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Database: UniProt
Entry: U2X7N1_9MICO
LinkDB: U2X7N1_9MICO
Original site: U2X7N1_9MICO 
ID   U2X7N1_9MICO            Unreviewed;      1081 AA.
AC   U2X7N1;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-SEP-2017, entry version 20.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=MTS1_00785 {ECO:0000313|EMBL:GAD33441.1};
OS   Microbacterium sp. TS-1.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1344956 {ECO:0000313|EMBL:GAD33441.1, ECO:0000313|Proteomes:UP000018080};
RN   [1] {ECO:0000313|EMBL:GAD33441.1, ECO:0000313|Proteomes:UP000018080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TS-1 {ECO:0000313|EMBL:GAD33441.1,
RC   ECO:0000313|Proteomes:UP000018080};
RA   Fujinami S., Takeda K., Onodera T., Satoh K., Sano M., Narumi I.,
RA   Ito M.;
RT   "Draft Genome Sequence of Sodium-Independent Alkaliphilic
RT   Microbacterium sp. Strain TS-1.";
RL   Genome Announc. 1:e01043-13(2013).
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:GAD33441.1}.
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DR   EMBL; BASQ01000001; GAD33441.1; -; Genomic_DNA.
DR   EnsemblBacteria; GAD33441; GAD33441; MTS1_00785.
DR   OrthoDB; POG091H04TS; -.
DR   Proteomes; UP000018080; 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; -; 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; 2.
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:UP000018080};
KW   Glycosidase {ECO:0000256|RuleBase:RU361166};
KW   Hydrolase {ECO:0000256|RuleBase:RU361166};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361166};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018080};
KW   Signal {ECO:0000256|RuleBase:RU361166};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL        1     34       {ECO:0000256|RuleBase:RU361166}.
FT   CHAIN        35   1081       Endoglucanase. {ECO:0000256|RuleBase:
FT                                RU361166}.
FT                                /FTId=PRO_5005147468.
FT   TRANSMEM   1056   1076       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       39    161       CBM-cenC. {ECO:0000259|Pfam:PF02018}.
FT   DOMAIN      193    304       CBM-cenC. {ECO:0000259|Pfam:PF02018}.
FT   DOMAIN      342    413       CelD_N. {ECO:0000259|Pfam:PF02927}.
SQ   SEQUENCE   1081 AA;  114247 MW;  A8854646EC607BC4 CRC64;
     MEAMRQRHRR RVTSVITTGL LVGAAMTTAP LAAAAAPAEL LRNGDFSTGH EPWWSAGVDG
     FDTATGAFCA GVPDTENPWD VLIGQSDLAL VDGAAYTLTA RVRADATATV VAQVAPTVPD
     AAYTTYLAQS TQLTDDWQLI RAEFTARDLG QGTVSELQFR LGANGATRFC VDDVSLVAHD
     ASTPPVTPIG DDELLPNPTL DDSTNPWWTS GPVSLSNPGQ RMCATVTEQT PNLWDVLLGH
     NDIFLPGETD FRLSFTASAS SIATASAKVG TYTGASPTDW LEQSFTLDTQ PQSFDIAFTT
     TPAADYHLGQ VQFRLGAVPA GTEICFDEIS LRGTVYSYTA DPGPAVKVNQ VGYLPQGPKR
     ATVVSDAAAP LPWTLEAPDG SVLAMGETEP AGFDASAGAS VHRIDFSDVT EEAVDVRLRV
     GTDISHPFAI SADLFQSLRA DSMRFFYTNR SGIDIDGDIA DAEYARPAGH IGASPNQGDD
     NVGCLEPQPW SDGWTCSDRH DVRGGWYDAG DHGKYVVNGG IAVAQVLSTY ERAVAAGTAD
     ALGDSTLAVP ERGNGVPDIL DEARWQMEFL LRMQVPSGDP LAGMAWHKVH DRAWTGLPLM
     PHDDPQERLL HRPSTAATLN LAATAAQASR LYEPFDASFA QRLLEAAERA YDAALAHPDL
     LAPEEDGTGG GTYADDEVTD EFYWAAAELY ITTGSDRYRA EVEGNPLHQA DVFEPGGFYW
     GEVAALGRMQ LARFATDLPD IDRIRASVID AAERLIADQR AQPFGQPYAP DEGLYDWGSN
     SSVLNNQVVL GTAFDLTQRP RYADAVVEGF DYLLGRNVLG QSYITGYGTN DARNQHSRWY
     ANALDPALPN PPVGTVAGGP NSSIQDPVAG AWLKGCAPQA CYVDNIGAWS VNEITVNWNS
     ALAWVSSFVA DLGDGLVAVS PRAVDDVASG PAGGRIAVHP LANDVAGDAD IPLVAASLAL
     IDADGAPTTT VVVEGQGRYE LNGDVVSFIA DVAFERTADP VSYRVADARG TEVTATITAT
     VTASPASEEP SGSGAAGSAA PSATGGVLAR SGMDPLPLWV LTGVAAALTA AGVCLLRRRL
     D
//
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