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Database: UniProt
Entry: V5G7X1_BYSSN
LinkDB: V5G7X1_BYSSN
Original site: V5G7X1_BYSSN 
ID   V5G7X1_BYSSN            Unreviewed;      1003 AA.
AC   V5G7X1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   16-JAN-2019, entry version 24.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PVAR5_6801 {ECO:0000313|EMBL:GAD98111.1};
OS   Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS   variotii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Byssochlamys.
OX   NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD98111.1, ECO:0000313|Proteomes:UP000018001};
RN   [1] {ECO:0000313|Proteomes:UP000018001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX   PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA   Oka T., Ekino K., Fukuda K., Nomura Y.;
RT   "Draft genome sequence of the formaldehyde-resistant fungus
RT   Byssochlamys spectabilis No. 5 (anamorph Paecilomyces variotii No. 5)
RT   (NBRC109023).";
RL   Genome Announc. 2:E0116213-E0116213(2014).
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:GAD98111.1}.
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DR   EMBL; BAUL01000229; GAD98111.1; -; Genomic_DNA.
DR   EnsemblFungi; GAD98111; GAD98111; PVAR5_6801.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000018001; 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:UP000018001};
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:UP000018001};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19   1003       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5004733580.
FT   DOMAIN      393    572       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1003 AA;  110499 MW;  B01FCB67459E24AF CRC64;
     MKLLSACAVA CLALQATAAV ISHKLNGFTL VEHPDPEKRA LTQNIIKWDE HSLFIRGERI
     MIFSGEFHPF RLPVPSLWLD VFQKVKALGF NCVSFYVDWA LLEGKPGEYR ADGIFALEPF
     FDAASEAGIY LLARPGPYIN AEVSGGGFPG WLQRINGTLR TSAKDYLDAT DNYMANVGAT
     IAKAQITNGG PVILWQPENE YTGACCGAKF PDYDYMQYVI DQARNAGIVI PLISNDASPE
     GHDVPGQGVG AVDIYGHDSY PLGFDCANPT TWPEGDLPTN FRTLHLQQSP STPYSLVEGG
     AFDPWGGLGF DACASLLNHE FESVFYKNDL SFGVTILNLY MIFGGSNWGN LGHPGGYSSY
     DYGSAITESR NVTREKYSEL KLIGNFVKVS EPYLTATPGN LTTGVYTDTT DLAVTPLFGN
     GSSGSFFVLR HLDYSSQEST SYKLKLPTSA GNLTIPQLGG LLTLNGRDSK IHITDYDVAG
     TNILYSTAEV FTWKKFEDKK VLVVYGGKGE HHEIAVSGST KASVTENSSS DISIKSKGKY
     VVIAWDASST RRIVQVGDLL LFLLDKNSAY NYWVPELPTD STSPGFSTQE KTASSIIVKA
     GYLVRTAYLK NNGLYLTADF NATTPIEIIG TPKAAKSLYI NGKKVNHSVD KNGIWSTTVE
     YSEPTIKVPS LKDLEWKYID TLPEIQSSYD DSAWVVANNK SRPNLNTPTS LYSSDYGFHT
     GYLLYRGHIV ATGSETQLSI ETQGGYAFGS SIWLDSTYIG SWTGVDKYSN YNSTYKLPNL
     KRGQEYVFTV LVDNMGLDED WTVGSDEMKW PRGILKYDLQ GNNASAFKWK LTGNLGGEDY
     QDKVRGPLNE GGLYAERQGF HQPYPPVQYW KPSSPFDGLT KPGVGFYAAE LELDIPSGWD
     VPLYFTFGNS TYPPPAYRVQ LYVNGYQFGK YVNNVGPQTS FPVPEGILNY RGTNWLALSL
     WAQESDGAKL DSFELESKTP VLTALEGVQS VEQPRYKKRD GAY
//
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