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Database: UniProt
Entry: E9S7A8_RUMAL
LinkDB: E9S7A8_RUMAL
Original site: E9S7A8_RUMAL 
ID   E9S7A8_RUMAL            Unreviewed;       999 AA.
AC   E9S7A8;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   22-NOV-2017, entry version 32.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=CUS_6119 {ECO:0000313|EMBL:EGC04798.1};
OS   Ruminococcus albus 8.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ruminococcus.
OX   NCBI_TaxID=246199 {ECO:0000313|EMBL:EGC04798.1, ECO:0000313|Proteomes:UP000004259};
RN   [1] {ECO:0000313|EMBL:EGC04798.1, ECO:0000313|Proteomes:UP000004259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8 {ECO:0000313|EMBL:EGC04798.1,
RC   ECO:0000313|Proteomes:UP000004259};
RA   Nelson K.E., Sutton G., Torralba M., Durkin S., Harkins D.,
RA   Montgomery R., Ziemer C., Klaassens E., Ocuiv P., Morrison M.;
RL   Submitted (FEB-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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EGC04798.1}.
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DR   EMBL; ADKM02000008; EGC04798.1; -; Genomic_DNA.
DR   RefSeq; WP_002846823.1; NZ_ADKM02000008.1.
DR   ProteinModelPortal; E9S7A8; -.
DR   STRING; 246199.CUS_6119; -.
DR   CAZy; CBM37; Carbohydrate-Binding Module Family 37.
DR   CAZy; CBM4; Carbohydrate-Binding Module Family 4.
DR   CAZy; GH9; Glycoside Hydrolase Family 9.
DR   EnsemblBacteria; EGC04798; EGC04798; CUS_6119.
DR   eggNOG; ENOG4105E08; Bacteria.
DR   eggNOG; ENOG410XNTA; LUCA.
DR   OrthoDB; POG091H04TS; -.
DR   BioCyc; RALB246199:G11YK-1960-MONOMER; -.
DR   Proteomes; UP000004259; Unassembled WGS sequence.
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; -; 2.
DR   InterPro; IPR008928; 6-hairpin_glycosidase-like.
DR   InterPro; IPR004197; Cellulase_Ig-like.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR018221; Glyco_hydro_9_His_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; PF00759; Glyco_hydro_9; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS00592; GLYCOSYL_HYDROL_F9_1; 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:UP000004259};
KW   Glycosidase {ECO:0000256|RuleBase:RU361166};
KW   Hydrolase {ECO:0000256|RuleBase:RU361166};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361166};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004259};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL        1     32       {ECO:0000256|RuleBase:RU361166}.
FT   CHAIN        33    999       Endoglucanase. {ECO:0000256|RuleBase:
FT                                RU361166}.
FT                                /FTId=PRO_5005128638.
FT   DOMAIN       37    174       CBM-cenC. {ECO:0000259|Pfam:PF02018}.
FT   DOMAIN      220    322       CelD_N. {ECO:0000259|Pfam:PF02927}.
SQ   SEQUENCE   999 AA;  111980 MW;  8C0224A7C3BCF966 CRC64;
     MHKTMKRIAA GLVAITASLS AAAASAPMSV FAEDEQILIR SDFEAGMGLP WHTLENAPAR
     QDFDISDGTY NITILNNDGP ESRWDLQLRC RNLVIQKGHT YKVHWKVNSS EEGELYTKIA
     NYGGNVEVWH NNCGNDNYNQ TWECVKIAKG DNTFDAEFTA KEDIEVAEWV FEYGGQGMYQ
     PVDCFPDGTI LKFDDLSLID TTPGGCIIEF NPNECGVVRP ESNVRLNQIG YYPQLEKKAS
     YVTDASSPLQ FEIRDKDGNV KYKGTTKVFG DDPDSGTGKT NSFQIGFNTV TRLKDSGSYV
     HIIDFSDFRT VGEYTIFVKD TVGVSGTQVM NSKGANDTKL SGDKLLWTNP VTLKTYTMNE
     SSPFRIDRQI YDDQLLRDSM NYFYQNRSGV PIESEYITSG DKSKLAHDKY GHNPDTAYVQ
     SKWVKTYEKD FSNGEKDNKI DVTGGWYAAN DHGKYVVEGG FSVWTLQNAY EFSRRSGNTY
     KWTDGTIAVP ENKDNAPDIL DEARVELEWM FKMINEDGFV YHSVQDHKWV GPLLTPWKDD
     TQQGFEPVRI VRPPTYAATF NMIACAAQAS RLWKGIDDDF AKECLQNAQN SWKAIMAKQS
     DWNVTSGYYY DDPYFAPSEF GGNNIFGDTY VVDDAYWAAC ELYATTGDSA YYDFLKDYNN
     YNDPSGQDKA FSLTSCLSGG ENNGSFGSFN WGNTAGLGTL SLYLSDNTSS ADRKIITKSI
     QNIADRYIAQ MRNQGMGIPY KSVTIGDYIG SDREVYKGYE YGSNSFVINN AMVLAYAYDT
     DDSKFIYRNG AAEALDYLFG RNGLGFSYVS GYGDKAMSSP HHRYWANSID PSFPAAPSGV
     LAGGPCSGMY RDNYLRGLGY KKGTLADQKY YVDSAEAWSV NDVSGSWNAP LVWMSSFMND
     RFGGSNPVPY PTNIKVDYSE EYHQVRFTWN KVENADRYGI AVYLAGKWRV QKQDITGNTY
     TSPKNLTPGV TYKVAIAARV NGRWDTENAI KRACTVTIK
//
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