ID A9AWC6_HERA2 Unreviewed; 1128 AA. AC A9AWC6; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 04-NOV-2026, entry version 90. DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361186}; DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361186}; GN OrderedLocusNames=Haur_2136 {ECO:0000313|EMBL:ABX04776.1}; OS Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95). OC Bacteria; Bacillati; Chloroflexota; Chloroflexia; Herpetosiphonales; OC Herpetosiphonaceae; Herpetosiphon. OX NCBI_TaxID=316274 {ECO:0000313|EMBL:ABX04776.1, ECO:0000313|Proteomes:UP000000787}; RN [1] {ECO:0000313|EMBL:ABX04776.1, ECO:0000313|Proteomes:UP000000787} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23779 / DSM 785 / 114-95 RC {ECO:0000313|Proteomes:UP000000787}; RX PubMed=22675585; DOI=10.4056/sigs.2194987; RA Kiss H., Nett M., Domin N., Martin K., Maresca J.A., Copeland A., RA Lapidus A., Lucas S., Berry K.W., Glavina Del Rio T., Dalin E., Tice H., RA Pitluck S., Richardson P., Bruce D., Goodwin L., Han C., Detter J.C., RA Schmutz J., Brettin T., Land M., Hauser L., Kyrpides N.C., Ivanova N., RA Goker M., Woyke T., Klenk H.P., Bryant D.A.; RT "Complete genome sequence of the filamentous gliding predatory bacterium RT Herpetosiphon aurantiacus type strain (114-95(T))."; RL Stand. Genomic Sci. 5:356-370(2011). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase family 6. CC {ECO:0000256|RuleBase:RU361186}. 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; CP000875; ABX04776.1; -; Genomic_DNA. DR AlphaFoldDB; A9AWC6; -. DR STRING; 316274.Haur_2136; -. DR KEGG; hau:Haur_2136; -. DR eggNOG; COG5297; Bacteria. DR HOGENOM; CLU_279369_0_0_0; -. DR InParanoid; A9AWC6; -. DR BioCyc; HAUR316274:GHYA-2164-MONOMER; -. DR Proteomes; UP000000787; Chromosome. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro. DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule. DR GO; GO:0030245; P:cellulose catabolic process; IEA:InterPro. DR Gene3D; 2.60.40.290; -; 1. DR Gene3D; 3.20.20.40; 1, 4-beta cellobiohydrolase; 2. DR InterPro; IPR016288; Beta_cellobiohydrolase. DR InterPro; IPR036434; Beta_cellobiohydrolase_sf. DR InterPro; IPR001919; CBD2. DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf. DR InterPro; IPR012291; CBM2_carb-bd_dom_sf. DR InterPro; IPR018366; CBM2_CS. DR InterPro; IPR001524; Glyco_hydro_6_CS. DR PANTHER; PTHR34876; -; 1. DR PANTHER; PTHR34876:SF4; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE C-RELATED; 1. DR Pfam; PF00553; CBM_2; 1. DR Pfam; PF01341; Glyco_hydro_6; 2. DR PRINTS; PR00733; GLHYDRLASE6. DR SMART; SM00637; CBD_II; 1. DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1. DR SUPFAM; SSF51989; Glycosyl hydrolases family 6, cellulases; 2. DR PROSITE; PS51173; CBM2; 1. DR PROSITE; PS00561; CBM2_A; 1. DR PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 2. DR PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 2. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, KW ECO:0000256|RuleBase:RU361186}; KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001, KW ECO:0000256|RuleBase:RU361186}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361186}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361186}; KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326, KW ECO:0000256|RuleBase:RU361186}; KW Reference proteome {ECO:0000313|Proteomes:UP000000787}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361186}. FT SIGNAL 1..34 FT /evidence="ECO:0000256|RuleBase:RU361186" FT CHAIN 35..1128 FT /note="Glucanase" FT /evidence="ECO:0000256|RuleBase:RU361186" FT /id="PRO_5051622804" FT DOMAIN 30..139 FT /note="CBM2" FT /evidence="ECO:0000259|PROSITE:PS51173" FT REGION 145..222 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 656..695 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 160..222 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 661..682 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 322 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10056" FT ACT_SITE 371 FT /note="Proton donor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10057" FT ACT_SITE 793 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10056" FT ACT_SITE 842 FT /note="Proton donor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10057" SQ SEQUENCE 1128 AA; 118205 MW; 592028CCB4B01C77 CRC64; MARIFNSRGL ILVLLTAVVG SGLGQLNAKP TAAATSCEVV YNIANDWGSG FIGDVTLKNT GSAVSSWTLG WSFAGNQNIS NLWGGVVAQN GANVSVSNAG WNGNIGTGGT VNFGFQAGYS GANAKPTVFT LNGVTCGGTV VPTTPPTNTT VPTTPPTNTP VPSATTRPTN TTVPTTPPTS TTGPTNVPTN TPVPSATTRP TNTTVPTTPP TSTTGPTNTP APTTVPGVHV ANPFVGAQGY INSEYAARVN AEANATGGTL GSQMRQVASY PTAVWLDRIA AIAGSSESMG LRAHLDAALV QQQTSGQQVA ISIVVYDLPN RDCAALASNG ELKISENGLN RYKTEYIDPI AAIVGESKYA SLRIVVILEP DSLSNLVTNA SIPACAEAIS SGAYVQGVQY AINKLNVTSN VYIYMDIAHS GWLGWDSNFT PAIQLYTQTV RGTTKGLNGI DGFISNTANY TPLNEVFLPN SGLTLGGGNP IRSSLFYEWN PYFDETDYVL AMRNAFITAG FPSGIGMLID TSRNGWGGTA RPTMVSSSNS LEIYVNDSKL DRRPHRGGWC NQAGAGIGER PTAAPVSGID AYVWVKPPGE SDGVATAGVI DPTDPAKQFD AMCDPNAQNR YNTAYPTNAL AGAPHAGRWF PSQFAMLVRN AYPPISQSTN PTTTPVATTV PPTSTPVGTP APTSTPAPTS TPAPTSVPGV HVANPFVGAQ GYINSEYAAR VNAEANATGG TLGSQMLKVA SYPTAVWLDR IAAIAGSSDS MGLRAHLDAA LVQQQTSGQV AISIVVYDLP NRDCAALASN GELKISENGL NRYKTEYIDP IAAIVGESKY ASLRIVVILE PDSLSNLVTN ASIPACAEAI SSGAYVQGVQ YAINKLNVTS NVYIYMDIAH SGWLGWDSNF TPAIQLYTQT VRGTTKGLNG IDGFISNTAN YTPLNEIFLP NSGLTLGGGN PIRSSLFYEW NPYFDETDYV LAMRNAFITA GFPSGIGMLI DTSRNGWGGT ARPTMVSSSN SLEIYVNDSK LDRRPHRGGW CNQAGAGIGE RPTAAPVSGI DAYVWVKPPG ESDGVATAGV IDPTDPAKQF DAMCDPNAQN RYNTAYPTNA LAGAPHAGRW FPSQFAMLVR NAYPAIAP //