ID A0A1J4K2K6_9EUKA Unreviewed; 755 AA.
AC A0A1J4K2K6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN Name=bglB {ECO:0000313|EMBL:OHT05032.1};
GN ORFNames=TRFO_27353 {ECO:0000313|EMBL:OHT05032.1};
OS Tritrichomonas foetus.
OC Eukaryota; Metamonada; Parabasalia; Tritrichomonadida; Tritrichomonadidae;
OC Tritrichomonas.
OX NCBI_TaxID=1144522 {ECO:0000313|EMBL:OHT05032.1, ECO:0000313|Proteomes:UP000179807};
RN [1] {ECO:0000313|Proteomes:UP000179807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K {ECO:0000313|Proteomes:UP000179807};
RA Benchimol M., Almeida L.G., Vasconcelos A.T., Perreira-Neves A., Rosa I.A.,
RA Tasca T., Bogo M.R., de Souza W.;
RL Submitted (OCT-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 -!- 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:OHT05032.1}.
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DR EMBL; MLAK01000772; OHT05032.1; -; Genomic_DNA.
DR VEuPathDB; TrichDB:TRFO_27353; -.
DR OrthoDB; 5485475at2759; -.
DR Proteomes; UP000179807; 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: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; 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: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.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000179807}.
FT DOMAIN 582..652
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 755 AA; 84953 MW; 4AE0497C1699CD84 CRC64;
MSQRVKEIVA KLTLEEKASM CSGKDTWXTV DIPRLNVPSI MVADGPHGLR KQDEEASTTS
VNDSKIAVCF PAACCTSSSF DPELLYKMGE TLGDQCQSEN VSVILGPAVN IKRSPLCGRN
FEYMSEDPHV ASKMSSGLIR GLQSQNVGAC IKHFACNNQE YRRMVCSSEI DPRAIREIYL
SAFEDAIKES QPWTVMCSYN KINGRFASEN EWLLEKVLRE EWGYEGFVMS DWGAVNDRIE
GVKAGLELQM PGPCNYNDAL LVKAVQENKL DEKILDRCCE RILNIVFKAV DGKKQSTFDK
EKAHEXARQV AEESIVLLKN XEHILPLKXT TKVSFIGEFA KTPRYQGSGS SHINPFKVSN
AFDFCKDKYN VTYSQGYQTE KDEIDSKLEE EAITNARNSE VSVIFAGLPD AFESEGYDRS
HLRMPXCQNH LIEEICKVQP NTIVVLHNGS PIVLPWLHQV KGVLEVYLGG QAIGEATSRI
LYGEVNPSGK LSETFPCRLE DTPSYGNFPG YSDKVVYREG IMVGYRYYDA RNMEVIFPFG
HGLSYTTFEY SNLQVDKKDF LDKDIITVNV DIKNTGSVAG KEIVQLYISD HTNLVERPPK
ELRSFTKVLL APNETKTVTF TLNYRTWAYY DTELNDWHVN TGDYEILIGK SSRNIVLTQT
VHVKCTNPIV KPITLNSTWG DLLVNPITKS ITDEILNNHP ALKATYENVG DPNSEFLRVF
IDSLPLRSLP VVFPFDLDVP IEMVEKAKKL LAEAK
//