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Database: UniProt
Entry: A0A194XGL9_9HELO
LinkDB: A0A194XGL9_9HELO
Original site: A0A194XGL9_9HELO 
ID   A0A194XGL9_9HELO        Unreviewed;       995 AA.
AC   A0A194XGL9;
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_706100 {ECO:0000313|EMBL:KUJ19279.1};
OS   Phialocephala scopiformis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiales incertae sedis; Phialocephala.
OX   NCBI_TaxID=149040 {ECO:0000313|EMBL:KUJ19279.1, ECO:0000313|Proteomes:UP000070700};
RN   [1] {ECO:0000313|EMBL:KUJ19279.1, ECO:0000313|Proteomes:UP000070700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 120377 {ECO:0000313|EMBL:KUJ19279.1,
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; KQ947411; KUJ19279.1; -; Genomic_DNA.
DR   RefSeq; XP_018073634.1; XM_018217498.1.
DR   EnsemblFungi; KUJ19279; KUJ19279; LY89DRAFT_706100.
DR   GeneID; 28827224; -.
DR   KEGG; psco:LY89DRAFT_706100; -.
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; -; 2.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070700};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     16       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        17    995       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5008268278.
FT   DOMAIN      393    555       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   995 AA;  108930 MW;  00D5CF734236F212 CRC64;
     MLLHWLFFAI AQACLCFVSV THRSRNSLIP KRQWLQDLVT WDQHSLIVRG ERVMIYSGEF
     HPFRLPSPGL WLDVFQKIKA LGFTGVSFYA DWGLLEGNPG HVVTDGVFSL DQFFAAASEA
     GIYLIARPGP YINAETAAGG MPGWTLRLNG TLRSTAPDYL NATVHYLSVI GKIIADAQIT
     NGGPVIMVQP ENEYSTWPGE SFAQFPELFN RELMTFTEDR LRDAGIVVPF AINDNENMGY
     FAPGSGLGAV DIYGIDAYPF RYDCGHPYVW PTYRFPTGWQ TNHTTFSPST PFTIMEFEGG
     SGDGWGGVGE DMCAILVNNE GVRVLFKNNY SFGVTIFNTY MIYGGTNWGN LGYHGGYTSY
     DYGASITEDR QIWREKYSEM KIQANFFKVS PAYLTATAGN VGNGSFVSTS TIAVTPLWGN
     GTTTNFYVAR HSDFTSTGNA SYTLTVSTSI GNVTIPQLGG TLSMIGRDSK IHATDYDVGG
     INLSVLVLYG GESEVHEFAL PMSTGEPKLS NNSTAKVAKL GSAWVINWQF TTSRQVVTIG
     DLTVYLLWRN EAYDLWVLEL PASEPIGNFT SMSKSNVIVK AGYLLRTAII DNNTLHLTGD
     INCTTTLELI ATPSDSLTSV TFNGSPLETT KSSTNNLLAT ISFSPPEIQL PDLSSPYHEW
     KYHDSLPELS PTYNDTIWTL CTHTSTTNPL GKRTPTSLYA SDYGFHTGSL LYRGYFTSTG
     TESTFTVNIT GGVGFGHSVL LNSTFLGSWA GSGANETWIQ NFAFPVTLEV GKNYVLTVLI
     DHMGQDEEAP GTDAVKYPRG ITDFSLQGRE MEDVEWKITG NLGGEQYLDL VRGPRNEGAM
     FAERMGWHLP SPPSEGWESR SPVCDGVDGA GVGFFTTGFE LDVPSGWDVP MSFVFNGTEG
     GEEGTGGNYR AQLFVNGWQF GKYVNNLGPQ TTFPVPEGIL NYNGKNDFSL ALWSLDAAGA
     KLGGFALVPK AFIKSGYSKP ALVDSPAWVK RENAY
//
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