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Database: UniProt
Entry: A0A2C6AI57_9HYPO
LinkDB: A0A2C6AI57_9HYPO
Original site: A0A2C6AI57_9HYPO 
ID   A0A2C6AI57_9HYPO        Unreviewed;      1010 AA.
AC   A0A2C6AI57;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   16-JAN-2019, entry version 7.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=CDD83_856 {ECO:0000313|EMBL:PHH91341.1};
OS   Cordyceps sp. RAO-2017.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Cordycipitaceae;
OC   Cordyceps.
OX   NCBI_TaxID=2004951 {ECO:0000313|EMBL:PHH91341.1};
RN   [1] {ECO:0000313|EMBL:PHH91341.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1346 {ECO:0000313|EMBL:PHH91341.1};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PHH91341.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1346 {ECO:0000313|EMBL:PHH91341.1};
RA   De Bekker C., 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   Submitted (OCT-2017) 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}.
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:PHH91341.1}.
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DR   EMBL; NJEV01000118; PHH91341.1; -; Genomic_DNA.
DR   OrthoDB; 179316at2759; -.
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   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869}; 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_5012699708.
FT   DOMAIN      393    570       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1010 AA;  110728 MW;  2313E2D3B20E4E10 CRC64;
     MKLSTAVLAV LGLPATWALS LTGDGGRPLY IVSENEKRAP LQDIVTWDEN SLFIHGERAM
     MFSGEFHPFR LPVPSLYLDI FQKIRALGFN MVSFYVDWAL LEGKPGEFRA DGIFDLEPFF
     EAAKRAGIYL LARPGPYINA EVSGGGFPGW LQRIKGVLRT DEGDYLSTTE NYMANICAII
     AKHQITRGGP VVLFQPENEY SSGTGIKFPN GKYFQYVIDQ ARKAGIVVPM INNDVGPVGF
     YAPGTGVGAM DIYGHDNYPL GFDCANPSDW PPNRFPTNFH QLHMKQSPKT PFSIVEFQGG
     SFDPWGGQGL EKCSALINHE FERVYYKNNI AAGVRIFNVY MIFGGTNWGN LGHPGGYTSY
     DYGACIRENR VIDREKYSEL KLEAEFLRVS PGYLETTPRN ATRGIFSDSE DITITPLVSK
     GKGNFYVTRH TDYAFPASAA YTLKLPTSEG TLIIPQSDRL LTLPGRDSRI HVTDYPVGDH
     FLLYSTAEIL TWKKFADRTV LVLYGGLGES HEFAVRSDAK MTRLEGDSYS LESMNGKAAI
     VAWTPALGRQ IAQIGDLVIY MLDRNSAYNY WVPVLPKDGS AYGSSLMNPE SIIVNGGYLI
     RSASVSGSTL SLKADFNAST TLEIIGVPKG VSKLQVNGIQ LGYTVRSGNW IAKPQIAIPK
     VAVPDLASLK WHRLDSLPEI QPGYDDSAWP VADLKTTSNS VFSLQTPVSL FGADYGFNTG
     TLVFRGHFTA RGDESQLKLR TSGGSAFASS VWLDGTFVGS FKNAEVAEDT LSTYGLPRPL
     RRGGRHVLTI VVDSTGLNEN FNPGTETFKA PRGIISYALG PANGTTATDI SPWKLTGNVG
     GEDYADKFRG PLNEGGLFFE RQGYHLPAPP LRRFRRGSPL DGLDRAGIAY YAARLPLALP
     ADRYDVPLSF VFDGHGTANQ TGDYRATLFV NGFQYGKYAS NIGPQTEFPV PEGILDHRGD
     NWLGLAVWAL DPAGARVPGL RLVAGTAVQS GRDRVDVVRG PSFSRRDKVY
//
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