ID   LAP1_ASPFN              Reviewed;         387 AA.
AC   B8NYX1;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 56.
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=AFLA_114830;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963487; EED44781.1; -; Genomic_DNA.
DR   RefSeq; XP_002385536.1; XM_002385495.1.
DR   AlphaFoldDB; B8NYX1; -.
DR   SMR; B8NYX1; -.
DR   STRING; 5059.CADAFLAP00013401; -.
DR   MEROPS; M28.022; -.
DR   EnsemblFungi; EED44781; EED44781; AFLA_114830.
DR   VEuPathDB; FungiDB:AFLA_114830; -.
DR   eggNOG; KOG2195; Eukaryota.
DR   HOGENOM; CLU_025866_0_0_1; -.
DR   OMA; QNFMDIT; -.
DR   Proteomes; UP000001875; 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; IPR045175; M28_fam.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147; PTHR12147; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW   Protease; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..87
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000412390"
FT   CHAIN           88..387
FT                   /note="Leucine aminopeptidase 1"
FT                   /id="PRO_0000412391"
FT   BINDING         187
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         272
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         354
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        321..325
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   387 AA;  43148 MW;  A61A2B47BBC00A3A CRC64;
     MKIRAALALS ATASGVLAAV VPQQALLNNP QIHHENEKYL IELAPYQTRW VTEEEKWALK
     LDGVNFIDIT EERNPGFYPT LHQASNVRYP TKMEHVEEVV GLTHRLTKAN MERDLEKFTS
     FHTRYYKSQT GIESATWLYN QVQTVIEQSG AAEHGATVDR FAHSWGQFSI IARIPGKSNK
     TVVLGAHQDS INLFLPSILA APGADDDGSG TVTILEALRG LLQSDTVAQG KAPNTIEFHW
     YSAEEGGMLG SQAIFSQYKQ ERRDIKAMLQ QDMTGYVQGA LNAGRKEAVG IMIDYVDRGL
     TQFLKDVVTA YCNVGYLETK CGYACSDHTS ASKYGYPSAM ATEAEMENTN KRIHTTDDRI
     KYLSFDHMLE HAKLTLGFAY ELAFASF