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Database: UniProt
Entry: A0A2B7XE77_9EURO
LinkDB: A0A2B7XE77_9EURO
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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
//
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