ID A0A0G2DY25_9EURO Unreviewed; 1906 AA.
AC A0A0G2DY25;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Probable beta-glucosidase G {ECO:0000256|ARBA:ARBA00039579};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE AltName: Full=Beta-D-glucoside glucohydrolase G {ECO:0000256|ARBA:ARBA00041276};
DE AltName: Full=Cellobiase G {ECO:0000256|ARBA:ARBA00041601};
DE AltName: Full=Gentiobiase G {ECO:0000256|ARBA:ARBA00041808};
GN ORFNames=UCRPC4_g06506 {ECO:0000313|EMBL:KKY15026.1};
OS Phaeomoniella chlamydospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY15026.1, ECO:0000313|Proteomes:UP000053317};
RN [1] {ECO:0000313|EMBL:KKY15026.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY15026.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY15026.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY15026.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) 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: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:KKY15026.1}.
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DR EMBL; LCWF01000197; KKY15026.1; -; Genomic_DNA.
DR OrthoDB; 1334586at2759; -.
DR Proteomes; UP000053317; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProt.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046165; P:alcohol biosynthetic process; IEA:UniProt.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0043386; P:mycotoxin biosynthetic process; IEA:UniProt.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd04717; BAH_polybromo; 1.
DR CDD; cd04369; Bromodomain; 1.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 2.
DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 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 InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
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; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF19; BETA-GLUCOSIDASE G-RELATED; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR SUPFAM; SSF47370; Bromodomain; 2.
DR SUPFAM; SSF48576; Terpenoid synthases; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 3: Inferred from homology;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000053317};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 69..139
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 280..342
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 385..504
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..38
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..208
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..598
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1906 AA; 212066 MW; 46B26FAD316EDF1C CRC64;
MADEEIQVSA NAASPQADED VKMEDDMNEE EQEEEDDDAT DSKVSRDHYA AMRNVVEIVN
THKITVCGEE HYPAHLFRRI VNKRLMPDYY EVIKDPIALS TIRSKILRKQ YTEFKEYVRD
FAQIVHNAKL YNRPNSGAYN DAIAFEDVVK SELAKLVESQ LISQEETEFP YLGEIPEATP
EPDPPEEEEL EEEGDEDEDD EDDEGDDSDD EKAGRRRRNR KSLGGRRRDD DDEKKGGDES
RKRRGRPPRV DTPMEARIKA VLKGIRKFKD EHGRLKVLHF QRLPDKVLNP EYYAAVQNPI
AIDLIKRKAK RKKYRSLDEF MKDLDLMFEN AKMYNEDDSD VYKAAADLQA QSHKLMEEEK
NKSDAELAGD DGRFPLPQGI LHNNEVYKVG DWVHIQNPND VTKPIVAQIY RTWQDSEKQM
WINACWYYRP EQTVHQFEKH FFPNEVVKTG QYRDHHIDEV VGRCFVMFFT RFSRGRPRGL
DPETEVYVCE ARYNEEKHKL NKIKTWASCL PDEVRENDYQ MDMFDQPRRI KKLPSPLLHL
LSDDTKEVRY PHEVPSPKWG APNAPPVVGA IYKGLRDENQ SPPPEPTPPP PPTPQPAPVS
QISMVSQEPP RRTLDAQGDA IMENGPRRPS MASASPAPQA GQYQSQQLVA RPPSSASPAP
VFQRNDSFNR QQPSSIPPQT PTPTYGLATP AYNPYSQPQI QSHRPPNIPT PTTGLTASYN
TNNVRSVETY VMSDTANAAI PPEIRQQFQT DEQGRILFFT APPVDRLPYV QPETGTPLAH
TAEYLAKKLQ KETALLEAEA DSKEQHVEDS SEGLTLKQKR FLELAHRANK RQKTEGDERR
ARFTSNAMLQ HHDNWMHSFY GITKGSHNAD SYEDFLEKET YLQRLRAEGF ETDNSTKNQI
LSQCGGLTAS ARPLGEGEAI QRAKKRLGER DSNITGAGGW ETALARAEDF LNQLTLAEKA
YLVTGVTGPC VGSIAPITRL GFSGLCLQDG PLSIRLADYV SVFPAGLSAA ASWDRDLIYQ
RGLLMAQEFK GKGSHIALGP VVGPLGRSGY GGRNWEGFSP DPYLTGEAVN ATIIAMQSTG
LQACVKHYIG NEQETQRNPS TENGVTIEAV SSNIDDRTMH ELYTWPFANA IRAGVASVMC
SYNRINGSYA CQNSKTLNGI LKEELAFQGY VDDYPTVDPS SADLEGFVAS ESPYQWDLSG
TKHRDLRDDH ASLIRNLGAS SATLLKNTNN ALPISKPPKV IGVFGNDAAD EADGLYQPED
YPANDYGYDI GTLYVGGGSG TGRLSYLVPP LDAIKAWARP SGSLVQYITS NSVAAESVST
IYPIPDVCFV FLKTYVTEGQ DRLSFDVDWN GTTVVNTVTK LCNNTIVVTH SGGVNTMPWA
DNPNVTAIIA AHLPGQETGN SLVDVISGKV NPSGKLPFTI AYNASDYNAP IVNFTGTDEP
DAWQSDFTEG LLIDYRHFDA SNITPRYELN SRFKEKNVGK QDASLKINRG PDGFGFAKAS
LNYRTYLAAA QTAFSGALPG KSRSTNDPLR IVGKELKFLN KNIRQLLGSG HRLLDTVGKY
YTQSEGKHVR PMLVLLMSQA VSEAPKKIRA HSSAFNDSNI NSPITSSNFL IDFNPNQPTS
NPLTNPTNDN DYTLSLNPDS SILPSQRRLA EITELIHLAS LLHDDVIDVA TTRRSKPSAN
VLFGNKMAVL AGDFLLGRAS VALARLRDPE VTELLATVIA NLVEGEFMQL KNTAEDEKHP
VWSEDTISYY LQKTYLKSAS LISKSCRATA LLGNSAPEVV DAAYAYGKNL GLAFQLVDDM
LDYTIAESEL GKPAGADLEL GLATAPLLFA WKQSPELGEL VGRRFSTEGD VKKARDIVAQ
SSGLEQTRAL AQEYADKAIA AIADFPESEA KDGLYDMCEK TMKRRK
//
