ID   LAP1_METAQ              Reviewed;         393 AA.
AC   E9DUF4;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Leucine aminopeptidase 1;
DE            EC=3.4.11.-;
DE   AltName: Full=Leucyl aminopeptidase 1;
DE            Short=LAP1;
DE   Flags: Precursor;
GN   Name=LAP1; ORFNames=MAC_01252;
OS   Metarhizium acridum (strain CQMa 102).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655827;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQMa 102;
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., Pei Y., Feng M.-G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
CC   -!- FUNCTION: Extracellular aminopeptidase that allows assimilation of
CC       proteinaceous substrates. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28E subfamily.
CC       {ECO:0000305}.
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DR   EMBL; GL698474; EFY92616.1; -; Genomic_DNA.
DR   RefSeq; XP_007807592.1; XM_007809401.1.
DR   AlphaFoldDB; E9DUF4; -.
DR   SMR; E9DUF4; -.
DR   STRING; 92637.XP_007807592.1; -.
DR   EnsemblFungi; EFY92616; EFY92616; MAC_01252.
DR   GeneID; 19245563; -.
DR   KEGG; maw:MAC_01252; -.
DR   eggNOG; KOG2195; Eukaryota.
DR   HOGENOM; CLU_025866_0_0_1; -.
DR   InParanoid; E9DUF4; -.
DR   OMA; QNFMDIT; -.
DR   OrthoDB; 1257666at2759; -.
DR   Proteomes; UP000002499; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147; PTHR12147; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW   Protease; Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..84
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000412415"
FT   CHAIN           85..393
FT                   /note="Leucine aminopeptidase 1"
FT                   /id="PRO_0000412416"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         241
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         350
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        317..321
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   393 AA;  43528 MW;  C6CD559BEC42E014 CRC64;
     MRLSQVSVLA ACVPAAMARF VELMEANNVV LGPDEPAFLI ETAPGKTQWV TEEQKWELRR
     DGQRFMDVTA TQDLGSQGLR IKESVEFPKK CVNQKEVNSL AKHLDTAPMK ANLEKLSSFH
     TRYYNSDWGL KSSDWVLKKV NEIIKEAGAD KTVTAQSFPH TWKQHSVIAT IPGQTNSTII
     IGAHQDSINL WLPILAAPGA DDDGSGTVTI MEVFRALLKS KDVVGGKAIN TIEFHWYSAE
     EGGLLGSQAI FQQYEKQQRD VKAMLQQDMT GYIKGTLDAD LPESVGVIVD YVHAGLTKFI
     KTVIEQYCAI PWVETKCGYA CSDHASASKA GYPSAFVIES SFDKSDPNIH TTSDLIEYLS
     FDHMLQHGHM TLGFVHELGF HNFAKTVEGE SEL