|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00120 |
PRK00120 |
dITP/XTP pyrophosphatase; Reviewed |
2-197 |
8.71e-125 |
|
dITP/XTP pyrophosphatase; Reviewed
Pssm-ID: 234648 [Multi-domain] Cd Length: 196 Bit Score: 349.77 E-value: 8.71e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 2 QKVVLATGNAGKVRELASLLNDFGLDVVAQTELGVDSAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVDFLGGAP 81
Cdd:PRK00120 1 MKIVLASHNAGKLRELKALLAPFGIEVVSQGELGVPEPEETGTTFVENALIKARHAAKATGLPALADDSGLCVDALGGAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 82 GIYSARYSGVDATDQQNLEKLLVALKDVPDEQRTAQFHCVLVYMRHaeDPTPIVCHGSWPGVITREAAGNGGFGYDPIFF 161
Cdd:PRK00120 81 GVYSARYAGEGASDAANNEKLLEELKGVPDEDRRARFVCVLVLVRP--DPTPLVAEGRWEGEILWEPRGENGFGYDPIFF 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 505384737 162 VPTEGKTAAELTREEKSAISHRGRALKLLLEALRNG 197
Cdd:PRK00120 159 PPGYGKTFAELTPEEKNAISHRGKALKLLLEALREL 194
|
|
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
3-196 |
3.85e-110 |
|
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];
Pssm-ID: 439897 [Multi-domain] Cd Length: 191 Bit Score: 312.77 E-value: 3.85e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 3 KVVLATGNAGKVRELASLLNDFGLDVVAQTELGVDSAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVDFLGGAPG 82
Cdd:COG0127 1 KLVFATGNAGKLREIRALLAPLGIEVVSLSDLGLPEPEETGDTFEENALIKARAAAKATGLPALADDSGLEVDALGGAPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 83 IYSARYSGVDATDQQNLEKLLVALKDVpDEQRTAQFHCVLVYMRHaeDPTPIVCHGSWPGVITREAAGNGGFGYDPIFFV 162
Cdd:COG0127 81 VYSARYAGEGADDEANNEKLLKLLEGV-DEDRRARFVCVLALADP--DGEPLVFEGEVEGEIAEEPRGEGGFGYDPIFIP 157
|
170 180 190
....*....|....*....|....*....|....
gi 505384737 163 PTEGKTAAELTREEKSAISHRGRALKLLLEALRN 196
Cdd:COG0127 158 DGYGKTFAELSPEEKNAISHRGRALRKLAEWLKE 191
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
3-195 |
1.03e-93 |
|
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: 270.78 E-value: 1.03e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 3 KVVLATGNAGKVRELASLLNDFGLDVVAQTELGvdSAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVDFLGGAPG 82
Cdd:TIGR00042 1 KIVFATGNPGKLKEVQSILSDLGDNEIEQLDLG--YPEETGLTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 83 IYSARYSGvdaTDQQNLEKLLVALKDVpdEQRTAQFHCVLVYMRHAEDPtpIVCHGSWPGVITREAAGNGGFGYDPIFFV 162
Cdd:TIGR00042 79 IYSARYQG---TDIGNLEKILKLLEGV--ENRQAYFVCVIGYCDPNGEP--LVFEGIVKGKITREPRGTYGFGYDPIFIP 151
|
170 180 190
....*....|....*....|....*....|...
gi 505384737 163 PTEGKTAAELTREEKSAISHRGRALKLLLEALR 195
Cdd:TIGR00042 152 PEEGKTFAELTTEEKNKISHRGKAFKKFKKFLL 184
|
|
| Ham1p_like |
pfam01725 |
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ... |
4-192 |
1.89e-93 |
|
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: 270.09 E-value: 1.89e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 4 VVLATGNAGKVRELASLLNDfGLDVVAQTELGVDS-AEETGLTFIENAILKARHAAQiTGLPAIADDSGLAVDFLGGAPG 82
Cdd:pfam01725 1 IVFATGNAGKLRELKAILAD-GIEVLSLKDLGELPeIEETGGTFEENALIKARAAAK-TGLPVLADDSGLEVDALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 83 IYSARYSGVDATDQQNLEKLLVALKdVPDEQRTAQFHCVLVYMRHaeDPTPIVCHGSWPGVITREAAGNGGFGYDPIFFV 162
Cdd:pfam01725 79 VYSARFAGEGGDDEANNAKLLEELE-VPDEDRSARFVCVIALADP--GGPELVFEGEVEGEIVEEPRGEGGFGYDPIFIP 155
|
170 180 190
....*....|....*....|....*....|
gi 505384737 163 PTEGKTAAELTREEKSAISHRGRALKLLLE 192
Cdd:pfam01725 156 PEGGKTFAELSPEEKNAISHRGKALRKLKE 185
|
|
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
4-193 |
2.19e-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: 259.76 E-value: 2.19e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 4 VVLATGNAGKVRELASLLNDFGLDVVAQTELGvdSAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVDFLGGAPGI 83
Cdd:cd00515 1 IVFATGNKGKLKEFKEILAPFGIEVVSLKDII--DIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 84 YSARYSGvDATDQQNLEKLLVALKDvpDEQRTAQFHCVLVYMRHaeDPTPIVCHGSWPGVITREAAGNGGFGYDPIFFVP 163
Cdd:cd00515 79 YSARFAG-EHDDAENNEKLLELLEG--DEDRSAYFVCVIALVDP--DGEPLVFEGEVEGKIVTEPRGTGGFGYDPIFIPE 153
|
170 180 190
....*....|....*....|....*....|
gi 505384737 164 TEGKTAAELTREEKSAISHRGRALKLLLEA 193
Cdd:cd00515 154 GYGKTFAEMSPEEKNAISHRGKALRKLKEF 183
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00120 |
PRK00120 |
dITP/XTP pyrophosphatase; Reviewed |
2-197 |
8.71e-125 |
|
dITP/XTP pyrophosphatase; Reviewed
Pssm-ID: 234648 [Multi-domain] Cd Length: 196 Bit Score: 349.77 E-value: 8.71e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 2 QKVVLATGNAGKVRELASLLNDFGLDVVAQTELGVDSAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVDFLGGAP 81
Cdd:PRK00120 1 MKIVLASHNAGKLRELKALLAPFGIEVVSQGELGVPEPEETGTTFVENALIKARHAAKATGLPALADDSGLCVDALGGAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 82 GIYSARYSGVDATDQQNLEKLLVALKDVPDEQRTAQFHCVLVYMRHaeDPTPIVCHGSWPGVITREAAGNGGFGYDPIFF 161
Cdd:PRK00120 81 GVYSARYAGEGASDAANNEKLLEELKGVPDEDRRARFVCVLVLVRP--DPTPLVAEGRWEGEILWEPRGENGFGYDPIFF 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 505384737 162 VPTEGKTAAELTREEKSAISHRGRALKLLLEALRNG 197
Cdd:PRK00120 159 PPGYGKTFAELTPEEKNAISHRGKALKLLLEALREL 194
|
|
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
3-196 |
3.85e-110 |
|
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];
Pssm-ID: 439897 [Multi-domain] Cd Length: 191 Bit Score: 312.77 E-value: 3.85e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 3 KVVLATGNAGKVRELASLLNDFGLDVVAQTELGVDSAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVDFLGGAPG 82
Cdd:COG0127 1 KLVFATGNAGKLREIRALLAPLGIEVVSLSDLGLPEPEETGDTFEENALIKARAAAKATGLPALADDSGLEVDALGGAPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 83 IYSARYSGVDATDQQNLEKLLVALKDVpDEQRTAQFHCVLVYMRHaeDPTPIVCHGSWPGVITREAAGNGGFGYDPIFFV 162
Cdd:COG0127 81 VYSARYAGEGADDEANNEKLLKLLEGV-DEDRRARFVCVLALADP--DGEPLVFEGEVEGEIAEEPRGEGGFGYDPIFIP 157
|
170 180 190
....*....|....*....|....*....|....
gi 505384737 163 PTEGKTAAELTREEKSAISHRGRALKLLLEALRN 196
Cdd:COG0127 158 DGYGKTFAELSPEEKNAISHRGRALRKLAEWLKE 191
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
3-195 |
1.03e-93 |
|
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: 270.78 E-value: 1.03e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 3 KVVLATGNAGKVRELASLLNDFGLDVVAQTELGvdSAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVDFLGGAPG 82
Cdd:TIGR00042 1 KIVFATGNPGKLKEVQSILSDLGDNEIEQLDLG--YPEETGLTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 83 IYSARYSGvdaTDQQNLEKLLVALKDVpdEQRTAQFHCVLVYMRHAEDPtpIVCHGSWPGVITREAAGNGGFGYDPIFFV 162
Cdd:TIGR00042 79 IYSARYQG---TDIGNLEKILKLLEGV--ENRQAYFVCVIGYCDPNGEP--LVFEGIVKGKITREPRGTYGFGYDPIFIP 151
|
170 180 190
....*....|....*....|....*....|...
gi 505384737 163 PTEGKTAAELTREEKSAISHRGRALKLLLEALR 195
Cdd:TIGR00042 152 PEEGKTFAELTTEEKNKISHRGKAFKKFKKFLL 184
|
|
| Ham1p_like |
pfam01725 |
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ... |
4-192 |
1.89e-93 |
|
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: 270.09 E-value: 1.89e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 4 VVLATGNAGKVRELASLLNDfGLDVVAQTELGVDS-AEETGLTFIENAILKARHAAQiTGLPAIADDSGLAVDFLGGAPG 82
Cdd:pfam01725 1 IVFATGNAGKLRELKAILAD-GIEVLSLKDLGELPeIEETGGTFEENALIKARAAAK-TGLPVLADDSGLEVDALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 83 IYSARYSGVDATDQQNLEKLLVALKdVPDEQRTAQFHCVLVYMRHaeDPTPIVCHGSWPGVITREAAGNGGFGYDPIFFV 162
Cdd:pfam01725 79 VYSARFAGEGGDDEANNAKLLEELE-VPDEDRSARFVCVIALADP--GGPELVFEGEVEGEIVEEPRGEGGFGYDPIFIP 155
|
170 180 190
....*....|....*....|....*....|
gi 505384737 163 PTEGKTAAELTREEKSAISHRGRALKLLLE 192
Cdd:pfam01725 156 PEGGKTFAELSPEEKNAISHRGKALRKLKE 185
|
|
| PRK14822 |
PRK14822 |
XTP/dITP diphosphatase; |
1-194 |
9.33e-91 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184835 [Multi-domain] Cd Length: 200 Bit Score: 264.06 E-value: 9.33e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 1 MQKVVLATGNAGKVRELASLLNDFGLDVVAQTELGVD-SAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVDFLGG 79
Cdd:PRK14822 1 MKEIVIATKNKGKVREFKEIFEKFDIEVKSLADFPPIpEVEETGTTFEENAILKAEAAAKALNKPVIADDSGLEVDALNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 80 APGIYSARYSGVDATDQQNLEKLLVALKDVPDEQRTAQFHCVLVyMRHAEDPTPIVcHGSWPGVITREAAGNGGFGYDPI 159
Cdd:PRK14822 81 APGVYSARYAGEAKDDAANNEKLLKELGGVPFEKRTARFHCVIA-VAFPGGETKTV-EGTCEGEILEEPRGENGFGYDPL 158
|
170 180 190
....*....|....*....|....*....|....*
gi 505384737 160 FFVPTEGKTAAELTREEKSAISHRGRALKLLLEAL 194
Cdd:PRK14822 159 FYVPEKGKTMAELSSEEKNAISHRGKALKKLEAEL 193
|
|
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
4-193 |
2.19e-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: 259.76 E-value: 2.19e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 4 VVLATGNAGKVRELASLLNDFGLDVVAQTELGvdSAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVDFLGGAPGI 83
Cdd:cd00515 1 IVFATGNKGKLKEFKEILAPFGIEVVSLKDII--DIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 84 YSARYSGvDATDQQNLEKLLVALKDvpDEQRTAQFHCVLVYMRHaeDPTPIVCHGSWPGVITREAAGNGGFGYDPIFFVP 163
Cdd:cd00515 79 YSARFAG-EHDDAENNEKLLELLEG--DEDRSAYFVCVIALVDP--DGEPLVFEGEVEGKIVTEPRGTGGFGYDPIFIPE 153
|
170 180 190
....*....|....*....|....*....|
gi 505384737 164 TEGKTAAELTREEKSAISHRGRALKLLLEA 193
Cdd:cd00515 154 GYGKTFAEMSPEEKNAISHRGKALRKLKEF 183
|
|
| PRK02491 |
PRK02491 |
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; ... |
4-193 |
2.41e-60 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed
Pssm-ID: 179431 [Multi-domain] Cd Length: 328 Bit Score: 191.18 E-value: 2.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 4 VVLATGNAGKVRELASLLNDFGLDVVAQTEL-GVDSAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVDFLGGAPG 82
Cdd:PRK02491 130 ILIATRNEGKTKEFRKLFGKLGYKVENLNDYpDLPEVAETGMTFEENARLKAETISRLTGKMVLADDSGLKVDALGGLPG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 83 IYSARYSGVDATDQQNLEKLLVALKDVPD-EQRTAQFHCVLVYMrhAEDPTPIVCHGSWPGVITREAAGNGGFGYDPIFF 161
Cdd:PRK02491 210 VWSARFSGPDATDAENNAKLLHELAMVFDlKDRSAQFHTTLVVA--APNKDSLVVEADWPGYIATEPKGENGFGYDPLFL 287
|
170 180 190
....*....|....*....|....*....|..
gi 505384737 162 VPTEGKTAAELTREEKSAISHRGRALKLLLEA 193
Cdd:PRK02491 288 VGETGRHAAELTAEEKNQLSHRGQAVKKLMEV 319
|
|
| PRK14824 |
PRK14824 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
3-197 |
1.19e-53 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 237824 [Multi-domain] Cd Length: 201 Bit Score: 169.94 E-value: 1.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 3 KVVLATGNAGKVRELASLLNDFGLDVVAQTE-LGVdsaEETGLTFIENAILKARHAAQITGLPAIADDSGLAVDFLGGAP 81
Cdd:PRK14824 2 KILLATTNEGKVREIKRLLSDLGIEVLSPDKkIEV---EEDGETFLENAYLKARAYAEFYKIPVLADDSGLEVPALEGYP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 82 GIYSARYSGVD---------ATDQQNLEKLLVALKDvpDEQRTAQFHCVLV-YMRHAEDPTPIVCHGSwpgvITREAAGN 151
Cdd:PRK14824 79 GVYSSRFYQIEfggkeevveSKDEANIRKLLRLLEG--KQNRKARFVAFVVlYFGDWGIWTEGECRGK----IAEEPRGS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505384737 152 GGFGYDPIfFVPtEG--KTAAELTREEKSAISHRGRALKLLLEALRNG 197
Cdd:PRK14824 153 GGFGYDPV-FIP-EGynKTMAELSPEEKNKISHRGKAVRKLVEILKYG 198
|
|
| PRK14826 |
PRK14826 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
4-196 |
7.48e-52 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173287 Cd Length: 222 Bit Score: 166.00 E-value: 7.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 4 VVLATGNAGKVRELASLLN--DFGLDVVAQTELGVDSA-EETGLTFIENAILKARH-----AAQITGLPAIADDSGLAVD 75
Cdd:PRK14826 11 IVLATGNRDKVRELRPLLEhiSPLFSVRSLADLGVEVDiEETEETLEGNALLKADAifellSDRFPFLIALADDTGLEVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 76 FLGGAPGIYSARYS----GVDATDQQNLEKLLVALKDVPDeqRTAQFHCVLVY---MRHAEDPTPI--VCHGSWPGVITR 146
Cdd:PRK14826 91 ALGGAPGVYSARFApvpeGEKPTYEDNVRHLLSEMEGKTE--RSARFRTVIALkgrLPGKNGAFEFeeTAEGVVEGSITT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505384737 147 EAAGNGGFGYDPIFFVPTEGKTAAELTREEKSAISHRGRALKLLLEALRN 196
Cdd:PRK14826 169 EKKGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRALAVQKAVKFLRT 218
|
|
| PRK14823 |
PRK14823 |
putative deoxyribonucleoside-triphosphatase; Provisional |
3-196 |
1.60e-49 |
|
putative deoxyribonucleoside-triphosphatase; Provisional
Pssm-ID: 237823 [Multi-domain] Cd Length: 191 Bit Score: 159.08 E-value: 1.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 3 KVVLATGNAGKVRELASLLNDfGLDVVAQTELGV-DSAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVDFLGGAP 81
Cdd:PRK14823 2 KLVFATNNKHKLEEIRSILPE-KIELLSLSDIGChEDIPETADTLEGNALLKAEYVYKKYGYDCFADDTGLEVEALNGAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 82 GIYSARYSGVDATDQQNLEKLLVALKDVPDeqRTAQFHCVL-VYMRHAEDPTPIVCHGSwpgvITREAAGNGGFGYDPIF 160
Cdd:PRK14823 81 GVYSARYAGGEHNAEANMRKLLEELEGKDN--RKAQFRTVIaLILDGKEHLFEGIIKGE----IIKEKRGDSGFGYDPIF 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 505384737 161 FVPTEGKTAAELTREEKSAISHRGRALKLLLEALRN 196
Cdd:PRK14823 155 VPEGYDKTFAELGLEIKNQISHRAKAVQKLIDFLSK 190
|
|
| PRK14821 |
PRK14821 |
XTP/dITP diphosphatase; |
3-196 |
2.07e-38 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184834 [Multi-domain] Cd Length: 184 Bit Score: 130.46 E-value: 2.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 3 KVVLATGNAGKVRELASLLNDFGLDVVAQT----ELGVDSAEETgltfienAILKARHAAQITGLPAIADDSGLAVDFLG 78
Cdd:PRK14821 2 KIYFATGNKGKVEEAKIILKPLGIEVEQIKieypEIQADTLEEV-------AAFGAKWVYNKLNRPVIVEDSGLFIEALN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 79 GAPGIYSArYsgvdATDQQNLEKLLVALKDVpdEQRTAQFHCVLVYMRHAEDP--TPIVChgswpGVITREAAGNGGFGY 156
Cdd:PRK14821 75 GFPGPYSA-F----VYKTLGNEGILKLLEGE--ENRRAYFKSVIGYCDPGGEKlfTGIVE-----GKIANEIRGKGGFGY 142
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505384737 157 DPIFFVPTEGKTAAELTREEKSAISHRGRALKLLLEALRN 196
Cdd:PRK14821 143 DPIFIPEGEEKTFAEMTTEEKNKISHRKRAFDEFKEWLKE 182
|
|
| Maf_Ham1 |
cd00985 |
Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum ... |
4-144 |
7.05e-27 |
|
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: 99.11 E-value: 7.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 4 VVLATGNAGKVRELASLLndfGLDVVAQTeLGVD---SAEETGLTFIENAILKARHAAQITG-LPAIADDSGLAVDflgG 79
Cdd:cd00985 1 LILASGSPRRLEELKQIG---GIEFEVLP-SDIDetgLKGEPEDTVEELALLKARAVAERLPdAPVIADDTGLVVD---G 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505384737 80 APGIYSARYSGvdatdqqnlekllVALKDVPDEQRTAQFHCVLVYMRHaeDPTPIVCHGSWPGVI 144
Cdd:cd00985 74 RPGGKPARFAE-------------ALEMLRGLSGRTAEFVTAVALVDP--DGKIITFEGETEGKI 123
|
|
| PRK14825 |
PRK14825 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
1-194 |
4.79e-26 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173286 Cd Length: 199 Bit Score: 99.24 E-value: 4.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 1 MQKVVLATGNAGKVRELASLLNDFGLDVVAQTELGVdsaEETGLTFIENAILKARHAAQITG--LPAIADDSGLAVDFLG 78
Cdd:PRK14825 1 MKTLFFATTNINKINEVKQILDIPNIKIEIPQNFDI---KETGKTFKENSLLKAKALFEILNnkQPVFSEDSGLCIEALN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384737 79 GAPGIYSARYsgvdatDQQNLEK----------LLVALKDvpDEQRTAQFHCVLVYMrhAEDPTPIVCHGSWPGVITR-- 146
Cdd:PRK14825 78 LEPGIYSKRY------DQYKLGKklstneknhlIIDLMKN--EKNRTAYFICNISYI--SKDGTILNFEGIIKGTIALsi 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505384737 147 EAAGNGGFGYDPIFFVpTEGKTAAELTREEKSAISHRGRAL----KLLLEAL 194
Cdd:PRK14825 148 DDYKKNGFGYDPIFLT-KNNKRLSELTLEEKNKISHRGIAFdkfkKFLMQSL 198
|
|
| |
