LAP1_PHANO
ID LAP1_PHANO Reviewed; 389 AA.
AC Q0U6L1;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=SNOG_12603;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445347; EAT79901.1; -; Genomic_DNA.
DR RefSeq; XP_001802824.1; XM_001802772.1.
DR AlphaFoldDB; Q0U6L1; -.
DR SMR; Q0U6L1; -.
DR STRING; 13684.SNOT_12603; -.
DR MEROPS; M28.022; -.
DR EnsemblFungi; SNOT_12603; SNOT_12603; SNOG_12603.
DR GeneID; 5979735; -.
DR KEGG; pno:SNOG_12603; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_025866_0_0_1; -.
DR InParanoid; Q0U6L1; -.
DR OMA; IMSSHID; -.
DR OrthoDB; 1257666at2759; -.
DR Proteomes; UP000001055; 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; IBA:GO_Central.
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..18
FT /evidence="ECO:0000255"
FT PROPEP 19..89
FT /evidence="ECO:0000250"
FT /id="PRO_0000412438"
FT CHAIN 90..389
FT /note="Leucine aminopeptidase 1"
FT /id="PRO_0000412439"
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 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 322..326
FT /evidence="ECO:0000250"
SQ SEQUENCE 389 AA; 42895 MW; 2B67019D1C4BBEA0 CRC64;
MKSSVLLSLC TAALVAGAAH PLEPQVVLKD GQSTFTEPDE YLIELSPGET RWVTEEGKWE
LRRQNINFFD ITHHEDLGTI NANRLIEKSV KFPSKPAFNK TVVPLLKKLK KDNMRKHLET
FTSFHTRYYK SQYGAQSSAW LLEQVSKTLS DAGAVNASVK AFPHPWGQSS IIATLPGKSN
KTVVIGAHQD SINLFLPSIL AAPGADDDGS GTVTILEALR VLLKSEGILD GSAPNTVEFH
WYSAEEGGLL GSQAIFQSYE KEGRDVKAML QQDMTGYVQK TLDAGEPESV GVITDFVDPG
LTEFIKQIIT VYCDIPFILT KCGYACSDHA SASKAGYPSA FVIESDFKYS DSKIHTTEDK
IEYLSFDHML QHAKLTLALA YELAFAEFK
