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Database: UniProt
Entry: A0A0J7YSX2_STRVR
LinkDB: A0A0J7YSX2_STRVR
Original site: A0A0J7YSX2_STRVR 
ID   A0A0J7YSX2_STRVR        Unreviewed;       946 AA.
AC   A0A0J7YSX2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Sugar hydrolase {ECO:0000313|EMBL:KMS66604.1};
GN   ORFNames=ACM01_45670 {ECO:0000313|EMBL:KMS66604.1};
OS   Streptomyces viridochromogenes.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1938 {ECO:0000313|EMBL:KMS66604.1, ECO:0000313|Proteomes:UP000037432};
RN   [1] {ECO:0000313|EMBL:KMS66604.1, ECO:0000313|Proteomes:UP000037432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3414 {ECO:0000313|EMBL:KMS66604.1,
RC   ECO:0000313|Proteomes:UP000037432};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUN-2015) 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:KMS66604.1}.
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DR   EMBL; LFNT01000152; KMS66604.1; -; Genomic_DNA.
DR   RefSeq; WP_048587458.1; NZ_LFNT01000152.1.
DR   AlphaFoldDB; A0A0J7YSX2; -.
DR   PATRIC; fig|1938.3.peg.2068; -.
DR   OrthoDB; 9803863at2; -.
DR   Proteomes; UP000037432; 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   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:KMS66604.1};
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..946
FT                   /note="Cellulose binding type IV"
FT                   /evidence="ECO:0000259|SMART:SM00606"
SQ   SEQUENCE   946 AA;  102558 MW;  617FC02E187450D0 CRC64;
     MTAQTPPTPP FRDRRLPFAK RIDDLLTRLT LDEKIGFLHQ FAPAVERLGI EGFRTGQEAL
     HGVAWMGPAT VFPQAVGLGA TWNTELVRRV GEAVSKETRA MRARDERVGL NVWAPTVNLL
     RHPLWGRNEE GYSEDPKLTS AIATAYTRGL RGDHPTYWRT APVLKHWLAH NNETGRDVTS
     SSVRPRVLHE YDLRAFRETV EAGGTAGVMP AYNLVNGRPN HVSPYLREHL RTWTDEDLLV
     CSDAGAPSNL VDSEHYFDTH EEATAAALLA GVDSFTDHGT DGSKITARVR GALERGLLTE
     ADIDTAVRRQ LSVRFRLGEF DPEYDPHTLT KDFDTPAHRA LAQEAAEQSV VLLKNSGGLL
     PLAPDTRLAV VGLLADECKL DWYSGTLIHR STPLEGVYER FGAERVEFAE GVDRVLLKTS
     TGAFLHVPEA DADDEVRGAE GALDPALLAG RTDLPPLTTD PTGTEFALVD WGEGVLTLRA
     PDGRYLSVAE DGCVRASADQ PGGWVVQETF RLEAHENGHL LRHMGTGRHV SVAADGVRVA
     EANPETFQLI VVENGEDAVT RVTAQADVVL VVAGNDPHIH GRETEDRSTL HLPAHQERLL
     RAAHAANPNT VLALVSAYPY AVDHAALPAL LWMSHGGQAA GTALARVLAG DVSPAGRLPQ
     TWYAADTDLP DLLDYDVIGS RQTYLYFEGT PLFPFGHGLS YAAFSYADLS TRTTDDSLHV
     SFTVTNTGDV PADEVAQLYT RAVDPAVPRP RRELMAHSRV RLAPGERTEL SFEVPLSAFA
     FWDVARGGWR REPGPYEVLA GASSEDVRLR TTVILDGEAS APRPVRRRGL AAADFDEQSG
     IAIVDRTKTT GDSVTPAQGR SGQLVYRDCD FGDGVTEVTA ALSGDGAVEV SLDGGAVLAI
     LTAEAADDAS PYDYATLRAG IIAEGVRDVH LRLRGPVRLA HVGFSG
//
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