ID H6W9C5_9HELO Unreviewed; 310 AA. AC H6W9C5; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 22-FEB-2023, entry version 28. DE SubName: Full=Polygalacturonase 5 {ECO:0000313|EMBL:AFA52629.1}; DE Flags: Fragment; OS Botrytis paeoniae. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes; OC Helotiales; Sclerotiniaceae; Botrytis. OX NCBI_TaxID=278948 {ECO:0000313|EMBL:AFA52629.1}; RN [1] {ECO:0000313|EMBL:AFA52629.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMK439 {ECO:0000313|EMBL:AFA52629.1}; RX PubMed=22253834; DOI=10.1371/journal.pone.0029943; RA Andrew M., Barua R., Short S.M., Kohn L.M.; RT "Evidence for a common toolbox based on necrotrophy in a fungal lineage RT spanning necrotrophs, biotrophs, endophytes, host generalists and RT specialists."; RL PLoS ONE 7:E29943-E29943(2012). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. CC {ECO:0000256|ARBA:ARBA00008834, ECO:0000256|RuleBase:RU361169}. 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; JQ035913; AFA52629.1; -; Genomic_DNA. DR AlphaFoldDB; H6W9C5; -. DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProt. DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1. DR InterPro; IPR000743; Glyco_hydro_28. DR InterPro; IPR006626; PbH1. DR InterPro; IPR012334; Pectin_lyas_fold. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR PANTHER; PTHR31884; POLYGALACTURONASE; 1. DR PANTHER; PTHR31884:SF1; POLYGALACTURONASE; 1. DR Pfam; PF00295; Glyco_hydro_28; 1. DR SMART; SM00710; PbH1; 6. DR SUPFAM; SSF51126; Pectin lyase-like; 1. DR PROSITE; PS00502; POLYGALACTURONASE; 1. PE 3: Inferred from homology; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361169}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361169}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Signal {ECO:0000256|ARBA:ARBA00022729}. FT ACT_SITE 205 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10052" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AFA52629.1" FT NON_TER 310 FT /evidence="ECO:0000313|EMBL:AFA52629.1" SQ SEQUENCE 310 AA; 31474 MW; 6E7BBE0904176F5E CRC64; KRATTCTFSG SGGASSASKS KTSCSTIILS ALAVPSGTTL DLTGLTKGTT VIFEGITTFG YEEWSGPLVS VSGTDITVTQ TTGAYLDGGG ASYWDGEGSN GGKTKPKFFY AHSLISSTIE NLYFYNPPVQ VMSINSATDL TVSGVTIDAQ DGDTDSLGAN TDGFDIGSST TVTITGANVY NQDDCVAINS GTGITFSGGV CSGGHGLSVG SVGGRDDNIV ETVLFENSEI KASQNGIRIK TISGDTGTVS GITYSGITLS GITDYGITVN QAYDGTSGEP TNGVAISNFI LENITGTVES TATNILIECG //