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Database: UniProt
Entry: A0A194X7J2_9HELO
LinkDB: A0A194X7J2_9HELO
Original site: A0A194X7J2_9HELO 
ID   A0A194X7J2_9HELO        Unreviewed;      1010 AA.
AC   A0A194X7J2;
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_75555 {ECO:0000313|EMBL:KUJ16140.1};
OS   Phialocephala scopiformis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiales incertae sedis; Phialocephala.
OX   NCBI_TaxID=149040 {ECO:0000313|EMBL:KUJ16140.1, ECO:0000313|Proteomes:UP000070700};
RN   [1] {ECO:0000313|EMBL:KUJ16140.1, ECO:0000313|Proteomes:UP000070700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 120377 {ECO:0000313|EMBL:KUJ16140.1,
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; KQ947416; KUJ16140.1; -; Genomic_DNA.
DR   RefSeq; XP_018070495.1; XM_018221353.1.
DR   EnsemblFungi; KUJ16140; KUJ16140; LY89DRAFT_75555.
DR   GeneID; 28831079; -.
DR   KEGG; psco:LY89DRAFT_75555; -.
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:KUJ16140.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070700};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19   1010       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5008267944.
FT   DOMAIN      395    572       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1010 AA;  110024 MW;  6C0DF3399E4C38EE CRC64;
     MRLLRAVTAA ALAAHAAALA IGGKQMHVER ESDGLQNIVT YDEHSLMIYG ERVFVFSGEF
     HPYRLPVPDL WLDVFQKVKA LGFNVVSFYV HWALVEGEPG TYLANDVFAF EPFFAAAQQA
     GIYLIARPGP YINAESSGGG FPGWLQRVKG QLRTRAPDYL AATDNYVANI GASIAKAQIT
     NGGPVILVQP ENEYTGSSGP VDGGFPDPVY FAYVKKQLRD AGIVVPFISN DASPTGLFAP
     GDVVNGTTEG DVNIYGHDSY PLGFDCANPY TWPAGDLPTY FHATHEEQSP STFYSLDEFQ
     GGSFDPWGGL GFAQCSVLLN MEFERVFYKN DFASGAALLN LYMIFGGTNW GNLGHPGGYT
     SYDYGASITE NRELYREKYS EVKLEANFLK VSPAYLTTSV GIASTSAYTD NTSIFTTPLF
     GNGTATNFYV VRHSDYQTEV AASYKFNVAT SQGTVSIPQL GGSLTLSGRD SKWHVTDYDL
     GGTTLLYSSA EIFTWKKFDN KTALVVYGGP GEQHELAVVS SSSAQTLEGD GVTTKAMNGT
     AILNWQTSST RRVVQVGSLF VYILDRNSAY NYWVPDFVRS DEWGAYTSNI GNTTSVIVEA
     GYLVRSVYIE GTALHIDGDL NATVPIKVIG APASTKDLHF NSLKLSFTTD PVTGEWSSTL
     PYTAPQITLP DLSTLDWKYV DNLPEISSSY DDSAWTSADH TTSNNTVFKL QTPTSLFSSD
     YGYHTGVLLY RGHFTANGQE TTLQIETQGG SAFGSSVWLN STYIGSWPGI DASSAWNSTY
     ILPNLVSGKP YIFTVVIDNN GLDENWVVGP DEMKDPRGIL NYSLDGHSQS DISWKLTGNL
     GGEAYIDKVR GPLNEGGLYA ERQGWTQPYP PNHNWVSGSP ETGISTAGVA FYQADFSLDL
     PNNYDIPLTF DFGNTTINGA TADYRAQLWV NGYQFGKYTN NVGPQSSFPV PQGILDYHGQ
     NWLAIELWAQ QASGAHLTNF SLGTGTVAWT SMPRPAMAPI PSYSKRPGAY
//
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