ID   AMPP2_CHAGB             Reviewed;         595 AA.
AC   Q2HA12;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Probable Xaa-Pro aminopeptidase CHGG_02942;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase;
DE   AltName: Full=Prolidase;
GN   ORFNames=CHGG_02942;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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; CH408030; EAQ91007.1; -; Genomic_DNA.
DR   RefSeq; XP_001229458.1; XM_001229457.1.
DR   AlphaFoldDB; Q2HA12; -.
DR   SMR; Q2HA12; -.
DR   STRING; 38033.XP_001229458.1; -.
DR   EnsemblFungi; EAQ91007; EAQ91007; CHGG_02942.
DR   GeneID; 4389537; -.
DR   eggNOG; KOG2737; Eukaryota.
DR   HOGENOM; CLU_017266_1_2_1; -.
DR   InParanoid; Q2HA12; -.
DR   OMA; LHYGANN; -.
DR   OrthoDB; 352329at2759; -.
DR   Proteomes; UP000001056; 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; 2.
DR   PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome.
FT   CHAIN           1..595
FT                   /note="Probable Xaa-Pro aminopeptidase CHGG_02942"
FT                   /id="PRO_0000411831"
FT   REGION          51..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         334
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         345
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         345
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         541
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         563
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         563
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   595 AA;  65842 MW;  A512A4CE40F6463E CRC64;
     MEFCDESYDL VNIDEFDALW VASRHGVAFG VPPCLLISDD DAIARSSIEL KSGPSSSNLS
     PSTLSTEKTS SDSSGVICDP QLHETWREGL GKFPAKEHAR KVARELGADH GIIFLLGQDE
     KYYEDSDMGP TFRQRRYFYY ITGADFPGCA VTYDILRDKL VLWIPRIEPR TVLWFGKVPT
     PEECKAASDV DSVYYIDFLH EKQCPVFKRG QTIHVLHPDQ IPPELDHLGK FIRIDAVRLK
     PAMDAARVIK TDYEIALIRR ANAVSSAAHK AVLRNIKRFT NEREIDALFR GYCIAHGAPI
     QSYPVIAASG INASTLHYDD NNQSLKNRQL LILDAGAEVH CYASDITRTI PLPGSFTPLA
     REIYRLVERM QDECIAQIKP GVRFSALHAH ACAVAVTGLL KLGILRGEEE EILARGTVAA
     FFPHGLGHHV GLEVHDVSGT ERLLLNGGPG SGPGSGGGYG CGASTWRGYR LRRRVMTKRE
     SLTPWEVAAL WEGAKPEKEK QQERWLLNNV PLDEVEAALT LASSSGARGQ KLAPGMVVTV
     EPGIYFLPRV LEKYWNVGGV RIEDDILVTK KGYENLTTAP KGDEMMKCMG ESGLL