ID F0XLR2_GROCL Unreviewed; 845 AA.
AC F0XLR2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
GN ORFNames=CMQ_5969 {ECO:0000313|EMBL:EFX01027.1};
OS Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS (Graphiocladiella clavigera).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN [1] {ECO:0000313|EMBL:EFX01027.1, ECO:0000313|Proteomes:UP000007796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
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}.
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DR EMBL; GL629794; EFX01027.1; -; Genomic_DNA.
DR RefSeq; XP_014170509.1; XM_014315034.1.
DR AlphaFoldDB; F0XLR2; -.
DR STRING; 655863.F0XLR2; -.
DR GeneID; 25979349; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_1_1; -.
DR InParanoid; F0XLR2; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000007796; Unassembled WGS sequence.
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:SF5; BETA-GLUCOSIDASE M-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 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:UP000007796}.
FT DOMAIN 757..833
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 845 AA; 90025 MW; A50EBE41281ECA9D CRC64;
MKSKIPPFLR TKKGITIVVA CTVIILGGGL SGLAALHNRG SHKSRGDTGD SSGMQVITSD
SYFYGQSPPV YPSPSMTGVG SWAVSYSKAV ALVNNMTLEE RVGLTTGASS YSNGCSGYIS
PVSRVGFPGM CLSDAGNGLR NTDFVSSWPS GIHVGASWNR DLAAQRARGM AAEFKKKGVN
VLLGPVVSPV GRTVRTGRFW EGFSVDPYLA GIMAYETVTG CQDEGVITST KHFIANEQET
NRQPIDGKEA VSSNIDDRTM HELYLWPFQD AVYAGTGNIM CSYNRVNNSY GCANSKTLNG
LLKTELGFQG FVVSDWGAQH AGVATSLSGM DMSMPSGSAF WGSHLVEAVQ NGSVAESRIT
DMATRIIATW YQMDQDSDFP TPGIGMPADL TKPHDIVDGR NSTAKQTLLD GAIEGHVLLK
NDNNALPLKA PNFISIFGYS AKAPDRNDFT PGSTTAWSFG AEPANETDTY LAFNSGPPKS
PSAIALNGTL FSGGGSGATS QSLVSAPFDA IMQQAWTDGT ELFWDFSTAS PSVNAASGAC
LVLVNAWASE GYDRPGVRDD YTDELIKNVA DQCSNTIVVV HNAGARVVDS WIDHANVTAL
IFAHLPGQYS GQALVSILYG QSNPSGKLPY TVAMNESDYG TILDPALPEG EYIKFPQADF
SEGVFIDYRR FDASNMTPRF EFGFGLSYTT FGYTGLQITK SLSGSASGNA STGNDNSTLF
ARYPTGAVRQ GGQADLWDTL VTVTANITNT GNVDGAEVAQ LYITIPGGGN DTSSDSAVPV
RQLRGFEKTF LNTSQTATVE FSLTRRDLSI WDTVAQKWLL QRGSYDVSVG SSSRSLPLVK
SFGIL
//
