ID   ECM14_TALSN             Reviewed;         592 AA.
AC   B8M2K0;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Inactive metallocarboxypeptidase ecm14 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ecm14; ORFNames=TSTA_091520;
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
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 490 essential for
CC       carbopeptidase activity. The mature form lacks catalytic activity
CC       towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EQ962653; EED21911.1; -; Genomic_DNA.
DR   RefSeq; XP_002478874.1; XM_002478829.1.
DR   AlphaFoldDB; B8M2K0; -.
DR   SMR; B8M2K0; -.
DR   STRING; 441959.B8M2K0; -.
DR   PRIDE; B8M2K0; -.
DR   EnsemblFungi; EED21911; EED21911; TSTA_091520.
DR   GeneID; 8098538; -.
DR   VEuPathDB; FungiDB:TSTA_091520; -.
DR   eggNOG; KOG2650; Eukaryota.
DR   HOGENOM; CLU_019326_1_0_1; -.
DR   InParanoid; B8M2K0; -.
DR   OMA; SACEGNV; -.
DR   OrthoDB; 524270at2759; -.
DR   PhylomeDB; B8M2K0; -.
DR   Proteomes; UP000001745; 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; IPR003146; M14A_act_pep.
DR   InterPro; IPR000834; Peptidase_M14.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   Pfam; PF02244; Propep_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..175
FT                   /evidence="ECO:0000250|UniProtKB:P38836"
FT                   /id="PRO_0000453252"
FT   CHAIN           176..592
FT                   /note="Inactive metallocarboxypeptidase ecm14"
FT                   /id="PRO_0000411191"
FT   BINDING         267..270
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         267
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
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         325
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         342..343
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         399
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         400..401
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   CARBOHYD        383
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        548
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        336..359
FT                   /evidence="ECO:0000250|UniProtKB:P15085"
SQ   SEQUENCE   592 AA;  67243 MW;  8C87CA5FC2DC75EF CRC64;
     MYRQDHVFVV LCAVLLAGQV TAVPAGTGIN PHSPPLGPFE SVRFASQTQS QIASSRGPFT
     WLRDTVIERI WGIDKKHSNK VGSQPRPEKS WSRYGSDIVL RMEVHSTEEV EALADAVNIL
     FLDVWDSNEN YVDIRMAKEV VPSLLGLLPQ SLQKSHTLLI EDLSKAIYES RYPTRDYQRH
     TIDQTDCHTV PRPLDVADLF FDHYQPFNVI LQWMRLIVSM FPSHAQLVNV GVTHEGRDIP
     AFRLGVRSRD DEQEGPRKTI MIVGGSHARE WISTSTVAYI AFQLVTEFGN SVAITKLLED
     FDWVLVPTIN PDGYVYSWDM DRLWRKNRQP TGLPFCPGID LDRSWGYEWD GQGTRANPCS
     ESYAGNNPFD SIETRTIAEW AYNQTQDKRT DFIGFLDLHS YSQQILYPYS YSCSTVPPTL
     ENLEELAFGI AKAIRMTNQE AYAVKSACEG VVTTDKGNGQ RVSANVESTG GSALDWFYHQ
     LHAKYSYQIK LRDKGMYGFL LPPEHIVPTG REIFNSVLVL GHFLLGEDAN ALEWEFIPGS
     KSTSEQENGS SRTFDRLFFN MNEDELEKPG NDRDYSSVVE EDVYQDEGWG LW