ID Q8NKE3_PENGR Unreviewed; 383 AA. AC Q8NKE3; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 22-FEB-2023, entry version 55. DE SubName: Full=Pectin lyase {ECO:0000313|EMBL:AAM23009.1}; GN Name=plg2 {ECO:0000313|EMBL:AAM23009.1}; OS Penicillium griseoroseum. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium. OX NCBI_TaxID=84562 {ECO:0000313|EMBL:AAM23009.1}; RN [1] {ECO:0000313|EMBL:AAM23009.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=17215898; DOI=10.1139/W06-070; RA Bazzolli D.S., Ribon A.O., de Queiroz M.V., de Araujo E.F.; RT "Molecular characterization and expression profile of pectin-lyase-encoding RT genes from Penicillium griseoroseum."; RL Can. J. Microbiol. 52:1070-1077(2006). CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613, CC ECO:0000256|RuleBase:RU361173}. CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family. CC {ECO:0000256|ARBA:ARBA00010980, ECO:0000256|RuleBase:RU361173}. 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; AF502280; AAM23009.1; -; Genomic_DNA. DR AlphaFoldDB; Q8NKE3; -. DR CAZy; PL1; Polysaccharide Lyase Family 1. DR BRENDA; 4.2.2.10; 7626. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0030570; F:pectate lyase activity; IEA:InterPro. DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW. DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1. DR InterPro; IPR002022; Pec_lyase. DR InterPro; IPR012334; Pectin_lyas_fold. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR InterPro; IPR045032; PEL. DR PANTHER; PTHR31683; PECTATE LYASE 18-RELATED; 1. DR PANTHER; PTHR31683:SF16; PECTIN LYASE A-RELATED; 1. DR Pfam; PF00544; Pectate_lyase_4; 1. DR SMART; SM00656; Amb_all; 1. DR SUPFAM; SSF51126; Pectin lyase-like; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, KW ECO:0000256|RuleBase:RU361173}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361173}; KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326, KW ECO:0000256|RuleBase:RU361173}; KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU361173}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..19 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 20..383 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004311286" FT DOMAIN 94..301 FT /note="Pectate lyase" FT /evidence="ECO:0000259|SMART:SM00656" FT REGION 304..329 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 315..329 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 383 AA; 40542 MW; ED23A1F7F1B8C12E CRC64; MKYAFVLTAI AAIASKVAAV GVSGTPEGFA SSATGGGNAT PVYPTSTDEL GSYLGDDEAR VIGLAKTFDF TDTEGSTTTS GCTPWGTGSA CQVAINKDDW CTNYEPDAAT TTVTYKNAGM LGITVGSNKS LIGEGTTGVI KGRGLRIVNG VKNVIVQNIA VTDINPQYVW GGDAITINQA DLVWLDHITT DLSHLDCSHW SSALRPGTEA DNRVSITNNY INGESDYSAT CDGHHYWNVY LDGSSDKVTF KGNYLYKTSG RAPKVQDNTY LHAVNNYWDE NSGHAFEIGT GGVPFLRRVT TSLNVNRGSS SHPPSRVPSS PPTPTPAPAP PLSVASCVVN VNGGTLDRHF RLTFWSVFKG ETLPLSAVAS TVPPWQPPAQ GNL //