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Database: UniProt
Entry: A0A2A9PCG4_9HYPO
LinkDB: A0A2A9PCG4_9HYPO
Original site: A0A2A9PCG4_9HYPO 
ID   A0A2A9PCG4_9HYPO        Unreviewed;       992 AA.
AC   A0A2A9PCG4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   16-JAN-2019, entry version 5.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=XA68_13462 {ECO:0000313|EMBL:PFH58602.1};
OS   Ophiocordyceps unilateralis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae;
OC   Ophiocordyceps.
OX   NCBI_TaxID=268505 {ECO:0000313|EMBL:PFH58602.1, ECO:0000313|Proteomes:UP000037136};
RN   [1] {ECO:0000313|EMBL:PFH58602.1, ECO:0000313|Proteomes:UP000037136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC16a {ECO:0000313|EMBL:PFH58602.1,
RC   ECO:0000313|Proteomes:UP000037136};
RX   PubMed=26285697; DOI=10.1186/s12864-015-1812-x;
RA   de Bekker C., Ohm R.A., Loreto R.G., Sebastian A., Albert I.,
RA   Merrow M., Brachmann A., Hughes D.P.;
RT   "Gene expression during zombie ant biting behavior reflects the
RT   complexity underlying fungal parasitic behavioral manipulation.";
RL   BMC Genomics 16:620-620(2015).
RN   [2] {ECO:0000313|EMBL:PFH58602.1, ECO:0000313|Proteomes:UP000037136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC16a {ECO:0000313|EMBL:PFH58602.1,
RC   ECO:0000313|Proteomes:UP000037136};
RX   PubMed=28970504; DOI=.1038/s41598-017-12863-w;
RA   de Bekker C., Ohm R.A., Evans H.C., Brachmann A., Hughes D.P.;
RT   "Ant-infecting Ophiocordyceps genomes reveal a high diversity of
RT   potential behavioral manipulation genes and a possible major role for
RT   enterotoxins.";
RL   Sci. Rep. 7:12508-12508(2017).
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}.
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:PFH58602.1}.
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DR   EMBL; LAZP02000276; PFH58602.1; -; Genomic_DNA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000037136; 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; 2.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF13364; BetaGal_dom4_5; 1.
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:UP000037136};
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:UP000037136};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    992       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5012043979.
FT   DOMAIN      389    569       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   992 AA;  107599 MW;  A01692CA6EF09508 CRC64;
     MKLSSTLLAA LAMAMSHALS LAGRPVKVLD VDKRAPLQDL VTWDDQSLFI RGERVMMYSG
     EFHPFRLPVP SLYLDIFQKI RALGFNLVSF YVDWALLEGK PGEFRADGIF DLEPFFDAAK
     KAGIYLLARP GPYINAEVSG GGFPGWLQRI KGILRTDAGD FLSTTDNYMA HICAIIAKHQ
     ITQGGPVVLF QPENEYSYGY RIPFPNGNYM QYVIDQARKA GIVVPTINND IGPGGNYAPG
     TGRGAMDIYG HDNYPLGFDC ANPSTWPSEK FPTNFHELHM KQSPNTPFSI IEFQGGSYDP
     WGGTGLEQCS ALINHEFERV YYKNNMAAGV RIFNVYMIFG GTNWGNLGHP GGYTSYDYGA
     AIRENGVIDR EKYSELKLEA EFLRVSPGYL VTTPGSATRG VYSANQDITV TPLLSQDAGS
     FFVVRHTNFA NTGSTTYTLR LPTSAGTLSI PQSGGELTLL GRDSKMLVTD YPVGGYTLLY
     STAEVFTWKR FADRTVLVLY GGGPDETNEF AVHGDDDQQV TQLEGSGVSL DSLAGVAVVV
     KWKTSSGRQV IKMGDLVVHL LDRNSAYKYW VPVLPSNGSA YGSSVMNPES LIVSGGYLVR
     SATISGSVLS LKADFNASTS LEIMGVPPGV SQLIVNGRPT RYSLSALGDW MAEPDIGIPK
     MVVPDLRALS WRRIDSLPEV QAGYDDSAWP VADKKKSSNT AFPSKTPVSL YGSDYGFHTG
     TLVFRGHFVA RGNESRLFLR TAGGSGFASS VWLDDTFLGS FTNTEAAAEE NNSTYRVPSL
     VSGRRHVLTV VVDNMGLNEV VNPGTETMKS PRGILDYALL SGDASANEPS VTDISPWKLT
     GNLGGEDYVD KSRGPLNEGG LFFERQAYHV PPTPSSSSSS SSSSSSSSPL LDRFTSASPW
     QGLDRAGIAF YAAELTLNYP SDKSNTFADF PVPEGILNYR GANWIGLAVW ALDAGGAKVP
     GFWLKVGTAV VTGREPVEVV NATAYAERFG AY
//
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