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Database: UniProt
Entry: A0A0M8MWQ6_9HYPO
LinkDB: A0A0M8MWQ6_9HYPO
Original site: A0A0M8MWQ6_9HYPO 
ID   A0A0M8MWQ6_9HYPO        Unreviewed;      1001 AA.
AC   A0A0M8MWQ6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   28-FEB-2018, entry version 11.
DE   SubName: Full=Putative beta-galactosidase A {ECO:0000313|EMBL:KOS20896.1};
GN   ORFNames=ESCO_004213 {ECO:0000313|EMBL:KOS20896.1};
OS   Escovopsis weberi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae;
OC   Escovopsis.
OX   NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS20896.1, ECO:0000313|Proteomes:UP000053831};
RN   [1] {ECO:0000313|EMBL:KOS20896.1, ECO:0000313|Proteomes:UP000053831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA   Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA   Currie C., Gerardo N.M.;
RT   "The genome of the fungus Escovopsis weberi, a specialized disease
RT   agent of ant agriculture.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
CC       galactose residues in beta-D-galactosides.
CC       {ECO:0000256|SAAS:SAAS00108875}.
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:KOS20896.1}.
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DR   EMBL; LGSR01000013; KOS20896.1; -; Genomic_DNA.
DR   EnsemblFungi; KOS20896; KOS20896; ESCO_004213.
DR   Proteomes; UP000053831; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.102.20.10; -; 1.
DR   Gene3D; 2.60.120.260; -; 3.
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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000053831};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053831};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25   1001       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5005818770.
FT   DOMAIN      386    540       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1001 AA;  109658 MW;  524AA5573FF0350D CRC64;
     MSSCIRLLSL LVAALTALPG SGHAAILAGR PPDQIPDTQP LQDLVTWDER SLFIRGERAF
     IFSGEVHPFR LPVASLYMDV FEKIKALGFN TVAFYIDWAL LEGTPGEVRA EGIFDLQPFF
     DAALSAGVYL IARPGPHING QVSGGGYPGW LQKVHGILRT DAEDYLNATE NYMEKILTII
     AKAQITNGGP VILVQAEDEY SMSKGGILFP NHAYMQYIID QLRNNGILVP LISSIPGFVG
     IGAPGSGPGS VDLYGTNIYP TGFDCGHPEY WPRDGLPVDM LMHHRTNNRQ FEGGTFDSYG
     GPGHDQCAAL FNQDFERVLY KDSVAAGATV LNVYMAFGGT NWGNLGHSHV YTSNDFGAPI
     REDRSVDREK YSELKLQGQF LKVSPGLLRA KPHHVSLAIS TNSRIRITGL TSNERGNFFL
     LGGNLTLHGR DSKWHVTDYD VGDYILLYCT AEVYTWKKFK DHTVLVLYGG EDEIHEFAFL
     NPLKIKADAE IEIMEGEAPI LKRSPNNTIT VQWNTSTTRT VIRYGDLDIY MVDRNSAYKY
     WVPTLPGEGK LAAYGTSLMN ADAVIVNGGY LIRSATVRDS TLSLRADFNA STTLEIIGAP
     VDAITLKVNG QRCHFTVSPL GNWIAKPNVE LPDVNLPDLS QLKWKQVDSL PEIHNEFDDA
     SWVEADLRIT TNPVAPLKTP VSLYGSDYGF HSGTLVFRGS FVAIAEVSRL GLVTQGGFAF
     GSSVWLDDTF VGSFKGLADA TNDSSVYNLK GLLPGKKHVL TIIVDNNGYN QNYYPGSDTM
     KEPRGILEYS LTTRDGTEIA ISSWRIAGNL GGEAYQDKLR GPLNEGGLFF ERQGYHLPSP
     PEKVFTSGSP LDGISGAGVV FYSAKLTLDI AADKYDVPLS FVFDNTTDSR PYRAWLYVNG
     FQYGKYISHL GPQTEFIVPE GILDYNGDNW IGIGLWAVSD AGAAMPGLKL EARHAVATSR
     EEVKLVPGLK TKQATPSRGG GKSKAKAMKD HWLTGQLPVV P
//
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