P20D1_COCPS
ID P20D1_COCPS Reviewed; 452 AA.
AC E9DG92;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Probable carboxypeptidase CPSG_08841;
DE EC=3.4.17.-;
DE AltName: Full=Peptidase M20 domain-containing protein CPSG_08841;
DE Flags: Precursor;
GN ORFNames=CPSG_08841;
OS Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=443226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 757 / Silveira;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Orbach M., Henn M.R., Cole G.T., Galgiani J., Gardner M.J.,
RA Kirkland T.N., Taylor J.W., Young S.K., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Pearson M.,
RA Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Coccidioides posadasii strain Silveira.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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; GL636505; EFW14583.1; -; Genomic_DNA.
DR AlphaFoldDB; E9DG92; -.
DR SMR; E9DG92; -.
DR STRING; 443226.E9DG92; -.
DR EnsemblFungi; EFW14583; EFW14583; CPSG_08841.
DR VEuPathDB; FungiDB:CPSG_08841; -.
DR eggNOG; KOG2275; Eukaryota.
DR HOGENOM; CLU_021802_3_0_1; -.
DR Proteomes; UP000002497; 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; Reference proteome; Secreted; Signal;
KW Zinc.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..452
FT /note="Probable carboxypeptidase CPSG_08841"
FT /id="PRO_0000411234"
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; 48336 MW; F71395A0E6D57A7A CRC64;
MRVFTLAPLA LLPLVLARPS QRSSSPQKPI MADNGDLVMI PEGHEKSNLD EIIASSELLS
LHRSLSEIES 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