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Database: UniProt
Entry: A0A165M871_EXIGL
LinkDB: A0A165M871_EXIGL
Original site: A0A165M871_EXIGL 
ID   A0A165M871_EXIGL        Unreviewed;      1072 AA.
AC   A0A165M871;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-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=EXIGLDRAFT_726788 {ECO:0000313|EMBL:KZV98894.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV98894.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV98894.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV98894.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K.,
RA   Labutti K., Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T.,
RA   Yoshinaga Y., Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi
RT   Provides Insights into the Origins of Lignocellulose Decay
RT   Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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; KV425914; KZV98894.1; -; Genomic_DNA.
DR   EnsemblFungi; KZV98894; KZV98894; EXIGLDRAFT_726788.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000077266; 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:UP000077266};
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:UP000077266}.
FT   DOMAIN      441    624       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1072 AA;  117606 MW;  054FF61E8017EBC7 CRC64;
     MDDVQTDKKE AALLQKSRAM TSTKSQTGPT SSVWFRLALA ACLLYLLPWD KLLHTLPDSL
     PALYKSLLAI RTPEPRALSS SGLTDLVQWD EYSLFVKGQR IFLWSGEFHT FRLPVPSLWP
     DILEKMKAAG LNAVSIYIDW ALVHPSPDAL DFDGFRALQP FFDACMAAGL WLVIRPGPYI
     NAEVNAGGIP GWVTSEVAGH LRSNDTDFED AWVPYMRRVI ELSRGAQITE GGPIIAWQIE
     NEYTADPNVG VPGKAEYMAR LEEFVRAEGI VVPLTFNDAS RDAQFAPGKK GEVDIYGIDS
     YPQSFDCSNP GVWKEVDTSY YSYHRRTNPR QPFYIPEFQG GAFDPWGPNA PGYDKCRTLT
     GPEFESVFYL QLWASNVKLI NLYMLYGGTS WGSLPFPGVY TSYDYGSPIL ENRSLGSKYT
     ELKREGLFLR STPEFAKTDV KGNSTDGTGV VTVDNEKVFV TALVNPDSGA GFYIARQTNS
     SSLDNVTFKM TVPTSEGALS IPHATPPISL SGRQSKVIVT DYAFGSDRML YSTASVLFAG
     IIDGRNVLFL HGDVMHSHEI LATLSSNGHS ALSASHEELV TLSHQQHNGR TLISIMHGVK
     GFVTLWESDK QLVLYADSDT AGTFWAPVLS SSSNDFGAFW SIGTNDTVIV GGPYLVREAS
     LVENGDHLAL RGDLQDDAFL TVIGPRDVKT ISWNGQPVEP LSSAKQSTGI FVGRLQTTKA
     LRAFTPPKLT KWKFKDGLPE IASQYDDSKW VTADHESTNL PYKPLFGAPP VLYGCDYGFC
     EGSVLWRGHF KGSADTTGVN LTINGGEAFA ASVWINDRFV KTTYGNSTNN LNIIAETNEL
     YEFPKGAVKM DEDNVITVLQ DNQGLDETDD WDADTSKSPR GIRGALLIGG EFSSWKVQGK
     LGGYTQFADK DRGVVNEGGT FGERAGWHLP SFDVSQWKSR DLSKGLPTSG AGVGVFVTKF
     QLDTPRGVDL HMSFVFDDGV GDTGVPYRAY LYVNGWMMGK RVANLGPQAK FPVHEGILDY
     HGDNTVAVVL WAMEASAAVR PTLQIVVDGR YDSGMAAVAV HNPGWSTRPE AL
//
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