ID   AMPP3_VERA1             Reviewed;         563 AA.
AC   C9SEV5;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Probable Xaa-Pro aminopeptidase PEPP;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase;
DE   AltName: Full=Prolidase;
GN   Name=PEPP; ORFNames=VDBG_02807;
OS   Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS   (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=526221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136;
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
CC   -!- FUNCTION: Catalyzes the removal of a penultimate prolyl residue from
CC       the N-termini of peptides. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of any N-terminal amino acid, including proline, that
CC         is linked to proline, even from a dipeptide or tripeptide.;
CC         EC=3.4.11.9;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR   EMBL; DS985216; EEY16698.1; -; Genomic_DNA.
DR   RefSeq; XP_003006668.1; XM_003006622.1.
DR   AlphaFoldDB; C9SEV5; -.
DR   SMR; C9SEV5; -.
DR   STRING; 526221.C9SEV5; -.
DR   EnsemblFungi; EEY16698; EEY16698; VDBG_02807.
DR   GeneID; 9532810; -.
DR   KEGG; val:VDBG_02807; -.
DR   eggNOG; KOG2737; Eukaryota.
DR   HOGENOM; CLU_017266_1_2_1; -.
DR   OMA; EPQATIN; -.
DR   Proteomes; UP000008698; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.350.10; -; 1.
DR   Gene3D; 3.90.230.10; -; 1.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000994; Pept_M24.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   SUPFAM; SSF53092; SSF53092; 1.
DR   SUPFAM; SSF55920; SSF55920; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome.
FT   CHAIN           1..563
FT                   /note="Probable Xaa-Pro aminopeptidase PEPP"
FT                   /id="PRO_0000411892"
FT   BINDING         331
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         342
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         342
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         491
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         532
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         532
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   563 AA;  60027 MW;  0BACEA0C22BA0697 CRC64;
     MASGDNVDYE AVMVDEFDAL NIEVRVSAGP SSSVPGAALS APRCPGMRAL PLKAPVMSTP
     VPAAAPLPTP PAVDDGPSAV GVGNVPPAVD DVPSAVDDVV IQKETTKYSA KLHAAKVADE
     LKASAGLVFL PGEPSRTYEY SDMGPAFSSN AATSSTSPAS TSLTPRKVLY NGRVPSIKDV
     LAASDVDEVR HMQDLPAFLH AYAHQHDKAT VYLLDASQSH PALVDNARVH IDTAALRPAM
     DEARVTKTAH EIALIREANA VSSAAHRAVM RHIRRFASER QVAALFTAEC TVRGAPTQAY
     APIAGSGPNA ATLHYGANDE PLAGRHVLVL DAGCEVNCYA SDVTRTLPLG PTGHFTPEAR
     HIYDLVERMQ EACVAAVAPG LLYYSLHLKA SAIALRGLLR LGILKGDEKA IWAAGTVAAF
     FPHGLGHHIG LETHDVTGRD RLLLAAGERE PRAKRDAVSA EMLVGLAAAV ATGPPYRGKQ
     MLRPGMVVTV EPGIYFNKDY IEGYFLREDK HRAFIDRDVL ARYYPVGGVR IEDCILVTDD
     GYENLTKAPK GEDMLRIIRG EAQ