ID A0A0A2JML0_PENEN Unreviewed; 658 AA.
AC A0A0A2JML0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Dipeptidyl-peptidase V {ECO:0000256|ARBA:ARBA00032829};
GN ORFNames=PEX2_061330 {ECO:0000313|EMBL:KGO53525.1};
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:KGO53525.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO53525.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO53525.1,
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 -!- SIMILARITY: Belongs to the peptidase S9C family.
CC {ECO:0000256|ARBA:ARBA00010040}.
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:KGO53525.1}.
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DR EMBL; JQFZ01000250; KGO53525.1; -; Genomic_DNA.
DR RefSeq; XP_016596127.1; XM_016743404.1.
DR AlphaFoldDB; A0A0A2JML0; -.
DR STRING; 27334.A0A0A2JML0; -.
DR GeneID; 27678824; -.
DR HOGENOM; CLU_008615_2_0_1; -.
DR OrthoDB; 2877590at2759; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:0072330; P:monocarboxylic acid biosynthetic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR42776:SF27; DIPEPTIDYL PEPTIDASE FAMILY MEMBER 6; 1.
DR PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR Pfam; PF07676; PD40; 2.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 439..657
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 658 AA; 72799 MW; AAEF7DA3188B6C66 CRC64;
MVTNPDHKVN LSLEALADLQ VPSDLCISPD ATRIAYKLRP FSKKDENATS SIWIAEVGKE
KSTRQFTSGL CNDELPQWSP DGTSLAFKSD RGHPGKGSTV YVMSVNGGEA YPITPVDDEK
PITAFEWSPD GAYIAFTSAD EKTTEQVRKE EEQDDATVWG ENLEHHRLKV AHIATRQVQT
IVSGDKHVHD FSWSPDSKQI IYIEHKDPDV NSAGFYGAKI CIVSLFGIKS SVVTKFPGPI
YQVAWGNSGI YFIAGVNPKH WATSLSLYQL DYQNGSYTEQ ESEESCCDSI QKNQSSLAYH
VQNNLHDEIL SIDGGNHTLI HRGEYDIASF DVSRTAKNTV IAITKGDGSN PEEVFSVTES
EGIVKLSDHN SSIAALEISK TFSISATASD GYSLDGVIYV PSKYKAEDGP LPTVLLPHGG
PYWRVNIGFS VCHCLEVPPL VSAGYAVLCP NYRGGSGRGE KHAAYSRGGM GKFDYTDCID
ILRNCIDKGL VDSSRVAIGG WPNGGFLSYL AVTRDDFQFR AAVCGAGIVD WDVMTMTSDA
YWLDIDLTGG APWDVDVNAV PDGTDLKSSK KWLRDTTGRW GSPLWHMRNV KTPVLIVHGE
NDVRVPLSQA IAFYRACIHN DLAVDMVTYP REGHFITERK HVIDMWKRMR RFYDMHLQ
//
