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Database: UniProt
Entry: W3WIS9_PESFW
LinkDB: W3WIS9_PESFW
Original site: W3WIS9_PESFW 
ID   W3WIS9_PESFW            Unreviewed;      1018 AA.
AC   W3WIS9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   16-JAN-2019, entry version 27.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PFICI_14719 {ECO:0000313|EMBL:ETS73773.1};
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:ETS73773.1, 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; ETS73773.1; -; Genomic_DNA.
DR   RefSeq; XP_007841491.1; XM_007843300.1.
DR   EnsemblFungi; ETS73773; ETS73773; PFICI_14719.
DR   GeneID; 19279732; -.
DR   KEGG; pfy:PFICI_14719; -.
DR   OMA; IDAYPMR; -.
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};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23   1018       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5004835018.
FT   DOMAIN      397    581       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1018 AA;  112330 MW;  DA351576904D9B0F CRC64;
     MAQSSFSRLF LCCLYLFTFA GAGLVRLENN GLPEPRDQLP DLVTWDKYSL SIRGERLFIF
     SGEFHPWRLP SPGLWLDVFQ KIKAMGFNAV SFYTYWGLVE GTPGAVRFDG VFALEPFFAA
     AAEAGIYLIA RPGPYINAET ALGGYPGWTA RIRAPLRGDD AEFVDATEAY AAEVGRLIAE
     AQITRGGPVV LLQPENEYDT WPGVNNSDFP AQLNRNYMEH VKQQFKDAGV VVPQMVNDHL
     NQGNWAPGSG LGETDLYGID AYPMRYDCAH PDVWPKIRWP EGWQTSHQQY SPNTPFFVAE
     FQGGSGTGWG SVNQDYCNAL VNQESVRVLW KNNYSFAIKL FNIYMTYGGT NWGNLGFRGG
     DSSYDYGAAI KENRHVWREK YSESKLEANF FKVSPAYLTS VAGNASNGSY VSTDQIATTP
     VFGTDAPTNF YVIRHADWTS LNTTNYKLIV PTSIGNISIP QLGGELTLSR RDSKIHVTDY
     DVGGVTLIYS TAEIFTWAQN QGGKRILILY GGEGELHEIA LDFSNLDRVP ICTTDTTDGK
     HRQTRNTTFI YQWTVSKERQ LLHFGDELEV HLLWRNEAYN YWAVELPAAS PISNYSSPSK
     SSVIVNGGYL IRSAEISEGL LSLTGDINAT TDIELVFDPT STVETLSFNG VQIGIEESDD
     GRRTSHIEYV PPDLALPDFA SLDWYYIDSL PEIQTSYDDS EWVTCDYTLT NNPQELVTPT
     SLYASDYGFH SGSLIYRGHF TAIGNESSLY VNITGGSGFG YSVWLNNALL SSWDGSGVAQ
     GNYTFESTIS LAGHSLSAGS QNVLTLLIDH MGQDEEAPGT DGIKLPMGLI NYSLSGHAQS
     DITWKLTGNL GGEDYQDLAR GPRNEGAMYA ERQGYHQPDP PVDDWAVASP FDDGVQGAGV
     GFYTTTFTLD VPDGYDVPLS FVFANTTTAA NYRVQLFVNG WQFGKYVANL GPQTVYPVPE
     GILNHNGLNT VAITLWSVDG SGAKVDGLSL EAEMPLWSGY RKPSLVDSPA WTQRDGAY
//
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