Q6MVL2 (DUT_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Deoxyuridine 5'-triphosphate nucleotidohydrolase
Short name=dUTPase
EC=3.6.1.23

Alternative name(s):
dUTP pyrophosphatase

Gene names

Name:	dut-1
ORF Names:	B8J22.110, NCU10893

Organism

Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]

Taxonomic identifier

367110 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora › Neurospora crassa

Protein attributes

Sequence length	165 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA By similarity.
Catalytic activity	dUTP + H2O = dUMP + diphosphate.
Cofactor	Magnesium By similarity.
Pathway	Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
Subunit structure	Homotrimer By similarity.
Sequence similarities	Belongs to the dUTPase family.
Sequence caution	The sequence EDO64923.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	dUMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway dUTP metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	dUTP diphosphatase 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 – 165	165	Deoxyuridine 5'-triphosphate nucleotidohydrolase		PRO_0000182934
Regions
	Region	77 – 79	3	Substrate binding By similarity
	Region	91 – 94	4	Substrate binding By similarity
	Region	150 – 151	2	Substrate binding By similarity
Sites
	Binding site	102	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	145	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6MVL2 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 2A575A279571A25A	FASTA	165	17,441
	10 20 30 40 50 60 MTADTQTPVT KVDQAPPLLI KKLSDKARLP TRGSAFAAGY DIYASKETTI PARGKGLVET 70 80 90 100 110 120 DISMAVPAGT YGRIAPRSGL AAKNFIDVGA GVIDADYRGQ VKVLLFNHSD VDFVVNEGDR 130 140 150 160 VAQLVLERIY TPEVVEVEQL EESVRGAGGF GSTGVGSGVG EQMKN

References

[1]

"What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence." Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U. Nucleic Acids Res. 31:1944-1954(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

[2]

"The genome sequence of the filamentous fungus Neurospora crassa." Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W. Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842627 Genomic DNA. Translation: CAE76286.1. AABX02000070 Genomic DNA. Translation: EDO64923.1. Different initiation.
RefSeq	XP_001728014.1. XM_001727962.1.
UniGene	Ncr.14848.
3D structure databases
ProteinModelPortal	Q6MVL2.
SMR	Q6MVL2. Positions 18-154.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	EFNCRT00000009084; EFNCRP00000009066; EFNCRG00000009069.
GeneID	5847067.
KEGG	ncr:NCU10893.
Phylogenomic databases
HOGENOM	HOG000028966.
KO	K01520.
OrthoDB	EOG47M57F.
Enzyme and pathway databases
UniPathway	UPA00610; UER00666.
Family and domain databases
InterPro	IPR008180. dUTP_pyroPase. IPR008181. dUTP_pyroPase_sf. [Graphical view]
PANTHER	PTHR11241. PTHR11241. 1 hit.
Pfam	PF00692. dUTPase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00576. dut. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DUT_NEUCR

Accession

Primary (citable) accession number: Q6MVL2
Secondary accession number(s): A7UXB3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 7, 2004
Last sequence update:	July 5, 2004
Last modified:	April 3, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program