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Database: UniProt
Entry: A0A168EAH3_9MICO
LinkDB: A0A168EAH3_9MICO
Original site: A0A168EAH3_9MICO 
ID   A0A168EAH3_9MICO        Unreviewed;      1051 AA.
AC   A0A168EAH3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-SEP-2017, entry version 8.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   Name=cenC {ECO:0000313|EMBL:ANC29802.1};
GN   ORFNames=I598_0211 {ECO:0000313|EMBL:ANC29802.1};
OS   Isoptericola dokdonensis DS-3.
OC   Bacteria; Actinobacteria; Micrococcales; Promicromonosporaceae;
OC   Isoptericola.
OX   NCBI_TaxID=1300344 {ECO:0000313|EMBL:ANC29802.1, ECO:0000313|Proteomes:UP000076794};
RN   [1] {ECO:0000313|EMBL:ANC29802.1, ECO:0000313|Proteomes:UP000076794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-3 {ECO:0000313|EMBL:ANC29802.1,
RC   ECO:0000313|Proteomes:UP000076794};
RA   Kwon S.-K., Kim J.F.;
RT   "Complete genome sequence of a soil Actinobacterium, Isoptericola
RT   dokdonensis DS-3.";
RL   Submitted (JAN-2016) 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; CP014209; ANC29802.1; -; Genomic_DNA.
DR   EnsemblBacteria; ANC29802; ANC29802; I598_0211.
DR   KEGG; ido:I598_0211; -.
DR   PATRIC; fig|1300344.3.peg.206; -.
DR   KO; K01179; -.
DR   Proteomes; UP000076794; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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; -; 2.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase-like.
DR   InterPro; IPR008965; Carb-bd_dom.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR004197; Cellulase_Ig-like.
DR   InterPro; IPR003305; CenC_carb-bd.
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; PF00553; CBM_2; 1.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF02927; CelD_N; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS51173; CBM2; 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:UP000076794};
KW   Glycosidase {ECO:0000256|RuleBase:RU361166,
KW   ECO:0000313|EMBL:ANC29802.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361166,
KW   ECO:0000313|EMBL:ANC29802.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361166};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076794};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL        1     33       {ECO:0000256|RuleBase:RU361166}.
FT   CHAIN        34   1051       Endoglucanase. {ECO:0000256|RuleBase:
FT                                RU361166}.
FT                                /FTId=PRO_5007749417.
FT   DOMAIN      935   1051       CBM2. {ECO:0000259|PROSITE:PS51173}.
SQ   SEQUENCE   1051 AA;  110742 MW;  481B2300EA028D95 CRC64;
     MKTRLDLWRV LAATVTTSAV VLAGAAVPVT AQADEPPNLV ANGAFEPGVH DQWWGITDAD
     VTDGELCLDV PAVERFGNFV ALGLTAGESY LFGFTAHGEP GTDGLEARVQ SDGAAGPEVF
     DVRETFAVEP EPQDYEWGFT ASGDAQRVQF ELAGAQPAGG LCLTDVHVTP LAHLAQNPTF
     DGLEPWWTTA NLALAETGGR MCGTVPAGGN QWDVILGQSG IALEPGSSYT VTLTASAPPG
     TTGRILVPRP GADWPPLFSA DVALDGTFTQ TFEVDAAADT QLQLQVGGNA AELELCLDLF
     SLTTGGTVPE FEHETGPRVR VNQVGYLPDG PKRATVVTDA TEPLPWELHD ATGAVVATGT
     TEPAGTDASA GLDVHTVDLG DVAATGEGFR LVADGEESYP FAISATVYDT LRTDALGIYY
     TQRSGTEIVP VVVDGVEEKA EHARPAGHVD APGDGVNQGD VDLPCLPPTG AVDANGAPQL
     GADDHYGVDG WACPDGYVRD VSGGWYDAGD HGKYVVNAGI SVYQLLSAYE RSLHAGTVES
     GALGDGTLVI PERGNDVPDV LDEVRHELEF MLAMQVPRGT TMTIDGESFD AGGLVHHKVH
     DIAWTGLNLL PSEDPQPRYL HRPSTAATLN LAAAAAQGAR LYEPYDAGFA DDLRRAAKRA
     WVAAAAHPEI YAPNTNVIDP NPGGGPYDDT DVTDERYWAA AQLYLTTGGQ RYADAVLGSP
     LHVGGAREDV WKPTGFDWGW TAPAARLDLA TVPSTLPGRA DVVASVVAAA DGYVAIQQSQ
     PFGLPYAPEG GYAWGSTHQV LNNAVVVATA YDLTGDQAYR DAALEAADYV LGRNAINNSY
     VKGYGTYFSQ RMHNRWMASA DRLPPHPDGM LSGGPNSALD DPVSRAALEG CAPQTCYIDH
     VDAWSTNEMT INWNSALAWY ASWADDMASV APDAWEPPTP TCEVGYTVHG TWPGGFVSQL
     WVTNLGPGAR DGWELGWRFD GDQRVVGLWG GEAVQDGAAV TVTNEPWNAR LADPGARGGS
     TVTLGFVGAA RTGTDHVPDA FTLDGMWCAT A
//
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