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Conserved domains on  [gi|15626999|ref|NP_258412|]
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inosine triphosphate pyrophosphatase isoform a [Homo sapiens]

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/ ...
 10-188 2.69e-81

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: 239.35  E-value: 2.69e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999  10 IVFVTGNAKKLEEVVQILGDkFPCTLVAQK--IDLPEYQGEPDEISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLPGPY 87
Cdd:cd00515   1 IVFATGNKGKLKEFKEILAP-FGIEVVSLKdiIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999  88 IKWFLE----KLKPEGLHQLLAGFEDKSAYALCTFALStgDPSQPVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQ 162
Cdd:cd00515  80 SARFAGehddAENNEKLLELLEGDEDRSAYFVCVIALV--DPDGEPLVFEGEVEGKIVtEPRGTGGFGYDPIFIPEGYGK 157

                       170       180
                ....*....|....*....|....*.
gi 15626999 163 TYAEMPKAEKNAVSHRFRALLELQEY 188
Cdd:cd00515 158 TFAEMSPEEKNAISHRGKALRKLKEF 183
 
Name Accession Description Interval E-value
HAM1 cd00515
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ...
 10-188 2.69e-81

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: 239.35  E-value: 2.69e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999  10 IVFVTGNAKKLEEVVQILGDkFPCTLVAQK--IDLPEYQGEPDEISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLPGPY 87
Cdd:cd00515   1 IVFATGNKGKLKEFKEILAP-FGIEVVSLKdiIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999  88 IKWFLE----KLKPEGLHQLLAGFEDKSAYALCTFALStgDPSQPVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQ 162
Cdd:cd00515  80 SARFAGehddAENNEKLLELLEGDEDRSAYFVCVIALV--DPDGEPLVFEGEVEGKIVtEPRGTGGFGYDPIFIPEGYGK 157

                       170       180
                ....*....|....*....|....*.
gi 15626999 163 TYAEMPKAEKNAVSHRFRALLELQEY 188
Cdd:cd00515 158 TFAEMSPEEKNAISHRGKALRKLKEF 183
Ham1p_like pfam01725
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ...
 10-188 3.85e-73

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: 218.86  E-value: 3.85e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999    10 IVFVTGNAKKLEEVVQILGDKFPCTLVAQK---IDLPEYQGEPDEISIQKCQEAVRQvQGPVLVEDTCLCFNALGGLPGP 86
Cdd:pfam01725   1 IVFATGNAGKLRELKAILADGIEVLSLKDLgelPEIEETGGTFEENALIKARAAAKT-GLPVLADDSGLEVDALNGFPGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999    87 YIKWFLEKLKP--EGLHQLLAGF----EDKSAYALCTFALStgDPSQPVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDG 159
Cdd:pfam01725  80 YSARFAGEGGDdeANNAKLLEELevpdEDRSARFVCVIALA--DPGGPELVFEGEVEGEIVeEPRGEGGFGYDPIFIPPE 157

                         170       180
                  ....*....|....*....|....*....
gi 15626999   160 YEQTYAEMPKAEKNAVSHRFRALLELQEY 188
Cdd:pfam01725 158 GGKTFAELSPEEKNAISHRGKALRKLKEF 186
RdgB COG0127
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ...
 9-189 9.37e-60

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


Pssm-ID: 439897 [Multi-domain]  Cd Length: 191  Bit Score: 184.88  E-value: 9.37e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999   9 KIVFVTGNAKKLEEVVQILGDkFPCTLVAQK-IDLPE--YQGE-PDEISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLP 84
Cdd:COG0127   1 KLVFATGNAGKLREIRALLAP-LGIEVVSLSdLGLPEpeETGDtFEENALIKARAAAKATGLPALADDSGLEVDALGGAP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999  85 GPYIKWFL-----EKLKPEGLHQLLAGF-EDKSAYALCTFALSTGDPSqpVRLFRGRTSGRIV-APRGCQDFGWDPCFQP 157
Cdd:COG0127  80 GVYSARYAgegadDEANNEKLLKLLEGVdEDRRARFVCVLALADPDGE--PLVFEGEVEGEIAeEPRGEGGFGYDPIFIP 157

                       170       180       190
                ....*....|....*....|....*....|..
gi 15626999 158 DGYEQTYAEMPKAEKNAVSHRFRALLELQEYF 189
Cdd:COG0127 158 DGYGKTFAELSPEEKNAISHRGRALRKLAEWL 189
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
 9-188 2.02e-51

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: 163.69  E-value: 2.02e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999     9 KIVFVTGNAKKLEEVVQILgDKFPCTLVAQ-KIDLPEYQGEP-DEISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLPGP 86
Cdd:TIGR00042   1 KIVFATGNPGKLKEVQSIL-SDLGDNEIEQlDLGYPEETGLTfEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999    87 YIKWFLEKLK--PEGLHQLLAGFEDKSAYALCTFALStgDPSQPVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQT 163
Cdd:TIGR00042  80 YSARYQGTDIgnLEKILKLLEGVENRQAYFVCVIGYC--DPNGEPLVFEGIVKGKITrEPRGTYGFGYDPIFIPPEEGKT 157

                         170       180
                  ....*....|....*....|....*
gi 15626999   164 YAEMPKAEKNAVSHRFRALLELQEY 188
Cdd:TIGR00042 158 FAELTTEEKNKISHRGKAFKKFKKF 182
PRK14821 PRK14821
XTP/dITP diphosphatase;
9-189 7.42e-43

XTP/dITP diphosphatase;


Pssm-ID: 184834 [Multi-domain]  Cd Length: 184  Bit Score: 141.63  E-value: 7.42e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999    9 KIVFVTGNAKKLEEVVQILGDkFPCTLVAQKIDLPEYQ-GEPDEISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLPGPY 87
Cdd:PRK14821   2 KIYFATGNKGKVEEAKIILKP-LGIEVEQIKIEYPEIQaDTLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPGPY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999   88 IKWFLEKLKPEGLHQLLAGFEDKSAY-----ALCtfalstgDPSQpVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYE 161
Cdd:PRK14821  81 SAFVYKTLGNEGILKLLEGEENRRAYfksviGYC-------DPGG-EKLFTGIVEGKIAnEIRGKGGFGYDPIFIPEGEE 152

                        170       180
                 ....*....|....*....|....*...
gi 15626999  162 QTYAEMPKAEKNAVSHRFRALLELQEYF 189
Cdd:PRK14821 153 KTFAEMTTEEKNKISHRKRAFDEFKEWL 180
 
Name Accession Description Interval E-value
HAM1 cd00515
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ...
 10-188 2.69e-81

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: 239.35  E-value: 2.69e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999  10 IVFVTGNAKKLEEVVQILGDkFPCTLVAQK--IDLPEYQGEPDEISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLPGPY 87
Cdd:cd00515   1 IVFATGNKGKLKEFKEILAP-FGIEVVSLKdiIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999  88 IKWFLE----KLKPEGLHQLLAGFEDKSAYALCTFALStgDPSQPVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQ 162
Cdd:cd00515  80 SARFAGehddAENNEKLLELLEGDEDRSAYFVCVIALV--DPDGEPLVFEGEVEGKIVtEPRGTGGFGYDPIFIPEGYGK 157

                       170       180
                ....*....|....*....|....*.
gi 15626999 163 TYAEMPKAEKNAVSHRFRALLELQEY 188
Cdd:cd00515 158 TFAEMSPEEKNAISHRGKALRKLKEF 183
Ham1p_like pfam01725
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ...
 10-188 3.85e-73

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: 218.86  E-value: 3.85e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999    10 IVFVTGNAKKLEEVVQILGDKFPCTLVAQK---IDLPEYQGEPDEISIQKCQEAVRQvQGPVLVEDTCLCFNALGGLPGP 86
Cdd:pfam01725   1 IVFATGNAGKLRELKAILADGIEVLSLKDLgelPEIEETGGTFEENALIKARAAAKT-GLPVLADDSGLEVDALNGFPGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999    87 YIKWFLEKLKP--EGLHQLLAGF----EDKSAYALCTFALStgDPSQPVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDG 159
Cdd:pfam01725  80 YSARFAGEGGDdeANNAKLLEELevpdEDRSARFVCVIALA--DPGGPELVFEGEVEGEIVeEPRGEGGFGYDPIFIPPE 157

                         170       180
                  ....*....|....*....|....*....
gi 15626999   160 YEQTYAEMPKAEKNAVSHRFRALLELQEY 188
Cdd:pfam01725 158 GGKTFAELSPEEKNAISHRGKALRKLKEF 186
RdgB COG0127
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ...
 9-189 9.37e-60

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


Pssm-ID: 439897 [Multi-domain]  Cd Length: 191  Bit Score: 184.88  E-value: 9.37e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999   9 KIVFVTGNAKKLEEVVQILGDkFPCTLVAQK-IDLPE--YQGE-PDEISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLP 84
Cdd:COG0127   1 KLVFATGNAGKLREIRALLAP-LGIEVVSLSdLGLPEpeETGDtFEENALIKARAAAKATGLPALADDSGLEVDALGGAP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999  85 GPYIKWFL-----EKLKPEGLHQLLAGF-EDKSAYALCTFALSTGDPSqpVRLFRGRTSGRIV-APRGCQDFGWDPCFQP 157
Cdd:COG0127  80 GVYSARYAgegadDEANNEKLLKLLEGVdEDRRARFVCVLALADPDGE--PLVFEGEVEGEIAeEPRGEGGFGYDPIFIP 157

                       170       180       190
                ....*....|....*....|....*....|..
gi 15626999 158 DGYEQTYAEMPKAEKNAVSHRFRALLELQEYF 189
Cdd:COG0127 158 DGYGKTFAELSPEEKNAISHRGRALRKLAEWL 189
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
 9-188 2.02e-51

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: 163.69  E-value: 2.02e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999     9 KIVFVTGNAKKLEEVVQILgDKFPCTLVAQ-KIDLPEYQGEP-DEISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLPGP 86
Cdd:TIGR00042   1 KIVFATGNPGKLKEVQSIL-SDLGDNEIEQlDLGYPEETGLTfEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999    87 YIKWFLEKLK--PEGLHQLLAGFEDKSAYALCTFALStgDPSQPVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQT 163
Cdd:TIGR00042  80 YSARYQGTDIgnLEKILKLLEGVENRQAYFVCVIGYC--DPNGEPLVFEGIVKGKITrEPRGTYGFGYDPIFIPPEEGKT 157

                         170       180
                  ....*....|....*....|....*
gi 15626999   164 YAEMPKAEKNAVSHRFRALLELQEY 188
Cdd:TIGR00042 158 FAELTTEEKNKISHRGKAFKKFKKF 182
PRK14821 PRK14821
XTP/dITP diphosphatase;
9-189 7.42e-43

XTP/dITP diphosphatase;


Pssm-ID: 184834 [Multi-domain]  Cd Length: 184  Bit Score: 141.63  E-value: 7.42e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999    9 KIVFVTGNAKKLEEVVQILGDkFPCTLVAQKIDLPEYQ-GEPDEISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLPGPY 87
Cdd:PRK14821   2 KIYFATGNKGKVEEAKIILKP-LGIEVEQIKIEYPEIQaDTLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPGPY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999   88 IKWFLEKLKPEGLHQLLAGFEDKSAY-----ALCtfalstgDPSQpVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYE 161
Cdd:PRK14821  81 SAFVYKTLGNEGILKLLEGEENRRAYfksviGYC-------DPGG-EKLFTGIVEGKIAnEIRGKGGFGYDPIFIPEGEE 152

                        170       180
                 ....*....|....*....|....*...
gi 15626999  162 QTYAEMPKAEKNAVSHRFRALLELQEYF 189
Cdd:PRK14821 153 KTFAEMTTEEKNKISHRKRAFDEFKEWL 180
PRK00120 PRK00120
dITP/XTP pyrophosphatase; Reviewed
 8-194 3.72e-38

dITP/XTP pyrophosphatase; Reviewed


Pssm-ID: 234648 [Multi-domain]  Cd Length: 196  Bit Score: 129.82  E-value: 3.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999    8 KKIVFVTGNAKKLEEVVQILGDkFPCTLVAQKiDLPEYqgEPDEI-------SIQKCQEAVRQVQGPVLVEDTCLCFNAL 80
Cdd:PRK00120   1 MKIVLASHNAGKLRELKALLAP-FGIEVVSQG-ELGVP--EPEETgttfvenALIKARHAAKATGLPALADDSGLCVDAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999   81 GGLPGPY-IKWF---------LEKLkpegLHQLLA-GFEDKSAYALCTFALSTGDPSqpVRLFRGRTSGRIV-APRGCQD 148
Cdd:PRK00120  77 GGAPGVYsARYAgegasdaanNEKL----LEELKGvPDEDRRARFVCVLVLVRPDPT--PLVAEGRWEGEILwEPRGENG 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 15626999  149 FGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFRALLELQEYFGSLAA 194
Cdd:PRK00120 151 FGYDPIFFPPGYGKTFAELTPEEKNAISHRGKALKLLLEALRELLA 196
PRK14822 PRK14822
XTP/dITP diphosphatase;
8-192 5.64e-31

XTP/dITP diphosphatase;


Pssm-ID: 184835 [Multi-domain]  Cd Length: 200  Bit Score: 111.52  E-value: 5.64e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999    8 KKIVFVTGNAKKLEEVVQILGdKFPCTLV--AQKIDLPEYQ--GEP-DEISIQKCQEAVRQVQGPVLVEDTCLCFNALGG 82
Cdd:PRK14822   2 KEIVIATKNKGKVREFKEIFE-KFDIEVKslADFPPIPEVEetGTTfEENAILKAEAAAKALNKPVIADDSGLEVDALNG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999   83 LPGPYIKWF----------LEKLKPEglhqlLAG--FEDKSAYALCTFALSTgdPSQPVRLFRGRTSGRIV-APRGCQDF 149
Cdd:PRK14822  81 APGVYSARYageakddaanNEKLLKE-----LGGvpFEKRTARFHCVIAVAF--PGGETKTVEGTCEGEILeEPRGENGF 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 15626999  150 GWDPCFQPDGYEQTYAEMPKAEKNAVSHRFRALLELQEYFGSL 192
Cdd:PRK14822 154 GYDPLFYVPEKGKTMAELSSEEKNAISHRGKALKKLEAELPEW 196
PRK14823 PRK14823
putative deoxyribonucleoside-triphosphatase; Provisional
 8-192 3.53e-27

putative deoxyribonucleoside-triphosphatase; Provisional


Pssm-ID: 237823 [Multi-domain]  Cd Length: 191  Bit Score: 101.68  E-value: 3.53e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999    8 KKIVFVTGNAKKLEEVVQILGDKFpcTLVAQK-----IDLPEYQGEPDEISIQKCQEAVRQVQGPVLVEDTCLCFNALGG 82
Cdd:PRK14823   1 MKLVFATNNKHKLEEIRSILPEKI--ELLSLSdigchEDIPETADTLEGNALLKAEYVYKKYGYDCFADDTGLEVEALNG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999   83 LPGPYIKWF----------LEKLkpegLHQLlAGFEDKSAYALCTFALSTgDPSQpvRLFRGRTSGRIVA-PRGCQDFGW 151
Cdd:PRK14823  79 APGVYSARYaggehnaeanMRKL----LEEL-EGKDNRKAQFRTVIALIL-DGKE--HLFEGIIKGEIIKeKRGDSGFGY 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15626999  152 DPCFQPDGYEQTYAEMPKAEKNAVSHRFRALLELQEYFGSL 192
Cdd:PRK14823 151 DPIFVPEGYDKTFAELGLEIKNQISHRAKAVQKLIDFLSKA 191
Maf_Ham1 cd00985
Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum ...
 10-140 1.22e-24

Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum formation in eukaryotes, bacteria and archaea. A Ham1-related protein from Methanococcus jannaschii is a novel NTPase that has been shown to hydrolyze nonstandard nucleotides, such as hypoxanthine/xanthine NTP, but not standard nucleotides.


Pssm-ID: 238485  Cd Length: 131  Bit Score: 93.33  E-value: 1.22e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999  10 IVFVTGNAKKLEEVVQILGDKFpctlVAQKIDLPEYQGE------PDEISIQKCQEAVRQVQG-PVLVEDTCLCFNalgG 82
Cdd:cd00985   1 LILASGSPRRLEELKQIGGIEF----EVLPSDIDETGLKgepedtVEELALLKARAVAERLPDaPVIADDTGLVVD---G 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15626999  83 LPGPYIKWFLEKLKpeglhqLLAGFEDKSAYALCTFALStgDPSQPVRLFRGRTSGRI 140
Cdd:cd00985  74 RPGGKPARFAEALE------MLRGLSGRTAEFVTAVALV--DPDGKIITFEGETEGKI 123
PRK14824 PRK14824
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 9-192 1.85e-23

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 237824 [Multi-domain]  Cd Length: 201  Bit Score: 92.13  E-value: 1.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999    9 KIVFVTGNAKKLEEVVQILGD-KFPCTLVAQKIDLPEYQGEPDEISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLPGPY 87
Cdd:PRK14824   2 KILLATTNEGKVREIKRLLSDlGIEVLSPDKKIEVEEDGETFLENAYLKARAYAEFYKIPVLADDSGLEVPALEGYPGVY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999   88 ------IKW---FLEKLKP-----EGLHQLLAGFEDKSAYALCTFALSTGDpsqpVRLF-RGRTSGRIVA-PRGCQDFGW 151
Cdd:PRK14824  82 ssrfyqIEFggkEEVVESKdeaniRKLLRLLEGKQNRKARFVAFVVLYFGD----WGIWtEGECRGKIAEePRGSGGFGY 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15626999  152 DPCFQPDGYEQTYAEMPKAEKNAVSHRFRA---LLELQEYFGSL 192
Cdd:PRK14824 158 DPVFIPEGYNKTMAELSPEEKNKISHRGKAvrkLVEILKYGGML 201
PRK14826 PRK14826
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 69-182 2.01e-12

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 173287  Cd Length: 222  Bit Score: 63.15  E-value: 2.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999   69 LVEDTCLCFNALGGLPGPYIKWFL---EKLKP---EGLHQLL---AGFEDKSAYALCTFALSTGDPS-QPVRLFR----G 134
Cdd:PRK14826  81 LADDTGLEVDALGGAPGVYSARFApvpEGEKPtyeDNVRHLLsemEGKTERSARFRTVIALKGRLPGkNGAFEFEetaeG 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 15626999  135 RTSGRIV-APRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFRAL 182
Cdd:PRK14826 161 VVEGSITtEKKGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRALAV 209
PRK02491 PRK02491
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; ...
 6-189 4.74e-11

putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed


Pssm-ID: 179431 [Multi-domain]  Cd Length: 328  Bit Score: 60.60  E-value: 4.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999    6 VGKKIVFVTGNAKKLEEVVQILGD---------KFPctlvaqkiDLPEYQ--GEPDEISIQKCQEAVRQVQGP-VLVEDT 73
Cdd:PRK02491 126 FGDTILIATRNEGKTKEFRKLFGKlgykvenlnDYP--------DLPEVAetGMTFEENARLKAETISRLTGKmVLADDS 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999   74 CLCFNALGGLPGPYIKWFL------EKLKPEGLHQLLAGFE--DKSAYALCTFALSTgdPSQPVRLFRGRTSGRI-VAPR 144
Cdd:PRK02491 198 GLKVDALGGLPGVWSARFSgpdatdAENNAKLLHELAMVFDlkDRSAQFHTTLVVAA--PNKDSLVVEADWPGYIaTEPK 275

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 15626999  145 GCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFRALLELQEYF 189
Cdd:PRK02491 276 GENGFGYDPLFLVGETGRHAAELTAEEKNQLSHRGQAVKKLMEVF 320
PRK14825 PRK14825
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 8-189 1.19e-09

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 173286  Cd Length: 199  Bit Score: 55.33  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999    8 KKIVFVTGNAKKLEEVVQILGDKFPCTLVAQKIDLPEYQGEPDEISIQKCQEAVRQV--QGPVLVEDTCLCFNALGGLPG 85
Cdd:PRK14825   2 KTLFFATTNINKINEVKQILDIPNIKIEIPQNFDIKETGKTFKENSLLKAKALFEILnnKQPVFSEDSGLCIEALNLEPG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15626999   86 PYIKWF-----LEKLKPEGLHQLLAGF----EDKSAYALCTFALSTGDPSqpVRLFRGRTSGRIVAPRGCQD---FGWDP 153
Cdd:PRK14825  82 IYSKRYdqyklGKKLSTNEKNHLIIDLmkneKNRTAYFICNISYISKDGT--ILNFEGIIKGTIALSIDDYKkngFGYDP 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 15626999  154 CFQPDGyEQTYAEMPKAEKNAVSHRFRALLELQEYF 189
Cdd:PRK14825 160 IFLTKN-NKRLSELTLEEKNKISHRGIAFDKFKKFL 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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