ID A0A2G5IEQ8_CERBT Unreviewed; 470 AA.
AC A0A2G5IEQ8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Beta-glucosidase 1B {ECO:0000313|EMBL:PIB03210.1};
GN ORFNames=CB0940_11847 {ECO:0000313|EMBL:PIB03210.1};
OS Cercospora beticola (Sugarbeet leaf spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=122368 {ECO:0000313|EMBL:PIB03210.1, ECO:0000313|Proteomes:UP000230605};
RN [1] {ECO:0000313|EMBL:PIB03210.1, ECO:0000313|Proteomes:UP000230605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=09-40 {ECO:0000313|EMBL:PIB03210.1,
RC ECO:0000313|Proteomes:UP000230605};
RA De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA Thomma B.P., Van De Peer Y., Bolton M.D.;
RT "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT several fungal lineages and shown to be expanded in Cercospora beticola
RT based on microsynteny with recipient genomes.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|RuleBase:RU003690}.
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:PIB03210.1}.
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DR EMBL; LKMD01000099; PIB03210.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5IEQ8; -.
DR SMR; A0A2G5IEQ8; -.
DR OrthoDB; 3373839at2759; -.
DR Proteomes; UP000230605; Chromosome 10.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 3: Inferred from homology;
SQ SEQUENCE 470 AA; 53334 MW; AC35FF8634DD1876 CRC64;
MTSARLPQDF LWGYATASYQ IEGGAHEDGR GDSIWDIFAG QPGKIADGSN GDIACDSYHR
YKEDVALLKE LGAKAYRFSV SWSRVIPLGG RQDPVNQAGL QYYLNLVDEL LANGIQPLVT
LFHWDLPQEL YTRYGGFLNK EEYVADFVNY SRLMFSTLGS KVKLWITYNE PWCTSILGYA
TGYFAPGHKS STEPWLVGHN ILLAHAAAVK VYREEFKPTQ QGQIGITLNG DWVEPWDANE
ALDVEACERK LEFSIAWFAD PVYHGDYPES MRRQLGDRLP TFTEAERAIV QGSNDFYGMN
HYTADYVKHR KDAPAEDDHG GNVETLKENK AGESIGPETQ SFWLRPHAVG FRKLINWISK
RYSRPTIYVT ENGTSLKGEN DLPLEQLLDD EFRAQYFRDY IGELAKAYSE DNIDVKGYMA
WSLMDNFEWA EGYETRFGVT YVDYAGGQKR MPKKSARVVA EVFSSLCGPK
//