LAP5_TRIVH
ID LAP5_TRIVH Reviewed; 357 AA.
AC P0CH60; D4D4Y0;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Probable leucine aminopeptidase TRV_02148.1;
DE EC=3.4.11.-;
DE AltName: Full=Leucyl aminopeptidase TRV_02148.1;
DE Flags: Precursor;
GN ORFNames=TRV_02148.1;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EFE43096.1; Type=Erroneous gene model prediction; Note=The predicted gene TRV_02148 has been split into 2 genes: TRV_02148.1 and TRV_02148.2.; Evidence={ECO:0000305};
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DR EMBL; ACYE01000114; EFE43096.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; P0CH60; -.
DR SMR; P0CH60; -.
DR EnsemblFungi; EFE43096; EFE43096; TRV_02148.
DR HOGENOM; CLU_366463_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..15
FT /evidence="ECO:0000255"
FT CHAIN 16..357
FT /note="Probable leucine aminopeptidase TRV_02148.1"
FT /id="PRO_0000397776"
FT REGION 169..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 291..295
FT /evidence="ECO:0000250"
SQ SEQUENCE 357 AA; 38516 MW; DBEE5EDDE03916B8 CRC64;
MKVLAALALS ALAMAKPTPP MPGMSLVQTG PQETRWVTAK EKHDMVMNHI GFFDITNRPE
SASIASKPKS YAFPGNVSHQ AEVKPLLEKI SADHIKSNLE MFSSYPNRYY DAQSGVESAQ
WVMEQAQAVV GNIQGAKVEM VKHDWMQPSI RAIIPGKSEK IVAVGAHQDS INGKNPQGEA
PGADDNGSGS MTILEALTAL VSDQKIAGGE AANTLEFHWY AGEEEGLLGS QDIFQQYSQE
GKEVVAMLNQ DMTGYGETMG VITDNSDPNL TKFTKMILDT YTSAKYSDSE CGYACSDHAS
ANKAGFPSAF VYEAVVGQDN PAIHSPDDTI EKLDPAKMAE HAKLVVGFAY ELAFATL
