ID A0A093YV76_9PEZI Unreviewed; 835 AA.
AC A0A093YV76;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=V492_05784 {ECO:0000313|EMBL:KFY08931.1};
OS Pseudogymnoascus sp. VKM F-4246.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY08931.1, ECO:0000313|Proteomes:UP000029299};
RN [1] {ECO:0000313|EMBL:KFY08931.1, ECO:0000313|Proteomes:UP000029299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY08931.1,
RC ECO:0000313|Proteomes:UP000029299};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFY08931.1}.
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DR EMBL; JPJU01002054; KFY08931.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093YV76; -.
DR STRING; 1420902.A0A093YV76; -.
DR HOGENOM; CLU_004542_2_0_1; -.
DR Proteomes; UP000029299; 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: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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
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:UP000029299};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..835
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001890159"
FT DOMAIN 757..825
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 657..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 835 AA; 90366 MW; FA2C53F16F7092CC CRC64;
MHIHSALVGA VALAAGASAQ TDGLSPPSYP SPWMHGGQGW DHAYKKAVEF VSQLTLLEKV
NITTGTGWMQ DLCVGATGGI PRLGFDGFCL QDSPLGIRFS DQNSAFPAGV NTAATWSKKL
FKARGEAMGE EFRDKGIDVI LGPVAGPLGR SPEGGRNWEG FAPDPVLTGV AMAETIKGIQ
DTGVIACAKH FVGNEQEHYR QQMSSNMDDT TMHEMYLWPF ADAVKAGVGS VMCSYNRLND
SYACENSYLL NHLLKNELDF QGFVMADWGA QHSGVASALA GLDMTMPGEQ VFGEGTYSYW
GGNLTAAVLN GTVPQWRVDD MAVRIMSAYY KVGRDKSRVP INFSSWTRNT TGYFHTLGEA
DFGVVNQHIN VQSDHKHVIR EIGARSTVLL KNTKRALPLN NPKSVAVIGE DAHLNPDGIN
ACDDRGCDKG TLAMGWGSGT ANFPYLIAPV DALREQAETD RSTFVNISNN YDLDAVRAAA
TGKSVALVFA NADAGEDYIT VDNNEGDRNN LTLWQNGDAV IRAVASVNPN TVVVLHTVGP
VLIEEYKNHP NITAILWAGI PGQESGNAIT DVLYGEINPS AKSVFTWGKE QKDWGVNILY
NDSSVVPQMD FVEGNFIDYR HFDAAGIEPS YEFGFGLSYT TFEYSAIGVR KLQDDEYKPT
TGKTKPAPTF GTIDNSTEAN KMPKDFKAVN KYVYPYLDET TGNAEGGNGD APKGSQDGSK
QKKLPAGGAQ GGNSGLWDEL YEVSATITNT GKLDGTEVVQ LYVSLGGPND PPVVLRGFND
LAIPRGRSKA FRWKLTRRDI SNWDAGKQDW VVSAHPKKVF VGPSSRKLTL TADLA
//
