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Database: UniProt
Entry: A0A101NI63_9ACTN
LinkDB: A0A101NI63_9ACTN
Original site: A0A101NI63_9ACTN 
ID   A0A101NI63_9ACTN        Unreviewed;       813 AA.
AC   A0A101NI63;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=AQI88_25960 {ECO:0000313|EMBL:KUM93529.1};
OS   Streptomyces cellostaticus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67285 {ECO:0000313|EMBL:KUM93529.1, ECO:0000313|Proteomes:UP000054241};
RN   [1] {ECO:0000313|EMBL:KUM93529.1, ECO:0000313|Proteomes:UP000054241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40189 {ECO:0000313|EMBL:KUM93529.1,
RC   ECO:0000313|Proteomes:UP000054241};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces cellostaticus DSM 40189, type strain
RT   for the species Streptomyces cellostaticus.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336}.
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:KUM93529.1}.
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DR   EMBL; LMWL01000047; KUM93529.1; -; Genomic_DNA.
DR   RefSeq; WP_067003668.1; NZ_KQ948029.1.
DR   AlphaFoldDB; A0A101NI63; -.
DR   STRING; 67285.AQI88_25960; -.
DR   OrthoDB; 9803863at2; -.
DR   Proteomes; UP000054241; 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; 2.60.120.380; -; 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; 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   InterPro; IPR011658; PA14_dom.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF28; 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   SMART; SM00758; PA14; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KUM93529.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054241};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..813
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007101546"
FT   DOMAIN          410..540
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|SMART:SM00758"
FT   DOMAIN          726..797
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   REGION          324..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   813 AA;  86188 MW;  465BE2C9D65E58FE CRC64;
     MKRRIWVPSV FLTVLALLNL GAAPGSPGRE ESRADRLVAQ MTLDEKLSFV HWGYDTTDPT
     AMVYLPGVPR LGIPKLRATD GPAGVTIHRP SLAMPAPVSL ASSFDDGLAE KYGQVLGREG
     RAFNMDVLFA PMVNSIRVPQ AGRNFETFSE DPLLTGRTAA AEIKGIQSQG LMATVKHYAA
     NTQENNRMGV DVKVDDRTLH EMELPGFEAA AEAGTASVMC AYPKVNGEPA CGNGQLLNGI
     LREQLKFQGF VTSDWLATHS TDAITKGLDQ ELGIDTTEAI PPGGEVPGGK YFGDTLKKAV
     TDGTIPLSVL DRSVNRIVGQ MDRFGLLDKN PPPRPQRDLP GGTRVAQKVA ESGAVLLRNQ
     DRMLPLDAAA TDNLAVIGPT AKTPKVTGLG SSYIVPDVAT APLDTITKKL GAGAHVSYAE
     GENIEGEPIP ASALQPAFAG GTVLQPAKSG VIYDGKLTVD KAGLYRIAAR VTGGNGAIQI
     DNGDFISIGE VFGKLTSVPL KLTAGTHTVK ISGGAVVGKP MTLDLSWVTP AKAQEAIDQA
     VATARKATTA VVFAYDDGAE GSDRTSLSLP GHQDELIKAV TAANPRTVVV LNTGSSVTMP
     WLDKTRAVLD MWYPGQAGAE ATADLLFGDA EPGGRLSQTF PASEQATPVA GDPGRYPGVD
     GVVRYSEGIY SGYRWYDHQG VKPLFPFGFG LSYTSFAYED QAVKRTADGF DVDVTVRNTG
     NRPGSEVVQV YLGPSGQLTL DQADKALAGY QKVELKAGES RRVHLHVAER ALQYWDTSAG
     AWKLGGGERR VLIGSSSDQI RLTATVRADR PGQ
//
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