ID   LAP1_COCPS              Reviewed;         388 AA.
AC   E9DBV9;
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=CPSG_07311;
OS   Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=443226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 757 / Silveira;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Orbach M., Henn M.R., Cole G.T., Galgiani J., Gardner M.J.,
RA   Kirkland T.N., Taylor J.W., Young S.K., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA   Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Pearson M.,
RA   Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S., Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Coccidioides posadasii strain Silveira.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GL636498; EFW16261.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9DBV9; -.
DR   SMR; E9DBV9; -.
DR   STRING; 199306.XP_003069987.1; -.
DR   MEROPS; M28.022; -.
DR   EnsemblFungi; EFW16261; EFW16261; CPSG_07311.
DR   VEuPathDB; FungiDB:CPSG_07311; -.
DR   eggNOG; KOG2195; Eukaryota.
DR   HOGENOM; CLU_025866_0_0_1; -.
DR   Proteomes; UP000002497; 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; Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..88
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000412403"
FT   CHAIN           89..388
FT                   /note="Leucine aminopeptidase 1"
FT                   /id="PRO_0000412404"
FT   BINDING         188
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         273
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         355
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        322..326
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   388 AA;  42971 MW;  73FC3BF6C1D01E94 CRC64;
     MKSLSLLALA AIAPPAAVAA VVDHQVPFEN RPVQGLPEKF LIQLGPEQTR WVTEDEKWAL
     KMEGVNFFDI TAEPDRGFSV KSHERIQVSF PSEVKHQTEL APLLEQLSKD NMRQNLVHFT
     SFHTRYYKSE TGVQSATWLF EQVEEAIQDS GAAQHAVKVE RFEHSWGQFS IIATIPGRTN
     KTVVIGAHQD SINLFLPSIL PAPGADDDGS GTVTILEAFR VLLQSEAVQQ GNAANTIEFH
     WYSAEEAGLL GSQAIFSDYS KTGRDIKAML QQDMTGYVEG TTKAGEVESV GVITDFVDPG
     LTEFIKRVIT GYCTIPFVLT QCGYACSDHA SASRYGYPSA FVIESEFKRS NQRIHTTGDT
     VDLLSFDHML QHARMTLAFA YELAFAEL