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Database: UniProt
Entry: A0A094FK61_9PEZI
LinkDB: A0A094FK61_9PEZI
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ID   A0A094FK61_9PEZI        Unreviewed;       800 AA.
AC   A0A094FK61;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=V497_03980 {ECO:0000313|EMBL:KFY59962.1};
OS   Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY59962.1, ECO:0000313|Proteomes:UP000029268};
RN   [1] {ECO:0000313|EMBL:KFY59962.1, ECO:0000313|Proteomes:UP000029268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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:KFY59962.1}.
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DR   EMBL; JPJZ01000848; KFY59962.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094FK61; -.
DR   STRING; 1420910.A0A094FK61; -.
DR   HOGENOM; CLU_004542_2_3_1; -.
DR   OrthoDB; 5486783at2759; -.
DR   Proteomes; UP000029268; Unassembled WGS sequence.
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:SF19; BETA-GLUCOSIDASE G-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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029268};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..800
FT                   /note="Probable beta-glucosidase G"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001901686"
FT   DOMAIN          716..788
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   800 AA;  85602 MW;  E195DEDE985C3D48 CRC64;
     MAYLRLGKFL TALLSLFFVA SAQSSWDHAL FTSSPPVYPS PSSDGIGWEA AFAKARTFVA
     NLTLDEKAGL LTGNIRGPCV GNLVPIPRLG FKGLCMQDGP AAIRQATFVS VFPAGLTIAA
     TWDRKLMNTR GSYLAAEFKA KGAHVVLGPV AGPLGRSAFA GRGWEGFSPD PYLTGVAMEQ
     TISGIQSVGV QANAKHWIGN EQETQRVPSN NGGVKIEAVS SNIDDRTMHE VYMWPFANAL
     HAGVASVMCA YNRLNASYAC QNSKILNGLL KDELGFQGYV VSDWGGTHSG VASVKAGLDM
     DMPGSINFQA PGPSYFGGNL TIGVNNGSLT MDRIDDMVHR VMTPYFFLNQ DTTYPSIDQS
     SAPLNKWGIH PYLQSFIYGA KANVDARGAH AKLIRDAAAA GTVLLKNEGN ILPLKAPKNI
     GVFGNDAGDN IDGVYTLNAI RDHGYEYGTL AIGGGSGTGR PTYVVTPMDA IKARAAADGA
     IVQFILNNNY LASDPNLAFS TFAPSPPDVC LVFLKTWATE GSDRTTLEAD WKSAAVVKNV
     ADRCPNTVVI THSGGPNTMP WASHPNVKGI LAAHFPGQES GNSIVDILYG VVNPSGKLPY
     TIANSEAEDK FAPITDSPEL RATTDPNAWQ SDFQEGPLID YRHFDYYNNS VLYEFGFGLS
     YTTFGMANLE IAKIDEKVTA RAPAAKTQPG GNPNLFKTVF RVTVAVSNTG TVAGAAVPQL
     YLSLPPVDGI TPSSLRVLRG FEKIVLQPGQ TETVTFNLMR RDVSFWDTTS QEWVIASGKI
     GVHAGFSSRD FKAEGSFTPL
//
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