ID   A0A3B3C6N3_ORYME        Unreviewed;       552 AA.
AC   A0A3B3C6N3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Dihydropyrimidinase-related protein 1-like {ECO:0000313|Ensembl:ENSOMEP00000012963.1};
OS   Oryzias melastigma (Marine medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000012963.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000012963.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Hydantoinase/dihydropyrimidinase family.
CC       {ECO:0000256|ARBA:ARBA00008829}.
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DR   AlphaFoldDB; A0A3B3C6N3; -.
DR   Ensembl; ENSOMET00000020455.1; ENSOMEP00000012963.1; ENSOMEG00000014427.1.
DR   GeneTree; ENSGT01030000234527; -.
DR   OMA; IANRINC; -.
DR   Proteomes; UP000261560; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01314; D-HYD; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR02033; D-hydantoinase; 1.
DR   PANTHER; PTHR11647:SF54; DIHYDROPYRIMIDINASE-RELATED PROTEIN 1; 1.
DR   PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 2.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   3: Inferred from homology;
FT   DOMAIN          67..456
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   REGION          502..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..552
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   552 AA;  60271 MW;  0671CC5B782A6D0F CRC64;
     MSGISYQGNN GIPHYTGERL LIRGGRVVND DRSFFGDVYI EDGLIKQVGE NLVVPGGVKV
     IEANGRMVIP GGIDVNTCLM KTYLGTQPVD DFLQGTKAAL AGGTTMIIDH VTPEPGGSLL
     EAFERWQESA DKRACCDYSL HVDIPQWNES VKDELEVLVQ DKGINSFQVY MAYKDVYQMT
     DSQLYEAFSF LKQLGAVVLV HAENGDLIFE EQRKILGMGI TGPEGHPLSR PEEVEAEAVF
     RAITLGNRVN CPVYITKVMS KSAADTIAQA RRKGSVVFGE PITAGLATDG SHYWSKNWAK
     AAAYVTSPPL SPDPTTPEHL HTLLASGDLQ VVGSSHCAYS LSQKAIGKDD FTLIPEGTNG
     VEERMGFVWD KAVAMGKMDE NQFVAVTSTN AAKIFNLYPR KGRIAVDSDA DIVIWDPDIV
     KTITAKQQQS AAEYNIFEGL ECRGGPALVL SQGRVVYEGG KLHIQQGTGR FIPRKPFADY
     AFQRVKFRNQ VNIKQGVTRG VYDGPVHDVA PTPKYITPSP SAKTSPTSHQ PPPVRNLHLS
     NFSLSGMQSE TT
//