ID E4ZPY2_LEPMJ Unreviewed; 882 AA.
AC E4ZPY2;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=LEMA_P044180.1 {ECO:0000313|EMBL:CBX93517.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FP929105; CBX93517.1; -; Genomic_DNA.
DR RefSeq; XP_003836882.1; XM_003836834.1.
DR AlphaFoldDB; E4ZPY2; -.
DR STRING; 985895.E4ZPY2; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR EnsemblFungi; CBX93517; CBX93517; LEMA_P044180.1.
DR GeneID; 13282677; -.
DR eggNOG; ENOG502QQ55; Eukaryota.
DR HOGENOM; CLU_004542_5_1_1; -.
DR InParanoid; E4ZPY2; -.
DR OMA; MSAYHSY; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000002668; Genome.
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; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC 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 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:UP000002668}.
FT DOMAIN 801..870
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 882 AA; 96310 MW; 12A8C8B348A08BC9 CRC64;
MSIVSWPPKA ISAYKKCSKK WKMLFALHRS DDMRVMIHTH VLHCPSLHRT ILSDMDNGNC
YFALITSCPL GRAGQDIDVV FGQQPTTINF DSHLKMRQFS LGTALLLGSS LFSTSTAYDL
IRKRQAANAT YKDASASVDD RVSDLLSRMT IEEKTSQLIQ GDLINWINST TNAFNSTGLE
WNFRVRAGQF YVGHAMPPEW ISAGIKTAQE YIMHNTTLGI PALTQTEGIH GLLVGNATIF
NSPIAMACSW NPELIYDMAV AIAKESQALG INQLFAPVVD LARELRFGRV EETYGEDPFL
AGELGYQYVK AVQSLNVSAT VKHFAGFSMP EQGLNTGPVH GGEREMRTTW LPPFKRSIID
AGAWNVMGAY HSYDGIPSIA DGHIQETILR EEWGYKYWVT SDAGATDRLC CTFKLCQCKT
ADKPIDKEAV TLMALPNGND VEMGGGSYNF EMIPKLVEEG KLDIEVVDRA VSRQLRAKFE
MGLFENPYLG ISENATSSII HTPENVALAR ELEAESIVLL ENKNAILPLS KSANIAVIGP
MANITNLGDY VVYRSQYNPT NVTPLQGLQN ATSGTVTYAQ GCERWSNDQS GFGAAISAAE
GADVAVVIVG TWSRDQNELW QGLNATTGEH VDVASLNLVG AMGPLVQAII DTGKPTVVVY
SSGKPITEPW ISENAAALVQ QFYPGEQGGN ALADVLYGNV NPSGKLSVSF PHDVGTLPVY
YDYLNSGRYT SPGAILPNGT LQFGHQYVLH TPQPLYEFGY GLSYANFTYS NVTLSKTEVT
ADEKITASVS ITNESGMDGK EVVQFYVQDV IASIVVPNKE LKGFKKVMVK AGETVDVSVE
LDVAQWGLWD RKMKYVVEKG EFVVHAGASS SDLRANGTVT VV
//
