ID A0A2B7XE77_9EURO Unreviewed; 984 AA.
AC A0A2B7XE77;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=GX51_01735 {ECO:0000313|EMBL:PGH07436.1};
OS Blastomyces parvus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060905 {ECO:0000313|EMBL:PGH07436.1, ECO:0000313|Proteomes:UP000224080};
RN [1] {ECO:0000313|EMBL:PGH07436.1, ECO:0000313|Proteomes:UP000224080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH130 {ECO:0000313|EMBL:PGH07436.1,
RC ECO:0000313|Proteomes:UP000224080};
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:PGH07436.1}.
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DR EMBL; PDNC01000014; PGH07436.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7XE77; -.
DR STRING; 2060905.A0A2B7XE77; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000224080; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:UP000224080};
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 52..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 866..975
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 984 AA; 106180 MW; 2686E5BF0859D681 CRC64;
MTTPPPPSLP PDPKPATPAS TDASSDDNRS TNASATASAT PRWWARRRVW RVFILPLGAV
VLVLVIVLAV LGAKGILSGR EKSGDDDDGN NGPMRVETRD GLSRPWYPSP RGGTVQNWTE
SYEKAQELVG RMSVVEKVNV TTGVGWQMGL CVGNTGPATS VGFPSLCLQD GPLGIRFADN
ISAFPAGVTI GATWSRDLMY KRGFALGKEA RLKGVNILLG PAMGPIGTLP AGGRNWEGFG
SDPVLQGVAA AETIRGIQDN GVMATAKHYV LNEQEHFRQE GEWGIPIAMS SNIDDRSLRE
VYVWPFAESV RAGVASVMCA YQMVNNSYAC QNSLILNGIL KDELGFQGFI QSDWLAQRSG
VASALAGLDV SMPGDGLGWA DGIPLWGPHL TRAVLNTSVP MDRLNDMVTR VVASWYQLKQ
DSWPKPPPDG DGGPNFSSWT HDRIGRLHQG SPSSDAEGVV NQYVNAQGEG DDAHGPLARE
IAAEGTILLK NENGFLPLSR DGPRLSDEKY RIGIYGEDAG AGDGPNACAD RACNQGTLGS
GWGSGAVDFP YLITPWKALS RAFNNQSTTV SGYLTNDRTP PEDMRDKDLC LVFANADSGE
GFGRWEDIHG DRNDLLLQKG TDSLVSQVAT ECGAGNGSTV VVIHSVGPVI VESWIDLPGV
KAVLLANLPG EESGNALADV LFGDVDAGGR LPYTMGKNLT DYGPEAGVLY ESNDVIPQKD
FSHGLYIDYR YFDAHNITPR YEFGYGLSYT TFNLSNLILT PLETKTPLPS PRPKEISPPS
YNATIPNVES ALFLEGFRIL TKYIYPYISS VDDIKREPPY EYPKGYDEAQ PPSPAGGGEG
GNPSLFEPFV MVNVTVSNTG TRVGKEVVQV YVSFPENVLD EPILDNNSSS SSSSSSNSTS
PNNSTMPNPT NNSTRTVDFP PRVLRNFHKV EVQPGQNATV SLSLTRKDLS YWSAVNQNWV
MPVGGKFRVW VGRSSRDLPL MAEY
//