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Database: UniProt
Entry: A0A093ZRB4_9PEZI
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ID   A0A093ZRB4_9PEZI        Unreviewed;       834 AA.
AC   A0A093ZRB4;
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=V492_03162 {ECO:0000313|EMBL:KFY13600.1};
OS   Pseudogymnoascus sp. VKM F-4246.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY13600.1, ECO:0000313|Proteomes:UP000029299};
RN   [1] {ECO:0000313|EMBL:KFY13600.1, ECO:0000313|Proteomes:UP000029299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY13600.1,
RC   ECO:0000313|Proteomes:UP000029299};
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:KFY13600.1}.
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DR   EMBL; JPJU01000973; KFY13600.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093ZRB4; -.
DR   STRING; 1420902.A0A093ZRB4; -.
DR   HOGENOM; CLU_004542_2_3_1; -.
DR   Proteomes; UP000029299; 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:UP000029299}.
FT   DOMAIN          750..822
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   834 AA;  89733 MW;  A6D1635740CE4B2A CRC64;
     MWEQAKYKTA AMLVPSGNGK SLFFEWIGDL FSYTMPYLHL GKLLTALLSL FLVAGAQSTW
     DHELFTSSPP VYPSPKTDGK GWEAAFAKAR TFTANLTLEE KAGLLTGNIR GPCVGNLVPI
     PRVGFKGLCM QDGPASLRQA TFVSVFPAGL TVAATWDRKL MNTRGSYLGA EFKEKGAHVL
     LGPVAGPLGR SAFAGRGWEG FSPDPYLTGV AMEETITGIQ SAGVQANAKH WIGNEQETQR
     VPSNNGGVKI EAVSSNIDDR TMHEVYMWPF ANALHAGVAS VMCAYNRLNA SYACQNSKIL
     NGLLKEELGF QGYVVSDWGG THSGVASVKA GLDMDMPGSI NFQAPGPSYF GGNLTIGVNN
     GSLTMARIDD MVHRVMTPYF LLNQDTTYPS VDAASAPLNK WGIHPYLQSF VYGPKKNVDV
     RGAHAKLIRD AAAAGTVLLK NTGNILPLKA PKNIGVFGND AGDNINGVYT LNAIRDKGYE
     YGNLLIGGGS GTGRPTYVVT PMDAIKARAA KDGAIVQFIL NNNYLASDPN LAFSTFAPSP
     PDVCLVFLKT WATEGSDRTT LEADWNSAAV VNNVADRCPN TVVITHSGGP NTMPWASHKN
     VKGIIAAHFP GQESGNSIVD ILYGDVNPSG KLPYTIANSE AEDKFAPIVD SPELRATTDP
     NAWQSDFEEG PLIDYRHFDY YNTSVLYEFG FGLSYTTFAM ANLRISKIDQ TVTARAAAAK
     TAPGGNPNLY KNIFRVLVSL TNTGKVAGAA VPQLYLSLPP VDGITPSPLR VLRGFEKVLL
     QPGEIQTVTF NLMRRDVSFW DTVSQEWVIA SGKIGVHAGF SSRDFQVEGS FSPL
//
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