ID   A0A3Q3EQG8_9LABR        Unreviewed;       564 AA.
AC   A0A3Q3EQG8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Dihydropyrimidinase-related protein 5-like {ECO:0000313|Ensembl:ENSLBEP00000008432.1};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000008432.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000008432.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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; A0A3Q3EQG8; -.
DR   STRING; 56723.ENSLBEP00000008432; -.
DR   Ensembl; ENSLBET00000008854.1; ENSLBEP00000008432.1; ENSLBEG00000006483.1.
DR   GeneTree; ENSGT01030000234527; -.
DR   InParanoid; A0A3Q3EQG8; -.
DR   Proteomes; UP000261660; 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:SF58; DIHYDROPYRIMIDINASE-RELATED PROTEIN 5; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000261660}.
FT   DOMAIN          57..446
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   REGION          502..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   564 AA;  61173 MW;  2C5CE4C01EE8DA9F CRC64;
     MSSSSAMVRI LIKGGKVVND DCTQEADVYI ENGIIQQVGK ELMIPGGAKV IDASGKLVLP
     GGIDTSVHLE ESFMNATTAD DFYSGTKAAL AGGTTMVIGH VLPEKNESLL EAYENCRSSA
     DSKSCCDYAL HVGVTWWGPK VRAEMEKLVR EKGVNSFQMF MAYKDMFMLR DSELFQALQQ
     CKDIGAIARV HAENGELVAE GAKEALDLGI SGPEGIEISR PEELEAEATH RAITIANRAN
     CPIYLVNVSS IAAGDVVATA KMQGKVVHGE TTTAHSVLNG MQYYHQDWAH AAAHVTVPPL
     RLDPNTPNFL MSLLGNDTLN VLASDHRPFT VKQRAMGKDD FTKIPHGLPG IQDRMSVIWE
     RGVLGGKMDE NRFVAVTSSN AAKIYNLYPR KGRIIPGADA DVVVWDPEGS KTISVDNQVQ
     GGDVNLYEGL RCHGVPLVTI SRGHLVYENG TFTCAEGSGK FCPLRTFPDY LYKKMVQREK
     SQAVKAVERE PYTGEVVEVI NSGKRDLGAP DGDTPTRPCT RHGGQRDLHE SSFSLSGAQI
     DDNIPKRSSA RILAPPGGRS SGIW
//