ID C6H1R4_AJECH Unreviewed; 845 AA.
AC C6H1R4;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 03-MAY-2023, entry version 58.
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=HCDG_00646 {ECO:0000313|EMBL:EER45067.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER45067.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) 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}.
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DR EMBL; GG692419; EER45067.1; -; Genomic_DNA.
DR AlphaFoldDB; C6H1R4; -.
DR STRING; 544712.C6H1R4; -.
DR VEuPathDB; FungiDB:HCDG_00646; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_0_1; -.
DR OMA; YYPSPWA; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000002624; 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:SF12; BETA-GLUCOSIDASE A-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:UP000002624};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..845
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002965850"
FT DOMAIN 763..831
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 845 AA; 91142 MW; 3F9E90F4774D9792 CRC64;
MRGGVLDLLP IGFASLAVAA EHLTQSPPYY PSPWASGHGG WEDAVERARD FVSQLTLVEK
VNLTTGVGWM QENCVGQVGS IPRMGLHSLC MQDGPLGIRF ADYVSAFPAG VNVGATFSKE
LAYLRGKAMG EEHRDKGVDV VLGPVVGPLG RSPDGGRNWE GFSPDPVNSG LLVAETIKGI
QSAGVIACVK HFIGNEQERF RQGPEAQGYG FDISESSSSN IDDVTMHELY LWPFADAVRA
GVGYTQNKLL KAELGFQGFI MSDWQAHHSG VGSALAGLDM SMPGDTVFGT GRSYWGPNLT
IAVANGTIPE WRVDDMAVRI MAAYFKVGRE AAKVPVNFNS WTRDEYGYTH ALVKEGYGKV
NERINVRAKH ASIIRQVGAA SVVLLKHTVS LPLTGLEKNV AVIGEDAGLN LWGPNGCPDR
RCDNGTLAMG WGSGTADFPY LVTPAEAIQN EILSKGEGSV FPIFDNWASD QIKSAASQAT
VSLVFVNADS GEGFISVDGN EGDRKNLTLW KGGDELIQTV ASYCNNTVVV IHSTGPVLVG
EWNEHPNITA ILWAGLPGQE SGNSIADVLY GKANPGGRTP FTWGRTAEDY GASILKEPNE
GNGAPQVDFT EGIFTDYRAF DKADIKPIYE FGFGLSYTSF SYSDLNVEVV RSEPYMPTRG
KTEPAPILGE SDRNLSSYLF PDGMDRVTYY IYPWLNVTDP AKASMDSHYG LQKEDYIPPG
ATDGSPQELL PAGGGPGGNP GLYEVLHRVT ATITNTGSVT GDEVPQLYVS LGGPNDAKVV
LRNFDRFTLA AGEAKIWTSI LTRRDLSNWD PVTQNWVISD YPKTVYVGSS SRKLLLSAPL
VSNNY
//
