LAP1_AJECH
ID LAP1_AJECH Reviewed; 385 AA.
AC C6HH71;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 38.
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=HCDG_05552;
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143;
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) 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}.
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DR EMBL; GG692427; EER40155.1; -; Genomic_DNA.
DR AlphaFoldDB; C6HH71; -.
DR SMR; C6HH71; -.
DR STRING; 544712.C6HH71; -.
DR MEROPS; M28.022; -.
DR EnsemblFungi; EER40155; EER40155; HCDG_05552.
DR VEuPathDB; FungiDB:HCDG_05552; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_025866_0_0_1; -.
DR OMA; QNFMDIT; -.
DR Proteomes; UP000002624; 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..87
FT /evidence="ECO:0000250"
FT /id="PRO_0000412376"
FT CHAIN 88..385
FT /note="Leucine aminopeptidase 1"
FT /id="PRO_0000412377"
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; 42590 MW; A1149B3D62AB18F6 CRC64;
MKFPNLLSLG VAASTTVLAA VPNQKPIGDT IEDVHLGKFL IELGPGDTRW VTEEEKWGLR
RDGRRFFDIT AEAEQNVFPR TFAQTTVTFP TELQNLAHVK KLASSLSKNR LQTFLTKFTS
FYTRYYKSES GRQSAIWLFE QIEKTIQESS ATEARVEKFE HPWGQFSIIA TIPGQTNKTV
VVGAHQDSIN LLMPSILAAP GADDDGSGTA TILEALRVLL KSEAVAQGKA PNTVEFHWYS
AEEAGLLGSQ AVFAQYKQDN RDVKSMLQQD MTGYSKGTMN AGHADSVGII TDFVDEGLTN
FIKKVVTGYC GISYVLTKCG YACSDHASAS RYGYPSAFVI ESKFEYSSKL IHTTRDEVSS
LDFDHMLQHA KMTLGLVYEL AFADL