ID   LAP4_TRIVH              Reviewed;         379 AA.
AC   D4DDS4;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Probable leucine aminopeptidase TRV_05286;
DE            EC=3.4.11.-;
DE   AltName: Full=Leucyl aminopeptidase TRV_05286;
DE   Flags: Precursor;
GN   ORFNames=TRV_05286;
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
CC   -!- FUNCTION: Probable extracellular aminopeptidase which contributes to
CC       pathogenicity. {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; ACYE01000271; EFE39991.1; -; Genomic_DNA.
DR   RefSeq; XP_003020609.1; XM_003020563.1.
DR   AlphaFoldDB; D4DDS4; -.
DR   SMR; D4DDS4; -.
DR   EnsemblFungi; EFE39991; EFE39991; TRV_05286.
DR   GeneID; 9577308; -.
DR   KEGG; tve:TRV_05286; -.
DR   HOGENOM; CLU_025866_0_0_1; -.
DR   Proteomes; UP000008383; 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; Secreted; Signal; Virulence; Zinc.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..379
FT                   /note="Probable leucine aminopeptidase TRV_05286"
FT                   /id="PRO_0000397774"
FT   BINDING         182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         201
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         201
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         240
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         267
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         345
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        226
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        312..316
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   379 AA;  41220 MW;  C368D9275F517734 CRC64;
     MKIATLAVVS AFAATAIAGP IRPDGVGNDK FLIELGPGET QWVTKQQKHE MRAYINSIYK
     AGQGFVDITD EFGTDFTTAE VVPANYPKSA LHAAVVNPMI AGLSKENLMR DLNTLVKFNN
     RYYESPTGVE SATWVFNEVQ KIIQASGVKG AKVEKFTNKF KQFNVIATIP GASKNTVIVG
     AHQDSINQKD PMKGRAPGAD DNGSGTVVVL EAFRNVLKSK AIQAANATNT LEFHWYAGEE
     GGLLGSNNIF KKYKADGRKV KAMLNQDLTG FTKKGNPEQF GLITDNTNAE LNEFCKTIVA
     KYAALKIVEA KCGYACSDHA SAHRNGFPSS FIAETNFRNT NPYLHTADDV IANLDFNHML
     EHAKVVVGFM GELAMTPNL