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InterPro: IPR002637 Ham1-like protein

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Accession

IPR002637 Ham1p-like

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01725	Ham1p_like	1980
PANTHER	PTHR11067	Ham1p_like	1969
TIGRFAMs	TIGR00042	Ham1p_like	1683
Signatures in BioMart

InterPro Relationships Help

Children

IPR020922 Nucleoside-triphosphatase

GO Term annotation Help

Function

GO:0016787 hydrolase activity

InterPro annotation

Entry Details in BioMart

Abstract

This family contains the Saccharomyces cerevisiae (Baker's yeast) HAM1 protein P47119 and other hypothetical archaeal, bacterial and Caenorhabditis elegans proteins. S. cerevisiae HAM1 protects against the mutagenic effects of the base analog 6-N-hydroxylaminopurine (HAP) which can be a natural product of monooxygenase activity on adenine. HAM1 protein protects the cell from HAP, either on the level of deoxynucleoside triphosphate or the DNA level by a yet unidentified set of reactions [1].

Structural links Help

PDB - click here

SCOP: c.51.4.1

CATH: 3.90.950.10

Database links Help

Enzyme: EC:3.6.1.15

PANDIT: PF01725

Blocks: IPB002637

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR002637

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P47119 Protein HAM1

P52061 Nucleoside-triphosphatase rdgB

P74432 Nucleoside-triphosphatase

Q9BY32 Inosine triphosphate pyrophosphatase

Q9D892 Inosine triphosphate pyrophosphatase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR020922	Nucleoside-triphosphatase
IPR002637	Ham1-like protein
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Noskov VN, Staak K, Shcherbakova PV, Kozmin SG, Negishi K, Ono BC, Hayatsu H, Pavlov YI. HAM1, the gene controlling 6-N-hydroxylaminopurine sensitivity and mutagenesis in the yeast Saccharomyces cerevisiae. Yeast 12 17-29 1996 [PubMed: 8789257] http://dx.doi.org/10.1002/(SICI)1097-0061(199601)12:1<17::AID-YEA875>3.3.CO;2-9

Additional Reading Open in usermanual
	Stenmark P, Kursula P, Flodin S, Graslund S, Landry R, Nordlund P, Schuler H. Crystal structure of human inosine triphosphatase. Substrate binding and implication of the inosine triphosphatase deficiency mutation P32T. J. Biol. Chem. 282 2007 3182-7 [PubMed: 17138556] http://dx.doi.org/10.1074/jbc.M609838200
	Lokanath NK, Pampa KJ, Takio K, Kunishima N. Structures of dimeric nonstandard nucleotide triphosphate pyrophosphatase from Pyrococcus horikoshii OT3: functional significance of interprotomer conformational changes. J. Mol. Biol. 375 2008 1013-25 [PubMed: 18062990] http://dx.doi.org/10.1016/j.jmb.2007.11.018
	Hwang KY, Chung JH, Kim SH, Han YS, Cho Y. Structure-based identification of a novel NTPase from Methanococcus jannaschii. Nat. Struct. Biol. 6 1999 691-6 [PubMed: 10404228] http://dx.doi.org/10.1038/10745
	Savchenko A, Proudfoot M, Skarina T, Singer A, Litvinova O, Sanishvili R, Brown G, Chirgadze N, Yakunin AF. Molecular basis of the antimutagenic activity of the house-cleaning inosine triphosphate pyrophosphatase RdgB from Escherichia coli. J. Mol. Biol. 374 2007 1091-103 [PubMed: 17976651] http://dx.doi.org/10.1016/j.jmb.2007.10.012
	Porta J, Kolar C, Kozmin SG, Pavlov YI, Borgstahl GE. Structure of the orthorhombic form of human inosine triphosphate pyrophosphatase. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 2006 1076-81 [PubMed: 17077483]
	Burgis NE, Brucker JJ, Cunningham RP. Repair system for noncanonical purines in Escherichia coli. J. Bacteriol. 185 2003 3101-10 [PubMed: 12730170] http://dx.doi.org/10.1128/JB.185.10.3101-3110.2003

InterPro 23.1