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Database: UniProt
Entry: A0A139GZU7_9PEZI
LinkDB: A0A139GZU7_9PEZI
Original site: A0A139GZU7_9PEZI 
ID   A0A139GZU7_9PEZI        Unreviewed;      1002 AA.
AC   A0A139GZU7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   16-JAN-2019, entry version 13.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=AC578_838 {ECO:0000313|EMBL:KXS95692.1};
OS   Mycosphaerella eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales; Mycosphaerellaceae;
OC   Mycosphaerella.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXS95692.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXS95692.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXS95692.1,
RC   ECO:0000313|Proteomes:UP000070133};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana
RT   suggests a link between parallel evolutionary changes in
RT   Pseudocercospora fijiensis and Pseudocercospora eumusae and increased
RT   virulence on the banana host.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KXS95692.1}.
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DR   EMBL; LFZN01000204; KXS95689.1; -; Genomic_DNA.
DR   EMBL; LFZN01000204; KXS95692.1; -; Genomic_DNA.
DR   EnsemblFungi; KXS95689; KXS95689; AC578_838.
DR   EnsemblFungi; KXS95692; KXS95692; AC578_838.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000070133; 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:UP000070133};
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:UP000070133};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24   1002       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007995316.
FT   DOMAIN      393    574       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1002 AA;  111023 MW;  790FD3C068C0101A CRC64;
     MGIHSLTWIS LLWLAISLPP LRALEAGPHQ VITPYKREPL QDIVTWDEHS LFVRGQRVLF
     FSGEFHPFRL PSPSLWLDVL QKIKAVGYNA VSAYWDWALL EGKPGHYVAD GVFALEPFLE
     AAHTAGLYVL ARPGPYINAE VSGGGFPGWL QRNPGKLRTR NQSYLNATEN YLSHIGRTIA
     RYQITNGGPV ILLQPENEFS PYPELPDPVY WNYVEHQYRN AGVVVPFINN DSPPYGYFAP
     GPPQRLNAVV DIYGHDGYPI GFDCSNPDQW PDAGLPTNWG DLHQKQSPST PYSIVEFQGG
     SFDPWGGSGF LNCSKLTGPE FQRVFNKNNY GFGVTIFNTY MAYGGTNWGN LGFPDGYTSY
     DYGAVISEDR FVDRAKYSEL KLQANFLQAS PAYLSATPQT NQNANGSYTG IESIAVTALL
     GNVTSFFVVR HAAYNSLNTT MFKIELPTSK GNITIPQLGE HVSLSLHGRD SKLYVTDYDV
     GGVNLLYSTA EIFTWKQYDN QRVLVVYAGP GETNELAVTC KSQPTVTEGT GILSESRDGS
     IFLQFDSNSN RRAVEFTSCN LTLYILDRAS AYRYWAVDSS PMPALATPII HGPYLVRTST
     IDGTALHLTG DIDCDTTVEI LGGAPQPLTL LTWNNVSVSF NQSRSGVVTA QIPFIKPVYT
     LPDLAFAKWK VIDSLPEILP SYDDAPWPLA SLNYTNNTSI RNLTTPASLY SADYGFHSGH
     FLYRGHFTSA GNESTFFVHL QGGSAFAYSV YLNSTFIASY PGKAGVGEYN ETYTLPALAE
     GKEYVITILM AMMGYTENQD LGIDYPSEMK GPRGILEYDL AGRAKEVVSW KMTGNLLGED
     YLDESRGPLN EGGLWAERHG FHLPGAPLRD WKNGRPQEGL KEAGVQFYCA DVDLRMPKGY
     DIPIAFDFGN SSGVAYQAQV WVNGWQFGRY INHIGPQKVF PVPEGIWQYR GSNRVCVSLW
     ALESKGARIE DLHLVAEREI QTGFGEVEMA PGSSWARRSG AY
//
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