|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00120 |
PRK00120 |
dITP/XTP pyrophosphatase; Reviewed |
5-194 |
2.58e-112 |
|
dITP/XTP pyrophosphatase; Reviewed
Pssm-ID: 234648 [Multi-domain] Cd Length: 196 Bit Score: 318.18 E-value: 2.58e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 5 QLVLASHNGGKLKELQAMLGGS-VTLRSVSEFSLVEPEETGLSFVENAILKARNAARLSGLPALADDSGLAVDFLGGAPG 83
Cdd:PRK00120 2 KIVLASHNAGKLRELKALLAPFgIEVVSQGELGVPEPEETGTTFVENALIKARHAAKATGLPALADDSGLCVDALGGAPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 84 IYSARYAD-GQGDAANNAKLLEALKDVPDEQRGAQFVCVLALVRHadDPLPILCEGLWHGRILHAASGEHGFGYDPLFWV 162
Cdd:PRK00120 82 VYSARYAGeGASDAANNEKLLEELKGVPDEDRRARFVCVLVLVRP--DPTPLVAEGRWEGEILWEPRGENGFGYDPIFFP 159
|
170 180 190
....*....|....*....|....*....|..
gi 695636957 163 PERNCSSAELGPTEKNQLSHRARAMVLLRQRL 194
Cdd:PRK00120 160 PGYGKTFAELTPEEKNAISHRGKALKLLLEAL 191
|
|
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
5-194 |
2.24e-102 |
|
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];
Pssm-ID: 439897 [Multi-domain] Cd Length: 191 Bit Score: 293.12 E-value: 2.24e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 5 QLVLASHNGGKLKELQAMLGG-SVTLRSVSEFSLVEPEETGLSFVENAILKARNAARLSGLPALADDSGLAVDFLGGAPG 83
Cdd:COG0127 1 KLVFATGNAGKLREIRALLAPlGIEVVSLSDLGLPEPEETGDTFEENALIKARAAAKATGLPALADDSGLEVDALGGAPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 84 IYSARYADGQG-DAANNAKLLEALKDVpDEQRGAQFVCVLALVRHadDPLPILCEGLWHGRILHAASGEHGFGYDPLFWV 162
Cdd:COG0127 81 VYSARYAGEGAdDEANNEKLLKLLEGV-DEDRRARFVCVLALADP--DGEPLVFEGEVEGEIAEEPRGEGGFGYDPIFIP 157
|
170 180 190
....*....|....*....|....*....|..
gi 695636957 163 PERNCSSAELGPTEKNQLSHRARAMVLLRQRL 194
Cdd:COG0127 158 DGYGKTFAELSPEEKNAISHRGRALRKLAEWL 189
|
|
| Ham1p_like |
pfam01725 |
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ... |
6-193 |
8.56e-92 |
|
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: 265.85 E-value: 8.56e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 6 LVLASHNGGKLKELQAMLGGSVTLRSVSEF-SLVEPEETGLSFVENAILKARNAARlSGLPALADDSGLAVDFLGGAPGI 84
Cdd:pfam01725 1 IVFATGNAGKLRELKAILADGIEVLSLKDLgELPEIEETGGTFEENALIKARAAAK-TGLPVLADDSGLEVDALNGFPGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 85 YSARYADGQG-DAANNAKLLEALKdVPDEQRGAQFVCVLALVRHadDPLPILCEGLWHGRILHAASGEHGFGYDPLFWVP 163
Cdd:pfam01725 80 YSARFAGEGGdDEANNAKLLEELE-VPDEDRSARFVCVIALADP--GGPELVFEGEVEGEIVEEPRGEGGFGYDPIFIPP 156
|
170 180 190
....*....|....*....|....*....|
gi 695636957 164 ERNCSSAELGPTEKNQLSHRARAMVLLRQR 193
Cdd:pfam01725 157 EGGKTFAELSPEEKNAISHRGKALRKLKEF 186
|
|
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
6-192 |
1.39e-87 |
|
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: 255.14 E-value: 1.39e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 6 LVLASHNGGKLKELQAMLGGS-VTLRSVSEfsLVEPEETGLSFVENAILKARNAARLSGLPALADDSGLAVDFLGGAPGI 84
Cdd:cd00515 1 IVFATGNKGKLKEFKEILAPFgIEVVSLKD--IIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 85 YSARYADGQGDAANNAKLLEALKDvpDEQRGAQFVCVLALVRHadDPLPILCEGLWHGRILHAASGEHGFGYDPLFWVPE 164
Cdd:cd00515 79 YSARFAGEHDDAENNEKLLELLEG--DEDRSAYFVCVIALVDP--DGEPLVFEGEVEGKIVTEPRGTGGFGYDPIFIPEG 154
|
170 180
....*....|....*....|....*...
gi 695636957 165 RNCSSAELGPTEKNQLSHRARAMVLLRQ 192
Cdd:cd00515 155 YGKTFAEMSPEEKNAISHRGKALRKLKE 182
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
6-194 |
6.32e-67 |
|
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: 202.98 E-value: 6.32e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 6 LVLASHNGGKLKELQAMLGGSVtLRSVSEFSLVEPEETGLSFVENAILKARNAARLSGLPALADDSGLAVDFLGGAPGIY 85
Cdd:TIGR00042 2 IVFATGNPGKLKEVQSILSDLG-DNEIEQLDLGYPEETGLTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 86 SARYADgqGDAANNAKLLEALKDVpdEQRGAQFVCVLALVRHADDPLpiLCEGLWHGRILHAASGEHGFGYDPLFWVPER 165
Cdd:TIGR00042 81 SARYQG--TDIGNLEKILKLLEGV--ENRQAYFVCVIGYCDPNGEPL--VFEGIVKGKITREPRGTYGFGYDPIFIPPEE 154
|
170 180
....*....|....*....|....*....
gi 695636957 166 NCSSAELGPTEKNQLSHRARAMVLLRQRL 194
Cdd:TIGR00042 155 GKTFAELTTEEKNKISHRGKAFKKFKKFL 183
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00120 |
PRK00120 |
dITP/XTP pyrophosphatase; Reviewed |
5-194 |
2.58e-112 |
|
dITP/XTP pyrophosphatase; Reviewed
Pssm-ID: 234648 [Multi-domain] Cd Length: 196 Bit Score: 318.18 E-value: 2.58e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 5 QLVLASHNGGKLKELQAMLGGS-VTLRSVSEFSLVEPEETGLSFVENAILKARNAARLSGLPALADDSGLAVDFLGGAPG 83
Cdd:PRK00120 2 KIVLASHNAGKLRELKALLAPFgIEVVSQGELGVPEPEETGTTFVENALIKARHAAKATGLPALADDSGLCVDALGGAPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 84 IYSARYAD-GQGDAANNAKLLEALKDVPDEQRGAQFVCVLALVRHadDPLPILCEGLWHGRILHAASGEHGFGYDPLFWV 162
Cdd:PRK00120 82 VYSARYAGeGASDAANNEKLLEELKGVPDEDRRARFVCVLVLVRP--DPTPLVAEGRWEGEILWEPRGENGFGYDPIFFP 159
|
170 180 190
....*....|....*....|....*....|..
gi 695636957 163 PERNCSSAELGPTEKNQLSHRARAMVLLRQRL 194
Cdd:PRK00120 160 PGYGKTFAELTPEEKNAISHRGKALKLLLEAL 191
|
|
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
5-194 |
2.24e-102 |
|
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];
Pssm-ID: 439897 [Multi-domain] Cd Length: 191 Bit Score: 293.12 E-value: 2.24e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 5 QLVLASHNGGKLKELQAMLGG-SVTLRSVSEFSLVEPEETGLSFVENAILKARNAARLSGLPALADDSGLAVDFLGGAPG 83
Cdd:COG0127 1 KLVFATGNAGKLREIRALLAPlGIEVVSLSDLGLPEPEETGDTFEENALIKARAAAKATGLPALADDSGLEVDALGGAPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 84 IYSARYADGQG-DAANNAKLLEALKDVpDEQRGAQFVCVLALVRHadDPLPILCEGLWHGRILHAASGEHGFGYDPLFWV 162
Cdd:COG0127 81 VYSARYAGEGAdDEANNEKLLKLLEGV-DEDRRARFVCVLALADP--DGEPLVFEGEVEGEIAEEPRGEGGFGYDPIFIP 157
|
170 180 190
....*....|....*....|....*....|..
gi 695636957 163 PERNCSSAELGPTEKNQLSHRARAMVLLRQRL 194
Cdd:COG0127 158 DGYGKTFAELSPEEKNAISHRGRALRKLAEWL 189
|
|
| Ham1p_like |
pfam01725 |
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ... |
6-193 |
8.56e-92 |
|
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: 265.85 E-value: 8.56e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 6 LVLASHNGGKLKELQAMLGGSVTLRSVSEF-SLVEPEETGLSFVENAILKARNAARlSGLPALADDSGLAVDFLGGAPGI 84
Cdd:pfam01725 1 IVFATGNAGKLRELKAILADGIEVLSLKDLgELPEIEETGGTFEENALIKARAAAK-TGLPVLADDSGLEVDALNGFPGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 85 YSARYADGQG-DAANNAKLLEALKdVPDEQRGAQFVCVLALVRHadDPLPILCEGLWHGRILHAASGEHGFGYDPLFWVP 163
Cdd:pfam01725 80 YSARFAGEGGdDEANNAKLLEELE-VPDEDRSARFVCVIALADP--GGPELVFEGEVEGEIVEEPRGEGGFGYDPIFIPP 156
|
170 180 190
....*....|....*....|....*....|
gi 695636957 164 ERNCSSAELGPTEKNQLSHRARAMVLLRQR 193
Cdd:pfam01725 157 EGGKTFAELSPEEKNAISHRGKALRKLKEF 186
|
|
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
6-192 |
1.39e-87 |
|
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: 255.14 E-value: 1.39e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 6 LVLASHNGGKLKELQAMLGGS-VTLRSVSEfsLVEPEETGLSFVENAILKARNAARLSGLPALADDSGLAVDFLGGAPGI 84
Cdd:cd00515 1 IVFATGNKGKLKEFKEILAPFgIEVVSLKD--IIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 85 YSARYADGQGDAANNAKLLEALKDvpDEQRGAQFVCVLALVRHadDPLPILCEGLWHGRILHAASGEHGFGYDPLFWVPE 164
Cdd:cd00515 79 YSARFAGEHDDAENNEKLLELLEG--DEDRSAYFVCVIALVDP--DGEPLVFEGEVEGKIVTEPRGTGGFGYDPIFIPEG 154
|
170 180
....*....|....*....|....*...
gi 695636957 165 RNCSSAELGPTEKNQLSHRARAMVLLRQ 192
Cdd:cd00515 155 YGKTFAEMSPEEKNAISHRGKALRKLKE 182
|
|
| PRK14822 |
PRK14822 |
XTP/dITP diphosphatase; |
4-194 |
1.19e-81 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184835 [Multi-domain] Cd Length: 200 Bit Score: 240.95 E-value: 1.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 4 TQLVLASHNGGKLKELQAMLGGS-VTLRSVSEFS-LVEPEETGLSFVENAILKARNAARLSGLPALADDSGLAVDFLGGA 81
Cdd:PRK14822 2 KEIVIATKNKGKVREFKEIFEKFdIEVKSLADFPpIPEVEETGTTFEENAILKAEAAAKALNKPVIADDSGLEVDALNGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 82 PGIYSARYA-DGQGDAANNAKLLEALKDVPDEQRGAQFVCVLALVRHADDPLPIlcEGLWHGRILHAASGEHGFGYDPLF 160
Cdd:PRK14822 82 PGVYSARYAgEAKDDAANNEKLLKELGGVPFEKRTARFHCVIAVAFPGGETKTV--EGTCEGEILEEPRGENGFGYDPLF 159
|
170 180 190
....*....|....*....|....*....|....
gi 695636957 161 WVPERNCSSAELGPTEKNQLSHRARAMVLLRQRL 194
Cdd:PRK14822 160 YVPEKGKTMAELSSEEKNAISHRGKALKKLEAEL 193
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
6-194 |
6.32e-67 |
|
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: 202.98 E-value: 6.32e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 6 LVLASHNGGKLKELQAMLGGSVtLRSVSEFSLVEPEETGLSFVENAILKARNAARLSGLPALADDSGLAVDFLGGAPGIY 85
Cdd:TIGR00042 2 IVFATGNPGKLKEVQSILSDLG-DNEIEQLDLGYPEETGLTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 86 SARYADgqGDAANNAKLLEALKDVpdEQRGAQFVCVLALVRHADDPLpiLCEGLWHGRILHAASGEHGFGYDPLFWVPER 165
Cdd:TIGR00042 81 SARYQG--TDIGNLEKILKLLEGV--ENRQAYFVCVIGYCDPNGEPL--VFEGIVKGKITREPRGTYGFGYDPIFIPPEE 154
|
170 180
....*....|....*....|....*....
gi 695636957 166 NCSSAELGPTEKNQLSHRARAMVLLRQRL 194
Cdd:TIGR00042 155 GKTFAELTTEEKNKISHRGKAFKKFKKFL 183
|
|
| PRK14823 |
PRK14823 |
putative deoxyribonucleoside-triphosphatase; Provisional |
5-195 |
3.76e-55 |
|
putative deoxyribonucleoside-triphosphatase; Provisional
Pssm-ID: 237823 [Multi-domain] Cd Length: 191 Bit Score: 173.33 E-value: 3.76e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 5 QLVLASHNGGKLKELQAMLGGSVTLRSVSEFSLVEP-EETGLSFVENAILKARNAARLSGLPALADDSGLAVDFLGGAPG 83
Cdd:PRK14823 2 KLVFATNNKHKLEEIRSILPEKIELLSLSDIGCHEDiPETADTLEGNALLKAEYVYKKYGYDCFADDTGLEVEALNGAPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 84 IYSARYADGQGDA-ANNAKLLEALKDVPDeqRGAQFVCVLALVrhaDDPLPILCEGLWHGRILHAASGEHGFGYDPLFwV 162
Cdd:PRK14823 82 VYSARYAGGEHNAeANMRKLLEELEGKDN--RKAQFRTVIALI---LDGKEHLFEGIIKGEIIKEKRGDSGFGYDPIF-V 155
|
170 180 190
....*....|....*....|....*....|....
gi 695636957 163 PE-RNCSSAELGPTEKNQLSHRARAMVLLRQRLG 195
Cdd:PRK14823 156 PEgYDKTFAELGLEIKNQISHRAKAVQKLIDFLS 189
|
|
| PRK02491 |
PRK02491 |
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; ... |
6-187 |
2.01e-49 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed
Pssm-ID: 179431 [Multi-domain] Cd Length: 328 Bit Score: 163.06 E-value: 2.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 6 LVLASHNGGKLKELQAMLGG-SVTLRSVSEF-SLVEPEETGLSFVENAILKARNAARLSGLPALADDSGLAVDFLGGAPG 83
Cdd:PRK02491 130 ILIATRNEGKTKEFRKLFGKlGYKVENLNDYpDLPEVAETGMTFEENARLKAETISRLTGKMVLADDSGLKVDALGGLPG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 84 IYSARYAD-GQGDAANNAKLLEALKDVPD-EQRGAQFVCvlALVRHADDPLPILCEGLWHGRILHAASGEHGFGYDPLFW 161
Cdd:PRK02491 210 VWSARFSGpDATDAENNAKLLHELAMVFDlKDRSAQFHT--TLVVAAPNKDSLVVEADWPGYIATEPKGENGFGYDPLFL 287
|
170 180
....*....|....*....|....*.
gi 695636957 162 VPERNCSSAELGPTEKNQLSHRARAM 187
Cdd:PRK02491 288 VGETGRHAAELTAEEKNQLSHRGQAV 313
|
|
| PRK14826 |
PRK14826 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
4-186 |
8.16e-45 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173287 Cd Length: 222 Bit Score: 147.89 E-value: 8.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 4 TQLVLASHNGGKLKELQAMLGG---SVTLRSVSEFSL-VEPEETGLSFVENAILKARN-----AARLSGLPALADDSGLA 74
Cdd:PRK14826 9 ITIVLATGNRDKVRELRPLLEHispLFSVRSLADLGVeVDIEETEETLEGNALLKADAifellSDRFPFLIALADDTGLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 75 VDFLGGAPGIYSARYA---DGQGD--AANNAKLLEALKDVPDeqRGAQFVCVLAL---VRHADDPLPI--LCEGLWHGRI 144
Cdd:PRK14826 89 VDALGGAPGVYSARFApvpEGEKPtyEDNVRHLLSEMEGKTE--RSARFRTVIALkgrLPGKNGAFEFeeTAEGVVEGSI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695636957 145 LHAASGEHGFGYDPLFWVPERNCSSAELGPTEKNQLSHRARA 186
Cdd:PRK14826 167 TTEKKGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRALA 208
|
|
| PRK14824 |
PRK14824 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
5-187 |
2.20e-42 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 237824 [Multi-domain] Cd Length: 201 Bit Score: 141.05 E-value: 2.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 5 QLVLASHNGGKLKELQAMLGGS-VTLRSVSEFslVEPEETGLSFVENAILKARNAARLSGLPALADDSGLAVDFLGGAPG 83
Cdd:PRK14824 2 KILLATTNEGKVREIKRLLSDLgIEVLSPDKK--IEVEEDGETFLENAYLKARAYAEFYKIPVLADDSGLEVPALEGYPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 84 IYSARYAD----------GQGDAANNAKLLEALKDvpDEQRGAQFVCVLALvrhADDPLPILCEGLWHGRILHAASGEHG 153
Cdd:PRK14824 80 VYSSRFYQiefggkeevvESKDEANIRKLLRLLEG--KQNRKARFVAFVVL---YFGDWGIWTEGECRGKIAEEPRGSGG 154
|
170 180 190
....*....|....*....|....*....|....*
gi 695636957 154 FGYDPLFwVPE-RNCSSAELGPTEKNQLSHRARAM 187
Cdd:PRK14824 155 FGYDPVF-IPEgYNKTMAELSPEEKNKISHRGKAV 188
|
|
| Maf_Ham1 |
cd00985 |
Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum ... |
6-144 |
7.28e-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: 7.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 6 LVLASHNGGKLKELQAMLGgsVTLRSVSEfslvEPEETGL------SFVENAILKARNAA-RLSGLPALADDSGLAVDfl 78
Cdd:cd00985 1 LILASGSPRRLEELKQIGG--IEFEVLPS----DIDETGLkgepedTVEELALLKARAVAeRLPDAPVIADDTGLVVD-- 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695636957 79 gGAPGIYSARYADgqgdaannakllEALKDVPDEQRGAQFVCVLALVRHadDPLPILCEGLWHGRI 144
Cdd:cd00985 73 -GRPGGKPARFAE------------ALEMLRGLSGRTAEFVTAVALVDP--DGKIITFEGETEGKI 123
|
|
| PRK14821 |
PRK14821 |
XTP/dITP diphosphatase; |
6-186 |
7.92e-22 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184834 [Multi-domain] Cd Length: 184 Bit Score: 87.70 E-value: 7.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 6 LVLASHNGGKLKELQAMLGG----------------SVTLRSVSEFslvepeetGLSFVENAILKarnaarlsglPALAD 69
Cdd:PRK14821 3 IYFATGNKGKVEEAKIILKPlgieveqikieypeiqADTLEEVAAF--------GAKWVYNKLNR----------PVIVE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 70 DSGLAVDFLGGAPGIYSARYADGQGdaanNAKLLEALKDVpdEQRGAQFVCVLALVrhADDPLPILcEGLWHGRILHAAS 149
Cdd:PRK14821 65 DSGLFIEALNGFPGPYSAFVYKTLG----NEGILKLLEGE--ENRRAYFKSVIGYC--DPGGEKLF-TGIVEGKIANEIR 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 695636957 150 GEHGFGYDPLFwVPE-RNCSSAELGPTEKNQLSHRARA 186
Cdd:PRK14821 136 GKGGFGYDPIF-IPEgEEKTFAEMTTEEKNKISHRKRA 172
|
|
| PRK14825 |
PRK14825 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
6-194 |
6.49e-19 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173286 Cd Length: 199 Bit Score: 80.36 E-value: 6.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 6 LVLASHNGGKLKELQAMLG-GSVTLRSVSEFSLvepEETGLSFVENAILKARNAARLSG--LPALADDSGLAVDFLGGAP 82
Cdd:PRK14825 4 LFFATTNINKINEVKQILDiPNIKIEIPQNFDI---KETGKTFKENSLLKAKALFEILNnkQPVFSEDSGLCIEALNLEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695636957 83 GIYSARYADGQ-----GDAANNAKLLEALKDvpDEQRGAQFVCVLALVrhADDPLPILCEGLWHGRILHAAS--GEHGFG 155
Cdd:PRK14825 81 GIYSKRYDQYKlgkklSTNEKNHLIIDLMKN--EKNRTAYFICNISYI--SKDGTILNFEGIIKGTIALSIDdyKKNGFG 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 695636957 156 YDPLFwVPERNCSSAELGPTEKNQLSHRARAMVLLRQRL 194
Cdd:PRK14825 157 YDPIF-LTKNNKRLSELTLEEKNKISHRGIAFDKFKKFL 194
|
|
| |
