ID   AMPP2_TRIVH             Reviewed;         507 AA.
AC   D4D6B8;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Probable Xaa-Pro aminopeptidase TRV_02643;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase;
DE   AltName: Full=Prolidase;
GN   ORFNames=TRV_02643;
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(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; ACYE01000137; EFE42609.1; -; Genomic_DNA.
DR   RefSeq; XP_003023227.1; XM_003023181.1.
DR   AlphaFoldDB; D4D6B8; -.
DR   SMR; D4D6B8; -.
DR   EnsemblFungi; EFE42609; EFE42609; TRV_02643.
DR   GeneID; 9583246; -.
DR   KEGG; tve:TRV_02643; -.
DR   HOGENOM; CLU_017266_1_2_1; -.
DR   Proteomes; UP000008383; 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   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
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.
DR   PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW   Protease.
FT   CHAIN           1..507
FT                   /note="Probable Xaa-Pro aminopeptidase TRV_02643"
FT                   /id="PRO_0000411854"
FT   BINDING         275
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         286
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         286
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         434
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         478
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         478
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   507 AA;  56310 MW;  0FF207101B29CDB6 CRC64;
     MASYSVTVSV AGTSINKYPA GSAGFDLAMA DSYDPGKQHA RRVAAYLPKQ QGLIYLPGQQ
     TVLSEDSDQD RPFKQRRYFF YVTGVVEPDC HVTYDIAEDK LTLYVPDFDF KRTIWTGPTL
     GKDEANQRYD VDRVEYFSAL EGDVLRWSQA NPSLSIYILH PDQRPVTPLT VAYFYESKSL
     KHAMDACRVI KDEHEIQLIQ RANRVSGAAH RSILANLHHF KNEAQIAGLF IDVCLSLRSK
     GTAYQTIAGS GSNGATLHYT RNNEPLAGRQ MVVLDAGAEW SCYASDVTRS FPIPSSVSGG
     RDWPSREAEQ IYAIVQRMQE ECISRVKEGA LFFSIHQHAH AIALEELLKL GILRIPQGST
     KADLIKAEVT ALFFPHGLGH HLGLEVHDVS PDSGTIPVEL AIEREKGLMS VTEHRPPCTL
     SAPPLASGMV ITVEPGLYFN RLAIDQARAE RDEPNSKGRF VNFDVVERYV DVGGVRIEDD
     VLVTKDGNKN LTDAPKGKEM LDLIYGR