ID   P20D1_TRIVH             Reviewed;         460 AA.
AC   D4D6R4;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Probable carboxypeptidase TRV_02791;
DE            EC=3.4.17.-;
DE   AltName: Full=Peptidase M20 domain-containing protein TRV_02791;
DE   Flags: Precursor;
GN   ORFNames=TRV_02791;
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR   EMBL; ACYE01000145; EFE42483.1; -; Genomic_DNA.
DR   RefSeq; XP_003023101.1; XM_003023055.1.
DR   AlphaFoldDB; D4D6R4; -.
DR   SMR; D4D6R4; -.
DR   EnsemblFungi; EFE42483; EFE42483; TRV_02791.
DR   GeneID; 9583121; -.
DR   KEGG; tve:TRV_02791; -.
DR   HOGENOM; CLU_021802_3_0_1; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Metal-binding; Protease; Secreted; Signal; Zinc.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..460
FT                   /note="Probable carboxypeptidase TRV_02791"
FT                   /id="PRO_0000411241"
FT   ACT_SITE        207
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        395
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   460 AA;  49832 MW;  0C81AD8143E4B83F CRC64;
     MQKTYLWALV SLLASSLVDA RSAVFDQTPL DIGGSDDSFD SIARIDPNSN DLLKSEMDKV
     IASSELLSLH RALVEIKSIS DNEQAVGGFL MDYLYSKNFT VEKQFVDYDD PTGKPIRTNR
     RFNIYAYPGN SASPGIILTS HIDTVPPFIP YSLSHPEPAS FKREDILISG RGTVDDKASV
     ACQVIAAMDH LEKHPDIPIG LLFVVSEEVG GRGMSTFSNS RLNSGTYHTI IFGEPTERAL
     VAGHKGMVSF TIRVHGKPAH SGYPWLGRSA VSEMLPILTE VDRLGDIPVS QGGLPSSEKY
     GRTTLNIGFM SGGVAANVVA EEAVANVAVR LAAGDPEDAK DIIFRAIRNA ATKHRKDATV
     VISNGLERPK GDIEVIFGLE AYGVVDIDAD VDGFNVTTVN YGTDIPHWKI YGDNVKRYLY
     GPGTIFVAHG KNEALTVGEL EAGLEGYKTL VAKAAERERS