ID A0A423WRV7_9PEZI Unreviewed; 909 AA.
AC A0A423WRV7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN ORFNames=VMCG_04596 {ECO:0000313|EMBL:ROW06222.1};
OS Valsa malicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=356882 {ECO:0000313|EMBL:ROW06222.1, ECO:0000313|Proteomes:UP000283895};
RN [1] {ECO:0000313|EMBL:ROW06222.1, ECO:0000313|Proteomes:UP000283895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-1 {ECO:0000313|EMBL:ROW06222.1,
RC ECO:0000313|Proteomes:UP000283895};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-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:ROW06222.1}.
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DR EMBL; LKEA01000011; ROW06222.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423WRV7; -.
DR STRING; 356882.A0A423WRV7; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000283895; 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:UP000283895};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..909
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019565136"
FT DOMAIN 813..887
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 909 AA; 97011 MW; 41CAF687625EF62A CRC64;
MAQPSGVPSR GLVISSLFAI SSLGASVGPR AAVPDPYVAA PYYPAPYTGW VSSWSDSVQK
AKALVDTMTL AEKANITAGT GIYMGEFSLR AVPLVLFRSL TLSQSEVCVG MTGSAPRVGF
PQLCVQDSAL GVRETDNITA FPPGITTGAT FDKSLMYQRG VGIGQEFRGK GCNVYLGPTV
GPIGRKPRDG RSWEGFGADP VLQAVAGSMT IKGVQEQGVM ATIKHLIGNE QEMWRMYNIL
QPAYSANIDD RTMHELYLWP FAEGVHAGVV SVMGAYNAVN GSASTQNSYL INNLLKDELG
FQGFIMSDWL AQISGVPAAL AGLDMAMPGD TMIPLLGTSY WMYEMTTAVL NGSMPVDRLD
DAATRIVAAW YQMGQDEDYP EPNFSSYTTT ATGPLHPASL TGPYGVVNQF VDVRADHATV
ARQVAQDAIT MLKNEDDLLP LSTDTPLFLF GTDQEVNPDG ANACIDRTCD TGTLGMGWGS
GTARYETFDD PLTAIKAKAA NVTSYYTDTF PTLKVGTPSS DDVAIVFISS DAGENSYTVE
GNAGDRSSSG LVAWHNGDEL VKAAAAKYSN VVVVVHTVGP LVVEPWINLD SVKAVLFAHL
PGQEAGESLT NVLFGSVSPS GHLPYTIPVA EDDYPDSVSL TGFAVGQIQD TYTEGLYIDY
RYLNSVGTKP RYAFGHGLSY TNFTYTNATI TKVTQLTRLP PARAAKTGLP DYNTTIPVAS
EAYKPADYSS FYVWRYLYPW LSETDANAAA AVGAAVTSGD KTGYPYPDGY STNQTAGPAA
GGGLGGNDAL WDTAYTVTVT VTNTGARNFS GKASAQGYVQ YPGDSAYDTP IVQLRDFEKT
DALAPGESQT VELTFTRKDV SVWDVVEQNW VVPVVDGAYK FWVGEASDAL YLACDASTLE
CEDGLDAPV
//
