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Conserved domains on  [gi|353558682|sp|A9VE54|]
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RecName: Full=Inosine triphosphate pyrophosphatase; Short=ITPase; Short=Inosine triphosphatase; AltName: Full=Non-canonical purine NTP pyrophosphatase; AltName: Full=Non-standard purine NTP pyrophosphatase; AltName: Full=Nucleoside-triphosphate diphosphatase; AltName: Full=Nucleoside-triphosphate pyrophosphatase; Short=NTPase

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:  22531138|17976651
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/ ...
 8-185 3.10e-72

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: 216.62  E-value: 3.10e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682   8 ITFVTGNAKKLQEVQQILGQgFPFELT--NRKIDLPELQGEPEDISREKCRLAAAEVKGPVMVEDTSLCFNALHGLPGPY 85
Cdd:cd00515    1 IVFATGNKGKLKEFKEILAP-FGIEVVslKDIIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682  86 IKWFL----DKTGHVGLNNLLAAYPDKSAYAQCIFAFTTGPGaEIQTFVGRTEGKIV-PARGPTDFGWDPVFQPDGFEET 160
Cdd:cd00515   80 SARFAgehdDAENNEKLLELLEGDEDRSAYFVCVIALVDPDG-EPLVFEGEVEGKIVtEPRGTGGFGYDPIFIPEGYGKT 158

                        170       180
                 ....*....|....*....|....*
gi 353558682 161 YAEMDKTIKNSISHRGRSLSALCAY 185
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/ ...
 8-185 3.10e-72

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: 216.62  E-value: 3.10e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682   8 ITFVTGNAKKLQEVQQILGQgFPFELT--NRKIDLPELQGEPEDISREKCRLAAAEVKGPVMVEDTSLCFNALHGLPGPY 85
Cdd:cd00515    1 IVFATGNKGKLKEFKEILAP-FGIEVVslKDIIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682  86 IKWFL----DKTGHVGLNNLLAAYPDKSAYAQCIFAFTTGPGaEIQTFVGRTEGKIV-PARGPTDFGWDPVFQPDGFEET 160
Cdd:cd00515   80 SARFAgehdDAENNEKLLELLEGDEDRSAYFVCVIALVDPDG-EPLVFEGEVEGKIVtEPRGTGGFGYDPIFIPEGYGKT 158

                        170       180
                 ....*....|....*....|....*
gi 353558682 161 YAEMDKTIKNSISHRGRSLSALCAY 185
Cdd:cd00515  159 FAEMSPEEKNAISHRGKALRKLKEF 183
Ham1p_like pfam01725
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ...
 8-185 1.14e-69

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: 210.00  E-value: 1.14e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682    8 ITFVTGNAKKLQEVQQILGQGFPFEL---TNRKIDLPELQGEPEDISREKCRlAAAEVKGPVMVEDTSLCFNALHGLPGP 84
Cdd:pfam01725   1 IVFATGNAGKLRELKAILADGIEVLSlkdLGELPEIEETGGTFEENALIKAR-AAAKTGLPVLADDSGLEVDALNGFPGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682   85 YIKWFL--DKTGHVGLNNLLAAY----PDKSAYAQCIFAFTTGPGAEIqTFVGRTEGKIVPA-RGPTDFGWDPVFQPDGF 157
Cdd:pfam01725  80 YSARFAgeGGDDEANNAKLLEELevpdEDRSARFVCVIALADPGGPEL-VFEGEVEGEIVEEpRGEGGFGYDPIFIPPEG 158

                         170       180
                  ....*....|....*....|....*...
gi 353558682  158 EETYAEMDKTIKNSISHRGRSLSALCAY 185
Cdd:pfam01725 159 GKTFAELSPEEKNAISHRGKALRKLKEF 186
RdgB COG0127
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ...
 8-186 5.44e-54

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


Pssm-ID: 439897 [Multi-domain]  Cd Length: 191  Bit Score: 170.24  E-value: 5.44e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682   8 ITFVTGNAKKLQEVQQILGqGFPFEL-TNRKIDLPE--LQGE-PEDISREKCRLAAAEVKGPVMVEDTSLCFNALHGLPG 83
Cdd:COG0127    2 LVFATGNAGKLREIRALLA-PLGIEVvSLSDLGLPEpeETGDtFEENALIKARAAAKATGLPALADDSGLEVDALGGAPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682  84 PYIKWFLDKTGHVGLNN--LLAA----YPDKSAYAQCIFAFTTgPGAEIQTFVGRTEGKIV-PARGPTDFGWDPVFQPDG 156
Cdd:COG0127   81 VYSARYAGEGADDEANNekLLKLlegvDEDRRARFVCVLALAD-PDGEPLVFEGEVEGEIAeEPRGEGGFGYDPIFIPDG 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 353558682 157 FEETYAEMDKTIKNSISHRGRSLSALCAYF 186
Cdd:COG0127  160 YGKTFAELSPEEKNAISHRGRALRKLAEWL 189
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
 8-182 1.21e-45

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: 149.05  E-value: 1.21e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682    8 ITFVTGNAKKLQEVQQILGQGFPFELTNRKIDLPELQGEP-EDISREKCRLAAAEVKGPVMVEDTSLCFNALHGLPGPYI 86
Cdd:TIGR00042   2 IVFATGNPGKLKEVQSILSDLGDNEIEQLDLGYPEETGLTfEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGIYS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682   87 KWFL--DKTGHVGLNNLLAAYPDKSAYAQCIFAFTTgPGAEIQTFVGRTEGKIVPA-RGPTDFGWDPVFQPDGFEETYAE 163
Cdd:TIGR00042  82 ARYQgtDIGNLEKILKLLEGVENRQAYFVCVIGYCD-PNGEPLVFEGIVKGKITREpRGTYGFGYDPIFIPPEEGKTFAE 160

                         170
                  ....*....|....*....
gi 353558682  164 MDKTIKNSISHRGRSLSAL 182
Cdd:TIGR00042 161 LTTEEKNKISHRGKAFKKF 179
PRK14821 PRK14821
XTP/dITP diphosphatase;
8-188 8.81e-41

XTP/dITP diphosphatase;


Pssm-ID: 184834 [Multi-domain]  Cd Length: 184  Bit Score: 136.62  E-value: 8.81e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682   8 ITFVTGNAKKLQEVQQILgQGFPFELTNRKIDLPELQ-GEPEDISREKCRLAAAEVKGPVMVEDTSLCFNALHGLPGPYI 86
Cdd:PRK14821   3 IYFATGNKGKVEEAKIIL-KPLGIEVEQIKIEYPEIQaDTLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPGPYS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682  87 KWFLDKTGHVGLNNLLAAYPDKSAYAQCIFAFTTGPGAEIqtFVGRTEGKIV-PARGPTDFGWDPVFQPDGFEETYAEMD 165
Cdd:PRK14821  82 AFVYKTLGNEGILKLLEGEENRRAYFKSVIGYCDPGGEKL--FTGIVEGKIAnEIRGKGGFGYDPIFIPEGEEKTFAEMT 159

                        170       180
                 ....*....|....*....|...
gi 353558682 166 KTIKNSISHRGRSLSALCAYFDT 188
Cdd:PRK14821 160 TEEKNKISHRKRAFDEFKEWLKE 182
 
Name Accession Description Interval E-value
HAM1 cd00515
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ...
 8-185 3.10e-72

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: 216.62  E-value: 3.10e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682   8 ITFVTGNAKKLQEVQQILGQgFPFELT--NRKIDLPELQGEPEDISREKCRLAAAEVKGPVMVEDTSLCFNALHGLPGPY 85
Cdd:cd00515    1 IVFATGNKGKLKEFKEILAP-FGIEVVslKDIIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682  86 IKWFL----DKTGHVGLNNLLAAYPDKSAYAQCIFAFTTGPGaEIQTFVGRTEGKIV-PARGPTDFGWDPVFQPDGFEET 160
Cdd:cd00515   80 SARFAgehdDAENNEKLLELLEGDEDRSAYFVCVIALVDPDG-EPLVFEGEVEGKIVtEPRGTGGFGYDPIFIPEGYGKT 158

                        170       180
                 ....*....|....*....|....*
gi 353558682 161 YAEMDKTIKNSISHRGRSLSALCAY 185
Cdd:cd00515  159 FAEMSPEEKNAISHRGKALRKLKEF 183
Ham1p_like pfam01725
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ...
 8-185 1.14e-69

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: 210.00  E-value: 1.14e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682    8 ITFVTGNAKKLQEVQQILGQGFPFEL---TNRKIDLPELQGEPEDISREKCRlAAAEVKGPVMVEDTSLCFNALHGLPGP 84
Cdd:pfam01725   1 IVFATGNAGKLRELKAILADGIEVLSlkdLGELPEIEETGGTFEENALIKAR-AAAKTGLPVLADDSGLEVDALNGFPGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682   85 YIKWFL--DKTGHVGLNNLLAAY----PDKSAYAQCIFAFTTGPGAEIqTFVGRTEGKIVPA-RGPTDFGWDPVFQPDGF 157
Cdd:pfam01725  80 YSARFAgeGGDDEANNAKLLEELevpdEDRSARFVCVIALADPGGPEL-VFEGEVEGEIVEEpRGEGGFGYDPIFIPPEG 158

                         170       180
                  ....*....|....*....|....*...
gi 353558682  158 EETYAEMDKTIKNSISHRGRSLSALCAY 185
Cdd:pfam01725 159 GKTFAELSPEEKNAISHRGKALRKLKEF 186
RdgB COG0127
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ...
 8-186 5.44e-54

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


Pssm-ID: 439897 [Multi-domain]  Cd Length: 191  Bit Score: 170.24  E-value: 5.44e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682   8 ITFVTGNAKKLQEVQQILGqGFPFEL-TNRKIDLPE--LQGE-PEDISREKCRLAAAEVKGPVMVEDTSLCFNALHGLPG 83
Cdd:COG0127    2 LVFATGNAGKLREIRALLA-PLGIEVvSLSDLGLPEpeETGDtFEENALIKARAAAKATGLPALADDSGLEVDALGGAPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682  84 PYIKWFLDKTGHVGLNN--LLAA----YPDKSAYAQCIFAFTTgPGAEIQTFVGRTEGKIV-PARGPTDFGWDPVFQPDG 156
Cdd:COG0127   81 VYSARYAGEGADDEANNekLLKLlegvDEDRRARFVCVLALAD-PDGEPLVFEGEVEGEIAeEPRGEGGFGYDPIFIPDG 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 353558682 157 FEETYAEMDKTIKNSISHRGRSLSALCAYF 186
Cdd:COG0127  160 YGKTFAELSPEEKNAISHRGRALRKLAEWL 189
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
 8-182 1.21e-45

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: 149.05  E-value: 1.21e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682    8 ITFVTGNAKKLQEVQQILGQGFPFELTNRKIDLPELQGEP-EDISREKCRLAAAEVKGPVMVEDTSLCFNALHGLPGPYI 86
Cdd:TIGR00042   2 IVFATGNPGKLKEVQSILSDLGDNEIEQLDLGYPEETGLTfEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGIYS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682   87 KWFL--DKTGHVGLNNLLAAYPDKSAYAQCIFAFTTgPGAEIQTFVGRTEGKIVPA-RGPTDFGWDPVFQPDGFEETYAE 163
Cdd:TIGR00042  82 ARYQgtDIGNLEKILKLLEGVENRQAYFVCVIGYCD-PNGEPLVFEGIVKGKITREpRGTYGFGYDPIFIPPEEGKTFAE 160

                         170
                  ....*....|....*....
gi 353558682  164 MDKTIKNSISHRGRSLSAL 182
Cdd:TIGR00042 161 LTTEEKNKISHRGKAFKKF 179
PRK14821 PRK14821
XTP/dITP diphosphatase;
8-188 8.81e-41

XTP/dITP diphosphatase;


Pssm-ID: 184834 [Multi-domain]  Cd Length: 184  Bit Score: 136.62  E-value: 8.81e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682   8 ITFVTGNAKKLQEVQQILgQGFPFELTNRKIDLPELQ-GEPEDISREKCRLAAAEVKGPVMVEDTSLCFNALHGLPGPYI 86
Cdd:PRK14821   3 IYFATGNKGKVEEAKIIL-KPLGIEVEQIKIEYPEIQaDTLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPGPYS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682  87 KWFLDKTGHVGLNNLLAAYPDKSAYAQCIFAFTTGPGAEIqtFVGRTEGKIV-PARGPTDFGWDPVFQPDGFEETYAEMD 165
Cdd:PRK14821  82 AFVYKTLGNEGILKLLEGEENRRAYFKSVIGYCDPGGEKL--FTGIVEGKIAnEIRGKGGFGYDPIFIPEGEEKTFAEMT 159

                        170       180
                 ....*....|....*....|...
gi 353558682 166 KTIKNSISHRGRSLSALCAYFDT 188
Cdd:PRK14821 160 TEEKNKISHRKRAFDEFKEWLKE 182
PRK00120 PRK00120
dITP/XTP pyrophosphatase; Reviewed
 12-185 4.74e-26

dITP/XTP pyrophosphatase; Reviewed


Pssm-ID: 234648 [Multi-domain]  Cd Length: 196  Bit Score: 99.00  E-value: 4.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682  12 TGNAKKLQEVQQILGqGFPFELTNRKiDLPElqGEPEDI-------SREKCRLAAAEVKGPVMVEDTSLCFNALHGLPGP 84
Cdd:PRK00120   7 SHNAGKLRELKALLA-PFGIEVVSQG-ELGV--PEPEETgttfvenALIKARHAAKATGLPALADDSGLCVDALGGAPGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682  85 YIKWFLDKTGHVGLNN--LLAA-----YPDKSAYAQCIFAFTTgPGAEIQTFVGRTEGKIV-PARGPTDFGWDPVFQPDG 156
Cdd:PRK00120  83 YSARYAGEGASDAANNekLLEElkgvpDEDRRARFVCVLVLVR-PDPTPLVAEGRWEGEILwEPRGENGFGYDPIFFPPG 161

                        170       180
                 ....*....|....*....|....*....
gi 353558682 157 FEETYAEMDKTIKNSISHRGRSLSALCAY 185
Cdd:PRK00120 162 YGKTFAELTPEEKNAISHRGKALKLLLEA 190
PRK14823 PRK14823
putative deoxyribonucleoside-triphosphatase; Provisional
 8-186 1.48e-22

putative deoxyribonucleoside-triphosphatase; Provisional


Pssm-ID: 237823 [Multi-domain]  Cd Length: 191  Bit Score: 89.74  E-value: 1.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682   8 ITFVTGNAKKLQEVQQILGQGFPFeLTNRKI----DLPELQGEPEDISREKCRLAAAEVKGPVMVEDTSLCFNALHGLPG 83
Cdd:PRK14823   3 LVFATNNKHKLEEIRSILPEKIEL-LSLSDIgcheDIPETADTLEGNALLKAEYVYKKYGYDCFADDTGLEVEALNGAPG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682  84 PYIKWFL--DKTGHVGLNNLLAAYPDKSAYAQCifaFTTGPGAEIQ----TFVGRTEGKIVPA-RGPTDFGWDPVFQPDG 156
Cdd:PRK14823  82 VYSARYAggEHNAEANMRKLLEELEGKDNRKAQ---FRTVIALILDgkehLFEGIIKGEIIKEkRGDSGFGYDPIFVPEG 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 353558682 157 FEETYAEMDKTIKNSISHRGRSLSALCAYF 186
Cdd:PRK14823 159 YDKTFAELGLEIKNQISHRAKAVQKLIDFL 188
PRK14822 PRK14822
XTP/dITP diphosphatase;
8-188 1.55e-22

XTP/dITP diphosphatase;


Pssm-ID: 184835 [Multi-domain]  Cd Length: 200  Bit Score: 89.95  E-value: 1.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682   8 ITFVTGNAKKLQEVQQILGqGFPFELTNRK--IDLPELQ--GEP-EDISREKCRLAAAEVKGPVMVEDTSLCFNALHGLP 82
Cdd:PRK14822   4 IVIATKNKGKVREFKEIFE-KFDIEVKSLAdfPPIPEVEetGTTfEENAILKAEAAAKALNKPVIADDSGLEVDALNGAP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682  83 GPYIKWF--LDKTGHVGLNNLLAA-----YPDKSAYAQCIFAFTTgPGAEIQTFVGRTEGKIVPA-RGPTDFGWDPVFQP 154
Cdd:PRK14822  83 GVYSARYagEAKDDAANNEKLLKElggvpFEKRTARFHCVIAVAF-PGGETKTVEGTCEGEILEEpRGENGFGYDPLFYV 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 353558682 155 DGFEETYAEMDKTIKNSISHRGRSLSALCAYFDT 188
Cdd:PRK14822 162 PEKGKTMAELSSEEKNAISHRGKALKKLEAELPE 195
PRK14824 PRK14824
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 8-182 1.26e-20

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 237824 [Multi-domain]  Cd Length: 201  Bit Score: 84.81  E-value: 1.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682   8 ITFVTGNAKKLQEVQQILGQ-GFPFELTNRKIDLPELQGEPEDISREKCRLAAAEVKGPVMVEDTSLCFNALHGLPGPYI 86
Cdd:PRK14824   3 ILLATTNEGKVREIKRLLSDlGIEVLSPDKKIEVEEDGETFLENAYLKARAYAEFYKIPVLADDSGLEVPALEGYPGVYS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682  87 KWFL--------------DKTGHVGLNNLLAAYPDKSAYAQCIFAFTtGPGAEIQTfVGRTEGKIV-PARGPTDFGWDPV 151
Cdd:PRK14824  83 SRFYqiefggkeevveskDEANIRKLLRLLEGKQNRKARFVAFVVLY-FGDWGIWT-EGECRGKIAeEPRGSGGFGYDPV 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 353558682 152 FQPDGFEETYAEMDKTIKNSISHRGRSLSAL 182
Cdd:PRK14824 161 FIPEGYNKTMAELSPEEKNKISHRGKAVRKL 191
PRK14826 PRK14826
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 1-181 1.69e-11

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 173287  Cd Length: 222  Bit Score: 60.84  E-value: 1.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682   1 MAKTTAAITFVTGNAKKLQEVQQILGQGFP-------FELtNRKIDLPELQGEPEDISREKCR--LAAAEVKGPVMV--- 68
Cdd:PRK14826   4 IATETITIVLATGNRDKVRELRPLLEHISPlfsvrslADL-GVEVDIEETEETLEGNALLKADaiFELLSDRFPFLIala 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682  69 EDTSLCFNALHGLPGPYIKWFL-----------DKTGHvgLNNLLAAYPDKSAYAQCIFAFT-TGPGAEI-----QTFVG 131
Cdd:PRK14826  83 DDTGLEVDALGGAPGVYSARFApvpegekptyeDNVRH--LLSEMEGKTERSARFRTVIALKgRLPGKNGafefeETAEG 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 353558682 132 RTEGKIVPAR-GPTDFGWDPVFQPDGFEETYAEMDKTIKNSISHRGRSLSA 181
Cdd:PRK14826 161 VVEGSITTEKkGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRALAVQK 211
PRK14825 PRK14825
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 10-176 7.83e-11

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 173286  Cd Length: 199  Bit Score: 58.79  E-value: 7.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682  10 FVTGNAKKLQEVQQILgqgfpfELTNRKIDLPEL--QGEPEDISREKCRLAAAEV------KGPVMVEDTSLCFNALHGL 81
Cdd:PRK14825   6 FATTNINKINEVKQIL------DIPNIKIEIPQNfdIKETGKTFKENSLLKAKALfeilnnKQPVFSEDSGLCIEALNLE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682  82 PGPYIKWF----------LDKTGHVGLnNLLAAYPDKSAYAQCIFAFTTGPGaEIQTFVGRTEGKI---VPARGPTDFGW 148
Cdd:PRK14825  80 PGIYSKRYdqyklgkklsTNEKNHLII-DLMKNEKNRTAYFICNISYISKDG-TILNFEGIIKGTIalsIDDYKKNGFGY 157

                        170       180
                 ....*....|....*....|....*...
gi 353558682 149 DPVFQPDGfEETYAEMDKTIKNSISHRG 176
Cdd:PRK14825 158 DPIFLTKN-NKRLSELTLEEKNKISHRG 184
PRK02491 PRK02491
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; ...
 8-186 1.97e-08

putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed


Pssm-ID: 179431 [Multi-domain]  Cd Length: 328  Bit Score: 52.89  E-value: 1.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682   8 ITFVTGNAKKLQEVQQILGQ-GFPFELTNRKIDLPELQgEPEDISREKCRLAA---AEVKGP-VMVEDTSLCFNALHGLP 82
Cdd:PRK02491 130 ILIATRNEGKTKEFRKLFGKlGYKVENLNDYPDLPEVA-ETGMTFEENARLKAetiSRLTGKmVLADDSGLKVDALGGLP 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558682  83 GPYIKWF-----LDKTGHVGLNNLLAA---YPDKSAYAQCIFAfTTGPGAEIQTFVGRTEGKI-VPARGPTDFGWDPVFQ 153
Cdd:PRK02491 209 GVWSARFsgpdaTDAENNAKLLHELAMvfdLKDRSAQFHTTLV-VAAPNKDSLVVEADWPGYIaTEPKGENGFGYDPLFL 287

                        170       180       190
                 ....*....|....*....|....*....|...
gi 353558682 154 PDGFEETYAEMDKTIKNSISHRGRSLSALCAYF 186
Cdd:PRK02491 288 VGETGRHAAELTAEEKNQLSHRGQAVKKLMEVF 320
 
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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