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Database: UniProt
Entry: A0A0A2VIC2_BEABA
LinkDB: A0A0A2VIC2_BEABA
Original site: A0A0A2VIC2_BEABA 
ID   A0A0A2VIC2_BEABA        Unreviewed;      1010 AA.
AC   A0A0A2VIC2;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   16-JAN-2019, entry version 18.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=BBAD15_g7345 {ECO:0000313|EMBL:KGQ07343.1};
OS   Beauveria bassiana D1-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Cordycipitaceae;
OC   Beauveria.
OX   NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ07343.1, ECO:0000313|Proteomes:UP000030106};
RN   [1] {ECO:0000313|EMBL:KGQ07343.1, ECO:0000313|Proteomes:UP000030106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-5 {ECO:0000313|EMBL:KGQ07343.1,
RC   ECO:0000313|Proteomes:UP000030106};
RA   Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J.,
RA   Lu Y., Du Q., Sun Z.;
RT   "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT   bassiana D1-5.";
RL   Submitted (OCT-2012) 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:KGQ07343.1}.
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DR   EMBL; ANFO01000703; KGQ07343.1; -; Genomic_DNA.
DR   EnsemblFungi; BB8028_0005g08210.1; BB8028_0005g08210.1; BB8028_0005g08210.
DR   EnsemblFungi; KGQ07343; KGQ07343; BBAD15_g7345.
DR   Proteomes; UP000030106; 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:UP000030106};
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:UP000030106};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19   1010       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5002006914.
FT   DOMAIN      392    568       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1010 AA;  110686 MW;  1A6CC8E12B29DB74 CRC64;
     MKLSHTLLAT LAAPVAQGLT LGSRNQAYSI IREPAKKELL QDLITWDDKS LFIRGERALI
     FSGEFHPFRL PVPSLYLDVF QKIRAMGFNV VSFYVDWALV EGKPGEFRAD GIFSLEPFFK
     AATEAGVYLL ARPGPYINAE VSGGGYPGWL QRIKGILRTD APDYLKATDN YMANIGAIIA
     KAQITNGGPV ILFQPENEYS GASVSPFPNK KYMQYVIDQA RKAGIVVPLI DNDSYPGGTG
     APGTGEGEVD IYGFDSYPLG FDCARPDVWP AGNLPTDLHK THMRLSPSTP FSIIEFQGGS
     YDPFGGYGYD QCYKLVNHEF SRVFDKNNLA AGVNIFNIYM IFGGTNWGNL GHPNGYTSYD
     YGASIREDRY IDREKYSQMK LEAQFMRVSP SILEATPGDP STGVYSENKD VTITPMLSNK
     TGNFFVARHT DYQRRDSTSY TVKLPTSLGT LSIPQFGGQL TLSGRDSKFH VTDYPVGNHT
     LLYSTAEILT WKKLDGQTVV IMYGGQGELH EFALQNAMDV HHSSGSQLSY KQSNSSVIVQ
     FTATSERKVI RMGDITVFML DRNSAYNYWV PVLPKGDSAY GSSVMNPETI IVNGAYLVRS
     ASVDGKTVSI QADFNQTTSL EVIGAPNGAS ELSINGKTTS YKKTNEGTWL CNPKISFPTV
     KLPNLRSLDW HAIDSLPEIK PGYDDSRWTK ANHTTTTNPK GTPLKTPVSL YGSDYGFNTG
     NMLFRGSFVA AGNEDRLVLT TSGGQAYAAS VWINQTFLGS FAGNKNWATV IVTHAVPQLR
     AGGRYTLTVV MDSLGFNENL TPGNDDMKAP RGILDYKLHS SSSAGSDPTP ITDWKIAGNL
     GGEDYKDKFR GPLNEGGLFF ERSGFHQPLP PLDLFSKATP FDGTAGAGIT YYTAKLDLDL
     PADEYDIPLA FRFDNSSAIA APAYRALLYV NGFQYGKYIS NIGPQTEFPV PEGILNHKGE
     NWLGVSVWAL NGNGAKVPGL TLTSRPPVLT SRNKVDFIQG PSYSKRDDAF
//
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