ID   P20D1_COCP7             Reviewed;         452 AA.
AC   C5PE42;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Probable carboxypeptidase CPC735_001200;
DE            EC=3.4.17.-;
DE   AltName: Full=Peptidase M20 domain-containing protein CPC735_001200;
DE   Flags: Precursor;
GN   ORFNames=CPC735_001200;
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR   EMBL; ACFW01000044; EER24775.1; -; Genomic_DNA.
DR   RefSeq; XP_003066920.1; XM_003066874.1.
DR   AlphaFoldDB; C5PE42; -.
DR   SMR; C5PE42; -.
DR   EnsemblFungi; EER24775; EER24775; CPC735_001200.
DR   GeneID; 9692345; -.
DR   KEGG; cpw:CPC735_001200; -.
DR   VEuPathDB; FungiDB:CPC735_001200; -.
DR   HOGENOM; CLU_021802_3_0_1; -.
DR   Proteomes; UP000009084; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Protease; Secreted; Signal; Zinc.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..452
FT                   /note="Probable carboxypeptidase CPC735_001200"
FT                   /id="PRO_0000411233"
FT   ACT_SITE        205
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   452 AA;  48334 MW;  4EA8E85DB611F612 CRC64;
     MRVFTLAPLA LLPLVLARPS QRSSSPQKPI MADNGDLVMI PEGHEKSNLD EIIASSKLLS
     LHRSLSQIES ISNNEGSVGD FLVEYLERHG FTVQKQAVPL DGHEVDEEER KPSRFNVYAY
     PASSPSPEII LTSHIDTVPP YIPYSLSLPP TASTGSSSID RRAIHISGRG TVDAKASVAC
     QIIATLSHLE SNPDTPLGLL FVVSEETGGQ GMHHFSNSPL NTSPPTFHTV IFGEPTESKL
     VSGHKGMLHF DVHVRGKPAH SGYPWLGRSA VSEILPILSK VDSLGDIPES EGGLPSSEKY
     GKTTLNIGVM EGGVATNVVP ASASARVAVR LAGGTVTHAK ETILAAVRSA SKNPEDVHVS
     FSAGGAYPPV DLDSDVEGFD VMTVNYGTDV PNWDIHDHDL PDHGKVKRYL YGPGSIFVAH
     GENEGLSVGD MEDAVEGYAR LIRAAVGRSE RK