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Database: UniProt
Entry: A0A1N6RIA4_9ACTN
LinkDB: A0A1N6RIA4_9ACTN
Original site: A0A1N6RIA4_9ACTN 
ID   A0A1N6RIA4_9ACTN        Unreviewed;       620 AA.
AC   A0A1N6RIA4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Cellulose binding domain-containing protein {ECO:0000313|EMBL:SIQ28610.1};
GN   ORFNames=SAMN05421833_101400 {ECO:0000313|EMBL:SIQ28610.1};
OS   Microbispora rosea.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Microbispora.
OX   NCBI_TaxID=58117 {ECO:0000313|EMBL:SIQ28610.1, ECO:0000313|Proteomes:UP000186096};
RN   [1] {ECO:0000313|EMBL:SIQ28610.1, ECO:0000313|Proteomes:UP000186096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12950 {ECO:0000313|EMBL:SIQ28610.1,
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; FTNI01000001; SIQ28610.1; -; Genomic_DNA.
DR   RefSeq; WP_076432197.1; NZ_FTNI01000001.1.
DR   AlphaFoldDB; A0A1N6RIA4; -.
DR   STRING; 58117.SAMN05421833_101400; -.
DR   OrthoDB; 9758333at2; -.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR43576:SF3; ALPHA-L-ARABINOFURANOSIDASE C; 1.
DR   PANTHER; PTHR43576; ALPHA-L-ARABINOFURANOSIDASE C-RELATED; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   PROSITE; PS51173; CBM2; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           40..620
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011958327"
FT   DOMAIN          517..620
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          340..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          476..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..512
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   620 AA;  62957 MW;  EA90CB76753610D4 CRC64;
     MHGSLTRRRR AGLALLTSAA LAAASAVVAA TAVSAPASAA TSATVTVNTG TSLGTIPAAG
     HGVNVAVYDG NMNSSPVSGL LRDAGFTAVR YPGGSYGDIY HWKTHTTEGG YVAPGTDFDT
     YVSTVRSAGA QPVVIANYGT GTAQEAADWV RYANVTKGYG VKYWEIGNEV YGNGHYGSGW
     EQDNHSDKSP RAYANNVLQY ISAMKAVDSS IKVGVVLTTP GGWPDGVVGS GDSADWNNTV
     MSIVQDKADF VIVHWYPGAT SAADSLTKVS QIAPMVSTIR SLLGRYAGSR ASSIGIAVTE
     ANLNYQLNSA TTALGAADSY LTWFENGVMN VDWWSLHNGT SSSPKTNDDG TTDYNDFGIL
     SSGSSGEPPV NTPLPPYYGL AMVGRAGSPG DTLVKASSSS SLLAAHAVRT SGGVNVVLVN
     KDLNNSTTVS LSYSGFSPGG TASVVQWRKG ATSIGTSTAS SATSITLPPY SITVLKASGG
     GTASPTPSPT PSPSRTPSPS PSASPSRTPS PSPSASPTAG GSGCSATYKV TNSWPGGFQA
     DVTVTNTRAT AISGWTVGWS FRSGQTISSS WNATVTQSGA AVTARNVSYN GGLAAGASTS
     FGFTGNGAGD VPAPISCTIG
//
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