ID A0A2S6BT09_9PEZI Unreviewed; 781 AA.
AC A0A2S6BT09;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=CBER1_05723 {ECO:0000313|EMBL:PPJ50600.1};
OS Cercospora berteroae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ50600.1, ECO:0000313|Proteomes:UP000237631};
RN [1] {ECO:0000313|Proteomes:UP000237631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631};
RA de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A.,
RA Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT "Conservation of a gene cluster reveals novel cercosporin biosynthetic
RT mechanisms and extends production to the genus Colletotrichum.";
RL bioRxiv 0:0-0(2017).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PPJ50600.1}.
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DR EMBL; PNEN01001780; PPJ50600.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6BT09; -.
DR STRING; 357750.A0A2S6BT09; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000237631; 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; 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:UP000237631}.
FT DOMAIN 700..769
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 781 AA; 84975 MW; A46DC4794BB58565 CRC64;
MTLAAAQSHY PTGNDSLANA PYKDASVPIE DRISDLLSKM TIEEKALQLM QGDISNWLNT
TDGRFNRTGL ELNFAQKAGM YYVGYPISWD WLADNIKIGQ DYAMNETRLG IPAIVQTEGI
HGFLIGNATI YNSPIAYACS WNRTQVHDMA VQIGEEARAL GVSQLFAPVQ DLARELRWGR
VEETFGEDGY LAGEIGLAYV VGLQSTNVSA MVKHFAADSK PEQGLNVGPV QGGERELRTT
WLPPYKKAII DGGVWSIMSG YNSWDGVPVV SDHHLLEEIL RKEWGYEFYV MSDAGATDRL
ATPMNICPAP LNKYGSPFNA GNECVTLDAL PAGGDVEMGG GSFSYRSIPD LVAAGRLEEV
VVDTAVARVL RTKFAMGLFE RPYQIVAPEE RENVINTPAA KQLARELDRD SIVLLKNDQN
ILPISKDKKV AVIGPMAHGF MNYGDYVVYR SQYRGITPLD GIQAAIGNDS VTYAPGCERW
SNDQSGFPEA IAAAEAADVA VVVVGTWSRD QQELWQGLNA TTGEHVDVNS LDLVGAQRPL
LEAIINTTTP TIVVFSSGKP ITEAWISNTT ASLLQQFYPS EQGGHALADI LFEGNTSPSG
KLSVSFPYSV GALPVWYDHL NSARQIGDSG SVDPITGQIT FGHQYVIGSP DPWFPFGFGL
SYTNFTYADT ISLSSTNVSA SDTITASIVV TNSGSVAGAE VIQLYIKDMI ATVDVPNIQL
KGFEKVFFEP GESKEISIEF NVSDVGLWNR KMEYVVEPGE FTVFLGGSSA DLGRNATFWV
E
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