ID   LAP1_GROCL              Reviewed;         408 AA.
AC   F0X8C8;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 37.
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=CMQ_3959;
OS   Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS   (Graphiocladiella clavigera).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Grosmannia.
OX   NCBI_TaxID=655863;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=kw1407 / UAMH 11150;
RX   PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA   DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA   Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA   Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA   Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT   "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT   symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(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; GL629735; EFX05890.1; -; Genomic_DNA.
DR   RefSeq; XP_014175372.1; XM_014319897.1.
DR   AlphaFoldDB; F0X8C8; -.
DR   SMR; F0X8C8; -.
DR   STRING; 655863.F0X8C8; -.
DR   EnsemblFungi; EFX05890; EFX05890; CMQ_3959.
DR   GeneID; 25977116; -.
DR   eggNOG; KOG2195; Eukaryota.
DR   HOGENOM; CLU_025866_0_0_1; -.
DR   InParanoid; F0X8C8; -.
DR   OrthoDB; 1257666at2759; -.
DR   Proteomes; UP000007796; 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..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..89
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000412409"
FT   CHAIN           90..408
FT                   /note="Leucine aminopeptidase 1"
FT                   /id="PRO_0000412410"
FT   BINDING         190
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         209
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         209
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         248
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         275
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         357
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        324..328
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   408 AA;  44744 MW;  81D56F1FA27CBDDE CRC64;
     MKVSSAIALL LPVVAARFVD SAFEQDHVQL HPEQAAAEQF LIELSPGETR WVTEDEKWEL
     RRNGQRFMDI TDNRDLGLAS AQSATTGPAR VFPPNVTLDE EVFPLLANLS KGELQTHLEK
     LTSFHTRYYR SEHGRASSNW LLGQVKKTVG EAGGFKHGIT VKPFKHPWGQ NSVIARIPGQ
     TNRTIVVGAH QDSINLFLPS VLSAPGADDD GSGTVTILEA LRVLLQSEAV LAGKAANTIE
     FHWYSAEEGG LLGSQAIFNT YEKASRDVRA MLQQDMTGFV QRTLDAGEVE SVGVIVDYVD
     PGLTAFIKKV ITAYCDIPFI ETKCGYACSD HASASKAGYP SAFVIESAFE RSDDHIHTSD
     DLIKYLSFDH MLQHARLTLA FVYELAFADF DKLDKAAAVS VAPEMGDL