ID A0A2P6NCX3_9EUKA Unreviewed; 680 AA.
AC A0A2P6NCX3;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=PROFUN_10779 {ECO:0000313|EMBL:PRP81790.1};
OS Planoprotostelium fungivorum.
OC Eukaryota; Amoebozoa; Evosea; Variosea; Cavosteliida; Cavosteliaceae;
OC Planoprotostelium.
OX NCBI_TaxID=1890364 {ECO:0000313|EMBL:PRP81790.1, ECO:0000313|Proteomes:UP000241769};
RN [1] {ECO:0000313|EMBL:PRP81790.1, ECO:0000313|Proteomes:UP000241769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jena {ECO:0000313|EMBL:PRP81790.1,
RC ECO:0000313|Proteomes:UP000241769};
RX PubMed=29378020; DOI=10.1093/gbe/evy011;
RA Hillmann F., Forbes G., Novohradska S., Ferling I., Riege K., Groth M.,
RA Westermann M., Marz M., Spaller T., Winckler T., Schaap P., Glockner G.;
RT "Multiple Roots of Fruiting Body Formation in Amoebozoa.";
RL Genome Biol. Evol. 10:591-606(2018).
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:PRP81790.1}.
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DR EMBL; MDYQ01000117; PRP81790.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6NCX3; -.
DR STRING; 1890364.A0A2P6NCX3; -.
DR InParanoid; A0A2P6NCX3; -.
DR Proteomes; UP000241769; 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 Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000241769};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..680
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015192338"
FT DOMAIN 601..668
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 680 AA; 74551 MW; 9587BA041BAB9850 CRC64;
MRILLLVFLL VGYSSCETPE QRARQLVSTL TLDEKISLVH GSRGSYVGVT PAIPRVNIPQ
ANDQDGPQGE SFLSRNTNVT SVGVGDGLKN VTFWPCTLSV ISTWDPELME QYAAAIGWEQ
RQKGVNIHLG PMVNIARNPV GGRNFESFGE DPHLSSIMAD RYVRGVQSNR IVATVKHFVL
NNQEYNRTTT SANAGIRATW EIYYPAFHSA VKAGVGAVMC SYNRINDTWA CENQETLNRD
LKGKMNFTGF VMSDWGATHS TAKAANNGLD QEMPDGTYFG QPLKDAVING QVSQERLDDM
VVRFLTALYR VGIMDELQTG TTTTNARNST HDALSRKLAA ASAVLLKNDD ETLPIKDTVK
KIAIIGLDGN DRVTAGGGGS GGVVPPYVVT PLQGIKSRAG PDVQITYDDG SDLKRAAALA
AKSDLAVVFV SSWSSEGSDR QNLNVQSNGD QLIEAIAAAQ PETIVHGFVA GAVVMPWHSK
VKSIVVQFFP GQEVGNAVAD VLFGDVNPSA RLPVTFPISY DQVPAEKKTQ YPGVDNEANY
DEGLFVGYRW YDQKKQKPLY PFGHGLSYTR FKYGEAEVVE NSDGSFNFTF PVANAGKRSG
AEMYLSYPTS ALEPPRVLRG FEKVQLEAGQ MQKMNFRLGE EDMQIWNVVE DRWTAVKGRF
TAHFGSSSRN LHTKKAFNRN
//
