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Database: UniProt/TrEMBL
Entry: B8I0M0_CLOCE
LinkDB: B8I0M0_CLOCE
Original site: B8I0M0_CLOCE 
ID   B8I0M0_CLOCE            Unreviewed;      1015 AA.
AC   B8I0M0;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   22-NOV-2017, entry version 62.
DE   SubName: Full=Carbohydrate binding family 6 {ECO:0000313|EMBL:ACL75595.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Ccel_1239 {ECO:0000313|EMBL:ACL75595.1};
OS   Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 /
OS   H10).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ruminiclostridium.
OX   NCBI_TaxID=394503 {ECO:0000313|EMBL:ACL75595.1, ECO:0000313|Proteomes:UP000001349};
RN   [1] {ECO:0000313|EMBL:ACL75595.1, ECO:0000313|Proteomes:UP000001349}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10
RC   {ECO:0000313|Proteomes:UP000001349};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E.,
RA   Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Zhou J., Richardson P.;
RT   "Complete sequence of Clostridium cellulolyticum H10.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|SAAS:SAAS00568376}.
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DR   EMBL; CP001348; ACL75595.1; -; Genomic_DNA.
DR   RefSeq; WP_015924744.1; NC_011898.1.
DR   ProteinModelPortal; B8I0M0; -.
DR   STRING; 394503.Ccel_1239; -.
DR   CAZy; CBM6; Carbohydrate-Binding Module Family 6.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   EnsemblBacteria; ACL75595; ACL75595; Ccel_1239.
DR   KEGG; cce:Ccel_1239; -.
DR   eggNOG; ENOG4105CNT; Bacteria.
DR   eggNOG; COG3250; LUCA.
DR   HOGENOM; HOG000022809; -.
DR   KO; K01190; -.
DR   OMA; CLHHDQG; -.
DR   OrthoDB; POG091H0F66; -.
DR   Proteomes; UP000001349; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; -; 2.
DR   Gene3D; 2.60.40.10; -; 3.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR006584; Cellulose-bd_IV.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR016134; Dockerin_dom.
DR   InterPro; IPR036439; Dockerin_dom_sf.
DR   InterPro; IPR032311; DUF4982.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF16355; DUF4982; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SMART; SM00606; CBD_IV; 1.
DR   SUPFAM; SSF49303; SSF49303; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF63446; SSF63446; 1.
DR   PROSITE; PS51175; CBM6; 1.
DR   PROSITE; PS51766; DOCKERIN; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001349};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00080608};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00080540};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001349};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     29       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        30   1015       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002873881.
FT   DOMAIN      820    943       CBM6. {ECO:0000259|PROSITE:PS51175}.
FT   DOMAIN      946   1012       Dockerin. {ECO:0000259|PROSITE:PS51766}.
SQ   SEQUENCE   1015 AA;  109949 MW;  B030E265201858FF CRC64;
     MLRKKILCIF LVTVLMLTIL PIPQQTVMAD TGVLKELKGT DIYNGLRGLN FNEGWKFNKG
     DVSNGQSTGY NDSGWSGVTL PHDWSIYNTF NKSSAAGAGG GYLDGGIGWY RKTFTVPSDY
     TGKKVFIEFD GAYMNSQVWI NGTLLGTRPY GYSSFEYDLT PYLNIGGSNV IAVRLNNNQP
     TSRWYSGSGI YRNVWLTVLD PVHVTYCGMF VTTPTVSSSS ATANVSTKVL NQGSTAKSVS
     LKTTITDAEG NVVATNTSSV ASIAGSGSNT FSQNLTVSNP HLWSPASPYL YAVQTQVIVD
     GNVTDTYSST LGIRYFSFSS TSGFSLNGVN MKINGVCLHH DLGSLGAAVN YRAIERELQI
     MKDMGCNAIR TSHNPPDPQM LEICDRLGLM VMDEAFDCWE TGKNSNDYHL YFNNWAQTDL
     QAMVTRDRNH PSIIMYSIGN EIPSPSVATA TKLKNWVKDV DNTRPVTLGT FAVSMGDATP
     QAVASVLDLV GYNYFPYMYD GGHNNHPEWK MFGSETSSAV RSRGVYKTPT NKNILTDSDN
     QCSSYDNSVV SWGNSAESSY NEINKRNYMA GEFIWTGFDY IGEPTPYEWP AKSSYFGIVD
     TCGFPKDIYY FYQSKWSTKP MVHILPHWNW STGTNVEVWA YSNCDTVELF LNGKSLGSKS
     VGTAGHLSWS VPWSSGTLRA KGTKGGTVVY DEVVTAGTPS KVLLKPDRTS VKADGKDLIY
     IETDIADGNN VTVPTADNTV NFSISGPGVI VGVDNGNPIS TEAYKGSSRK AFNGKCLVIV
     QPTKVNGTIV VTASSNGLSS GSVSIASTGG AEAPIVSAYK KIEAENYDNQ SGIQTEACSE
     GGQDVGFIEN GDYTVYNNVD FGSGAESFTA RAASATSGGN IEIRLDSPNG TLIGTCPVAG
     TGDWQTYADV NCSVSEVSGK HDLYLKFTGD SGYLFNINWF TFTARNSAKL GDLNSDDQID
     AMDFQLMKKY LLGLGEIKDT KLADLDASGT IDVLDLMLLK QYLLGTITSF PGQGT
//
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