ID A0A5N7EEK7_9EURO Unreviewed; 422 AA. AC A0A5N7EEK7; DT 22-APR-2020, integrated into UniProtKB/TrEMBL. DT 22-APR-2020, sequence version 1. DT 12-OCT-2022, entry version 7. DE RecName: Full=Dipeptidase {ECO:0000256|RuleBase:RU341113}; DE EC=3.4.13.19 {ECO:0000256|RuleBase:RU341113}; GN ORFNames=BDV36DRAFT_309925 {ECO:0000313|EMBL:KAE8416763.1}; OS Aspergillus pseudocaelatus. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=1825620 {ECO:0000313|EMBL:KAE8416763.1, ECO:0000313|Proteomes:UP000325395}; RN [1] {ECO:0000313|EMBL:KAE8416763.1, ECO:0000313|Proteomes:UP000325395} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 117616 {ECO:0000313|EMBL:KAE8416763.1, RC ECO:0000313|Proteomes:UP000325395}; RG DOE Joint Genome Institute; RA Mondo S., Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S., RA Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E., RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M., RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Riley R., RA Salamov A., Simmons B.A., Magnuson J.K., Henrissat B., Mortensen U.H., RA Larsen T.O., Devries R.P., Grigoriev I.V., Machida M., Baker S.E., RA Andersen M.R., Cantor M.N., Hua S.X.; RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases. 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; CC Evidence={ECO:0000256|RuleBase:RU341113}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|RuleBase:RU341113}; CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Peptidase M19 family. {ECO:0000256|RuleBase:RU341113}. 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; ML735747; KAE8416763.1; -; Genomic_DNA. DR Proteomes; UP000325395; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule. DR CDD; cd01301; rDP_like; 1. 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; PS51365; RENAL_DIPEPTIDASE_2; 1. PE 3: Inferred from homology; KW Dipeptidase {ECO:0000256|ARBA:ARBA00022997, ECO:0000256|RuleBase:RU341113}; KW Hydrolase {ECO:0000256|RuleBase:RU341113}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU341113}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, KW ECO:0000256|RuleBase:RU341113}; Protease {ECO:0000256|RuleBase:RU341113}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Zinc {ECO:0000256|RuleBase:RU341113}. FT TRANSMEM 28..45 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" SQ SEQUENCE 422 AA; 47274 MW; 936B14E767F47B55 CRC64; MTMDKKGDLE WMPLQVEPVH WGKRQRSLAY SVTLTLVALF LTFTLRPEAF PFFLARKSLQ ESPLEQVLTR VPLTDGHNDF AIWTRAFYQN HIYQANFTGH NELYGQVDFP RLRKGRLGAQ FWSVYVECAR NPNEPGAQYE IVRDTFQQID LVHRMIDHFP DFLVPASSVA DVHYNFYHSP ERISSLLGIE GLHQIGGSAS VLRMYHELGV RYASLTHTCH NEYADSEAPA EPRHDGLSAA GEAIVAEMNR VGMIVDLSHT SVATQRAVFN VSRAPVMYSH SSAYALCPHS RNVPDDLLQM LKENDGIVMI SLYPEYTNCH DADAASLADV ADHIQYVGNL IGYRHVGLGS DFDGMPHGPK GLEDVSKYPD LIQELLDRGV SVDDLVGVTG GNVLRVLGIV EHVARSLADK LPLEDDVKPF FE //