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Database: UniProt
Entry: A0A139GZX5_9PEZI
LinkDB: A0A139GZX5_9PEZI
Original site: A0A139GZX5_9PEZI 
ID   A0A139GZX5_9PEZI        Unreviewed;      1009 AA.
AC   A0A139GZX5;
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:KXS95688.1};
OS   Mycosphaerella eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales; Mycosphaerellaceae;
OC   Mycosphaerella.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXS95688.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXS95688.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXS95688.1,
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:KXS95688.1}.
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DR   EMBL; LFZN01000204; KXS95688.1; -; Genomic_DNA.
DR   EMBL; LFZN01000204; KXS95691.1; -; Genomic_DNA.
DR   EnsemblFungi; KXS95688; KXS95688; AC578_838.
DR   EnsemblFungi; KXS95691; KXS95691; 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   1009       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007995314.
FT   DOMAIN      400    581       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1009 AA;  111751 MW;  08AF1EED5B80E48E 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
     DEQAMPGSFD PWGGSGFLNC SKLTGPEFQR VFNKNNYGFG VTIFNTYMAY GGTNWGNLGF
     PDGYTSYDYG AVISEDRFVD RAKYSELKLQ ANFLQASPAY LSATPQTNQN ANGSYTGIES
     IAVTALLGNV TSFFVVRHAA YNSLNTTMFK IELPTSKGNI TIPQLGEHVS LSLHGRDSKL
     YVTDYDVGGV NLLYSTAEIF TWKQYDNQRV LVVYAGPGET NELAVTCKSQ PTVTEGTGIL
     SESRDGSIFL QFDSNSNRRA VEFTSCNLTL YILDRASAYR YWAVDSSPMP ALATPIIHGP
     YLVRTSTIDG TALHLTGDID CDTTVEILGG APQPLTLLTW NNVSVSFNQS RSGVVTAQIP
     FIKPVYTLPD LAFAKWKVID SLPEILPSYD DAPWPLASLN YTNNTSIRNL TTPASLYSAD
     YGFHSGHFLY RGHFTSAGNE STFFVHLQGG SAFAYSVYLN STFIASYPGK AGVGEYNETY
     TLPALAEGKE YVITILMAMM GYTENQDLGI DYPSEMKGPR GILEYDLAGR AKEVVSWKMT
     GNLLGEDYLD ESRGPLNEGG LWAERHGFHL PGAPLRDWKN GRPQEGLKEA GVQFYCADVD
     LRMPKGYDIP IAFDFGNSSG VAYQAQVWVN GWQFGRYINH IGPQKVFPVP EGIWQYRGSN
     RVCVSLWALE SKGARIEDLH LVAEREIQTG FGEVEMAPGS SWARRSGAY
//
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