ID   A0A239KKM3_9ACTN        Unreviewed;       923 AA.
AC   A0A239KKM3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Exo-1,4-beta-glucosidase {ECO:0000313|EMBL:SNT18242.1};
GN   ORFNames=SAMN05216276_102788 {ECO:0000313|EMBL:SNT18242.1};
OS   Streptosporangium subroseum.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Streptosporangium.
OX   NCBI_TaxID=106412 {ECO:0000313|EMBL:SNT18242.1, ECO:0000313|Proteomes:UP000198282};
RN   [1] {ECO:0000313|EMBL:SNT18242.1, ECO:0000313|Proteomes:UP000198282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.2132 {ECO:0000313|EMBL:SNT18242.1,
RC   ECO:0000313|Proteomes:UP000198282};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FZOD01000027; SNT18242.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239KKM3; -.
DR   OrthoDB; 3187421at2; -.
DR   Proteomes; UP000198282; 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.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198282};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          706..776
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   DOMAIN          795..921
FT                   /note="Cellulose binding type IV"
FT                   /evidence="ECO:0000259|SMART:SM00606"
SQ   SEQUENCE   923 AA;  100259 MW;  2968A4DA7BE2FA20 CRC64;
     MNEPFRDPEL PLARRIADLQ ARLTLEEKVG LLHQYHAPVE RLGLGRFRTG TEALHGLAWM
     GPATVFPQAV GLASTWDPEL VRRVGEATSD EVVAFHHKDP DAAGLNVWAP VVNPLRDPRW
     GRNEEGYSED PWLTGVMATA YASGLRGSDP TVLKTAPTLK HFLGYNNETD RCVTSSNLPP
     RVLHEYELPA YRPALEQGAA VAVMPSYNLV NGRPAHLSPL INEVLRGWAP DDVLVVSDAY
     APGNLTGLQA YHDDGPEAYA HAIKAGLDSF TQDDDRTEVT LGHIRRALER DLLTESDLDV
     AVRHALSIRF RLGEFDPATP YDDITEAVVN CPEHQALARE AARRSIVLLR NDGILPLTSV
     RTIAVIGQLG DTLMEDWYSG TLPYAVTARA GLSERCETLF CEAVDRITLS AEDGPVIVDL
     DGGPLGIGTE PDTFDLFDWG GGSYALRATA TGRYLSVDDG GVLVNDQPGP SGWEVRQTFR
     MEDRPRGALA LRHISTGRYV ALEGEVFRLV DDADAAVWLT MERIVNGAEA AAALAATVDV
     AVVVVGDHPL VNGRETEDRL DLALPAAQQA VVRAVRAANP RTVMVISSGY PVTWADEDLP
     AVLWSSHGGQ EYGHALAEVL FGDADPEGRL TQTWYRSARE LPDLLDYDII AADATYQYFR
     GTPLYPFGHG LSYTTFDYGD LTVSVLDGRV TASATVTNTG SRAGVEVVQI YTHQQRSRVK
     QALRRLRGFV KVRLAPGEST RVGWTFDVGD LAFWDVTRNR SVVEDAPHKI MIGGSARDFR
     LSARFHVEGE NIPPRAVLDG PIPAVDHDEY DSVAFVDADR VSGDAVRSTA EGAWILFRSV
     DLGAGAASCA VRAVGTEGGV ITLRLDDPLY GPVIGDIPVP RAGRYDLAEL RTGLADARGV
     HDLYVVLENT GITVATLTFG KAV
//