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Database: UniProt
Entry: R5ECR6_9CLOT
LinkDB: R5ECR6_9CLOT
Original site: R5ECR6_9CLOT 
ID   R5ECR6_9CLOT            Unreviewed;       772 AA.
AC   R5ECR6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-SEP-2017, entry version 16.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=BN724_01362 {ECO:0000313|EMBL:CCX86577.1};
OS   Clostridium sp. CAG:590.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium; environmental samples.
OX   NCBI_TaxID=1262825 {ECO:0000313|EMBL:CCX86577.1, ECO:0000313|Proteomes:UP000017939};
RN   [1] {ECO:0000313|EMBL:CCX86577.1, ECO:0000313|Proteomes:UP000017939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:590 {ECO:0000313|Proteomes:UP000017939};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J.,
RA   Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E.,
RA   Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J.,
RA   Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F.,
RA   Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S.,
RA   Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F.,
RA   Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E.,
RA   Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T.,
RA   MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J.,
RA   Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units
RT   of genetic variation.";
RL   Submitted (NOV-2012) 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:CCX86577.1}.
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DR   EMBL; CAXF010000082; CCX86577.1; -; Genomic_DNA.
DR   Proteomes; UP000017939; 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; -; 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:UP000017939};
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:UP000017939};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL        1     26       {ECO:0000256|RuleBase:RU361166}.
FT   CHAIN        27    772       Endoglucanase. {ECO:0000256|RuleBase:
FT                                RU361166}.
FT                                /FTId=PRO_5005145472.
FT   DOMAIN       61    187       CBM-cenC. {ECO:0000259|Pfam:PF02018}.
FT   DOMAIN      231    310       CelD_N. {ECO:0000259|Pfam:PF02927}.
SQ   SEQUENCE   772 AA;  84334 MW;  4048EBDD221D81EE CRC64;
     MTRWKRGVAL LLVAAMTCSI AGCSSKKEES TTATTEVETT EEAKEDTTTE ESTQEVASTD
     GNMIRNGDFS NGVGNFSSYT NGGQMTMDVN DDGELQIDIA KTGSVEHGVQ VYYDGFELRE
     GGVYTFSFDV HSTVERDIAW RVQVNGGDYH AYATETVSVG PDVQHVESEF TMEEANDPAP
     RLCFNLGLLQ SMKDAGMDGS SLGEHSIYLD NLSLTVKDDS QMAADTEAVE APKVKVNQIG
     YATADKKTVI FSDLDEDDTT FQVINVDTNK SVYDGKISER ALNVSANEWN NNGDFSDVKD
     KGTYKIVTGK GEESYAFTIG DGIYDDAFKS IVKMLYLQRC GMELTSDKAG EFAHPVCHNT
     QATVYGTSKK VDVSGGWHDA GDYGRYVVSG AKTVADLLLA FEKQGGKIHA KDADNFDIPE
     SNNGVNDLID EVKYELDWML KMQDSSGGVY HKVTCKVFPE TVMPQDETDE LILSPISNTA
     TGDFAAVMAL ASRIYTEYGD SSDKAYAKIC LDAAKKAWSY LEKNKDADGF KNPEDIVTGE
     YPDGRSTDEA FWAAAELYKT TGDDTYKKAL SEYVSDSANL TGLGWASVGA YGSYAVLTND
     KLLTDSTNLT KDVRNAMVAA ADEAVAISKE NGYMVNRERS YEWGSNMGIA NTGMLLLMVN
     DISPKEEYVT YAKQHLNYLM GVNATGYCFV TGCGTLSPEH PHHRPSEVLE KCMPGMLVGG
     PDNGMEDPYA KAVFLNTAPA KCYVDNAQSY STNEVTIYWN SPLIYLMVAS QK
//
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