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Database: UniProt
Entry: A0A163K1L3_DIDRA
LinkDB: A0A163K1L3_DIDRA
Original site: A0A163K1L3_DIDRA 
ID   A0A163K1L3_DIDRA        Unreviewed;      1003 AA.
AC   A0A163K1L3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   16-JAN-2019, entry version 12.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=ST47_g2155 {ECO:0000313|EMBL:KZM26721.1};
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:KZM26721.1, ECO:0000313|Proteomes:UP000076837};
RN   [1] {ECO:0000313|EMBL:KZM26721.1, ECO:0000313|Proteomes:UP000076837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ArDII {ECO:0000313|EMBL:KZM26721.1,
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:KZM26721.1}.
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DR   EMBL; JYNV01000101; KZM26721.1; -; Genomic_DNA.
DR   EnsemblFungi; KZM26721; KZM26721; ST47_g2155.
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     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22   1003       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007843586.
FT   DOMAIN      390    567       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1003 AA;  109812 MW;  E48CA5F017B5ADEE CRC64;
     MRLNQVLAWV TLSLLPTQAT ARALGSKPSD LIIAERAPLQ DIVTWDEHSL IVHGKRVIFW
     GGEVHPFRLP VPSLWLDIFQ KIKALGYNGV SIYTPWVLHE PKSGSFQAEG VFDYEPFFDA
     AKKAGIYLVA RPGPYINAEV SGGGLPGWLQ RISGNLRTPD ADYQQASKNY IEHITPIIAK
     AQITNGGPVI LFQPENEYSA GLNNVTFPDA DYMNHLMKQF RDLGINIPLI NNVAWPSGTN
     APGTDAPVDI YGHDAYPLGM NCTVPSYWID DALPANWRET HLEQSPNTPY MLVEYQGGAY
     QPWGGDGFEK CAEFTNHEFE RVFYKNNIAA GATIFNVYMT FGGTNWGNLG HAGGYTSYDY
     GAAITEERQV HREKYSEAKL IANFVHASPA LAAAVPGYNS TAVYTDTNAI TTTPLFGNKT
     NFYVTRQTKY NSLASTSYKL KVQTSAGNLT LPQLGGQLSI NGRDSKVHVT DYDVGGFNLL
     YSTAEIFTWK KYGSRSVLVV HGGPNEQHEL AVSETGGGTA VEGSGIKFAN RNGNTILNWQ
     TDAKRRVVRI GSDLYIVIVS RNEAYNYWTV STLPEGGRYS HDATLSSDLI VHAGYLVRSA
     SVSNGKIDLI GDINATTTVE IIGGAHDNID GLSWNGKQLE VKRDRNGFLS GTIPFSAPDI
     QIPDLKSLSW KSIDALPELQ PEYNDSAWTD ADHTETKNTY WNLTTPTVLW GAEYGYNTGS
     LIFRGHFSAT GNETHMHLNV SGGSAFAFSA WVNSTFLSSW TGTGEAAIAN QTLSLPKLQR
     GSNYVLTVFI GYNEMKTPRG IHGYDFPSHT PQPANSSRAD DGIRWKITGN LGGESHRGGP
     RGPLNEGALY PERNGFHLPS APTDSWSSSA VGPTSGLQKP GVRFYQTTFQ LDMPKGWDVP
     LSFVFDGDAF TGRGRGWRAQ LWVNGYQFGK FANGIGPQRR FPVPEGIFDY HGLNTVAISI
     WALEEGGATP EGIELVAGMP VQSGYGDVAL SPMTGWEERE GAY
//
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