ID   S4MS65_9ACTN            Unreviewed;       962 AA.
AC   S4MS65;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Putative Exoglucanase B {ECO:0000313|EMBL:EPJ39541.1};
GN   ORFNames=STAFG_3421 {ECO:0000313|EMBL:EPJ39541.1};
OS   Streptomyces afghaniensis 772.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1283301 {ECO:0000313|EMBL:EPJ39541.1, ECO:0000313|Proteomes:UP000015001};
RN   [1] {ECO:0000313|EMBL:EPJ39541.1, ECO:0000313|Proteomes:UP000015001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=772 {ECO:0000313|EMBL:EPJ39541.1,
RC   ECO:0000313|Proteomes:UP000015001};
RA   Gruening B.A., Praeg A., Erxleben A., Guenther S., Fiedler H.-P.,
RA   Goodfellow M., Mueller M.;
RT   "Draft Genome Sequence of Streptomyces afghaniensis, Which Produces
RT   Compounds of the Julimycin B-Complex.";
RL   Submitted (FEB-2013) 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:EPJ39541.1}.
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DR   EMBL; AOPY01001415; EPJ39541.1; -; Genomic_DNA.
DR   AlphaFoldDB; S4MS65; -.
DR   PATRIC; fig|1283301.3.peg.3392; -.
DR   HOGENOM; CLU_302839_0_0_11; -.
DR   Proteomes; UP000015001; Unassembled WGS sequence.
DR   GO; GO:0008810; F:cellulase activity; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 2.170.160.10; Endo-1,4-beta-glucanase f. Domain 2; 1.
DR   Gene3D; 4.10.870.10; Endo-1,4-beta-glucanase f. Domain 3; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR023309; Endo-1-4-beta-glucanase_dom2.
DR   InterPro; IPR027390; Endoglucanase_F_dom3.
DR   InterPro; IPR000556; Glyco_hydro_48F.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF17957; Big_7; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF02011; Glyco_hydro_48; 1.
DR   PRINTS; PR00844; GLHYDRLASE48.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS51173; CBM2; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015001};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..962
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004521159"
FT   DOMAIN          26..135
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
SQ   SEQUENCE   962 AA;  102343 MW;  BDD4F46DF8FBC78A CRC64;
     MRRLWTAALA ALALPLTMLS SGSTSAQAAA LQCSVDYKTN DWGSGFTADL TLTNRGTDAI
     DGWTLTYAYS GNQKLGNGWN GTWSQSGQNI TVKNAPHNAR VAAGAAVSTG AQFSYSGSNT
     APTSFTVNGT PCTGAHQPPI AVLTSPAAGA VYTQGEAVPL AATAAAADNA TISKVEFYDD
     TKLLGTDTSA PYALSVSDLT VGSHSLVAKA YDSMGASADS TPVGITVASG PTVVASPLQL
     GVQSGKSGTY EVKLSKQPAS NVTVTSTRAS GNSGLSVTGG ASLTFTPQNW NTAQKVTVTA
     ADSGTGSAVF ESTAAGHAKA SVTVTQLAAA KTYDARFLEL YGKITNPANG YFSPEGIPYH
     SVETLIVEAP DHGHETTSEA YSYLLWLQAM YGKVTGDWSK FNGAWDLMEK YMIPTKADQP
     TNSFYNASKP ATYAPELDTP GEYPAKLDTG VSVGRDPIAA ELKSAYGTDD VYGMHWLQDV
     DNVYGYGNSP GKCEAGPSDT GPSYINTFQR GPQESVWETV PQPTCDAFKY GGKNGYLDLF
     TGDASYAKQW KFTNAPDADA RAVQAAYWAD LWAKEQGKGG QVSATVAKAA KMGDYLRYSM
     FDKYFKKIGN CVGPSACPAG TGKDASMYLM SWYYAWGGAT DTSAGWAWRI GSSHAHGGYQ
     NPLAAYALSS YAPLKPKSAT GAADWAKSMD RQLEFYRWLQ SDEGAIAGGA TNSWAGRYAT
     PPAGKSTFYG MYYDEKPVYH DPPSNQWFGF QAWSMERVAE LYQQTGNAQA KTVLDKWVDW
     ALSKTTFNPD GTFRIPSTLQ WSGQPDTWNA SSPGSNSGLH VTVADYTNDV GVAAAYAKTL
     TYYADRSGDT EAAAAAKKLL DGMWANHQDD IGLAVPENRA DYNRFDDSVS IPSGWTGTMP
     NGDAINSSST FDSIRSFYED DPAWSKIESY LAGGAVPSFT YHRFWAQADI ALAMGSYAEL
     LE
//