ID   ECM14_ARTBC             Reviewed;         596 AA.
AC   D4AKU7;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Inactive metallocarboxypeptidase ECM14 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ECM14; ORFNames=ARB_04942;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
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; ABSU01000002; EFE36006.1; -; Genomic_DNA.
DR   RefSeq; XP_003016651.1; XM_003016605.1.
DR   AlphaFoldDB; D4AKU7; -.
DR   SMR; D4AKU7; -.
DR   STRING; 663331.D4AKU7; -.
DR   EnsemblFungi; EFE36006; EFE36006; ARB_04942.
DR   GeneID; 9522135; -.
DR   KEGG; abe:ARB_04942; -.
DR   eggNOG; KOG2650; Eukaryota.
DR   HOGENOM; CLU_019326_1_0_1; -.
DR   OMA; SACEGNV; -.
DR   Proteomes; UP000008866; 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; Reference proteome; 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_0000453232"
FT   CHAIN           185..596
FT                   /note="Inactive metallocarboxypeptidase ECM14"
FT                   /id="PRO_0000411173"
FT   REGION          182..211
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   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;  66460 MW;  24C51996F4DF6E73 CRC64;
     MHFSVRLSLF LTLASSLPLV SAVPQHEDQA YTFSSSGRSA ATDTDPALEV RQETQRTPSA
     WTRLRDSLVE SVWGLPQRSE GCESRPRNRA KTVSRAPATL QARYGEDVVL RFTIKNQEEV
     KALVEASNIL FLDVWGSHDD WVDIRLSRDV IPSLLGLLPP SLQTSHVPLI RDLAQTIYES
     YPKAGSASPS QQGPTTRRFS PSASTSKSKP HETKNIFFQD 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
     EPATSSALES TAGSALDWFF HDLDVRFSYQ IKLRDRGSYG FLLPREHIVP TGKEIYRAMV
     AMGKFLVSPH VLEEDIDGLR ASEEPQDYDN DLEDGEDDKD EQGSTVFRAQ ADDLQS