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Conserved domains on  [gi|31982664|ref|NP_080198|]
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inosine triphosphate pyrophosphatase isoform 1 [Mus musculus]

Protein Classification

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

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

CATH:  3.90.950.10
EC:  3.6.1.-
Gene Ontology:  GO:0047429|GO:0009146|GO:0000166
PubMed:  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/ ...
 10-188 4.92e-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: 238.57  E-value: 4.92e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664  10 IVFVTGNAKKLEEVIQILGDnFPCTLEAQK--IDLPEYQGEPDEISIQKCREAARQVQGPVLVEDTCLCFNALGGLPGPY 87
Cdd:cd00515   1 IVFATGNKGKLKEFKEILAP-FGIEVVSLKdiIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664  88 IKWFLQ----KLKPEGLHQLLAGFEDKSAYALCTFALStgDPSQPVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQ 162
Cdd:cd00515  80 SARFAGehddAENNEKLLELLEGDEDRSAYFVCVIALV--DPDGEPLVFEGEVEGKIVTePRGTGGFGYDPIFIPEGYGK 157

                       170       180
                ....*....|....*....|....*.
gi 31982664 163 TYAEMPKSEKNTISHRFRALHKLQEY 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 4.92e-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: 238.57  E-value: 4.92e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664  10 IVFVTGNAKKLEEVIQILGDnFPCTLEAQK--IDLPEYQGEPDEISIQKCREAARQVQGPVLVEDTCLCFNALGGLPGPY 87
Cdd:cd00515   1 IVFATGNKGKLKEFKEILAP-FGIEVVSLKdiIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664  88 IKWFLQ----KLKPEGLHQLLAGFEDKSAYALCTFALStgDPSQPVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQ 162
Cdd:cd00515  80 SARFAGehddAENNEKLLELLEGDEDRSAYFVCVIALV--DPDGEPLVFEGEVEGKIVTePRGTGGFGYDPIFIPEGYGK 157

                       170       180
                ....*....|....*....|....*.
gi 31982664 163 TYAEMPKSEKNTISHRFRALHKLQEY 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 2.96e-75

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: 224.25  E-value: 2.96e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664    10 IVFVTGNAKKLEEVIQILGDNFPCTLEAQK---IDLPEYQGEPDEISIQKCREAARQvQGPVLVEDTCLCFNALGGLPGP 86
Cdd:pfam01725   1 IVFATGNAGKLRELKAILADGIEVLSLKDLgelPEIEETGGTFEENALIKARAAAKT-GLPVLADDSGLEVDALNGFPGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664    87 YIKWFLQKLKP--EGLHQLLAGF----EDKSAYALCTFALStgDPSQPVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDG 159
Cdd:pfam01725  80 YSARFAGEGGDdeANNAKLLEELevpdEDRSARFVCVIALA--DPGGPELVFEGEVEGEIVEePRGEGGFGYDPIFIPPE 157

                         170       180
                  ....*....|....*....|....*....
gi 31982664   160 YEQTYAEMPKSEKNTISHRFRALHKLQEY 188
Cdd:pfam01725 158 GGKTFAELSPEEKNAISHRGKALRKLKEF 186
RdgB COG0127
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ...
 9-189 3.03e-61

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


Pssm-ID: 439897 [Multi-domain]  Cd Length: 191  Bit Score: 188.73  E-value: 3.03e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664   9 KIVFVTGNAKKLEEVIQILGDnFPCTLEAQK-IDLPE--YQGE-PDEISIQKCREAARQVQGPVLVEDTCLCFNALGGLP 84
Cdd:COG0127   1 KLVFATGNAGKLREIRALLAP-LGIEVVSLSdLGLPEpeETGDtFEENALIKARAAAKATGLPALADDSGLEVDALGGAP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664  85 GPYIKWFL-----QKLKPEGLHQLLAGF-EDKSAYALCTFALSTGDPSqpVLLFRGQTSGQIVM-PRGSRDFGWDPCFQP 157
Cdd:COG0127  80 GVYSARYAgegadDEANNEKLLKLLEGVdEDRRARFVCVLALADPDGE--PLVFEGEVEGEIAEePRGEGGFGYDPIFIP 157

                       170       180       190
                ....*....|....*....|....*....|..
gi 31982664 158 DGYEQTYAEMPKSEKNTISHRFRALHKLQEYF 189
Cdd:COG0127 158 DGYGKTFAELSPEEKNAISHRGRALRKLAEWL 189
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
 9-188 4.96e-50

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: 160.22  E-value: 4.96e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664     9 KIVFVTGNAKKLEEVIQILGDNFPCTLEAQKIDLPEYQGEP-DEISIQKCREAARQVQGPVLVEDTCLCFNALGGLPGPY 87
Cdd:TIGR00042   1 KIVFATGNPGKLKEVQSILSDLGDNEIEQLDLGYPEETGLTfEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGIY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664    88 IKWFLQKLK--PEGLHQLLAGFEDKSAYALCTFALStgDPSQPVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQTY 164
Cdd:TIGR00042  81 SARYQGTDIgnLEKILKLLEGVENRQAYFVCVIGYC--DPNGEPLVFEGIVKGKITRePRGTYGFGYDPIFIPPEEGKTF 158

                         170       180
                  ....*....|....*....|....
gi 31982664   165 AEMPKSEKNTISHRFRALHKLQEY 188
Cdd:TIGR00042 159 AELTTEEKNKISHRGKAFKKFKKF 182
PRK14821 PRK14821
XTP/dITP diphosphatase;
9-190 4.83e-43

XTP/dITP diphosphatase;


Pssm-ID: 184834 [Multi-domain]  Cd Length: 184  Bit Score: 142.40  E-value: 4.83e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664    9 KIVFVTGNAKKLEEVIQILGDnFPCTLEAQKIDLPEYQ-GEPDEISIQKCREAARQVQGPVLVEDTCLCFNALGGLPGPY 87
Cdd:PRK14821   2 KIYFATGNKGKVEEAKIILKP-LGIEVEQIKIEYPEIQaDTLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPGPY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664   88 IKWFLQKLKPEGLHQLLAGFEDKSAY-----ALCtfalstgDPSQpVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYE 161
Cdd:PRK14821  81 SAFVYKTLGNEGILKLLEGEENRRAYfksviGYC-------DPGG-EKLFTGIVEGKIANeIRGKGGFGYDPIFIPEGEE 152

                        170       180
                 ....*....|....*....|....*....
gi 31982664  162 QTYAEMPKSEKNTISHRFRALHKLQEYFS 190
Cdd:PRK14821 153 KTFAEMTTEEKNKISHRKRAFDEFKEWLK 181
 
Name Accession Description Interval E-value
HAM1 cd00515
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ...
 10-188 4.92e-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: 238.57  E-value: 4.92e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664  10 IVFVTGNAKKLEEVIQILGDnFPCTLEAQK--IDLPEYQGEPDEISIQKCREAARQVQGPVLVEDTCLCFNALGGLPGPY 87
Cdd:cd00515   1 IVFATGNKGKLKEFKEILAP-FGIEVVSLKdiIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664  88 IKWFLQ----KLKPEGLHQLLAGFEDKSAYALCTFALStgDPSQPVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQ 162
Cdd:cd00515  80 SARFAGehddAENNEKLLELLEGDEDRSAYFVCVIALV--DPDGEPLVFEGEVEGKIVTePRGTGGFGYDPIFIPEGYGK 157

                       170       180
                ....*....|....*....|....*.
gi 31982664 163 TYAEMPKSEKNTISHRFRALHKLQEY 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 2.96e-75

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: 224.25  E-value: 2.96e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664    10 IVFVTGNAKKLEEVIQILGDNFPCTLEAQK---IDLPEYQGEPDEISIQKCREAARQvQGPVLVEDTCLCFNALGGLPGP 86
Cdd:pfam01725   1 IVFATGNAGKLRELKAILADGIEVLSLKDLgelPEIEETGGTFEENALIKARAAAKT-GLPVLADDSGLEVDALNGFPGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664    87 YIKWFLQKLKP--EGLHQLLAGF----EDKSAYALCTFALStgDPSQPVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDG 159
Cdd:pfam01725  80 YSARFAGEGGDdeANNAKLLEELevpdEDRSARFVCVIALA--DPGGPELVFEGEVEGEIVEePRGEGGFGYDPIFIPPE 157

                         170       180
                  ....*....|....*....|....*....
gi 31982664   160 YEQTYAEMPKSEKNTISHRFRALHKLQEY 188
Cdd:pfam01725 158 GGKTFAELSPEEKNAISHRGKALRKLKEF 186
RdgB COG0127
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ...
 9-189 3.03e-61

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


Pssm-ID: 439897 [Multi-domain]  Cd Length: 191  Bit Score: 188.73  E-value: 3.03e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664   9 KIVFVTGNAKKLEEVIQILGDnFPCTLEAQK-IDLPE--YQGE-PDEISIQKCREAARQVQGPVLVEDTCLCFNALGGLP 84
Cdd:COG0127   1 KLVFATGNAGKLREIRALLAP-LGIEVVSLSdLGLPEpeETGDtFEENALIKARAAAKATGLPALADDSGLEVDALGGAP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664  85 GPYIKWFL-----QKLKPEGLHQLLAGF-EDKSAYALCTFALSTGDPSqpVLLFRGQTSGQIVM-PRGSRDFGWDPCFQP 157
Cdd:COG0127  80 GVYSARYAgegadDEANNEKLLKLLEGVdEDRRARFVCVLALADPDGE--PLVFEGEVEGEIAEePRGEGGFGYDPIFIP 157

                       170       180       190
                ....*....|....*....|....*....|..
gi 31982664 158 DGYEQTYAEMPKSEKNTISHRFRALHKLQEYF 189
Cdd:COG0127 158 DGYGKTFAELSPEEKNAISHRGRALRKLAEWL 189
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
 9-188 4.96e-50

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: 160.22  E-value: 4.96e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664     9 KIVFVTGNAKKLEEVIQILGDNFPCTLEAQKIDLPEYQGEP-DEISIQKCREAARQVQGPVLVEDTCLCFNALGGLPGPY 87
Cdd:TIGR00042   1 KIVFATGNPGKLKEVQSILSDLGDNEIEQLDLGYPEETGLTfEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGIY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664    88 IKWFLQKLK--PEGLHQLLAGFEDKSAYALCTFALStgDPSQPVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQTY 164
Cdd:TIGR00042  81 SARYQGTDIgnLEKILKLLEGVENRQAYFVCVIGYC--DPNGEPLVFEGIVKGKITRePRGTYGFGYDPIFIPPEEGKTF 158

                         170       180
                  ....*....|....*....|....
gi 31982664   165 AEMPKSEKNTISHRFRALHKLQEY 188
Cdd:TIGR00042 159 AELTTEEKNKISHRGKAFKKFKKF 182
PRK14821 PRK14821
XTP/dITP diphosphatase;
9-190 4.83e-43

XTP/dITP diphosphatase;


Pssm-ID: 184834 [Multi-domain]  Cd Length: 184  Bit Score: 142.40  E-value: 4.83e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664    9 KIVFVTGNAKKLEEVIQILGDnFPCTLEAQKIDLPEYQ-GEPDEISIQKCREAARQVQGPVLVEDTCLCFNALGGLPGPY 87
Cdd:PRK14821   2 KIYFATGNKGKVEEAKIILKP-LGIEVEQIKIEYPEIQaDTLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPGPY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664   88 IKWFLQKLKPEGLHQLLAGFEDKSAY-----ALCtfalstgDPSQpVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYE 161
Cdd:PRK14821  81 SAFVYKTLGNEGILKLLEGEENRRAYfksviGYC-------DPGG-EKLFTGIVEGKIANeIRGKGGFGYDPIFIPEGEE 152

                        170       180
                 ....*....|....*....|....*....
gi 31982664  162 QTYAEMPKSEKNTISHRFRALHKLQEYFS 190
Cdd:PRK14821 153 KTFAEMTTEEKNKISHRKRAFDEFKEWLK 181
PRK00120 PRK00120
dITP/XTP pyrophosphatase; Reviewed
 8-188 7.52e-38

dITP/XTP pyrophosphatase; Reviewed


Pssm-ID: 234648 [Multi-domain]  Cd Length: 196  Bit Score: 129.43  E-value: 7.52e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664    8 KKIVFVTGNAKKLEEVIQILGDnFPCTLEAQKiDLPEYqgEPDEI-------SIQKCREAARQVQGPVLVEDTCLCFNAL 80
Cdd:PRK00120   1 MKIVLASHNAGKLRELKALLAP-FGIEVVSQG-ELGVP--EPEETgttfvenALIKARHAAKATGLPALADDSGLCVDAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664   81 GGLPGPY--------------IKWFLQKLKPEGlhqllagFEDKSAYALCTFALSTGDPSqpVLLFRGQTSGQIVM-PRG 145
Cdd:PRK00120  77 GGAPGVYsaryagegasdaanNEKLLEELKGVP-------DEDRRARFVCVLVLVRPDPT--PLVAEGRWEGEILWePRG 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 31982664  146 SRDFGWDPCFQPDGYEQTYAEMPKSEKNTISHRFRALHKLQEY 188
Cdd:PRK00120 148 ENGFGYDPIFFPPGYGKTFAELTPEEKNAISHRGKALKLLLEA 190
PRK14822 PRK14822
XTP/dITP diphosphatase;
8-189 2.31e-32

XTP/dITP diphosphatase;


Pssm-ID: 184835 [Multi-domain]  Cd Length: 200  Bit Score: 115.37  E-value: 2.31e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664    8 KKIVFVTGNAKKLEEVIQILGDnFPCTLE--AQKIDLPEYQ--GEP-DEISIQKCREAARQVQGPVLVEDTCLCFNALGG 82
Cdd:PRK14822   2 KEIVIATKNKGKVREFKEIFEK-FDIEVKslADFPPIPEVEetGTTfEENAILKAEAAAKALNKPVIADDSGLEVDALNG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664   83 LPGPY--------------IKWFLQKLkpEGLHQllagfEDKSAYALCTFALSTgdPSQPVLLFRGQTSGQIV-MPRGSR 147
Cdd:PRK14822  81 APGVYsaryageakddaanNEKLLKEL--GGVPF-----EKRTARFHCVIAVAF--PGGETKTVEGTCEGEILeEPRGEN 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 31982664  148 DFGWDPCFQPDGYEQTYAEMPKSEKNTISHRFRALHKLQEYF 189
Cdd:PRK14822 152 GFGYDPLFYVPEKGKTMAELSSEEKNAISHRGKALKKLEAEL 193
PRK14824 PRK14824
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 9-187 4.63e-28

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 237824 [Multi-domain]  Cd Length: 201  Bit Score: 104.46  E-value: 4.63e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664    9 KIVFVTGNAKKLEEVIQILGDnfpctLEAQKIDLPEY-QGEPD-----EISIQKCREAARQVQGPVLVEDTCLCFNALGG 82
Cdd:PRK14824   2 KILLATTNEGKVREIKRLLSD-----LGIEVLSPDKKiEVEEDgetflENAYLKARAYAEFYKIPVLADDSGLEVPALEG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664   83 LPGPYIKWFLQ--------------KLKPEGLHQLLAGFEDKSAYALCTFALSTGDPSqpvLLFRGQTSGQIVM-PRGSR 147
Cdd:PRK14824  77 YPGVYSSRFYQiefggkeevveskdEANIRKLLRLLEGKQNRKARFVAFVVLYFGDWG---IWTEGECRGKIAEePRGSG 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 31982664  148 DFGWDPCFQPDGYEQTYAEMPKSEKNTISHRFRALHKLQE 187
Cdd:PRK14824 154 GFGYDPVFIPEGYNKTMAELSPEEKNKISHRGKAVRKLVE 193
PRK14823 PRK14823
putative deoxyribonucleoside-triphosphatase; Provisional
 8-190 2.07e-27

putative deoxyribonucleoside-triphosphatase; Provisional


Pssm-ID: 237823 [Multi-domain]  Cd Length: 191  Bit Score: 102.45  E-value: 2.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664    8 KKIVFVTGNAKKLEEVIQILGDNFPcTLEAQKI----DLPEYQGEPDEISIQKCREAARQVQGPVLVEDTCLCFNALGGL 83
Cdd:PRK14823   1 MKLVFATNNKHKLEEIRSILPEKIE-LLSLSDIgcheDIPETADTLEGNALLKAEYVYKKYGYDCFADDTGLEVEALNGA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664   84 PGPYIKWF----------LQKLkpegLHQLlAGFEDKSAYALCTFALSTgDPSQpvLLFRGQTSGQIVM-PRGSRDFGWD 152
Cdd:PRK14823  80 PGVYSARYaggehnaeanMRKL----LEEL-EGKDNRKAQFRTVIALIL-DGKE--HLFEGIIKGEIIKeKRGDSGFGYD 151

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 31982664  153 PCFQPDGYEQTYAEMPKSEKNTISHRFRALHKLQEYFS 190
Cdd:PRK14823 152 PIFVPEGYDKTFAELGLEIKNQISHRAKAVQKLIDFLS 189
Maf_Ham1 cd00985
Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum ...
 10-140 6.12e-26

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: 96.80  E-value: 6.12e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664  10 IVFVTGNAKKLEEVIQILGDNFpctlEAQKIDLPEYQGE------PDEISIQKCREAARQVQG-PVLVEDTCLCFNalgG 82
Cdd:cd00985   1 LILASGSPRRLEELKQIGGIEF----EVLPSDIDETGLKgepedtVEELALLKARAVAERLPDaPVIADDTGLVVD---G 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 31982664  83 LPGPYIKWFlqklkpEGLHQLLAGFEDKSAYALCTFALStgDPSQPVLLFRGQTSGQI 140
Cdd:cd00985  74 RPGGKPARF------AEALEMLRGLSGRTAEFVTAVALV--DPDGKIITFEGETEGKI 123
PRK02491 PRK02491
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; ...
 6-189 4.90e-14

putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed


Pssm-ID: 179431 [Multi-domain]  Cd Length: 328  Bit Score: 69.07  E-value: 4.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664    6 VGKKIVFVTGNAKKLEEVIQILGD---------NFPctleaqkiDLPEYQ--GEPDEISIQKCREAARQVQGP-VLVEDT 73
Cdd:PRK02491 126 FGDTILIATRNEGKTKEFRKLFGKlgykvenlnDYP--------DLPEVAetGMTFEENARLKAETISRLTGKmVLADDS 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664   74 CLCFNALGGLPGPYIKWFL------QKLKPEGLHQLLAGFE--DKSAYALCTFALSTgdPSQPVLLFRGQTSGQIVM-PR 144
Cdd:PRK02491 198 GLKVDALGGLPGVWSARFSgpdatdAENNAKLLHELAMVFDlkDRSAQFHTTLVVAA--PNKDSLVVEADWPGYIATePK 275

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 31982664  145 GSRDFGWDPCFQPDGYEQTYAEMPKSEKNTISHRFRALHKLQEYF 189
Cdd:PRK02491 276 GENGFGYDPLFLVGETGRHAAELTAEEKNQLSHRGQAVKKLMEVF 320
PRK14826 PRK14826
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 69-190 5.95e-14

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 173287  Cd Length: 222  Bit Score: 67.38  E-value: 5.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664   69 LVEDTCLCFNALGGLPGPYIKWFL---QKLKP---EGLHQLL---AGFEDKSAYALCTFALSTGDPS-QPVLLFR----G 134
Cdd:PRK14826  81 LADDTGLEVDALGGAPGVYSARFApvpEGEKPtyeDNVRHLLsemEGKTERSARFRTVIALKGRLPGkNGAFEFEetaeG 160

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31982664  135 QTSGQIVM-PRGSRDFGWDPCFQPDGYEQTYAEMPKSEKNTISHRFRALHK----LQEYFS 190
Cdd:PRK14826 161 VVEGSITTeKKGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRALAVQKavkfLRTILS 221
PRK14825 PRK14825
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
 8-189 6.41e-10

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 173286  Cd Length: 199  Bit Score: 56.10  E-value: 6.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664    8 KKIVFVTGNAKKLEEVIQILgDNFPCTLE-AQKIDLPEYQGEPDEISIQKCREAARQV--QGPVLVEDTCLCFNALGGLP 84
Cdd:PRK14825   2 KTLFFATTNINKINEVKQIL-DIPNIKIEiPQNFDIKETGKTFKENSLLKAKALFEILnnKQPVFSEDSGLCIEALNLEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982664   85 GPYIKWFLQ-----KLKPEGLHQLLAGF----EDKSAYALCTFALSTGDPSqpVLLFRGQTSGQIVMP---RGSRDFGWD 152
Cdd:PRK14825  81 GIYSKRYDQyklgkKLSTNEKNHLIIDLmkneKNRTAYFICNISYISKDGT--ILNFEGIIKGTIALSiddYKKNGFGYD 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 31982664  153 PCFQPDGyEQTYAEMPKSEKNTISHRFRALHKLQEYF 189
Cdd:PRK14825 159 PIFLTKN-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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