ID A0A0A2KNU9_PENIT Unreviewed; 798 AA.
AC A0A0A2KNU9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Pectin lyase fold/virulence factor {ECO:0000313|EMBL:KGO69522.1};
GN ORFNames=PITC_014120 {ECO:0000313|EMBL:KGO69522.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO69522.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO69522.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO69522.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:KGO69522.1}.
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DR EMBL; JQGA01001137; KGO69522.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2KNU9; -.
DR STRING; 40296.A0A0A2KNU9; -.
DR HOGENOM; CLU_002540_1_0_1; -.
DR OMA; AYIENFW; -.
DR OrthoDB; 3714838at2759; -.
DR PhylomeDB; A0A0A2KNU9; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR InterPro; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR039279; QRT3-like.
DR PANTHER; PTHR33928:SF2; PECTATE LYASE SUPERFAMILY PROTEIN DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR33928; POLYGALACTURONASE QRT3; 1.
DR Pfam; PF12708; Pectate_lyase_3; 2.
DR SUPFAM; SSF51126; Pectin lyase-like; 2.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:KGO69522.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 72..309
FT /note="Pectate lyase superfamily protein"
FT /evidence="ECO:0000259|Pfam:PF12708"
FT DOMAIN 427..488
FT /note="Pectate lyase superfamily protein"
FT /evidence="ECO:0000259|Pfam:PF12708"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 798 AA; 86213 MW; 47894D36857C1A90 CRC64;
MASSSKMTHD TSPQASAPTP SPMSQKDHSP VKNVCAVPSN KSPETYWFDA QDHNQQGAGF
APYAKTSLYP VYRNVMDYSV VNDGSGDQTP KLQKAIDDDG VGGSRKGQGV TRYPAQVYLP
GGVYQLESTL NLTVGTIIVG NPLNPPIIKA APGFRGDYLI MGYDSHNGNP ETSFLTLVKN
VILDTTALMP DRQVTALQWG VAQGSGLTNV KIRMPKNSSG HTGIAINAGS TIAVTDVVSN
PEKPKERKKK RPNKVKDIIG GAIGIKNSNQ QVNFKNIYFE SCRTAFSAAG GWTVLLQQAT
FESCGTGIDM TANALGSLVL LDSTSTNTGP VVRFHDSSRD FGNRNSQFLI QNLKHDTSNA
IAVDAQGNVA LAATSFIDTW VWGTVAPETY QTGASWKTKR PADLLVGDKY FTKAQPTYQD
YSAADIINVK TVSGHTVKGD GNTDDTKSLN AILAENADSC KIIYIPFGVY RVSDTIFVPV
GTRIVGEAWS VISGYGDKFK DSDNPRPVVQ LGNPGDVGVI EIQDMRFSVG EILPGAKIIE
INAAGDQPGD VGLWNTMAMV GGTADTSISG ACTSQDPKDC MAAFMVMHLT ESSSAYIENF
WGWTADHNLD SESLLTIIST GRGILVESTK GTWLTGTGSE HHWLYNYNFH NAQNVFAGLL
QTETPYMQGQ GEYQAAPAPW TAVAKYGDPD FSWCAAEDQK CRTAIATNVD GGSNIALYNS
AAWAFFDGYW NGLYNEPCNG NCQTNMMRVT NDPHNLVWYS ISTRMTDVMV LDGKSNPRES
DHKGGWEAII QVYGQFTA
//
