ID   ECM14_ASPFN             Reviewed;         604 AA.
AC   B8NBP9;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Inactive metallocarboxypeptidase ecm14 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ecm14; ORFNames=AFLA_046240;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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 482 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; EQ963476; EED52922.1; -; Genomic_DNA.
DR   RefSeq; XP_002378086.1; XM_002378045.1.
DR   AlphaFoldDB; B8NBP9; -.
DR   SMR; B8NBP9; -.
DR   STRING; 5059.CADAFLAP00005951; -.
DR   EnsemblFungi; EED52922; EED52922; AFLA_046240.
DR   VEuPathDB; FungiDB:AFLA_046240; -.
DR   eggNOG; KOG2650; Eukaryota.
DR   HOGENOM; CLU_019326_1_0_1; -.
DR   OMA; SACEGNV; -.
DR   Proteomes; UP000001875; 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   Gene3D; 3.30.70.340; -; 1.
DR   InterPro; IPR036990; M14A-like_propep.
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..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..169
FT                   /evidence="ECO:0000250|UniProtKB:P38836"
FT                   /id="PRO_0000453236"
FT   CHAIN           170..604
FT                   /note="Inactive metallocarboxypeptidase ecm14"
FT                   /id="PRO_0000411177"
FT   REGION          542..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..569
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         260..263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         260
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         263
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         335..336
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         392
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         393..394
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   CARBOHYD        376
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        329..352
FT                   /evidence="ECO:0000250|UniProtKB:P15085"
SQ   SEQUENCE   604 AA;  68117 MW;  F3C4371DED1A9E71 CRC64;
     MRYLFLIILV AFAALTTAVP AGSSITPPPP IEPVQLLSPQ SSDVRRPWTR VRDWIIETVW
     GLPKPTSYRL PFNHLSHDQS APSRVQARYG SDVVLRFRLR NDKEAEALEQ ATEILFLDVW
     ASTSDFVDVR LAEEVIPSLL GLLPDSLRTA YSPLIDNLPE LIYTTYPTRR PIGLEGQPGF
     RPSVRQSAQL GDLFFQDYQP LSVIVPWMRL MASMFPSHVR MINVGISYEG REIPALRLGA
     GSNRAQSAPR RTIVMVGGSH AREWISTSTV TYVASNLISN FGKSRAVTRL LEDFDVVLVP
     TINPDGYVYT WEVDRLWRKS RQRTSLRFCP GIDLDRSWNF EWDGERTRSN PCSENYAGDE
     PFEGVEAAQF AQWALNETQN NNVDIVGFLD LHSYSQQVLY PFSFSCSSVP PTLETLEELA
     MGFAKVIRQT THEIYDVTSA CEGTVTATDK ASAKTFFPVS GGGSALDWFY HQLHASFAYQ
     IKLRDRGSYG FLIPSEYIVP TGKEIYNVVL KMGEFLVKET ASPANKADIN WGADLLVHDD
     STRTSSSESV SDPLSEANID STSTVKATPL PFPEDTLDSE WVPFDQNEEE NEEEQNWELR
     RRRR