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Database: UniProt
Entry: U3R8K1_9BACT
LinkDB: U3R8K1_9BACT
Original site: U3R8K1_9BACT 
ID   U3R8K1_9BACT            Unreviewed;       499 AA.
AC   U3R8K1;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:AGW99973.1};
RN   [1] {ECO:0000313|EMBL:AGW99973.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Pandey S., Tiwari R., Nain L., Saxena A.K.;
RT   "Diversity of endoglucanase gene in bacillus species.";
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC         cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000966,
CC         ECO:0000256|RuleBase:RU361153};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|RuleBase:RU361153}.
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DR   EMBL; KF240843; AGW99973.1; -; Genomic_DNA.
DR   AlphaFoldDB; U3R8K1; -.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.710; Endoglucanase-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR001956; CBM3.
DR   InterPro; IPR036966; CBM3_sf.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR   Pfam; PF00942; CBM_3; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SMART; SM01067; CBM_3; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   PROSITE; PS51172; CBM3; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361153};
KW   Cellulose degradation {ECO:0000256|RuleBase:RU361153};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:AGW99973.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361153};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..499
FT                   /note="Endoglucanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004648110"
FT   DOMAIN          350..499
FT                   /note="CBM3"
FT                   /evidence="ECO:0000259|PROSITE:PS51172"
FT   REGION          326..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   499 AA;  55105 MW;  B4FAA33FDD9CA11A CRC64;
     MKRSISIFIT CLLIAVLTMG GLLPSPASAG GTKTPAAKNG QLSIKGTQLV NRDGKAVQLK
     GISSHGLQWY GDFVNKDSLK WLRDDWGITV FRAAMYTADG GYIDNPSVKN KVKEAVEAAK
     ELGIYVIIDW HILNDGNPNQ NKEKAKEFFK EMSSLYGNTP NVIYEIANEP NGDVNWKRDI
     KPYAEEVISV IRKNDPDNII IVGTGTWSQD VNDAADAQFK DANVLYALHF YAGTHGQFLR
     DKANYALSKG APIFVTEWGT SDASGNGGVF LDQSREWLNY LDSKNISWVN WNLSDKQESS
     SALKPGASKT GGWPLTDLTA SGTFVRENIR GTKDSTKDGP ETPAQDNPTQ EKGVSVQYKA
     GDGRVNSNQI RPQLHIKNNG DAMVDLKDVT ARYWYNAKNK GQNVDCDYAQ MGCGNLTHKF
     VTLHKPKQGA DTYLELGFKT GTLSPGASTG NIQLRLHNDD WSNYAQSGDY SFFQSNTFKT
     TKKITLYHQG KQIWGTEPN
//
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