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Database: UniProt
Entry: A0A168ETR1_9HYPO
LinkDB: A0A168ETR1_9HYPO
Original site: A0A168ETR1_9HYPO 
ID   A0A168ETR1_9HYPO        Unreviewed;      1015 AA.
AC   A0A168ETR1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   16-JAN-2019, entry version 17.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=AAL_02688 {ECO:0000313|EMBL:KZZ99137.1};
OS   Moelleriella libera RCEF 2490.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC   Moelleriella.
OX   NCBI_TaxID=1081109 {ECO:0000313|EMBL:KZZ99137.1, ECO:0000313|Proteomes:UP000078544};
RN   [1] {ECO:0000313|EMBL:KZZ99137.1, ECO:0000313|Proteomes:UP000078544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 2490 {ECO:0000313|EMBL:KZZ99137.1,
RC   ECO:0000313|Proteomes:UP000078544};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
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:KZZ99137.1}.
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DR   EMBL; AZGY01000004; KZZ99137.1; -; Genomic_DNA.
DR   EnsemblFungi; KZZ99137; KZZ99137; AAL_02688.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000078544; 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:UP000078544};
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:UP000078544};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     17       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        18   1015       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007896633.
FT   DOMAIN      393    571       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1015 AA;  111076 MW;  8B4FA8BB18612EC6 CRC64;
     MKFSALSAAL LLPLSQALRL TGSGGQSYRI ILETDKRAPN IRDFVTWDEH SLFIRGERAM
     MFSGEVHPFR LPVPSLYIDL MEKIKALGFN LVSFYVDWAL VEGKPGEFRA DGIFALEPFF
     RAAKEAGIYL LARPGPYINA EVSGGGFPGY LQRLKGVLRS QAPDFLNATD NYMANVCKII
     AQHQITNGGP IVLFQPENEY SFGHNIPFPN GQYMQYVINQ ARSAGVSVPM INNDVGPYGY
     YAPGSGVGAM DIYGHDNYPL GFDCANPTVW PANSLPTNFH QLHLKQSPKT PYSIVEFQGG
     SYDPWGGPGF EKCAALVNNE FSRVFYKNNL AAGITIFSLY MIFGGTNWGN LGHPGGYTSY
     DYGACIRENR VIDRENYAEI KLQGQFLKVS PGYITSSVGA ASTSLFSDNA GITVTPLTGN
     KTGNYFIARQ TDHTATGTLS YTLKLPTANG TLTIPQRGGT LSLHGRDSKI HLTDYPVGDS
     TLLYTTAEVF TWKKYADKTV LILYGGPDEL HEFAVSAPFE AKVTQVEGDN ISARAESFSI
     IVQWRTGPKR QFVRVGNLAI YLVDRNTAYT YWVPLLPGPG ASQYGTSLMN PEAVIVAGAY
     LIRSASLSGT TLSIRADFNG STPLEVIGFP PTVNKVSVNG KLLKHTTTAT GTLLTQPEVN
     IPRIQLPELA TLSWYSVDSL PEVQAKFDDS RWPVADKKPD VKPEATYKVS NFTVQDASPV
     SLYGSDYGFN TGTLVFRGHF TSTGSEKSFR VWTTGGTAYA SSVWLDDRFL GSFKNSDRAE
     DANSTYNLPN LRSGQKCVLT VVVDSMGLNE NLNSGYDDMK VPRGIFSYTL EGGADISTWK
     LTGNLGGESY VDKFRGPLNE GGLFFERQGF HYPSPPVDSF VNASSPLNGV DRAGITYYTA
     NMPLNLPSET HDIPLSFVFA SPPAQGGDYR ALLYVNGFQF GKYVSNIGPQ TEFPVPEGIL
     NYKGDNWIGL ALWALDDVGA KVRGFTLKAG TPVQSSRSKV EFVRGPSYSK RQEAY
//
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