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Database: UniProt
Entry: A0A0L6WKZ8_9AGAR
LinkDB: A0A0L6WKZ8_9AGAR
Original site: A0A0L6WKZ8_9AGAR 
ID   A0A0L6WKZ8_9AGAR        Unreviewed;      1037 AA.
AC   A0A0L6WKZ8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   16-JAN-2019, entry version 17.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=J132_00738 {ECO:0000313|EMBL:KNZ75988.1};
OS   Termitomyces sp. J132.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Lyophyllaceae;
OC   Termitomyces.
OX   NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ75988.1, ECO:0000313|Proteomes:UP000053712};
RN   [1] {ECO:0000313|Proteomes:UP000053712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA   Hu H., Poulsen M.;
RT   "The genome of Termitomyces.";
RL   Submitted (JAN-2014) 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; KQ412599; KNZ75988.1; -; Genomic_DNA.
DR   EnsemblFungi; KNZ75988; KNZ75988; J132_00738.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000053712; 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:UP000053712};
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:UP000053712};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26   1037       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5005569125.
FT   DOMAIN      394    587       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1037 AA;  114157 MW;  4094CBDE2ED1A0B8 CRC64;
     MHILPSPRST LITLLGVASC LRTLAVPQEN SFPGSSNTFI NTTGLTDIVG WDSYSFYVHG
     RRIFLQSGEF HTWRLPVPAL WKDIVQKAKA AGLNALSIYI HWHLLNPKKG VVDMTGINDL
     QPLFDAAKEA GLFVIARPGP YINAETTTGG LPGHVATIPG DPFWNPYNGE IRSNDTYYHD
     AWQDYWNAVI PVIAENQITN GGPVIMVQIE NEYYNGPGQN EYVAQLRQRA LDLGIVVPTV
     INDSGEFQNL VDSADIYGID AYPVTFNCAD PTAWKDIPTT WRTYHESVTP EIPFMFPEFQ
     GGSYDPWGSK GGYAACRELT DPNFQRVHYF ALWANGVTAV NFYMFYGGTS WAQLPYTNAY
     TSYDYGAAVA ENRELSAKFG ELKLQSLFLR TFNDIYKTDY QGEDNTTFAG VTTTHLQNPD
     TGASFYITRH ITTSNPASVP LMLTVAVGST NKTVPQLSGN STLLGRDSFI ISTNLAFGSS
     KLLYSTAMLL STFQLDGNDA LVVYGKGSLV YEVSVQLDRE PAVITSGTTQ ITTKYFSVCI
     TACFGLIHSL TRVVNFAVAH GITTVALETT QKTVVILIAD YDTATNLWMP TIAGNGDLAE
     YVDIKASAPL LIRGPYLVRT ATLAQTQNAL ALTGDLTAEG STVLTVYGPS TLTSISWNGK
     ELERVKKVAG GTWQVEIVTS GASVEIPDLL QAEWRYRDSL PEIGAGFEDE SLVFANHTTT
     TNTFPPYYGG PWILYADDYG FHAGNMLWRG TFQQNDSFPV PTAINISVSG GIHFAASAWL
     NEHFLGSSDT LLATNNESWP VTRDMLVDGE NRITILQDHM GGNLAGQLVC CTPGGRQRDL
     QQPRGLQGYY LVGRPDDAQF TKWELAGNYG GEDFPDKTRK ILNEGGLYAE RKGWHLPGFD
     DSKWELRTPF QGLDKPGVGF FRTTFNLSLP KNHDIPLSIM FDDMPGHYRS QLYINGWQMG
     KRVANIGPQI SFVVHQGILN YEGENVIGVS VWGLEEDEGD LRIPSLRIVR DGGVYEGGVG
     GVGVEWWKGA GWEALRG
//
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