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Conserved domains on  [gi|6322529|ref|NP_012603|]
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nucleoside triphosphate pyrophosphohydrolase HAM1 [Saccharomyces cerevisiae S288C]

Protein Classification

non-canonical purine NTP pyrophosphatase( domain architecture ID 10794425)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
5-193 1.82e-84

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: 247.66  E-value: 1.82e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529      5 EIVFVTGNANKLKEVQSILTQEVDNnnKTIHLINEaldLEELQDTDLNAIALAKGKQAVAALGKgkPVFVEDTALRFDEF 84
Cdd:TIGR00042   1 KIVFATGNPGKLKEVQSILSDLGDN--EIEQLDLG---YPEETGLTFEENALLKAKHAAKILNK--PVIAEDSGLFVDAL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529     85 NGLPGAYIKWFLK--SMGLEKIVKMLEPFENKNAEAVTTICFADSRGEYHFFQGITRGKIVPS-RGPTTFGWDSIFEPFD 161
Cdd:TIGR00042  74 NGFPGIYSARYQGtdIGNLEKILKLLEGVENRQAYFVCVIGYCDPNGEPLVFEGIVKGKITREpRGTYGFGYDPIFIPPE 153
                         170       180       190
                  ....*....|....*....|....*....|..
gi 6322529    162 sHGLTYAEMSKDAKNAISHRGKAFAQFKEYLY 193
Cdd:TIGR00042 154 -EGKTFAELTTEEKNKISHRGKAFKKFKKFLL 184
 
Name Accession Description Interval E-value
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
5-193 1.82e-84

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: 247.66  E-value: 1.82e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529      5 EIVFVTGNANKLKEVQSILTQEVDNnnKTIHLINEaldLEELQDTDLNAIALAKGKQAVAALGKgkPVFVEDTALRFDEF 84
Cdd:TIGR00042   1 KIVFATGNPGKLKEVQSILSDLGDN--EIEQLDLG---YPEETGLTFEENALLKAKHAAKILNK--PVIAEDSGLFVDAL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529     85 NGLPGAYIKWFLK--SMGLEKIVKMLEPFENKNAEAVTTICFADSRGEYHFFQGITRGKIVPS-RGPTTFGWDSIFEPFD 161
Cdd:TIGR00042  74 NGFPGIYSARYQGtdIGNLEKILKLLEGVENRQAYFVCVIGYCDPNGEPLVFEGIVKGKITREpRGTYGFGYDPIFIPPE 153
                         170       180       190
                  ....*....|....*....|....*....|..
gi 6322529    162 sHGLTYAEMSKDAKNAISHRGKAFAQFKEYLY 193
Cdd:TIGR00042 154 -EGKTFAELTTEEKNKISHRGKAFKKFKKFLL 184
HAM1 cd00515
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ...
6-191 4.83e-68

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: 205.83  E-value: 4.83e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529    6 IVFVTGNANKLKEVQSILtqevdnNNKTIHLI--NEALDLEELQDTdLNAIALAKGKQAVAALGKgkPVFVEDTALRFDE 83
Cdd:cd00515   1 IVFATGNKGKLKEFKEIL------APFGIEVVslKDIIDIEETGST-FEENALLKARAAAEALGL--PVLADDSGLCVDA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529   84 FNGLPGAYIKWFLKS----MGLEKIVKMLEPFENKNAEAVTTICFADSRGEYHFFQGITRGKIV-PSRGPTTFGWDSIFE 158
Cdd:cd00515  72 LNGFPGVYSARFAGEhddaENNEKLLELLEGDEDRSAYFVCVIALVDPDGEPLVFEGEVEGKIVtEPRGTGGFGYDPIFI 151
                       170       180       190
                ....*....|....*....|....*....|...
gi 6322529  159 PfDSHGLTYAEMSKDAKNAISHRGKAFAQFKEY 191
Cdd:cd00515 152 P-EGYGKTFAEMSPEEKNAISHRGKALRKLKEF 183
Ham1p_like pfam01725
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ...
6-191 6.74e-67

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: 203.07  E-value: 6.74e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529      6 IVFVTGNANKLKEVQSILTQEVdnNNKTIHLINEALDLEELQDTdLNAIALAKgkqAVAALGKGKPVFVEDTALRFDEFN 85
Cdd:pfam01725   1 IVFATGNAGKLRELKAILADGI--EVLSLKDLGELPEIEETGGT-FEENALIK---ARAAAKTGLPVLADDSGLEVDALN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529     86 GLPGAYIKWFLK-----SMGLEKIVKMLE-PFENKNAEAVTTICFADSRGEYHFFQGITRGKIVPS-RGPTTFGWDSIFE 158
Cdd:pfam01725  75 GFPGVYSARFAGeggddEANNAKLLEELEvPDEDRSARFVCVIALADPGGPELVFEGEVEGEIVEEpRGEGGFGYDPIFI 154
                         170       180       190
                  ....*....|....*....|....*....|...
gi 6322529    159 PfDSHGLTYAEMSKDAKNAISHRGKAFAQFKEY 191
Cdd:pfam01725 155 P-PEGGKTFAELSPEEKNAISHRGKALRKLKEF 186
RdgB COG0127
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ...
5-192 1.69e-55

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


Pssm-ID: 439897 [Multi-domain]  Cd Length: 191  Bit Score: 174.10  E-value: 1.69e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529    5 EIVFVTGNANKLKEVQSILtqevdnNNKTIHLIN-EALDLEE--LQDTDLNAIALAKGKQAVAALGKgkPVFVEDTALRF 81
Cdd:COG0127   1 KLVFATGNAGKLREIRALL------APLGIEVVSlSDLGLPEpeETGDTFEENALIKARAAAKATGL--PALADDSGLEV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529   82 DEFNGLPGAYIKWFL-----KSMGLEKIVKMLEPF-ENKNAEAVTTICFADSRGEYHFFQGITRGKIVPS-RGPTTFGWD 154
Cdd:COG0127  73 DALGGAPGVYSARYAgegadDEANNEKLLKLLEGVdEDRRARFVCVLALADPDGEPLVFEGEVEGEIAEEpRGEGGFGYD 152
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 6322529  155 SIFEPfDSHGLTYAEMSKDAKNAISHRGKAFAQFKEYL 192
Cdd:COG0127 153 PIFIP-DGYGKTFAELSPEEKNAISHRGRALRKLAEWL 189
PRK14821 PRK14821
XTP/dITP diphosphatase;
5-196 2.50e-41

XTP/dITP diphosphatase;


Pssm-ID: 184834 [Multi-domain]  Cd Length: 184  Bit Score: 137.78  E-value: 2.50e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529     5 EIVFVTGNANKLKEVQSILtQEVDnnnktIHLINEALDLEELQDTDLNAIALAKGKQAVAALGKgkPVFVEDTALRFDEF 84
Cdd:PRK14821   2 KIYFATGNKGKVEEAKIIL-KPLG-----IEVEQIKIEYPEIQADTLEEVAAFGAKWVYNKLNR--PVIVEDSGLFIEAL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529    85 NGLPGAYIKWFLKSMGLEKIVKMLEPFENKNAEAVTTICFADSrGEYHFFQGITRGKIVPS-RGPTTFGWDSIFEPfDSH 163
Cdd:PRK14821  74 NGFPGPYSAFVYKTLGNEGILKLLEGEENRRAYFKSVIGYCDP-GGEKLFTGIVEGKIANEiRGKGGFGYDPIFIP-EGE 151
                        170       180       190
                 ....*....|....*....|....*....|...
gi 6322529   164 GLTYAEMSKDAKNAISHRGKAFAQFKEYLYQND 196
Cdd:PRK14821 152 EKTFAEMTTEEKNKISHRKRAFDEFKEWLKENL 184
 
Name Accession Description Interval E-value
TIGR00042 TIGR00042
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ...
5-193 1.82e-84

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: 247.66  E-value: 1.82e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529      5 EIVFVTGNANKLKEVQSILTQEVDNnnKTIHLINEaldLEELQDTDLNAIALAKGKQAVAALGKgkPVFVEDTALRFDEF 84
Cdd:TIGR00042   1 KIVFATGNPGKLKEVQSILSDLGDN--EIEQLDLG---YPEETGLTFEENALLKAKHAAKILNK--PVIAEDSGLFVDAL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529     85 NGLPGAYIKWFLK--SMGLEKIVKMLEPFENKNAEAVTTICFADSRGEYHFFQGITRGKIVPS-RGPTTFGWDSIFEPFD 161
Cdd:TIGR00042  74 NGFPGIYSARYQGtdIGNLEKILKLLEGVENRQAYFVCVIGYCDPNGEPLVFEGIVKGKITREpRGTYGFGYDPIFIPPE 153
                         170       180       190
                  ....*....|....*....|....*....|..
gi 6322529    162 sHGLTYAEMSKDAKNAISHRGKAFAQFKEYLY 193
Cdd:TIGR00042 154 -EGKTFAELTTEEKNKISHRGKAFKKFKKFLL 184
HAM1 cd00515
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ...
6-191 4.83e-68

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: 205.83  E-value: 4.83e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529    6 IVFVTGNANKLKEVQSILtqevdnNNKTIHLI--NEALDLEELQDTdLNAIALAKGKQAVAALGKgkPVFVEDTALRFDE 83
Cdd:cd00515   1 IVFATGNKGKLKEFKEIL------APFGIEVVslKDIIDIEETGST-FEENALLKARAAAEALGL--PVLADDSGLCVDA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529   84 FNGLPGAYIKWFLKS----MGLEKIVKMLEPFENKNAEAVTTICFADSRGEYHFFQGITRGKIV-PSRGPTTFGWDSIFE 158
Cdd:cd00515  72 LNGFPGVYSARFAGEhddaENNEKLLELLEGDEDRSAYFVCVIALVDPDGEPLVFEGEVEGKIVtEPRGTGGFGYDPIFI 151
                       170       180       190
                ....*....|....*....|....*....|...
gi 6322529  159 PfDSHGLTYAEMSKDAKNAISHRGKAFAQFKEY 191
Cdd:cd00515 152 P-EGYGKTFAEMSPEEKNAISHRGKALRKLKEF 183
Ham1p_like pfam01725
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ...
6-191 6.74e-67

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: 203.07  E-value: 6.74e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529      6 IVFVTGNANKLKEVQSILTQEVdnNNKTIHLINEALDLEELQDTdLNAIALAKgkqAVAALGKGKPVFVEDTALRFDEFN 85
Cdd:pfam01725   1 IVFATGNAGKLRELKAILADGI--EVLSLKDLGELPEIEETGGT-FEENALIK---ARAAAKTGLPVLADDSGLEVDALN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529     86 GLPGAYIKWFLK-----SMGLEKIVKMLE-PFENKNAEAVTTICFADSRGEYHFFQGITRGKIVPS-RGPTTFGWDSIFE 158
Cdd:pfam01725  75 GFPGVYSARFAGeggddEANNAKLLEELEvPDEDRSARFVCVIALADPGGPELVFEGEVEGEIVEEpRGEGGFGYDPIFI 154
                         170       180       190
                  ....*....|....*....|....*....|...
gi 6322529    159 PfDSHGLTYAEMSKDAKNAISHRGKAFAQFKEY 191
Cdd:pfam01725 155 P-PEGGKTFAELSPEEKNAISHRGKALRKLKEF 186
RdgB COG0127
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ...
5-192 1.69e-55

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


Pssm-ID: 439897 [Multi-domain]  Cd Length: 191  Bit Score: 174.10  E-value: 1.69e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529    5 EIVFVTGNANKLKEVQSILtqevdnNNKTIHLIN-EALDLEE--LQDTDLNAIALAKGKQAVAALGKgkPVFVEDTALRF 81
Cdd:COG0127   1 KLVFATGNAGKLREIRALL------APLGIEVVSlSDLGLPEpeETGDTFEENALIKARAAAKATGL--PALADDSGLEV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529   82 DEFNGLPGAYIKWFL-----KSMGLEKIVKMLEPF-ENKNAEAVTTICFADSRGEYHFFQGITRGKIVPS-RGPTTFGWD 154
Cdd:COG0127  73 DALGGAPGVYSARYAgegadDEANNEKLLKLLEGVdEDRRARFVCVLALADPDGEPLVFEGEVEGEIAEEpRGEGGFGYD 152
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 6322529  155 SIFEPfDSHGLTYAEMSKDAKNAISHRGKAFAQFKEYL 192
Cdd:COG0127 153 PIFIP-DGYGKTFAELSPEEKNAISHRGRALRKLAEWL 189
PRK14821 PRK14821
XTP/dITP diphosphatase;
5-196 2.50e-41

XTP/dITP diphosphatase;


Pssm-ID: 184834 [Multi-domain]  Cd Length: 184  Bit Score: 137.78  E-value: 2.50e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529     5 EIVFVTGNANKLKEVQSILtQEVDnnnktIHLINEALDLEELQDTDLNAIALAKGKQAVAALGKgkPVFVEDTALRFDEF 84
Cdd:PRK14821   2 KIYFATGNKGKVEEAKIIL-KPLG-----IEVEQIKIEYPEIQADTLEEVAAFGAKWVYNKLNR--PVIVEDSGLFIEAL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529    85 NGLPGAYIKWFLKSMGLEKIVKMLEPFENKNAEAVTTICFADSrGEYHFFQGITRGKIVPS-RGPTTFGWDSIFEPfDSH 163
Cdd:PRK14821  74 NGFPGPYSAFVYKTLGNEGILKLLEGEENRRAYFKSVIGYCDP-GGEKLFTGIVEGKIANEiRGKGGFGYDPIFIP-EGE 151
                        170       180       190
                 ....*....|....*....|....*....|...
gi 6322529   164 GLTYAEMSKDAKNAISHRGKAFAQFKEYLYQND 196
Cdd:PRK14821 152 EKTFAEMTTEEKNKISHRKRAFDEFKEWLKENL 184
PRK00120 PRK00120
dITP/XTP pyrophosphatase; Reviewed
6-192 6.56e-29

dITP/XTP pyrophosphatase; Reviewed


Pssm-ID: 234648 [Multi-domain]  Cd Length: 196  Bit Score: 106.32  E-value: 6.56e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529     6 IVFVTGNANKLKEVQSILtqevdnnnktihlinEALDLEELQDTDLNAI------------ALAKGKQAVAALGKgkPVF 73
Cdd:PRK00120   3 IVLASHNAGKLRELKALL---------------APFGIEVVSQGELGVPepeetgttfvenALIKARHAAKATGL--PAL 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529    74 VEDTALRFDEFNGLPG---A-YIKWFLKSMglEKIVKMLE-----PFENKNAEAVTTICFADSRGEYHFFQGITRGKIV- 143
Cdd:PRK00120  66 ADDSGLCVDALGGAPGvysArYAGEGASDA--ANNEKLLEelkgvPDEDRRARFVCVLVLVRPDPTPLVAEGRWEGEILw 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 6322529   144 PSRGPTTFGWDSIFEPfDSHGLTYAEMSKDAKNAISHRGKAFAQFKEYL 192
Cdd:PRK00120 144 EPRGENGFGYDPIFFP-PGYGKTFAELTPEEKNAISHRGKALKLLLEAL 191
PRK14823 PRK14823
putative deoxyribonucleoside-triphosphatase; Provisional
5-192 1.38e-28

putative deoxyribonucleoside-triphosphatase; Provisional


Pssm-ID: 237823 [Multi-domain]  Cd Length: 191  Bit Score: 105.53  E-value: 1.38e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529     5 EIVFVTGNANKLKEVQSILTQEVdnnnKTIHL--INEALDLEELQDT-DLNAIAlakgKQAVAALGKGKPVFVEDTALRF 81
Cdd:PRK14823   2 KLVFATNNKHKLEEIRSILPEKI----ELLSLsdIGCHEDIPETADTlEGNALL----KAEYVYKKYGYDCFADDTGLEV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529    82 DEFNGLPGAYIKWFL-----KSMGLEKIVKMLEPFENKNAEAVTTICFADSRGEyHFFQGITRGKIVPS-RGPTTFGWDS 155
Cdd:PRK14823  74 EALNGAPGVYSARYAggehnAEANMRKLLEELEGKDNRKAQFRTVIALILDGKE-HLFEGIIKGEIIKEkRGDSGFGYDP 152
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 6322529   156 IFEPfDSHGLTYAEMSKDAKNAISHRGKAFAQFKEYL 192
Cdd:PRK14823 153 IFVP-EGYDKTFAELGLEIKNQISHRAKAVQKLIDFL 188
PRK14822 PRK14822
XTP/dITP diphosphatase;
5-192 6.89e-27

XTP/dITP diphosphatase;


Pssm-ID: 184835 [Multi-domain]  Cd Length: 200  Bit Score: 101.12  E-value: 6.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529     5 EIVFVTGNANKLKEVQSILTQeVDNNNKTIHLINEALDLEELQDT-DLNAIAlaKGKQAVAALGKgkPVFVEDTALRFDE 83
Cdd:PRK14822   3 EIVIATKNKGKVREFKEIFEK-FDIEVKSLADFPPIPEVEETGTTfEENAIL--KAEAAAKALNK--PVIADDSGLEVDA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529    84 FNGLPGAYIKWFlksMGLEK-----IVKMLE-----PFENKNAEAVTTICFADSRGEYHFFQGITRGKIVPS-RGPTTFG 152
Cdd:PRK14822  78 LNGAPGVYSARY---AGEAKddaanNEKLLKelggvPFEKRTARFHCVIAVAFPGGETKTVEGTCEGEILEEpRGENGFG 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 6322529   153 WDSIFEpFDSHGLTYAEMSKDAKNAISHRGKAFAQFKEYL 192
Cdd:PRK14822 155 YDPLFY-VPEKGKTMAELSSEEKNAISHRGKALKKLEAEL 193
PRK14825 PRK14825
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
6-194 2.97e-18

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 173286  Cd Length: 199  Bit Score: 78.82  E-value: 2.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529     6 IVFVTGNANKLKEVQSILtqevDNNNKTIhLINEALDLEELQDTdLNAIALAKGKQAVAALGKGKPVFVEDTALRFDEFN 85
Cdd:PRK14825   4 LFFATTNINKINEVKQIL----DIPNIKI-EIPQNFDIKETGKT-FKENSLLKAKALFEILNNKQPVFSEDSGLCIEALN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529    86 GLPGAYIKWF-----LKSMGLEK----IVKMLEPFENKNAEAVTTICFADSRGEYHFFQGITRGKI---VPSRGPTTFGW 153
Cdd:PRK14825  78 LEPGIYSKRYdqyklGKKLSTNEknhlIIDLMKNEKNRTAYFICNISYISKDGTILNFEGIIKGTIalsIDDYKKNGFGY 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 6322529   154 DSIFEPFDSHGLTyaEMSKDAKNAISHRGKAFAQFKEYLYQ 194
Cdd:PRK14825 158 DPIFLTKNNKRLS--ELTLEEKNKISHRGIAFDKFKKFLMQ 196
PRK14824 PRK14824
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
6-192 6.74e-18

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 237824 [Multi-domain]  Cd Length: 201  Bit Score: 77.88  E-value: 6.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529     6 IVFVTGNANKLKEVQSILTqevdNNNKTIHLINEALDLEELQDTDL-NAIALAKgkqavaALGK--GKPVFVEDTALRFD 82
Cdd:PRK14824   3 ILLATTNEGKVREIKRLLS----DLGIEVLSPDKKIEVEEDGETFLeNAYLKAR------AYAEfyKIPVLADDSGLEVP 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529    83 EFNGLPGAYIKWFLK--------------SMGLEKIVKMLEPFENKNAEAVTTICFADsrGEYHFF-QGITRGKIVPS-R 146
Cdd:PRK14824  73 ALEGYPGVYSSRFYQiefggkeevveskdEANIRKLLRLLEGKQNRKARFVAFVVLYF--GDWGIWtEGECRGKIAEEpR 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 6322529   147 GPTTFGWDSIFEPfDSHGLTYAEMSKDAKNAISHRGKAFAQFKEYL 192
Cdd:PRK14824 151 GSGGFGYDPVFIP-EGYNKTMAELSPEEKNKISHRGKAVRKLVEIL 195
PRK14826 PRK14826
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
6-192 2.04e-13

putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional


Pssm-ID: 173287  Cd Length: 222  Bit Score: 66.23  E-value: 2.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529     6 IVFVTGNANKLKEVQSILTQ-----EVdnnnKTIHLINEALDLEELQDTdLNAIALAKGKQAVAALGKGKPVFV---EDT 77
Cdd:PRK14826  11 IVLATGNRDKVRELRPLLEHisplfSV----RSLADLGVEVDIEETEET-LEGNALLKADAIFELLSDRFPFLIalaDDT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322529    78 ALRFDEFNGLPGAYIKWFLK---------SMGLEKIVKMLEPFENKNAEAVTTICF-------ADSRGEYHFFQGITRGK 141
Cdd:PRK14826  86 GLEVDALGGAPGVYSARFAPvpegekptyEDNVRHLLSEMEGKTERSARFRTVIALkgrlpgkNGAFEFEETAEGVVEGS 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6322529   142 IVPSR-GPTTFGWDSIFEPfDSHGLTYAEMSKDAKNAISHRGKAFAQFKEYL 192
Cdd:PRK14826 166 ITTEKkGDGGFGYDPIFRV-EATGKTFAEMSTEEKNTISHRALAVQKAVKFL 216
 
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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