ID A0A5M9JC89_MONFR Unreviewed; 834 AA.
AC A0A5M9JC89;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN ORFNames=EYC84_010636 {ECO:0000313|EMBL:KAA8564865.1};
OS Monilinia fructicola (Brown rot fungus) (Ciboria fructicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Monilinia.
OX NCBI_TaxID=38448 {ECO:0000313|EMBL:KAA8564865.1, ECO:0000313|Proteomes:UP000322873};
RN [1] {ECO:0000313|EMBL:KAA8564865.1, ECO:0000313|Proteomes:UP000322873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mfrc123 {ECO:0000313|EMBL:KAA8564865.1,
RC ECO:0000313|Proteomes:UP000322873};
RA De Miccolis Angelini R.M., Landi L., Abate D., Pollastro S., Romanazzi G.,
RA Faretra F.;
RT "Genome Sequence of the Brown Rot Fungal Pathogen Monilinia fructicola.";
RL Submitted (JUN-2019) 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:KAA8564865.1}.
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DR EMBL; VICG01000014; KAA8564865.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5M9JC89; -.
DR VEuPathDB; FungiDB:MFRU_008g02920; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000322873; 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; 2.60.120.260; Galactose-binding domain-like; 1.
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 InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF28; BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR Pfam; PF07691; PA14; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SMART; SM00758; PA14; 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.
DR PROSITE; PS51820; PA14; 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:UP000322873}.
FT DOMAIN 396..556
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 834 AA; 91712 MW; 7476D76ED061DE43 CRC64;
MTNRIDVEDV LSKLDNVEKV SLLAGVDWWH TNAIPKYNVP SIRVSDGPNG VRGTRFFNGI
SAACFPCGTG LAATWDTKLL HRAGVLMGEE AKAKGAHVIL GPTINMQRSP LGGRGFESLS
EDPVLSGLGA AALVNGIQET GVQATIKHFV CNDQEHNRNG VNVIITERAL REIYLLPFQL
VVRDSKPGLF MTAYNKVNGT HVSENPRILK NILRGEWGWE GCVMSDWWGT YSTTGAINAG
LDLEMPGATK WRGQLLIQAV STGKVPQHVL DERARNVLRL VNRVADANIP ENAEEKTADT
PETATLLRKI GGDSIVLMKN EGNVLPLRKD KKTLVVGPNA KIATYHGGGS ASLAAYYAVT
PFHGISAQLE SAPTYTVGAY AHKDLPLLGL LLKTDKGETG VTFRAYNDPP TTENRQVADE
FTLTKTELLM MDYYSSKLKD ELWWADIEGY LTAEEDSDFE FGLGVYGTAN LYVDGKLVID
NTTKQTRGTM FFSCGTVEER GVVQLKKGQK YHIKVEFASA PSCKLDRGDN VLFGPGAVRI
GGAKIIDADE EIAHAAKLAK EADQVIICAG LNSDWEGEGA DREIFGLPLH LNKLISTLTP
INPNTVVVIQ SGTPIALPFL STTPALLQAW YGGNETGNAI ADVIFGKTNP SAKLPLTFPN
RIEDNPAFLS FRSERGRVIY GEDIYMGYRW YEALNLPVLF PFGHGLSYTQ FSISDLTVEK
IEKSIKVRVK VKNIGEIPGA EVVQVYIKQQ NPSIRRPNKE LKGFDKVFLE AGEEKTVEVN
IDIKYAAAFW DEVREAWIVE KDEYEVIVGN TSEEGNGELR GKFEVEKTEW WNGL
//
