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Database: UniProt
Entry: K3UTF4_FUSPC
LinkDB: K3UTF4_FUSPC
Original site: K3UTF4_FUSPC 
ID   K3UTF4_FUSPC            Unreviewed;       813 AA.
AC   K3UTF4;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=FPSE_03936 {ECO:0000313|EMBL:EKJ75756.1};
OS   Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ75756.1, ECO:0000313|Proteomes:UP000007978};
RN   [1] {ECO:0000313|EMBL:EKJ75756.1, ECO:0000313|Proteomes:UP000007978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS3096 {ECO:0000313|EMBL:EKJ75756.1,
RC   ECO:0000313|Proteomes:UP000007978};
RX   PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA   Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA   Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT   "Comparative pathogenomics reveals horizontally acquired novel virulence
RT   genes in fungi infecting cereal hosts.";
RL   PLoS Pathog. 8:E1002952-E1002952(2012).
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:EKJ75756.1}.
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DR   EMBL; AFNW01000081; EKJ75756.1; -; Genomic_DNA.
DR   RefSeq; XP_009255329.1; XM_009257054.1.
DR   AlphaFoldDB; K3UTF4; -.
DR   EnsemblFungi; EKJ75756; EKJ75756; FPSE_03936.
DR   GeneID; 20362554; -.
DR   KEGG; fpu:FPSE_03936; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_2_3_1; -.
DR   OrthoDB; 5486783at2759; -.
DR   Proteomes; UP000007978; Chromosome 3.
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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..813
FT                   /note="Probable beta-glucosidase G"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003870252"
FT   DOMAIN          728..799
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   813 AA;  88482 MW;  0A39BAAFB997F32A CRC64;
     MASLRSVLVS GLLATSVSAQ NFGGGARDEE AFSWVQPKNT TILGQYGHSP HYNSTYATGK
     GWEEGFAKAK EFLAKLTLEE KADMVTGTPG PCVGNIIAIP RLGFKGLCLH DGPLAIRVAD
     YASVFSAGVS AASSWDKDLL YQRGLAMGQE FKAKGAHILL GPVAGPLGRS AYSGRNWEGF
     SPDPYLTGVA MEHTINGHQD AGVQATAKHF IGNEQEVMRN PNFKKDGYVG EVDEEALSSN
     MDDRTMHELY LWPFANAAHA KAASFMCAYQ RLNGSYSCQN SKLLNGILRD ELGFQGYVMS
     DWGGTHAGVA TIESGLDMDM PGGIGAYGMD FKAGSFFGGN LTRAVTNGTL EEARVDDMIM
     RIMAPYFWLG QDKEDYPSID ESSADLNTFS PRKTWLKEFN FTGTRSRDVR GDHGALIRKH
     GAESTVLLKN ENNALPLKKP KSIAVFGNDA GDITEGFYNQ KDFEFGNLVV GGGSGTGRLT
     YLVSPLTAIN ARAKQDGTLV QQWMNNTLIT TSNVTDLWIP ALPDVCLVFL KTWATEGADR
     GHLSVDWNGD EVVLSVAKSC NNTVVVTHSS GINTLPWADH PNVTAILAAH YPGEESGNSL
     VDLLYGDVNP SGRLPYTIAL NGTDYNAPPT TAINTTGTDD WQSWFDEKLE IDYRYFDAQN
     MSVRYEFGFG LSYSTFEISD ISAEPLADDI TAMPEALPVQ PGGNPALWES IYNVTVSVAN
     SGKVDGATVP QLYVSFPESA PKGTPPKQLR GFEKVFLEAG ESKSVSFELM RRDLSYWDII
     SQQWVIPEGE FTIRVGFSSR DLKEETKVTL VKA
//
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