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Database: UniProt
Entry: V5G2W5_BYSSN
LinkDB: V5G2W5_BYSSN
Original site: V5G2W5_BYSSN 
ID   V5G2W5_BYSSN            Unreviewed;       996 AA.
AC   V5G2W5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   16-JAN-2019, entry version 26.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PVAR5_7449 {ECO:0000313|EMBL:GAD98748.1};
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:GAD98748.1, 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:GAD98748.1}.
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DR   EMBL; BAUL01000259; GAD98748.1; -; Genomic_DNA.
DR   EnsemblFungi; GAD98748; GAD98748; PVAR5_7449.
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; 2.
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     28       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        29    996       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5004733596.
FT   DOMAIN      380    557       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   996 AA;  110539 MW;  3E8EE36468CEA6A2 CRC64;
     MAAVICIFYY TILQSLWFLS VLANPVHTSE IQERAPLQDI VTWDEYSIRV YGERVVLLSG
     EFHPFRLPSP GLWLDVFQKI RALGFSAVSF YVDWALLEGE PGHIRTEGVF SLDQFFNAAN
     EAGIYLIARP GPYINSEVSG GGFPGWLARL KGRLKTTDPD YLDAITPYIR TIGNIISKAQ
     ITQGGPVILL QPENEYTMCA NNTGYVQANN FTTNSWDTAC LEKEYMAYVE QQYRKAGIVV
     PFINNDAAPD GNFAPGTGLG AVDIYSFDDY PLGWSTAPLE PSNWSSLTDP LGGVGVQKSA
     AYINQEFERI FYKVNYGFRA AIHSLYMWIF GGTNWGNLGH PGGYTSYDVG AAIAENREVS
     REKYSELKLQ GSFLQASPAY LTSDPENGTF GVYTDTHGLV VNKLRGSPTC FYIVRHRNLT
     SFASTNYTFL VPTSIGNLTI PQLGGSLSLN GRDSKFHVVD YDIGGITLIY STAEVFTWKK
     AISKTVLVLY GGENELHEFA LPVGLGVPSA VEGRGVKIHK SISAIVLRWE VNPSRRIVIF
     DNNLEVHLLW RNEAYNYWVL DLPDPEPLGL HASEARSDEA VIMKAGYLLR TATISGHSLH
     LIGDVNATTD IEIISTPTNV SSIFFNGKEV DTRINHGRLG GTIAFKHPKF TLPDLQNSDW
     RHINSLPEIN TSYDDSKWTI CNLTKSNNPR DLSTPTSLYA SDYGYNAGSL LYRGTFTANG
     SESSIYLLTE AGYAFGYSAW LNSTYLGSWP GSAAEMFHNE TISFQKELHP GSTYILTILI
     DHMGLDENFP ANVQTMKDPR GILDYDLKGR DKSSISWKIT GNLGGERYHY LSRGPLNEGA
     LYAERQGYHL PGVPTEQWMS GTPLQGVREP GVGFFVTSFD LHIPEGYDIP LSVVFTNTTS
     EHDPSTPAKF RSELFVNGWQ FGKYINNIGP QVRYPVPEGI LNYNGSNYLA LSLWSQEKGP
     VKIDGLKLEA DAVIQSGYKK PALVEGEQYA MRSDSY
//
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