|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00120 |
PRK00120 |
dITP/XTP pyrophosphatase; Reviewed |
1-205 |
4.91e-76 |
|
dITP/XTP pyrophosphatase; Reviewed
Pssm-ID: 234648 [Multi-domain] Cd Length: 196 Bit Score: 226.89 E-value: 4.91e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 1 MRLILATSNQDKIREIKEIYAALAkrlkLEILAWDKLITPfEIEENGKNFKENALIKSKAVFEALKNkgilkcddIVLSD 80
Cdd:PRK00120 1 MKIVLASHNAGKLRELKALLAPFG----IEVVSQGELGVP-EPEETGTTFVENALIKARHAAKATGL--------PALAD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 81 DSGICVDALGGKPGIHSARYSG--GNAVDNLNLLCAEVAKLPHKTSNAHYCACIGISSAQG-DFSAHGFMYGRVISTPKG 157
Cdd:PRK00120 68 DSGLCVDALGGAPGVYSARYAGegASDAANNEKLLEELKGVPDEDRRARFVCVLVLVRPDPtPLVAEGRWEGEILWEPRG 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 736160583 158 QNGFGYDPMFIPKGFEQTLAELSSEEKNAISHRTQALENASYVLQALR 205
Cdd:PRK00120 148 ENGFGYDPIFFPPGYGKTFAELTPEEKNAISHRGKALKLLLEALRELL 195
|
|
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
2-195 |
8.01e-71 |
|
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];
Pssm-ID: 439897 [Multi-domain] Cd Length: 191 Bit Score: 213.39 E-value: 8.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 2 RLILATSNQDKIREIKEIyaaLAKrLKLEILAWDKLITPfEIEENGKNFKENALIKSKAVFEALKnkgilkcdDIVLSDD 81
Cdd:COG0127 1 KLVFATGNAGKLREIRAL---LAP-LGIEVVSLSDLGLP-EPEETGDTFEENALIKARAAAKATG--------LPALADD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 82 SGICVDALGGKPGIHSARYSGGNAVD--NLNLLCAEVAKLPHKTSnAHYCACIGISSAQGD-FSAHGFMYGRVISTPKGQ 158
Cdd:COG0127 68 SGLEVDALGGAPGVYSARYAGEGADDeaNNEKLLKLLEGVDEDRR-ARFVCVLALADPDGEpLVFEGEVEGEIAEEPRGE 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 736160583 159 NGFGYDPMFIPKGFEQTLAELSSEEKNAISHRTQALE 195
Cdd:COG0127 147 GGFGYDPIFIPDGYGKTFAELSPEEKNAISHRGRALR 183
|
|
| Ham1p_like |
pfam01725 |
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ... |
3-195 |
7.09e-66 |
|
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: 200.76 E-value: 7.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 3 LILATSNQDKIREIKEIYAALakrlkLEILAWDKLITPFEIEENGKNFKENALIKSKAVFEAlknkgilkcDDIVLSDDS 82
Cdd:pfam01725 1 IVFATGNAGKLRELKAILADG-----IEVLSLKDLGELPEIEETGGTFEENALIKARAAAKT---------GLPVLADDS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 83 GICVDALGGKPGIHSARYSG--GNAVDNLNLLCAEVAKlPHKTSNAHYCACIGISSAQGD-FSAHGFMYGRVISTPKGQN 159
Cdd:pfam01725 67 GLEVDALNGFPGVYSARFAGegGDDEANNAKLLEELEV-PDEDRSARFVCVIALADPGGPeLVFEGEVEGEIVEEPRGEG 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 736160583 160 GFGYDPMFIPKGFEQTLAELSSEEKNAISHRTQALE 195
Cdd:pfam01725 146 GFGYDPIFIPPEGGKTFAELSPEEKNAISHRGKALR 181
|
|
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
3-195 |
7.56e-62 |
|
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: 190.42 E-value: 7.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 3 LILATSNQDKIREIKEIyaalAKRLKLEILAwdkLITPFEIEENGKNFKENALIKSKAVFEALKnkgilkcdDIVLSDDS 82
Cdd:cd00515 1 IVFATGNKGKLKEFKEI----LAPFGIEVVS---LKDIIDIEETGSTFEENALLKARAAAEALG--------LPVLADDS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 83 GICVDALGGKPGIHSARYSG-GNAVDNLNLLCAEVAKLPHKTsnAHYCACIGISSAQGD-FSAHGFMYGRVISTPKGQNG 160
Cdd:cd00515 66 GLCVDALNGFPGVYSARFAGeHDDAENNEKLLELLEGDEDRS--AYFVCVIALVDPDGEpLVFEGEVEGKIVTEPRGTGG 143
|
170 180 190
....*....|....*....|....*....|....*
gi 736160583 161 FGYDPMFIPKGFEQTLAELSSEEKNAISHRTQALE 195
Cdd:cd00515 144 FGYDPIFIPEGYGKTFAEMSPEEKNAISHRGKALR 178
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
3-195 |
2.37e-47 |
|
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: 153.68 E-value: 2.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 3 LILATSNQDKIREIKEIyaalAKRLKLEILAWDKLItpfEIEENGKNFKENALIKSKAVFEALKNKgilkcddiVLSDDS 82
Cdd:TIGR00042 2 IVFATGNPGKLKEVQSI----LSDLGDNEIEQLDLG---YPEETGLTFEENALLKAKHAAKILNKP--------VIAEDS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 83 GICVDALGGKPGIHSARYSGGNAvDNLNLLCAEVAKLPHKtsNAHYCACIGISSAQGDF-SAHGFMYGRVISTPKGQNGF 161
Cdd:TIGR00042 67 GLFVDALNGFPGIYSARYQGTDI-GNLEKILKLLEGVENR--QAYFVCVIGYCDPNGEPlVFEGIVKGKITREPRGTYGF 143
|
170 180 190
....*....|....*....|....*....|....
gi 736160583 162 GYDPMFIPKGFEQTLAELSSEEKNAISHRTQALE 195
Cdd:TIGR00042 144 GYDPIFIPPEEGKTFAELTTEEKNKISHRGKAFK 177
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00120 |
PRK00120 |
dITP/XTP pyrophosphatase; Reviewed |
1-205 |
4.91e-76 |
|
dITP/XTP pyrophosphatase; Reviewed
Pssm-ID: 234648 [Multi-domain] Cd Length: 196 Bit Score: 226.89 E-value: 4.91e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 1 MRLILATSNQDKIREIKEIYAALAkrlkLEILAWDKLITPfEIEENGKNFKENALIKSKAVFEALKNkgilkcddIVLSD 80
Cdd:PRK00120 1 MKIVLASHNAGKLRELKALLAPFG----IEVVSQGELGVP-EPEETGTTFVENALIKARHAAKATGL--------PALAD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 81 DSGICVDALGGKPGIHSARYSG--GNAVDNLNLLCAEVAKLPHKTSNAHYCACIGISSAQG-DFSAHGFMYGRVISTPKG 157
Cdd:PRK00120 68 DSGLCVDALGGAPGVYSARYAGegASDAANNEKLLEELKGVPDEDRRARFVCVLVLVRPDPtPLVAEGRWEGEILWEPRG 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 736160583 158 QNGFGYDPMFIPKGFEQTLAELSSEEKNAISHRTQALENASYVLQALR 205
Cdd:PRK00120 148 ENGFGYDPIFFPPGYGKTFAELTPEEKNAISHRGKALKLLLEALRELL 195
|
|
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
2-195 |
8.01e-71 |
|
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];
Pssm-ID: 439897 [Multi-domain] Cd Length: 191 Bit Score: 213.39 E-value: 8.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 2 RLILATSNQDKIREIKEIyaaLAKrLKLEILAWDKLITPfEIEENGKNFKENALIKSKAVFEALKnkgilkcdDIVLSDD 81
Cdd:COG0127 1 KLVFATGNAGKLREIRAL---LAP-LGIEVVSLSDLGLP-EPEETGDTFEENALIKARAAAKATG--------LPALADD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 82 SGICVDALGGKPGIHSARYSGGNAVD--NLNLLCAEVAKLPHKTSnAHYCACIGISSAQGD-FSAHGFMYGRVISTPKGQ 158
Cdd:COG0127 68 SGLEVDALGGAPGVYSARYAGEGADDeaNNEKLLKLLEGVDEDRR-ARFVCVLALADPDGEpLVFEGEVEGEIAEEPRGE 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 736160583 159 NGFGYDPMFIPKGFEQTLAELSSEEKNAISHRTQALE 195
Cdd:COG0127 147 GGFGYDPIFIPDGYGKTFAELSPEEKNAISHRGRALR 183
|
|
| Ham1p_like |
pfam01725 |
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ... |
3-195 |
7.09e-66 |
|
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: 200.76 E-value: 7.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 3 LILATSNQDKIREIKEIYAALakrlkLEILAWDKLITPFEIEENGKNFKENALIKSKAVFEAlknkgilkcDDIVLSDDS 82
Cdd:pfam01725 1 IVFATGNAGKLRELKAILADG-----IEVLSLKDLGELPEIEETGGTFEENALIKARAAAKT---------GLPVLADDS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 83 GICVDALGGKPGIHSARYSG--GNAVDNLNLLCAEVAKlPHKTSNAHYCACIGISSAQGD-FSAHGFMYGRVISTPKGQN 159
Cdd:pfam01725 67 GLEVDALNGFPGVYSARFAGegGDDEANNAKLLEELEV-PDEDRSARFVCVIALADPGGPeLVFEGEVEGEIVEEPRGEG 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 736160583 160 GFGYDPMFIPKGFEQTLAELSSEEKNAISHRTQALE 195
Cdd:pfam01725 146 GFGYDPIFIPPEGGKTFAELSPEEKNAISHRGKALR 181
|
|
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
3-195 |
7.56e-62 |
|
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: 190.42 E-value: 7.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 3 LILATSNQDKIREIKEIyaalAKRLKLEILAwdkLITPFEIEENGKNFKENALIKSKAVFEALKnkgilkcdDIVLSDDS 82
Cdd:cd00515 1 IVFATGNKGKLKEFKEI----LAPFGIEVVS---LKDIIDIEETGSTFEENALLKARAAAEALG--------LPVLADDS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 83 GICVDALGGKPGIHSARYSG-GNAVDNLNLLCAEVAKLPHKTsnAHYCACIGISSAQGD-FSAHGFMYGRVISTPKGQNG 160
Cdd:cd00515 66 GLCVDALNGFPGVYSARFAGeHDDAENNEKLLELLEGDEDRS--AYFVCVIALVDPDGEpLVFEGEVEGKIVTEPRGTGG 143
|
170 180 190
....*....|....*....|....*....|....*
gi 736160583 161 FGYDPMFIPKGFEQTLAELSSEEKNAISHRTQALE 195
Cdd:cd00515 144 FGYDPIFIPEGYGKTFAEMSPEEKNAISHRGKALR 178
|
|
| PRK14822 |
PRK14822 |
XTP/dITP diphosphatase; |
1-195 |
1.42e-56 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184835 [Multi-domain] Cd Length: 200 Bit Score: 177.77 E-value: 1.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 1 MRLILATSNQDKIREIKEIYaalaKRLKLEILAWDKLITPFEIEENGKNFKENALIKSKAVFEALkNKgilkcddIVLSD 80
Cdd:PRK14822 2 KEIVIATKNKGKVREFKEIF----EKFDIEVKSLADFPPIPEVEETGTTFEENAILKAEAAAKAL-NK-------PVIAD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 81 DSGICVDALGGKPGIHSARYSGGNAVD--NLNLLCAEVAKLPHKTSNAHYCACIGISSAQGD-FSAHGFMYGRVISTPKG 157
Cdd:PRK14822 70 DSGLEVDALNGAPGVYSARYAGEAKDDaaNNEKLLKELGGVPFEKRTARFHCVIAVAFPGGEtKTVEGTCEGEILEEPRG 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 736160583 158 QNGFGYDPMFIPKGFEQTLAELSSEEKNAISHRTQALE 195
Cdd:PRK14822 150 ENGFGYDPLFYVPEKGKTMAELSSEEKNAISHRGKALK 187
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
3-195 |
2.37e-47 |
|
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: 153.68 E-value: 2.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 3 LILATSNQDKIREIKEIyaalAKRLKLEILAWDKLItpfEIEENGKNFKENALIKSKAVFEALKNKgilkcddiVLSDDS 82
Cdd:TIGR00042 2 IVFATGNPGKLKEVQSI----LSDLGDNEIEQLDLG---YPEETGLTFEENALLKAKHAAKILNKP--------VIAEDS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 83 GICVDALGGKPGIHSARYSGGNAvDNLNLLCAEVAKLPHKtsNAHYCACIGISSAQGDF-SAHGFMYGRVISTPKGQNGF 161
Cdd:TIGR00042 67 GLFVDALNGFPGIYSARYQGTDI-GNLEKILKLLEGVENR--QAYFVCVIGYCDPNGEPlVFEGIVKGKITREPRGTYGF 143
|
170 180 190
....*....|....*....|....*....|....
gi 736160583 162 GYDPMFIPKGFEQTLAELSSEEKNAISHRTQALE 195
Cdd:TIGR00042 144 GYDPIFIPPEEGKTFAELTTEEKNKISHRGKAFK 177
|
|
| PRK14823 |
PRK14823 |
putative deoxyribonucleoside-triphosphatase; Provisional |
1-195 |
3.14e-43 |
|
putative deoxyribonucleoside-triphosphatase; Provisional
Pssm-ID: 237823 [Multi-domain] Cd Length: 191 Bit Score: 143.28 E-value: 3.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 1 MRLILATSNQDKIREIKEIyaaLAKrlKLEILAWDKLITPFEIEENGKNFKENALIKSKAVfealKNKGILKCddivLSD 80
Cdd:PRK14823 1 MKLVFATNNKHKLEEIRSI---LPE--KIELLSLSDIGCHEDIPETADTLEGNALLKAEYV----YKKYGYDC----FAD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 81 DSGICVDALGGKPGIHSARYSGG--NAVDNLNLLCAEVAKLPHKTSNAHYCACIGISSAQGDFSahGFMYGRVISTPKGQ 158
Cdd:PRK14823 68 DTGLEVEALNGAPGVYSARYAGGehNAEANMRKLLEELEGKDNRKAQFRTVIALILDGKEHLFE--GIIKGEIIKEKRGD 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 736160583 159 NGFGYDPMFIPKGFEQTLAELSSEEKNAISHRTQALE 195
Cdd:PRK14823 146 SGFGYDPIFVPEGYDKTFAELGLEIKNQISHRAKAVQ 182
|
|
| PRK14824 |
PRK14824 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
1-202 |
6.58e-41 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 237824 [Multi-domain] Cd Length: 201 Bit Score: 137.58 E-value: 6.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 1 MRLILATSNQDKIREIKEIYaalaKRLKLEILAWDKLItpfEIEENGKNFKENALIKSKAVFEALKNKgilkcddiVLSD 80
Cdd:PRK14824 1 MKILLATTNEGKVREIKRLL----SDLGIEVLSPDKKI---EVEEDGETFLENAYLKARAYAEFYKIP--------VLAD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 81 DSGICVDALGGKPGIHSARYS----GGNAVDNLNLLCAEVAKL-----PHKTSNAHYCACIGISSAQGDFSAHGFMYGRV 151
Cdd:PRK14824 66 DSGLEVPALEGYPGVYSSRFYqiefGGKEEVVESKDEANIRKLlrlleGKQNRKARFVAFVVLYFGDWGIWTEGECRGKI 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 736160583 152 ISTPKGQNGFGYDPMFIPKGFEQTLAELSSEEKNAISHRTQALENASYVLQ 202
Cdd:PRK14824 146 AEEPRGSGGFGYDPVFIPEGYNKTMAELSPEEKNKISHRGKAVRKLVEILK 196
|
|
| PRK14826 |
PRK14826 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
3-198 |
6.11e-39 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173287 Cd Length: 222 Bit Score: 133.25 E-value: 6.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 3 LILATSNQDKIREIKEIYAALAKRLKLEILAwdKLITPFEIEENGKNFKENALIKSKAVFEALKNK-GILkcddIVLSDD 81
Cdd:PRK14826 11 IVLATGNRDKVRELRPLLEHISPLFSVRSLA--DLGVEVDIEETEETLEGNALLKADAIFELLSDRfPFL----IALADD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 82 SGICVDALGGKPGIHSARYS---GGNA---VDNLNLLCAEVAKLphKTSNAHYCACIG----ISSAQGDF----SAHGFM 147
Cdd:PRK14826 85 TGLEVDALGGAPGVYSARFApvpEGEKptyEDNVRHLLSEMEGK--TERSARFRTVIAlkgrLPGKNGAFefeeTAEGVV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 736160583 148 YGRVISTPKGQNGFGYDPMFIPKGFEQTLAELSSEEKNAISHRTQALENAS 198
Cdd:PRK14826 163 EGSITTEKKGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRALAVQKAV 213
|
|
| PRK02491 |
PRK02491 |
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; ... |
3-195 |
4.08e-33 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed
Pssm-ID: 179431 [Multi-domain] Cd Length: 328 Bit Score: 121.07 E-value: 4.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 3 LILATSNQDKIREIKEIYAALAkrLKLEILAwDKLITPfEIEENGKNFKENALIKSKAVFEaLKNKgilkcddIVLSDDS 82
Cdd:PRK02491 130 ILIATRNEGKTKEFRKLFGKLG--YKVENLN-DYPDLP-EVAETGMTFEENARLKAETISR-LTGK-------MVLADDS 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 83 GICVDALGGKPGIHSARYSGGNAVDNLNllcaeVAKLPH--------KTSNAHYCACIGISSAQGD-FSAHGFMYGRVIS 153
Cdd:PRK02491 198 GLKVDALGGLPGVWSARFSGPDATDAEN-----NAKLLHelamvfdlKDRSAQFHTTLVVAAPNKDsLVVEADWPGYIAT 272
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 736160583 154 TPKGQNGFGYDPMFIPKGFEQTLAELSSEEKNAISHRTQALE 195
Cdd:PRK02491 273 EPKGENGFGYDPLFLVGETGRHAAELTAEEKNQLSHRGQAVK 314
|
|
| PRK14821 |
PRK14821 |
XTP/dITP diphosphatase; |
1-196 |
7.63e-29 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184834 [Multi-domain] Cd Length: 184 Bit Score: 106.19 E-value: 7.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 1 MRLILATSNQDKIREIKEIYaalaKRLKLEILAwDKLITPfEIEENgkNFKENALIKSKAVFEALKNKgilkcddiVLSD 80
Cdd:PRK14821 1 MKIYFATGNKGKVEEAKIIL----KPLGIEVEQ-IKIEYP-EIQAD--TLEEVAAFGAKWVYNKLNRP--------VIVE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 81 DSGICVDALGGKPGIHSA---RYSGGNAVdnLNLLCAEvaklphKTSNAHYCACIGISSAQGDFSAHGFMYGRVISTPKG 157
Cdd:PRK14821 65 DSGLFIEALNGFPGPYSAfvyKTLGNEGI--LKLLEGE------ENRRAYFKSVIGYCDPGGEKLFTGIVEGKIANEIRG 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 736160583 158 QNGFGYDPMFIPKGFEQTLAELSSEEKNAISHRTQALEN 196
Cdd:PRK14821 137 KGGFGYDPIFIPEGEEKTFAEMTTEEKNKISHRKRAFDE 175
|
|
| PRK14825 |
PRK14825 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
3-204 |
1.95e-28 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173286 Cd Length: 199 Bit Score: 105.40 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 3 LILATSNQDKIREIKEIYAAlaKRLKLEIlawdklITPFEIEENGKNFKENALIKSKAVFEALKNKgilkcdDIVLSDDS 82
Cdd:PRK14825 4 LFFATTNINKINEVKQILDI--PNIKIEI------PQNFDIKETGKTFKENSLLKAKALFEILNNK------QPVFSEDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 83 GICVDALGGKPGIHSARYSG---GNAVDN--LNLLCAEVAKlpHKTSNAHYCACIgISSAQGDFSAHGF--MYGRVISTP 155
Cdd:PRK14825 70 GLCIEALNLEPGIYSKRYDQyklGKKLSTneKNHLIIDLMK--NEKNRTAYFICN-ISYISKDGTILNFegIIKGTIALS 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 736160583 156 ---KGQNGFGYDPMFIPKGfEQTLAELSSEEKNAISHRTQALEN-ASYVLQAL 204
Cdd:PRK14825 147 iddYKKNGFGYDPIFLTKN-NKRLSELTLEEKNKISHRGIAFDKfKKFLMQSL 198
|
|
| Maf_Ham1 |
cd00985 |
Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum ... |
3-102 |
6.24e-15 |
|
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: 68.30 E-value: 6.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736160583 3 LILATSNQDKIREIKEIyaalakrLKLEILawdklITPFEIEENGKN------FKENALIKSKAVFEALKnkgilkcDDI 76
Cdd:cd00985 1 LILASGSPRRLEELKQI-------GGIEFE-----VLPSDIDETGLKgepedtVEELALLKARAVAERLP-------DAP 61
|
90 100
....*....|....*....|....*.
gi 736160583 77 VLSDDSGICVDalgGKPGIHSARYSG 102
Cdd:cd00985 62 VIADDTGLVVD---GRPGGKPARFAE 84
|
|
| |
