ID A0A0A0BUA0_9CELL Unreviewed; 372 AA.
AC A0A0A0BUA0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Cellulose-binding protein {ECO:0000313|EMBL:KGM10704.1};
GN ORFNames=N869_01100 {ECO:0000313|EMBL:KGM10704.1};
OS Cellulomonas bogoriensis 69B4 = DSM 16987.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1386082 {ECO:0000313|EMBL:KGM10704.1, ECO:0000313|Proteomes:UP000054314};
RN [1] {ECO:0000313|EMBL:KGM10704.1, ECO:0000313|Proteomes:UP000054314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=69B4 {ECO:0000313|EMBL:KGM10704.1,
RC ECO:0000313|Proteomes:UP000054314};
RA Chen F., Li Y., Wang G.;
RT "Genome sequencing of Cellulomonas bogoriensis 69B4.";
RL Submitted (AUG-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:KGM10704.1}.
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DR EMBL; AXCZ01000135; KGM10704.1; -; Genomic_DNA.
DR RefSeq; WP_035061660.1; NZ_AXCZ01000135.1.
DR AlphaFoldDB; A0A0A0BUA0; -.
DR OrthoDB; 5179374at2; -.
DR Proteomes; UP000054314; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd21177; LPMO_AA10; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.70.50.50; chitin-binding protein cbp21; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR004302; Cellulose/chitin-bd_N.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR34823:SF1; CHITIN-BINDING TYPE-4 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR34823; GLCNAC-BINDING PROTEIN A; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF03067; LPMO_10; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR PROSITE; PS51173; CBM2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000054314};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..36
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 37..372
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038705792"
FT DOMAIN 278..372
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 221..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..243
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 372 AA; 39161 MW; 91E4F099B526DC68 CRC64;
MTARARLRKI AIALPVVVAA PLAVTAIMAS PAAAHGAVTD PPTRNFGCLD RWRNNHLAPE
MRDQDPMCQG AYQAEPGAMW NWNGLYQDNV GGRHEAAVPD GTLCSGGNAE GGRYDFLDTP
GDWIAKDMPN DFTLTLTDEA RHGADYLRIY VSKPSFDPTT EALGWGDLDL VKETGRFAPA
DQYQTDVSLP GRSGRAVLYT IWQASHMDQT YYLCSDINIG GTGGGTPQPQ PEPTPAPEPT
PEPEPTEPGD DHDHGGDHGG DHGDHGGDHG HPSPDPEPAP GNGACTATVR VINTWPNGYQ
AELDITAGSE PLSAWSATVD GATITQAWNG TQAGSTITSA HWNSDVEAGG ATSAGFLGSG
SPDELTATCN GR
//
