ID A0A3R7JYT0_9STRA Unreviewed; 782 AA.
AC A0A3R7JYT0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=BBI17_000957 {ECO:0000313|EMBL:RLN44424.1}, BBO99_00000863
GN {ECO:0000313|EMBL:RLN85017.1};
OS Phytophthora kernoviae.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=325452 {ECO:0000313|EMBL:RLN85017.1, ECO:0000313|Proteomes:UP000285624};
RN [1] {ECO:0000313|Proteomes:UP000285624, ECO:0000313|Proteomes:UP000285883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chile2 {ECO:0000313|EMBL:RLN44424.1}, and Chile4
RC {ECO:0000313|EMBL:RLN85017.1};
RA Studholme D.J., Sanfuentes E., Panda P., Hill R., Sambles C., Grant M.,
RA Williams N.M., Mcdougal R.L.;
RT "Genome sequencing of oomycete isolates from Chile give support for New
RT Zealand origin for Phytophthora kernoviae and make available the first
RT Nothophytophthora sp. genome.";
RL Submitted (JUL-2018) 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 -!- 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:RLN85017.1}.
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DR EMBL; MAYM02000295; RLN44424.1; -; Genomic_DNA.
DR EMBL; MBDN02000012; RLN85017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7JYT0; -.
DR STRING; 325452.A0A3R7JYT0; -.
DR Proteomes; UP000285624; Unassembled WGS sequence.
DR Proteomes; UP000285883; 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; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC 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.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000285624};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..782
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033805537"
FT DOMAIN 672..746
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 782 AA; 85987 MW; 85905B3FA3E4D8EB CRC64;
MQSKLLYSAA LLSLPGAALA ASAADEMVYD AKAQAIVDGF TTAEVIGQMT QLDISLVINP
KDNTLNEDYV RVYAQQYVGS YLNTIWDEPM EKKFGWTASE FRAIVTRIQE ITMEENGGHP
MIYGIDSVHG ANYVDGAVIF PHQINSGASF NPDLVYEVGR ITARDTQAAG IPWIFGPILE
IAQNPLWSRT HETFGEDPYM ASVMADAIVR GLQSYNQSAA CMKHFIGYSK TPTGHDRDNV
IMADYDLLNY FLPPFKAAME AGAMSTMENY ISINGDPVIS SPRILKDLLR SDLGFDGVLL
SDWNEVNNLK DWHRIVSTYE EAVALSLKET SLDMSMVPND TKFIDYATNM LKTYPENEAR
LRESAKRIIK MKLKLGLYDN PVPGAQFEFM VGNDDDKATA LNMARESIVL LKNAEDVLPL
PKGASVFLTG HSADNVGYQC SGWSRSWQGY SGNKMYPNGV SVRQGFENLV GNDSFTYFNG
LLANGSISDE ELAMAVELAS QHEYTVAVIG EAHYTEKPGD IDNLELPEGQ VKFIEALRAT
GTKMIVVLFE GRPRLLGSIP DNSMAIINGM LPCEHGGQAM AEILYGEVNP SGRLPITYPK
DSGNIAIPYN HRVTTRCAYD NCWPQWEFGS GLSYTQFNYS AVTLDTTTIT SADSTLTATV
TITNVGDRAG KETVMLFVIQ PFRKISVPEI KQLKKFKKIE LEAGASMDVS FTLTTDDLSV
YDPQIGKGLK RVFEDSDYVV AVGPWTWCDV YNNITNPLCA EFSIDTSSGA GTVNVGAGVS
LV
//
