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PR01404

Identifier
NPPPHYDRLASE  [View Relations]  [View Alignment]  
Accession
PR01404
No. of Motifs
5
Creation Date
30-APR-2000
Title
DATP pyrophosphohydrolase signature
Database References
PRINTS; PR00502 NUDIXFAMILY
PROSITE; PS00893 ; MUTT
BLOCKS; BL00893
PFAM; PF00293 mutT
INTERPRO; IPR000086
Literature References
1. MICHAELS, M.L. AND MILLER, J.H.
The GO system protects organisms from the mutagenic effect of the
spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine).
J.BACTERIOL. 174(20) 6321-6325 (1992).
 
2. KOONIN, E.V.
A highly conserved sequence motif defining the family of mutT-related
proteins from eubacteria, eukaryotes and viruses.
NUCLEIC ACIDS RES. 21 4847 (1993).
 
3. MEJEAN, V., SALLES, C., BULLIONS, M.J., BESSMAN, M.J. AND CLAVEREYS, J.P.
Characterisation of the mutX gene of Streptococcus pneumoniae as a homolog
of Escherichia coli mutT, and tentative definition of a catalytic domain of
the dGTP pyrophosphohydrolases.
MOL.MICROBIOL. 11(2) 323-330 (1994).
 
4. SAKUMI, K., FURUICHI, M., TSUZUKI, T., KAKUMA, T., KAWABATA, S.,
MAKI, H. AND SEKIGUCHI, M.
Cloning and expression of cDNA for a human enzyme that hydrolses 8-oxo-dGTP,
a mutagenic substrate for DNA synthesis.
J.BIOL.CHEM. 268 23524-23530 (1993).
 
5. MCLENNAN, A.G. 
The MutT motif family of nucleotide phosphohydrolases in man and human
pathogens.
INT.J.MOL.MED. 4(1) 79-89 (1999).
 
6. BESSMAN, M. J., FRICK, D. N., AND O'HANDLEY, S. F. 
The MutT proteins or "Nudix" hydrolases, a family of versatile, widely
distributed, "housecleaning" enzymes.
J.BIOL.CHEM. 271 25059-25062 (1996). 

Documentation
MutT is a small bacterial protein (~12-15kDa) involved in the GO system [1]
responsible for removing an oxidatively damaged form of guanine (8-hydroxy-
guanine or 7,8-dihydro-8-oxoguanine) from the nucleotide pool.
8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with
near equal efficiency, leading to A.T to G.C transversions. MutT
specifically degrades 8-oxo-dGTP to the monophosphate, with the concomitant
release of pyrophosphate. A short conserved N-terminal region of mutT 
(designated the MutT domain) is also found in a variety of other
prokaryotic, viral, and eukaryotic proteins [2-5]. Recently, the generic
name `NUDIX hydrolases' (NUcleoside DIphosphate linked to some other moeity
X) has been coined for this domain family [6].
 
DATP pyrophosphohydrolase hydrolyses nucleoside triphosphates with a
preference for DATP. The protein sequence shares significant similarity
to proteins with a core MutT domain.
 
NPPPHYDRLASE is a 5-element fingerprint that provides a signature for 
DATP pyrophosphohydrolases. The fingerprint was derived from an initial
alignment of 2 sequences: the motifs were drawn from conserved regions
spanning the N- and C-terminal portions of the alignment - motifs 1
and 2 lie N-terminal to the MutT domain; and motifs 3-5 lie C-terminal to
it. Two iterations on SPTR37_10f were required to reach convergence, at
which point a true set comprising 3 sequences was identified.
Summary Information
3 codes involving  5 elements
0 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
533333
400000
300000
200000
12345
True Positives
NTPA_ECOLI    NTPA_HAEIN    Q47419        
Sequence Titles
NTPA_ECOLI  DATP PYROPHOSPHOHYDROLASE (EC 3.6.1.-) - ESCHERICHIA COLI. 
NTPA_HAEIN DATP PYROPHOSPHOHYDROLASE (EC 3.6.1.-) - HAEMOPHILUS INFLUENZAE.
Q47419 HYPOTHETICAL 16.8 KD PROTEIN - ESCHERICHIA COLI.
Scan History
SPTR37_10f 2  100  NSINGLE    
Initial Motifs
Motif 1  width=18
Element Seqn Id St Int Rpt
YKNNQSVLVVIYTKDTNR NTPA_HAEIN 13 13 -
YKRPVSILVVIYAQDTKR NTPA_ECOLI 6 6 -

Motif 2 width=22
Element Seqn Id St Int Rpt
RVLMLQRQDDPDFWQSVTGTIE NTPA_HAEIN 30 -1 -
RVLMLQRRDDPDFWQSVTGSVE NTPA_ECOLI 23 -1 -

Motif 3 width=20
Element Seqn Id St Int Rpt
DCNESIEFEIFPHFRYKYAP NTPA_HAEIN 81 29 -
DCQRTVEFEIFSHLRHRYAP NTPA_ECOLI 74 29 -

Motif 4 width=22
Element Seqn Id St Int Rpt
WFCLALPHERQIVFTEHLAYKW NTPA_ECOLI 102 8 -
WFLCEVEKEFIPVLSEHLDFCW NTPA_HAEIN 109 8 -

Motif 5 width=14
Element Seqn Id St Int Rpt
AAALTKSWSNRQAI NTPA_ECOLI 129 5 -
AVEMTKSQNNAEAI NTPA_HAEIN 136 5 -
Final Motifs
Motif 1  width=18
Element Seqn Id St Int Rpt
YKNNQSVLVVIYTKDTNR NTPA_HAEIN 13 13 -
YKRPVSILVVIYAQDTKR NTPA_ECOLI 6 6 -
YKRPVSILVVIYAQDTKR Q47419 2 2 -

Motif 2 width=22
Element Seqn Id St Int Rpt
RVLMLQRQDDPDFWQSVTGTIE NTPA_HAEIN 30 -1 -
RVLMLQRRDDPDFWQSVTGSVE NTPA_ECOLI 23 -1 -
RVLMLQRRDDPDFWQSVTGSVE Q47419 19 -1 -

Motif 3 width=20
Element Seqn Id St Int Rpt
DCNESIEFEIFPHFRYKYAP NTPA_HAEIN 81 29 -
DCQRTVEFEIFSHLRHRYAP NTPA_ECOLI 74 29 -
DCQRTVEFEIFSHLRHRYAP Q47419 70 29 -

Motif 4 width=22
Element Seqn Id St Int Rpt
WFLCEVEKEFIPVLSEHLDFCW NTPA_HAEIN 109 8 -
WFCLALPHERQIVFTEHLAYKW NTPA_ECOLI 102 8 -
WFCLALPHERQIVFTEHLAYKW Q47419 98 8 -

Motif 5 width=14
Element Seqn Id St Int Rpt
AAALTKSWSNRQAI NTPA_ECOLI 129 5 -
AAALTKSWSNRQAI Q47419 125 5 -
AVEMTKSQNNAEAI NTPA_HAEIN 136 5 -