ID A0A1V9Z510_9STRA Unreviewed; 750 AA.
AC A0A1V9Z510;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, 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=ACHHYP_03011 {ECO:0000313|EMBL:OQR93007.1};
OS Achlya hypogyna.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Achlya.
OX NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR93007.1, ECO:0000313|Proteomes:UP000243579};
RN [1] {ECO:0000313|EMBL:OQR93007.1, ECO:0000313|Proteomes:UP000243579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR93007.1,
RC ECO:0000313|Proteomes:UP000243579};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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:OQR93007.1}.
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DR EMBL; JNBR01000433; OQR93007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9Z510; -.
DR STRING; 1202772.A0A1V9Z510; -.
DR OrthoDB; 5485475at2759; -.
DR Proteomes; UP000243579; 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, ECO:0000313|EMBL:OQR93007.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243579}.
FT DOMAIN 649..723
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 750 AA; 81456 MW; E252A475BED86C71 CRC64;
MVYPAPCPNV EERVRAIVES MDVDALVGQM TQLDISMLLK DDDKTLDLEK VRHFAKMKVG
SYLNSPFNGG PDANGKIGYS AEEWRAMLET IQAIHMEEND GHPIVYGIDS VHGAIYVRDA
IVFGQQINGA ATFNPTLVEQ MGYYTGRDTE AAGIPWIFAP ILDVSKNPLW PRTFETFGED
PHTVAVMGAA TVRGMQRNPQ TAACLKHFIG YSKSALGHDK DPVTLSDYEL LNHFAVPFLA
AIDAGAKTIM ENYVSVNDVP TMANSKLMID LLRHDMGYEG MVVTDWDEIN NLHTAHRVAK
TKADAVRLAL TRTSIDMSMV PFETSFIELT KALVATKPEL LARLRESVTR IVRLKVQLGL
YETPVPGLGN VVGAPDATAA ALAMAHESIV LLENKDSVLP LPEAASVFVT GHAADNVGYL
CGGWTVQWQG VSGNHQFAHG VTLKDGVMRI APQATYFNGC AADGTLTDMD TVLAHAAAAA
YTIVTVGEGS YCEKPGDIPC LDLPAGQAEY VRRIAATGTK VILVLVEGRP RLLHGLADVV
HAVVHAMLPG EVGGQAIADV LFGTVNPSGR LPITYPKDHA NILAQYNRRT MVRITDKEIG
VEWPFGHGLS YTTFAYSNLE LSRRVVESVD DVIDVRVTVT NTGTVTGKEV VMLFLAQPFR
TLAVPEVKQL KKFEKIELAP GASTVVTLSL TFADIGVFAP QIGYGFKRVV EEGDFVVLVK
PDTVVDVYAD DWAHPLAAKF TVACDLEQLL
//