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Database: UniProt
Entry: F8QCG4_SERL3
LinkDB: F8QCG4_SERL3
Original site: F8QCG4_SERL3 
ID   F8QCG4_SERL3            Unreviewed;      1021 AA.
AC   F8QCG4;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   13-FEB-2019, entry version 35.
DE   SubName: Full=Glycoside hydrolase family 35 protein {ECO:0000313|EMBL:EGN93829.1};
GN   ORFNames=SERLA73DRAFT_171732 {ECO:0000313|EMBL:EGN93829.1};
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|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; GL945490; EGN93829.1; -; Genomic_DNA.
DR   EnsemblFungi; EGN93829; EGN93829; SERLA73DRAFT_171732.
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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008063};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:EGN93829.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008063}.
FT   DOMAIN      371    555       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1021 AA;  111844 MW;  B420A96BCC5DA461 CRC64;
     MVRYQARSRV LHLRKREESS VGNLTSNGRT TEVEWDSYSL VIKGQRVFIH SGEFHTFRLP
     VPGLWLDILQ KAKAAGFNAL SVYTHMALVN PSPGVIDFND YRALEPLYEA AKQTGIFIVL
     RPGPYINAES TAGGIAHWIT SQVAGELRTN ATDWRASWQD YIQGIIDQTA PYQITQGGPV
     IDNEYSQSGY GHAEYFAELE EVFHNSSIVV PLTANDPGEG RDWVNGTGAV DIYGLDSYPQ
     GFDCSNPTVW SPVVTNYYSY HESVDPSEPW YFPEFQGGSF DAWGPTAPGY DQCRVLTGAD
     FENVFNLNLW ASNAKLINYY MLYGGTSWGG LPFPGVYTSY DYGSAIAENR ELTTKYPELK
     REGLFLRSSP EFYKTSWIGN SSTSAVIVSN SSAFVTLLRN PDTSTSFYIA RQNDSTSTGI
     TTFKLNVTTS AGNLEIPQVV PEITLGGRQS KLIVTDYSFG SSNVLYSTAQ VLYAGQIGGR
     DVLYLYGDST QEHEVSLVLT GTPRLQADTP HISSHLSTGQ GTIISFLSGI EGLVTVWDSS
     EQLILYSDAD TAGTFWSPEI PSNATSGDAA TFSNYWQFGT NTSILVGGPY LVRNATITGS
     TLNLRGDLND SVRLTVIAPE TVTSITWNGM DISADVAATS NLTTQGGFVA QIQPASGISS
     IPVPTLSNWK YANSLPEIQS NFSDASWTLA NHTTTNIPFK PYYGDGRVLY GCDYEYCENI
     VLWHGHFNAT ENTKSVNLSI NGGEAFAASV WVNDVFLNTS YGNSTNNANI VDETDEKFYF
     PSGSLNYGQD NVITILQVST HIHLSSTDEL YVCVPKDNMG LDESGSEIDE EKSPRGVRGF
     QLNTGDFGEW KVQGKIGGYT NYPDKVRGVL NEGGLYGERL GWHLPGFDTS IWESRDITEG
     LPGSAAGVGF FVTTFDLQIP EYYDAPMSFT FDQSSQPYRV QLYVNGWMMG KRVANLGPQY
     KFPVHQGILN YSGPNTVAIA LWAMEPTAIS PTVALTVDGV FEGGVGGIEV NNPAWSPEGR
     Q
//
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