|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00120 |
PRK00120 |
dITP/XTP pyrophosphatase; Reviewed |
6-195 |
2.37e-110 |
|
dITP/XTP pyrophosphatase; Reviewed
Pssm-ID: 234648 [Multi-domain] Cd Length: 196 Bit Score: 313.17 E-value: 2.37e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 6 QLVLASHNAGKLKELQAML-GASVKVRSIGEFSQVEPEETGLSFVENAILKARNAARISGLPALADDSGLAVDFLGGAPG 84
Cdd:PRK00120 2 KIVLASHNAGKLRELKALLaPFGIEVVSQGELGVPEPEETGTTFVENALIKARHAAKATGLPALADDSGLCVDALGGAPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 85 IYSARYAD-GRGDAANNAKLLEALKDVPDAGRGAQFVSVLALVRHadDPLPILCEGIWEGRILREARGAHGFGYDPLFWV 163
Cdd:PRK00120 82 VYSARYAGeGASDAANNEKLLEELKGVPDEDRRARFVCVLVLVRP--DPTPLVAEGRWEGEILWEPRGENGFGYDPIFFP 159
|
170 180 190
....*....|....*....|....*....|..
gi 501021323 164 PERDCSSAELAPEEKNRLSHRARAMALLKQRL 195
Cdd:PRK00120 160 PGYGKTFAELTPEEKNAISHRGKALKLLLEAL 191
|
|
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
6-195 |
3.82e-101 |
|
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];
Pssm-ID: 439897 [Multi-domain] Cd Length: 191 Bit Score: 290.04 E-value: 3.82e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 6 QLVLASHNAGKLKELQAML-GASVKVRSIGEFSQVEPEETGLSFVENAILKARNAARISGLPALADDSGLAVDFLGGAPG 84
Cdd:COG0127 1 KLVFATGNAGKLREIRALLaPLGIEVVSLSDLGLPEPEETGDTFEENALIKARAAAKATGLPALADDSGLEVDALGGAPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 85 IYSARYA-DGRGDAANNAKLLEALKDVPDAgRGAQFVSVLALVRHadDPLPILCEGIWEGRILREARGAHGFGYDPLFWV 163
Cdd:COG0127 81 VYSARYAgEGADDEANNEKLLKLLEGVDED-RRARFVCVLALADP--DGEPLVFEGEVEGEIAEEPRGEGGFGYDPIFIP 157
|
170 180 190
....*....|....*....|....*....|..
gi 501021323 164 PERDCSSAELAPEEKNRLSHRARAMALLKQRL 195
Cdd:COG0127 158 DGYGKTFAELSPEEKNAISHRGRALRKLAEWL 189
|
|
| Ham1p_like |
pfam01725 |
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ... |
7-194 |
1.42e-91 |
|
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: 265.47 E-value: 1.42e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 7 LVLASHNAGKLKELQAMLGASVKVRSIGEFSQV-EPEETGLSFVENAILKARNAARIsGLPALADDSGLAVDFLGGAPGI 85
Cdd:pfam01725 1 IVFATGNAGKLRELKAILADGIEVLSLKDLGELpEIEETGGTFEENALIKARAAAKT-GLPVLADDSGLEVDALNGFPGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 86 YSARYAD-GRGDAANNAKLLEALKdVPDAGRGAQFVSVLALVRHadDPLPILCEGIWEGRILREARGAHGFGYDPLFWVP 164
Cdd:pfam01725 80 YSARFAGeGGDDEANNAKLLEELE-VPDEDRSARFVCVIALADP--GGPELVFEGEVEGEIVEEPRGEGGFGYDPIFIPP 156
|
170 180 190
....*....|....*....|....*....|
gi 501021323 165 ERDCSSAELAPEEKNRLSHRARAMALLKQR 194
Cdd:pfam01725 157 EGGKTFAELSPEEKNAISHRGKALRKLKEF 186
|
|
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
7-193 |
8.40e-88 |
|
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: 255.91 E-value: 8.40e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 7 LVLASHNAGKLKELQAMLGAS-VKVRSIGEfsQVEPEETGLSFVENAILKARNAARISGLPALADDSGLAVDFLGGAPGI 85
Cdd:cd00515 1 IVFATGNKGKLKEFKEILAPFgIEVVSLKD--IIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 86 YSARYADGRGDAANNAKLLEALKDVPDagRGAQFVSVLALVRHadDPLPILCEGIWEGRILREARGAHGFGYDPLFWVPE 165
Cdd:cd00515 79 YSARFAGEHDDAENNEKLLELLEGDED--RSAYFVCVIALVDP--DGEPLVFEGEVEGKIVTEPRGTGGFGYDPIFIPEG 154
|
170 180
....*....|....*....|....*...
gi 501021323 166 RDCSSAELAPEEKNRLSHRARAMALLKQ 193
Cdd:cd00515 155 YGKTFAEMSPEEKNAISHRGKALRKLKE 182
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
7-195 |
6.66e-71 |
|
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: 213.00 E-value: 6.66e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 7 LVLASHNAGKLKELQAML---GASVKVRSIGEfsqvEPEETGLSFVENAILKARNAARISGLPALADDSGLAVDFLGGAP 83
Cdd:TIGR00042 2 IVFATGNPGKLKEVQSILsdlGDNEIEQLDLG----YPEETGLTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 84 GIYSARYADGrgDAANNAKLLEALKDVPDagRGAQFVSVLALVRHADDPLpiLCEGIWEGRILREARGAHGFGYDPLFWV 163
Cdd:TIGR00042 78 GIYSARYQGT--DIGNLEKILKLLEGVEN--RQAYFVCVIGYCDPNGEPL--VFEGIVKGKITREPRGTYGFGYDPIFIP 151
|
170 180 190
....*....|....*....|....*....|..
gi 501021323 164 PERDCSSAELAPEEKNRLSHRARAMALLKQRL 195
Cdd:TIGR00042 152 PEEGKTFAELTTEEKNKISHRGKAFKKFKKFL 183
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00120 |
PRK00120 |
dITP/XTP pyrophosphatase; Reviewed |
6-195 |
2.37e-110 |
|
dITP/XTP pyrophosphatase; Reviewed
Pssm-ID: 234648 [Multi-domain] Cd Length: 196 Bit Score: 313.17 E-value: 2.37e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 6 QLVLASHNAGKLKELQAML-GASVKVRSIGEFSQVEPEETGLSFVENAILKARNAARISGLPALADDSGLAVDFLGGAPG 84
Cdd:PRK00120 2 KIVLASHNAGKLRELKALLaPFGIEVVSQGELGVPEPEETGTTFVENALIKARHAAKATGLPALADDSGLCVDALGGAPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 85 IYSARYAD-GRGDAANNAKLLEALKDVPDAGRGAQFVSVLALVRHadDPLPILCEGIWEGRILREARGAHGFGYDPLFWV 163
Cdd:PRK00120 82 VYSARYAGeGASDAANNEKLLEELKGVPDEDRRARFVCVLVLVRP--DPTPLVAEGRWEGEILWEPRGENGFGYDPIFFP 159
|
170 180 190
....*....|....*....|....*....|..
gi 501021323 164 PERDCSSAELAPEEKNRLSHRARAMALLKQRL 195
Cdd:PRK00120 160 PGYGKTFAELTPEEKNAISHRGKALKLLLEAL 191
|
|
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
6-195 |
3.82e-101 |
|
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];
Pssm-ID: 439897 [Multi-domain] Cd Length: 191 Bit Score: 290.04 E-value: 3.82e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 6 QLVLASHNAGKLKELQAML-GASVKVRSIGEFSQVEPEETGLSFVENAILKARNAARISGLPALADDSGLAVDFLGGAPG 84
Cdd:COG0127 1 KLVFATGNAGKLREIRALLaPLGIEVVSLSDLGLPEPEETGDTFEENALIKARAAAKATGLPALADDSGLEVDALGGAPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 85 IYSARYA-DGRGDAANNAKLLEALKDVPDAgRGAQFVSVLALVRHadDPLPILCEGIWEGRILREARGAHGFGYDPLFWV 163
Cdd:COG0127 81 VYSARYAgEGADDEANNEKLLKLLEGVDED-RRARFVCVLALADP--DGEPLVFEGEVEGEIAEEPRGEGGFGYDPIFIP 157
|
170 180 190
....*....|....*....|....*....|..
gi 501021323 164 PERDCSSAELAPEEKNRLSHRARAMALLKQRL 195
Cdd:COG0127 158 DGYGKTFAELSPEEKNAISHRGRALRKLAEWL 189
|
|
| Ham1p_like |
pfam01725 |
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ... |
7-194 |
1.42e-91 |
|
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: 265.47 E-value: 1.42e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 7 LVLASHNAGKLKELQAMLGASVKVRSIGEFSQV-EPEETGLSFVENAILKARNAARIsGLPALADDSGLAVDFLGGAPGI 85
Cdd:pfam01725 1 IVFATGNAGKLRELKAILADGIEVLSLKDLGELpEIEETGGTFEENALIKARAAAKT-GLPVLADDSGLEVDALNGFPGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 86 YSARYAD-GRGDAANNAKLLEALKdVPDAGRGAQFVSVLALVRHadDPLPILCEGIWEGRILREARGAHGFGYDPLFWVP 164
Cdd:pfam01725 80 YSARFAGeGGDDEANNAKLLEELE-VPDEDRSARFVCVIALADP--GGPELVFEGEVEGEIVEEPRGEGGFGYDPIFIPP 156
|
170 180 190
....*....|....*....|....*....|
gi 501021323 165 ERDCSSAELAPEEKNRLSHRARAMALLKQR 194
Cdd:pfam01725 157 EGGKTFAELSPEEKNAISHRGKALRKLKEF 186
|
|
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
7-193 |
8.40e-88 |
|
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: 255.91 E-value: 8.40e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 7 LVLASHNAGKLKELQAMLGAS-VKVRSIGEfsQVEPEETGLSFVENAILKARNAARISGLPALADDSGLAVDFLGGAPGI 85
Cdd:cd00515 1 IVFATGNKGKLKEFKEILAPFgIEVVSLKD--IIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 86 YSARYADGRGDAANNAKLLEALKDVPDagRGAQFVSVLALVRHadDPLPILCEGIWEGRILREARGAHGFGYDPLFWVPE 165
Cdd:cd00515 79 YSARFAGEHDDAENNEKLLELLEGDED--RSAYFVCVIALVDP--DGEPLVFEGEVEGKIVTEPRGTGGFGYDPIFIPEG 154
|
170 180
....*....|....*....|....*...
gi 501021323 166 RDCSSAELAPEEKNRLSHRARAMALLKQ 193
Cdd:cd00515 155 YGKTFAEMSPEEKNAISHRGKALRKLKE 182
|
|
| PRK14822 |
PRK14822 |
XTP/dITP diphosphatase; |
5-195 |
2.32e-79 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184835 [Multi-domain] Cd Length: 200 Bit Score: 235.17 E-value: 2.32e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 5 EQLVLASHNAGKLKELQAML-GASVKVRSIGEFSQV-EPEETGLSFVENAILKARNAARISGLPALADDSGLAVDFLGGA 82
Cdd:PRK14822 2 KEIVIATKNKGKVREFKEIFeKFDIEVKSLADFPPIpEVEETGTTFEENAILKAEAAAKALNKPVIADDSGLEVDALNGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 83 PGIYSARYA-DGRGDAANNAKLLEALKDVPDAGRGAQFVSVLALVRHADDPLPIlcEGIWEGRILREARGAHGFGYDPLF 161
Cdd:PRK14822 82 PGVYSARYAgEAKDDAANNEKLLKELGGVPFEKRTARFHCVIAVAFPGGETKTV--EGTCEGEILEEPRGENGFGYDPLF 159
|
170 180 190
....*....|....*....|....*....|....
gi 501021323 162 WVPERDCSSAELAPEEKNRLSHRARAMALLKQRL 195
Cdd:PRK14822 160 YVPEKGKTMAELSSEEKNAISHRGKALKKLEAEL 193
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
7-195 |
6.66e-71 |
|
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: 213.00 E-value: 6.66e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 7 LVLASHNAGKLKELQAML---GASVKVRSIGEfsqvEPEETGLSFVENAILKARNAARISGLPALADDSGLAVDFLGGAP 83
Cdd:TIGR00042 2 IVFATGNPGKLKEVQSILsdlGDNEIEQLDLG----YPEETGLTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 84 GIYSARYADGrgDAANNAKLLEALKDVPDagRGAQFVSVLALVRHADDPLpiLCEGIWEGRILREARGAHGFGYDPLFWV 163
Cdd:TIGR00042 78 GIYSARYQGT--DIGNLEKILKLLEGVEN--RQAYFVCVIGYCDPNGEPL--VFEGIVKGKITREPRGTYGFGYDPIFIP 151
|
170 180 190
....*....|....*....|....*....|..
gi 501021323 164 PERDCSSAELAPEEKNRLSHRARAMALLKQRL 195
Cdd:TIGR00042 152 PEEGKTFAELTTEEKNKISHRGKAFKKFKKFL 183
|
|
| PRK14823 |
PRK14823 |
putative deoxyribonucleoside-triphosphatase; Provisional |
5-191 |
3.74e-57 |
|
putative deoxyribonucleoside-triphosphatase; Provisional
Pssm-ID: 237823 [Multi-domain] Cd Length: 191 Bit Score: 178.34 E-value: 3.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 5 EQLVLASHNAGKLKELQAMLGASVKVRSIGEFSQVEP-EETGLSFVENAILKARNAARISGLPALADDSGLAVDFLGGAP 83
Cdd:PRK14823 1 MKLVFATNNKHKLEEIRSILPEKIELLSLSDIGCHEDiPETADTLEGNALLKAEYVYKKYGYDCFADDTGLEVEALNGAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 84 GIYSARYADGRGDA-ANNAKLLEALKDVPDagRGAQFVSVLALVrhaDDPLPILCEGIWEGRILREARGAHGFGYDPLFw 162
Cdd:PRK14823 81 GVYSARYAGGEHNAeANMRKLLEELEGKDN--RKAQFRTVIALI---LDGKEHLFEGIIKGEIIKEKRGDSGFGYDPIF- 154
|
170 180 190
....*....|....*....|....*....|
gi 501021323 163 VPE-RDCSSAELAPEEKNRLSHRARAMALL 191
Cdd:PRK14823 155 VPEgYDKTFAELGLEIKNQISHRAKAVQKL 184
|
|
| PRK02491 |
PRK02491 |
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; ... |
5-191 |
5.90e-50 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed
Pssm-ID: 179431 [Multi-domain] Cd Length: 328 Bit Score: 164.21 E-value: 5.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 5 EQLVLASHNAGKLKELQAMLGA-SVKVRSIGEFSQV-EPEETGLSFVENAILKARNAARISGLPALADDSGLAVDFLGGA 82
Cdd:PRK02491 128 DTILIATRNEGKTKEFRKLFGKlGYKVENLNDYPDLpEVAETGMTFEENARLKAETISRLTGKMVLADDSGLKVDALGGL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 83 PGIYSARYAD-GRGDAANNAKLLEALKDVPD-AGRGAQFVSVLalVRHADDPLPILCEGIWEGRILREARGAHGFGYDPL 160
Cdd:PRK02491 208 PGVWSARFSGpDATDAENNAKLLHELAMVFDlKDRSAQFHTTL--VVAAPNKDSLVVEADWPGYIATEPKGENGFGYDPL 285
|
170 180 190
....*....|....*....|....*....|.
gi 501021323 161 FWVPERDCSSAELAPEEKNRLSHRARAMALL 191
Cdd:PRK02491 286 FLVGETGRHAAELTAEEKNQLSHRGQAVKKL 316
|
|
| PRK14824 |
PRK14824 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
6-195 |
1.29e-46 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 237824 [Multi-domain] Cd Length: 201 Bit Score: 151.84 E-value: 1.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 6 QLVLASHNAGKLKELQAMLGAS-VKVRSIGEFSQVEpeETGLSFVENAILKARNAARISGLPALADDSGLAVDFLGGAPG 84
Cdd:PRK14824 2 KILLATTNEGKVREIKRLLSDLgIEVLSPDKKIEVE--EDGETFLENAYLKARAYAEFYKIPVLADDSGLEVPALEGYPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 85 IYSARYAD----GR------GDAANNAKLLEALKDVPDagRGAQFVSVLALvrhADDPLPILCEGIWEGRILREARGAHG 154
Cdd:PRK14824 80 VYSSRFYQiefgGKeevvesKDEANIRKLLRLLEGKQN--RKARFVAFVVL---YFGDWGIWTEGECRGKIAEEPRGSGG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 501021323 155 FGYDPLFwVPERDCSS-AELAPEEKNRLSHRARAMALLKQRL 195
Cdd:PRK14824 155 FGYDPVF-IPEGYNKTmAELSPEEKNKISHRGKAVRKLVEIL 195
|
|
| PRK14826 |
PRK14826 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
7-187 |
4.64e-45 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173287 Cd Length: 222 Bit Score: 148.66 E-value: 4.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 7 LVLASHNAGKLKELQAML---GASVKVRSIGEFS-QVEPEETGLSFVENAILKARN-----AARISGLPALADDSGLAVD 77
Cdd:PRK14826 11 IVLATGNRDKVRELRPLLehiSPLFSVRSLADLGvEVDIEETEETLEGNALLKADAifellSDRFPFLIALADDTGLEVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 78 FLGGAPGIYSARYA---DGRGD--AANNAKLLEALKDVPDagRGAQFVSVLAL---VRHADDPLPI--LCEGIWEGRILR 147
Cdd:PRK14826 91 ALGGAPGVYSARFApvpEGEKPtyEDNVRHLLSEMEGKTE--RSARFRTVIALkgrLPGKNGAFEFeeTAEGVVEGSITT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 501021323 148 EARGAHGFGYDPLFWVPERDCSSAELAPEEKNRLSHRARA 187
Cdd:PRK14826 169 EKKGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRALA 208
|
|
| PRK14821 |
PRK14821 |
XTP/dITP diphosphatase; |
7-195 |
4.53e-28 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184834 [Multi-domain] Cd Length: 184 Bit Score: 103.88 E-value: 4.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 7 LVLASHNAGKLKELQAMLGA-SVKVRSIgefsQVE-PEETGLSFVENAILKARNAARISGLPALADDSGLAVDFLGGAPG 84
Cdd:PRK14821 3 IYFATGNKGKVEEAKIILKPlGIEVEQI----KIEyPEIQADTLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 85 IYSARYADGRGdaanNAKLLEALKDVPDagRGAQFVSVLALVrhADDPLPILcEGIWEGRILREARGAHGFGYDPLFwVP 164
Cdd:PRK14821 79 PYSAFVYKTLG----NEGILKLLEGEEN--RRAYFKSVIGYC--DPGGEKLF-TGIVEGKIANEIRGKGGFGYDPIF-IP 148
|
170 180 190
....*....|....*....|....*....|..
gi 501021323 165 E-RDCSSAELAPEEKNRLSHRARAMALLKQRL 195
Cdd:PRK14821 149 EgEEKTFAEMTTEEKNKISHRKRAFDEFKEWL 180
|
|
| Maf_Ham1 |
cd00985 |
Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum ... |
7-145 |
9.19e-28 |
|
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: 101.42 E-value: 9.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 7 LVLASHNAGKLKELQAMLGASVKVRSIgefsqvEPEETGL------SFVENAILKARNAA-RISGLPALADDSGLAVDfl 79
Cdd:cd00985 1 LILASGSPRRLEELKQIGGIEFEVLPS------DIDETGLkgepedTVEELALLKARAVAeRLPDAPVIADDTGLVVD-- 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501021323 80 gGAPGIYSARYADgrgdaannakllEALKDVPDAGRGAQFVSVLALVRHadDPLPILCEGIWEGRI 145
Cdd:cd00985 73 -GRPGGKPARFAE------------ALEMLRGLSGRTAEFVTAVALVDP--DGKIITFEGETEGKI 123
|
|
| PRK14825 |
PRK14825 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
4-195 |
4.09e-19 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173286 Cd Length: 199 Bit Score: 80.75 E-value: 4.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 4 LEQLVLASHNAGKLKELQAMLG-ASVKVRSIGEFsqvEPEETGLSFVENAILKARNAARISG--LPALADDSGLAVDFLG 80
Cdd:PRK14825 1 MKTLFFATTNINKINEVKQILDiPNIKIEIPQNF---DIKETGKTFKENSLLKAKALFEILNnkQPVFSEDSGLCIEALN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501021323 81 GAPGIYSARYADGR-----GDAANNAKLLEALKDvpDAGRGAQFVSVLALVrhADDPLPILCEGIWEGRILR--EARGAH 153
Cdd:PRK14825 78 LEPGIYSKRYDQYKlgkklSTNEKNHLIIDLMKN--EKNRTAYFICNISYI--SKDGTILNFEGIIKGTIALsiDDYKKN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 501021323 154 GFGYDPLFwVPERDCSSAELAPEEKNRLSHRARAMALLKQRL 195
Cdd:PRK14825 154 GFGYDPIF-LTKNNKRLSELTLEEKNKISHRGIAFDKFKKFL 194
|
|
| |
