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Database: UniProt
Entry: W3WIY2_PESFW
LinkDB: W3WIY2_PESFW
Original site: W3WIY2_PESFW 
ID   W3WIY2_PESFW            Unreviewed;      1041 AA.
AC   W3WIY2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   16-JAN-2019, entry version 26.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PFICI_14784 {ECO:0000313|EMBL:ETS73838.1};
OS   Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Xylariomycetidae; Xylariales; Sporocadaceae;
OC   Pestalotiopsis.
OX   NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS73838.1, ECO:0000313|Proteomes:UP000030651};
RN   [1] {ECO:0000313|Proteomes:UP000030651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX   PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA   Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA   Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT   "Genomic and transcriptomic analysis of the endophytic fungus
RT   Pestalotiopsis fici reveals its lifestyle and high potential for
RT   synthesis of natural products.";
RL   BMC Genomics 16:28-28(2015).
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; KI912121; ETS73838.1; -; Genomic_DNA.
DR   RefSeq; XP_007841556.1; XM_007843365.1.
DR   EnsemblFungi; ETS73838; ETS73838; PFICI_14784.
DR   GeneID; 19279797; -.
DR   KEGG; pfy:PFICI_14784; -.
DR   OMA; GETHEFA; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000030651; 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:UP000030651};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030651}.
FT   DOMAIN      417    596       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1041 AA;  113872 MW;  69F6EBC10C23C1DB CRC64;
     MVLLRQFQQV ALFALLYFNA TLAFSNLPRV EQSTNELLQD IVTWDQYSIM VRGERVLFLS
     AEFHPFRLPS PGLWLDVFQK IKAIGFSGVS FYVNWALLEG TPGEFRADGV FALEGFFDAA
     TQAGIYLLAR PGPYINSEVS GGGYPGWTSR LKGPIRTNAT DWLDATQNYI TNIGAIISKA
     QITNGGPIIL FQPENEYTIC AAALAGADLG SIGDLGELST CLNHYYMADV EAMWREAGIV
     LPFLINDAFP IGNFAPGSGV GAGDIYGFDG YPLGWGGACF DPSNWDRENA IFPTLATNFT
     IHEQMSPSTP FSIVEFQGGT AEPWQVFIMG GAGIDSCAAL LNNEFERVFY KVVYAFRTTI
     LNLYMMFGGT NWGNLGHPLG YTSYDVGAAI NEKRQVTREK YSELKLQANF LQVSPAYLTS
     APSEGTFGIF TDTSDLVTTE LAATEEDGAF YIVRHSDWTT HSTVNYTLRI TSSGRNLTIP
     QMGGSLSLPG RDSKIHVVDY DVGGIKLDYS SAEILTWKKS TSKTVLIMYG GMGETHEFAL
     SSSSGVPTSV EGDGIRSAHL SGSTVVQWDV QSSRRVVHFG RGLEVHLLWR NSAYRYWILD
     LPKPDPVGKF VSASRVNDTD ASVIVKAGYL LRNATVSENS LHLCGDVNQT TTIEVIAAPL
     SCGATLFFNG HQVNDTRYVQ GRLTGTVKYY EPEIILPDFG ALEWKHIDSL PETTDSYDDC
     SWPLLNKTTT NNTRSLTTPT SLYASDYGFH SGSLIYRGHF EATGNESSLF LSISGGNAFG
     HSAWLNSTYL GSWAGDPNEA IHNQTFVLNS ALQPIGNYVI TVLIDHMGLT EVTFIGAEGI
     KEPRGILDYS LSGHASQSDI TWKMTGNIGG EDYLDLSRGP RNEGALFAER QGYHLPGAPI
     LDMQTRSPIA DGEVNAGVGF YATTFEMNVP AGYDAPMSFV FTNASQELNG TQPEAYRVQL
     FVNGWQFGEY VNNIGPQVSF PVPEGILDYN GENYVALTLW SLESIGAKLA GFSLVVDQAV
     QSGYTKPFLV EGQSYEQRSA Y
//
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