ID A0A1G9W966_9BACI Unreviewed; 1005 AA.
AC A0A1G9W966;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:SDM80989.1};
GN ORFNames=SAMN05216244_3476 {ECO:0000313|EMBL:SDM80989.1};
OS Sediminibacillus halophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Sediminibacillus.
OX NCBI_TaxID=482461 {ECO:0000313|EMBL:SDM80989.1, ECO:0000313|Proteomes:UP000182347};
RN [1] {ECO:0000313|EMBL:SDM80989.1, ECO:0000313|Proteomes:UP000182347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6199 {ECO:0000313|EMBL:SDM80989.1,
RC ECO:0000313|Proteomes:UP000182347};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNHF01000005; SDM80989.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9W966; -.
DR STRING; 482461.SAMN05216244_3476; -.
DR OrthoDB; 9805821at2; -.
DR Proteomes; UP000182347; Unassembled WGS sequence.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:InterPro.
DR CDD; cd04084; CBM6_xylanase-like; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
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; IPR008999; Actin-crosslinking.
DR InterPro; IPR044993; BXL.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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; PTHR42721:SF3; BETA-D-XYLOSIDASE 5-RELATED; 1.
DR PANTHER; PTHR42721; SUGAR HYDROLASE-RELATED; 1.
DR Pfam; PF03422; CBM_6; 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; SM00606; CBD_IV; 1.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF50405; Actin-crosslinking proteins; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51175; CBM6; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1005
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039319146"
FT DOMAIN 883..1005
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT REGION 512..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1005 AA; 111125 MW; A27F9B7CD47EB9D8 CRC64;
MILKKCWKVS LSLLLILVLV AQGFPAEKAD TIHAEHPAYE FSFQNPNLPL EKRVDDLLSR
LTLDEKVSLL HQYQPAIPRL GIKSFRTGTE ALHGVSWLGE ATVFPQATGL ANTWNKSLIK
EVGSAVGDEV RAFHKKYPED VGLSVWAPVV DLQRDPRAGR NEEGYGEDPY LAGQISTAYS
NGLKGSDSFY VKTIPTLKHF LGYNNEENRG ASSSSLDPRN LNEYQMKSFE YAIESGAALS
MMPAYNAING KPANLSPLIN DVVKDEWADD FFVVSDAGDI SGLVNDHQYV DTYAEAAALS
IKAGVDSFTD QDDNSEIVTG WVHDALDQGL LIESDIDKAI RNILTVRFRT GEFDGPELDP
YASIDEDVIN SEAHQRLALE TAREQLVLLK NDQQALPLNK DGEEKVAVIG PLADQVFNDF
YSGTLPYTVS TLDGVKEKVG GDRVDFSRGV DQIALQSKAT GQYVTASPDG DMNLAANADE
IGKNETFSLY DFGWDQYLLR SHANDKYVAN KNGSHDVVNN ETSPGRQENR PGTQDWFTYQ
NYNYEKQDDG SFALYNYQTG HWDTGLEGGR YVTVGEEAPH ALTATKQSVT GDTEKFEQTV
VVDGEAEAQK AAKDAETAIV VVGDQTMLNA RETIDREDII LPPSQKELIE KVAAVNENTI
VVLVSSYPMA MPEIENHPNV KSILYSAHGG QEEGNAIADA LFGDYAPAGR LNQTWYESVD
QLTDIMEYDI IKGERTYQYF EGEPLYPFGH GLTYTVFEYS NLRLNSHHIK DDGEVTVRAD
VTNTGSIASD EVTQLYVHDK KASVKRPIEE LKGFERIHLE PGETKTITFT LPASELAFWD
VSQDKYVVES GTFDIMVGRS SENLKLKGTL KVDGEKVAPR DLTKVTNAEN YDDYSGVKIV
EESQSGYEAI GEIDTGDWTA FKNVKFSKGI SQLEVRVASN KGGGTIELRL NDPVSGKLAG
TIDVPETGGL QDWETVTTKV KKLAGKHDVY LTFNGNFRLD TFRLK
//
