ID A0A1N7GL07_9ACTN Unreviewed; 487 AA.
AC A0A1N7GL07;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Cellulose binding domain-containing protein {ECO:0000313|EMBL:SIS13275.1};
GN ORFNames=SAMN05421833_1305 {ECO:0000313|EMBL:SIS13275.1};
OS Microbispora rosea.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=58117 {ECO:0000313|EMBL:SIS13275.1, ECO:0000313|Proteomes:UP000186096};
RN [1] {ECO:0000313|EMBL:SIS13275.1, ECO:0000313|Proteomes:UP000186096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12950 {ECO:0000313|EMBL:SIS13275.1,
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; FTNI01000030; SIS13275.1; -; Genomic_DNA.
DR RefSeq; WP_076440739.1; NZ_FTNI01000030.1.
DR AlphaFoldDB; A0A1N7GL07; -.
DR STRING; 58117.SAMN05421833_1305; -.
DR OrthoDB; 5240321at2; -.
DR Proteomes; UP000186096; Unassembled WGS sequence.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031221; P:arabinan metabolic process; IEA:InterPro.
DR GO; GO:0019566; P:arabinose metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR InterPro; IPR015289; A-L-arabinofuranosidase_B_cat.
DR InterPro; IPR038964; ABFB.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR PANTHER; PTHR39447; ALPHA-L-ARABINOFURANOSIDASE B; 1.
DR PANTHER; PTHR39447:SF2; ALPHA-L-ARABINOFURANOSIDASE B; 1.
DR Pfam; PF09206; ArabFuran-catal; 1.
DR Pfam; PF00553; CBM_2; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS51173; CBM2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR638964-3};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..487
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038367792"
FT DOMAIN 34..143
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 144..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 374
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT ACT_SITE 450
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT DISULFID 174..184
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 234..239
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 329..330
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
SQ SEQUENCE 487 AA; 49995 MW; 40F68EE31C1A10FF CRC64;
MRHVSSFHRR LRLSAAAVAA LLTAGVGVAG THAASAAASG CKVTYTVTNQ WPGGFGTNVS
IDNLGDPVNG WKLTWSFSAG QTITQLWNGT YTQSGSQVTV TNASYNGAIP SGGSTSFGFN
GAFNGSNPAP SSFALNGVTC TGGVTSPSPG TSPTASPSVS PSASPSPPSS RQPCDIYAAG
GTPCVAAHST TRALYANYNG SLYQVRRSSD NTTRDIGVLS TGSAADAAAQ DAFCASTTCL
ITKIYDQSGR NNHLTQAPPG GFSGPAAGGY DNLATATKAP TTVYGQKAYG VYVDPGVGYR
NNATNGVARG DQPEGMYAVF DGTHYNGGCC FDYGNAETNS RDNGNGTMEA IYFGNIKVWG
YGTGNGPWVM ADLENGLFSG VNPGYNANDP SVNHRYLTAI VKGEPNHWAI RAGNAQSGGL
STFYDGKRPN ASGYNPMKKE GAIILGIGGD NSHGSAGTFY EGVMTSGYPT AATENEVQAN
IVAAGYR
//