ID   F1S1E7_PIG              Unreviewed;       519 AA.
AC   F1S1E7;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 3.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=Dihydropyrimidinase {ECO:0000313|EMBL:HDA43711.1, ECO:0000313|EMBL:HDB34768.1, ECO:0000313|Ensembl:ENSSSCP00000043882.1};
GN   Name=DPYS {ECO:0000313|Ensembl:ENSSSCP00000043882.1,
GN   ECO:0000313|VGNC:VGNC:87429};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|EMBL:HDB34768.1};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000043882.1, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000043882.1,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:HDB34768.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30723633; DOI=.7717/peerj.6374;
RA   Gilbert D.G.;
RT   "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL   PeerJ 7:E6374-E6374(2019).
RN   [3] {ECO:0000313|Ensembl:ENSSSCP00000043882.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two divalent
CC       metal cations. {ECO:0000256|PIRSR:PIRSR611778-50}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Hydantoinase/dihydropyrimidinase family.
CC       {ECO:0000256|ARBA:ARBA00008829}.
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DR   EMBL; DQIR01088235; HDA43711.1; -; Transcribed_RNA.
DR   EMBL; DQIR01088514; HDA43990.1; -; Transcribed_RNA.
DR   EMBL; DQIR01089366; HDA44842.1; -; Transcribed_RNA.
DR   EMBL; DQIR01179291; HDB34768.1; -; Transcribed_RNA.
DR   EMBL; DQIR01181343; HDB36820.1; -; Transcribed_RNA.
DR   RefSeq; XP_001925286.2; XM_001925251.4.
DR   RefSeq; XP_013852012.1; XM_013996558.1.
DR   STRING; 9823.ENSSSCP00000043882; -.
DR   PaxDb; 9823-ENSSSCP00000006453; -.
DR   Ensembl; ENSSSCT00000037104.2; ENSSSCP00000043882.1; ENSSSCG00000006040.5.
DR   GeneID; 100156500; -.
DR   KEGG; ssc:100156500; -.
DR   CTD; 1807; -.
DR   VGNC; VGNC:87429; DPYS.
DR   eggNOG; KOG2584; Eukaryota.
DR   GeneTree; ENSGT01030000234527; -.
DR   HOGENOM; CLU_015572_2_2_1; -.
DR   OMA; SAETHHM; -.
DR   OrthoDB; 1772494at2759; -.
DR   Reactome; R-SSC-73621; Pyrimidine catabolism.
DR   Proteomes; UP000008227; Chromosome 4.
DR   Bgee; ENSSSCG00000006040; Expressed in metanephros cortex and 19 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004157; F:dihydropyrimidinase activity; IBA:GO_Central.
DR   GO; GO:0051219; F:phosphoprotein binding; IEA:Ensembl.
DR   GO; GO:0006248; P:CMP catabolic process; IEA:Ensembl.
DR   GO; GO:0006249; P:dCMP catabolic process; IEA:Ensembl.
DR   GO; GO:0046079; P:dUMP catabolic process; IEA:Ensembl.
DR   GO; GO:0006208; P:pyrimidine nucleobase catabolic process; IBA:GO_Central.
DR   GO; GO:0046050; P:UMP catabolic process; IEA:Ensembl.
DR   GO; GO:0006212; P:uracil catabolic process; IEA:Ensembl.
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:SF50; DIHYDROPYRIMIDINASE; 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   1: Evidence at protein level;
KW   Proteomics identification {ECO:0007829|PeptideAtlas:F1S1E7};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT   DOMAIN          58..447
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   REGION          483..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         159
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611778-50"
SQ   SEQUENCE   519 AA;  56752 MW;  7BFF8B8A5885F768 CRC64;
     MAAPSRLLIR GGRVVNDDSS QVADVLVEDG VVRALGRDLL PPGGAPAGLR VLDAAGKLVL
     PGGIDTHTHM QFPFMGSRSV DDFHQGTKAA LAGGTTMIID FAIPHKGHSL VEAFETWRSW
     ADSKVCCDYS LHVAVTWWSD QVKEEMKILT QEKGVNSFKM FMAYKDLYML RDVELYTVFS
     WCKEIGAIAQ VHAENGDLIA EGAKKMLALG ITGPEGHELC RPEAVEAEAT LRAITIASAV
     NCPLYVVHVM SKSAARVIAD ARRDGKVVYG EPIAAGLGTD GTHYWNRDWH HAAHHVMGPP
     LRPDPSTPDF LLNLLANDDL TTTGSDHCTF NTCQKALGKD DFTKIPNGVN GVEDRMSVIW
     EKAVHSGKMD ENRFVAVTST NAAKIFNLYP RKGRIAVGSD ADIVIWDPKA TRTISAKTHH
     QAVNFNIFEG MVCHGVPLVT ISRGRVVYEA GVFTVTAGHG KFIPRKPFAD YIYKRIKQRD
     ETCAPTPVER EPYKGEVVTL KSRGTEDDST AGTSKQAHH
//