ID A0A2K1QXC2_9PEZI Unreviewed; 807 AA.
AC A0A2K1QXC2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Probable beta-glucosidase G {ECO:0000256|ARBA:ARBA00039579};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE AltName: Full=Beta-D-glucoside glucohydrolase G {ECO:0000256|ARBA:ARBA00041276};
DE AltName: Full=Cellobiase G {ECO:0000256|ARBA:ARBA00041601};
DE AltName: Full=Gentiobiase G {ECO:0000256|ARBA:ARBA00041808};
GN ORFNames=CAC42_7397 {ECO:0000313|EMBL:PNS19553.1};
OS Sphaceloma murrayae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Sphaceloma.
OX NCBI_TaxID=2082308 {ECO:0000313|EMBL:PNS19553.1, ECO:0000313|Proteomes:UP000243797};
RN [1] {ECO:0000313|EMBL:PNS19553.1, ECO:0000313|Proteomes:UP000243797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQ-2017a {ECO:0000313|EMBL:PNS19553.1,
RC ECO:0000313|Proteomes:UP000243797};
RA Cheng Q.;
RT "Draft genome sequence of a variant of Elsinoe murrayae.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes
CC involved in the degradation of cellulosic biomass. Catalyzes the last
CC step releasing glucose from the inhibitory cellobiose.
CC {ECO:0000256|ARBA:ARBA00024983}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:PNS19553.1}.
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DR EMBL; NKHZ01000031; PNS19553.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1QXC2; -.
DR STRING; 2082308.A0A2K1QXC2; -.
DR InParanoid; A0A2K1QXC2; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000243797; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:SF19; BETA-GLUCOSIDASE G-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:UP000243797};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..807
FT /note="Probable beta-glucosidase G"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014471839"
FT DOMAIN 719..793
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 807 AA; 85683 MW; 46F973090B7CDE7B CRC64;
MAKLSFKGTI LLCISHFAQA RINTPSNLPW NQADYATIAN GQGWEAAFAQ ADSFVSNLTL
EEKAYVVTGV LGPCTGTIKT IPRLGFDGLC LQDGPLAIRQ ADFASVFPAG LTVAAAWDKG
LARVRGVQLG AEFAGKGSNI ALGPVAGPLG RSPLGGRNWE GFSPDPYLTG ELFGETIEGM
QEAGAQACAK HYIGNEQEIQ RNPSTTGNGT VIQAVSSNID DRTMHEVYLW PFANAVKSGV
SSVMCAYQRV NGSYACQNSK ILNGLLKGEL GFQGYVVSDW GGTRSGVTAI QAGLDMDMPG
SISFTDFSGA SYFGANITAA VNNGSLSIER LDDMVKRVMM PYFKLGQDQA SFPKIDPAVA
PLNFFAQLAR GVPNNNTWPY NNQSSVDVRA DHAQSIRELG AAGIVLLKNE NKALPLQRLR
NIAVYGNDVG DLTEGLYANP LSGGNEFGYE FGVLGSGGGS GTGRFSYIIS PLEAMKARAR
LDGTIVQYVQ NNTLANLAGA STIITGTPPE ACVVFLKTYA AEGDDRASLL VDWDGTALVN
TVASFCNNTI VVTNSAGLNV LPFANNTNVT AILAAHLGGQ ETGDSIVDVL YGAVNPSGHL
PYTIPLSEDD YSFVPLTNSS ALLNTTNTTA WQSDFTEGPL LDYRHFDYYN LPVLYPFGHG
LSYTSFSVSN FSVDPVTQGP VPALPPTAPT APGGNPTLWD VLYRVSVDVS NTGSVDGSAV
PQLYLAIPGA TPPGQGQQPA RVLRGFEKVA VRAGETARVG FDVMRRDVSY WDVVRQEWVI
AEGEVGVRVG FSSRDAGVEG RFTPVRS
//
