ID   U7Q0W2_SPOS1            Unreviewed;       800 AA.
AC   U7Q0W2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=HMPREF1624_01857 {ECO:0000313|EMBL:ERT00630.1};
OS   Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS   disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX   NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERT00630.1, ECO:0000313|Proteomes:UP000018087};
RN   [1] {ECO:0000313|Proteomes:UP000018087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58251 / de Perez 2211183
RC   {ECO:0000313|Proteomes:UP000018087};
RX   PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA   Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA   Goldberg J., Young S., Zeng Q., Birren B.W.;
RT   "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT   58251).";
RL   Genome Announc. 2:E0044614-E0044614(2014).
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; KI440843; ERT00630.1; -; Genomic_DNA.
DR   AlphaFoldDB; U7Q0W2; -.
DR   STRING; 1391915.U7Q0W2; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_2_1_1; -.
DR   OrthoDB; 5486783at2759; -.
DR   Proteomes; UP000018087; 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:SF5; BETA-GLUCOSIDASE M-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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000018087}.
FT   DOMAIN          705..787
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   800 AA;  85829 MW;  63CD4D07F92E56DE CRC64;
     MKISPLSYVV LFFSGGCRAR GSISGASPPS EVPYYGLSPP VYPSPQGNGT TDSRWARAYQ
     QARSLVEQLT LEEKVNLTHG HPGPCAGNSL PIPRLGLPSF CFSDAPTGVR GQEFVSGFPA
     GIHVAATFDA DLMYRYGEAV GQEFYGKGVH AALGPVSGPL GRIARGGRNW EGLGNDPYLS
     GIAVGAVTRG MQSAGVIATP KHFLLNEQEF RRRDAERQRG DHVVGEGISS NVDDRALHEL
     YVFPFMNALR AGAASIMCSY QRANHSYASQ NSKLLNGILK TELGFEGFVI SDWDAQHSGV
     ASALAGLDVA MPDSKGYWGD GLLLAAVNNG SVAVERIDDM ATRLLAAWHY VGETDTGGAA
     FPSPPAIYPT STQRHAIVDV QADHASLIRM IGAAGTVLVK NVNNTLPLQR PRFLCVYGYD
     AVLKADPWDN PSRFGGGYEV NFGWNTLNGT LITGGGSGGT SPPYVVSPFQ ALQERVVQDG
     GILRWDFFSE KPAVAYANAD ACLVFINAYA SESFDRPSLS DAFSDNLVNN VASMCANTIV
     VVHSAGIRVV DAWIDHVNVT AVLFAGLPGQ ESGHSLTDIL YGDVNPSGRL PYTVARREAD
     YGDLLNSSYS TDYFPEDNYD EGLYIDYRAF DHKGLVPRFS FGFGLSYTTF SYSRSLSAEL
     VSTGTPSKFP DPSVPVVQGG HPSLWDTIAE VKCSVTNTGR VAGTEVVQLY VGVPGANGDD
     PATQTAAGGD SPVRQLRGFH RVGPLSPGET SDVTFALTRR DLSVWDVEAQ QWRIRRGVFR
     LYIGASSRDL RLNGTLNISG
//