LAP2_TRIVH
ID LAP2_TRIVH Reviewed; 495 AA.
AC D4D3D1;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Probable leucine aminopeptidase 2;
DE EC=3.4.11.-;
DE AltName: Full=Leucyl aminopeptidase 2;
DE Short=LAP2;
DE Flags: Precursor;
GN Name=LAP2; ORFNames=TRV_01590;
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: Extracellular aminopeptidase that releases a wide variety of
CC amino acids from natural peptides and contributes to pathogenicity.
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P80561};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P80561};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC {ECO:0000305}.
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DR EMBL; ACYE01000083; EFE43629.1; -; Genomic_DNA.
DR RefSeq; XP_003024240.1; XM_003024194.1.
DR AlphaFoldDB; D4D3D1; -.
DR SMR; D4D3D1; -.
DR EnsemblFungi; EFE43629; EFE43629; TRV_01590.
DR GeneID; 9579360; -.
DR KEGG; tve:TRV_01590; -.
DR HOGENOM; CLU_024336_0_2_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 CDD; cd03876; M28_SGAP_like; 1.
DR InterPro; IPR029514; Ape3.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR041756; M28_SGAP-like.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR PANTHER; PTHR12147:SF17; PTHR12147:SF17; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Secreted; Signal; Virulence; Zinc.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..495
FT /note="Probable leucine aminopeptidase 2"
FT /id="PRO_0000397770"
FT DOMAIN 130..216
FT /note="PA"
FT ACT_SITE 303
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT SITE 429
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 495 AA; 53241 MW; E91475B895C8537D CRC64;
MKSQLLSLAV AVTTISQGVV GQEPFGWPFK PMVTQDDLQN KIKLKDIMAG VEKLQSISDA
HPEKNRVFGG NGHKDTVEWI YNEIKATGYY DVKKQEQVHL WSHAEATVSA NGKDLKASAM
SYSPPASKIM AELVVAKNNG CNATDYPENT QGKIVLVERG VCSFGEKSSQ AGDAKAAGAI
VYNNVPGSLA GTLGGLDKRH VPTAGLSQED GKNLATLIAS GKVDVTMNVI SLFENRTTWN
VIAETKGGDH NNVIMLGAHS DSVDAGPGIN DNGSGSIGIM TVAKALTNFK LNNAVRFAWW
TAEEFGLLGS TFYVNSLDDR ELHKVKLYLN FDMIGSPNFA NQIYDGDGSA YNMTGPAGSA
EIEYLFEKFF DDQGIPHQPT AFTGRSDYSA FIKRNVPAGG LFTGAEVVKT PEQVKLFGGE
AGVAYDKNYH GKGDTVANIN KGAIFLNTRA IAYSVAEYAR SLKGFPTRPK TGKRDVNPQY
SKMPGGGCGH HTVFM
