DPEP1_COCP7
ID DPEP1_COCP7 Reviewed; 444 AA.
AC C5PCZ0;
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=Putative dipeptidase CPC735_015490;
DE EC=3.4.13.19 {ECO:0000255|PROSITE-ProRule:PRU10073};
DE Flags: Precursor;
GN ORFNames=CPC735_015490;
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: Hydrolyzes a wide range of dipeptides. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid;
CC Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869,
CC ChEBI:CHEBI:77460; EC=3.4.13.19; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10073};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10073};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Peptidase M19 family. {ECO:0000255|PROSITE-ProRule:PRU10073}.
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DR EMBL; ACFW01000043; EER24951.1; -; Genomic_DNA.
DR RefSeq; XP_003067096.1; XM_003067050.1.
DR AlphaFoldDB; C5PCZ0; -.
DR SMR; C5PCZ0; -.
DR EnsemblFungi; EER24951; EER24951; CPC735_015490.
DR GeneID; 9692567; -.
DR KEGG; cpw:CPC735_015490; -.
DR VEuPathDB; FungiDB:CPC735_015490; -.
DR HOGENOM; CLU_031404_4_2_1; -.
DR Proteomes; UP000009084; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01301; rDP_like; 1.
DR InterPro; IPR000180; Dipep_AS.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR008257; Pept_M19.
DR PANTHER; PTHR10443; PTHR10443; 1.
DR Pfam; PF01244; Peptidase_M19; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS00869; RENAL_DIPEPTIDASE_1; 1.
DR PROSITE; PS51365; RENAL_DIPEPTIDASE_2; 1.
PE 3: Inferred from homology;
KW Dipeptidase; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Signal; Zinc.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..444
FT /note="Putative dipeptidase CPC735_015490"
FT /id="PRO_0000411213"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 118..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
SQ SEQUENCE 444 AA; 49351 MW; 139F0A86FA3F1B87 CRC64;
MSQRTEHNGS WLRNAGSLLS VLACVAVLAS PASATPASAA AAAAPRTDDY LKRAERILKF
TPLIDGHNDL PNFIRKTTKN QIYEGKIPFE DELPGHTDLK RLRKGRVGGQ FWSVYTPCPD
PPVPIDNPTW SVRDTLEQID VTKRLIEKYS RDLQFCGDAR CARRAFRRGK IASFLGIEGG
HQIGNSLGDL RRVYELGVRY ITVTHNCDNA FATAQSTVAD GLPDTGLMKP FGIEFVKEMN
RLGMLVDLSH VSANTMRDTL KVARAPVIFS HSSAYAVSNH LRNVPDDVLK EVAKNNGVVM
VTFVSRFVNV ENPDAADINT VVDHIFHIAK VAGWDHVGIG GDYDGTVYLP KGLEDVSKYP
HLIARVLERG ATTQQVRKLV GENILRVWTE VERIAKRLQK TELPNEAYWE GRNWTRPAKR
DLNADFEGRS VPLFTSASNG DFCD
