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Database: UniProt
Entry: E9SDS5_RUMAL
LinkDB: E9SDS5_RUMAL
Original site: E9SDS5_RUMAL 
ID   E9SDS5_RUMAL            Unreviewed;       912 AA.
AC   E9SDS5;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-SEP-2017, entry version 26.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=CUS_7090 {ECO:0000313|EMBL:EGC02640.1};
OS   Ruminococcus albus 8.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ruminococcus.
OX   NCBI_TaxID=246199 {ECO:0000313|EMBL:EGC02640.1, ECO:0000313|Proteomes:UP000004259};
RN   [1] {ECO:0000313|EMBL:EGC02640.1, ECO:0000313|Proteomes:UP000004259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8 {ECO:0000313|EMBL:EGC02640.1,
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:EGC02640.1}.
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DR   EMBL; ADKM02000091; EGC02640.1; -; Genomic_DNA.
DR   RefSeq; WP_002850623.1; NZ_ADKM02000091.1.
DR   ProteinModelPortal; E9SDS5; -.
DR   STRING; 246199.CUS_7090; -.
DR   EnsemblBacteria; EGC02640; EGC02640; CUS_7090.
DR   eggNOG; ENOG4105E08; Bacteria.
DR   eggNOG; ENOG410XNTA; LUCA.
DR   OrthoDB; POG091H04TS; -.
DR   BioCyc; RALB246199:G11YK-898-MONOMER; -.
DR   Proteomes; UP000004259; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 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; PF00759; Glyco_hydro_9; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF81296; SSF81296; 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:UP000004259};
KW   Glycosidase {ECO:0000256|RuleBase:RU361166};
KW   Hydrolase {ECO:0000256|RuleBase:RU361166};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361166};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004259};
KW   Signal {ECO:0000256|RuleBase:RU361166};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL        1     24       {ECO:0000256|RuleBase:RU361166}.
FT   CHAIN        25    912       Endoglucanase. {ECO:0000256|RuleBase:
FT                                RU361166}.
FT                                /FTId=PRO_5005128628.
FT   TRANSMEM    869    890       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       36    176       CBM-cenC. {ECO:0000259|Pfam:PF02018}.
FT   DOMAIN      218    295       CelD_N. {ECO:0000259|Pfam:PF02927}.
SQ   SEQUENCE   912 AA;  99771 MW;  7BC5DBF704718EA5 CRC64;
     MSKGILKRVL SAAAAAVLTM NSTAALGVFA GQQLGQTDFD DGVGLPWHIC ESTTGEMDFD
     IADGKYKITI VNPGGASNGG EDRWDCQFRH RGLKIVSGHQ YKVSYEITPS NSGKYYTKIG
     NLDGDVEVWH NMSNGYDLDS TWDPIPIGAN ETKKVEVTFT ASQNIDVAEW AFHLGGDGQY
     TPGGCFPAGT VITFDNMSLI DLTSDENDYV FPEVWQRADI LTNQVGYFAE REKKATLLCT
     DKDEVGFELI DESGDSVYEG KSEYFGYDED SEDTVHILDF SDFDGSGTFH IEADNGAVSR
     DFKVFAKDEV SDYSAMLYDS LNYFYQNRSG IEIKEEYISS GDKSSLARAA GHTTDNAEIQ
     QTWGYSGTSG TVDVTGGWYD AGDHGKYTVN GGLSLWMLQD LYEFFVYTGN EKIFADGSMI
     IPESGNGFPD LLDEARWEME WMLKMQIDGG DYSGMAYHKA HDETWTGLGV APADDDKKRI
     IKPQTTAATL NLAACAAQSA RLWEDLDKEF SDKCLDAAEK AYEAAKKHPD MYAPLDESVG
     GGAYGDNDVT DEFYWAAMEL YVSTGKDNYL KDAEKSDFYM TVPVTLGGGE SVDTVGTFDW
     GNTAALGTFT ALLNFESFDD VKKAEKSLKE AADHYLDTEN AQGFGLPYGQ STLSYNDKDK
     GYLWGSNSFV ADNAIVLAFA AVMNEDDSYT DGALQGLDYL LGRNAMDYSY VTGYGTHTTE
     NPHHRWWSNQ IDDAFPKAPC GVLSGGPNSG MQDPWVRGMG WKKGEIAPQK CYVDHVEAWC
     VNECTINWNA SLAWLTAFSA LNAEIKPGEG GKDIGVENDG GGASSTEKTT YDEEKAEENA
     AKSGKSAKSR SSAKDADDEN GEGISSTKLV VIIVAAVAVI ILIIATYVFI FEMTKLNRQS
     QNNNNGNNGD DK
//
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