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Database: UniProt
Entry: F7ZZT2_CELGA
LinkDB: F7ZZT2_CELGA
Original site: F7ZZT2_CELGA 
ID   F7ZZT2_CELGA            Unreviewed;      1212 AA.
AC   F7ZZT2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-SEP-2017, entry version 32.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   OrderedLocusNames=Celgi_2074 {ECO:0000313|EMBL:AEI12575.1};
OS   Cellulomonas gilvus (strain ATCC 13127 / NRRL B-14078) (Cellvibrio
OS   gilvus).
OC   Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=593907 {ECO:0000313|EMBL:AEI12575.1, ECO:0000313|Proteomes:UP000000485};
RN   [1] {ECO:0000313|Proteomes:UP000000485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13127 / NRRL B-14078 {ECO:0000313|Proteomes:UP000000485};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Munk A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D.,
RA   Brumm P., Woyke T.;
RT   "Complete sequence of Cellvibrio gilvus ATCC 13127.";
RL   Submitted (APR-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}.
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DR   EMBL; CP002665; AEI12575.1; -; Genomic_DNA.
DR   ProteinModelPortal; F7ZZT2; -.
DR   STRING; 593907.Celgi_2074; -.
DR   EnsemblBacteria; AEI12575; AEI12575; Celgi_2074.
DR   KEGG; cga:Celgi_2074; -.
DR   eggNOG; ENOG4105E08; Bacteria.
DR   eggNOG; ENOG410XNTA; LUCA.
DR   KO; K01179; -.
DR   OMA; CAPQLCY; -.
DR   OrthoDB; POG091H04TS; -.
DR   Proteomes; UP000000485; Chromosome.
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; -; 2.
DR   Gene3D; 2.60.40.10; -; 4.
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; IPR007110; Ig-like_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF02927; CelD_N; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   Pfam; PF07679; I-set; 1.
DR   SMART; SM00409; IG; 3.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF48726; SSF48726; 3.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS00698; GLYCOSYL_HYDROL_F9_2; 1.
DR   PROSITE; PS50835; IG_LIKE; 3.
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:UP000000485};
KW   Glycosidase {ECO:0000256|RuleBase:RU361166};
KW   Hydrolase {ECO:0000256|RuleBase:RU361166,
KW   ECO:0000313|EMBL:AEI12575.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361166};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000485};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL        1     42       {ECO:0000256|RuleBase:RU361166}.
FT   CHAIN        43   1212       Endoglucanase. {ECO:0000256|RuleBase:
FT                                RU361166}.
FT                                /FTId=PRO_5005130382.
FT   DOMAIN      941   1026       Ig-like. {ECO:0000259|PROSITE:PS50835}.
FT   DOMAIN     1032   1118       Ig-like. {ECO:0000259|PROSITE:PS50835}.
FT   DOMAIN     1124   1209       Ig-like. {ECO:0000259|PROSITE:PS50835}.
SQ   SEQUENCE   1212 AA;  127283 MW;  8DA8D907C1853B83 CRC64;
     MVSSKYPWRA PRSGHARTAS LVGGVAAGAL VIGVAVAPLA AADPLDEVHD FSDGTQGWYG
     YGGGPAMSTG VVDGELCVVV PAGTDEPWDV AIQHDDIDFA AGDRYTVGFT AHATSPVTVN
     LRGGIGYPDD VASSVSVGTE TDAYSFTWEP EFSGSGNISF QLGAQAQDYT LCIDDFVIDS
     GQELVPDTTF DGVLPDGWTN DGWTVTSEAG EGEPLCFEVP GTAGTYAGLV LNGLPIEEGG
     NYELTYTASA SNGATIRTVV GENAAPWRTA FVDNTELSTD LTEHALAFTS TFTFPAESAD
     PAVGVGQVAL QMGARGDFTF CITSLSLKKV ATPPPPYEPD TRGPVRVNQL GYLTNGPKNA
     TVVSESATPL AWQLQDASHA VVAEGEATPA GVDPTSQLTV QTIDFSDVTA AGQGYTLVVG
     EDRSDPFAIG DDLYEQFRYD ALNYYYPVRS GIAVDVPDDR YDRPAGHVDG PDGAVNKGDQ
     DVACLTAADD GASWSYGSWT CPQGYSLDVV GGWYDAGDHG KYVVNGGISV AQLMSAYERT
     LHVDHASDDA FADGTLDVPA DESGNGVPDV LDEARWELEF FLAMQVPAGS GMTVSDTDDR
     SLDGLVHHKI HDVGWTGLDL LPSADPQQRR LHRPSTAATL NLAATAAQGA RLFRAYDAAF
     ADELLEAAET AYAAAQRVPD LYAPASAGAN GGGPYDDADV SDEFYWAAAE LYLTTAADEY
     EADVLASEHA DDDIWTRGAF SWGAVAALGR MDLATVPSEL PTRAAVRASV VEGAQKYLAW
     QQAEAFGTAY PGGEDLSYEW GSNSMVLNTQ VILATAYDLT GEPAFAAAVV ESMDYLLGRN
     ALNNSYVTGY GTTFSSHQHS RWLVPPMPGT VAGGPNSKRG TWDPVMNGLY PEGHECAPQL
     CYVDSIEAWS VNELTINWNA PLAWVVSFVD DLGAGVTAQA PVVTTQPASV TVALGAKATF
     TAAASGTPAP TVTWQWRAPG GTWKTVAGAT SPSLTVTATA ATDGRQYRAV FTSSAGTATS
     DVATLRVRAV KPVVTTHPAS ASAALGRKVT LRADASGYPT PTVRWQQQRP GSSTWTDVKG
     ATSRTLVVAV TRATDGVRYR AVFTNRAGSA TSRAAKVTLV RAAPRFVDHP DGTTVRAGQK
     VTLSATVLAY PAATLTWYVK APGSSSWKAV PGATGTRLTL VASRSLDGAQ YKVVARNALG
     SAWSKAALLR VR
//
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