ID AMPP2_ARTGP Reviewed; 487 AA.
AC E4V1Q7;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Probable Xaa-Pro aminopeptidase MGYG_06974;
DE EC=3.4.11.9;
DE AltName: Full=Aminoacylproline aminopeptidase;
DE AltName: Full=Prolidase;
GN ORFNames=MGYG_06974;
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893;
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS989827; EFR03972.1; -; Genomic_DNA.
DR RefSeq; XP_003170980.1; XM_003170932.1.
DR AlphaFoldDB; E4V1Q7; -.
DR SMR; E4V1Q7; -.
DR STRING; 535722.E4V1Q7; -.
DR GeneID; 10026223; -.
DR VEuPathDB; FungiDB:MGYG_06974; -.
DR eggNOG; KOG2737; Eukaryota.
DR HOGENOM; CLU_017266_1_2_1; -.
DR InParanoid; E4V1Q7; -.
DR OMA; YELRMIR; -.
DR OrthoDB; 1377484at2759; -.
DR Proteomes; UP000002669; 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 CDD; cd01087; Prolidase; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 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 PANTHER; PTHR43226; XAA-PRO AMINOPEPTIDASE 3; 1.
DR PANTHER; PTHR43226:SF3; XAA-PRO AMINOPEPTIDASE AN0832-RELATED; 1.
DR Pfam; PF05195; AMP_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SMART; SM01011; AMP_N; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 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..487
FT /note="Probable Xaa-Pro aminopeptidase MGYG_06974"
FT /id="PRO_0000411821"
FT BINDING 255
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 414
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 487 AA; 54153 MW; 26603AF49D997F29 CRC64;
MASYSIILSV GGTSINKYPG KQHARRVAAY LPKHQGLIYL PGQQTVLSED SDQARPFKQR
RYFFYVTGVV EPDCHVTYDI AEDKLTLYVP DFDFKRTIWT GPTLGKDEAS QRHVEYYSSL
EGDVQRWSQG NPSSPIYILH PDQRPVTPLT VAYLYESKSL KHAMDACRVI KDEHEVQLIQ
RANRVSGAAH RSILANLRHF KNEAQIAGLF IDVCLSLRSK GTAYETIAGS GSNGATLHYT
RNNEPLAGRQ MVVLDAGAEW SCYASDVTRS FPIPSSVRGG GDWPSREAEQ IYTIVQRMQE
ECISRVKEGA LFFSIHQHAH AVALEELLKL GILRIPRGST KADLIKAEAT ALFFPHGLGH
HLGLEVHDVS PDSGTIPLDL AIACQNGLMS VTEHRPPCTL SAPPLASGMV ITVEPGLYFN
RLAINQAREE RDKPDSKGRF VNFDVVERYV DVGGVRIEDD VLVTKNGNRN LTDAPKGREM
LDLIYGR
//
