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Conserved domains on  [gi|31657144|ref|NP_852470|]
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inosine triphosphate pyrophosphatase isoform b [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/ ...
 8-171 2.40e-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: 215.85  E-value: 2.40e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144   8 QILGDkFPCTLVAQK--IDLPEYQGEPDEISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLPGPYIKWFLE----KLKPE 81
Cdd:cd00515  16 EILAP-FGIEVVSLKdiIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVYSARFAGehddAENNE 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144  82 GLHQLLAGFEDKSAYALCTFALStgDPSQPVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSH 160
Cdd:cd00515  95 KLLELLEGDEDRSAYFVCVIALV--DPDGEPLVFEGEVEGKIVtEPRGTGGFGYDPIFIPEGYGKTFAEMSPEEKNAISH 172

                       170
                ....*....|.
gi 31657144 161 RFRALLELQEY 171
Cdd:cd00515 173 RGKALRKLKEF 183
 
Name Accession Description Interval E-value
HAM1 cd00515
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ...
 8-171 2.40e-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: 215.85  E-value: 2.40e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144   8 QILGDkFPCTLVAQK--IDLPEYQGEPDEISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLPGPYIKWFLE----KLKPE 81
Cdd:cd00515  16 EILAP-FGIEVVSLKdiIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVYSARFAGehddAENNE 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144  82 GLHQLLAGFEDKSAYALCTFALStgDPSQPVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSH 160
Cdd:cd00515  95 KLLELLEGDEDRSAYFVCVIALV--DPDGEPLVFEGEVEGKIVtEPRGTGGFGYDPIFIPEGYGKTFAEMSPEEKNAISH 172

                       170
                ....*....|.
gi 31657144 161 RFRALLELQEY 171
Cdd:cd00515 173 RGKALRKLKEF 183
Ham1p_like pfam01725
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ...
 8-171 3.96e-63

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: 192.67  E-value: 3.96e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144     8 QILGDKFPCTLVAQK---IDLPEYQGEPDEISIQKCQEAVRQvQGPVLVEDTCLCFNALGGLPGPYIKWFLEKLKP--EG 82
Cdd:pfam01725  16 AILADGIEVLSLKDLgelPEIEETGGTFEENALIKARAAAKT-GLPVLADDSGLEVDALNGFPGVYSARFAGEGGDdeAN 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144    83 LHQLLAGF----EDKSAYALCTFALStgDPSQPVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNA 157
Cdd:pfam01725  95 NAKLLEELevpdEDRSARFVCVIALA--DPGGPELVFEGEVEGEIVeEPRGEGGFGYDPIFIPPEGGKTFAELSPEEKNA 172

                         170
                  ....*....|....
gi 31657144   158 VSHRFRALLELQEY 171
Cdd:pfam01725 173 ISHRGKALRKLKEF 186
RdgB COG0127
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ...
 8-172 1.06e-49

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


Pssm-ID: 439897 [Multi-domain]  Cd Length: 191  Bit Score: 158.69  E-value: 1.06e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144   8 QILGDkFPCTLVAQK-IDLPE--YQGE-PDEISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLPGPYIKWFL-----EKL 78
Cdd:COG0127  17 ALLAP-LGIEVVSLSdLGLPEpeETGDtFEENALIKARAAAKATGLPALADDSGLEVDALGGAPGVYSARYAgegadDEA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144  79 KPEGLHQLLAGF-EDKSAYALCTFALSTGDPSqpVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQTYAEMPKAEKN 156
Cdd:COG0127  96 NNEKLLKLLEGVdEDRRARFVCVLALADPDGE--PLVFEGEVEGEIAeEPRGEGGFGYDPIFIPDGYGKTFAELSPEEKN 173

                       170
                ....*....|....*.
gi 31657144 157 AVSHRFRALLELQEYF 172
Cdd:COG0127 174 AISHRGRALRKLAEWL 189
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
 7-171 2.69e-44

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: 144.82  E-value: 2.69e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144     7 VQILGDKFPCTLVAQ-KIDLPEYQGEP-DEISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLPGPYIKWFLEKLK--PEG 82
Cdd:TIGR00042  15 VQSILSDLGDNEIEQlDLGYPEETGLTfEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGIYSARYQGTDIgnLEK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144    83 LHQLLAGFEDKSAYALCTFALStgDPSQPVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHR 161
Cdd:TIGR00042  95 ILKLLEGVENRQAYFVCVIGYC--DPNGEPLVFEGIVKGKITrEPRGTYGFGYDPIFIPPEEGKTFAELTTEEKNKISHR 172

                         170
                  ....*....|
gi 31657144   162 FRALLELQEY 171
Cdd:TIGR00042 173 GKAFKKFKKF 182
PRK14821 PRK14821
XTP/dITP diphosphatase;
9-172 6.46e-35

XTP/dITP diphosphatase;


Pssm-ID: 184834 [Multi-domain]  Cd Length: 184  Bit Score: 120.83  E-value: 6.46e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144    9 ILGDkFPCTLVAQKIDLPEYQ-GEPDEISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLPGPYIKWFLEKLKPEGLHQLL 87
Cdd:PRK14821  19 ILKP-LGIEVEQIKIEYPEIQaDTLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPGPYSAFVYKTLGNEGILKLL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144   88 AGFEDKSAY-----ALCtfalstgDPSQpVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHR 161
Cdd:PRK14821  98 EGEENRRAYfksviGYC-------DPGG-EKLFTGIVEGKIAnEIRGKGGFGYDPIFIPEGEEKTFAEMTTEEKNKISHR 169

                        170
                 ....*....|.
gi 31657144  162 FRALLELQEYF 172
Cdd:PRK14821 170 KRAFDEFKEWL 180
 
Name Accession Description Interval E-value
HAM1 cd00515
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ...
 8-171 2.40e-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: 215.85  E-value: 2.40e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144   8 QILGDkFPCTLVAQK--IDLPEYQGEPDEISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLPGPYIKWFLE----KLKPE 81
Cdd:cd00515  16 EILAP-FGIEVVSLKdiIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVYSARFAGehddAENNE 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144  82 GLHQLLAGFEDKSAYALCTFALStgDPSQPVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSH 160
Cdd:cd00515  95 KLLELLEGDEDRSAYFVCVIALV--DPDGEPLVFEGEVEGKIVtEPRGTGGFGYDPIFIPEGYGKTFAEMSPEEKNAISH 172

                       170
                ....*....|.
gi 31657144 161 RFRALLELQEY 171
Cdd:cd00515 173 RGKALRKLKEF 183
Ham1p_like pfam01725
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ...
 8-171 3.96e-63

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: 192.67  E-value: 3.96e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144     8 QILGDKFPCTLVAQK---IDLPEYQGEPDEISIQKCQEAVRQvQGPVLVEDTCLCFNALGGLPGPYIKWFLEKLKP--EG 82
Cdd:pfam01725  16 AILADGIEVLSLKDLgelPEIEETGGTFEENALIKARAAAKT-GLPVLADDSGLEVDALNGFPGVYSARFAGEGGDdeAN 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144    83 LHQLLAGF----EDKSAYALCTFALStgDPSQPVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNA 157
Cdd:pfam01725  95 NAKLLEELevpdEDRSARFVCVIALA--DPGGPELVFEGEVEGEIVeEPRGEGGFGYDPIFIPPEGGKTFAELSPEEKNA 172

                         170
                  ....*....|....
gi 31657144   158 VSHRFRALLELQEY 171
Cdd:pfam01725 173 ISHRGKALRKLKEF 186
RdgB COG0127
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ...
 8-172 1.06e-49

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


Pssm-ID: 439897 [Multi-domain]  Cd Length: 191  Bit Score: 158.69  E-value: 1.06e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144   8 QILGDkFPCTLVAQK-IDLPE--YQGE-PDEISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLPGPYIKWFL-----EKL 78
Cdd:COG0127  17 ALLAP-LGIEVVSLSdLGLPEpeETGDtFEENALIKARAAAKATGLPALADDSGLEVDALGGAPGVYSARYAgegadDEA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144  79 KPEGLHQLLAGF-EDKSAYALCTFALSTGDPSqpVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQTYAEMPKAEKN 156
Cdd:COG0127  96 NNEKLLKLLEGVdEDRRARFVCVLALADPDGE--PLVFEGEVEGEIAeEPRGEGGFGYDPIFIPDGYGKTFAELSPEEKN 173

                       170
                ....*....|....*.
gi 31657144 157 AVSHRFRALLELQEYF 172
Cdd:COG0127 174 AISHRGRALRKLAEWL 189
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
 7-171 2.69e-44

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: 144.82  E-value: 2.69e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144     7 VQILGDKFPCTLVAQ-KIDLPEYQGEP-DEISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLPGPYIKWFLEKLK--PEG 82
Cdd:TIGR00042  15 VQSILSDLGDNEIEQlDLGYPEETGLTfEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGIYSARYQGTDIgnLEK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144    83 LHQLLAGFEDKSAYALCTFALStgDPSQPVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHR 161
Cdd:TIGR00042  95 ILKLLEGVENRQAYFVCVIGYC--DPNGEPLVFEGIVKGKITrEPRGTYGFGYDPIFIPPEEGKTFAELTTEEKNKISHR 172

                         170
                  ....*....|
gi 31657144   162 FRALLELQEY 171
Cdd:TIGR00042 173 GKAFKKFKKF 182
PRK14821 PRK14821
XTP/dITP diphosphatase;
9-172 6.46e-35

XTP/dITP diphosphatase;


Pssm-ID: 184834 [Multi-domain]  Cd Length: 184  Bit Score: 120.83  E-value: 6.46e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144    9 ILGDkFPCTLVAQKIDLPEYQ-GEPDEISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLPGPYIKWFLEKLKPEGLHQLL 87
Cdd:PRK14821  19 ILKP-LGIEVEQIKIEYPEIQaDTLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPGPYSAFVYKTLGNEGILKLL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144   88 AGFEDKSAY-----ALCtfalstgDPSQpVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHR 161
Cdd:PRK14821  98 EGEENRRAYfksviGYC-------DPGG-EKLFTGIVEGKIAnEIRGKGGFGYDPIFIPEGEEKTFAEMTTEEKNKISHR 169

                        170
                 ....*....|.
gi 31657144  162 FRALLELQEYF 172
Cdd:PRK14821 170 KRAFDEFKEWL 180
PRK00120 PRK00120
dITP/XTP pyrophosphatase; Reviewed
 8-177 8.34e-31

dITP/XTP pyrophosphatase; Reviewed


Pssm-ID: 234648 [Multi-domain]  Cd Length: 196  Bit Score: 110.56  E-value: 8.34e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144    8 QILGDkFPCTLVAQKiDLPEYqgEPDEI-------SIQKCQEAVRQVQGPVLVEDTCLCFNALGGLPGPY-IKWF----- 74
Cdd:PRK00120  18 ALLAP-FGIEVVSQG-ELGVP--EPEETgttfvenALIKARHAAKATGLPALADDSGLCVDALGGAPGVYsARYAgegas 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144   75 ----LEKLkpegLHQLLA-GFEDKSAYALCTFALSTGDPSqpVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQTYA 148
Cdd:PRK00120  94 daanNEKL----LEELKGvPDEDRRARFVCVLVLVRPDPT--PLVAEGRWEGEILwEPRGENGFGYDPIFFPPGYGKTFA 167

                        170       180
                 ....*....|....*....|....*....
gi 31657144  149 EMPKAEKNAVSHRFRALLELQEYFGSLAA 177
Cdd:PRK00120 168 ELTPEEKNAISHRGKALKLLLEALRELLA 196
PRK14822 PRK14822
XTP/dITP diphosphatase;
33-175 5.81e-26

XTP/dITP diphosphatase;


Pssm-ID: 184835 [Multi-domain]  Cd Length: 200  Bit Score: 98.04  E-value: 5.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144   33 DEISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLPGPYIKWF----------LEKLKPEglhqlLAG--FEDKSAYALCT 100
Cdd:PRK14822  48 EENAILKAEAAAKALNKPVIADDSGLEVDALNGAPGVYSARYageakddaanNEKLLKE-----LGGvpFEKRTARFHCV 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31657144  101 FALSTgdPSQPVRLFRGRTSGRIV-APRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFRALLELQEYFGSL 175
Cdd:PRK14822 123 IAVAF--PGGETKTVEGTCEGEILeEPRGENGFGYDPLFYVPEKGKTMAELSSEEKNAISHRGKALKKLEAELPEW 196
PRK14824 PRK14824
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 34-175 1.93e-19

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 237824 [Multi-domain]  Cd Length: 201  Bit Score: 81.34  E-value: 1.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144   34 EISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLPGPY------IKW---FLEKL-KPEG----LHQLLAGFEDKSAYALC 99
Cdd:PRK14824  45 ENAYLKARAYAEFYKIPVLADDSGLEVPALEGYPGVYssrfyqIEFggkEEVVEsKDEAnirkLLRLLEGKQNRKARFVA 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144  100 TFALSTGDpsqpVRLF-RGRTSGRIVA-PRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFRA---LLELQEYFGS 174
Cdd:PRK14824 125 FVVLYFGD----WGIWtEGECRGKIAEePRGSGGFGYDPVFIPEGYNKTMAELSPEEKNKISHRGKAvrkLVEILKYGGM 200


                 .
gi 31657144  175 L 175
Cdd:PRK14824 201 L 201
PRK14823 PRK14823
putative deoxyribonucleoside-triphosphatase; Provisional
 24-175 4.25e-19

putative deoxyribonucleoside-triphosphatase; Provisional


Pssm-ID: 237823 [Multi-domain]  Cd Length: 191  Bit Score: 80.11  E-value: 4.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144   24 DLPEYQGEPDEISIQKCQEAVRQVQGPVLVEDTCLCFNALGGLPGPYIKWF----------LEKLkpegLHQLlAGFEDK 93
Cdd:PRK14823  37 DIPETADTLEGNALLKAEYVYKKYGYDCFADDTGLEVEALNGAPGVYSARYaggehnaeanMRKL----LEEL-EGKDNR 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144   94 SAYALCTFALSTgDPSQpvRLFRGRTSGRIVA-PRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFRALLELQEYF 172
Cdd:PRK14823 112 KAQFRTVIALIL-DGKE--HLFEGIIKGEIIKeKRGDSGFGYDPIFVPEGYDKTFAELGLEIKNQISHRAKAVQKLIDFL 188


                 ...
gi 31657144  173 GSL 175
Cdd:PRK14823 189 SKA 191
Maf_Ham1 cd00985
Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum ...
 7-123 6.98e-19

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: 77.93  E-value: 6.98e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144   7 VQILGDKFPCTLVAQKIDLPEYQGE------PDEISIQKCQEAVRQVQG-PVLVEDTCLCFNalgGLPGPYIKWFLEKLK 79
Cdd:cd00985  11 LEELKQIGGIEFEVLPSDIDETGLKgepedtVEELALLKARAVAERLPDaPVIADDTGLVVD---GRPGGKPARFAEALE 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 31657144  80 peglhqLLAGFEDKSAYALCTFALStgDPSQPVRLFRGRTSGRI 123
Cdd:cd00985  88 ------MLRGLSGRTAEFVTAVALV--DPDGKIITFEGETEGKI 123
PRK14826 PRK14826
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 52-165 1.38e-12

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 173287  Cd Length: 222  Bit Score: 63.15  E-value: 1.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144   52 LVEDTCLCFNALGGLPGPYIKWFL---EKLKP---EGLHQLL---AGFEDKSAYALCTFALSTGDPS-QPVRLFR----G 117
Cdd:PRK14826  81 LADDTGLEVDALGGAPGVYSARFApvpEGEKPtyeDNVRHLLsemEGKTERSARFRTVIALKGRLPGkNGAFEFEetaeG 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 31657144  118 RTSGRIV-APRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFRAL 165
Cdd:PRK14826 161 VVEGSITtEKKGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRALAV 209
PRK02491 PRK02491
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; ...
 24-172 1.52e-10

putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed


Pssm-ID: 179431 [Multi-domain]  Cd Length: 328  Bit Score: 58.67  E-value: 1.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144   24 DLPEYQ--GEPDEISIQKCQEAVRQVQGP-VLVEDTCLCFNALGGLPGPYIKWFL------EKLKPEGLHQLLAGFE--D 92
Cdd:PRK02491 162 DLPEVAetGMTFEENARLKAETISRLTGKmVLADDSGLKVDALGGLPGVWSARFSgpdatdAENNAKLLHELAMVFDlkD 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144   93 KSAYALCTFALSTgdPSQPVRLFRGRTSGRI-VAPRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFRALLELQEY 171
Cdd:PRK02491 242 RSAQFHTTLVVAA--PNKDSLVVEADWPGYIaTEPKGENGFGYDPLFLVGETGRHAAELTAEEKNQLSHRGQAVKKLMEV 319


                 .
gi 31657144  172 F 172
Cdd:PRK02491 320 F 320
PRK14825 PRK14825
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 50-172 6.19e-06

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 173286  Cd Length: 199  Bit Score: 44.54  E-value: 6.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657144   50 PVLVEDTCLCFNALGGLPGPYIKWF-----LEKLKPEGLHQLLAGF----EDKSAYALCTFALSTGDPSqpVRLFRGRTS 120
Cdd:PRK14825  63 PVFSEDSGLCIEALNLEPGIYSKRYdqyklGKKLSTNEKNHLIIDLmkneKNRTAYFICNISYISKDGT--ILNFEGIIK 140

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 31657144  121 GRIVAPRGCQD---FGWDPCFQPDGyEQTYAEMPKAEKNAVSHRFRALLELQEYF 172
Cdd:PRK14825 141 GTIALSIDDYKkngFGYDPIFLTKN-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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