ID A0A559US88_9ACTN Unreviewed; 861 AA. AC A0A559US88; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 12-AUG-2020, entry version 4. DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166}; DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166}; GN ORFNames=FB456_102190 {ECO:0000313|EMBL:TVZ89714.1}; OS Streptomyces sp. CNZ289. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=2572907 {ECO:0000313|EMBL:TVZ89714.1, ECO:0000313|Proteomes:UP000316355}; RN [1] {ECO:0000313|EMBL:TVZ89714.1, ECO:0000313|Proteomes:UP000316355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CNZ289 {ECO:0000313|EMBL:TVZ89714.1, RC ECO:0000313|Proteomes:UP000316355}; RA Jensen P.; RT "Genome sequnecing to address fundamental questions about secondary RT metabolites and their potential function as extracellular electron shuttles RT (EESs)."; RL Submitted (JUN-2019) 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|RuleBase:RU361166}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family. CC {ECO:0000256|PROSITE-ProRule:PRU10060, ECO:0000256|RuleBase:RU361166}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:TVZ89714.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; VIST01000002; TVZ89714.1; -; Genomic_DNA. DR Proteomes; UP000316355; Unassembled WGS sequence. DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC. DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule. DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW. DR CDD; cd02850; E_set_Cellulase_N; 1. DR Gene3D; 1.50.10.10; -; 1. DR Gene3D; 2.60.120.260; -; 1. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 2.60.40.290; -; 1. DR InterPro; IPR008928; 6-hairpin_glycosidase_sf. DR InterPro; IPR012341; 6hp_glycosidase-like_sf. DR InterPro; IPR001919; CBD2. DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf. DR InterPro; IPR012291; CBM2_carb-bd_dom_sf. 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; PF00553; CBM_2; 1. DR Pfam; PF02018; CBM_4_9; 1. 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; 1. DR SUPFAM; SSF81296; SSF81296; 1. DR PROSITE; PS51173; CBM2; 1. DR PROSITE; PS00698; GH9_3; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, KW ECO:0000256|PROSITE-ProRule:PRU10060, ECO:0000256|RuleBase:RU361166}; KW Cellulose degradation {ECO:0000256|RuleBase:RU361166}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE- KW ProRule:PRU10060, ECO:0000256|RuleBase:RU361166}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE- KW ProRule:PRU10060, ECO:0000256|RuleBase:RU361166}; KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326, KW ECO:0000256|PROSITE-ProRule:PRU10060, ECO:0000256|RuleBase:RU361166}; KW Signal {ECO:0000256|RuleBase:RU361166}. FT SIGNAL 1..26 FT /evidence="ECO:0000256|RuleBase:RU361166" FT CHAIN 27..861 FT /note="Endoglucanase" FT /evidence="ECO:0000256|RuleBase:RU361166" FT /id="PRO_5022269425" FT DOMAIN 757..861 FT /note="CBM2" FT /evidence="ECO:0000259|PROSITE:PS51173" FT REGION 659..701 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 720 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060" FT ACT_SITE 729 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060" SQ SEQUENCE 861 AA; 89088 MW; FDBDC0A08216988B CRC64; MRRHIPRALA AALVAGALAA PGAAAADEGP ELIVNGGFDA GAAPWWFTPD SPGTVVDGRL CADVPAGTVN PWDAIIGQDG LPITAGETYA LSYTATATTP VTIRTNVQQG VEPWGQFFSS ADQVTDTAQT FEHVFTATAA DDAAQLAFQI GGSDTAYTFC VDDVSLRGGA EQPPYDPDTG SPVRVNQVGY LTDGPKNGTF VTDATEPLGW TLNAADGTEK ANGTTVPAGT DPTSLQNVHT FAFGDFTEAG DGYTVTIDGE TSEPFAIGDD IYGKLRTDAL AYFYHNRSGI EIDAELVGEE YARPAGHVGV APNQGDDGVP CQAGVCDYTL DAAGGWYDAG DHGKYVVNGG IAAAQVMAAY ERTLTTEGAD GEPVGDGKLA VPERGNGVPD VLDEARWQLE FLLAMQVPAG EELAGMAHHK LHDAQWTALP TLPHEDPQPR ELHPPSTAAT LNLAATGAQC GRLYADFDAD FADRCLSAAR TAYAAAKANP DMLADPNDGT GGGAYSDGDV SDEFYWAAAE LYLSTGEDAY LQDVLGSPLH GDAAAVFPGG GMSWGATAGL GALDLATVDS GLTDAQLAVV RGMVTDAADG YAADAANAAY GLPYAPEGGR YVWGSNSQVL NNMVVLATAH GLTGEAGYRD AVLTGLDYVL GRNPLNQSYV TGHGERDSKN QHHRHWANQL DPSLPNPPPG ALAGGPDSQL EDPVAQRELT GCAPAMCYID DIESYSTNEV TINWNAPLAW IAGYADDLGA GGGPGTGPGP GEECAAAYDV PNQWPGGFTG TVTISCDGAA LDGWTAEWDF PDGQRLQNAW NAVCTQAGTT VSCRNTPYNG AVPDGGSVSF GFNAGWSGSN GAPRDVKLGG T //