ID   A0A0N1N9Z5_9ACTN        Unreviewed;       885 AA.
AC   A0A0N1N9Z5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Cellulose-binding family II {ECO:0000313|EMBL:KPH99295.1};
DE   Flags: Precursor;
GN   ORFNames=OK006_8461 {ECO:0000313|EMBL:KPH99295.1};
OS   Actinobacteria bacterium OK006.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1592326 {ECO:0000313|EMBL:KPH99295.1, ECO:0000313|Proteomes:UP000037912};
RN   [1] {ECO:0000313|EMBL:KPH99295.1, ECO:0000313|Proteomes:UP000037912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK006 {ECO:0000313|EMBL:KPH99295.1,
RC   ECO:0000313|Proteomes:UP000037912};
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT   "Draft genome sequences for four Actinobacteria strains OK006 OK074 OV450
RT   and OV320.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC       {ECO:0000256|ARBA:ARBA00037986}.
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:KPH99295.1}.
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DR   EMBL; LJCU01000272; KPH99295.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1N9Z5; -.
DR   PATRIC; fig|1592326.3.peg.10914; -.
DR   Proteomes; UP000037912; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd15482; Sialidase_non-viral; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR002860; BNR_rpt.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR018366; CBM2_CS.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR43739; XYLOGLUCANASE (EUROFUNG); 1.
DR   PANTHER; PTHR43739:SF2; XYLOGLUCANASE (EUROFUNG); 1.
DR   Pfam; PF02012; BNR; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 2.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00561; CBM2_A; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..885
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005878706"
FT   DOMAIN          775..885
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          760..781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   885 AA;  93099 MW;  FB02C2E7CB241BE5 CRC64;
     MRRIRILTAV LALAAGLMAG SPSALASSTP TTTLAADTYT WKNARIDGGG FVPGIVFNRS
     EKNLAYARTD IGGAYRWQES TKTWTPLTDS IGWDRWGHTG VVSLASDSVD PNKVYAAVGT
     YTNSWDPGNG AVLRSADRGA SWQRTDLPFK LGGNMPGRGM GERLAIDPHK DSVLYLGAPS
     GKGLWRSTGS GVTWSQVTNF PNVGTYVQDA TDTSGYTSDN QGIVWVTFDE STGTPGSATQ
     TIYVGVADQD NVVYRSTDGG ATWSRLAGQP TGQLAHKGVL DATNGYLYLA YSDKGGPYDG
     GKGRLWRYAT RTGTWTNISP VAEADTSYGF SGLTVDRQHP GTVMPTAYSS WWPDTQIFRS
     TDSGGTWTKA WDYTSYPNRS NRYTMDVSSV PWLTFNPNPS PPEQAPKLGW MTEGLEIDPF
     NSARMMYGTG ATIYGTENLT NWDSDSQFTI RPMVQGLEET AVNDLASPPS GATLLSALGD
     IGGFRHTDLT KVPSMMYTSP NFTTTTSLDY AETDPNTVVR VGNLDSGPHI AFSTDNGANW
     FAGTDPSSVS GGGTVAAASD GSRFLWSPVG AGVRYTASFG TSWSASGGIP SGAIVESDRV
     DPKTFYGFKS GNFYVSSDGG ATFTASAATG LPSGDSVRFK ALPGAKGDVW LAGGASDGAY
     GLWHSTDGGA SFTKLSNVDR ADTIGFGKAA TGASYQTLYT SAKIGGVRGI FRSTDKGASW
     TRINDDAHQW GWTGGAITGD PRIYGRVYIA TNGRGIIYGD SSDTGGGGGG GTDPTPPPTG
     ACGATYKITN QWSGGFQADV ALTNTGTTAW SGWSLSWAFA DGQKITQAWN ADAAQSGTSV
     TAKNLTWNAN VAAGSSVSFG FTGSRTGSNA TPTSFKLGDQ TCTVR
//