ID   A0A1Q9CHG0_SYMMI        Unreviewed;       928 AA.
AC   A0A1Q9CHG0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   Name=bglX {ECO:0000313|EMBL:OLP82372.1};
GN   ORFNames=AK812_SmicGene36981 {ECO:0000313|EMBL:OLP82372.1};
OS   Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS   microadriatica).
OC   Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC   Symbiodinium.
OX   NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP82372.1, ECO:0000313|Proteomes:UP000186817};
RN   [1] {ECO:0000313|EMBL:OLP82372.1, ECO:0000313|Proteomes:UP000186817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP82372.1,
RC   ECO:0000313|Proteomes:UP000186817};
RA   Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA   Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA   Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT   "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT   adaptations to a symbiotic lifestyle.";
RL   Submitted (FEB-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   -!- 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:OLP82372.1}.
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DR   EMBL; LSRX01001199; OLP82372.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q9CHG0; -.
DR   OMA; DWSATMA; -.
DR   OrthoDB; 366914at2759; -.
DR   Proteomes; UP000186817; 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; 2.
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:SF121; PERIPLASMIC 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; 2.
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:UP000186817};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..928
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013045164"
FT   TRANSMEM        489..522
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          763..832
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   928 AA;  98096 MW;  DA6AD986618D7D1F CRC64;
     MVALQLLPLF LLWRLCHSRG LQSTLPEDGL IEQLLEKMTV EEKVGQLGVF TRPSPGEDAW
     NTTLSQVRRG EVGGFFNGAG VAMNRHLQRL AVEESRLGIP LLFAGDVWHG MWTIFPVPLA
     EASAWSPYLS EETARATAVE AGASGLSWTF APMVDLARDQ RWGRNVEGAG EDPFLASLLA
     EARVRGFQGP DLHLNTSLGA CLKHFAGYSG VEAGLDYSET DISLQTFREM FLPPFQAGID
     AGAVSVMSAL NALNGVPCSG NRWLLSDLLR GELQFLGLVV SDYESDTEMV PFGFVQDDSD
     AARVALAAGV DMSMQSGAFR SHLPKLAAHG RLDMKRLDEA VRHVLQLKAR LGLFQDPYRS
     LDPRGEWPQG GLAEKHDELA RRAARESLVL LKNDGQLLPL TKCYAKIALV GWWENDMDNA
     EGCEGGGGGS GDGGGGGGGG GGGGSGGAGA GAGAGAGAGA GAGAGAGAGA GAGAGGGGGG
     GGAEVVVTVV AAVVVLVLVL VLVLALLVVL AAVAAIVAAV AWRGGGEACV GVNWGNKSHT
     VTLRQGLLDV VGAENLRALA GSRMDTRIPG GITAAVEAAS WADVVVLALG EGVNYTGESR
     SRWDIGLPSA QQELAEAVAL TGKPLVVLLK NGRALQLDGA VKDAASIMVT WFLGKMTGAA
     IADVLFGDYS PSGRLPVSFP ISGGQAPYHY NHRSTGRPCA WPKHFTNCWV DGPSRALYPF
     GHGLTYSQVI YEDLWLSSDK LDWDGEIWIQ CTVVNAGRRA VQEVVQLYVR DRVASRIRPI
     RELKGFRKLL LEPGKRETVS FSLARHQLSF FVEGAVPTAE PGAFDVFVAP SSAGGTGKRF
     ELLPPLETHV RSLEQPPCVS LFLFRLHRLS HHTVSASIDA GGNAFHSAPG ISEASIQAET
     KERKLTKEEI ETKVLEYMRQ GPAQEKSS
//