Q60Q85 (DHP1_CAEBR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydropyrimidinase 1
EC=3.5.2.2

Gene names

Name:	dhp-1
ORF Names:	CBG21922

Organism

Caenorhabditis briggsae

Taxonomic identifier

6238 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	489 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	5,6-dihydrouracil + H2O = 3-ureidopropanoate.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subunit structure	Homotetramer By similarity.
Subcellular location	Nucleus By similarity.
Post-translational modification	Carbamylation allows a single lysine to coordinate two zinc ions By similarity.
Sequence similarities	Belongs to the DHOase family. Hydantoinase/dihydropyrimidinase subfamily.

Ontologies

Keywords
Cellular component	Nucleus
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	pyrimidine base catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	dihydropyrimidinase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 489	489	Dihydropyrimidinase 1		PRO_0000165928
Sites
	Metal binding	61	1	Zinc 1 By similarity
	Metal binding	63	1	Zinc 1 By similarity
	Metal binding	156	1	Zinc 1; via carbamate group By similarity
	Metal binding	156	1	Zinc 2; via carbamate group By similarity
	Metal binding	189	1	Zinc 2 By similarity
	Metal binding	245	1	Zinc 2 By similarity
	Metal binding	323	1	Zinc 1 By similarity
	Binding site	161	1	Substrate By similarity
	Binding site	295	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	344	1	Substrate; via carbonyl oxygen By similarity
Amino acid modifications
	Modified residue	156	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q60Q85 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: 573FBF5DC04C545A	FASTA	489	53,528
	10 20 30 40 50 60 MSPPLVIKNG TVVNEDGMFK ADVLVKNGII VEVSPKIIAL PEMEIIDATD RLVIPGGIDP 70 80 90 100 110 120 HTHMQMPYAG EVTKDDFLRG TQAAVAGGTT MIIDFCCPDH RNGESLMAGY ARWRSWADPK 130 140 150 160 170 180 VCCDYGLSVA ITQWRPETAD QMAVITSPEF GVNSFKFYMA YEGTLMVRDD EMYRAMQECA 190 200 210 220 230 240 KLRALARVHA ENGSVIKERE IDLLAKGVTG PEGHTQSRPE EIEAEATNRA CVLAAQANCP 250 260 270 280 290 300 VYIVHVMTKG AAAAISHHRA QGSIVFGEPI AAGLALDGSH YYNEDWLHAA RYVMSPPLSR 310 320 330 340 350 360 DPTTPELLMK LLAAGELHLT GTDNCTYDGC QKSLGKGNFT KIPNGINGVE DRMSVVWEKG 370 380 390 400 410 420 VHSGIIDPMR YVSITSATAA KIFNIYPKKG RIAVGSDADI VIFNPNATRT ISAETHHHNL 430 440 450 460 470 480 DFNIFEGIKC HGVAEITISR GRIVWANGQL QTVPGSGKFV PLLANSPFVF SSHEIREKKK EPRIVERLE

References

[1]

"The genome sequence of Caenorhabditis briggsae: a platform for comparative genomics." Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., Hillier L.W. , Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M., Waterston R.H. PLoS Biol. 1:166-192(2003) [PubMed: 14624247] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AF16.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CAAC02000587 Genomic DNA. Translation: CAP38640.1.
RefSeq	XP_002629885.1. XM_002629839.1.
3D structure databases
ProteinModelPortal	Q60Q85.
SMR	Q60Q85. Positions 2-482.
ModBase	Search...
Protein-protein interaction databases
STRING	Q60Q85.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	8572900.
KEGG	cbr:CBG21922.
Organism-specific databases
CTD	8572900.
WormBase	CBG21922; CBP05205; WBGene00040591.
Phylogenomic databases
HOGENOM	HBG724623.
OMA	CTFNSTQ.
PhylomeDB	Q60Q85.
Family and domain databases
InterPro	IPR006680. Amidohydro_1. IPR011778. Hydantoinase/dihydroPyrase. IPR011059. Metal-dep_hydrolase_composite. [Graphical view]
Pfam	PF01979. Amidohydro_1. 1 hit. [Graphical view]
SUPFAM	SSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMs	TIGR02033. D-hydantoinase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DHP1_CAEBR

Accession

Primary (citable) accession number: Q60Q85
Secondary accession number(s): A8Y179

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	November 23, 2004
Last modified:	September 21, 2011
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project