Reviewed, UniProtKB/Swiss-Prot Q18677 (DHP2_CAEEL)

Names and origin

Protein names

Recommended name:
    Dihydropyrimidinase 2
    EC=3.5.2.2
Alternative name(s):
    CeCRMP/DHP-2
    UlipA

Gene names

Name:	dhp-2
ORF Names:	C47E12.8

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	5,6-dihydrouracil + H2O = 3-ureidopropanoate. Ref.1
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subunit structure	Homotetramer By similarity.
Tissue specificity	Body wall muscles. Ref.1
Developmental stage	All developmental stages. Ref.1
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
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Molecular function	dihydropyrimidinase activity Inferred from electronic annotation. Source: EC zinc 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 – 520	520	Dihydropyrimidinase 2		PRO_0000165931
Sites
	Metal binding	59	1	Zinc 1 By similarity
	Metal binding	61	1	Zinc 1 By similarity
	Metal binding	152	1	Zinc 1; via carbamate group By similarity
	Metal binding	152	1	Zinc 2; via carbamate group By similarity
	Metal binding	185	1	Zinc 2 By similarity
	Metal binding	241	1	Zinc 2 By similarity
	Metal binding	319	1	Zinc 1 By similarity
	Binding site	157	1	Substrate By similarity
	Binding site	291	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	340	1	Substrate; via carbonyl oxygen By similarity
Amino acid modifications
	Modified residue	152	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q18677-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 4912F1635D82ECFB	FASTA	520	56,293
	10 20 30 40 50 60 MSLLIKNGTI VNDDAIFKSD VLVLDGRIVE IAPSIQPTPG LEVVDATDRL VIPGGIDPHT 70 80 90 100 110 120 HMQLPFMGEI AKDDFHRGTE AAVAGGTTMI IDFVIPTKGE SLLVAYDRWR GWADPKVVCD 130 140 150 160 170 180 YGLSMAITSW GPEIAKEMEI VTGAEYGINS FKFFLAYAGV FMVRDEEFYQ GMIQCAKLRA 190 200 210 220 230 240 LARVHAENGS VIAERCEHLL SSGITGPEGH TQSRPEELEA EATFRACTMA SQANCPLYVV 250 260 270 280 290 300 HVMSKGAAAA IAHHRKKGAV VFGEPIAAGL ATDGSHYYNE DWLHAARYVM SPPLSRDPST 310 320 330 340 350 360 PSALMKLLAA GELHLTATDN CTFDCQQKSL GKDDFTKIPN GVNGVEDRMS VVWDKGVHAG 370 380 390 400 410 420 IIDPMRFVAV TSTMAAKIFN CYPQKGRIAV GSDADIVIWN ANATRTISKD THHHAIDFNI 430 440 450 460 470 480 FEGMQVHGVP EITISRGRTV WANGQLKTVQ GSGQFIPLAP DSQIVFSAVD NRKKAMEPVK 490 500 510 520 IDRIPYEPSA LQTPDANANI VVKAPVRAAI PPGGASSIQF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of the Caenorhabditis elegans CeCRMP/DHP-1 and -2; common ancestors of CRMP and dihydropyrimidinase?" Takemoto T., Sasaki Y., Hamajima N., Goshima Y., Nonaka M., Kimura H. Gene 261:259-267(2000) [PubMed: 11167013] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: Bristol N2.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[3]	"The Ulip family phosphoproteins -- common and specific properties." Byk T., Ozon S., Sobel A. Eur. J. Biochem. 254:14-24(1998) [PubMed: 9652388] [Abstract] Cited for: IDENTIFICATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB040993 mRNA. Translation: BAB21561.1. Z68882 Genomic DNA. Translation: CAA93104.1.
PIR	T20007.
RefSeq	NP_501797.1.
UniGene	Cel.19393
3D structure databases
HSSP	HSSP built from PDB template 1K1D based on UniProtKB Q45515.
ModBase	Search...
Genome annotation databases
Ensembl	C47E12.8. Caenorhabditis elegans. [Contig view]
GeneID	177852.
KEGG	cel:C47E12.8.
NMPDR	fig|6239.3.peg.14729.
Organism-specific databases
WormBase	WBGene00000964. dhp-2.
WormPep	C47E12.8. CE05452. [WorfDB]
Phylogenomic databases
OMA	Q18677. YEAGVFS.
Enzyme and pathway databases
BRENDA	3.5.2.2. 672.
Gene expression databases
ArrayExpress	Q18677.
Family and domain databases
InterPro	IPR006680. Amidohydro_1. IPR011778. D-hydantoinase. [Graphical view]
Pfam	PF01979. Amidohydro_1. 1 hit. [Graphical view]
ProDom	PD000518. DHOase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR02033. D-hydantoinase. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	898656.

Entry information

Entry name

DHP2_CAEEL

Accession

Primary (citable) accession number: Q18677

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project