ID   A0A243RYN1_9ACTN        Unreviewed;       948 AA.
AC   A0A243RYN1;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Sugar hydrolase {ECO:0000313|EMBL:OUC99633.1};
GN   ORFNames=CA983_27715 {ECO:0000313|EMBL:OUC99633.1};
OS   Streptomyces swartbergensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=487165 {ECO:0000313|EMBL:OUC99633.1, ECO:0000313|Proteomes:UP000195105};
RN   [1] {ECO:0000313|EMBL:OUC99633.1, ECO:0000313|Proteomes:UP000195105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMC13 {ECO:0000313|EMBL:OUC99633.1};
RA   Le Roes-Hill M., Prins A., Durrell K.A.;
RT   "Biotechnological potential of actinobacteria isolated from South African
RT   environments.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:OUC99633.1}.
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DR   EMBL; NGFN01000207; OUC99633.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A243RYN1; -.
DR   Proteomes; UP000195105; 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, ECO:0000313|EMBL:OUC99633.1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          734..804
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   DOMAIN          823..948
FT                   /note="Cellulose binding type IV"
FT                   /evidence="ECO:0000259|SMART:SM00606"
SQ   SEQUENCE   948 AA;  101871 MW;  49FBF5A5B06E0B15 CRC64;
     MTAHTPPSPQ FRDPRLPFAK RIDDLLSRLT PAEKIAFLHQ FAPAVERLGI AAFRTGQEAL
     HGVAWMGPAT VFPQAVGLGA TWNPELVRRV GDAVSKEIRA LRAKDDRVGL NVWAPTVNLL
     RHPLWGRNEE GYSEDPKLTS AIATAYTHGL RGDHPTYWRT APVLKHWLAH NNETDRSTTS
     SSVRPRVLHE YDLKAFRETV EAGAVAGVMP AYNLVNGRPN HVSPYLGEHL RAWTDEDLLV
     CSDAGAPSNL VDSEHYFDTH EEATAASLVA GVDSFTDHGT DSSQMIGRLR GALERGLLTE
     ADVDTAVRRQ LSVRFRLGEF DPEYDPHDAT SEFDTPAHRA LAQEAAEQAV VLLKNDGLLP
     LAPDTRVAVV GLLADECKLD WYSGTLIHRS TPLEGLYERF GAERVEFAEG VDRVRLKTSA
     GTFLHVPVTE DAADEVRGGE GALDPALLAG RTDLPALTTD AAGTELALVD WGEDVLTLRA
     PDGRYLSVAD DGYVRASADQ PGGWIVQETF RLEPHENGHL LKHLGTGRHV SVSADGVKVA
     DEDPEVFELV VTERGEEAVA RAAAQADVVV VVAGNDPHIN GRETEDRTTL RLPGHQERLL
     RAARAANPAT VLTLVSAYPY AIDPADVPAV LWTAHGGQAA GTALARVLAG DVSPAGRLPQ
     TWYADDADLP GLLDYDLIGS RQTYLYFEGT PLFPFGHGLS YTSFAYDGLT ARVEDGSVHV
     SFTVTNTGDV TADEVAQLYT RALDPSVPRP RRELLDHRRV TLAPGATAEL GFQVPLSAFD
     FWDVAQDRWR LEPGAYELLA GASSEDVRLR TTVTLDGEPA LPRAVVADGL AAAGFDEQSG
     IEIVDRTKVS GDAVTPADGT AGELVYRACD FGPGISGVTV EVAGEGAVEL SLDGGPALAV
     LSTATPTSGQ YDYVSLGASV AAAGVHDVHD LHLRLRGPLR LAHVGFSG
//