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Database: UniProt
Entry: M2QZB2_COCSN
LinkDB: M2QZB2_COCSN
Original site: M2QZB2_COCSN 
ID   M2QZB2_COCSN            Unreviewed;       869 AA.
AC   M2QZB2;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=COCSADRAFT_40034 {ECO:0000313|EMBL:EMD60394.1};
OS   Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS   spot blotch fungus) (Bipolaris sorokiniana).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD60394.1, ECO:0000313|Proteomes:UP000016934};
RN   [1] {ECO:0000313|EMBL:EMD60394.1, ECO:0000313|Proteomes:UP000016934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2] {ECO:0000313|Proteomes:UP000016934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(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   -!- 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; KB445650; EMD60394.1; -; Genomic_DNA.
DR   RefSeq; XP_007703594.1; XM_007705404.1.
DR   AlphaFoldDB; M2QZB2; -.
DR   SMR; M2QZB2; -.
DR   STRING; 665912.M2QZB2; -.
DR   GeneID; 19139627; -.
DR   KEGG; bsc:COCSADRAFT_40034; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_2_0_1; -.
DR   OMA; YYPSPWA; -.
DR   OrthoDB; 5486783at2759; -.
DR   Proteomes; UP000016934; Unassembled WGS sequence.
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:SF12; BETA-GLUCOSIDASE A-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, ECO:0000313|EMBL:EMD60394.1};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016934};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..869
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012949180"
FT   DOMAIN          786..854
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   869 AA;  94233 MW;  4F32FAB8106D8C98 CRC64;
     MLWLAQALLV GLAQASPRFP RATNDTGSGS LNNAQSPPFY PSPWVDPTTK DWAAAYEKAK
     AFVSQLTLIE KVNLTTGTGW QSDHCVGNVG AIPRLDFDPL CLQDSPLGIR FADYVSAFPA
     GGTVAASWDR YEFYTRGNEM GKEHRKKGVD IQLGPAIGPL GRHPKGGRNW EGFSPDPVLS
     GIAVAETVRG IQDAGVIACT KHYLLNEQEH FRQPGGFKDI PFVDAISSNT DDKTLHELYL
     WPFADAVRAG TGSIMCSYNK ANNSQVCQNS YLQNYILKGE LGFQGFILSD WDAQHSGVAS
     AYAGLDMTMP GDTGFNSGLS FWGTNLTVSI LNGTIPQWRL DDAAIRIMAA YYFVGLDESI
     PVNFDSWQTS TYGFEHFFGK KSFGLVNKHV DVREEHFRSI RRSAAKSTVL LKNSGVLPLS
     GKEKWTAVFG EDAGENPLGP NGCADRGCNS GTLAMGWGSG TADFPYLITP LEAIKREVNE
     NGGMITSVTD NYATSQIQNM ASRASHSIVF VNADSGEGYI TVDNNMGDRN NLTVWGNGDV
     LVKNVSALCN NTIVVIHSVG PVIVDAWKEN ANVTAILWAG LPGQESGNSI ADILYGHHNP
     GGKLPFTIGS SAEEYGPDII YEPTNGILSP QANFEEGVFI DYRAFDKAGI EPTYEFGFGL
     SYTTFEYSDI KVTAQSAKAY KPFTGQTSAA PTFGNFSKNP EDYQYPPGLV YPDTFIYPYL
     NSTDLKTASQ DPEYGLNVTW PKGSTDGSPQ ARIAAGGAPG GNPQLWDVLF KVEATITNTG
     DVAGDEVAQA YISLGGPHDP KVQLRDFDRL TIQPGESVVF TANITRRDVS NWDTVSQNWV
     ITEYPKTIHV GASSRNLPLS APLDTSSFK
//
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