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Database: UniProt
Entry: S0EKU6_GIBF5
LinkDB: S0EKU6_GIBF5
Original site: S0EKU6_GIBF5 
ID   S0EKU6_GIBF5            Unreviewed;       837 AA.
AC   S0EKU6;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   22-FEB-2023, entry version 37.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
GN   ORFNames=FFUJ_10572 {ECO:0000313|EMBL:CCT74517.1};
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS   and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT74517.1, ECO:0000313|Proteomes:UP000016800};
RN   [1] {ECO:0000313|Proteomes:UP000016800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC   {ECO:0000313|Proteomes:UP000016800};
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA   Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA   Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA   Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA   Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT   Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT   novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(2013).
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         ECO:0000256|RuleBase:RU361161};
CC   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC       {ECO:0000256|ARBA:ARBA00004987, ECO:0000256|RuleBase:RU361161}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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DR   EMBL; HF679032; CCT74517.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0EKU6; -.
DR   STRING; 1279085.S0EKU6; -.
DR   EnsemblFungi; CCT74517; CCT74517; FFUJ_10572.
DR   VEuPathDB; FungiDB:FFUJ_10572; -.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000016800; Chromosome 10.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 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   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
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   InterPro; IPR037524; PA14/GLEYA.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF3; BETA-GLUCOSIDASE B; 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.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
DR   PROSITE; PS51820; PA14; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361161};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016800}.
FT   DOMAIN          408..557
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   837 AA;  91135 MW;  8A9C0069692CDCA8 CRC64;
     MADTDIDAII QSLTLEEKIS LLAGRNFSET VGYPEKGVPS IKTADGPNGI RSAATDLDIK
     SACFPAACNL AATFDLDLAE KFGKALGAEA RGKRVNCMLG PTVCMHRHPL GGRNFESYSE
     DPFLTGKMSS KVIQGLQSLG ISATIKHFVA NEQETARTTV DETIDERALR EIYLRPFEIA
     VKEANPWAIM TAYNHVNGVH CDEHKWLLQD VLRGEWGWKG LVMSDWGGTN SVAAALNAGL
     DLEMPGPPRL RKEDAVKEAL ERGELTESTI NERAKSVVEW ALKLKAREAE SHSVALGQDT
     NTPELRSMIR EAGARGIVLL KNQGDLLPLT KEKVQKKKVA LIGFAKDAMA HGGGSAAVNA
     YRKITPWQGL HEALGDDVEF TYARGAHRER LLPAIHPDGL CGKVVGLDGK PGFSRQLFKE
     GESEPVSTVG QPTSAYSPLG SQESLWRRLE IVGDFTPAET GEHYIACSGL GPTRVYVDGE
     IIYEQTANCT DPMGSLFLAA PEPEFRHKFE GGKTYRLKIC SDPPTKIGLT ILEGRSGVRV
     GFSLESDHDA DLVGEAAEVA KAADYAIVFT GHDPQWETEG RDQDGFNLPR KGTQDALVST
     VASVNPNTVV VNSTGVAIAM PWLEQVPAVV QAWFPGQECG YSIADVLTGA VNPEGRLPVS
     FPKSIEDCPA HGNFPGEYID GQLKVTYAEG VFVGYRHFDR LPREKVNFPF GHGLSYTTFT
     HDLVNFSREV DDWYVSAEVS NTGKQAGSTL VQIYAGPAEQ SPDHPIKALV AFQKVRLEPG
     ETKLVKLLVK QRDLAHFNSG LKKWVIDEGE YRFSLGVSSA DIVGDTVVKV HKAIFDP
//
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