ID   ECM14_TRIVH             Reviewed;         596 AA.
AC   D4DIW7;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Inactive metallocarboxypeptidase ECM14 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ECM14; ORFNames=TRV_07128;
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: Inactive carboxypeptidase that may play a role in cell wall
CC       organization and biogenesis. {ECO:0000250|UniProtKB:P38836}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P00730};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730};
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250|UniProtKB:P38836}. Secreted
CC       {ECO:0000250|UniProtKB:P38836}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC   -!- CAUTION: Lacks the conserved Glu residue in position 512 essential for
CC       carbopeptidase activity. The mature form lacks catalytic activity
CC       towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}.
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DR   EMBL; ACYE01000415; EFE38215.1; -; Genomic_DNA.
DR   RefSeq; XP_003018860.1; XM_003018814.1.
DR   AlphaFoldDB; D4DIW7; -.
DR   SMR; D4DIW7; -.
DR   EnsemblFungi; EFE38215; EFE38215; TRV_07128.
DR   GeneID; 9581504; -.
DR   KEGG; tve:TRV_07128; -.
DR   HOGENOM; CLU_019326_1_0_1; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR000834; Peptidase_M14.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW   Metal-binding; Secreted; Signal; Vacuole; Zinc.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..184
FT                   /evidence="ECO:0000250|UniProtKB:P38836"
FT                   /id="PRO_0000453253"
FT   CHAIN           185..596
FT                   /note="Inactive metallocarboxypeptidase ECM14"
FT                   /id="PRO_0000411192"
FT   REGION          181..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..210
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         285..288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         285
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         288
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         343
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         360..361
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         417
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         418..419
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   CARBOHYD        370
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        354..377
FT                   /evidence="ECO:0000250|UniProtKB:P15085"
SQ   SEQUENCE   596 AA;  66596 MW;  209CE2DBF708C4F5 CRC64;
     MHFSVRLSLF LTLASSLPLV SAVPQHEDQA YTFSSSGRSA TTDTDPALDV RQETLRTPSA
     WTRLRDSLVE SVWGLPQRSE GCESRPRNRA KTVSRAPATL QARYGEDVVL RFTIKNQEEV
     KALVEASNIL FLDVWGSHDD WVDIRLSRDV IPSLLGLLPP SLQTSHVPLI RDLAQTIYES
     YPKAGSAPPS QQGPTTRRFS PSASTSKSKP HEAKNIFFQD YQPLSVLLPW MRLLVSMFSS
     HTTLISVGTT AEGRDIPALR VGVHPTNNAQ QAPRRRTIVI SGGTHAREWI SVSTVSYIAY
     SFITGYGKSK SITKLLEQFD YVFIPTVNPD GYAYTFSTDR LWRKNRQQTS LSFCPGIDLD
     HSWGYEWDGN ATRSNPCSES YAGDQPFEAV EAREIASWAR NEVTVNNVHF VAFVDLHSYS
     QQILYPYGHS CAHLPANLEN LEELGAGLAK AIRKSSRENY DVKAACRGIV ASCTGDKDAD
     EPVTSSALER TAGSALDWFF HDLDVRFSYQ IKLRDRGSYG FLLPREHIVP TGKEIYRAMV
     AMGKFLVSPH VLEEDIDGLR ASEEPQDYDN DLEDGEDDKD EQDSTVFRAQ ADDLQS