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Database: UniProt
Entry: W3WK50_PESFW
LinkDB: W3WK50_PESFW
Original site: W3WK50_PESFW 
ID   W3WK50_PESFW            Unreviewed;       701 AA.
AC   W3WK50;
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_14025 {ECO:0000313|EMBL:ETS74159.1};
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:ETS74159.1, 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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
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DR   EMBL; KI912120; ETS74159.1; -; Genomic_DNA.
DR   RefSeq; XP_007840797.1; XM_007842606.1.
DR   EnsemblFungi; ETS74159; ETS74159; PFICI_14025.
DR   GeneID; 19279038; -.
DR   KEGG; pfy:PFICI_14025; -.
DR   OMA; GWGKGIV; -.
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; 2.60.120.260; -; 2.
DR   InterPro; IPR026283; B-gal_1-like.
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; PF13364; BetaGal_dom4_5; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PIRSF; PIRSF006336; B-gal; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF49785; SSF49785; 1.
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     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    701       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5004833488.
FT   DOMAIN       44    366       Glyco_hydro_35. {ECO:0000259|Pfam:
FT                                PF01301}.
FT   DOMAIN      578    659       BetaGal_dom4_5. {ECO:0000259|Pfam:
FT                                PF13364}.
FT   ACT_SITE    194    194       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006336-1}.
FT   ACT_SITE    270    270       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006336-1}.
SQ   SEQUENCE   701 AA;  76731 MW;  85621C9D29C0A809 CRC64;
     MVNFQASLAL MAGIAAGWAQ QVVSETITTV SKTPAAFSYN NDTFLLHGEP FTIIGGQMDP
     QRIPYQYWRD RLSKARAMGL NTIFSYIFWN NLEPQSGNWT SDDPQNDIAE YFRIAQEEGL
     WVVLRPGPYI CGEHEWGGFP AWLNEISGMV VRTNNTPFLE ETKKYIVNLA TTSGFADLQV
     SRGGPILMVQ VENEYGSFGE NHNYTAALRD ILRESFEVPL YTNDGGVDWT LEGGQVPTVL
     AEIDGGSWAL PARDLYITDP TELGPLLDGE YYTWAPDQWG SYNSHNTTEG HDDYDASIVS
     DIAYHLGNYS ASISFYMVHG GTNFGFQNGA MWQNRTTVFT SSYDYGSPID ETGRTRALYF
     KMREAILPFT ANGSVPEPPE NLPLSSIPQF TLCQSSSLFA VRGEKTTAAS PLTMEALGQS
     YGFTLYEYKH TANASVEGQL QAGDRPRDRI LVYKNEAILG VIDSQYQHPL NVSVSLEPGD
     TLQLLVENLG RVDYYSRGNP YANHLQDQSK GIKGDVSLGE EVLEGWDMYA LQLDTLPPLE
     NCGGATSAPA SSSSAAAATA LGPGEGAAKR AGAAQTAAAA TTTTTDSPFF YRGTFVGPAI
     ANDSTMTLDT FITLPNGVKG NLWVNGFHLG RYWLVGPQQS LYLPGAVVRP EEANEVVVLE
     LEPWQMKQQT NETTVAAGMV AYGTSERVWG NQLDPDCLAC V
//
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