AMPP2_NEUCR
ID AMPP2_NEUCR Reviewed; 468 AA.
AC A7UWH7; U9W5I3;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Probable Xaa-Pro aminopeptidase NCU11288;
DE EC=3.4.11.9;
DE AltName: Full=Aminoacylproline aminopeptidase;
DE AltName: Full=Prolidase;
GN ORFNames=NCU11288;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ESA43463.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ESA43464.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CM002238; ESA43463.1; ALT_INIT; Genomic_DNA.
DR EMBL; CM002238; ESA43464.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_011394002.1; XM_011395700.1.
DR RefSeq; XP_011394003.1; XM_011395701.1.
DR AlphaFoldDB; A7UWH7; -.
DR SMR; A7UWH7; -.
DR STRING; 5141.EFNCRP00000004637; -.
DR EnsemblFungi; ESA43463; ESA43463; NCU11288.
DR EnsemblFungi; ESA43464; ESA43464; NCU11288.
DR GeneID; 5847519; -.
DR KEGG; ncr:NCU11288; -.
DR HOGENOM; CLU_017266_1_2_1; -.
DR InParanoid; A7UWH7; -.
DR OMA; DQKFIYN; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
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..468
FT /note="Probable Xaa-Pro aminopeptidase NCU11288"
FT /id="PRO_0000411841"
FT BINDING 264
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 438
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 438
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 468 AA; 52536 MW; B56995F7E2CEF5B2 CRC64;
MTTTAARMDF ETTLKGKYPA KRHAQRVADY IRNKMPGASG VLYLEGRATK LLEDNDEAEP
FRQRRYFYYL TGCPLADCHY MYDLDADKST LFIPPIDPDS VIWSGLPVSV DEAKQRWDVD
DVKYTSDVNA TLAHVGSSKP KGSSVFALAN QVSDKVTFLE FDNKNFSILK EAIEVTRVVK
DEYELAIMAK ANEISSDGHK MVMQKVKHVQ NERELEAVFL GHCIAKGARN QAYHSIVASG
RAAATLHYVP NNADMAGKLN LLLDAGGEWD CYASDITRTF PINGKFTKES REIYDIVLKM
QNECIAALKE GVLWDDVHLL AHKIAIDGLL QIGILQGDKD EILESRTSVA FFPHGLGHYL
GMDTHDTGGN PNYADKDTMF RYLRVRGRLP AGSVITVEPG IYFCNFIIEP FLKDPKHSKY
INADVLEKYW DVGGVRIEDN LVITKDGTYN LTTAPKDPEE MEKIIQQS
