ID   ECM14_COCP7             Reviewed;         582 AA.
AC   C5PHW9;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Inactive metallocarboxypeptidase ECM14 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ECM14; ORFNames=CPC735_054920;
OS   Coccidioides posadasii (strain C735) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=222929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C735;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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 488 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; ACFW01000049; EER24122.1; -; Genomic_DNA.
DR   RefSeq; XP_003066267.1; XM_003066221.1.
DR   AlphaFoldDB; C5PHW9; -.
DR   SMR; C5PHW9; -.
DR   EnsemblFungi; EER24122; EER24122; CPC735_054920.
DR   GeneID; 9691737; -.
DR   KEGG; cpw:CPC735_054920; -.
DR   VEuPathDB; FungiDB:CPC735_054920; -.
DR   HOGENOM; CLU_019326_1_0_1; -.
DR   Proteomes; UP000009084; 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.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW   Metal-binding; Secreted; Signal; Vacuole; Zinc.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..172
FT                   /evidence="ECO:0000250|UniProtKB:P38836"
FT                   /id="PRO_0000453241"
FT   CHAIN           173..582
FT                   /note="Inactive metallocarboxypeptidase ECM14"
FT                   /id="PRO_0000411181"
FT   REGION          561..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         265..268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         265
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         268
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         323
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         340..341
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         397
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         398..399
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        387
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        571
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        334..357
FT                   /evidence="ECO:0000250|UniProtKB:P15085"
SQ   SEQUENCE   582 AA;  65614 MW;  DB2BF7976B337B05 CRC64;
     MHILQVITGA TLVSVPFVSA IPSSTSEFLP STAEQNSAVL HSQGRSPPRL WTRLRDSIIE
     TIWRVPSRQH NPSRIPSSLS IPRAPSSIRA RYGDDVVLRF TIRSQNDVQA LIEASNILFL
     DIWASTNEWV DIRLAKDVVS SLLGLLPSSL RTAHVPIIHD LAQAVYESYP QPVSSVPNPH
     HAFSPSVQQS SETQNIFFQD YQPLSVIIPW MRLLASMFST HVRLVNLGTS YEGREIVGFR
     IGVRPANADL PTERRKTIVI TGGSHAREWI GVSTVNYVAY SLITGYGKSR AITKLVEEFD
     WVLIPTMNPD GYVYTWETDR LWRKNRQENN LQFCPGVDLD RTWGYEWDGS DSRSNPCSED
     FAGDGPFGGR ESKVIAQWAL NETNHHNVTF VGFLDLHSYS QQILYPYSYS CTNIPPTLEN
     LEELAIGIAK AIRLTDHEHY DVSSACEGSV SSHKKRRGAA LRSMQSAGGS ALDWFYHDLH
     VRYAYQLKLR DKGGYGFLLP KKNIVPTGKE VYNAVLVFGQ FLLGRGAQDI DWEGDFQFPA
     HSRPNVPEKE YRGPDEEYEI SNQLEDDDNE NDTLLGFRTQ KV