(data stored in ACNUC7421 zone)

SWISSPROT: D3F517_CONWI

ID   D3F517_CONWI            Unreviewed;       542 AA.
AC   D3F517;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   07-JUN-2017, entry version 40.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
DE   Flags: Precursor;
GN   OrderedLocusNames=Cwoe_0159 {ECO:0000313|EMBL:ADB48595.1};
OS   Conexibacter woesei (strain DSM 14684 / JCM 11494 / NBRC 100937 /
OS   ID131577).
OC   Bacteria; Actinobacteria; Thermoleophilia; Solirubrobacterales;
OC   Conexibacteraceae; Conexibacter.
OX   NCBI_TaxID=469383 {ECO:0000313|EMBL:ADB48595.1, ECO:0000313|Proteomes:UP000008229};
RN   [1] {ECO:0000313|Proteomes:UP000008229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14684 / JCM 11494 / NBRC 100937 / ID131577
RC   {ECO:0000313|Proteomes:UP000008229};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K.,
RA   Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Conexibacter woesei DSM 14684.";
RL   Submitted (JAN-2010) 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:RU361153}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A)
CC       family. {ECO:0000256|RuleBase:RU361153}.
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DR   EMBL; CP001854; ADB48595.1; -; Genomic_DNA.
DR   RefSeq; WP_012931648.1; NC_013739.1.
DR   ProteinModelPortal; D3F517; -.
DR   STRING; 469383.Cwoe_0159; -.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   EnsemblBacteria; ADB48595; ADB48595; Cwoe_0159.
DR   KEGG; cwo:Cwoe_0159; -.
DR   eggNOG; ENOG4106R7G; Bacteria.
DR   eggNOG; COG2730; LUCA.
DR   HOGENOM; HOG000225207; -.
DR   KO; K01179; -.
DR   OMA; TWCCGAD; -.
DR   OrthoDB; POG091H1DNW; -.
DR   BioCyc; CWOE469383:GH82-159-MONOMER; -.
DR   Proteomes; UP000008229; 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   InterPro; IPR008965; Carb-bd_dom.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3F517.
DR   SWISS-2DPAGE; D3F517.
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361153};
KW   Cellulose degradation {ECO:0000256|RuleBase:RU361153};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008229};
KW   Glycosidase {ECO:0000256|RuleBase:RU361153,
KW   ECO:0000313|EMBL:ADB48595.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153,
KW   ECO:0000313|EMBL:ADB48595.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361153};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008229};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25    542       Endoglucanase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003043211.
FT   DOMAIN       51    355       Cellulase. {ECO:0000259|Pfam:PF00150}.
FT   DOMAIN      452    537       CBM2 (carbohydrate binding type-2).
FT                                {ECO:0000259|Pfam:PF00553}.
SQ   SEQUENCE   542 AA;  57881 MW;  F70018E9A17A4660 CRC64;
     MRRLAPLILA GLLLASLGAA TAHAGGRMIS TPLSTKGARI VDAGGRTVVL QGVNWFGFET
     ANHLVHGLWA RDYRDVLAQV RRLGFNTIRL PFSLEAIRST APVSGADFSG GRNAALKGAT
     PLEAMDAVVE EAGRQGLLIL LDNHSHADDA YQQGLWYGQG FSEDDWVATW KRLAARYRDQ
     RNVIGADLKN EPHAEATWGT GGPTDWRRAA ERAGNAVLSV APQWLVVVEG VGGGAPVPGQ
     RLDTHWWGGN LEGVRTHPVR LDRANRLVYS PHEYGPGVFP QPWFGKPNTP ALLEERWRTG
     FGFIAEQGIA PILVGEFGGR NVDRESAEGR WQRQFFDFIG RTGASWTYWA LNPNSGDTGG
     VLKDDWSSVQ PAKTALLQRM IARQRIAFRG SGAVFTAPRR ATTPRRGGKA APKTPARSQT
     AAPTQPSAPA QPPAQPPADD APGPPAPGSL SARVVVENRW DAGWCGHLEV SGPDATLAAA
     RATLTLPPGT RIAQSWNAQR SGDGGRVELR FPAWAKVAGG APYAATGFCV DGSGEAADVT
     VG
//

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