ID H6W9D2_9HELO Unreviewed; 310 AA. AC H6W9D2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 18-JAN-2017, entry version 16. DE SubName: Full=Polygalacturonase 5 {ECO:0000313|EMBL:AFA52636.1}; DE Flags: Fragment; OS Botryotinia calthae. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes; OC Helotiales; Sclerotiniaceae; Botryotinia. OX NCBI_TaxID=38488 {ECO:0000313|EMBL:AFA52636.1}; RN [1] {ECO:0000313|EMBL:AFA52636.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMK753 {ECO:0000313|EMBL:AFA52636.1}; 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 RT lineage spanning necrotrophs, biotrophs, endophytes, host generalists RT and specialists."; RL PLoS ONE 7:E29943-E29943(2012). CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|SAAS:SAAS00564398}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. CC {ECO:0000256|RuleBase:RU361169, ECO:0000256|SAAS:SAAS00560517}. 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; JQ035920; AFA52636.1; -; Genomic_DNA. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR Gene3D; 2.160.20.10; -; 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 Pfam; PF00295; Glyco_hydro_28; 1. DR SMART; SM00710; PbH1; 6. DR SUPFAM; SSF51126; SSF51126; 1. DR PROSITE; PS00502; POLYGALACTURONASE; 1. PE 3: Inferred from homology; KW Cell wall biogenesis/degradation {ECO:0000256|SAAS:SAAS00055145}; KW Glycosidase {ECO:0000256|RuleBase:RU361169, KW ECO:0000256|SAAS:SAAS00054963}; KW Hydrolase {ECO:0000256|RuleBase:RU361169, KW ECO:0000256|SAAS:SAAS00485328}; KW Secreted {ECO:0000256|SAAS:SAAS00078733}. FT ACT_SITE 205 205 {ECO:0000256|PROSITE-ProRule:PRU10052}. FT NON_TER 1 1 {ECO:0000313|EMBL:AFA52636.1}. FT NON_TER 310 310 {ECO:0000313|EMBL:AFA52636.1}. SQ SEQUENCE 310 AA; 31349 MW; 2C7A1AA010347C04 CRC64; KRATTCTFSG SGGASSASKS KTSCSTIILS ALAVPSGTTL DLTGLTKGTT VIFEGITTFG YEEWSGPLVS VSGTDITVTQ TTGAYLDGGG ASYWDGDGSN GGKTKPKFFY AHSLISSTIE NLYFLNPPVQ VMSINSATDL TVSGVTINAQ DGDTGSLGAN TDGFDIGSST TVTITGANVY NQDDCVAINS GTGITFSGGV CSGGHGLSIG SVGGRDDNIV ETVLFENSEI KASQNGIRIK TISGDTGTVS GITYSGITLS GITDYGIVVN QAYDGTSGEP TNGVAISKFI LENISGTVES TATNILVECG //