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Database: UniProt
Entry: Q21N17_SACD2
LinkDB: Q21N17_SACD2
Original site: Q21N17_SACD2 
ID   Q21N17_SACD2            Unreviewed;       558 AA.
AC   Q21N17;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   24-JAN-2024, entry version 89.
DE   SubName: Full=Putative cellulose-binding protein {ECO:0000313|EMBL:ABD79912.1};
GN   Name=cbm2D {ECO:0000313|EMBL:ABD79912.1};
GN   OrderedLocusNames=Sde_0650 {ECO:0000313|EMBL:ABD79912.1};
OS   Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Saccharophagus.
OX   NCBI_TaxID=203122 {ECO:0000313|EMBL:ABD79912.1, ECO:0000313|Proteomes:UP000001947};
RN   [1] {ECO:0000313|EMBL:ABD79912.1, ECO:0000313|Proteomes:UP000001947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-40 / ATCC 43961 / DSM 17024
RC   {ECO:0000313|Proteomes:UP000001947};
RX   PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA   Weiner R.M., Taylor L.E.II., Henrissat B., Hauser L., Land M.,
RA   Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA   Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA   Richardson P.M., Borovok I., Hutcheson S.;
RT   "Complete genome sequence of the complex carbohydrate-degrading marine
RT   bacterium, Saccharophagus degradans strain 2-40 T.";
RL   PLoS Genet. 4:E1000087-E1000087(2008).
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DR   EMBL; CP000282; ABD79912.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q21N17; -.
DR   STRING; 203122.Sde_0650; -.
DR   CAZy; CBM10; Carbohydrate-Binding Module Family 10.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   KEGG; sde:Sde_0650; -.
DR   eggNOG; COG3386; Bacteria.
DR   eggNOG; COG3693; Bacteria.
DR   HOGENOM; CLU_488237_0_0_6; -.
DR   OrthoDB; 9775889at2; -.
DR   Proteomes; UP000001947; Chromosome.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 2.30.32.30; CBM10; 1.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR002883; CBM10/Dockerin_dom.
DR   InterPro; IPR036601; CBM10_sf.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR018366; CBM2_CS.
DR   InterPro; IPR009031; CBM_fam10.
DR   InterPro; IPR048955; Cip1-like_core.
DR   Pfam; PF02013; CBM_10; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF21340; Polysacc_lyase-like; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SMART; SM01064; CBM_10; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF57615; Type X cellulose binding domain, CBDX; 1.
DR   PROSITE; PS51763; CBM10; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00561; CBM2_A; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001947};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..558
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004200110"
FT   DOMAIN          21..129
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   DOMAIN          182..211
FT                   /note="CBM10"
FT                   /evidence="ECO:0000259|PROSITE:PS51763"
FT   REGION          127..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          215..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   558 AA;  56322 MW;  08ED77F5672D8FBC CRC64;
     MSTQGKPCLK KLWPALALAA AVASPNAFSA CEYVVSNQWD SGYSATIKIH NDTNSTINGW
     NVNWQYSGDN RVTNLWNAAY VGSNPYSASN LSWNSTVGAG QTIEFGFQGA KNGGSAEVPV
     VTGDVCSGGG SSSGSSSSSS SSSSTGSSTS SSSSSSSSSS TGGSTSSSSS SSSTGGNGGA
     QQCNWYGEIR PLCNNQDSGW GWENQQSCIG RDTCSNQSGN GGIIGGSSSS SSSSSTGSSS
     SSSSSSSSSS SSSSSTSSSS SSSSSTSSSS SSSSSSSSSS STSSSSSSSS SSSSSSSSST
     SSSSSSSSSS SSSSSSSSSS SSSSSSSGGG VIFSADFESD SDSTQPAGWD NFIGWRQNGP
     NPNGSTFALV ESGRAHSGNN AVHFSGGASP AMIARALPAD LDTLYVRAWV YMTRQLGMNP
     GDNHETLIAL RGSAGNANNE VRFGEIKGVI GTNEVPSDNI APTMASWGGG PAYASDTWHC
     IEVAFLSQPA YDTVNAWVND ALVHTIDEGS DWNNGALEAD WLSNKYVELA FGWHSFSGND
     VDVWMDDIVV STTPIGCD
//
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