ID A0A1V9YY64_9STRA Unreviewed; 823 AA.
AC A0A1V9YY64;
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=THRCLA_09261 {ECO:0000313|EMBL:OQR90597.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:OQR90597.1, ECO:0000313|Proteomes:UP000243217};
RN [1] {ECO:0000313|EMBL:OQR90597.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQR90597.1,
RC ECO:0000313|Proteomes:UP000243217};
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:OQR90597.1}.
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DR EMBL; JNBS01002513; OQR90597.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9YY64; -.
DR STRING; 74557.A0A1V9YY64; -.
DR OrthoDB; 5485475at2759; -.
DR Proteomes; UP000243217; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000243217};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 5..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 732..806
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 823 AA; 90440 MW; BD04B663000D0C71 CRC64;
MILRYVVLIS SAIIAWSVLY IAQMHNTLIS PVALQEKAVG DDTISIDEQV EKLLQSMTLA
QKVGQMTQID VSDVLYGKSR DPVLAINRAR VAVYAKLGIG SYFNSPFDAT IHPHGRTGWT
ATEWRMFLGS IQAIYKEHNA IPFIYGIDTT HGANYVQNAT IFPQPLATAS TFNPELAHAM
GRIEAKDSIA AGIPWIFSPV LGIAMQPKWS RVYETFGEDP YLVSQMGVAV IRGIQSLNLS
AACMKHFIGY SNPTSGNDRA DSVITDFELL NYYAPPFIAA VRDGNVLSAM ETYTSVNGDP
VVQSRKLLVD LLRNDIQFDG LLVSDDDEIH RLVAEHHVAR NELEALEMVM NHTSLDMNMV
SEKHRSTSLL SKLINASHIP TSRLDDSVRR ILKLKASLGL LPTSESEAAK HATITSNHLT
SVGSQEDLQL AQTTADESII LLKNKMQEPI DAVNPKLVLP IIDPNSKIFI TGPLAHNKAY
LCGGWTVYWQ GTDDSDQIPH GLTIKEALEA RFKNVVHHEG VDIDGYADGE VRAPIADEEE
NILTLSAKYN TSLARAAAAD YTIVVVGEAP YAEKSGDIDD LTLPQGQLDY ITTLSSVKST
NVIVVIIAGR PRLLAKSLAN VQAVLLSFLP CEAGGEAIAK VIAGDVNPSG RLPLTYPSST
GHIHVPYFHR MNIACKESFS ECPVEWPFGS GLSYTTFKYD NLTLSEWRVN KENGTLGVQV
AVTNTGTRAG KEVVMLFVSQ KVRHFSVPET KMLRRFKKID LPPGGVEIVH FELTSEDWSY
YAPQIGNGFQ SVAEEGLFHV LIKHDTTCNS VKKNSMCAHF HVV
//
