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Database: UniProt
Entry: Q21P73_SACD2
LinkDB: Q21P73_SACD2
Original site: Q21P73_SACD2 
ID   Q21P73_SACD2            Unreviewed;       681 AA.
AC   Q21P73;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Putative polysaccharide-binding protein {ECO:0000313|EMBL:ABD79506.1};
GN   Name=cbm6A {ECO:0000313|EMBL:ABD79506.1};
GN   OrderedLocusNames=Sde_0242 {ECO:0000313|EMBL:ABD79506.1};
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:ABD79506.1, ECO:0000313|Proteomes:UP000001947};
RN   [1] {ECO:0000313|EMBL:ABD79506.1, 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; ABD79506.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q21P73; -.
DR   STRING; 203122.Sde_0242; -.
DR   CAZy; CBM6; Carbohydrate-Binding Module Family 6.
DR   KEGG; sde:Sde_0242; -.
DR   eggNOG; COG3291; Bacteria.
DR   eggNOG; COG5434; Bacteria.
DR   HOGENOM; CLU_336401_0_0_6; -.
DR   OrthoDB; 5441506at2; -.
DR   Proteomes; UP000001947; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   CDD; cd04080; CBM6_cellulase-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR   InterPro; IPR006584; Cellulose-bd_IV.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR024535; Pectate_lyase_SF_prot.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF12708; Pectate_lyase_3; 1.
DR   SMART; SM00606; CBD_IV; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   PROSITE; PS51175; CBM6; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001947};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..681
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004200537"
FT   DOMAIN          83..207
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
FT   REGION          29..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   681 AA;  72458 MW;  BE062BFBD3880706 CRC64;
     MRISTAITQF LIVIATLILA ACSGSGGGAN SGGSNPGASS SSSSSSSSSN SSSSSTSSSS
     SSGGSSGAAV SLPSTIAAMD FVAAYDTDNA NSGDCGNGPV DMQTSTDTQG AACTVGWTKA
     GEWLAYDVSV AVTQKMDIVF RVATNQNSRA LKVQLNNKTL GVLNVSGTAF DEWQTVSLKD
     IEIPAGTHQL KLVWMTGAIN VNTLSFTAHS AYGQTTNLWG SNGAEHDPSG VLSDWSYAGY
     HWGEEEPPVK SPTINVVTDH GAIADDDSDD SAAFIAALTA ANNGDVVYVP EGRFILTQVL
     SIPNGVVLQG AGSELTTLYI PTNLNEATGI DPSFTGGFIE MKGSSSDGSK LSTITAAAAR
     GSNQITVESV AGLTVGDWVQ IQQTDVNGNF LLEALYAGYT AGLSDYSNLV NDAELEFFSR
     ITNISGNTLT LERPLPITVS PNYMAELHSV SVAYGEVGFE GMTLEFPETT YPGHFNELGY
     NGIDMRAQHS WVRDVVVKNI DYGINLRGSH FVSILDFTVI NTNDRSGHHG ISVGSSTDCL
     IRGFDIQAEL VHDLTVEWYA YGNVFTQGRG KNITLDHHRA AAYANLFTQI DLGEATRAWK
     TGGRSDRGYK TAVYSTFWNM TAEQAIDWPA NDFGPRMVFM GLTMDGSHSS VLDWVVEDIS
     ADDIYPPNLW LSQREKRLGR Q
//
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