ID C7PVM8_CATAD Unreviewed; 562 AA.
AC C7PVM8;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Cellulose-binding family II {ECO:0000313|EMBL:ACU69384.1};
DE Flags: Precursor;
GN OrderedLocusNames=Caci_0432 {ECO:0000313|EMBL:ACU69384.1};
OS Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS B-24433 / ID139908).
OC Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC Catenulisporaceae; Catenulispora.
OX NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69384.1, ECO:0000313|Proteomes:UP000000851};
RN [1] {ECO:0000313|EMBL:ACU69384.1, ECO:0000313|Proteomes:UP000000851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908
RC {ECO:0000313|Proteomes:UP000000851};
RX PubMed=21304647; DOI=10.4056/sigs.17259;
RA Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT 139908).";
RL Stand. Genomic Sci. 1:119-125(2009).
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DR EMBL; CP001700; ACU69384.1; -; Genomic_DNA.
DR RefSeq; WP_012784679.1; NC_013131.1.
DR AlphaFoldDB; C7PVM8; -.
DR STRING; 479433.Caci_0432; -.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR KEGG; cai:Caci_0432; -.
DR eggNOG; COG3469; Bacteria.
DR HOGENOM; CLU_019399_4_1_11; -.
DR InParanoid; C7PVM8; -.
DR OrthoDB; 99456at2; -.
DR Proteomes; UP000000851; Chromosome.
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; cd00063; FN3; 1.
DR CDD; cd06543; GH18_PF-ChiA-like; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42976; BIFUNCTIONAL CHITINASE/LYSOZYME-RELATED; 1.
DR PANTHER; PTHR42976:SF1; GH18 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00041; fn3; 1.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS50853; FN3; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..562
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002982533"
FT DOMAIN 50..160
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT DOMAIN 168..253
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 29..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 562 AA; 57545 MW; 81948113AE288216 CRC64;
MLRALRASLI AAGAGALLVS GLTIASPTAS AATTPTPTAT APTTPTATAP TTPTPLPTAV
YSKTSDWGSG FQAQYVITNP MSVPLNTWSL QFSLPSTEKI TSMWGGTDTA SGTTHTVLAQ
SYDTTIAAGA SITIGFDGSY SGTYADPSAC KLNSDPCDGS ADAQAPTAPT ALTTLSTTSS
AASLSWTGSA DNVTVAGYNV YSGSTMVATS PGTAATVTGL APSTSYSFTV RAVDEAGNLS
APSAAVSATT LASTGGGHLP GVAAPFVDIG AWPTPNLTQI AETTGLRQFS LGFIVNGTAT
CTPSWFNAYA MSAGFEQSDI ATLRAIGGDV KPSFGGEAGT ELAQSCTDVP SLTAAYQSAI
TAYNLTQIDF DIEGSAVADP ASIDRRSQAI AALQKNAAAA GKPLTVTLTL PILPSGLTTD
GLYVVQSAVK YGAKITTVNG MAMDFGDIEA PNPSGKMGTY AIDTAQSLHT QLTPLYPALT
ATQLWNMIGV TPMIGQNDNS SEVFYQTDMH QLLTFAQQQH LGELAFWDVT RDANACTGSL
SKCTDIPQTP YEFSKMIAPY QG
//
