ID A0A094CU30_9PEZI Unreviewed; 964 AA.
AC A0A094CU30;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=V497_05348 {ECO:0000313|EMBL:KFY57706.1};
OS Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY57706.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY57706.1, ECO:0000313|Proteomes:UP000029268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
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 -!- 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:KFY57706.1}.
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DR EMBL; JPJZ01001004; KFY57706.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094CU30; -.
DR STRING; 1420910.A0A094CU30; -.
DR HOGENOM; CLU_004542_2_0_1; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000029268; 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; 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: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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000029268};
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 69..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 865..955
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 964 AA; 104030 MW; C8D6997B07B8757C CRC64;
MVRNSTADGA NESREGLLRP SLEQAYRSSS DSDIDATDYL KYQNPPITEP YEMKPLSKLR
RSCSRRSKCC LIFAVVVIIV GIVVGGGGWW AYNMVPVDGE SPPWYPSPRG GEIDTPWKES
YIKAAKLVEK MTLPEKVNVS TGVGWQMGLA VGNTGPATHV GFPSLALQDG PLGIRFADNA
TAFPAGLTVG ATWNRTLMHA RGKAHGEEAR LKGVNVLLGP CVGPLGRMPA GGRNWEGFGA
DPYLQGVAAA ETVKGIQGEG VMATIKHYIG NEQEHFRQAR EWAIPNALSS NIGDRTLHEL
YLWPFADAVK AGVASVMCSY QMTNNSYSCA NSKLLNGILK DELGFQGFVQ SDWLAQRAGV
ASTLAGLDMS MPGDGLTWAN GQSLWGPELI KSVLNGSVPV SRLNDMVTRI VAAWYQLGQD
DKSKFDGKGP NFSSWTNDAK GRLHHGSPDE QSLQIVNQFI NVQGDEENSH AKIAREVAIQ
GTVLLKNNGI LPLSRAGWSD DAAHDRKFKL GIFGEDSGPG NGPNACEDRA CNQGTLGSGW
GSGAVEFPYL ITPVSAIKAT VDKAKVDVAD SLANKVPKES SSMLKDQDLC IVFVNADSGE
GYKSSDGISG DRNDLKLQKD GDKLVKQVAN DCGGGKGNTV VVIHAVGPVL VESWIDLPGV
KAVVMAHLPG QESGNALVDI LFGDANPSGK LPYTIGKSLD DYGSGAKVLY LPNAPIPQQN
FSEGIYIDYR HFDKYDITPR FEFGFGLSYT KFEYSDIQVT TVKGKSALPS QRPNATSAPT
YDETLPDPST ALYPSGFRRL AKYIYPYIDN VSEIATGPYP YPDGYNTTQL PSQAGGGEGG
NPSLFDVHAT VSVTLKNTGA VPGAEVAQLY LSYPKSPVTG DAMGGMRQGG WFDTDMSDFP
VKVLRGFEKI NLKPGEIKAV DFKLTRRDLS YWDVREQNWV MPVEGAFTIR VGSSSRDIRQ
EGKF
//
