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AMPP1_NEUCR
ID   AMPP1_NEUCR             Reviewed;         684 AA.
AC   Q7RYL6;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Probable Xaa-Pro aminopeptidase P;
DE            Short=AMPP;
DE            Short=Aminopeptidase P;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase;
DE   AltName: Full=Prolidase;
GN   Name=ampp; ORFNames=NCU00112;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002238; EAA28000.2; -; Genomic_DNA.
DR   RefSeq; XP_957236.2; XM_952143.2.
DR   AlphaFoldDB; Q7RYL6; -.
DR   SMR; Q7RYL6; -.
DR   STRING; 5141.EFNCRP00000000161; -.
DR   MEROPS; M24.A10; -.
DR   PRIDE; Q7RYL6; -.
DR   EnsemblFungi; EAA28000; EAA28000; NCU00112.
DR   GeneID; 3873358; -.
DR   KEGG; ncr:NCU00112; -.
DR   VEuPathDB; FungiDB:NCU00112; -.
DR   HOGENOM; CLU_011781_2_2_1; -.
DR   InParanoid; Q7RYL6; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd01085; APP; 1.
DR   Gene3D; 3.40.350.10; -; 2.
DR   Gene3D; 3.90.230.10; -; 1.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000587; Creatinase_N.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR033740; Pept_M24B.
DR   InterPro; IPR032416; Peptidase_M24_C.
DR   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR   Pfam; PF01321; Creatinase_N; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   Pfam; PF16188; Peptidase_M24_C; 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; Reference proteome.
FT   CHAIN           1..684
FT                   /note="Probable Xaa-Pro aminopeptidase P"
FT                   /id="PRO_0000411799"
FT   BINDING         481
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         492
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         492
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         590
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         604
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         604
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   684 AA;  75615 MW;  EF1065880CE25558 CRC64;
     MRSFWSFPSS CLTAVASSVP RPASRSQAAR VLHNLPRALT AFPQPSRTTR AFSLTSRLFQ
     HLRAASDEET MTVNTTDRLA ALRSLMKERN VDIYVVPSED SHASEYIAEC DARRAFISGF
     TGSAGTAVVT LDKAALATDG RYFNQASKQL DENWHLLKTG LQDVPTWQEW TADESAGGKS
     VGIDPTLISP AVADKLDGDI KKHGGAGLKA INENLVDLVW GDSRPPRPSE PVFLLGAKYS
     GKGTAEKLTN LRKELEKKKA AAFVVSMLDE VAWLFNLRGN DITYNPVFFS YAIVTKDSAT
     LYVDESKLND EVKQYLAENG TGIKPYNDLF KDTEILANAA KSTSESDKPT KYLVSNKASW
     ALKLALGGEK HVDEVRSPIG DAKAIKNETE LEGMRRCHIR DGAALIKYFA WLEDQLINKK
     AKLDEVEAAD QLEQFRSEQA DFVGLSFDTI SSTGPNGAII HYKPERGACS VIDPDAIYLC
     DSGAQFCDGT TDVTRTLHFG QPTDAERKSY TLVLKGNIAL DTAVFPKGTS GFALDALARQ
     FLWKYGLDYR HGTGHGVGSF LNVHEGPIGI GTRKAYIDVP LAPGNVLSIE PGYYEDGNYG
     IRIENLAIVR EVKTEHQFGD KPYLGFEHVT MVPYCRKLID ESLLTQEEKD WLNKSNEEIR
     KNMAGYFDGD QLTTEWLLRE TSPF
 
 
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