ID A0A0A2JPD7_PENEN Unreviewed; 398 AA.
AC A0A0A2JPD7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Peptidase C13, legumain {ECO:0000313|EMBL:KGO54235.1};
GN ORFNames=PEX2_039390 {ECO:0000313|EMBL:KGO54235.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO54235.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO54235.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO54235.1,
RC ECO:0000313|Proteomes:UP000030143};
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 -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
CC -!- SIMILARITY: Belongs to the peptidase C13 family.
CC {ECO:0000256|ARBA:ARBA00009941}.
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:KGO54235.1}.
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DR EMBL; JQFZ01000230; KGO54235.1; -; Genomic_DNA.
DR RefSeq; XP_016596708.1; XM_016741214.1.
DR AlphaFoldDB; A0A0A2JPD7; -.
DR STRING; 27334.A0A0A2JPD7; -.
DR GeneID; 27676633; -.
DR HOGENOM; CLU_044656_2_2_1; -.
DR OrthoDB; 1122658at2759; -.
DR PhylomeDB; A0A0A2JPD7; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0042765; C:GPI-anchor transamidase complex; IEA:InterPro.
DR GO; GO:0003923; F:GPI-anchor transamidase activity; IEA:InterPro.
DR GO; GO:0016255; P:attachment of GPI anchor to protein; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1460; -; 1.
DR InterPro; IPR028361; GPI_transamidase.
DR InterPro; IPR001096; Peptidase_C13.
DR PANTHER; PTHR48067; GPI-ANCHOR TRANSAMIDASE; 1.
DR PANTHER; PTHR48067:SF1; GPI-ANCHOR TRANSAMIDASE; 1.
DR Pfam; PF01650; Peptidase_C13; 1.
DR PIRSF; PIRSF500138; GPI8; 1.
DR PIRSF; PIRSF019663; Legumain; 1.
DR PRINTS; PR00776; HEMOGLOBNASE.
PE 3: Inferred from homology;
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..398
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028399667"
FT ACT_SITE 146
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT ACT_SITE 188
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
SQ SEQUENCE 398 AA; 44462 MW; D6D300A595A1D8AF CRC64;
MALLFHFLQA FVLLLLASAV AAEHTSNWAV LVSTSRFWFN YRHLANVLSL YRTVKRLGIP
DSQIILMLPD DMACNPRNAF PGTVYSNADR AVDLYGDNIE VDYRGYEVTV ENFIRLLTDR
LDEDVPRSKR LGSDAGSNVL VYMTGHGGDQ FLKFQDAEEI GAWDLADAFG QMWEKKRYHE
LLFMIDTCQA NTMYTHFYSP NIVATGSSEI DQSSYSHHAD NDVGVAVIDR WTYYVLDFLE
TQVTSVTSKL NLGDLFDSYD ESKIHSQPGV RWDLFPGGEQ EGRLRTVVDF FGNVQNVEVE
NANATEPGSL KEDLAEIARL VEKWQRRDEE YSAILGGSSG NVTEDLHSSS LHLKLKNTVG
PTKMAEESSW GKQLVGISVV GACTAIWVAG SILGRSSV
//
