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Database: UniProt
Entry: R5KL57_9CLOT
LinkDB: R5KL57_9CLOT
Original site: R5KL57_9CLOT 
ID   R5KL57_9CLOT            Unreviewed;       766 AA.
AC   R5KL57;
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=BN572_01003 {ECO:0000313|EMBL:CCY61841.1};
OS   Clostridium sp. CAG:264.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium; environmental samples.
OX   NCBI_TaxID=1262786 {ECO:0000313|EMBL:CCY61841.1, ECO:0000313|Proteomes:UP000018342};
RN   [1] {ECO:0000313|EMBL:CCY61841.1, ECO:0000313|Proteomes:UP000018342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:264 {ECO:0000313|Proteomes:UP000018342};
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:CCY61841.1}.
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DR   EMBL; CAYM010000217; CCY61841.1; -; Genomic_DNA.
DR   Proteomes; UP000018342; 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:UP000018342};
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:UP000018342};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL        1     31       {ECO:0000256|RuleBase:RU361166}.
FT   CHAIN        32    766       Endoglucanase. {ECO:0000256|RuleBase:
FT                                RU361166}.
FT                                /FTId=PRO_5005145499.
FT   DOMAIN       75    200       CBM-cenC. {ECO:0000259|Pfam:PF02018}.
FT   DOMAIN      239    316       CelD_N. {ECO:0000259|Pfam:PF02927}.
SQ   SEQUENCE   766 AA;  84362 MW;  158ECEB3C1C2309D CRC64;
     MRKMKKVAVL CLTAAMTMSL LAGCGGTKKN ADGETTEVTT EAESTEEEET TTEKATEEET
     EEPTTEALGV SDGDKVININ FDDKDTDGFH TYTNGGNEEM TNEDGELHIN IKKTGSADYA
     NQIYYDGFRL YQGCVYEYSF DVRCDIERTI EWRLQINGGD YHAYTSDVIT IGPETQHITA
     QFTMEEDSDP APRLCFNMGK QEGMTGDEAE HNIYFDNILL EAVDASGAQQ VEATPDPMAI
     NVNQVGYLTG DSKVATVIGK NAKSFEVIDV TSNKSVYSAD LPEEATYDPP SEMFCKQADF
     SSVKDAGTYK IKTDDGEESA EFKIGDDIYG DLYKDVVLML YNQRCGVELD SSIAGEFAHP
     ACHTGEAVVY GTDKKIDVTG GWHDAGDYGR YVVSGAKTVQ DLFMTYEDNE YKADDIGIPE
     SGNGVPDILD EARYELDWML KMQDDNGGVY HKVTCDVFPE TVMPEKETAQ LIACPISNTA
     TGDFTAVMAK ASVLYKEYDA DFAAKCLEAS KKAYEYLSGN MDAHGFSNPD DIVTGEYPDT
     IFRDEAIWAA VELYAATGDD SYKKAVDAII EGDDIVNYGL GWADVGYYAL YDYIKYDGGS
     AKANELFFNE VDKTVEQIKD NGFGVWVSPT KTFAWGSNMN IANKGMLLLM ANKLKPDADY
     VKYASYQRDY LLGRNAVGYC YVTGFGTRTP LHPHHRPSQV LDVAMPGMLV GGADSNLEDP
     YAKAVLLGKA PESRYADNAQ SFSCNEITIY WNSPLIYLLS GLGNTK
//
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