ID A0A0D8XRU0_DICVI Unreviewed; 570 AA.
AC A0A0D8XRU0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Dihydropyrimidinase {ECO:0000313|EMBL:KJH47220.1};
GN ORFNames=DICVIV_06674 {ECO:0000313|EMBL:KJH47220.1};
OS Dictyocaulus viviparus (Bovine lungworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae; Dictyocaulus.
OX NCBI_TaxID=29172 {ECO:0000313|EMBL:KJH47220.1, ECO:0000313|Proteomes:UP000053766};
RN [1] {ECO:0000313|EMBL:KJH47220.1, ECO:0000313|Proteomes:UP000053766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HannoverDv2000 {ECO:0000313|EMBL:KJH47220.1,
RC ECO:0000313|Proteomes:UP000053766};
RA Mitreva M.;
RT "Draft genome of the bovine lungworm Dictyocaulus viviparus.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HannoverDv2000 {ECO:0000313|Proteomes:UP000053766};
RX PubMed=26856411; DOI=10.1038/srep20316;
RA McNulty S.N., Strube C., Rosa B.A., Martin J.C., Tyagi R., Choi Y.J.,
RA Wang Q., Hallsworth Pepin K., Zhang X., Ozersky P., Wilson R.K.,
RA Sternberg P.W., Gasser R.B., Mitreva M.;
RT "Dictyocaulus viviparus genome, variome and transcriptome elucidate
RT lungworm biology and support future intervention.";
RL Sci. Rep. 6:20316-20316(2016).
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; KN716316; KJH47220.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D8XRU0; -.
DR STRING; 29172.A0A0D8XRU0; -.
DR MEROPS; M38.973; -.
DR Proteomes; UP000053766; Unassembled WGS sequence.
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; 2.
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:SF1; COLLAPSIN RESPONSE MEDIATOR PROTEIN; 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:UP000053766}.
FT DOMAIN 50..502
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT MOD_RES 152
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611778-50"
SQ SEQUENCE 570 AA; 62965 MW; 4C6BBC938608B2E7 CRC64;
MALLIVNGTV VNEDAMFKAD VLIKDGIIID VGLSLKVEDD VEVLDANGKL VIPGGIDPHT
HMQLPFMGEV AVDDFYHGTR AALAGGTTMI IDFIIPTKES SPILAYNQWR KWADPKVCCD
YALSMAITSW NSTVQREMEQ LVKPEYGINS FKFFLAYSGM FMVSDEEFYQ GMLICSRLGA
LARVHAENGS VIAEKSRALL EQGVTGPEGH AQSRPEELEA EATNRACVMA SQANCPLYVV
HVMSRGAAEV IAHHRQKGNI VFGEPIVAGL AVDGSHYYDE DWSHAAQYVM SPPLSRDPST
PETLMDLLAA GELHLTGSDN CTFNCHQKLV GRYDFTKIPN GVNGVEDRMS LVWDRGVHSG
KIDPMRFVQI TSGELHLTGS DNCTFNCHQK LVGRYDFTKI PNGVNGVEDR MSLVWDRGVH
SGKIDPMRFV QITSSMAAKL FNIYPKKGRI AVGSDADIVI WNPMKNRTIS KDTHHHVVDY
NIFEGMVVHG VAETTISRGK IVWKNNILTV EAGYGRYVPL LPFAPVAFAT ISQRAKVMAP
KAVKRDDIIE MKLLKNHTVA INKFTIAKTP
//
