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Database: UniProt
Entry: A0A0V8TA57_9CELL
LinkDB: A0A0V8TA57_9CELL
Original site: A0A0V8TA57_9CELL 
ID   A0A0V8TA57_9CELL        Unreviewed;      1129 AA.
AC   A0A0V8TA57;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   22-NOV-2017, entry version 12.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=ATM99_07590 {ECO:0000313|EMBL:KSW29539.1};
OS   Cellulomonas sp. B6.
OC   Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1295626 {ECO:0000313|EMBL:KSW29539.1, ECO:0000313|Proteomes:UP000054319};
RN   [1] {ECO:0000313|EMBL:KSW29539.1, ECO:0000313|Proteomes:UP000054319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B6 {ECO:0000313|EMBL:KSW29539.1,
RC   ECO:0000313|Proteomes:UP000054319};
RA   Piccinni F.E., Campos E.;
RT   "Draft Genome Sequence of Cellulolytic and Xylanolytic Cellulomonas
RT   strain Isolated from Decaying Forest Soil.";
RL   Submitted (NOV-2015) 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:KSW29539.1}.
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DR   EMBL; LNTD01000056; KSW29539.1; -; Genomic_DNA.
DR   RefSeq; WP_062101697.1; NZ_LNTD01000056.1.
DR   EnsemblBacteria; KSW29539; KSW29539; ATM99_07590.
DR   Proteomes; UP000054319; 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; -; 2.
DR   Gene3D; 2.60.40.10; -; 2.
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_sf.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR013098; Ig_I-set.
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   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
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:UP000054319};
KW   Glycosidase {ECO:0000256|RuleBase:RU361166};
KW   Hydrolase {ECO:0000256|RuleBase:RU361166,
KW   ECO:0000313|EMBL:KSW29539.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361166};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054319};
KW   Signal {ECO:0000256|RuleBase:RU361166};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL        1     33       {ECO:0000256|RuleBase:RU361166}.
FT   CHAIN        34   1129       Endoglucanase. {ECO:0000256|RuleBase:
FT                                RU361166}.
FT                                /FTId=PRO_5006774143.
FT   TRANSMEM   1101   1121       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       43    147       CBM-cenC. {ECO:0000259|Pfam:PF02018}.
FT   DOMAIN      355    435       CelD_N. {ECO:0000259|Pfam:PF02927}.
FT   DOMAIN      959   1057       I-set. {ECO:0000259|Pfam:PF07679}.
SQ   SEQUENCE   1129 AA;  118826 MW;  8CA0ED1D40FC2649 CRC64;
     MVPSHDPRRR RRTRWLAGAT SAALLLMPVL ASTATGAPVD QPHDFADGDA QGWHAYANTG
     SVTSGVTGGE MCATAEGGEN PWDVALQHDA MTFERGTTYT VSFDARASAP VTIPMQGGLG
     YPAAFGHPVV LDGTDTPQRV EFTFTPADWP TAPDSALAAD WTSGTGEISF QLGKQAAPYT
     LCIDDFSMTS GTRIVHSFAG GDLGGFDLYD NPGDGAGVPR ASADGSATCI DLRGGYTNAY
     QAGLELKHVA VEKDRTYQLR LTASSSVDGT PVNAIVGQYG APWDRAGSTS FDLTTTPQTF
     TFTFTAAVDL SAGTDEPYGR IQLELGRATD PYTFCITDLS FVETTEAPPA YEPETGPRVR
     VNQVGYLPDG PKRATLVTEA TDPVAWQLTS GSTVVARGTT TPRGVDPTAG VNVHEIEFDD
     VTAPGTYTLT ADDDTSYPFT IGADLYQDLR HDALNYFYPA RSGIAIDGSI MGDEAYSREA
     GHVGRPGDAT PNQGDYAVPC ITPEEAQGLY GDWTCDYTLD VVGGWYDAGD HGKYVVNGGI
     AVAQVLGTYE RALTSPTGDT APLGDGSLDI PRDEQTNGVP DPLDEARWEL EWMMRMQVPA
     GQPLAGMVHH KVHDVDWTGL PLLPADDPQP RRLHRPSTAA TLNFAAVAAQ GARLWEQYDP
     EFAADLLAAG RVAYDAAVAH PDLLQPAPNA DPSPGGGPYD DDDVQDEFYW AAAELYLTTG
     EQTYQDAVLA NEYHTADLFT KGGFFWGDVA ALGRMDLATV ESQIPGRTAI RQSVVDGAEL
     YLSRQSKEPF GTAYSGNAKG VYEWGSNSAV LNNQVVLGTA FDLTSDQRFA DAVVESMDYL
     MGRNALNSSY VTGYGTVFSE NQHSRWFSSS LTGSLPHPPR GSVAGGPNSD VGTWDPVIQG
     LYDPEHMCAP QLCYVDDIQS WSTNEITVNW NSALSWVASF VADQQAGDRS DAGTVAWVTT
     DPADVAAVEG TDATFTVAAT GSPTPTVTWQ RLVDGTWTDV DGAGATARTV STARAAVLAD
     GTTLTVPARV ADSGAQFRAY VANEFGGAYS APATLTVTAA AGPDGDPTAG PTDGPTSGTP
     TDGTAAPAAA SRPLATTGAN VGVALGVGLA LVLGGAAAVA LRRRARLRG
//
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