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Database: UniProt
Entry: A0A0S6XGV9_9FUNG
LinkDB: A0A0S6XGV9_9FUNG
Original site: A0A0S6XGV9_9FUNG 
ID   A0A0S6XGV9_9FUNG        Unreviewed;      1011 AA.
AC   A0A0S6XGV9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   16-JAN-2019, entry version 14.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=ANO11243_031210 {ECO:0000313|EMBL:GAM85117.1};
OS   fungal sp. No.11243.
OC   Eukaryota; Fungi.
OX   NCBI_TaxID=1603295 {ECO:0000313|EMBL:GAM85117.1, ECO:0000313|Proteomes:UP000054361};
RN   [1] {ECO:0000313|Proteomes:UP000054361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No.11243 {ECO:0000313|Proteomes:UP000054361};
RA   Matsui M., Yokoyama T., Nemoto K., Kumagai T., Terai G., Arita M.,
RA   Machida M., Shibata T.;
RT   "Genome Sequence of Fungal Species No.11243, Which Produces the
RT   Antifungal Antibiotic FR901469.";
RL   Genome Announc. 3:e00118-15(2015).
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}.
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DR   EMBL; DF938583; GAM85117.1; -; Genomic_DNA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000054361; 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:UP000054361};
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:UP000054361};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22   1011       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5006632335.
FT   DOMAIN      393    570       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1011 AA;  109560 MW;  605384A194BA4315 CRC64;
     MFAPRVFATL WLMVLAGLAS ARSIAGRPGN YIIDNSKRGL LQDIVTFDNS SIFIRGERVV
     LYSGEFHPFR LPVPALWLDI FQKIKALGYN GVSFYTDWAL LEGKPGSFSA KGIFDFQPFF
     DAASTAGIYL LARPGPYINA EASGGGFPGW LARVKGVPRT ADPSYLDATA NYVKNMGNII
     AGAQITNGGP IILVQPENEY SAAEAGIKFP DPVYFNYVKQ QFRNAGIIVP FINNDAGPHG
     YDSPSSAAPV DIYGHDNYPL GFDCANPYDW PPNALPTNFY TLHEEQSPTT PYSLVEYQGG
     SFDPWGGSGF AKCLALVNEE FERVFYKNVF SFGATIFNIY MTYGGSNWGN LGHPGGYSSY
     DYGAPIAEDR TVSREKYSEA KLLANFIRAS PAYITAVPQN NFATNEFTND KSITISQSKG
     NPTNFYFVRH SAYNSQNTSY YTITIPTSQG NFTLPQLGGE LSLLGRDSNV YVSDYDVAGT
     NLLYSTADIF TWKKYAPKAV LVVYGGTGQI QELAFKSNAP ATLVEGTGAK IVSKDGIIIV
     QYVASSNRQI IRIGGGLYVH LLDRNSAYNY WTVDLPTGLS SSGDPNEGIK NAAIINGPYL
     MRTAAVNGTT MSLTGDVNMT TTIEIIGGAP KGLTSVLFNG QSLDFQLKHG SIVAATIIFR
     APDISVPNLS SVKWKTINSL PEIESGYDDS LWTEASLPYS NNTARNLTTP TSLYSFDYGF
     STGNLLYRGR FTATGSESLL YITTQGGSAY GASIWLDSTF MTSFHGFDAA ASSALTVHLP
     KLTAGAEYVI TVLTDNMGLD ENYDIGSSEA KDPRGILDFD LVGRPQNAIS WKLTGNLGGE
     DFYDPSRGPL NEGGLYIERQ GWHLPGAPTE DWAESRGPTE GINTAGVQFY STTFDLDFPD
     GYDIPLAIQF TNGTDTDSAG LSTAYRCQLY VNGFQFGKFV HNIGPQTVFP VPQGIWNYSG
     SNYLGITLWA LEGTGAKVDS ISIVAGPVVQ SGYGSVENSP ASGWTKREGA Y
//
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