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Database: UniProt
Entry: G8M2I7_CLOCD
LinkDB: G8M2I7_CLOCD
Original site: G8M2I7_CLOCD 
ID   G8M2I7_CLOCD            Unreviewed;       877 AA.
AC   G8M2I7;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   07-JUN-2017, entry version 32.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   OrderedLocusNames=Clocl_3917 {ECO:0000313|EMBL:AEV70357.1};
OS   Clostridium clariflavum (strain DSM 19732 / NBRC 101661 / EBR45).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ruminiclostridium.
OX   NCBI_TaxID=720554 {ECO:0000313|EMBL:AEV70357.1, ECO:0000313|Proteomes:UP000005435};
RN   [1] {ECO:0000313|Proteomes:UP000005435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19732 / NBRC 101661 / EBR45
RC   {ECO:0000313|Proteomes:UP000005435};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Kitzmiller T., Lynd L.,
RA   Izquierdo J., Woyke T.;
RT   "Complete sequence of Clostridium clariflavum DSM 19732.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-glucosidic
CC       linkages in cellulose, lichenin and cereal beta-D-glucans.
CC       {ECO:0000256|RuleBase:RU361166}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E)
CC       family. {ECO:0000256|RuleBase:RU361166}.
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DR   EMBL; CP003065; AEV70357.1; -; Genomic_DNA.
DR   RefSeq; WP_014256858.1; NC_016627.1.
DR   ProteinModelPortal; G8M2I7; -.
DR   STRING; 720554.Clocl_3917; -.
DR   EnsemblBacteria; AEV70357; AEV70357; Clocl_3917.
DR   KEGG; ccl:Clocl_3917; -.
DR   eggNOG; ENOG4105E08; Bacteria.
DR   eggNOG; ENOG410XNTA; LUCA.
DR   KO; K01179; -.
DR   OMA; YPWHTCE; -.
DR   OrthoDB; POG091H04TS; -.
DR   Proteomes; UP000005435; Chromosome.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd02850; E_set_Cellulase_N; 1.
DR   Gene3D; 2.60.120.260; -; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase-like.
DR   InterPro; IPR004197; Cellulase_Ig-like.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR002105; Dockerin_1_rpt.
DR   InterPro; IPR016134; Dockerin_dom.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF02927; CelD_N; 1.
DR   Pfam; PF00404; Dockerin_1; 2.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF63446; SSF63446; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS51766; DOCKERIN; 1.
DR   PROSITE; PS00698; GLYCOSYL_HYDROL_F9_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361166};
KW   Cellulose degradation {ECO:0000256|RuleBase:RU361166};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005435};
KW   Glycosidase {ECO:0000256|RuleBase:RU361166,
KW   ECO:0000313|EMBL:AEV70357.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361166,
KW   ECO:0000313|EMBL:AEV70357.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361166};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005435};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL        1     35       {ECO:0000256|RuleBase:RU361166}.
FT   CHAIN        36    877       Endoglucanase. {ECO:0000256|RuleBase:
FT                                RU361166}.
FT                                /FTId=PRO_5005133020.
FT   DOMAIN      811    877       Dockerin. {ECO:0000259|PROSITE:PS51766}.
SQ   SEQUENCE   877 AA;  97771 MW;  CA03CAA33A849085 CRC64;
     MIYNRVKNAN KLKSVIAAFA VTTLLTTSIQ PAVYAGEDNH PELPPYQKDL LYERTFDEGL
     CYPWHTCEDS GGVCDFDIKN GALVLKITNP GQNEWSCQMR HRGITLVQGH TYTVRFKVWS
     NKNGAKVYAK IGMQGEPYTD YWNNQWQKID LTTSPKLVQA EFTMNSATDE TVEFTFHAGG
     ALNTAGTEIY FDDISLYDPL HDKPVIEVLE MPDVRVNQVG YYPNRAKKAT VVTNSTSPVG
     WTLYDSSGRA VKTGTTKVKG LDKDSQDYVH IIDFSDFTTP GKGYYFKVDT NSSKNYSHKF
     DISEDILSDM KMDAIKYFYH NRSGIAIEMP YAGRQDLTRP AGHIGVYPNL GDTNVPTWPN
     TGQKNYSLDV SGGWYDAGDH GKYVVNGGIS LWTMLNQYER AKKDNVLHLA PYKDGSMNIP
     ESGNGLYDIL DEAKWEMDFI LKMQVPSSKD PDLAGMVHHK VHDESWTALG LLPHEDPKQR
     YLRPVSTAAT LNLAATAAQA ARIWKDIDPS YSNKCLQAAE AAWEAAKKHP KIYAPNEQPG
     GGPYNDEYVE DEFYWAACEL FITTGKSEYK DYIKSSRHYL EMPSILSSGE DDGLYGCFTW
     GSTQGLGTVS LALIPNDLGE SEIQKARQNI AKAADVWLAN IEEQGYGLPI KADRNGNYPW
     GSNSFILNTM IVFAYAYEYT GDTKYLDGMT SSMDYILGRN ALDQCYVTGY GERPLQNPHH
     RFWAYQLSKK FPKPPAGCVS GGPNSNFQDP TINAAMKKDT PPQKCFMDHI DSWSTNEITI
     NWNAPFAWAT AYLDEKGNTP SNGGGTNPGG EDIVLGDINF DGDINSIDYA LLKAHLLGIN
     KLSGDALKAA DVDKNGDVNS IDYAKMKQYL LGISKEF
//
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