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Database: UniProt
Entry: A0A163BH30_DIDRA
LinkDB: A0A163BH30_DIDRA
Original site: A0A163BH30_DIDRA 
ID   A0A163BH30_DIDRA        Unreviewed;      1014 AA.
AC   A0A163BH30;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   16-JAN-2019, entry version 13.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=ST47_g7065 {ECO:0000313|EMBL:KZM21765.1};
OS   Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS   rabiei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Didymellaceae; Ascochyta.
OX   NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM21765.1, ECO:0000313|Proteomes:UP000076837};
RN   [1] {ECO:0000313|EMBL:KZM21765.1, ECO:0000313|Proteomes:UP000076837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ArDII {ECO:0000313|EMBL:KZM21765.1,
RC   ECO:0000313|Proteomes:UP000076837};
RX   PubMed=27091329; DOI=10.1038/srep24638;
RA   Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D.,
RA   Verma P.K.;
RT   "Draft genome sequencing and secretome analysis of fungal
RT   phytopathogen Ascochyta rabiei provides insight into the necrotrophic
RT   effector repertoire.";
RL   Sci. Rep. 6:24638-24638(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:KZM21765.1}.
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DR   EMBL; JYNV01000240; KZM21765.1; -; Genomic_DNA.
DR   EnsemblFungi; KZM21765; KZM21765; ST47_g7065.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000076837; 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:UP000076837};
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:UP000076837};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25   1014       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007841917.
FT   DOMAIN      399    578       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1014 AA;  110439 MW;  2FD2D64A759B371A CRC64;
     MKGILKLGGA VALSCFAIES AARAVGFQPD QWITPYKRDA LQDIVTWDKD SIFVHGERIF
     LYSGEIHPYR LPVPDLYLDL FQKVKALGYN GVSFYVDWAL LEGKPGEYRE EGVFDLQPFF
     DAASEAGIYL IARPGPYINA ESSGGGFPGW IQRVNGTLRT RAPDFLAATD NYMKNVGKKI
     ASAQITNGGP IILVQPENEY TQATSAIKPF PDPEYMQYVI DQLHDAGVIV PLISNDASPK
     GYNAPIPTAP GYPAVVDIYG HDGYPLGFDC ANPTVWPNNA LPTNWHDLHL KQSPNTPYSI
     LEFQAGSFDP WGGPGFDKCN ILVNAEMERV FYKNLYSFGV TVLNLYMTYG GTNWGNLGHP
     GGYTSYDYAA IIREDRRVDR EKYSEQKLQA NFFKVSPAYL TAARGNASTT AWTNTPALTV
     TPAFGNTTNF YFVRHSKYNT LDSTTYKLNI PTKAFGNITV PQVNGTSLTL NGRDSKIHVS
     DYSIGGATIV YSTAEIFTWH KYDDKTVLVV YGGPGETHEL ALAVTGLEVL EGDLKSITTR
     GYTVLNFNVD GGRKVAKIGV ESNPIYVYIV DRNEAYKYWA IDQAPHDSSS PVILKAGSLT
     RTAKVSGDTL TLTGDLNNTT SIEIIGVAST VSKVTFNGKD VSVQASKAGA LSGTVELPKA
     DISVPKLNEL EWKYIDTLPE LQADYDDSKW KAADLKKTYN SLRPLTTPVS LYSSDYGFHT
     GTLLYRGTFK ATGNETTFYV WTQGGSAFGS SIWIGDQFLG SWTGYDKATN GNSTVTLPNL
     SAGKEYTITV VIDNQGLDQT WTIGTETGKN PRGILNYKLA GHSQSDVSWK LTGNLGGEDY
     VDISRGPLNE GGLFAERNGL HQPGALSANV SWKASKGPVT DGIPAPGIGF FATEFDLDLP
     KNFDIPVSFT FTNGTSSNST GSGSSVSAYR VQLYVNGWQY GKYVNNVGPQ TNFPVPEGIL
     NYRGTNYLAI SLWGLDAGAT KIAGLELVVD GEVWGGVEVG VVEGQKYEAR EGAY
//
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