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Database: UniProt
Entry: R4LN52_9ACTN
LinkDB: R4LN52_9ACTN
Original site: R4LN52_9ACTN 
ID   R4LN52_9ACTN            Unreviewed;      1016 AA.
AC   R4LN52;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-SEP-2017, entry version 24.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   Name=cel1 {ECO:0000313|EMBL:AGL16685.1};
GN   ORFNames=L083_3175 {ECO:0000313|EMBL:AGL16685.1};
OS   Actinoplanes sp. N902-109.
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Actinoplanes.
OX   NCBI_TaxID=649831 {ECO:0000313|EMBL:AGL16685.1, ECO:0000313|Proteomes:UP000013541};
RN   [1] {ECO:0000313|EMBL:AGL16685.1, ECO:0000313|Proteomes:UP000013541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N902-109 {ECO:0000313|EMBL:AGL16685.1,
RC   ECO:0000313|Proteomes:UP000013541};
RA   Hu H., Huang H., Lu X., Zhu B.;
RT   "Comparative analysis of rapamycin biosynthesis clusters between
RT   Streptomyces hygroscopicus ATCC 29253 and Actinoplanes sp. N902-109.";
RL   Submitted (MAY-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}.
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DR   EMBL; CP005929; AGL16685.1; -; Genomic_DNA.
DR   EnsemblBacteria; AGL16685; AGL16685; L083_3175.
DR   KEGG; actn:L083_3175; -.
DR   PATRIC; fig|649831.3.peg.3127; -.
DR   KO; K01179; -.
DR   OrthoDB; POG091H04TS; -.
DR   Proteomes; UP000013541; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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; IPR008965; Carb-bd_dom.
DR   InterPro; IPR001919; CBD2.
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   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF02018; CBM_4_9; 2.
DR   Pfam; PF02927; CelD_N; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS51173; CBM2; 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:UP000013541};
KW   Glycosidase {ECO:0000256|RuleBase:RU361166};
KW   Hydrolase {ECO:0000256|RuleBase:RU361166,
KW   ECO:0000313|EMBL:AGL16685.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361166};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013541};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL        1     33       {ECO:0000256|RuleBase:RU361166}.
FT   CHAIN        34   1016       Endoglucanase. {ECO:0000256|RuleBase:
FT                                RU361166}.
FT                                /FTId=PRO_5005145398.
FT   DOMAIN      903   1016       CBM2. {ECO:0000259|PROSITE:PS51173}.
SQ   SEQUENCE   1016 AA;  106083 MW;  21CF618AB27EE9C0 CRC64;
     MTPHLRRRVT MLTAAATAAM LALTSLTANP ASAEPAQLIA NGDFATGTTG WWSTDNAPIS
     AAGGELCADV PGGTTNAWDV SLGYNDVPLV AGAAYRLSFR AHADAPVTVR ANVQLNEDPY
     TAALSRSVAL TTAAQTFDSS FTSSLQSANG TLTFQLGGSA QAFRFCLDDV SLTSDTAAPP
     AGAEQLENGD FSDGTAGWYS YGTTATGVDD GQLCTTVPGG LANPWDAGIG QNNVTLQAGS
     AYTLSFDATA SPGATVRAAV QLGADPYTSY LSRDVALTPA RQHLEYTFTA SEDTTAGQVA
     FQVGGAAAEY RLCLDNVSLT GGEAEPPYVP DTGPRVRVNQ VGYLPAGPKN ATLVTDATTA
     LDWQLKNAAG SVVRSGRSTP RGVDAASGQN VHTIDFTGYT TAGTGYTLVA DGQTSHPFDI
     SGTVYERLRP DALQFFYIQR SGIAIDGGLV GEQYARPAGH LGVAPNKGDT DVPCRANTCD
     YRLDVRGGWY DAGDQGKYVV NGGIAVQQLM SSFERTKTAV TAAHGAGLAD STLRVPERGN
     KVPDILDEAR WELEFLMRMQ VPAGQPLAGM AHHKMHDANW TGLPMQPQDD PEQRELQPPS
     TAATLNLAAT TAQCARLFAP YDATFAAKCL TVARTAYAAA KANPAKLAQD LGGGGGSYGD
     DDVSDEFYWA AAELYLTTGE AAFLTDVTAS RHHTGDVFAA TGFGWASTAA LGRLDLATVP
     SALPAADRER VRQSVLTAAD GYLATVGAQA YGLPMPGNAG AYFWGANSNI LNNVQVLATA
     FDMTGAAKYR DAAVQGVDYI FGRNALNQSY VTGWGEKASE NQHTRIYAHE KDAALPHPPA
     GSLAGGANAG LDDPYAKSLL TGCKPMFCYV DDIESYATNE LAINWNSALA WVASFLADQG
     RGEPAAAVSC RATYTNYGDW ADKSGFTAQL AVTNTGTKAI DGWAVRFAFL GGQKVRDAWS
     AEATQSGATV TAKNLAANQR IQPGATVYFG FNATTPGGPN PAPELITLNG SACGRS
//
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