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Database: UniProt
Entry: A0A165EMW4_EXIGL
LinkDB: A0A165EMW4_EXIGL
Original site: A0A165EMW4_EXIGL 
ID   A0A165EMW4_EXIGL        Unreviewed;       407 AA.
AC   A0A165EMW4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   16-JAN-2019, entry version 10.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KZV87312.1};
DE   Flags: Fragment;
GN   ORFNames=EXIGLDRAFT_565299 {ECO:0000313|EMBL:KZV87312.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV87312.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV87312.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV87312.1,
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|SAAS:SAAS00534244}.
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DR   EMBL; KV426129; KZV87312.1; -; Genomic_DNA.
DR   EnsemblFungi; KZV87312; KZV87312; EXIGLDRAFT_565299.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.102.20.10; -; 1.
DR   Gene3D; 2.60.120.260; -; 1.
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; 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; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF117100; SSF117100; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000077266};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT   DOMAIN       54    234       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:KZV87312.1}.
FT   NON_TER     407    407       {ECO:0000313|EMBL:KZV87312.1}.
SQ   SEQUENCE   407 AA;  43571 MW;  62601E02847B6FEE CRC64;
     SLYMLYGGTN WGGLSCPLVG TSYDYSSPIQ ETRIISTKYQ ETKLIGLQVR AAKDLVATER
     AGNGTSYSSN PLIWTTELRS VDTNSGFYIV RHNPSNLLSA DSFKLSVSTT RGNFTIPQSD
     GEFVLNGHES KILSVDYALT GGRALVYSTA EVLALSTVDA RAPVLTLWAP AGTVGEFLLS
     GVRSGRFFQG SGKITNRPDG TTLVSIPQVA GVSVLQFADG LRIVVLDKPA AYSTFVPSLT
     ADPAAPHNKN LVVVGPHLVR SAKINGLVVA LTGDMNTATT VEVFAPLPAI ALTWNGRLLI
     ATRTLYGSLK ARYTPPALDG VKFGKAVWRS ADGLPESRAD YDDSRWTKAD KMSTLSTFQP
     DTLPVLYGEE YGIWMGNILW RGRFTGADAT GVFLSVAGGN AMGYSAY
//
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