|
Name |
Accession |
Description |
Interval |
E-value |
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
7-199 |
8.83e-93 |
|
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];
Pssm-ID: 439897 [Multi-domain] Cd Length: 191 Bit Score: 268.85 E-value: 8.83e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 7 VVLSSRNRKKIGEVMELLAPWEIQVQGVSEFEsIRDVAETGSTFAENADLKATTVARQLHRWTIAEDSGLCVPALGHAPG 86
Cdd:COG0127 2 LVFATGNAGKLREIRALLAPLGIEVVSLSDLG-LPEPEETGDTFEENALIKARAAAKATGLPALADDSGLEVDALGGAPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 87 VYSARYAGEPSNDQRNNTKLLAEMSSLQgDDRAAYYVCHAVLSDPAGQIRVrVEGRCWGRILTQPSGDHGFGYDPLFLVP 166
Cdd:COG0127 81 VYSARYAGEGADDEANNEKLLKLLEGVD-EDRRARFVCVLALADPDGEPLV-FEGEVEGEIAEEPRGEGGFGYDPIFIPD 158
|
170 180 190
....*....|....*....|....*....|...
gi 752754537 167 EYHLTFGQLAPAVKRHISHRARAFEQFIPQMIA 199
Cdd:COG0127 159 GYGKTFAELSPEEKNAISHRGRALRKLAEWLKE 191
|
|
| PRK00120 |
PRK00120 |
dITP/XTP pyrophosphatase; Reviewed |
7-197 |
2.45e-89 |
|
dITP/XTP pyrophosphatase; Reviewed
Pssm-ID: 234648 [Multi-domain] Cd Length: 196 Bit Score: 260.40 E-value: 2.45e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 7 VVLSSRNRKKIGEVMELLAPWEIQVQGVSEFeSIRDVAETGSTFAENADLKATTVARQLHRWTIAEDSGLCVPALGHAPG 86
Cdd:PRK00120 3 IVLASHNAGKLRELKALLAPFGIEVVSQGEL-GVPEPEETGTTFVENALIKARHAAKATGLPALADDSGLCVDALGGAPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 87 VYSARYAGEPSNDQRNNTKLLAEMSSLQGDDRAAYYVCHAVLSDPAGQIRVrVEGRCWGRILTQPSGDHGFGYDPLFLVP 166
Cdd:PRK00120 82 VYSARYAGEGASDAANNEKLLEELKGVPDEDRRARFVCVLVLVRPDPTPLV-AEGRWEGEILWEPRGENGFGYDPIFFPP 160
|
170 180 190
....*....|....*....|....*....|.
gi 752754537 167 EYHLTFGQLAPAVKRHISHRARAFEQFIPQM 197
Cdd:PRK00120 161 GYGKTFAELTPEEKNAISHRGKALKLLLEAL 191
|
|
| Ham1p_like |
pfam01725 |
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ... |
7-196 |
2.90e-84 |
|
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: 247.36 E-value: 2.90e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 7 VVLSSRNRKKIGEVMELLAPwEIQVQGVSEFESIRDVAETGSTFAENADLKATTVARqLHRWTIAEDSGLCVPALGHAPG 86
Cdd:pfam01725 1 IVFATGNAGKLRELKAILAD-GIEVLSLKDLGELPEIEETGGTFEENALIKARAAAK-TGLPVLADDSGLEVDALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 87 VYSARYAGEPSNDQRNNTKLLAEMSSlQGDDRAAYYVCHAVLSDPAGQIRVrVEGRCWGRILTQPSGDHGFGYDPLFLVP 166
Cdd:pfam01725 79 VYSARFAGEGGDDEANNAKLLEELEV-PDEDRSARFVCVIALADPGGPELV-FEGEVEGEIVEEPRGEGGFGYDPIFIPP 156
|
170 180 190
....*....|....*....|....*....|
gi 752754537 167 EYHLTFGQLAPAVKRHISHRARAFEQFIPQ 196
Cdd:pfam01725 157 EGGKTFAELSPEEKNAISHRGKALRKLKEF 186
|
|
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
7-196 |
8.12e-83 |
|
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: 243.58 E-value: 8.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 7 VVLSSRNRKKIGEVMELLAPWEIQVQGVSEFEsirDVAETGSTFAENADLKATTVARQLHRWTIAEDSGLCVPALGHAPG 86
Cdd:cd00515 1 IVFATGNKGKLKEFKEILAPFGIEVVSLKDII---DIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 87 VYSARYAGEPsNDQRNNTKLLAEMSSLqgDDRAAYYVCHAVLSDPAGQIRVrVEGRCWGRILTQPSGDHGFGYDPLFLVP 166
Cdd:cd00515 78 VYSARFAGEH-DDAENNEKLLELLEGD--EDRSAYFVCVIALVDPDGEPLV-FEGEVEGKIVTEPRGTGGFGYDPIFIPE 153
|
170 180 190
....*....|....*....|....*....|
gi 752754537 167 EYHLTFGQLAPAVKRHISHRARAFEQFIPQ 196
Cdd:cd00515 154 GYGKTFAEMSPEEKNAISHRGKALRKLKEF 183
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
7-198 |
6.51e-55 |
|
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: 172.94 E-value: 6.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 7 VVLSSRNRKKIGEVMELLAPWEIQVQGVSEFESIRdvaETGSTFAENADLKATTVARQLHRWTIAEDSGLCVPALGHAPG 86
Cdd:TIGR00042 2 IVFATGNPGKLKEVQSILSDLGDNEIEQLDLGYPE---ETGLTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 87 VYSARYAGepsNDQRNNTKLLAEMSSLqgDDRAAYYVCHAVLSDPAGQIRVrVEGRCWGRILTQPSGDHGFGYDPLFLVP 166
Cdd:TIGR00042 79 IYSARYQG---TDIGNLEKILKLLEGV--ENRQAYFVCVIGYCDPNGEPLV-FEGIVKGKITREPRGTYGFGYDPIFIPP 152
|
170 180 190
....*....|....*....|....*....|..
gi 752754537 167 EYHLTFGQLAPAVKRHISHRARAFEQFIPQMI 198
Cdd:TIGR00042 153 EEGKTFAELTTEEKNKISHRGKAFKKFKKFLL 184
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
7-199 |
8.83e-93 |
|
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];
Pssm-ID: 439897 [Multi-domain] Cd Length: 191 Bit Score: 268.85 E-value: 8.83e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 7 VVLSSRNRKKIGEVMELLAPWEIQVQGVSEFEsIRDVAETGSTFAENADLKATTVARQLHRWTIAEDSGLCVPALGHAPG 86
Cdd:COG0127 2 LVFATGNAGKLREIRALLAPLGIEVVSLSDLG-LPEPEETGDTFEENALIKARAAAKATGLPALADDSGLEVDALGGAPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 87 VYSARYAGEPSNDQRNNTKLLAEMSSLQgDDRAAYYVCHAVLSDPAGQIRVrVEGRCWGRILTQPSGDHGFGYDPLFLVP 166
Cdd:COG0127 81 VYSARYAGEGADDEANNEKLLKLLEGVD-EDRRARFVCVLALADPDGEPLV-FEGEVEGEIAEEPRGEGGFGYDPIFIPD 158
|
170 180 190
....*....|....*....|....*....|...
gi 752754537 167 EYHLTFGQLAPAVKRHISHRARAFEQFIPQMIA 199
Cdd:COG0127 159 GYGKTFAELSPEEKNAISHRGRALRKLAEWLKE 191
|
|
| PRK00120 |
PRK00120 |
dITP/XTP pyrophosphatase; Reviewed |
7-197 |
2.45e-89 |
|
dITP/XTP pyrophosphatase; Reviewed
Pssm-ID: 234648 [Multi-domain] Cd Length: 196 Bit Score: 260.40 E-value: 2.45e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 7 VVLSSRNRKKIGEVMELLAPWEIQVQGVSEFeSIRDVAETGSTFAENADLKATTVARQLHRWTIAEDSGLCVPALGHAPG 86
Cdd:PRK00120 3 IVLASHNAGKLRELKALLAPFGIEVVSQGEL-GVPEPEETGTTFVENALIKARHAAKATGLPALADDSGLCVDALGGAPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 87 VYSARYAGEPSNDQRNNTKLLAEMSSLQGDDRAAYYVCHAVLSDPAGQIRVrVEGRCWGRILTQPSGDHGFGYDPLFLVP 166
Cdd:PRK00120 82 VYSARYAGEGASDAANNEKLLEELKGVPDEDRRARFVCVLVLVRPDPTPLV-AEGRWEGEILWEPRGENGFGYDPIFFPP 160
|
170 180 190
....*....|....*....|....*....|.
gi 752754537 167 EYHLTFGQLAPAVKRHISHRARAFEQFIPQM 197
Cdd:PRK00120 161 GYGKTFAELTPEEKNAISHRGKALKLLLEAL 191
|
|
| Ham1p_like |
pfam01725 |
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ... |
7-196 |
2.90e-84 |
|
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: 247.36 E-value: 2.90e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 7 VVLSSRNRKKIGEVMELLAPwEIQVQGVSEFESIRDVAETGSTFAENADLKATTVARqLHRWTIAEDSGLCVPALGHAPG 86
Cdd:pfam01725 1 IVFATGNAGKLRELKAILAD-GIEVLSLKDLGELPEIEETGGTFEENALIKARAAAK-TGLPVLADDSGLEVDALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 87 VYSARYAGEPSNDQRNNTKLLAEMSSlQGDDRAAYYVCHAVLSDPAGQIRVrVEGRCWGRILTQPSGDHGFGYDPLFLVP 166
Cdd:pfam01725 79 VYSARFAGEGGDDEANNAKLLEELEV-PDEDRSARFVCVIALADPGGPELV-FEGEVEGEIVEEPRGEGGFGYDPIFIPP 156
|
170 180 190
....*....|....*....|....*....|
gi 752754537 167 EYHLTFGQLAPAVKRHISHRARAFEQFIPQ 196
Cdd:pfam01725 157 EGGKTFAELSPEEKNAISHRGKALRKLKEF 186
|
|
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
7-196 |
8.12e-83 |
|
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: 243.58 E-value: 8.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 7 VVLSSRNRKKIGEVMELLAPWEIQVQGVSEFEsirDVAETGSTFAENADLKATTVARQLHRWTIAEDSGLCVPALGHAPG 86
Cdd:cd00515 1 IVFATGNKGKLKEFKEILAPFGIEVVSLKDII---DIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 87 VYSARYAGEPsNDQRNNTKLLAEMSSLqgDDRAAYYVCHAVLSDPAGQIRVrVEGRCWGRILTQPSGDHGFGYDPLFLVP 166
Cdd:cd00515 78 VYSARFAGEH-DDAENNEKLLELLEGD--EDRSAYFVCVIALVDPDGEPLV-FEGEVEGKIVTEPRGTGGFGYDPIFIPE 153
|
170 180 190
....*....|....*....|....*....|
gi 752754537 167 EYHLTFGQLAPAVKRHISHRARAFEQFIPQ 196
Cdd:cd00515 154 GYGKTFAEMSPEEKNAISHRGKALRKLKEF 183
|
|
| PRK14822 |
PRK14822 |
XTP/dITP diphosphatase; |
7-192 |
7.96e-81 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184835 [Multi-domain] Cd Length: 200 Bit Score: 239.02 E-value: 7.96e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 7 VVLSSRNRKKIGEVMELLAPWEIQVQGVSEFESIRDVAETGSTFAENADLKATTVARQLHRWTIAEDSGLCVPALGHAPG 86
Cdd:PRK14822 4 IVIATKNKGKVREFKEIFEKFDIEVKSLADFPPIPEVEETGTTFEENAILKAEAAAKALNKPVIADDSGLEVDALNGAPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 87 VYSARYAGEPSNDQRNNTKLLAEMSSLQGDDRAAYYVCHAVLSDPAGQIRVrVEGRCWGRILTQPSGDHGFGYDPLFLVP 166
Cdd:PRK14822 84 VYSARYAGEAKDDAANNEKLLKELGGVPFEKRTARFHCVIAVAFPGGETKT-VEGTCEGEILEEPRGENGFGYDPLFYVP 162
|
170 180
....*....|....*....|....*.
gi 752754537 167 EYHLTFGQLAPAVKRHISHRARAFEQ 192
Cdd:PRK14822 163 EKGKTMAELSSEEKNAISHRGKALKK 188
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
7-198 |
6.51e-55 |
|
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: 172.94 E-value: 6.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 7 VVLSSRNRKKIGEVMELLAPWEIQVQGVSEFESIRdvaETGSTFAENADLKATTVARQLHRWTIAEDSGLCVPALGHAPG 86
Cdd:TIGR00042 2 IVFATGNPGKLKEVQSILSDLGDNEIEQLDLGYPE---ETGLTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 87 VYSARYAGepsNDQRNNTKLLAEMSSLqgDDRAAYYVCHAVLSDPAGQIRVrVEGRCWGRILTQPSGDHGFGYDPLFLVP 166
Cdd:TIGR00042 79 IYSARYQG---TDIGNLEKILKLLEGV--ENRQAYFVCVIGYCDPNGEPLV-FEGIVKGKITREPRGTYGFGYDPIFIPP 152
|
170 180 190
....*....|....*....|....*....|..
gi 752754537 167 EYHLTFGQLAPAVKRHISHRARAFEQFIPQMI 198
Cdd:TIGR00042 153 EEGKTFAELTTEEKNKISHRGKAFKKFKKFLL 184
|
|
| PRK14824 |
PRK14824 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
7-189 |
1.82e-46 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 237824 [Multi-domain] Cd Length: 201 Bit Score: 151.84 E-value: 1.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 7 VVLSSRNRKKIGEVMELLAPWEIQVqgVSEFESIrDVAETGSTFAENADLKATTVARQLHRWTIAEDSGLCVPALGHAPG 86
Cdd:PRK14824 3 ILLATTNEGKVREIKRLLSDLGIEV--LSPDKKI-EVEEDGETFLENAYLKARAYAEFYKIPVLADDSGLEVPALEGYPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 87 VYSAR-----YAGE----PSNDQRNNTKLLAEMSSLQgdDRAAYYVCHAVLSDPagQIRVRVEGRCWGRILTQPSGDHGF 157
Cdd:PRK14824 80 VYSSRfyqieFGGKeevvESKDEANIRKLLRLLEGKQ--NRKARFVAFVVLYFG--DWGIWTEGECRGKIAEEPRGSGGF 155
|
170 180 190
....*....|....*....|....*....|...
gi 752754537 158 GYDPLFlVPE-YHLTFGQLAPAVKRHISHRARA 189
Cdd:PRK14824 156 GYDPVF-IPEgYNKTMAELSPEEKNKISHRGKA 187
|
|
| PRK02491 |
PRK02491 |
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; ... |
5-194 |
4.18e-46 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed
Pssm-ID: 179431 [Multi-domain] Cd Length: 328 Bit Score: 154.58 E-value: 4.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 5 ESVVLSSRNRKKIGEVMELLAPWEIQVQGVSEFESIRDVAETGSTFAENADLKATTVARQLHRWTIAEDSGLCVPALGHA 84
Cdd:PRK02491 128 DTILIATRNEGKTKEFRKLFGKLGYKVENLNDYPDLPEVAETGMTFEENARLKAETISRLTGKMVLADDSGLKVDALGGL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 85 PGVYSARYAGEPSNDQRNNTKLLAEMSS-LQGDDRAAYYVCHAVLSDPAGQIRVrVEGRCWGRILTQPSGDHGFGYDPLF 163
Cdd:PRK02491 208 PGVWSARFSGPDATDAENNAKLLHELAMvFDLKDRSAQFHTTLVVAAPNKDSLV-VEADWPGYIATEPKGENGFGYDPLF 286
|
170 180 190
....*....|....*....|....*....|.
gi 752754537 164 LVPEYHLTFGQLAPAVKRHISHRARAFEQFI 194
Cdd:PRK02491 287 LVGETGRHAAELTAEEKNQLSHRGQAVKKLM 317
|
|
| PRK14823 |
PRK14823 |
putative deoxyribonucleoside-triphosphatase; Provisional |
7-194 |
1.81e-44 |
|
putative deoxyribonucleoside-triphosphatase; Provisional
Pssm-ID: 237823 [Multi-domain] Cd Length: 191 Bit Score: 146.36 E-value: 1.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 7 VVLSSRNRKKIGEVMELLaPWEIQVQGVSEFESIRDVAETGSTFAENADLKATTVARQLHRWTIAEDSGLCVPALGHAPG 86
Cdd:PRK14823 3 LVFATNNKHKLEEIRSIL-PEKIELLSLSDIGCHEDIPETADTLEGNALLKAEYVYKKYGYDCFADDTGLEVEALNGAPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 87 VYSARYAGEPSNDQRNNTKLLAEMSSlqGDDRAAYYVCHAVLSDPAGQirVRVEGRCWGRILTQPSGDHGFGYDPLFlVP 166
Cdd:PRK14823 82 VYSARYAGGEHNAEANMRKLLEELEG--KDNRKAQFRTVIALILDGKE--HLFEGIIKGEIIKEKRGDSGFGYDPIF-VP 156
|
170 180
....*....|....*....|....*....
gi 752754537 167 E-YHLTFGQLAPAVKRHISHRARAFEQFI 194
Cdd:PRK14823 157 EgYDKTFAELGLEIKNQISHRAKAVQKLI 185
|
|
| PRK14826 |
PRK14826 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
7-194 |
1.48e-35 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173287 Cd Length: 222 Bit Score: 124.39 E-value: 1.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 7 VVLSSRNRKKIGE---VMELLAPwEIQVQGVSEFESIRDVAETGSTFAENADLKATTV-----ARQLHRWTIAEDSGLCV 78
Cdd:PRK14826 11 IVLATGNRDKVRElrpLLEHISP-LFSVRSLADLGVEVDIEETEETLEGNALLKADAIfellsDRFPFLIALADDTGLEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 79 PALGHAPGVYSARYA----GEPSNDQRNNTKLLAEMSSLQgdDRAAYY--VCHAVLSDPAGQ----IRVRVEGRCWGRIL 148
Cdd:PRK14826 90 DALGGAPGVYSARFApvpeGEKPTYEDNVRHLLSEMEGKT--ERSARFrtVIALKGRLPGKNgafeFEETAEGVVEGSIT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 752754537 149 TQPSGDHGFGYDPLFLVPEYHLTFGQLAPAVKRHISHRARAFEQFI 194
Cdd:PRK14826 168 TEKKGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRALAVQKAV 213
|
|
| PRK14821 |
PRK14821 |
XTP/dITP diphosphatase; |
7-193 |
1.59e-24 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184834 [Multi-domain] Cd Length: 184 Bit Score: 95.02 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 7 VVLSSRNRKKIGEVMELLAPWEIQVQGVS------EFESIRDVAETGstfaenadlkATTVARQLHRWTIAEDSGLCVPA 80
Cdd:PRK14821 3 IYFATGNKGKVEEAKIILKPLGIEVEQIKieypeiQADTLEEVAAFG----------AKWVYNKLNRPVIVEDSGLFIEA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 81 LGHAPGVYSArYAgepsNDQRNNTKLLAEMSSLqgDDRAAYYVCHAVLSDPaGQIRVrVEGRCWGRILTQPSGDHGFGYD 160
Cdd:PRK14821 73 LNGFPGPYSA-FV----YKTLGNEGILKLLEGE--ENRRAYFKSVIGYCDP-GGEKL-FTGIVEGKIANEIRGKGGFGYD 143
|
170 180 190
....*....|....*....|....*....|...
gi 752754537 161 PLFLVPEYHLTFGQLAPAVKRHISHRARAFEQF 193
Cdd:PRK14821 144 PIFIPEGEEKTFAEMTTEEKNKISHRKRAFDEF 176
|
|
| PRK14825 |
PRK14825 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
5-193 |
2.04e-23 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173286 Cd Length: 199 Bit Score: 92.31 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 5 ESVVLSSRNRKKIGEVMELLAPWEIQVQGVSEFesirDVAETGSTFAENADLKATTVARQLHRW--TIAEDSGLCVPALG 82
Cdd:PRK14825 2 KTLFFATTNINKINEVKQILDIPNIKIEIPQNF----DIKETGKTFKENSLLKAKALFEILNNKqpVFSEDSGLCIEALN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 83 HAPGVYSARY----AGEPSNDQRNNTKLLAEMSslQGDDRAAYYVCHAVLSDPAGQIrVRVEGRCWGRILTQPS--GDHG 156
Cdd:PRK14825 78 LEPGIYSKRYdqykLGKKLSTNEKNHLIIDLMK--NEKNRTAYFICNISYISKDGTI-LNFEGIIKGTIALSIDdyKKNG 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 752754537 157 FGYDPLFLVPEyHLTFGQLAPAVKRHISHRARAFEQF 193
Cdd:PRK14825 155 FGYDPIFLTKN-NKRLSELTLEEKNKISHRGIAFDKF 190
|
|
| Maf_Ham1 |
cd00985 |
Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum ... |
7-147 |
5.33e-20 |
|
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: 81.39 E-value: 5.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752754537 7 VVLSSRNRKKIGEVMELLApWEIQVQgVSEFESIRDVAETGSTFAENADLKATTVARQL-HRWTIAEDSGLCVPAlghAP 85
Cdd:cd00985 1 LILASGSPRRLEELKQIGG-IEFEVL-PSDIDETGLKGEPEDTVEELALLKARAVAERLpDAPVIADDTGLVVDG---RP 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 752754537 86 GVYSARYAGEpsndqrnntklLAEMSSLQGddRAAYYVCHAVLSDPAGQIRVrVEGRCWGRI 147
Cdd:cd00985 76 GGKPARFAEA-----------LEMLRGLSG--RTAEFVTAVALVDPDGKIIT-FEGETEGKI 123
|
|
| |
