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Database: UniProt
Entry: A0A0S7DIN2_9EURO
LinkDB: A0A0S7DIN2_9EURO
Original site: A0A0S7DIN2_9EURO 
ID   A0A0S7DIN2_9EURO        Unreviewed;      1011 AA.
AC   A0A0S7DIN2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-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=ALT_2670 {ECO:0000313|EMBL:GAQ05349.1};
OS   Aspergillus lentulus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=293939 {ECO:0000313|EMBL:GAQ05349.1, ECO:0000313|Proteomes:UP000051487};
RN   [1] {ECO:0000313|EMBL:GAQ05349.1, ECO:0000313|Proteomes:UP000051487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 54703 {ECO:0000313|EMBL:GAQ05349.1,
RC   ECO:0000313|Proteomes:UP000051487};
RA   Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT   "Aspergillus lentulus strain IFM 54703T.";
RL   Submitted (NOV-2015) 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:GAQ05349.1}.
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DR   EMBL; BCLY01000004; GAQ05349.1; -; Genomic_DNA.
DR   EnsemblFungi; GAQ05349; GAQ05349; ALT_2670.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000051487; 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:UP000051487};
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:UP000051487};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20   1011       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5006633824.
FT   DOMAIN      396    575       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1011 AA;  111408 MW;  34428A106BF2BE5D CRC64;
     MKFLFRRLIA LAAASLVVAA PSGRHLSLQG AANKRDLLQD LVTWDQHSLF VRGERLMVFS
     GEFHPFRLPV PGLWFDVFQK IKSLGFNAVS FYTDWGLMEG NPGHVVTDGI WSLEEFFAAA
     SEAGIYLIAR PGPYINAETS AGGIPGWVLR LKSIIRSNSE DYLRATGKYM ATLGKIIAKA
     QITNGGPVIL VQPENEYTTW PNVSESEFPT TMNKEVMAYA EKQLRDAGVV VPTVVNDNKN
     LGYFAPGTGL GETDLYGIDA YPMRYDCGNP YVWPTYRFPR DWQQTHRNHS PSTPFAIMEF
     QGGSGGGWGG VTEDGCAILV NNEAVRVVYK NNYGFGVKVF NIYMTYGGTN WGNLGYHGGY
     TSYDYGAAIT EDRQIWREKY SEEKLQANFL KVSPAYLTAT PGNGVNGSYT GNKDIAVTPL
     FGNGTTTNFY LVRHADFTST ENAEYRLQVS TSVGNVTIPQ LGGSLSLNGR DSKFHLTDYD
     VGGSNLIYSS AEVFTWAKGD NKKRVLVLYG GAGELHEIAL PKHLPRPTVV DGSDVKTAKK
     GSSWVVQWEV TAQRRVLRAG KLEIHLLWRN DAYQHWVLEL PAKQPIANYS SPSKETVIVK
     GGYLLRSASI ADNKLHLIGD VNATTALEVI TAPSRLDGIV FNGQFLKPTW SKIGNLAATV
     HYKPPAISLP ELKRLAWKYL DSLPEISRDY SDESWTPLTN TYTNNTRQFT GPTCLYADDY
     GYHGGSVIYR GHFKANGDES WVFLNTSGGV GFSNSVWLNQ TFLGSWTGSG KNMTYPRNIS
     LPHELSPGEP YFLTVVIDHM GQDEEAPGTD AIKFPRGILD YALSGHKLSD VAWKMTGNLG
     GEQYQDLTRG PLNEGAMYAE RQGYHLPEPP TSSWKSSSPI NDGLTGAGIG FYATSFSLDL
     PEGYDIPLSF VFNTSASDAR SGTSYRCQLF VNGYQFGKYV NDLGPQTNFP VPEGILNYNG
     VNYVALTLWA LEHQGALVGG LELVASTPIL SGYRKPAQAP QPRWKPRQGA Y
//
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