ID A0A1V8STB6_9PEZI Unreviewed; 982 AA.
AC A0A1V8STB6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=B0A48_11805 {ECO:0000313|EMBL:OQO02251.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO02251.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-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:OQO02251.1}.
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; NAJO01000028; OQO02251.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8STB6; -.
DR STRING; 1507870.A0A1V8STB6; -.
DR InParanoid; A0A1V8STB6; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000192596; 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:UP000192596};
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 90..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 889..969
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 982 AA; 105827 MW; 271C57F1047E280C CRC64;
MSLKNPQVYE LDRSDSPSRG PYDQPYRYSS DSDDGQDTPL SSQRAYQDDA SQPLQPGSFS
KETAGKQPLA WLDAKRTRTG WTRYLVPSRF LCSLIVLFIV ALSLLLGVGG FWAHSKSVPL
DGQSPPWYPS PAGGSVKAWS ESYEKAAKLV GQMTLVEKVN VTTGIGWSMG MCVGNTGPVE
RLGFPSLCLQ DGPLGLRFAD NATAFPAGVT VGATWNKKLM YQRGKAHGFE AKKKGINALL
GPSMGPLGRL PAGGRNWEGF GADPVLQGYA AAQTIKGIQD SGVIATAKHY VANEQEHFRQ
SWEWGTPNAI SSNIDDRTMR EMYAWPFAES VRAGVASVMC SYNQVNNSYA CQNSALLNGI
LKDELGFQGF VQSDWLAQRS GVASALAGLD MTMPGDGLSW ADGKSLWGSE LTKAVLNSSV
PMDRLNDMTM RIVAAWYQLG QDSATAWPAE KDGGGPNFSS WTDDEEGLLH PGSPDAKQKG
VVNKFVQTQN TTEGGDHDTL ARQIAAEGIV MVKNEGDVIP LRRDGSGFET SNEKVKIAVF
GDGAFPNPAG DNACKDRACN TGTLAMGWGS GAVELPYLST PVDALHHNFD SGKVEFSGLA
DNSGKKVAEL AKAQDLCIAF ISADAGEGFV SWNGVKGDRN DLYAQKGGDK LVKDVAENCG
GDTVVVINTV GPVILEKWID LPSVKAVLIT HLPGQEAGNA LADVLFGDVN PSGALPYTIA
KDEKDYGPTS GIMYLPNGVV PQQDFTEGLY IDYRHFDKQS IAPRYDFGFG LSYTTFKLSS
MFLNPQGFSG ATPAPRPDAL VAPQLSTEIP DATEALWPKG TKKLKKYVYP YIPSLSSIKV
GAYPYPVGYA TPTPLSPAGG AEGGNPDLYT TALKVQATLT NTGSVPGQAV VQAYLSFPPN
VMSPSGKPID FPVRVLRQWD KIFVGTSNEE KRQPVRLELT RKDCSYWDVE VQNWVVPKGE
FKVCLGFSSR DEGHCSTFEL VR
//
