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Database: UniProt
Entry: A0A094AQD4_9PEZI
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ID   A0A094AQD4_9PEZI        Unreviewed;       872 AA.
AC   A0A094AQD4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=V494_08664 {ECO:0000313|EMBL:KFY29563.1};
OS   Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY29563.1, ECO:0000313|Proteomes:UP000029288};
RN   [1] {ECO:0000313|EMBL:KFY29563.1, ECO:0000313|Proteomes:UP000029288}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
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:KFY29563.1}.
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DR   EMBL; JPJW01003425; KFY29563.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094AQD4; -.
DR   STRING; 1420907.A0A094AQD4; -.
DR   HOGENOM; CLU_004542_2_1_1; -.
DR   OrthoDB; 5486783at2759; -.
DR   Proteomes; UP000029288; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; 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: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:UP000029288}.
FT   DOMAIN          788..860
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   872 AA;  93846 MW;  75ADE68AC5EF9F99 CRC64;
     MSRAVMFPLP EFPQVVADAP SAVWEQAKYK TAAMLVPSGN GKSLFFEWIG DLFSYTMPYL
     HLGKLLTALL SLFLVAGAQS TWDHELFTSS PPVYPSPQTD GKGWEAAFAK ARTFTANLTL
     EEKAGLLTGN IRGPCVGKNT HMKPITDLLT QLGNLVPIPR VGFKGLCMQD GPASLRQATF
     VSVFPAGLTV AATWDRKLMN TRGSYLGAEF KEKGAHVLLG PVAGPLGRSA FAGRGWEGFS
     PDPYLTGVAM EETITGIQSA GVQANAKHWI GNEQETQRVP SNNGGVKIEA VSSNIDDRTM
     HEVYMWPFAN ALHAGVASVM CAYNRLNASY ACQNSKILNG LLKEELGFQG YVVSDWGGTH
     SGVASVKAGL DMDMPGSINF QAPGPSYFGG NLTIGVNNGS LTMARIDDMV HRVMTPYFLL
     NQDTTYPSVD AASAPLNKWG IHPYLQAFVY GPKKNVDVRG AHAKLIRDAA AAGTVLLKNT
     GNILPLKAPK NIGVFGNDAG DNIDGVYTLN AIRDKGYEYG NLLIGGGSGT GRPTYVVTPM
     DAIKARAAKD GAIVQFILNN NYLASDPNLA FSTFAPSPPD VCLVFLKTWA TEGSDRTTLE
     ADWNSAAVVN NVADRCPNTV VITHSGGPNT MPWASHKNVK GIIAAHFPGQ ESGNSIVDIL
     YGDVNPSGKL PYTIANSEAE DKFAPIVDSP ELRATTDPNA WQSDFEEGPL IDYRHFDYYN
     TSVLYEFGFG LSYTTFAMAN LRISKIDQTV TARAAPAKTA PGGNPNLYKN IFRVLVSLTN
     TGKVAGAAVP QLYLSLPPVD GITPSPLRVL RGFEKVLLQP GQIQTVTFNL MRRDVSFWDT
     VSQEWVIASG KIGVHAGFSS RDFQVEGSFS PL
//
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