT_167797.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000008063; 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:UP000008063};
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:EGN99924.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008063};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     17       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        18    997       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5003376786.
FT   DOMAIN      381    566       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   997 AA;  109160 MW;  2BCF8EEB8F769AB5 CRC64;
     MLFSKLVALL SATLVLASSK PRSVQKLNII RDTDGLQTNV TWDEYSLMIN GERMFMFSGE
     VHPYRMPSQS LYLDILQKVK SMGFNTVSFY VFWGIVEPKR GVISFEGFRD LQPFFDAAME
     AGIYLMARPG PYINAETTAG GFPGWGTYTP SLWRTSNTTY YEAWQNYVST TAHILAENQI
     TNGGPIILVQ SENEYTGWAP GYSEDFTYEA ELLSAWRTAG IKVPITFNDA SPEGHYLTVN
     IWGYDSYPNG FDCSSPYTWA SNAVPTYFWS AHEEYAPEEP NAVYEYQGGA FDGWGGSGYD
     TCAILTGPDF ERVFYKNELA TSTTYLNLYM IYGGTNWGGI AHPGVYTSYD YGSAIAEDRT
     LREKYYELKL QANFLRVSPA YLTTRPMNSY SNQGAFTGNQ ALLTTQVLDV VGNQTGFYVI
     RQANASSNAM EMYTLTLPTS VGNLTVPVLG GQLTLDGKDS KVHVVDYAAG ANTLLYSTAE
     ITTWATIDGR DIIVVYGNAG ELHETAFKFD GTVPAATVVS GSEQLKSETI NSTNLVIQYT
     TTGQTVVEVG SDVLLYILDR ANAYEFWVLY PPTTGAYANY STADPILVKG GYFIRSVDVS
     GSTLALLGDL NSTASFEIIA PAASSAQVTF NGEPLTLEKT SYGTLTAEKT VSLPQVNIPT
     LESLTWKTAD SLPEITPTYD DSSWTTANHT TTVNPTQPST PVVLYAGDYG YHTGNILWRA
     HFTSLGAETG FTLNVQGGSA FGYSVWLDSS FIGSWVGDAV YESYQSSFSF PGTLSKGSAH
     VLTILQDHMG YEEDWTAASD DFKAPRGLLS YSFEGSNATT VDLWKVIGNL GGEDYVDTTR
     GPLNEGGLYG ERQGWHLPDF DDSYWADGLP TNGISSAGVS FYRTTFELDI PSGVDYPMAI
     VTTNMTTNPY FRSQFYVNGY QFGKYVNSVG PQQAFPVPQG ILNYNGLNTL AVSLWAHENE
     GAKLSSIALE VLAQVESSMA AVVNQPMPPW TPRPGAS
//
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