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Database: UniProt
Entry: R5V1N3_9FIRM
LinkDB: R5V1N3_9FIRM
Original site: R5V1N3_9FIRM 
ID   R5V1N3_9FIRM            Unreviewed;      1029 AA.
AC   R5V1N3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   10-MAY-2017, entry version 18.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=BN566_00362 {ECO:0000313|EMBL:CCZ84463.1};
OS   Ruminococcus sp. CAG:254.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ruminococcus; environmental samples.
OX   NCBI_TaxID=1262953 {ECO:0000313|EMBL:CCZ84463.1, ECO:0000313|Proteomes:UP000018181};
RN   [1] {ECO:0000313|EMBL:CCZ84463.1, ECO:0000313|Proteomes:UP000018181}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:254 {ECO:0000313|Proteomes:UP000018181};
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:CCZ84463.1}.
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DR   EMBL; CBAR010000238; CCZ84463.1; -; Genomic_DNA.
DR   Proteomes; UP000018181; 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; IPR016134; Dockerin_dom.
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; SSF63446; SSF63446; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS51766; DOCKERIN; 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:UP000018181};
KW   Glycosidase {ECO:0000256|RuleBase:RU361166};
KW   Hydrolase {ECO:0000256|RuleBase:RU361166,
KW   ECO:0000313|EMBL:CCZ84463.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361166};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018181};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL        1     35       {ECO:0000256|RuleBase:RU361166}.
FT   CHAIN        36   1029       Endoglucanase. {ECO:0000256|RuleBase:
FT                                RU361166}.
FT                                /FTId=PRO_5005145533.
FT   DOMAIN      951   1025       Dockerin. {ECO:0000259|PROSITE:PS51766}.
SQ   SEQUENCE   1029 AA;  112069 MW;  E10A8BABD3CF3792 CRC64;
     MLKNKFGKKA VAAVMAAAMT VSATAMGLSS ITASAAVTGF EEFGAGTFND GVGLPWHICE
     SATGTMKFEV ANGCYNILIT NPGGLSNNGE GRWDCQFRHR GLTIEAGHTY RYTYSIWSNK
     DAKIYCKLGD ITNDDLENWH QNGDKLQMDY DESLDDQQLT EKLKSASKTG EKVDFGMGWD
     SWKNQPTVTA NKWTTYAWEF TAEKDSKGTA EMTFHLGGTS AYNDFICCEA GTLLKFDNLA
     LVDMTDDKSN YNAEAAYQPT GVEVNQVGYY PLLEKKATLI LDGPDTTAKD FQVKDSSGAV
     VYEGKTDASR GNQICDGSET YNQIIDFSDF QTEGTGYTIT CDGKTSLPFD IGNNIYDGMT
     TNAMNYFYQN RSGVNIDAAY ITSQGENSDK SKLARKAGHN PDTAYIQNKW VYIIPDENSI
     EKNNGTIDVT GGWYDAGDHG KYVVNGGVSM WTLLNLYESD LMAGDASKWA DGSGTVVVPE
     NGNSMPDILD EVKIEADFFK KMQRNDGMVY HKIHDYKWTA LCVAPADDEL TRIVKPVTYA
     ATLNFAAAMA QYARLAKDYD KDASGYLADA EKAYKAAKAS YKPFSNDWGT DQYADLESLY
     APIAQNKGGG PYGDTDVEDE FYWAACELYI ATGDASYKTD LEGYSAGAGA YGVDTALYGG
     ENNGTRSSFT WGTLASLGTF SLCVNAKDMQ EKGLLSAEEV STIQKNVKQA ADYFIDLENA
     SDFGIPYVGH DYNADVWSVA DYEAGNGVDG VVSKELKNGY EWGSNSMVMN NAITMALAYD
     IDHEAKYING VSTAMDYILG RNVIEQSYVT GYGEHCLKYP HHRWWSGQLD AERFPYAPDG
     VLSGGPNSQM QDPMIQGAGY KAGSLAPMAC YLDNVEAWSV NECTINWNSP LVWIASFLED
     EAPNVNNETT KPSTTTTTDS DTTTTTTTTV ATTTASGETT TAGSTTTVDP NADNIGDVNL
     DGIVDIADAV TLNKYLAGVV QLSDQALRNA NCDQSPTDID NVGDKDTTAL VRFVLNMEGY
     QDLPFIAAE
//
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