ID F8MYF0_NEUT8 Unreviewed; 1352 AA.
AC F8MYF0;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN ORFNames=NEUTE1DRAFT_149165 {ECO:0000313|EMBL:EGO51347.1};
OS Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO51347.1};
RN [1] {ECO:0000313|EMBL:EGO51347.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO51347.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Submitted (APR-2011) 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 ECO:0000256|RuleBase:RU361161};
CC -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987, ECO:0000256|RuleBase:RU361161}.
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, ECO:0000256|RuleBase:RU361161}.
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DR EMBL; GL891382; EGO51347.1; -; Genomic_DNA.
DR RefSeq; XP_009854989.1; XM_009856687.1.
DR GeneID; 20827069; -.
DR KEGG; nte:NEUTE1DRAFT149165; -.
DR VEuPathDB; FungiDB:NEUTE1DRAFT_149165; -.
DR HOGENOM; CLU_004542_2_0_1; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000008065; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd14686; bZIP; 1.
DR Gene3D; 1.20.5.170; -; 1.
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; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR019800; Glyco_hydro_3_AS.
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; PF07716; bZIP_2; 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; SM00338; BRLZ; 1.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361161};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361161};
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 78..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1291..1348
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1303..1337
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 27..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1022
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1352 AA; 147108 MW; 58BC1084238C9904 CRC64;
MAAHDPSKQG LLGSTSTEHH ADYSSDSDDN VNINTTPKRP TPRQKQQRTR RTRPTNPALP
TFQPLPTRKS WLARRSRYCL IFAAFGLILF VILLVGGGLG YKAALQEPPY GLSPPWYPSP
KGGIAGTWYE SYQKAAKLVS KMTLAEKVNI TTGVGWQMGL AVGTTAPAVL VGFPALQLQD
GPLGIRNADN ITAFPAGITV GATWNRQLMY ARGKAHAIEA RAKGVNAILG PCVGPLGRMP
AGGRNWEGFG SDPYLQGIAG AGTIKGIQSE GVMATVKHFI ANEQEHFRQP WEWGLPNAIS
SNVDDRTLHE LYAWPFGDAV KAGVASVMCS YNMVNNSYAC GNSKLLNGIL KDELGFQGFV
MSDWLAQRAG VSTALAGLDM TMPGDGLRWA NGKSLWGKEL SKAVMNGSVP VERIDDMATR
VVAAWYQMGQ DNEEKWPRDK GPNFSSWTSE QMGVVSPGSP TEQQTVVVNQ FVDVQANHSV
IARQVAAEGT VLLKNEGPVL PLSRAGLRKR QDANNTPDRV KIGIFGEDAG PLPGGPNSCP
DRGCNQGTLG SGWGSGAVEF PYLVTPVEAL RKQFDSSKVE LHEHLSNQLP FSLSEKAVID
DLDLCLVFVN ADAGEGFKAW ENVRGDRPDL FLQKNGDALI QEVAARCGGG FSDVVVVIHA
VGPVVMERWI DLPQIKAVVF ANLPGEESGN ALVDVLFGHV NPSGHLPFTI GKSLEDYGPG
GQVLYLPNGV VPQQNFSEGL YVDYRWFDKK GITPRFEFGY GLSYTPFELG NATVKTIRPK
SALPFPRLDA LVEPPTYSTD IPPVEEVLWP EGDKEIRRLD KYIYPYLSAD EAHNAVASRK
GGKKYPYPDG YDTPAPLSQA GGDEGGNPEL WAVYAQVTVD VRNTGKVAGS VVPQLYLSYP
DSPKESANGT VEVDFPVKVL RGFDKVYLEA GKSAKVEFNL TRRDLSYWDV EVQNWVMIME
GEYTFHSGDS DWQPPLHLTP SRQSSPGLDR EAVHTLQEWP PQHAQQPPAS ASRSSSSSLQ
YSLQDTPPFD FDFSCDLLTD YDFLHQQQQQ DFNWADPLLF PDQQDLTSLA FPISTTTTTT
TTCDTAPTST TVSPFAPTLP LSVTPSPLLA DTNDIFQQQG WADPSPSAPP QPPMHLSLDH
HHLSSDDPYA AASLSHVTDT LSTTMGLTMP SGRNTTTLGM DLYRTASNNS GSSSNNMGYS
QLNAATSSSS RDHSTTPPTS QSSGSTSPTA STSHHGHGGQ GHLYPGLTLP SPVDASSKPK
RGRPPGPKKR ALSPSVAAEA ELTDSEDILI KRQRNNIAAK KYRQKKIDRI QELEEEVDQI
KKERDELRLM LAKRDAEVGM LREMLVMAKQ GR
//
