ID   C9Z277_STRSW            Unreviewed;       950 AA.
AC   C9Z277;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Putative glycosyl hydrolase {ECO:0000313|EMBL:CBG69669.1};
GN   OrderedLocusNames=SCAB_25641 {ECO:0000313|EMBL:CBG69669.1};
OS   Streptomyces scabiei (strain 87.22).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG69669.1, ECO:0000313|Proteomes:UP000001444};
RN   [1] {ECO:0000313|EMBL:CBG69669.1, ECO:0000313|Proteomes:UP000001444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.22 {ECO:0000313|EMBL:CBG69669.1,
RC   ECO:0000313|Proteomes:UP000001444};
RX   PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA   Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA   Loria R.;
RT   "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT   cluster that contributes to plant-microbe interactions.";
RL   Mol. Plant Microbe Interact. 23:161-175(2010).
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DR   EMBL; FN554889; CBG69669.1; -; Genomic_DNA.
DR   RefSeq; WP_013000357.1; NC_013929.1.
DR   AlphaFoldDB; C9Z277; -.
DR   STRING; 680198.SCAB_25641; -.
DR   CAZy; CBM6; Carbohydrate-Binding Module Family 6.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   GeneID; 24313200; -.
DR   KEGG; scb:SCAB_25641; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_004542_5_3_11; -.
DR   Proteomes; UP000001444; Chromosome.
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:CBG69669.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001444};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          739..809
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   DOMAIN          828..950
FT                   /note="Cellulose binding type IV"
FT                   /evidence="ECO:0000259|SMART:SM00606"
SQ   SEQUENCE   950 AA;  102083 MW;  AA436F2B3D4766AD CRC64;
     MTAETTPTPP FRDPQLPVAK RIDDLLQRLT PDERIAFLHQ FAPAVDRLGV AAFRTGQEAL
     HGVAWMGPAT VFPQAVGLGA TWNEELVRRV GEAVSGEVRA MRARDDRVGL NVWSPTVNLL
     RHPLWGRNEE GYSEDPRLTS AIATAYTRGL RGDHPTYWRT APVLKHWLAH NNETDRSTTS
     SSVRPRVLRE YDLRAFRETV EAGAVAGVMP AYNLVNGRPN HVSPLLAEQL RTWTDEPLLV
     CSDAGAPSNL VDSEHYFDTH EEATAASLRA GVDSFTDHGT DGSTITGRVR DALTRSLLTM
     DDIDEAVRRQ LSVRFRLGEF DPGSDPYAGV EDFDTPAHRA LAREAAEQAV VLLRNEGGLL
     PLAADTRVAV VGPLADECKL DWYSGTLLHR STPLEGLYDR FGAERVTFAE GVDRVRLRAH
     STGAFVSVPE APEAADEVRG AQGALDPALL AGRTDLSPLT TDPDGSELAL VDWGEGVLTL
     RAPDGRYLSV ADDGFLRASA DQPGGWFVQE TFRLEPCAPH GTGHLLKHLG TGRYVTVGTD
     GVKVADGDPE TFDVVVTEHG EAAVARAAAE ADVVLVVAGN DPHINGRETE DRTTLALPAH
     QERLLRAART ANPNTALVLV SAYPYAVDVT GLPAVLWTAH GGQAAGTALA RVVAGDVSPA
     GRLPQTWYAS DADLPGLLDY DVIGSRQTYL YFEGTPLFPF GHGLSYAEFA YGNLTARVGD
     ADLTVSFTVT NTGAVTADEV AQLYVRAEDP SVPRPRRELA GHRRVTLAPG ASTELTFRLP
     LSVLEFWDVT HGAWHREPGA YELLAGASSE DIRLRTTVTV DGEPLAPRPV LARGLDAADY
     DEQRDTEIVD RTRVSGDAVT PAGDRPGELL YRACDFGAGV TEVTVEVAGA GSVELALADG
     PAPVTLTLDR PTAGPYAYTT LRAAVSAAGT RDVRLVLRGP LRLAHVGFSG
//