ID A0A2B7XN08_9EURO Unreviewed; 1006 AA.
AC A0A2B7XN08;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=AJ80_07479 {ECO:0000313|EMBL:PGH10536.1};
OS Polytolypa hystricis UAMH7299.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Polytolypa.
OX NCBI_TaxID=1447883 {ECO:0000313|EMBL:PGH10536.1, ECO:0000313|Proteomes:UP000224634};
RN [1] {ECO:0000313|EMBL:PGH10536.1, ECO:0000313|Proteomes:UP000224634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH7299 {ECO:0000313|EMBL:PGH10536.1,
RC ECO:0000313|Proteomes:UP000224634};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-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: 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:PGH10536.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PDNA01000145; PGH10536.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7XN08; -.
DR STRING; 1447883.A0A2B7XN08; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000224634; 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:UP000224634};
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 100..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 901..997
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1006 AA; 109084 MW; 2AD8F25A0BCF3F6C CRC64;
MSKPVNDPSG SLPNQAASNT ETSGIKNSPL ATIRIISPES ECEPPHKALD QAKSQTPHVD
DVYHGEDISD EEETSFLHPS DEMTRSKLIP ERPRRKTCRI ILGLGGIIVA AAIVLAVLGA
TGKFEKKRES NIPKDGLSPP WYPTPKGGTV SKWAESYSKA QKLVEKMSLP EKVNVTTGVG
WAMGLCVGNT GPATLTGFPS LCLQDGPLGL RFADNITAFP AGITVGATWS QDLMRKRGQA
LGKEARLKGV NVILGPSMGP IGTLPAGGRN WEGFGSDPVL QGIAAAETIR GIQENGVIAT
AKHYVLNEQE HFRKCFEWEL PNDNAMSTNI DDRTLREVFI WPFAESVRAG VASVMCSYQL
VNNSFACGNS LLMNGILKDE LGFQGFVQSD WLAQRSGVAS ALAGLDVTMP GDGLHNSDGN
SLWGGRLAQA VLNTSVPLER LNDMTTRVVA AWYQLKQDSW PKPPPEGDGG PNFSSWTNDR
IGRIHQGSDD ETAAVVNRYV RAQGEGKDAH KHLARQIAAE GTVLVKNVNG FLPLARTIAS
GAGKYRVGVF GEDAGPGRGP NACTDRSCNQ GTLGSGWGSG AVDFPYLITP WKSLSTAFNN
DTVTVSGYLN NNVRDEDIHN SSLCIVFANS DAGEGYLRYE DIRGDRNDLF LQKDGGNLVQ
NVATRCGNGT GSTVVVVHAV GPVILEPWVE LPGVKAVLLA NLPGQESGDA LVDVLFGDVD
VSGRLPYTMG KKLEDYGPEA GVLYQSSDPV PQKNFSHGMY LDYRYFDKHN ITPRYEFGFG
LSYTTFELSN LRITRLREKT PLPSPRPSSP DVSPPSYSTK IPSPESALFP KGFRKLKKYV
YPYISSIDEI KQGKYQYPDG YDKLQPPSQA GGGEGGNPSL FESVLNVNVT IRNTGSRTGK
QVAQLYVSFP DNVVDTGNTT SSKDGEKTED VKTDPADTID FPVRVLRNFQ KVELHAGQSV
TVSMSLTRKD LSFWSTRRQN WVMPVEGKFK ISVGRSSRDL PLVGEF
//
