|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00120 |
PRK00120 |
dITP/XTP pyrophosphatase; Reviewed |
2-197 |
1.04e-126 |
|
dITP/XTP pyrophosphatase; Reviewed
Pssm-ID: 234648 [Multi-domain] Cd Length: 196 Bit Score: 354.77 E-value: 1.04e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 2 KKIVLATGNQGKVREMADLLADFGFDVVAQSEFNVSEVAETGTTFIENAIIKARHAAKETGLPAIADDSGLEVDYLGGAP 81
Cdd:PRK00120 1 MKIVLASHNAGKLRELKALLAPFGIEVVSQGELGVPEPEETGTTFVENALIKARHAAKATGLPALADDSGLCVDALGGAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 82 GVYSARYAGEDASDQQNLEKLLDAMKDVPEAQRSARFHCVLVLMRHenDPTPLVCHGKWEGRILTQAHGSNGFGYDPIFF 161
Cdd:PRK00120 81 GVYSARYAGEGASDAANNEKLLEELKGVPDEDRRARFVCVLVLVRP--DPTPLVAEGRWEGEILWEPRGENGFGYDPIFF 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 692124388 162 VPEENCASAQLEPVRKKQLSHRGQALKKLFQAIEEQ 197
Cdd:PRK00120 159 PPGYGKTFAELTPEEKNAISHRGKALKLLLEALREL 194
|
|
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
3-196 |
3.82e-113 |
|
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];
Pssm-ID: 439897 [Multi-domain] Cd Length: 191 Bit Score: 320.47 E-value: 3.82e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 3 KIVLATGNQGKVREMADLLADFGFDVVAQSEFNVSEVAETGTTFIENAIIKARHAAKETGLPAIADDSGLEVDYLGGAPG 82
Cdd:COG0127 1 KLVFATGNAGKLREIRALLAPLGIEVVSLSDLGLPEPEETGDTFEENALIKARAAAKATGLPALADDSGLEVDALGGAPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 83 VYSARYAGEDASDQQNLEKLLDAMKDVPEaQRSARFHCVLVLMRHenDPTPLVCHGKWEGRILTQAHGSNGFGYDPIFFV 162
Cdd:COG0127 81 VYSARYAGEGADDEANNEKLLKLLEGVDE-DRRARFVCVLALADP--DGEPLVFEGEVEGEIAEEPRGEGGFGYDPIFIP 157
|
170 180 190
....*....|....*....|....*....|....
gi 692124388 163 PEENCASAQLEPVRKKQLSHRGQALKKLFQAIEE 196
Cdd:COG0127 158 DGYGKTFAELSPEEKNAISHRGRALRKLAEWLKE 191
|
|
| Ham1p_like |
pfam01725 |
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ... |
4-192 |
4.10e-95 |
|
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: 274.71 E-value: 4.10e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 4 IVLATGNQGKVREMADLLADfGFDVVAQSEF-NVSEVAETGTTFIENAIIKARHAAKeTGLPAIADDSGLEVDYLGGAPG 82
Cdd:pfam01725 1 IVFATGNAGKLRELKAILAD-GIEVLSLKDLgELPEIEETGGTFEENALIKARAAAK-TGLPVLADDSGLEVDALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 83 VYSARYAGEDASDQQNLEKLLDAMKdVPEAQRSARFHCVLVLMRHenDPTPLVCHGKWEGRILTQAHGSNGFGYDPIFFV 162
Cdd:pfam01725 79 VYSARFAGEGGDDEANNAKLLEELE-VPDEDRSARFVCVIALADP--GGPELVFEGEVEGEIVEEPRGEGGFGYDPIFIP 155
|
170 180 190
....*....|....*....|....*....|
gi 692124388 163 PEENCASAQLEPVRKKQLSHRGQALKKLFQ 192
Cdd:pfam01725 156 PEGGKTFAELSPEEKNAISHRGKALRKLKE 185
|
|
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
4-193 |
7.00e-89 |
|
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: 258.61 E-value: 7.00e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 4 IVLATGNQGKVREMADLLADFGFDVVAQSEfnVSEVAETGTTFIENAIIKARHAAKETGLPAIADDSGLEVDYLGGAPGV 83
Cdd:cd00515 1 IVFATGNKGKLKEFKEILAPFGIEVVSLKD--IIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 84 YSARYAGEdASDQQNLEKLLDAMKDvpEAQRSARFHCVLVLMRHenDPTPLVCHGKWEGRILTQAHGSNGFGYDPIFFVP 163
Cdd:cd00515 79 YSARFAGE-HDDAENNEKLLELLEG--DEDRSAYFVCVIALVDP--DGEPLVFEGEVEGKIVTEPRGTGGFGYDPIFIPE 153
|
170 180 190
....*....|....*....|....*....|
gi 692124388 164 EENCASAQLEPVRKKQLSHRGQALKKLFQA 193
Cdd:cd00515 154 GYGKTFAEMSPEEKNAISHRGKALRKLKEF 183
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
3-195 |
8.24e-79 |
|
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: 233.41 E-value: 8.24e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 3 KIVLATGNQGKVREMADLLADFGFDVVAQSEFNVSEvaETGTTFIENAIIKARHAAKETGLPAIADDSGLEVDYLGGAPG 82
Cdd:TIGR00042 1 KIVFATGNPGKLKEVQSILSDLGDNEIEQLDLGYPE--ETGLTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 83 VYSARYAGedaSDQQNLEKLLDAMKDVPeaQRSARFHCVLVLMRHENDptPLVCHGKWEGRILTQAHGSNGFGYDPIFFV 162
Cdd:TIGR00042 79 IYSARYQG---TDIGNLEKILKLLEGVE--NRQAYFVCVIGYCDPNGE--PLVFEGIVKGKITREPRGTYGFGYDPIFIP 151
|
170 180 190
....*....|....*....|....*....|...
gi 692124388 163 PEENCASAQLEPVRKKQLSHRGQALKKLFQAIE 195
Cdd:TIGR00042 152 PEEGKTFAELTTEEKNKISHRGKAFKKFKKFLL 184
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00120 |
PRK00120 |
dITP/XTP pyrophosphatase; Reviewed |
2-197 |
1.04e-126 |
|
dITP/XTP pyrophosphatase; Reviewed
Pssm-ID: 234648 [Multi-domain] Cd Length: 196 Bit Score: 354.77 E-value: 1.04e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 2 KKIVLATGNQGKVREMADLLADFGFDVVAQSEFNVSEVAETGTTFIENAIIKARHAAKETGLPAIADDSGLEVDYLGGAP 81
Cdd:PRK00120 1 MKIVLASHNAGKLRELKALLAPFGIEVVSQGELGVPEPEETGTTFVENALIKARHAAKATGLPALADDSGLCVDALGGAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 82 GVYSARYAGEDASDQQNLEKLLDAMKDVPEAQRSARFHCVLVLMRHenDPTPLVCHGKWEGRILTQAHGSNGFGYDPIFF 161
Cdd:PRK00120 81 GVYSARYAGEGASDAANNEKLLEELKGVPDEDRRARFVCVLVLVRP--DPTPLVAEGRWEGEILWEPRGENGFGYDPIFF 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 692124388 162 VPEENCASAQLEPVRKKQLSHRGQALKKLFQAIEEQ 197
Cdd:PRK00120 159 PPGYGKTFAELTPEEKNAISHRGKALKLLLEALREL 194
|
|
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
3-196 |
3.82e-113 |
|
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];
Pssm-ID: 439897 [Multi-domain] Cd Length: 191 Bit Score: 320.47 E-value: 3.82e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 3 KIVLATGNQGKVREMADLLADFGFDVVAQSEFNVSEVAETGTTFIENAIIKARHAAKETGLPAIADDSGLEVDYLGGAPG 82
Cdd:COG0127 1 KLVFATGNAGKLREIRALLAPLGIEVVSLSDLGLPEPEETGDTFEENALIKARAAAKATGLPALADDSGLEVDALGGAPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 83 VYSARYAGEDASDQQNLEKLLDAMKDVPEaQRSARFHCVLVLMRHenDPTPLVCHGKWEGRILTQAHGSNGFGYDPIFFV 162
Cdd:COG0127 81 VYSARYAGEGADDEANNEKLLKLLEGVDE-DRRARFVCVLALADP--DGEPLVFEGEVEGEIAEEPRGEGGFGYDPIFIP 157
|
170 180 190
....*....|....*....|....*....|....
gi 692124388 163 PEENCASAQLEPVRKKQLSHRGQALKKLFQAIEE 196
Cdd:COG0127 158 DGYGKTFAELSPEEKNAISHRGRALRKLAEWLKE 191
|
|
| Ham1p_like |
pfam01725 |
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ... |
4-192 |
4.10e-95 |
|
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: 274.71 E-value: 4.10e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 4 IVLATGNQGKVREMADLLADfGFDVVAQSEF-NVSEVAETGTTFIENAIIKARHAAKeTGLPAIADDSGLEVDYLGGAPG 82
Cdd:pfam01725 1 IVFATGNAGKLRELKAILAD-GIEVLSLKDLgELPEIEETGGTFEENALIKARAAAK-TGLPVLADDSGLEVDALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 83 VYSARYAGEDASDQQNLEKLLDAMKdVPEAQRSARFHCVLVLMRHenDPTPLVCHGKWEGRILTQAHGSNGFGYDPIFFV 162
Cdd:pfam01725 79 VYSARFAGEGGDDEANNAKLLEELE-VPDEDRSARFVCVIALADP--GGPELVFEGEVEGEIVEEPRGEGGFGYDPIFIP 155
|
170 180 190
....*....|....*....|....*....|
gi 692124388 163 PEENCASAQLEPVRKKQLSHRGQALKKLFQ 192
Cdd:pfam01725 156 PEGGKTFAELSPEEKNAISHRGKALRKLKE 185
|
|
| PRK14822 |
PRK14822 |
XTP/dITP diphosphatase; |
1-196 |
1.10e-93 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184835 [Multi-domain] Cd Length: 200 Bit Score: 271.38 E-value: 1.10e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 1 MKKIVLATGNQGKVREMADLLADFGFDVVAQSEF-NVSEVAETGTTFIENAIIKARHAAKETGLPAIADDSGLEVDYLGG 79
Cdd:PRK14822 1 MKEIVIATKNKGKVREFKEIFEKFDIEVKSLADFpPIPEVEETGTTFEENAILKAEAAAKALNKPVIADDSGLEVDALNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 80 APGVYSARYAGEDASDQQNLEKLLDAMKDVPEAQRSARFHCVLVLMRhENDPTpLVCHGKWEGRILTQAHGSNGFGYDPI 159
Cdd:PRK14822 81 APGVYSARYAGEAKDDAANNEKLLKELGGVPFEKRTARFHCVIAVAF-PGGET-KTVEGTCEGEILEEPRGENGFGYDPL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 692124388 160 FFVPEENCASAQLEPVRKKQLSHRGQALKKLFQAIEE 196
Cdd:PRK14822 159 FYVPEKGKTMAELSSEEKNAISHRGKALKKLEAELPE 195
|
|
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
4-193 |
7.00e-89 |
|
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: 258.61 E-value: 7.00e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 4 IVLATGNQGKVREMADLLADFGFDVVAQSEfnVSEVAETGTTFIENAIIKARHAAKETGLPAIADDSGLEVDYLGGAPGV 83
Cdd:cd00515 1 IVFATGNKGKLKEFKEILAPFGIEVVSLKD--IIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 84 YSARYAGEdASDQQNLEKLLDAMKDvpEAQRSARFHCVLVLMRHenDPTPLVCHGKWEGRILTQAHGSNGFGYDPIFFVP 163
Cdd:cd00515 79 YSARFAGE-HDDAENNEKLLELLEG--DEDRSAYFVCVIALVDP--DGEPLVFEGEVEGKIVTEPRGTGGFGYDPIFIPE 153
|
170 180 190
....*....|....*....|....*....|
gi 692124388 164 EENCASAQLEPVRKKQLSHRGQALKKLFQA 193
Cdd:cd00515 154 GYGKTFAEMSPEEKNAISHRGKALRKLKEF 183
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
3-195 |
8.24e-79 |
|
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: 233.41 E-value: 8.24e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 3 KIVLATGNQGKVREMADLLADFGFDVVAQSEFNVSEvaETGTTFIENAIIKARHAAKETGLPAIADDSGLEVDYLGGAPG 82
Cdd:TIGR00042 1 KIVFATGNPGKLKEVQSILSDLGDNEIEQLDLGYPE--ETGLTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 83 VYSARYAGedaSDQQNLEKLLDAMKDVPeaQRSARFHCVLVLMRHENDptPLVCHGKWEGRILTQAHGSNGFGYDPIFFV 162
Cdd:TIGR00042 79 IYSARYQG---TDIGNLEKILKLLEGVE--NRQAYFVCVIGYCDPNGE--PLVFEGIVKGKITREPRGTYGFGYDPIFIP 151
|
170 180 190
....*....|....*....|....*....|...
gi 692124388 163 PEENCASAQLEPVRKKQLSHRGQALKKLFQAIE 195
Cdd:TIGR00042 152 PEEGKTFAELTTEEKNKISHRGKAFKKFKKFLL 184
|
|
| PRK02491 |
PRK02491 |
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; ... |
4-193 |
1.32e-57 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed
Pssm-ID: 179431 [Multi-domain] Cd Length: 328 Bit Score: 184.25 E-value: 1.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 4 IVLATGNQGKVREMADLLADFGFDVVAQSEF-NVSEVAETGTTFIENAIIKARHAAKETGLPAIADDSGLEVDYLGGAPG 82
Cdd:PRK02491 130 ILIATRNEGKTKEFRKLFGKLGYKVENLNDYpDLPEVAETGMTFEENARLKAETISRLTGKMVLADDSGLKVDALGGLPG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 83 VYSARYAGEDASDQQNLEKLLDAMKDVPEAQ-RSARFHCVLVLMRHENDptPLVCHGKWEGRILTQAHGSNGFGYDPIFF 161
Cdd:PRK02491 210 VWSARFSGPDATDAENNAKLLHELAMVFDLKdRSAQFHTTLVVAAPNKD--SLVVEADWPGYIATEPKGENGFGYDPLFL 287
|
170 180 190
....*....|....*....|....*....|..
gi 692124388 162 VPEENCASAQLEPVRKKQLSHRGQALKKLFQA 193
Cdd:PRK02491 288 VGETGRHAAELTAEEKNQLSHRGQAVKKLMEV 319
|
|
| PRK14823 |
PRK14823 |
putative deoxyribonucleoside-triphosphatase; Provisional |
2-190 |
3.52e-54 |
|
putative deoxyribonucleoside-triphosphatase; Provisional
Pssm-ID: 237823 [Multi-domain] Cd Length: 191 Bit Score: 171.02 E-value: 3.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 2 KKIVLATGNQGKVREMADLLADfGFDVVAQSEFNVSE-VAETGTTFIENAIIKARHAAKETGLPAIADDSGLEVDYLGGA 80
Cdd:PRK14823 1 MKLVFATNNKHKLEEIRSILPE-KIELLSLSDIGCHEdIPETADTLEGNALLKAEYVYKKYGYDCFADDTGLEVEALNGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 81 PGVYSARYAGEDASDQQNLEKLLDAMKDVPeaQRSARFHCVLVLMRHENDPTplvCHGKWEGRILTQAHGSNGFGYDPIf 160
Cdd:PRK14823 80 PGVYSARYAGGEHNAEANMRKLLEELEGKD--NRKAQFRTVIALILDGKEHL---FEGIIKGEIIKEKRGDSGFGYDPI- 153
|
170 180 190
....*....|....*....|....*....|.
gi 692124388 161 FVPEE-NCASAQLEPVRKKQLSHRGQALKKL 190
Cdd:PRK14823 154 FVPEGyDKTFAELGLEIKNQISHRAKAVQKL 184
|
|
| PRK14824 |
PRK14824 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
3-190 |
1.37e-51 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 237824 [Multi-domain] Cd Length: 201 Bit Score: 164.55 E-value: 1.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 3 KIVLATGNQGKVREMADLLADFGFDVVAQSEFnvSEVAETGTTFIENAIIKARHAAKETGLPAIADDSGLEVDYLGGAPG 82
Cdd:PRK14824 2 KILLATTNEGKVREIKRLLSDLGIEVLSPDKK--IEVEEDGETFLENAYLKARAYAEFYKIPVLADDSGLEVPALEGYPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 83 VYSAR-----YAGED----ASDQQNLEKLLDAMKDvpEAQRSARFHCVLVLMRHEndpTPLVCHGKWEGRILTQAHGSNG 153
Cdd:PRK14824 80 VYSSRfyqieFGGKEevveSKDEANIRKLLRLLEG--KQNRKARFVAFVVLYFGD---WGIWTEGECRGKIAEEPRGSGG 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 692124388 154 FGYDPIfFVPE-ENCASAQLEPVRKKQLSHRGQALKKL 190
Cdd:PRK14824 155 FGYDPV-FIPEgYNKTMAELSPEEKNKISHRGKAVRKL 191
|
|
| PRK14826 |
PRK14826 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
4-189 |
8.00e-49 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173287 Cd Length: 222 Bit Score: 158.29 E-value: 8.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 4 IVLATGNQGKVREMADLLA--DFGFDVVAQSEFNVS-EVAETGTTFIENAIIKARH-----AAKETGLPAIADDSGLEVD 75
Cdd:PRK14826 11 IVLATGNRDKVRELRPLLEhiSPLFSVRSLADLGVEvDIEETEETLEGNALLKADAifellSDRFPFLIALADDTGLEVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 76 YLGGAPGVYSARYA----GEDASDQQNLEKLLDAMKDVPEaqRSARFHCVLVL---MRHENDPT--PLVCHGKWEGRILT 146
Cdd:PRK14826 91 ALGGAPGVYSARFApvpeGEKPTYEDNVRHLLSEMEGKTE--RSARFRTVIALkgrLPGKNGAFefEETAEGVVEGSITT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 692124388 147 QAHGSNGFGYDPIFFVPEENCASAQLEPVRKKQLSHRGQALKK 189
Cdd:PRK14826 169 EKKGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRALAVQK 211
|
|
| PRK14821 |
PRK14821 |
XTP/dITP diphosphatase; |
3-196 |
4.92e-31 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184834 [Multi-domain] Cd Length: 184 Bit Score: 111.58 E-value: 4.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 3 KIVLATGNQGKVREMADLLADFGFDVVaQSEFNVSEVAETgtTFIENAIIKARHAAKETGLPAIADDSGLEVDYLGGAPG 82
Cdd:PRK14821 2 KIYFATGNKGKVEEAKIILKPLGIEVE-QIKIEYPEIQAD--TLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 83 VYSARyagedASDQQNLEKLLDAMKDvpEAQRSARFHCVLVLMRHENDPtplVCHGKWEGRILTQAHGSNGFGYDPIfFV 162
Cdd:PRK14821 79 PYSAF-----VYKTLGNEGILKLLEG--EENRRAYFKSVIGYCDPGGEK---LFTGIVEGKIANEIRGKGGFGYDPI-FI 147
|
170 180 190
....*....|....*....|....*....|....*
gi 692124388 163 PE-ENCASAQLEPVRKKQLSHRGQALKKLFQAIEE 196
Cdd:PRK14821 148 PEgEEKTFAEMTTEEKNKISHRKRAFDEFKEWLKE 182
|
|
| Maf_Ham1 |
cd00985 |
Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum ... |
4-144 |
4.42e-30 |
|
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: 107.59 E-value: 4.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 4 IVLATGNQGKVREMADLLadfGFDVVAQSefnvSEVAETG------TTFIENAIIKARHAAKETG-LPAIADDSGLEVDy 76
Cdd:cd00985 1 LILASGSPRRLEELKQIG---GIEFEVLP----SDIDETGlkgepeDTVEELALLKARAVAERLPdAPVIADDTGLVVD- 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 692124388 77 lgGAPGVYSARYAGEdasdqqnleklldAMKDVPEAQRSARFHCVLVLMRheNDPTPLVCHGKWEGRI 144
Cdd:cd00985 73 --GRPGGKPARFAEA-------------LEMLRGLSGRTAEFVTAVALVD--PDGKIITFEGETEGKI 123
|
|
| PRK14825 |
PRK14825 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
1-190 |
9.41e-23 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173286 Cd Length: 199 Bit Score: 90.38 E-value: 9.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 1 MKKIVLATGNQGKVREMADLLADFGFDVVAQSEFNVSEvaeTGTTFIENAIIKARHAAKETG--LPAIADDSGLEVDYLG 78
Cdd:PRK14825 1 MKTLFFATTNINKINEVKQILDIPNIKIEIPQNFDIKE---TGKTFKENSLLKAKALFEILNnkQPVFSEDSGLCIEALN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692124388 79 GAPGVYSARY----AGEDASDQQNLEKLLDAMKDvpEAQRSARFHCVLVLMrhENDPTPLVCHGKWEGRIL--TQAHGSN 152
Cdd:PRK14825 78 LEPGIYSKRYdqykLGKKLSTNEKNHLIIDLMKN--EKNRTAYFICNISYI--SKDGTILNFEGIIKGTIAlsIDDYKKN 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 692124388 153 GFGYDPIFFVpEENCASAQLEPVRKKQLSHRGQALKKL 190
Cdd:PRK14825 154 GFGYDPIFLT-KNNKRLSELTLEEKNKISHRGIAFDKF 190
|
|
| |
