ID A0A166XJR8_9PEZI Unreviewed; 889 AA.
AC A0A166XJR8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
DE Flags: Fragment;
GN ORFNames=CT0861_07004 {ECO:0000313|EMBL:KZL76672.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL76672.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL76672.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL76672.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00000448,
CC ECO:0000256|RuleBase:RU361161};
CC -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987, ECO:0000256|RuleBase:RU361161}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZL76672.1}.
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DR EMBL; LFIV01000013; KZL76672.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166XJR8; -.
DR STRING; 708197.A0A166XJR8; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000076552; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR019800; Glyco_hydro_3_AS.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361161};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000076552}.
FT DOMAIN 794..867
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KZL76672.1"
SQ SEQUENCE 889 AA; 95566 MW; 5881EF1419EFA67B CRC64;
LPPSTLCDCN TTLRPLFHFR CSPEKFQGHI NTMASTVSVK SLAVTLLVSQ VSLCDGAVIN
ARSDVPPGYV AAPYYPAPYG GWASDWSDSY RRAKEVVDRM TLAEKTNITS GTGIFMDSAT
GVRQADNVTV FPSGITTGAT FDKDLMYARA VAIGKEFRGK GANVYLGPSV GPLGRKPRGG
RNWEGFGSDP VLQGKAAALT IKGVQEQGVI ATIKHLVGNE QEMFRMYNPL QQGYSANIDD
RTLHELYLWP FADGVREGVG SVMTAYNAVN GSASSQNSYL INGILKDELG FQGFVMSDWL
SHMSGVGSAL AGLDFNAPGD QQVPLTGYSY WMYDLTRAVL NGSVPVDRIN DMATRVLATW
YQMGQDEGFP ATNWATGTRN REGDFYPAAW PFSPSGVVNE FVKVQDDHYL VARQVAQEAI
TLLKNNGSLL PITTSAPIKI IGTHAQTNPD GPNACGDRAC NKGLLGIGWG SGTVDYEYLD
DPLTAFKKRA GNVVYYNTDS FPSVPAPTVD DVAFVFITSD SGENQYTVEG NNGDRSASGL
NAWHNGNKLV KDAAAKYQNV VVVIHTVGPI LVDEWIDLPS VKSVLVAHLP GQEAGESLAN
VVFGDASPSG HLPYSMTKKE SDLPASVTQL VGGSLGQPQD TFSEGLYIDY RYLNKNGIKP
RFAFGHGLSY TNFSFSDATI SSVTPLSASP PARPAKQGIL EYDAPIPDWT EGVAPAGFNK
IFRYIYSWCT ESEAKDAVAA SKTKTYPYPE GYSTAQKPGP PGGGAQGGNP ALFDVAFTVS
VKVTNTGAKH SGKASAQAYV QFPDGGPETP AIQLRDFEKT KNLAPGESAT VTLELTRRDV
SVWDVVSQNW VVPNPTGRYK IWVGEASDKL FLACYTDSGD CEEGLESPV
//
