ID DPEP2_COCP7 Reviewed; 464 AA. AC C5PCN6; DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot. DT 01-SEP-2009, sequence version 1. DT 22-FEB-2023, entry version 59. DE RecName: Full=Putative dipeptidase CPC735_014430; DE EC=3.4.13.19 {ECO:0000255|PROSITE-ProRule:PRU10073}; GN ORFNames=CPC735_014430; 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; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10073}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Peptidase M19 family. {ECO:0000255|PROSITE-ProRule:PRU10073}. 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; ACFW01000043; EER24847.1; -; Genomic_DNA. DR RefSeq; XP_003066992.1; XM_003066946.1. DR AlphaFoldDB; C5PCN6; -. DR SMR; C5PCN6; -. DR GeneID; 9692463; -. DR KEGG; cpw:CPC735_014430; -. DR VEuPathDB; FungiDB:CPC735_014430; -. DR HOGENOM; CLU_031404_4_2_1; -. DR OrthoDB; 5476406at2759; -. DR Proteomes; UP000009084; Unassembled WGS sequence. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. 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 Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR InterPro; IPR000180; Dipep_AS. DR InterPro; IPR032466; Metal_Hydrolase. DR InterPro; IPR008257; Pept_M19. DR PANTHER; PTHR10443:SF12; DIPEPTIDASE; 1. DR PANTHER; PTHR10443; MICROSOMAL DIPEPTIDASE; 1. DR Pfam; PF01244; Peptidase_M19; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 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; Membrane; KW Metal-binding; Metalloprotease; Protease; Transmembrane; KW Transmembrane helix; Zinc. FT CHAIN 1..464 FT /note="Putative dipeptidase CPC735_014430" FT /id="PRO_0000411216" FT TRANSMEM 40..56 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 1..34 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 93 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 95 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 206 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 206 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 233 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073" FT BINDING 277 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 298 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 309 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073" FT BINDING 369 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073" FT CARBOHYD 382 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 145..235 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073" SQ SEQUENCE 464 AA; 51382 MW; 632DEA67DC973F69 CRC64; MSTMSARDNE KGSARSQPSH AAASEIENVP RPSRQQSWTG TMIKVFIICA CAGIVSKYII PLDSIFKSVH IDPHDYATRA NRILSTTPLI DGHNDLPYLI RLETKNKIYD HEKLPFRTGL LSHTDQIKIQ EGKLGGQFWS VFVECATDPN AEIDDPTWAV RDTLEQIDVT KRLVQEYPDL LEYCESASCA KAAFKRGKVG SFLGIEGGHQ IGNSLASLRQ VYDLGVRYIT VTHNCDNAFA TAASTVAVGK PDLGLTDFGR EFVKEMNRLG MLVDLSHVSH QTMRDILSVT KAPVMFSHSS SYALSKHLRN VPDDVLNGVT KNGGVVMVTF VPSFLKVDDP ASATIHDAVD HILHVAKVAG WDHVGIGSDF DGTADVPEGL ENVSKYPRLI ELLLERGVTD EQARKLIGEN ILRVWSNVEE IAENIRALGE KPNEETWSGR KWTAAIDIPM PFMFKDSADK RKEL //