ID A0A1E3HMC1_9TREE Unreviewed; 897 AA.
AC A0A1E3HMC1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=L202_04664 {ECO:0000313|EMBL:ODN77490.1};
OS Cryptococcus amylolentus CBS 6039.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN77490.1, ECO:0000313|Proteomes:UP000094065};
RN [1] {ECO:0000313|EMBL:ODN77490.1, ECO:0000313|Proteomes:UP000094065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN77490.1,
RC ECO:0000313|Proteomes:UP000094065};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-2016) 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 -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987}.
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:ODN77490.1}.
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DR EMBL; AWGJ01000007; ODN77490.1; -; Genomic_DNA.
DR RefSeq; XP_018992726.1; XM_019138783.1.
DR AlphaFoldDB; A0A1E3HMC1; -.
DR STRING; 1295533.A0A1E3HMC1; -.
DR GeneID; 30155973; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000094065; 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 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:SF10; BETA-GLUCOSIDASE F-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:ARBA00023001};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW Reference proteome {ECO:0000313|Proteomes:UP000094065};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..897
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009129290"
FT DOMAIN 814..883
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 34..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 897 AA; 96488 MW; 8AB149CD2B54EF2F CRC64;
MLASPLTLLL LGAGVPAAIA SPFRLINLRD DANSTDPVTD APTASWTQNS TTSASATEGW
NSTESWSSTA SASPVSVTSS VIEASTVSST IADPTSLTSW AESSVSATAS ESATADETWP
SEAPADDGTI SSYHTSDITY ISPNIPAPLN ATHANSSPKW EAAHSRARER LAGWSLEEKV
HLTTGVGWMQ GKCVGNIPAV ESQGFGGLCL QDSPLGVRFA DYVSAFPAGI NAAATFDKDL
IYARGYAMGQ EFKGKGVNVA LGPMTNMGRV AAGGRNWEGF GADPYLSGWA TDATVRGIQD
AGVQACVKHY VGNEQERNRT TSSSNIDDRT LREIYTHPFL RAVQADVAAV MCSYNLVNGS
WACQDSKTLN GVLKTDFGFQ GYVTADWGAQ HSGVLSANTG LDMTMPGDIS FGSLTSYWGQ
NLTDSVNNGS VKAERVDDMA ERILAAYYLL GQDEDYPEVN FDSFRLFGSN QSHVDVRDDH
YKVIRHVGAS STVLLKNENK ALPLTTPRHI ALIGSDLGPA IKGPNGISDR GGIDGTTAMG
WGSGTAEFPY LVDPLSAISQ RAREHGAILN SWLDDWDVAS AQYWAAPAEV AIVGVHATSG
EEYITVDGNV GDRNNLTLWT NGDALVQGVA AVNNNTIVVV HAPGPILMEE WISNPNVTAV
LWAGLPGQES GNALVDILWG DYNPSGRLPY TIAKDRADYP ADIVYTNTDD PIEPQVDYTE
GLNIDYRHFL AEGIEPRFAF GYGLSYTSFD FKDLKVEAVE GEKRKRDDVP EFPEVDESPQ
GEVVVGRFTV DSLHKPRWTV SIDVTNTGDI NGCEVPQLYL VFPEHAGEPP KVLRDFARIN
LDPGATKTVS WNLSQYDVSI WDVETQEWTV PEGDFGVEVG KYVADVDAQT SSFCFKA
//
