ID A0A0G2DWK1_9PEZI Unreviewed; 1129 AA.
AC A0A0G2DWK1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Probable beta-glucosidase E {ECO:0000256|ARBA:ARBA00039576};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE AltName: Full=Beta-D-glucoside glucohydrolase E {ECO:0000256|ARBA:ARBA00041269};
DE AltName: Full=Cellobiase E {ECO:0000256|ARBA:ARBA00041599};
DE AltName: Full=Gentiobiase E {ECO:0000256|ARBA:ARBA00041811};
GN ORFNames=UCDDS831_g07682 {ECO:0000313|EMBL:KKY15292.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY15292.1, ECO:0000313|Proteomes:UP000034182};
RN [1] {ECO:0000313|EMBL:KKY15292.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY15292.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY15292.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY15292.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) 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: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004606}.
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:KKY15292.1}.
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DR EMBL; LAQI01000197; KKY15292.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2DWK1; -.
DR Proteomes; UP000034182; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; 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; 2.
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:SF20; BETA-GLUCOSIDASE E-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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KKY15292.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 124..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 934..1120
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 57..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..987
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1035
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1129 AA; 122990 MW; B866E87640B2EF95 CRC64;
MPNDYELRGK YTAVENADNH DGNYLQSHKH LHLRNASTGS SLRPSLDAAY LSSDDDDLNE
FDPLNEESTP LDTGKRRKRR PRSESRVGAA ADAYTGERWR RNDEARRPPW ARVAAACTPA
RKRLWCWLPL LFVLALLLLL GAGGLWAWRA GPAEGQSPPW YPAPRGGTDA AWAEAYDRAS
LLVAGMTLAE KVNVTTGVGW EMGMCVGNTG PVERLGFPSL CLQDGPLGLR FADRATAWPA
GLTVGATWSK ELMYLRGQAH AREAKGKGVN VLLGPAMGPL GRLPAGGRNW EGFGADPVLQ
GLAAAWTIKG IQDEGVMATA KHWVGNEQEH FRQSFEWGAP NALSSNIDDR TLHEIYAWPF
ADSVRVGVAS VMCSYNQVNN SYACQNSKLL NGVLKDELGF QGFVQSDWLA QRSGVASALA
GLDMSMPGDG LRWQDGKALW GPELTRAALN GSVPMERLND MVTRIVAAWY QLGQDDPEKF
PQDGPNFSSW TDEEVGLLHP GSDDKTTGKV NKFVDVQANG SHGELARRIA AEGIVLVKNE
NDTLPISRQG HSIASGFVSN KDDFKMHVGI YGEDARGNPD GRNACPDRGC NEGTLASGWG
SGAADFPYLV TPLEALRREF DIDMVLLHEY PANEIPETKQ RALEAQDLCL AFVNSDAGEG
YISWEGINGD RNDLYTQKGG DKLVETVAKR CGGGDSPVIV VVHAVGPVIL ENWIDIPNVK
AVLLAHLPGQ ESGNAIADVI FGEVNPSGRL PYTVAKDEDD YGPDSHVMYY PNAVVPQQNF
TEGLYFDYRY FDKNGIAPRY EFGYGLSYST FELSELQIVT DPTKKTLLPA PRPDPRVLPV
PPTYDNGTGP AEDALFPSGF RRLSKYIYPY LNSLSGTANP GVPDKAWPEA FADEKLHAEP
SQAGGGPGGN PDLYTYVANI SFTIRNTSPV RGSAVPQLYV SYPKHWTDPE NPAMMSTAGM
MKGGGHHDHH TARAAAAATK DDDDAPVNEG IISDDGKVTS PFENGPLPPP KSNSNNHNNN
NKVHNSNQNH TTTPLDLPPD RHDPAVVAQL RVVDFPVRVL RGFEKVELAP AGDDGDAARV
SFAVTRRDLS YWDTRRQNWV MPTSGDGTAR EFGVWIGWSS RDLVLSGMV
//
