ID   MCPAL_TRIVH             Reviewed;         422 AA.
AC   D4D675;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Metallocarboxypeptidase A-like protein TRV_02598;
DE            EC=3.4.17.-;
DE   Flags: Precursor;
GN   ORFNames=TRV_02598;
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 metalloprotease that contributes to
CC       pathogenicity. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR   EMBL; ACYE01000134; EFE42646.1; -; Genomic_DNA.
DR   RefSeq; XP_003023264.1; XM_003023218.1.
DR   AlphaFoldDB; D4D675; -.
DR   SMR; D4D675; -.
DR   MEROPS; M14.014; -.
DR   EnsemblFungi; EFE42646; EFE42646; TRV_02598.
DR   GeneID; 9583272; -.
DR   KEGG; tve:TRV_02598; -.
DR   HOGENOM; CLU_019326_1_1_1; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.340; -; 1.
DR   InterPro; IPR036990; M14A-like_propep.
DR   InterPro; IPR003146; M14A_act_pep.
DR   InterPro; IPR000834; Peptidase_M14.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   Pfam; PF02244; Propep_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Disulfide bond; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Secreted; Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..119
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000397756"
FT   CHAIN           120..422
FT                   /note="Metallocarboxypeptidase A-like protein TRV_02598"
FT                   /id="PRO_0000397757"
FT   ACT_SITE        387
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         185..188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         240
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         256..257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         311
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         312..313
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        250..273
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   422 AA;  46504 MW;  06403DF7081DE70A CRC64;
     MQSLLLLATL LGSALGGAIP SQSANYNGYK VMRVSGDDTS KISHIVSKLG LETWKFPKAA
     NANVDIVVPP KKVAEFEKMS HAAGLKKQVM HENLGDSIKS EMSFRPYSCE LLTLDGGAND
     TWFQSYHKYE DHLKFMQDFQ SAHSQNSEIV TSGKSHEGRD ITGVHVWGSG EKGSKPAVVF
     HGTVHAREWI TTMTVEYILA QLFDDKEAGA ALLEKFDFYI FPIANPDGFV FTTESDRMWR
     KNREQNEGGC YGTDLNRNWP YKWEGDGSTT DPCSETYRGP SPGFAPETKA STSFIKGLAD
     GAGVKMFVDW HSYSQLFMTP YGYSCSARAP NDDVLQEMAS SFADAVKAVH GTSFTTGPIC
     NTIYQANGNS VDWIVDEIKG ETAFAAELRD TGMYGFVLPP EQIIPSGEET WAGVKAMFSK
     LK