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Database: UniProt
Entry: A0A194WY01_9HELO
LinkDB: A0A194WY01_9HELO
Original site: A0A194WY01_9HELO 
ID   A0A194WY01_9HELO        Unreviewed;      1011 AA.
AC   A0A194WY01;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-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=LY89DRAFT_709663 {ECO:0000313|EMBL:KUJ12477.1};
OS   Phialocephala scopiformis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiales incertae sedis; Phialocephala.
OX   NCBI_TaxID=149040 {ECO:0000313|EMBL:KUJ12477.1, ECO:0000313|Proteomes:UP000070700};
RN   [1] {ECO:0000313|EMBL:KUJ12477.1, ECO:0000313|Proteomes:UP000070700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 120377 {ECO:0000313|EMBL:KUJ12477.1,
RC   ECO:0000313|Proteomes:UP000070700};
RG   DOE Joint Genome Institute;
RA   Walker A.K., Frasz S.L., Seifert K.A., Miller J.D., Mondo S.J.,
RA   Labutti K., Lipzen A., Dockter R., Kennedy M., Grigoriev I.V.,
RA   Spatafora J.W.;
RT   "Full genome of DAOMC 229536 Phialocephala scopiformis, a fungal
RT   endophyte of spruce producing the potent anti-insectan compound
RT   rugulosin.";
RL   Submitted (OCT-2015) 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}.
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DR   EMBL; KQ947424; KUJ12477.1; -; Genomic_DNA.
DR   RefSeq; XP_018066832.1; XM_018217776.1.
DR   EnsemblFungi; KUJ12477; KUJ12477; LY89DRAFT_709663.
DR   GeneID; 28827502; -.
DR   KEGG; psco:LY89DRAFT_709663; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000070700; 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:UP000070700};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869, ECO:0000313|EMBL:KUJ12477.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070700};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19   1011       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5008267585.
FT   DOMAIN      405    582       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1011 AA;  112825 MW;  8BDCD9BC6761FF2C CRC64;
     MWLSRGLLLL TLVQTGFGLQ NWNIRRESVL LQNIVTYDEH SLLVHGQRIF IFGGEFHPFR
     LPVPDLWLDI FQKIKAMGYN TVSFYVNWAL IEGEPGVYRA DGIFALEPFF EAATTAGVYL
     IARPGPYINA EASGGGYPGW LQRVPGLLRT KATTYVEATA LYIKTVGEII AKAQITNGGP
     VILFQPENEY YNANLNTGTC DNYTSYDRPY NDCDADYMQG LLDMYRAAGI VLPFIDNDSS
     APSKGGIFAP EWRIDNSSKG DADIWGHDSY PLGFNCSNPT VWPDGYLYTI GYERQQTLSP
     SRFEAITEFQ GGTFDQWGGT GYEKCIQMYN EEFERVFMKN NFASAPGLIN VYMTFGGTSW
     GNMAWSQAYS SYDYASAIAE DRTLTREKYS ELKLEANFLR VTPAYSNSSV QNLTTELYTN
     NAAVAVTPLI GNGTSTNLYI MRHSNYSENS SLAYKFIANT TEGYFTVPNL GGNLTLSGRD
     SKWHVTNYQF GSHSLIYSTA EIFTWKEYKS LTLLIVYGGP GETHEIAIST NLTSNQLEGP
     KISTTSGNGS LILNWETSTT RRVIQIGDIF VYIFDRNSAY NLWVMDFESL GLWGNYSANV
     GNTTSAVVVD AGYLIRNAEF DRAGLYIEGD LNSTVPLKII GAPESAQSLF FNGAELEYSS
     NPVTNEWSTI LKYETPTIEI LDLDTLEWKF IDNLPELQPD YDDSLWTLAD HTTTNNTRRP
     LLTPTCIFAS DYGYNSGGVL IYRGHFTANG NETSLWLATQ GGMAYGSSVW LNSTYLGSTI
     DSPSYTQLNN TYNFTTSPGK SYVFTILVVN MGFEENPDPG ADQMKEPRGI LDYEFQGRNK
     TTITWKLTGN FGGEQYPDKD RGPMNEGGLF AERQAFTQPF PPSESWEAGA GFWTAGFELD
     LPYGYDIPLS FDVEPSVTNG TLDAFRAWIW VNGYQYGRYI NHIGPQTNFP VPQGILNYHG
     MNWVSVEIWA QQETGAKLAN FTLTAGVPVL TSLKTPRMAP MPSFTPRLGS Y
//
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