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Database: UniProt
Entry: A0A0A0BZU9_9CELL
LinkDB: A0A0A0BZU9_9CELL
Original site: A0A0A0BZU9_9CELL 
ID   A0A0A0BZU9_9CELL        Unreviewed;      1175 AA.
AC   A0A0A0BZU9;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   22-NOV-2017, entry version 20.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=N869_15565 {ECO:0000313|EMBL:KGM13202.1};
OS   Cellulomonas bogoriensis 69B4 = DSM 16987.
OC   Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1386082 {ECO:0000313|EMBL:KGM13202.1, ECO:0000313|Proteomes:UP000054314};
RN   [1] {ECO:0000313|EMBL:KGM13202.1, ECO:0000313|Proteomes:UP000054314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=69B4 {ECO:0000313|EMBL:KGM13202.1,
RC   ECO:0000313|Proteomes:UP000054314};
RA   Chen F., Li Y., Wang G.;
RT   "Genome sequencing of Cellulomonas bogoriensis 69B4.";
RL   Submitted (AUG-2013) 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:KGM13202.1}.
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DR   EMBL; AXCZ01000058; KGM13202.1; -; Genomic_DNA.
DR   EnsemblBacteria; KGM13202; KGM13202; N869_15565.
DR   Proteomes; UP000054314; 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; 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; 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:UP000054314};
KW   Glycosidase {ECO:0000256|RuleBase:RU361166};
KW   Hydrolase {ECO:0000256|RuleBase:RU361166,
KW   ECO:0000313|EMBL:KGM13202.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361166};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054314};
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   1175       Endoglucanase. {ECO:0000256|RuleBase:
FT                                RU361166}.
FT                                /FTId=PRO_5005108387.
FT   TRANSMEM   1146   1166       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       34    138       CBM-cenC. {ECO:0000259|Pfam:PF02018}.
FT   DOMAIN      334    416       CelD_N. {ECO:0000259|Pfam:PF02927}.
SQ   SEQUENCE   1175 AA;  122294 MW;  A4EF84AA9AB3F0D6 CRC64;
     MVSLLRRGSR AAGVGALTAG VLALGGLTGP ALAVVDESFD DGGSAWDSYG LDPTSTEDGT
     FCAEVPASDN PWDAGVVLNG VAVEEGTIYD FAFTASGDPG HTIRAVVGQD GAPYATVLDE
     NVALSPELAE HAFTFTADLS LPATSGPEDP RGQIAFQVGG SGEAWTFCLD AVSLGGDTEL
     LPQTSFADGA GVWDVSGETS QEVVEDALCL GVPAGGNPWS TGLTFNGLPI EEGGNYVLSF
     TASSDPSAGL RVLVGENAAP HRMVIEEHPV LSPEPEEHVF AFTASHTFPA ESEDEPIGQL
     AFHLGAQAQD YTFCITDVSL VATATPPPPY SPDTGPAVRV NQHGYLPEGP KRATLVTDAE
     EPLAWELRDG DGQVAASGET LPHGFDPMAG LDVHVIDFTD TSLTGAGLTL AVGDEVSHPF
     AIGADLYQQL RYDALNYFYL ARSGIDIDAA IVGEEYAREA GHVNDPERTR VPDSPNRGDY
     QVPCLTPEDE GSAWAYGDWS CPEGYALDVV GGWYDAGDHG KYVVNGGISV AQLMGLYERS
     VHAPTGDVDA LGDGTLALPE TGNGVPDVLD EARWQLQFLL SMQVPEGNPL AGMAHHKIHD
     VGWTGLPLMP AADPQERRLH RPSTAATLNL AATAAQGARL FADHEDVYPG FAGELLDAAR
     LAWAAALENP ELYAPAAAGG NGGGPYDDDE VTDEFYWAAA ELYLTTGEPE FEQAVLDNPL
     HEADIWGPSG FTWGDTAALG RLNLATVPND LPGRDAVRES VVEGARTYLA WQAQEPFATT
     YPGVDGDYEW GSNSMVVNNQ VVLATAFDLT GQEEFRDGVV EAMDYLLGRN ALNLSYLTGY
     GTVYSENQHS RWFAAQVNPA LPNPPPGSLA GGPNSMRSTW DPTMQGLFGG GNDCAPAACY
     VDHINSWASN EITINWNAAM SWVASFLADQ GDGSVAPAPA AVTVTEHPAD VTVAEGAQGR
     FSAAASGEVL SVRWQRADAD GDWVDVPDAS TTELVLVASL EDDGARVRAV FTGPDGDVVT
     EAATMTVVPA EVAPGAAVVE LSDDQVRAGD ELGVTVHDVA PGEQVEIWLT SDPVLLATVE
     ADGEGTLEVV VVVPADTQAG PHTVVALGLA SGIEGSAALQ VLAADDGGPG AGADGPGGLA
     LTGASVVWLV AAIVLLLVAG GAAVAVTRAR ARREG
//
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