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Database: UniProt
Entry: F9X9Y9_ZYMTI
LinkDB: F9X9Y9_ZYMTI
Original site: F9X9Y9_ZYMTI 
ID   F9X9Y9_ZYMTI            Unreviewed;       774 AA.
AC   F9X9Y9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   Name=MgBGL1 {ECO:0000313|EMBL:EGP87784.1};
GN   ORFNames=MYCGRDRAFT_85505 {ECO:0000313|EMBL:EGP87784.1};
OS   Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS   fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP87784.1, ECO:0000313|Proteomes:UP000008062};
RN   [1] {ECO:0000313|EMBL:EGP87784.1, ECO:0000313|Proteomes:UP000008062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX   PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA   Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA   Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA   Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA   Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA   Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA   van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA   Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA   Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA   Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA   Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA   de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA   Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT   "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT   reveals dispensome structure, chromosome plasticity, and stealth
RT   pathogenesis.";
RL   PLoS Genet. 7:E1002070-E1002070(2011).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336}.
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DR   EMBL; CM001199; EGP87784.1; -; Genomic_DNA.
DR   RefSeq; XP_003852808.1; XM_003852760.1.
DR   AlphaFoldDB; F9X9Y9; -.
DR   STRING; 336722.F9X9Y9; -.
DR   EnsemblFungi; Mycgr3T85505; Mycgr3P85505; Mycgr3G85505.
DR   GeneID; 13397129; -.
DR   KEGG; ztr:MYCGRDRAFT_85505; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_2_1_1; -.
DR   InParanoid; F9X9Y9; -.
DR   OrthoDB; 5486783at2759; -.
DR   Proteomes; UP000008062; Chromosome 4.
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:SF5; BETA-GLUCOSIDASE M-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:UP000008062};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..774
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003395560"
FT   DOMAIN          696..762
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   774 AA;  84329 MW;  16AF0CED82071F0A CRC64;
     MKSPTLILLQ AGALLLQVPS VDAIAYTNVS EIPLCGQSPP VYPTPQGTGG PSSAWRNSYA
     SALALVNQLT LEEKVNLTRG HVGTCVGNTP AVPRLGIRSL CFSDAPSGIR GQEFVSSFPA
     QLTVGATFDK ELMLAYGEAL GEEYHGKGIN IALLPVAGPL GRTARGGRNW EGFGADHYLS
     GVGMGLVTRG LQSKGVIAQM KHWLLNEQEW RRLPREDLGE SVSTNADDRT IWEGYVWPFM
     DALREGCGSA MCSYQRINNS YGCQNSKLLN GILKTDLGFQ GFVTSDWNAQ HAGVASANAG
     LDLVMPDGGY WGDNLTEAVT NGSVSSTRLD DMVTRILATW YHFNQDDVAA FPDPSVFNYD
     TQHPIVDVRG DHAAVIREIA AAGTVLVKNV DKALPLKAPR FLNIYGYDAT IPTAPWNTSA
     RFGGGYDVNF GWNTFDGTLI TAGGSGSNTP SGLVSPFEAI QRRVQADRGT TRWDFVNVQP
     TVYASADASI VFINAYASES FDRTTLADEW SDQLVNNVAA KHNNTIVVIH SAGIRLVDRW
     IEHPNVTAVV FALLPGEQSG NSIVDVLYGD VVPSGRLPFT VAKKEEDYGN LLNSSGTALP
     DPFPQIDFTE GLHVDYKYFD QQNLDVRFEF GYGLSYTEFE YGSTVEVVAV GDGPKDEYPA
     HLAPEDIPQG GSPKLWEVVY NVTFSIKNIG DVEAAEVPQL YLAVPNAPKW QLRGFEKTFL
     RCGEEKQVTL GLTRRDLSIW DVVAQNWRMQ KGTYGLFVGA SSRDKRIEGH LVVE
//
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