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Database: UniProt
Entry: A0A0F4GFR3_9PEZI
LinkDB: A0A0F4GFR3_9PEZI
Original site: A0A0F4GFR3_9PEZI 
ID   A0A0F4GFR3_9PEZI        Unreviewed;       631 AA.
AC   A0A0F4GFR3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=TI39_contig803g00002 {ECO:0000313|EMBL:KJX96143.1};
OS   Zymoseptoria brevis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX96143.1, ECO:0000313|Proteomes:UP000033647};
RN   [1] {ECO:0000313|EMBL:KJX96143.1, ECO:0000313|Proteomes:UP000033647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zb18110 {ECO:0000313|EMBL:KJX96143.1,
RC   ECO:0000313|Proteomes:UP000033647};
RA   Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT   "RNA-seq based gene annotation and comparative genomics of four
RT   Zymoseptoria species reveal species-specific pathogenicity related genes
RT   and transposable element activity.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KJX96143.1}.
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DR   EMBL; LAFY01000795; KJX96143.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4GFR3; -.
DR   STRING; 1047168.A0A0F4GFR3; -.
DR   OrthoDB; 2657687at2759; -.
DR   Proteomes; UP000033647; Unassembled WGS sequence.
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; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   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   PANTHER; PTHR30620:SF120; BETA-GLUCOSIDASE C; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033647};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..631
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002468660"
FT   DOMAIN          66..414
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
SQ   SEQUENCE   631 AA;  68977 MW;  91F1D13EB605D721 CRC64;
     MSFSAGRKAF FATLLVTASF TRADTAVAPQ LTSRQTNAAT GEVLPYRNAT LCIDERLDDL
     LSRMTVAEKA GQLFHASITM GKNGTLAEAT SYRNSSAMEI GEKLISHFNY GGDVENVREV
     AGWHNLLQRT ALETRLGIPI SISSDPRHSF TENIGTGFAA KSLSQWPESL GLAALRDPAW
     TLKFAEIARE EYMALGIRGA LHPQVDLSTE YRWARIANTM GEDANLTSQL VAAYIKGFQG
     EELGHNSVTT VTKHFPGAGP MENGEDSHFT YGKNQVYPGL NFEHHLIPFK AAIAAGARQM
     MPYYSRPIGT QYEEVAFSFN KGIITGLLRN ELGFEGIVVS DWGLITDTVI AGQDMPARAW
     GVEQLSELDR AARVLGAGVD QFGGEQRTEL IIELVENGSV FEERLDVSVR RLLREKFILG
     LFDNPFIDVD RAEQIVGNPY FVRLGAEAQR ASYTLLKNEN SLLPIKNPAG MKIYIDGFNT
     TYLDGRDVTL VDSPEEAELA IVRLQAPFEP RPGGFESMYT AGSLEFNTTE KARQAAIYSA
     VPTVVDTKLG RPAAIPEIAE QAAALFGNYG ASPEALLDVI FNVQGAKPLG KLPFDLPRSD
     AAVEASKEDV PFDTVDPVYR FGDGLAYADE C
//
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