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Database: UniProt
Entry: A0A165PW94_EXIGL
LinkDB: A0A165PW94_EXIGL
Original site: A0A165PW94_EXIGL 
ID   A0A165PW94_EXIGL        Unreviewed;       997 AA.
AC   A0A165PW94;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   28-FEB-2018, entry version 10.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=EXIGLDRAFT_813087 {ECO:0000313|EMBL:KZW02751.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW02751.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZW02751.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZW02751.1,
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: Hydrolysis of terminal non-reducing beta-D-
CC       galactose residues in beta-D-galactosides.
CC       {ECO:0000256|RuleBase:RU000675, ECO:0000256|SAAS:SAAS00108875}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
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DR   EMBL; KV425886; KZW02751.1; -; Genomic_DNA.
DR   EnsemblFungi; KZW02751; KZW02751; EXIGLDRAFT_813087.
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; -; 3.
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};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    997       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007864410.
FT   DOMAIN      370    564       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   997 AA;  106818 MW;  6F36BC35FDE02EAD CRC64;
     MRFWATCLSA LALGRAAFAV SNNLTTDVTW DPFSLSILGQ RIFLHSGEFH PWRLPSRSLW
     KDIMQKAAAG GLNGVSLYAH LGLMNPAPGV LDFDGLRSME DAILEAQAAG LWVTARIGPY
     VNGETTGGGL PGWMMSLNAT LRTNDATYTQ AWTPYWTAMA KILAKHQITA GGPVILVQVE
     NEFDNVRTTP ATYMVLLEQS LRSNGVVVPT THNNKGLRDI TYAAGTGAVD IWGIDSYPGN
     GCASSWSAVV TNYNDFKNTS GNPTLPLYSP EFVGGWFDPW GSTGNYAACR AKIGPEFERV
     FYEALWAQNA KMINFYMYYG GTNWGGLAAP VVYTSYDYGA AIPENRVIGD KFNELKLLGL
     FIRSARDFRQ TSFAPEVTTL TSSADVTTAE MRNAQTGATF YLLRHTTSQS TATVSTTLKI
     TTKDGAFTIP QTSGSQITLL GHDSRAIVAD YQFGATRVLY STAAVLLGTT IDGVDWLVVH
     GYPQADAGYE VVFAGVTGRL HDDDSQYYCE SPTSSPPFGA LLMHDSICQA GLLANFRITA
     GGRALLSVGS VRLLALDTTV ARTFWAPVLP ASSGTFKQFA EVGSNATIIV AGPALVRTAA
     ITNKVLALTG DTNRTTTLQV YGGSNLFSSV TWNGAQVSGG LDTIGAWSAT LDGPSSAALS
     FVPPTLAAWK FKDSLPEIST TYNDSRWVTA SKTSTFLTMP AYPRDTSALL GEQDYGFFTG
     NVLFRGHFTS TGKETGVFLG INGGQAFAAS AWLNGVYLGS TTSFNSTDSD VKNVTLSFPS
     GALRSGDNVV TVLKDNMGLN EWSGPSGIKQ ARGIVGFQVQ GGANSTWKIQ GNFGGNTNFP
     DKVRGSLNEG GLFAERAGWH LPGFDDSTWE SRTPVQGLTK PGVGFFRTTF DLSVPSGHDV
     AMSFVFRGGG ATRVQLYVNG WQMGKYVANL GPQTVFPVHE GILDYHGKNT VAVSLWAVGN
     STTDFAISDL QLKVDAVLRG GVIVQVANPV WSARDVF
//
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