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Database: UniProt
Entry: A0A284R5W9_9AGAR
LinkDB: A0A284R5W9_9AGAR
Original site: A0A284R5W9_9AGAR 
ID   A0A284R5W9_9AGAR        Unreviewed;      1033 AA.
AC   A0A284R5W9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   16-JAN-2019, entry version 8.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=ARMOST_07441 {ECO:0000313|EMBL:SJL04082.1};
OS   Armillaria ostoyae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Physalacriaceae;
OC   Armillaria.
OX   NCBI_TaxID=47428 {ECO:0000313|EMBL:SJL04082.1, ECO:0000313|Proteomes:UP000219338};
RN   [1] {ECO:0000313|EMBL:SJL04082.1, ECO:0000313|Proteomes:UP000219338}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C18/9 {ECO:0000313|EMBL:SJL04082.1,
RC   ECO:0000313|Proteomes:UP000219338};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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; FUEG01000004; SJL04082.1; -; Genomic_DNA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000219338; 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:UP000219338};
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:UP000219338};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     16       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        17   1033       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5012063364.
FT   DOMAIN      408    592       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1033 AA;  112606 MW;  3D7EE13E6D6007AF CRC64;
     MLVYLLLALF LTCNLGILVE SLHTYSRRNS TGLTDEVTWD PYSLSIYGQR VFILAAEVHP
     WRIPGDPAIW ADIFQKVKAN GFNTVSFYVN WALHYPVPDT NGGRGDFEEG TYRDIQGFID
     QAKKAGLWMI ARPGPYINGE TTGGGFPGWV GNIAGNLRSN NPNYTEAWTP YLTSISKIIA
     KNQITNGGPI ILVQAENEYS ESAGNDEYMQ AIIDLYRDNG IVIPTTHNDQ HSGQAGNFSP
     DRPGLGRVNI YWYILRSLSP SGISLVNSSG DSYPQGSNRW AQVQSIYYSA HKAVAPSNPL
     CLAEFGGGFL LQWGSVTPRG GTGYEKYSNA NGLTDATYDI YMLFGGTNWG QTAAPVSYTS
     YDYGGGVVIY FCLCARNLFQ KGINENRVAN TKMNEMRLQG LFLRVSRDLL SSDLIANSTN
     YTTSSLIHTA ELRNPITGAA FYVTRHNDST STELTTTQIR VNTSQGSLLI PQTGVLTFNG
     RESKIIVTDY VFGRSSTTIL YSTAEIMTWT TIGDTDYLIL YAPEGQTGET AFLLSTELKV
     SNLQDAPGAS ATLSDGRLTL QYTLKGSQSI PIQLQSTKFV VILLDKATAY QWHAPIIEGS
     GTFGNFFSIG TNETVLVGGP YVLRSSSLSG NTLELTGDLN GTTSVEFIAP SSISRLSWNG
     KDIPISKSSR GTFVATIQGA KVGINLPTLG DWKVSGSLPE IEPDFDDSQF VLADIRTTNY
     TNLPPLFGDV VLYSQQYGFY GGNLIFRGHF EASGDETTVK LAVQYGFAGG YTAWLNGVFL
     GSGQGNSTVS LSEDSWAIPA NTLQVGKDNV LVVVQDHTGI SETSTNGGKE PRGIRGYAIE
     GGNATFTLWR LQGNQGGAAN TPDTYRGYLN EGGLYAERIG AHLPGYPDVQ WKNGTPLSGG
     GLSRAGINFY RTTFDLRVPD SVDFPIRLSI TPSDISSNFR VQIYLNGWQV GKYINNIGPQ
     TDFVLPASVL RRSSTNTLSL SLWSLDNSGA SITGLKLISD GIFSTSFVFN DYRTPDYIEQ
     QKNRPSGTYY EPM
//
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