ID   AMPP2_FUSV7             Reviewed;         462 AA.
AC   C7Z837;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Probable Xaa-Pro aminopeptidase NECHADRAFT_60613;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase;
DE   AltName: Full=Prolidase;
GN   ORFNames=NECHADRAFT_60613;
OS   Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL
OS   45880 / 77-13-4) (Fusarium solani subsp. pisi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex; Fusarium vanettenii.
OX   NCBI_TaxID=660122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4;
RX   PubMed=19714214; DOI=10.1371/journal.pgen.1000618;
RA   Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C.,
RA   Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C.,
RA   Freitag M., Ma L.-J., Danchin E.G.J., Henrissat B., Coutinho P.M.,
RA   Nelson D.R., Straney D., Napoli C.A., Barker B.M., Gribskov M., Rep M.,
RA   Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L.,
RA   Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E.,
RA   Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E.,
RA   VanEtten H.D.;
RT   "The genome of Nectria haematococca: contribution of supernumerary
RT   chromosomes to gene expansion.";
RL   PLoS Genet. 5:E1000618-E1000618(2009).
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}.
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; GG698911; EEU39803.1; -; Genomic_DNA.
DR   RefSeq; XP_003045516.1; XM_003045470.1.
DR   AlphaFoldDB; C7Z837; -.
DR   SMR; C7Z837; -.
DR   STRING; 140110.NechaP60613; -.
DR   EnsemblFungi; NechaT60613; NechaP60613; NechaG60613.
DR   GeneID; 9672417; -.
DR   KEGG; nhe:NECHADRAFT_60613; -.
DR   eggNOG; KOG2737; Eukaryota.
DR   HOGENOM; CLU_017266_1_2_1; -.
DR   InParanoid; C7Z837; -.
DR   OMA; DQKFIYN; -.
DR   OrthoDB; 352329at2759; -.
DR   Proteomes; UP000005206; Unassembled WGS sequence.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
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; IPR007865; Aminopep_P_N.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000994; Pept_M24.
DR   Pfam; PF05195; AMP_N; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   SMART; SM01011; AMP_N; 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..462
FT                   /note="Probable Xaa-Pro aminopeptidase NECHADRAFT_60613"
FT                   /id="PRO_0000411839"
FT   BINDING         259
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         270
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         270
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         393
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         433
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         433
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   462 AA;  51879 MW;  45DFA9BBD9E30C18 CRC64;
     MVAEDFEAVL KAKYPSKSHA KRVVDLIREK IPNANGILYL ESRMTKLLED NDEPEPFRQR
     RFFYYLTGCN LPDCYYIYDI QSSKSILFIP PIDPDSVIWS GLPLSIDEAL QKYDVDDVKL
     TSELNATLAH LGQANPQSTA YAIANQVSDH VTFLEFEKKN FDALKEAIEV SRVVKDEFEV
     AMIRKANHVS DIAHRAVLEK AKTAVNEREF EAAFLERCVA HGAKEMAYHP IAASGRAAAT
     LHYVTNESPL EGKLNLLMDA GAEWNNYAAD ITRTFPLSGK FSKESREIYE IVLKMQNDCI
     AVLKEGVLWD DVHLLAHKIA IDGLLSIGIL KGDKDEILKG RTSAAFLPHG LGHYLGMDTH
     DTGGNANYED KDKLFRYLRV RGNLPSGSVI TVEPGIYFCN FIIAPYLEDP VHSKFIDSAV
     LDKYWDVGGV RIEDNILITK DGYENLTITP KEVDEIETLV SN