ID A0A3P8XJJ5_ESOLU Unreviewed; 511 AA.
AC A0A3P8XJJ5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Dihydropyrimidinase {ECO:0000313|Ensembl:ENSELUP00000004736.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000004736.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000004736.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000004736.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3P8XJJ5; -.
DR STRING; 8010.ENSELUP00000004736; -.
DR Ensembl; ENSELUT00000011844.2; ENSELUP00000004736.2; ENSELUG00000005860.2.
DR GeneTree; ENSGT01030000234527; -.
DR OrthoDB; 1772494at2759; -.
DR Proteomes; UP000265140; LG20.
DR Bgee; ENSELUG00000005860; Expressed in liver and 12 other cell types or tissues.
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: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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000265140}.
FT DOMAIN 54..443
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT MOD_RES 155
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611778-50"
SQ SEQUENCE 511 AA; 56411 MW; 7B5ADA04E4F76F7A CRC64;
MTNPSRIIIK GGKVVNEDCS VISDVYIENG RIVEVGLNLI VPAGVTVIDA TDKLVIPGGI
DTHTHMEFEF MGTKAVDDFY IGTKAALAGG TTMILDFVIP QRGTSLLEAY DRWRDTADNK
VCCDYSLHVA VTWWSDKVKK EMEILAKEKG VNSFKMFMAY KDMFMLKDHE LYAAFSQCKE
IGAIAQVHAE NGDLIAEGAK KMLSLGIRGP EGHELCRPEE VEAEATQRAI TIAHTVNCPL
YVVHVMSKSA AKVVSSARRN GRVVFGEPIA AGLGTDGTHY WHKDWSHAAQ FVMGPPLRPD
PSTPGYLMDL LANDDLSVTG TDNCTFSVCQ KALGKDDFTK IPNGVNGVED RMSVIWEKGV
HSGKMDENRF VAVTSSNAAK IFNFYPQKGR IAKGSDADVV VWDPKATRKV SAATHHQAVE
YNIFEGMECH GVPVVTISRG KVVYDKGQLK TKRGEGRFIP REPYAEFVYK RVNQREQVCQ
NIVPSCGRGK NVSFFIIGKN LSSYLMNLQV Q
//
