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Conserved domains on  [gi|353558693|sp|D0MY11|]
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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/ ...
 8-184 3.64e-74

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: 221.24  E-value: 3.64e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693   8 LTFVTGNANKLKEVVAILGaDFPFELRNQ--AVDLPELQGEPADIAKEKCRLAAKQVQGAVLVEDTSLCFNALKGLPGPY 85
Cdd:cd00515    1 IVFATGNKGKLKEFKEILA-PFGIEVVSLkdIIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693  86 IKWFLE----KTGHDGLNNMLAAYEDKSAYAQCIFAYAPAGAEPQVFVGQTHGKIV-PARGPTTFGWDPVFQPDGFEQTY 160
Cdd:cd00515   80 SARFAGehddAENNEKLLELLEGDEDRSAYFVCVIALVDPDGEPLVFEGEVEGKIVtEPRGTGGFGYDPIFIPEGYGKTF 159

                        170       180
                 ....*....|....*....|....
gi 353558693 161 AEMEKVTKNQISHRYKALEALKTH 184
Cdd:cd00515  160 AEMSPEEKNAISHRGKALRKLKEF 183
 
Name Accession Description Interval E-value
HAM1 cd00515
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ...
 8-184 3.64e-74

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: 221.24  E-value: 3.64e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693   8 LTFVTGNANKLKEVVAILGaDFPFELRNQ--AVDLPELQGEPADIAKEKCRLAAKQVQGAVLVEDTSLCFNALKGLPGPY 85
Cdd:cd00515    1 IVFATGNKGKLKEFKEILA-PFGIEVVSLkdIIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693  86 IKWFLE----KTGHDGLNNMLAAYEDKSAYAQCIFAYAPAGAEPQVFVGQTHGKIV-PARGPTTFGWDPVFQPDGFEQTY 160
Cdd:cd00515   80 SARFAGehddAENNEKLLELLEGDEDRSAYFVCVIALVDPDGEPLVFEGEVEGKIVtEPRGTGGFGYDPIFIPEGYGKTF 159

                        170       180
                 ....*....|....*....|....
gi 353558693 161 AEMEKVTKNQISHRYKALEALKTH 184
Cdd:cd00515  160 AEMSPEEKNAISHRGKALRKLKEF 183
Ham1p_like pfam01725
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ...
 8-182 3.76e-70

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: 211.16  E-value: 3.76e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693    8 LTFVTGNANKLKEVVAILGADFPFELRNQA---VDLPELQGEPADIAKEKCRLAAKQvQGAVLVEDTSLCFNALKGLPGP 84
Cdd:pfam01725   1 IVFATGNAGKLRELKAILADGIEVLSLKDLgelPEIEETGGTFEENALIKARAAAKT-GLPVLADDSGLEVDALNGFPGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693   85 YIKWFLEKTGHDGLNN--MLAAY----EDKSAYAQCIFAYAPAGAEPQVFVGQTHGKIVPA-RGPTTFGWDPVFQPDGFE 157
Cdd:pfam01725  80 YSARFAGEGGDDEANNakLLEELevpdEDRSARFVCVIALADPGGPELVFEGEVEGEIVEEpRGEGGFGYDPIFIPPEGG 159

                         170       180
                  ....*....|....*....|....*
gi 353558693  158 QTYAEMEKVTKNQISHRYKALEALK 182
Cdd:pfam01725 160 KTFAELSPEEKNAISHRGKALRKLK 184
RdgB COG0127
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ...
 8-187 1.44e-56

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


Pssm-ID: 439897 [Multi-domain]  Cd Length: 191  Bit Score: 176.79  E-value: 1.44e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693   8 LTFVTGNANKLKEVVAILgADFPFELRNQA-VDLPE--LQGE-PADIAKEKCRLAAKQVQGAVLVEDTSLCFNALKGLPG 83
Cdd:COG0127    2 LVFATGNAGKLREIRALL-APLGIEVVSLSdLGLPEpeETGDtFEENALIKARAAAKATGLPALADDSGLEVDALGGAPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693  84 PYIKWFLEKTGHDGLNN------MLAAYEDKSAYAQCIFAYAPAGAEPQVFVGQTHGKIV-PARGPTTFGWDPVFQPDGF 156
Cdd:COG0127   81 VYSARYAGEGADDEANNekllklLEGVDEDRRARFVCVLALADPDGEPLVFEGEVEGEIAeEPRGEGGFGYDPIFIPDGY 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 353558693 157 EQTYAEMEKVTKNQISHRYKALEALKTHLVK 187
Cdd:COG0127  161 GKTFAELSPEEKNAISHRGRALRKLAEWLKE 191
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
 8-185 7.90e-49

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: 156.76  E-value: 7.90e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693    8 LTFVTGNANKLKEVVAILgADFPFELRNQA-VDLPELQGEP-ADIAKEKCRLAAKQVQGAVLVEDTSLCFNALKGLPGPY 85
Cdd:TIGR00042   2 IVFATGNPGKLKEVQSIL-SDLGDNEIEQLdLGYPEETGLTfEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGIY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693   86 IKWFLEKT--GHDGLNNMLAAYEDKSAYAQCIFAYAPAGAEPQVFVGQTHGKIVPA-RGPTTFGWDPVFQPDGFEQTYAE 162
Cdd:TIGR00042  81 SARYQGTDigNLEKILKLLEGVENRQAYFVCVIGYCDPNGEPLVFEGIVKGKITREpRGTYGFGYDPIFIPPEEGKTFAE 160

                         170       180
                  ....*....|....*....|...
gi 353558693  163 MEKVTKNQISHRYKALEALKTHL 185
Cdd:TIGR00042 161 LTTEEKNKISHRGKAFKKFKKFL 183
PRK14821 PRK14821
XTP/dITP diphosphatase;
10-185 3.48e-41

XTP/dITP diphosphatase;


Pssm-ID: 184834 [Multi-domain]  Cd Length: 184  Bit Score: 137.39  E-value: 3.48e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693  10 FVTGNANKLKEVVAILgADFPFELRNQAVDLPELQ-GEPADIAKEKCRLAAKQVQGAVLVEDTSLCFNALKGLPGPYIKW 88
Cdd:PRK14821   5 FATGNKGKVEEAKIIL-KPLGIEVEQIKIEYPEIQaDTLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPGPYSAF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693  89 FLEKTGHDGLNNMLAAYEDKSAYAQCIFAYAPAGAEPqVFVGQTHGKIV-PARGPTTFGWDPVFQPDGFEQTYAEMEKVT 167
Cdd:PRK14821  84 VYKTLGNEGILKLLEGEENRRAYFKSVIGYCDPGGEK-LFTGIVEGKIAnEIRGKGGFGYDPIFIPEGEEKTFAEMTTEE 162

                        170
                 ....*....|....*...
gi 353558693 168 KNQISHRYKALEALKTHL 185
Cdd:PRK14821 163 KNKISHRKRAFDEFKEWL 180
 
Name Accession Description Interval E-value
HAM1 cd00515
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ...
 8-184 3.64e-74

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: 221.24  E-value: 3.64e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693   8 LTFVTGNANKLKEVVAILGaDFPFELRNQ--AVDLPELQGEPADIAKEKCRLAAKQVQGAVLVEDTSLCFNALKGLPGPY 85
Cdd:cd00515    1 IVFATGNKGKLKEFKEILA-PFGIEVVSLkdIIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693  86 IKWFLE----KTGHDGLNNMLAAYEDKSAYAQCIFAYAPAGAEPQVFVGQTHGKIV-PARGPTTFGWDPVFQPDGFEQTY 160
Cdd:cd00515   80 SARFAGehddAENNEKLLELLEGDEDRSAYFVCVIALVDPDGEPLVFEGEVEGKIVtEPRGTGGFGYDPIFIPEGYGKTF 159

                        170       180
                 ....*....|....*....|....
gi 353558693 161 AEMEKVTKNQISHRYKALEALKTH 184
Cdd:cd00515  160 AEMSPEEKNAISHRGKALRKLKEF 183
Ham1p_like pfam01725
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ...
 8-182 3.76e-70

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: 211.16  E-value: 3.76e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693    8 LTFVTGNANKLKEVVAILGADFPFELRNQA---VDLPELQGEPADIAKEKCRLAAKQvQGAVLVEDTSLCFNALKGLPGP 84
Cdd:pfam01725   1 IVFATGNAGKLRELKAILADGIEVLSLKDLgelPEIEETGGTFEENALIKARAAAKT-GLPVLADDSGLEVDALNGFPGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693   85 YIKWFLEKTGHDGLNN--MLAAY----EDKSAYAQCIFAYAPAGAEPQVFVGQTHGKIVPA-RGPTTFGWDPVFQPDGFE 157
Cdd:pfam01725  80 YSARFAGEGGDDEANNakLLEELevpdEDRSARFVCVIALADPGGPELVFEGEVEGEIVEEpRGEGGFGYDPIFIPPEGG 159

                         170       180
                  ....*....|....*....|....*
gi 353558693  158 QTYAEMEKVTKNQISHRYKALEALK 182
Cdd:pfam01725 160 KTFAELSPEEKNAISHRGKALRKLK 184
RdgB COG0127
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ...
 8-187 1.44e-56

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


Pssm-ID: 439897 [Multi-domain]  Cd Length: 191  Bit Score: 176.79  E-value: 1.44e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693   8 LTFVTGNANKLKEVVAILgADFPFELRNQA-VDLPE--LQGE-PADIAKEKCRLAAKQVQGAVLVEDTSLCFNALKGLPG 83
Cdd:COG0127    2 LVFATGNAGKLREIRALL-APLGIEVVSLSdLGLPEpeETGDtFEENALIKARAAAKATGLPALADDSGLEVDALGGAPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693  84 PYIKWFLEKTGHDGLNN------MLAAYEDKSAYAQCIFAYAPAGAEPQVFVGQTHGKIV-PARGPTTFGWDPVFQPDGF 156
Cdd:COG0127   81 VYSARYAGEGADDEANNekllklLEGVDEDRRARFVCVLALADPDGEPLVFEGEVEGEIAeEPRGEGGFGYDPIFIPDGY 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 353558693 157 EQTYAEMEKVTKNQISHRYKALEALKTHLVK 187
Cdd:COG0127  161 GKTFAELSPEEKNAISHRGRALRKLAEWLKE 191
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
 8-185 7.90e-49

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: 156.76  E-value: 7.90e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693    8 LTFVTGNANKLKEVVAILgADFPFELRNQA-VDLPELQGEP-ADIAKEKCRLAAKQVQGAVLVEDTSLCFNALKGLPGPY 85
Cdd:TIGR00042   2 IVFATGNPGKLKEVQSIL-SDLGDNEIEQLdLGYPEETGLTfEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGIY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693   86 IKWFLEKT--GHDGLNNMLAAYEDKSAYAQCIFAYAPAGAEPQVFVGQTHGKIVPA-RGPTTFGWDPVFQPDGFEQTYAE 162
Cdd:TIGR00042  81 SARYQGTDigNLEKILKLLEGVENRQAYFVCVIGYCDPNGEPLVFEGIVKGKITREpRGTYGFGYDPIFIPPEEGKTFAE 160

                         170       180
                  ....*....|....*....|...
gi 353558693  163 MEKVTKNQISHRYKALEALKTHL 185
Cdd:TIGR00042 161 LTTEEKNKISHRGKAFKKFKKFL 183
PRK14821 PRK14821
XTP/dITP diphosphatase;
10-185 3.48e-41

XTP/dITP diphosphatase;


Pssm-ID: 184834 [Multi-domain]  Cd Length: 184  Bit Score: 137.39  E-value: 3.48e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693  10 FVTGNANKLKEVVAILgADFPFELRNQAVDLPELQ-GEPADIAKEKCRLAAKQVQGAVLVEDTSLCFNALKGLPGPYIKW 88
Cdd:PRK14821   5 FATGNKGKVEEAKIIL-KPLGIEVEQIKIEYPEIQaDTLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPGPYSAF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693  89 FLEKTGHDGLNNMLAAYEDKSAYAQCIFAYAPAGAEPqVFVGQTHGKIV-PARGPTTFGWDPVFQPDGFEQTYAEMEKVT 167
Cdd:PRK14821  84 VYKTLGNEGILKLLEGEENRRAYFKSVIGYCDPGGEK-LFTGIVEGKIAnEIRGKGGFGYDPIFIPEGEEKTFAEMTTEE 162

                        170
                 ....*....|....*...
gi 353558693 168 KNQISHRYKALEALKTHL 185
Cdd:PRK14821 163 KNKISHRKRAFDEFKEWL 180
PRK00120 PRK00120
dITP/XTP pyrophosphatase; Reviewed
 12-185 6.69e-32

dITP/XTP pyrophosphatase; Reviewed


Pssm-ID: 234648 [Multi-domain]  Cd Length: 196  Bit Score: 113.64  E-value: 6.69e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693  12 TGNANKLKEVVAILgADFPFELRNQAvDLPElqGEPADI-------AKEKCRLAAKQVQGAVLVEDTSLCFNALKGLPGP 84
Cdd:PRK00120   7 SHNAGKLRELKALL-APFGIEVVSQG-ELGV--PEPEETgttfvenALIKARHAAKATGLPALADDSGLCVDALGGAPGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693  85 YIKWFLEKTGHDGLNN--MLAA-----YEDKSAYAQCIFAYAPAGAEPQVFVGQTHGKIV-PARGPTTFGWDPVFQPDGF 156
Cdd:PRK00120  83 YSARYAGEGASDAANNekLLEElkgvpDEDRRARFVCVLVLVRPDPTPLVAEGRWEGEILwEPRGENGFGYDPIFFPPGY 162

                        170       180
                 ....*....|....*....|....*....
gi 353558693 157 EQTYAEMEKVTKNQISHRYKALEALKTHL 185
Cdd:PRK00120 163 GKTFAELTPEEKNAISHRGKALKLLLEAL 191
PRK14823 PRK14823
putative deoxyribonucleoside-triphosphatase; Provisional
 8-187 5.93e-26

putative deoxyribonucleoside-triphosphatase; Provisional


Pssm-ID: 237823 [Multi-domain]  Cd Length: 191  Bit Score: 98.22  E-value: 5.93e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693   8 LTFVTGNANKLKEVVAILGADFpfELR-----NQAVDLPElqgePADIAKEKCRLAAKQVQGA----VLVEDTSLCFNAL 78
Cdd:PRK14823   3 LVFATNNKHKLEEIRSILPEKI--ELLslsdiGCHEDIPE----TADTLEGNALLKAEYVYKKygydCFADDTGLEVEAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693  79 KGLPGPYIKWFL--EKTGHDGLNNMLAAYEDK---SAYAQCIFAYAPAGAEpQVFVGQTHGKIVPA-RGPTTFGWDPVFQ 152
Cdd:PRK14823  77 NGAPGVYSARYAggEHNAEANMRKLLEELEGKdnrKAQFRTVIALILDGKE-HLFEGIIKGEIIKEkRGDSGFGYDPIFV 155

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 353558693 153 PDGFEQTYAEMEKVTKNQISHRYKALEALKTHLVK 187
Cdd:PRK14823 156 PEGYDKTFAELGLEIKNQISHRAKAVQKLIDFLSK 190
PRK14822 PRK14822
XTP/dITP diphosphatase;
8-185 1.42e-24

XTP/dITP diphosphatase;


Pssm-ID: 184835 [Multi-domain]  Cd Length: 200  Bit Score: 94.95  E-value: 1.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693   8 LTFVTGNANKLKEVVAILgADFPFELRNQAvDLPEL-----QGEP-ADIAKEKCRLAAKQVQGAVLVEDTSLCFNALKGL 81
Cdd:PRK14822   4 IVIATKNKGKVREFKEIF-EKFDIEVKSLA-DFPPIpeveeTGTTfEENAILKAEAAAKALNKPVIADDSGLEVDALNGA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693  82 PGPYIKWFLEKTGHDGLNN--MLAA-----YEDKSAYAQCIFAYAPAGAEPQVFVGQTHGKIVPA-RGPTTFGWDPVFQP 153
Cdd:PRK14822  82 PGVYSARYAGEAKDDAANNekLLKElggvpFEKRTARFHCVIAVAFPGGETKTVEGTCEGEILEEpRGENGFGYDPLFYV 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 353558693 154 DGFEQTYAEMEKVTKNQISHRYKALEALKTHL 185
Cdd:PRK14822 162 PEKGKTMAELSSEEKNAISHRGKALKKLEAEL 193
PRK14824 PRK14824
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 12-187 1.68e-15

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 237824 [Multi-domain]  Cd Length: 201  Bit Score: 71.33  E-value: 1.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693  12 TGNANKLKEVVAILGA-DFPFELRNQAVDLPELQGEPADIAKEKCRLAAKQVQGAVLVEDTSLCFNALKGLPGPY----- 85
Cdd:PRK14824   7 TTNEGKVREIKRLLSDlGIEVLSPDKKIEVEEDGETFLENAYLKARAYAEFYKIPVLADDSGLEVPALEGYPGVYssrfy 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693  86 -IKW---FLEKTGHDGLNN-----MLAAYEDKSA-YAQCIFAYAPagaEPQVFV-GQTHGKIV-PARGPTTFGWDPVFQP 153
Cdd:PRK14824  87 qIEFggkEEVVESKDEANIrkllrLLEGKQNRKArFVAFVVLYFG---DWGIWTeGECRGKIAeEPRGSGGFGYDPVFIP 163

                        170       180       190
                 ....*....|....*....|....*....|....
gi 353558693 154 DGFEQTYAEMEKVTKNQISHRYKALEALKtHLVK 187
Cdd:PRK14824 164 EGYNKTMAELSPEEKNKISHRGKAVRKLV-EILK 196
PRK14826 PRK14826
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 1-180 9.77e-13

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 173287  Cd Length: 222  Bit Score: 63.92  E-value: 9.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693   1 MSSAKPVLTFV--TGNANKLKEVVAILGADFP-------FELrNQAVDLPELQGEPADIAKEKCR-----LAAKQVQGAV 66
Cdd:PRK14826   2 PQIATETITIVlaTGNRDKVRELRPLLEHISPlfsvrslADL-GVEVDIEETEETLEGNALLKADaifelLSDRFPFLIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693  67 LVEDTSLCFNALKGLPGPYIKWF------LEKTGHDGLNNMLAAYE---DKSAYAQCIFAYA---PAGAEPQVF----VG 130
Cdd:PRK14826  81 LADDTGLEVDALGGAPGVYSARFapvpegEKPTYEDNVRHLLSEMEgktERSARFRTVIALKgrlPGKNGAFEFeetaEG 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 353558693 131 QTHGKIVPAR-GPTTFGWDPVFQPDGFEQTYAEMEKVTKNQISHRYKALEA 180
Cdd:PRK14826 161 VVEGSITTEKkGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRALAVQK 211
PRK02491 PRK02491
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; ...
 7-181 1.73e-12

putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed


Pssm-ID: 179431 [Multi-domain]  Cd Length: 328  Bit Score: 64.45  E-value: 1.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693   7 VLTFVTGNANKLKEVVAILGA-DFPFELRNQAVDLPELQgEPADIAKEKCRLAAK---QVQGA-VLVEDTSLCFNALKGL 81
Cdd:PRK02491 129 TILIATRNEGKTKEFRKLFGKlGYKVENLNDYPDLPEVA-ETGMTFEENARLKAEtisRLTGKmVLADDSGLKVDALGGL 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693  82 PGPYIKWFLEKTGHDGLNN--------MLAAYEDKSAYAQCIFAYAPAGAEPQVFVGQTHGKI-VPARGPTTFGWDPVFQ 152
Cdd:PRK02491 208 PGVWSARFSGPDATDAENNakllhelaMVFDLKDRSAQFHTTLVVAAPNKDSLVVEADWPGYIaTEPKGENGFGYDPLFL 287

                        170       180
                 ....*....|....*....|....*....
gi 353558693 153 PDGFEQTYAEMEKVTKNQISHRYKALEAL 181
Cdd:PRK02491 288 VGETGRHAAELTAEEKNQLSHRGQAVKKL 316
PRK14825 PRK14825
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 8-190 3.14e-11

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 173286  Cd Length: 199  Bit Score: 59.56  E-value: 3.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693   8 LTFVTGNANKLKEVVAILgaDFPfelrNQAVDLPEL--QGEPADIAKEKCRLAAKQV------QGAVLVEDTSLCFNALK 79
Cdd:PRK14825   4 LFFATTNINKINEVKQIL--DIP----NIKIEIPQNfdIKETGKTFKENSLLKAKALfeilnnKQPVFSEDSGLCIEALN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353558693  80 GLPGPYIKWF-----LEKTGHDGLN----NMLAAYEDKSAYAQCIFAYAPAGAEPQVFVGQTHGKI---VPARGPTTFGW 147
Cdd:PRK14825  78 LEPGIYSKRYdqyklGKKLSTNEKNhliiDLMKNEKNRTAYFICNISYISKDGTILNFEGIIKGTIalsIDDYKKNGFGY 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 353558693 148 DPVFQPDGfEQTYAEMEKVTKNQISHRYKALEALKTHLVKPVD 190
Cdd:PRK14825 158 DPIFLTKN-NKRLSELTLEEKNKISHRGIAFDKFKKFLMQSLF 199
 
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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