ID   ECM14_TALMQ             Reviewed;         595 AA.
AC   B6Q972;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Inactive metallocarboxypeptidase ecm14 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ecm14; ORFNames=PMAA_071100;
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(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 493 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; DS995900; EEA26026.1; -; Genomic_DNA.
DR   RefSeq; XP_002146573.1; XM_002146537.1.
DR   AlphaFoldDB; B6Q972; -.
DR   SMR; B6Q972; -.
DR   STRING; 441960.B6Q972; -.
DR   EnsemblFungi; EEA26026; EEA26026; PMAA_071100.
DR   GeneID; 7024244; -.
DR   KEGG; tmf:PMAA_071100; -.
DR   VEuPathDB; FungiDB:PMAA_071100; -.
DR   HOGENOM; CLU_019326_1_0_1; -.
DR   OrthoDB; 524270at2759; -.
DR   PhylomeDB; B6Q972; -.
DR   Proteomes; UP000001294; 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.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 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..178
FT                   /evidence="ECO:0000250|UniProtKB:P38836"
FT                   /id="PRO_0000453250"
FT   CHAIN           179..595
FT                   /note="Inactive metallocarboxypeptidase ecm14"
FT                   /id="PRO_0000411189"
FT   BINDING         270..273
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         273
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         328
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         345..346
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         402
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         403..404
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   CARBOHYD        386
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        339..362
FT                   /evidence="ECO:0000250|UniProtKB:P15085"
SQ   SEQUENCE   595 AA;  67288 MW;  3EE827C76F75649E CRC64;
     MYRPDHVFVI LCAVFFTGQV TAVPAGTGIT HPHSPQLGPF EPVGFASQTQ TQLAPSRGPF
     TWLRDSVIER IWGIDKEKQS LSKPGPRPVP EKSWSRYGSD IVLRIEVHNA EEVEALAEAV
     NILFLDVWDS NENYVDIRLA KEVVPSLLGL LPQSLQKTHT LLIEDLSKMI YESQYPSRGF
     KHHKNDQTTR HTGFQSSDVG DLFFDNYQPF PVILQWMRLL VSMFPSHVQL INVGVTHEGR
     DIPAFRLGAR PSGDQNEEPR KTVMIVGGSH AREWISTSTV AYIAFQLITE FGNSPPITKL
     LEDFDWILVP TINPDGYVYS WDMDRLWRKN RQQTGLPFCP GIDLDRSWGY EWDGQGTRAN
     PCSESYAGNN AFDSMETRTI AEWAYNQTQN KQSDFVGFLD LHSYSQQILY PYSYSCSTVP
     PTLENLEELA FGIAKAIRMT NQETYVVKSA CEGVVTTEKG TGQRVSTNVE STGGSALDWF
     YHQLHAKYSY QIKLRDKGMY GFLLPPENIV PTGREIFNSV LVLGHFLLGE GANGLEWSFL
     SGSGSAAGKE DDSSRTFDRL FFDNNEEQLE KSADDRDYFS VVEEDVYQDE GWGLW