ID A0A0F4ZC90_9PEZI Unreviewed; 854 AA.
AC A0A0F4ZC90;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Probable beta-glucosidase F {ECO:0000256|ARBA:ARBA00039577};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE AltName: Full=Beta-D-glucoside glucohydrolase F {ECO:0000256|ARBA:ARBA00041270};
DE AltName: Full=Cellobiase F {ECO:0000256|ARBA:ARBA00041600};
DE AltName: Full=Gentiobiase F {ECO:0000256|ARBA:ARBA00041810};
GN ORFNames=TD95_003253 {ECO:0000313|EMBL:KKA27855.1};
OS Thielaviopsis punctulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA27855.1, ECO:0000313|Proteomes:UP000033483};
RN [1] {ECO:0000313|EMBL:KKA27855.1, ECO:0000313|Proteomes:UP000033483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA27855.1};
RA Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL Submitted (MAR-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 -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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:KKA27855.1}.
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DR EMBL; LAEV01001554; KKA27855.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4ZC90; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000033483; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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; 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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000033483}.
FT DOMAIN 758..832
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 854 AA; 92510 MW; 841E4A25DA2E57DE CRC64;
MGGVQSQAVS PPYYPAPFGG WVSDWASSYE KAKILVDNMT LAEKTNITAG TGIYMGEIYR
CVGNTGSALR VGFPQLCLGD AANGVRLVDN VTVFPAGITT GATWDKDLIY RRGVALGEEF
RGKGINIYLG PTVGPLGKRP KGGRNWEGFG ADPVLQAVGG RQTIKGVQKQ GVIATIKHFI
GNEQEMYRMY NPFMSGYSSN IDDRTLHELY LWPFAEAIHE GVGAMMTAYN GVNNSACSQN
SYLINGIAKQ ELGFQGFVMS DWISHMSGVA SALAGLDMDM PGDTQIPVLG FSYWMYDLTR
AVLNGSVPMT RLNDMATRIV ATWYKFGQDE GYPHVSFSTN TADAYGDLYA GAWPNSPQGL
VNEFVNVQAD HYLVAREVAQ DAITLLKNNG SFLPLDTSQA LHLFGTDAAA NPDGINACND
RSCNKGTLGQ GWGSGTVQYP YLDDPHTALL KRTQNLTFYN TDSWPSNVPD ATENDVAIVF
LSSDSGENSY TVEGNHGDRD ASGLQAWHGG DKLVAQVAAH YSNVVVVVHT VGPLIVEPWI
DLPSVKAVLF AHLPGQEAGE SLANVLYGDV SPSGHLPYTI THQETDLPDS LSQLVGFSFP
NPQDNYSEGL YIDYRYLNKA GIKPRFAFGF GLSYTDFVYD NITISAGVGL TRLPPEPPAK
GTVLDYDAPV PDASEALAPA GFNKIFRYIY SWLQPDEATA AVNDRKTKTY DYPAGYSTVQ
KAGMRAGGGE GGNPALWDQA YTLTLHVSNT GTQHSGRAVV QAYLQFPEDA GYDTPIIQLR
DFEKTDALAP GDGQTLTLTL TRKDLSVWDV VLQDWVVPSV GGRFTIWLGD SSDNLHTACY
TDTLECETGL DSPV
//
