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Database: UniProt
Entry: C9Z0D5_STRSW
LinkDB: C9Z0D5_STRSW
Original site: C9Z0D5_STRSW 
ID   C9Z0D5_STRSW            Unreviewed;       747 AA.
AC   C9Z0D5;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   22-NOV-2017, entry version 53.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   Name=cel1 {ECO:0000313|EMBL:CBG68068.1};
GN   OrderedLocusNames=SCAB_8871 {ECO:0000313|EMBL:CBG68068.1};
OS   Streptomyces scabiei (strain 87.22).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG68068.1, ECO:0000313|Proteomes:UP000001444};
RN   [1] {ECO:0000313|EMBL:CBG68068.1, ECO:0000313|Proteomes:UP000001444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.22 {ECO:0000313|EMBL:CBG68068.1,
RC   ECO:0000313|Proteomes:UP000001444};
RX   PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA   Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H.,
RA   Parry R.J., Loria R.;
RT   "Streptomyces scabies 87-22 contains a coronafacic acid-like
RT   biosynthetic cluster that contributes to plant-microbe interactions.";
RL   Mol. Plant Microbe Interact. 23:161-175(2010).
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; FN554889; CBG68068.1; -; Genomic_DNA.
DR   RefSeq; WP_012998800.1; NC_013929.1.
DR   ProteinModelPortal; C9Z0D5; -.
DR   STRING; 680198.SCAB_8871; -.
DR   CAZy; CBM4; Carbohydrate-Binding Module Family 4.
DR   CAZy; GH9; Glycoside Hydrolase Family 9.
DR   EnsemblBacteria; CBG68068; CBG68068; SCAB_8871.
DR   GeneID; 24310606; -.
DR   KEGG; scb:SCAB_8871; -.
DR   eggNOG; ENOG4105E08; Bacteria.
DR   eggNOG; ENOG410XNTA; LUCA.
DR   HOGENOM; HOG000245359; -.
DR   KO; K01179; -.
DR   OMA; YYTQRSG; -.
DR   OrthoDB; POG091H04TS; -.
DR   Proteomes; UP000001444; 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; -; 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; 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   InterPro; IPR006311; TAT_signal.
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; SSF81296; SSF81296; 1.
DR   PROSITE; PS00698; GLYCOSYL_HYDROL_F9_2; 1.
DR   PROSITE; PS51318; TAT; 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:UP000001444};
KW   Glycosidase {ECO:0000256|RuleBase:RU361166};
KW   Hydrolase {ECO:0000256|RuleBase:RU361166};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361166};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001444};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL        1     29       {ECO:0000256|RuleBase:RU361166}.
FT   CHAIN        30    747       Endoglucanase. {ECO:0000256|RuleBase:
FT                                RU361166}.
FT                                /FTId=PRO_5005125930.
FT   DOMAIN       33    155       CBM-cenC. {ECO:0000259|Pfam:PF02018}.
FT   DOMAIN      182    264       CelD_N. {ECO:0000259|Pfam:PF02927}.
SQ   SEQUENCE   747 AA;  80245 MW;  0E68B5D4B13EAA19 CRC64;
     MKRRRTSLLA LTALLAAALT ALPGGSAQAD EVEQVKNGTF DTTTAPWWTT GNVTAGLTDG
     RLCADIPGGT ANRWDAAVGQ NDITLVKGES YRFRFSASGS PQGNVLRAIV GLSVDPYDTY
     FEVSPQLNVS GDSYTYTFTS PVDTAQAQVG FQVGGNANPF TFCMDDVSLL GGVPPEVYEP
     DTGPRVRVNQ VAYLPAGPKN ATLVTDATAK LPWKLKNASG AVVAHGRTAP RGLDASSGQK
     VHSIDFGAYR KRGTAFTLVV DGETSRPFDI DPRAYERLRL DSLKYYYTQR SGTPISDALR
     PGYGRAAGHV DVAPNQGDGN VPCQPGVCDY RLDVTGGWYD AGDHGKYVVN GGISTWEVLS
     TYERALHART GKAGRLGDGS LDIPESGNKV PDLLDEVRWE LDFLLRMQVP KGRPLAGMAH
     HKIHDEQWTG LPLMPAADPQ KRELHPPSTA ATLNLAATAA QAARLYRPYD RAFAAKALAA
     ARTAWAAAVE HPAMYASESD GVGGGTYADG NVTDEFYWAA SQLYLTTGEK AFREYVLASP
     VHTADIFGPV GFDWARTAAA GRLDLATVPN KLPGRDKVRK SVVEGADRYL AALKAQPYGM
     PYAPDGSVYD WGSNHQILNN AVVVATAYDI TGASKYREGA LQSMDYLFGR NALNISYVTG
     YGEVAAHNQH SRWYAHQLDP NQPSPPAGTL AGGANSGIQD PYAQSKLQGC VGQFCYIDDI
     QSWSTNEHTI NWNAALARMA SFVADQT
//
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