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Database: UniProt
Entry: A0A137QU55_9AGAR
LinkDB: A0A137QU55_9AGAR
Original site: A0A137QU55_9AGAR 
ID   A0A137QU55_9AGAR        Unreviewed;      1034 AA.
AC   A0A137QU55;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-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=AN958_03982 {ECO:0000313|EMBL:KXN90697.1};
OS   Leucoagaricus sp. SymC.cos.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Agaricaceae;
OC   Leucoagaricus.
OX   NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN90697.1, ECO:0000313|Proteomes:UP000070249};
RN   [1] {ECO:0000313|EMBL:KXN90697.1, ECO:0000313|Proteomes:UP000070249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SymC.cos {ECO:0000313|EMBL:KXN90697.1,
RC   ECO:0000313|Proteomes:UP000070249};
RA   Hu H.;
RT   "Leucoagaricus sp. SymC.cos WGS genome.";
RL   Submitted (JAN-2016) 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}.
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DR   EMBL; KQ962042; KXN90697.1; -; Genomic_DNA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000070249; 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   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; 2.
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:UP000070249};
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:UP000070249};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     16       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        17   1034       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007295586.
FT   DOMAIN      404    582       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1034 AA;  111270 MW;  C38A021F86CE1414 CRC64;
     MLALLLSVVL LALSCASVNL TPRNSTGLTD AVTWDSHSLS ILGQRIFILS AEFHPWRLPG
     NPDLWADVFQ KIKANGFNAV SFYVNWAVHY PTPSTNNGQG DFQTGTYRDI QGFIDEAKKA
     GLWLIARPGP YINGETTGGG FPGWVGNVAG NLRTNNPSYQ QALTAWTPYM TAISKIIARN
     QITNGGPIIL VQAENEFSAS ADHNVYMQAI IDLYRANGIV VPITHNDQHA GQAGNFSPDL
     PGTHVDIYCG DSYPQGGNSW AQVQAIYYSA HKAVAPNNPL CLAEFGGGFL LGWGSVATRG
     GTANDLTNAT YENVFYKENY AQTATILTDR VFLRYLQCVY HWHLIWIALD SSTVLFGGTN
     WGQTLEPTVY SSYDYGGGIN ENRVATSKMN EMRLQGLFLR VSRDLLGADL IANGTNYTTS
     SLTHTAELRN SITGAGFYFV RHDASTSLAL TTTQLTVRTS AGTILVPKTG AITLNGREAK
     FLVTDYVFGQ AKTKILYSTA EHFSIDGADY LLLYSPAGQE GETAFTFSSA PTVSTPPNIT
     SNFSNGLLTL HYTLTGIQTV SITTGGKKIN LLIMDKVAAN MWHAPVIAQS GNFGNFFSVG
     SNTTVLVGGP YVLRDARISG STLAMVRDSE QSPGFNQLMS SLKSGDLNGT TTIEFFAPAA
     VTALNWNGVN HSVTRTSRGS LSAIVNGTGS APALPALQDW KVMGSLPEID PGFDDSSFVT
     ADQTTTNYTN LPPLTGTQVL YSQQYGFYSF YGGNLIFRGH FTASGRETVI VTAVQFGFAG
     GYSAWLNGKF LGSAQGSASV SMTDDTWTIP SGSLHVGGDN VFVIVQANGG KEPRGIRGYS
     IIGGNTTFRS WKLQGNQGGA ANTPDTFRGY LNEGGLYAER IGAHLPGFPD STWATGSPTA
     NGVRSAGINF YRTTFNLSIP DGIDTPVRLS ITPSAISSNF RVQIYLNGWQ IGKYINNIGP
     QTLYVLPAGI LRRRSTNTLA LSLWSLDGSG VKLSGLQLVS DGIFSTSLQF EDYETPDYAE
     QQSSRPSPMN VLPM
//
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