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Database: UniProt
Entry: A0A0S7E717_9EURO
LinkDB: A0A0S7E717_9EURO
Original site: A0A0S7E717_9EURO 
ID   A0A0S7E717_9EURO        Unreviewed;      1006 AA.
AC   A0A0S7E717;
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_7860 {ECO:0000313|EMBL:GAQ10539.1};
OS   Aspergillus lentulus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=293939 {ECO:0000313|EMBL:GAQ10539.1, ECO:0000313|Proteomes:UP000051487};
RN   [1] {ECO:0000313|EMBL:GAQ10539.1, ECO:0000313|Proteomes:UP000051487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 54703 {ECO:0000313|EMBL:GAQ10539.1,
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:GAQ10539.1}.
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DR   EMBL; BCLY01000016; GAQ10539.1; -; Genomic_DNA.
DR   EnsemblFungi; GAQ10539; GAQ10539; ALT_7860.
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     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19   1006       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5006634521.
FT   DOMAIN      395    573       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1006 AA;  110061 MW;  9055705E5C192066 CRC64;
     MKLLSACAVA LLAAQAAGAS IKHKLNGYTI MEHSDPAKRE LLQKYVTWDE KSLFVNGERI
     MIFSGEVHPF RLPVPSLWLD VFQKIKALGF NCVSFYVDWA VLEGKPGEYR AEGNFALEPF
     FDAAKQAGIY LLARPGPYIN AEASGGGFPG WLQRVNGTLR TSDPAYLKAT DNYIANVAAT
     VAKGQITNGG PVILYQPENE YSGACCNATF PDGDYMQYVI DQARNAGIVV PLINNDAWTG
     GHNAPGTGKG EVDIYGHDSY PLGFDCGHPS VWPKGNLPTT FRTDHLRQSP TTPYSLVEFQ
     AGSFDPWGGP GFEACAALVN HEFERVFYKN DLSFGAAILN LYMTFGGTNW GNLGHPGGYT
     SYDYGSPLTE SRNVTREKYS ELKLIGNFVK ASPSYLLATP GNLTTSGYAD TADLTVTPLL
     GNGTGSYFVV RHTDYTSQAS TPYKLSLPTS AGKLTVPQLG GTLTLNGRDS KVHVVDYNVG
     GTNILYSTAE VFTWKKFGDS KVLVLYGGPG EHHELAVSLK SDIKVAEGSD SEVTSKKVGD
     VVVVAWDVSS SRRIVQIGDL KIFLLDRNSA YNYWVPQLDK DDSSTGYSSE KTTASSIIVK
     AGYLVRTAYT KGSGLYLTAD FNATTPVEVI GAPSNVRNLY INGEKTQFKT DKNGIWSTEV
     KYSAPKINLP SMKDLNWKYL DTLPEVQSTY DDSAWRAADL DTTPNTLRPL TTPKSLYSSD
     YGFHTGYLIY RGHFVADGSE TTFDVRTQGG SAFGSSVWLN GTFLGSWTGL NANADYNSTY
     KLPQVQKGKN YVLTVVIDTM GLNENWVVGT DEMKNPRGIL SYKLSGRDAS AITWKLTGNL
     GGEDYQDKIR GPLNEGGLYA ERQGFHQPEP PSEKWKSASP LEGLSKPGIG FYSAQFELDI
     PSGWDVPLYF NFGNSTKSAY RVQLYVNGYQ YGKLVSNIGP QTSFPVPQGI LNYQGTNWVA
     LTLWALESDG AKLDDFELVN TTPVMTALSK IRPSKQPSYR QRKGAY
//
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