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Database: UniProt
Entry: N1RTQ3_FUSC4
LinkDB: N1RTQ3_FUSC4
Original site: N1RTQ3_FUSC4 
ID   N1RTQ3_FUSC4            Unreviewed;       838 AA.
AC   N1RTQ3;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN   ORFNames=FOC4_g10005674 {ECO:0000313|EMBL:EMT67572.1};
OS   Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=2502994 {ECO:0000313|EMBL:EMT67572.1, ECO:0000313|Proteomes:UP000016929};
RN   [1] {ECO:0000313|Proteomes:UP000016929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RA   Fang X., Huang J.;
RT   "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT   banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000016929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RX   PubMed=24743270;
RA   Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA   Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA   Fang X., Peng M., Huang J.;
RT   "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT   oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL   PLoS ONE 9:E95543-E95543(2014).
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; KB726570; EMT67572.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1RTQ3; -.
DR   STRING; 1229665.N1RTQ3; -.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000016929; Unassembled WGS sequence.
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   InterPro; IPR011658; PA14_dom.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF28; BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   Pfam; PF07691; PA14; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SMART; SM00758; PA14; 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:UP000016929}.
FT   DOMAIN          403..563
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   838 AA;  91331 MW;  00FEA841E855880F CRC64;
     MHILQRQPID VESTLASLTL AEKISLLSGS DFWNSQAISS HGISSVKCTD GPNGARGGRF
     FNPVPALCIP CGTGLGATWN PDLLYSAGQL LSRECDAKGA HVWLGPTVNL VRGPLNGRGF
     ESFSEDPHLS GVLATAIING VQSRGTAAAL KHFVANDQET AKMSTDICMS ERALREVYLK
     PFQMAVRDAK PKIVMSSYNK VNGVHVSESR KLLKDVLRSE WGFDGLVMSD WYGTYGCTDA
     LNAGVDIEMP GPSRHRADKA LVAVVSGKVS RKTIDERARK VLELGNATAS ARVSTKESTR
     DSPEDRALNR RLATESLVLL KNSDKILPIN PQDCEDIAII GPNAKLPAAC GGGSANLRPY
     YTSSVFQGIS DQLPSNANVH FEPGVFGHVL LPYFTGDHVT DENGMPGVSI SFFNEPESAW
     QTRKPFDRQS IPDTTYQLMD YDHPERGGTF YMSMTAYYKP DIEGTYEFGL ASYGVSRLYI
     DEHLVIDNAT SQTHAGMFFG HGSREERGTH EMKPGKTYRL RVEAGSASTS ITTGGSFIPI
     PGGACRLGGC LKLDPEEGIR RAVTVAKKCK HTFVVVGLNA DFEKEGKDRE SMSLPPHVDD
     LVSAVLKAQP NAIVVTQAGN PIEMPWRHKA KTILHSWYGG NEAGNAVADV VFGKVNPSGK
     LPITFPSRLQ DGPTFLSFGS DNGRVYYSED VFVGHRWFDA RGIEPAFEFG HGLSYTTFST
     SNILVAEDGV RVKVKNTGKM AGAEVVMLYV SYDAAKSGQK SRFHRPVRTL IGFQKVFLEP
     GQEATAFVAL DKYSTAVWDE TADSWLCEAG TYTASFRSSS DSLEVSFKVE RDLYWNGA
//
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