ID W9W491_9EURO Unreviewed; 773 AA.
AC W9W491;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
GN ORFNames=A1O7_03319 {ECO:0000313|EMBL:EXJ62877.1};
OS Cladophialophora yegresii CBS 114405.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182544 {ECO:0000313|EMBL:EXJ62877.1, ECO:0000313|Proteomes:UP000019473};
RN [1] {ECO:0000313|EMBL:EXJ62877.1, ECO:0000313|Proteomes:UP000019473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114405 {ECO:0000313|EMBL:EXJ62877.1,
RC ECO:0000313|Proteomes:UP000019473};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora yegresii CBS 114405.";
RL Submitted (MAR-2013) 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 ECO:0000256|RuleBase:RU361161};
CC -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987, ECO:0000256|RuleBase:RU361161}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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:EXJ62877.1}.
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DR EMBL; AMGW01000002; EXJ62877.1; -; Genomic_DNA.
DR RefSeq; XP_007755531.1; XM_007757341.1.
DR AlphaFoldDB; W9W491; -.
DR STRING; 1182544.W9W491; -.
DR GeneID; 19177916; -.
DR VEuPathDB; FungiDB:A1O7_03319; -.
DR eggNOG; ENOG502QQ55; Eukaryota.
DR HOGENOM; CLU_004542_5_1_1; -.
DR OrthoDB; 5485475at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000019473; Unassembled WGS sequence.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
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; IPR019800; Glyco_hydro_3_AS.
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:SF28; 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.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361161};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000019473};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..773
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004934295"
FT DOMAIN 693..761
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 773 AA; 83759 MW; A5B0DE08EAEB23B6 CRC64;
MAGFLFCLLA LDISTALSAV LLPRQGDPTW QDTTLPAAQR ADALLPQLSW EEKIAQMGGI
RRLLGANATF NRTAWEALYP LQHGILSYGS QLNQAQDVLP YANMVREEQL NSSKVPWITV
TDSVNSIYVP GGTLFPATLS LSTSWNLPLY EEIVASIRDE NMALGTHWVL SPELDIAKEP
RNGRVGEMYG EDVYLVGEFA AQYVKTMQER DEGGHMKVAT TVKHFLYGQG SGGVNTASMD
GGVNHLYNDL AIPYIRVLKE KPASIMISYS SVDRIPMSMN TALIQDMLRS EMGFTGLIMS
DAMGILHLYT ESNVASSYKD AAIKALRAGL QLELAPGQPA CFPYLVNSSS DQEIVDLVNE
AARQHLIIKF DTAMFDLPLP TMENLNRTLR APQHLDVNRR ASREAIVLLS NDGFLPQANF
SQVALIGPFG DIIDPGSYAP TTSANPEYGR TLRGSLEARM GAGNVRYVKG VDIRTTSPND
TAGIQEAVAV AKAAGVAIVS LGSLSVYSQD AAVNQRTDGE FYSHASLAFP GNQQQLLDAV
LDTGVPTILV LNGGQAFVLN NSTMRCNAIL HQFLGGEFSA DALVEIITGQ VNPSGKLTIS
MPQADGAFPI YYDFLPSDNV GGGGSDPTDS TVCAGDWNLP CLNRDGAPMA FGYGLSYTTF
DISGPQVTNS NSSGGSISIF CTITNTGNVA GKEVVQVYFR QQYSDIELPN KRLVRFQKVE
LQPGEARQVK FVIDKADLGY YNNAKYQVDS GHYTFWVGSS SRMADLKNAT ISL
//