ID A0A1N7H1I0_9ACTN Unreviewed; 489 AA.
AC A0A1N7H1I0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Cellulose 1,4-beta-cellobiosidase {ECO:0000313|EMBL:SIS18675.1};
GN ORFNames=SAMN05421833_13564 {ECO:0000313|EMBL:SIS18675.1};
OS Microbispora rosea.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=58117 {ECO:0000313|EMBL:SIS18675.1, ECO:0000313|Proteomes:UP000186096};
RN [1] {ECO:0000313|EMBL:SIS18675.1, ECO:0000313|Proteomes:UP000186096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12950 {ECO:0000313|EMBL:SIS18675.1,
RC ECO:0000313|Proteomes:UP000186096};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FTNI01000035; SIS18675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7H1I0; -.
DR STRING; 58117.SAMN05421833_13564; -.
DR Proteomes; UP000186096; 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; cd00063; FN3; 3.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
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; IPR013783; Ig-like_fold.
DR PANTHER; PTHR26391; INACTIVE TYROSINE-PROTEIN KINASE 7; 1.
DR PANTHER; PTHR26391:SF18; PROTEIN KINASE RECEPTOR TIE-1, PUTATIVE-RELATED; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00041; fn3; 1.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00060; FN3; 3.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS50853; FN3; 2.
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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..489
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039676182"
FT DOMAIN 164..264
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 276..371
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 381..489
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 145..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..166
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 489 AA; 49671 MW; 64D6B670728A29B9 CRC64;
MRRAAPIGKV NHMPVKGLRP ASVILGAGLA LAASAAPAVG AADTTPPSAP GTLFHCPLPG
APGSGLGVGV SLCWGAATDD VGVTGYDVQI KQDGVFTAVR TTTGTGSIVS GLTLGQSYTF
RVIARDVAGN AGPPSNEVTQ AANYLSGMSP SAPPPSPSPI DRTPPTRPEG LGPYSVYING
AAGLTWTRST DNVAVSGYDV YAWIDGAFSK VPAQVSTPAD DKVLAIVGLT PGRDYLFYVV
AKDAAGNLSA PSDLVRQRAM VEPPAASPSP GTDTTPPGTP TGLTSVSGMD IPGGVFLAWN
SVSDDSGVPS KYDLFRQTDH GYAYEGENGI PRDIVSGLEG GKPYTFQVVA RDAAGNLSNP
SAPYTAVAQP GGTSSPSPSP SASSGSTCKV TYAPTTWGGG FTATVTITNT GTAAIAGWKL
GFSFPLASQR VTNGWSAVWT QSGTAVTAEN YEWNKTIKPG QSLYLGFNGA YSGENPPPAA
FTLNGTTCS
//
