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Database: UniProt
Entry: A0A2C5YEA5_9HYPO
LinkDB: A0A2C5YEA5_9HYPO
Original site: A0A2C5YEA5_9HYPO 
ID   A0A2C5YEA5_9HYPO        Unreviewed;      1007 AA.
AC   A0A2C5YEA5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   16-JAN-2019, entry version 7.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=CDD81_3070 {ECO:0000313|EMBL:PHH65211.1};
OS   Ophiocordyceps australis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae;
OC   Ophiocordyceps.
OX   NCBI_TaxID=1399860 {ECO:0000313|EMBL:PHH65211.1, ECO:0000313|Proteomes:UP000226192};
RN   [1] {ECO:0000313|EMBL:PHH65211.1, ECO:0000313|Proteomes:UP000226192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Map64 {ECO:0000313|EMBL:PHH65211.1,
RC   ECO:0000313|Proteomes:UP000226192};
RA   De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT   "Ant-infecting Ophiocordyceps genomes reveal a high diversity of
RT   potential behavioral manipulation genes and a possible major role for
RT   enterotoxins.";
RL   Submitted (JUN-2017) 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:PHH65211.1}.
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DR   EMBL; NJET01000020; PHH65211.1; -; Genomic_DNA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000226192; 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:UP000226192};
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:UP000226192};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     15       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        16   1007       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5012767507.
FT   DOMAIN      387    565       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1007 AA;  110849 MW;  301FE0140F0ED52F CRC64;
     MKLLVPLSAA FAMAALPVAN VTDSNNAKIE LLPEMQNAVT WDQHSFFIRG ERAMLFSGEV
     HPFRLPVPSL YLDVFQKIKA LGFNMVSFYP NWALLEGKPG QYRGTGIFDL EPFFEAAKKA
     GIYLLARPGP YINAEVSGGG FPGWLQRING TLRTDSPEFL KATENYMRNV CQTIAKYQIT
     NGGPIVLFQP ENEYSIGHDI PFPNGKYMQY IIHQARNAGI KVPMINNDVA PLGYYAPGTG
     LGQMDIYGHD SYPLGFNCGK PDVWPPGRLP TNFHQLHQMQ SPNTPYSIIE FQGGSFDAWG
     GHGLDKCYTL INHEFARVFN KNNFAAGVTL FSIYMIFGGT NWGNIGHPGG YTSYDYGACI
     RENRAVDREK YSEVKLEAEF LKVSPGYLVA TPAPTSPNIV VDSTAVTATL LHGNRSGSFI
     VVRHTDYSST ASVSYRLRLE TSEMSLTVPQ TGGMLTLSGR DSKVHLVDYP VGRHVLLYST
     CEVFTWKQFS SKTVLILYGG LGETHEFAVK GHHDDVLSLE GQDFSTRQDS QLGTIVRWAV
     SSQRSVLQFQ DLEVYLVDRN AAYKYWVPVL QQQDNAYGTS LMNPEAVIIN GGYLIRSASV
     AGSTLSLKAD FNTSTTLEII GSPPGVCDLE INGKVLPFVL NELGNWLVSP RVALLKIAVP
     DLSKLHWHAI DSLPEVKQGY DDSAWPVANR GTSDNSVTPL KTPVSLYASD YGFNAGTLVF
     RGHFTASGTE SQFRIDTAGG EAYATSVWLN DTFLGSFKNT QAVADGSATY ALHKLTRGAH
     YVFTVVVDNM GLNENYNPGW DVMKAPRGIL DYALTSPDGS QTPISSWKIT GNFGAEDYVD
     LSRGPLNEGG FFFERLGLHL PDPPLAEAPF VPDRSPFDPI PSPGVSFFVA KMPLSLPSLS
     HDVPLSFVFD NNTAATQRSD YRAMLFVNGF QYGRYVSNIG PQTEFPVPEG ILDYNGDNWI
     GLAIWALDAS GLTFPGLFLQ AGTAVQTARE PVEVVRAWPY WRRDGAY
//
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