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
