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Conserved domains on  [gi|1380941520|ref|NP_001349577|]
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inosine triphosphate pyrophosphatase isoform 2 [Mus musculus]

Protein Classification

non-canonical purine NTP pyrophosphatase( domain architecture ID 10087719)

RdgB/HAM1 family pyrophosphatase that hydrolyzes non-canonical purine nucleotides to their respective monophosphates and prevents their incorporation into DNA

CATH:  3.90.950.10
EC:  3.6.1.-
Gene Ontology:  GO:0047429|GO:0009146|GO:0000166
PubMed:  17976651|22531138
SCOP:  4000518

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAM1 cd00515
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ...
 15-114 9.52e-41

NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ inosine triphosphatase. HAM1 protects the cell against mutagenesis by the base analog 6-N-hydroxylaminopurine (HAP) in E. Coli and S. cerevisiae. A Ham1-related protein from Methanococcus jannaschii is a novel NTPase that has been shown to hydrolyze nonstandard nucleotides such as XTP to XMP and ITP to IMP, but not the standard nucleotides, in the presence of Mg or Mn ions. The enzyme exists as a homodimer. The HAM1 protein may be acting as an NTPase by hydrolyzing the HAP triphosphate.


:

Pssm-ID: 238285 [Multi-domain]  Cd Length: 183  Bit Score: 133.42  E-value: 9.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941520  15 KWFLQ----KLKPEGLHQLLAGFEDKSAYALCTFALStgDPSQPVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQT 89
Cdd:cd00515    81 ARFAGehddAENNEKLLELLEGDEDRSAYFVCVIALV--DPDGEPLVFEGEVEGKIVTePRGTGGFGYDPIFIPEGYGKT 158

                          90       100
                  ....*....|....*....|....*
gi 1380941520  90 YAEMPKSEKNTISHRFRALHKLQEY 114
Cdd:cd00515   159 FAEMSPEEKNAISHRGKALRKLKEF 183
 
Name Accession Description Interval E-value
HAM1 cd00515
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ...
 15-114 9.52e-41

NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ inosine triphosphatase. HAM1 protects the cell against mutagenesis by the base analog 6-N-hydroxylaminopurine (HAP) in E. Coli and S. cerevisiae. A Ham1-related protein from Methanococcus jannaschii is a novel NTPase that has been shown to hydrolyze nonstandard nucleotides such as XTP to XMP and ITP to IMP, but not the standard nucleotides, in the presence of Mg or Mn ions. The enzyme exists as a homodimer. The HAM1 protein may be acting as an NTPase by hydrolyzing the HAP triphosphate.


Pssm-ID: 238285 [Multi-domain]  Cd Length: 183  Bit Score: 133.42  E-value: 9.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941520  15 KWFLQ----KLKPEGLHQLLAGFEDKSAYALCTFALStgDPSQPVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQT 89
Cdd:cd00515    81 ARFAGehddAENNEKLLELLEGDEDRSAYFVCVIALV--DPDGEPLVFEGEVEGKIVTePRGTGGFGYDPIFIPEGYGKT 158

                          90       100
                  ....*....|....*....|....*
gi 1380941520  90 YAEMPKSEKNTISHRFRALHKLQEY 114
Cdd:cd00515   159 FAEMSPEEKNAISHRGKALRKLKEF 183
Ham1p_like pfam01725
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ...
 18-114 1.59e-38

Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and C. elegans proteins. HAM1 controls 6-N-hydroxylaminopurine (HAP) sensitivity and mutagenesis in S. cerevisiae. The 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.


Pssm-ID: 460306 [Multi-domain]  Cd Length: 186  Bit Score: 127.95  E-value: 1.59e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941520  18 LQKLkpegLHQLLAGFEDKSAYALCTFALStgDPSQPVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQTYAEMPKS 96
Cdd:pfam01725  95 NAKL----LEELEVPDEDRSARFVCVIALA--DPGGPELVFEGEVEGEIVEePRGEGGFGYDPIFIPPEGGKTFAELSPE 168

                          90
                  ....*....|....*...
gi 1380941520  97 EKNTISHRFRALHKLQEY 114
Cdd:pfam01725 169 EKNAISHRGKALRKLKEF 186
RdgB COG0127
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ...
 24-115 5.90e-32

Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];


Pssm-ID: 439897 [Multi-domain]  Cd Length: 191  Bit Score: 111.31  E-value: 5.90e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941520  24 EGLHQLLAGF-EDKSAYALCTFALSTGDPSqpVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQTYAEMPKSEKNTI 101
Cdd:COG0127    98 EKLLKLLEGVdEDRRARFVCVLALADPDGE--PLVFEGEVEGEIAEePRGEGGFGYDPIFIPDGYGKTFAELSPEEKNAI 175

                          90
                  ....*....|....
gi 1380941520 102 SHRFRALHKLQEYF 115
Cdd:COG0127   176 SHRGRALRKLAEWL 189
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
 24-114 5.11e-24

non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 protects against the mutagenic effects of the base analog 6-N-hydroxylaminopurine, which can be a natural product of monooxygenase activity on adenine. Methanococcus jannaschii MJ0226 and E. coli RdgB are also characterized as pyrophosphatases active against non-standard purines NTPs. E. coli RdgB appears to act by intercepting non-canonical deoxyribonucleotide triphosphates from replication precursor pools. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 272870 [Multi-domain]  Cd Length: 184  Bit Score: 90.89  E-value: 5.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941520  24 EGLHQLLAGFEDKSAYALCTFALStgDPSQPVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQTYAEMPKSEKNTIS 102
Cdd:TIGR00042  93 EKILKLLEGVENRQAYFVCVIGYC--DPNGEPLVFEGIVKGKITRePRGTYGFGYDPIFIPPEEGKTFAELTTEEKNKIS 170

                          90
                  ....*....|..
gi 1380941520 103 HRFRALHKLQEY 114
Cdd:TIGR00042 171 HRGKAFKKFKKF 182
PRK00120 PRK00120
dITP/XTP pyrophosphatase; Reviewed
 26-114 3.46e-23

dITP/XTP pyrophosphatase; Reviewed


Pssm-ID: 234648 [Multi-domain]  Cd Length: 196  Bit Score: 88.99  E-value: 3.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941520  26 LHQLLAG--FEDKSAYALCTFALSTGDPSqpVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQTYAEMPKSEKNTIS 102
Cdd:PRK00120  101 LLEELKGvpDEDRRARFVCVLVLVRPDPT--PLVAEGRWEGEILWePRGENGFGYDPIFFPPGYGKTFAELTPEEKNAIS 178

                          90
                  ....*....|..
gi 1380941520 103 HRFRALHKLQEY 114
Cdd:PRK00120  179 HRGKALKLLLEA 190
 
Name Accession Description Interval E-value
HAM1 cd00515
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ...
 15-114 9.52e-41

NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ inosine triphosphatase. HAM1 protects the cell against mutagenesis by the base analog 6-N-hydroxylaminopurine (HAP) in E. Coli and S. cerevisiae. A Ham1-related protein from Methanococcus jannaschii is a novel NTPase that has been shown to hydrolyze nonstandard nucleotides such as XTP to XMP and ITP to IMP, but not the standard nucleotides, in the presence of Mg or Mn ions. The enzyme exists as a homodimer. The HAM1 protein may be acting as an NTPase by hydrolyzing the HAP triphosphate.


Pssm-ID: 238285 [Multi-domain]  Cd Length: 183  Bit Score: 133.42  E-value: 9.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941520  15 KWFLQ----KLKPEGLHQLLAGFEDKSAYALCTFALStgDPSQPVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQT 89
Cdd:cd00515    81 ARFAGehddAENNEKLLELLEGDEDRSAYFVCVIALV--DPDGEPLVFEGEVEGKIVTePRGTGGFGYDPIFIPEGYGKT 158

                          90       100
                  ....*....|....*....|....*
gi 1380941520  90 YAEMPKSEKNTISHRFRALHKLQEY 114
Cdd:cd00515   159 FAEMSPEEKNAISHRGKALRKLKEF 183
Ham1p_like pfam01725
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ...
 18-114 1.59e-38

Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and C. elegans proteins. HAM1 controls 6-N-hydroxylaminopurine (HAP) sensitivity and mutagenesis in S. cerevisiae. The 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.


Pssm-ID: 460306 [Multi-domain]  Cd Length: 186  Bit Score: 127.95  E-value: 1.59e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941520  18 LQKLkpegLHQLLAGFEDKSAYALCTFALStgDPSQPVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQTYAEMPKS 96
Cdd:pfam01725  95 NAKL----LEELEVPDEDRSARFVCVIALA--DPGGPELVFEGEVEGEIVEePRGEGGFGYDPIFIPPEGGKTFAELSPE 168

                          90
                  ....*....|....*...
gi 1380941520  97 EKNTISHRFRALHKLQEY 114
Cdd:pfam01725 169 EKNAISHRGKALRKLKEF 186
RdgB COG0127
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ...
 24-115 5.90e-32

Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];


Pssm-ID: 439897 [Multi-domain]  Cd Length: 191  Bit Score: 111.31  E-value: 5.90e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941520  24 EGLHQLLAGF-EDKSAYALCTFALSTGDPSqpVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQTYAEMPKSEKNTI 101
Cdd:COG0127    98 EKLLKLLEGVdEDRRARFVCVLALADPDGE--PLVFEGEVEGEIAEePRGEGGFGYDPIFIPDGYGKTFAELSPEEKNAI 175

                          90
                  ....*....|....
gi 1380941520 102 SHRFRALHKLQEYF 115
Cdd:COG0127   176 SHRGRALRKLAEWL 189
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
 24-114 5.11e-24

non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 protects against the mutagenic effects of the base analog 6-N-hydroxylaminopurine, which can be a natural product of monooxygenase activity on adenine. Methanococcus jannaschii MJ0226 and E. coli RdgB are also characterized as pyrophosphatases active against non-standard purines NTPs. E. coli RdgB appears to act by intercepting non-canonical deoxyribonucleotide triphosphates from replication precursor pools. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 272870 [Multi-domain]  Cd Length: 184  Bit Score: 90.89  E-value: 5.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941520  24 EGLHQLLAGFEDKSAYALCTFALStgDPSQPVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQTYAEMPKSEKNTIS 102
Cdd:TIGR00042  93 EKILKLLEGVENRQAYFVCVIGYC--DPNGEPLVFEGIVKGKITRePRGTYGFGYDPIFIPPEEGKTFAELTTEEKNKIS 170

                          90
                  ....*....|..
gi 1380941520 103 HRFRALHKLQEY 114
Cdd:TIGR00042 171 HRGKAFKKFKKF 182
PRK00120 PRK00120
dITP/XTP pyrophosphatase; Reviewed
 26-114 3.46e-23

dITP/XTP pyrophosphatase; Reviewed


Pssm-ID: 234648 [Multi-domain]  Cd Length: 196  Bit Score: 88.99  E-value: 3.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941520  26 LHQLLAG--FEDKSAYALCTFALSTGDPSqpVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQTYAEMPKSEKNTIS 102
Cdd:PRK00120  101 LLEELKGvpDEDRRARFVCVLVLVRPDPT--PLVAEGRWEGEILWePRGENGFGYDPIFFPPGYGKTFAELTPEEKNAIS 178

                          90
                  ....*....|..
gi 1380941520 103 HRFRALHKLQEY 114
Cdd:PRK00120  179 HRGKALKLLLEA 190
PRK14822 PRK14822
XTP/dITP diphosphatase;
26-115 7.97e-22

XTP/dITP diphosphatase;


Pssm-ID: 184835 [Multi-domain]  Cd Length: 200  Bit Score: 85.32  E-value: 7.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941520  26 LHQLLAG--FEDKSAYALCTFALSTgdPSQPVLLFRGQTSGQIV-MPRGSRDFGWDPCFQPDGYEQTYAEMPKSEKNTIS 102
Cdd:PRK14822  103 LLKELGGvpFEKRTARFHCVIAVAF--PGGETKTVEGTCEGEILeEPRGENGFGYDPLFYVPEKGKTMAELSSEEKNAIS 180

                          90
                  ....*....|...
gi 1380941520 103 HRFRALHKLQEYF 115
Cdd:PRK14822  181 HRGKALKKLEAEL 193
PRK14821 PRK14821
XTP/dITP diphosphatase;
17-116 5.58e-20

XTP/dITP diphosphatase;


Pssm-ID: 184834 [Multi-domain]  Cd Length: 184  Bit Score: 80.38  E-value: 5.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941520  17 FLQK-LKPEGLHQLLAGFEDKSAY-----ALCtfalstgDPSQpVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQT 89
Cdd:PRK14821   83 FVYKtLGNEGILKLLEGEENRRAYfksviGYC-------DPGG-EKLFTGIVEGKIANeIRGKGGFGYDPIFIPEGEEKT 154

                          90       100
                  ....*....|....*....|....*..
gi 1380941520  90 YAEMPKSEKNTISHRFRALHKLQEYFS 116
Cdd:PRK14821  155 FAEMTTEEKNKISHRKRAFDEFKEWLK 181
PRK14823 PRK14823
putative deoxyribonucleoside-triphosphatase; Provisional
 57-116 4.84e-19

putative deoxyribonucleoside-triphosphatase; Provisional


Pssm-ID: 237823 [Multi-domain]  Cd Length: 191  Bit Score: 78.18  E-value: 4.84e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1380941520  57 LFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQTYAEMPKSEKNTISHRFRALHKLQEYFS 116
Cdd:PRK14823  129 LFEGIIKGEIIKeKRGDSGFGYDPIFVPEGYDKTFAELGLEIKNQISHRAKAVQKLIDFLS 189
PRK14824 PRK14824
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 26-113 5.43e-18

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 237824 [Multi-domain]  Cd Length: 201  Bit Score: 75.57  E-value: 5.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941520  26 LHQLLAGFEDKSAYALCTFALSTGDPSqpvLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQTYAEMPKSEKNTISHR 104
Cdd:PRK14824  108 LLRLLEGKQNRKARFVAFVVLYFGDWG---IWTEGECRGKIAEePRGSGGFGYDPVFIPEGYNKTMAELSPEEKNKISHR 184


                  ....*....
gi 1380941520 105 FRALHKLQE 113
Cdd:PRK14824  185 GKAVRKLVE 193
PRK14826 PRK14826
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 60-116 6.66e-12

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 173287  Cd Length: 222  Bit Score: 59.68  E-value: 6.66e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1380941520  60 GQTSGQIVM-PRGSRDFGWDPCFQPDGYEQTYAEMPKSEKNTISHRFRALHK----LQEYFS 116
Cdd:PRK14826  160 GVVEGSITTeKKGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRALAVQKavkfLRTILS 221
PRK02491 PRK02491
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; ...
 26-115 2.07e-10

putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed


Pssm-ID: 179431 [Multi-domain]  Cd Length: 328  Bit Score: 56.36  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941520  26 LHQLLAGFE--DKSAYALCTFALSTgdPSQPVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQTYAEMPKSEKNTIS 102
Cdd:PRK02491  230 LHELAMVFDlkDRSAQFHTTLVVAA--PNKDSLVVEADWPGYIATePKGENGFGYDPLFLVGETGRHAAELTAEEKNQLS 307

                          90
                  ....*....|...
gi 1380941520 103 HRFRALHKLQEYF 115
Cdd:PRK02491  308 HRGQAVKKLMEVF 320
PRK14825 PRK14825
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 34-115 6.63e-03

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 173286  Cd Length: 199  Bit Score: 34.91  E-value: 6.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941520  34 EDKSAYALCTFALSTGDPSqpVLLFRGQTSGQIVMP---RGSRDFGWDPCFQPDGyEQTYAEMPKSEKNTISHRFRALHK 110
Cdd:PRK14825  113 KNRTAYFICNISYISKDGT--ILNFEGIIKGTIALSiddYKKNGFGYDPIFLTKN-NKRLSELTLEEKNKISHRGIAFDK 189


                  ....*
gi 1380941520 111 LQEYF 115
Cdd:PRK14825  190 FKKFL 194
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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