LAP1_AJECN
ID LAP1_AJECN Reviewed; 385 AA.
AC A6REE0;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 52.
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=HCAG_08005;
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC unclassified Histoplasma.
OX NCBI_TaxID=2059318;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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; CH476664; EDN04339.1; -; Genomic_DNA.
DR RefSeq; XP_001536896.1; XM_001536846.1.
DR AlphaFoldDB; A6REE0; -.
DR SMR; A6REE0; -.
DR STRING; 339724.A6REE0; -.
DR MEROPS; M28.022; -.
DR EnsemblFungi; EDN04339; EDN04339; HCAG_08005.
DR GeneID; 5443216; -.
DR KEGG; aje:HCAG_08005; -.
DR VEuPathDB; FungiDB:HCAG_08005; -.
DR HOGENOM; CLU_025866_0_0_1; -.
DR OMA; QNFMDIT; -.
DR OrthoDB; 1257666at2759; -.
DR Proteomes; UP000009297; 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..20
FT /evidence="ECO:0000255"
FT PROPEP 21..87
FT /evidence="ECO:0000250"
FT /id="PRO_0000412380"
FT CHAIN 88..385
FT /note="Leucine aminopeptidase 1"
FT /id="PRO_0000412381"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 319..323
FT /evidence="ECO:0000250"
SQ SEQUENCE 385 AA; 42429 MW; C6B3BE5AFFD9CE22 CRC64;
MKLPSLLSLG VAASTTIVAA VPDQKPIGDT IEDVHLGKFL IELGPGDTRW VTEEEKWGLR
RDGRRFFDIT AEAEQNVFPK TFAQTTVTFP SELQNVAHVK KLASSLSKNR LQTFLTKFTS
FHTRYYKSES GRQSAIWLFE QIEKIIQESS ATGARVEKFE HPWGQFSIIA TIPGQTNKTV
VVGAHQDSIN LLMPSILPAP GADDDGSGTA TILEALRILL KSEAVAQGKA PNTVEFHWYS
AEEAGLLGSQ AVFAQYKQDN RDVKSMLQQD MTGYSKGTMN AGHVDSVGII TDFVDEGLTN
FITKVVTGYC GISYVLTKCG YACSDHASAS RYGYPSAFVI ESKFEYSSKL IHTTRDEVSS
LDFDHMLQHA KMTLGLVYEL AFADL