ID A0A9P5HU67_9HELO Unreviewed; 450 AA. AC A0A9P5HU67; DT 13-SEP-2023, integrated into UniProtKB/TrEMBL. DT 13-SEP-2023, sequence version 1. DT 02-OCT-2024, entry version 7. DE RecName: Full=Probable glucan endo-1,3-beta-glucosidase eglC {ECO:0000256|ARBA:ARBA00019762}; DE EC=3.2.1.39 {ECO:0000256|ARBA:ARBA00012780}; DE AltName: Full=Endo-1,3-beta-glucanase eglC {ECO:0000256|ARBA:ARBA00032134}; DE AltName: Full=Laminarinase eglC {ECO:0000256|ARBA:ARBA00032906}; GN ORFNames=EAE97_011423 {ECO:0000313|EMBL:KAF7920530.1}; OS Botrytis byssoidea. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes; OC Helotiales; Sclerotiniaceae; Botrytis. OX NCBI_TaxID=139641 {ECO:0000313|EMBL:KAF7920530.1, ECO:0000313|Proteomes:UP000710849}; RN [1] {ECO:0000313|EMBL:KAF7920530.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MUCL 94 {ECO:0000313|EMBL:KAF7920530.1}; RA Valero Jimenez C.A., Steentjes M., Scholten O.E., Van Kan J.A.L.; RT "Comparative genomics of Sclerotiniaceae."; RL Genome Biol. Evol. 0:0-0(2020). CC -!- FUNCTION: Glucanases play a role in cell expansion during growth, in CC cell-cell fusion during mating, and in spore release during CC sporulation. This enzyme may be involved in beta-glucan degradation and CC also function biosynthetically as a transglycosylase. CC {ECO:0000256|ARBA:ARBA00025152}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)- CC beta-D-glucans.; EC=3.2.1.39; CC Evidence={ECO:0000256|ARBA:ARBA00000382}; CC -!- SUBCELLULAR LOCATION: Secreted, cell wall CC {ECO:0000256|ARBA:ARBA00004191}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. CC {ECO:0000256|ARBA:ARBA00008773, ECO:0000256|RuleBase:RU004335}. 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:KAF7920530.1}. 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; RCSW01000037; KAF7920530.1; -; Genomic_DNA. DR Proteomes; UP000710849; Unassembled WGS sequence. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR050732; Beta-glucan_modifiers. DR InterPro; IPR000490; Glyco_hydro_17. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR16631; GLUCAN 1,3-BETA-GLUCOSIDASE; 1. DR PANTHER; PTHR16631:SF13; GLUCAN ENDO-1,3-BETA-GLUCOSIDASE EGLC-RELATED; 1. DR Pfam; PF00332; Glyco_hydro_17; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. PE 3: Inferred from homology; KW Cell wall {ECO:0000256|ARBA:ARBA00022512}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..18 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 19..450 FT /note="Probable glucan endo-1,3-beta-glucosidase eglC" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5040264055" FT REGION 362..430 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 450 AA; 43874 MW; 30D71589094678C0 CRC64; MLSKTLFVVA ASLSTASAIN QGFNYGATNA DGSYRVQSDF QDAFETANSL VGTSGFTSAR LYTMLQGDTT EPTSAIPAAI ASDTTLLLGL WASGGAAGVT AEINALKAAI TKYGTAFTSR VVGISVGSED LYRNSPTGIA ANSGYGANPA DLVDYIKQVR EAIAGTGLSG ASIGHVDTWT AWVNGSNSAV AEALDWVGMD AYPYFQDTEA NGVSEGKSLF NSALAATQSA TGKTVWVTET GWPVTGATAG DGVPSADNAK TYWDDVGCPN FGKINMYWYT LQDQNAASSV TPSFGIVGST LSTTPLFDLS CSNTTSSSSS TASSKATSGI AAVATGGSVA SAGSGLSPTG MGAGISAVSG AASPSGTGSA GGSPAGGSTN GTYTASTLKS SAGSSATGTS TSGSGSSGSS SGSASGSSSS SPSESTGGAA SLTGSVAIAL GAVFAVAAAL //