|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14822 |
PRK14822 |
XTP/dITP diphosphatase; |
1-195 |
1.05e-116 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184835 [Multi-domain] Cd Length: 200 Bit Score: 329.54 E-value: 1.05e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 1 MKEIVIASNNQGKINDFKVIF--PDYHVIGISELIPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNG 78
Cdd:PRK14822 1 MKEIVIATKNKGKVREFKEIFekFDIEVKSLADFPPIPEVEETGTTFEENAILKAEAAAKALNKPVIADDSGLEVDALNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 79 EPGIYSARYAGENKSDEANIEKLLNKLGNT--TDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGENGFGYDPIFY 156
Cdd:PRK14822 81 APGVYSARYAGEAKDDAANNEKLLKELGGVpfEKRTARFHCVIAVAFPGGETKTVEGTCEGEILEEPRGENGFGYDPLFY 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 577530842 157 VPKLDKTMAQLSKEQKGQISHRRNAINLLQAFLEGEKNV 195
Cdd:PRK14822 161 VPEKGKTMAELSSEEKNAISHRGKALKKLEAELPEWLKV 199
|
|
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
3-191 |
1.35e-96 |
|
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];
Pssm-ID: 439897 [Multi-domain] Cd Length: 191 Bit Score: 278.10 E-value: 1.35e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 3 EIVIASNNQGKINDFKVIFPDYH--VIGISELiPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEP 80
Cdd:COG0127 1 KLVFATGNAGKLREIRALLAPLGieVVSLSDL-GLPEPEETGDTFEENALIKARAAAKATGLPALADDSGLEVDALGGAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 81 GIYSARYAGENKSDEANIEKLLNKLGNT-TDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGENGFGYDPIFYVPK 159
Cdd:COG0127 80 GVYSARYAGEGADDEANNEKLLKLLEGVdEDRRARFVCVLALADPDGEPLVFEGEVEGEIAEEPRGEGGFGYDPIFIPDG 159
|
170 180 190
....*....|....*....|....*....|..
gi 577530842 160 LDKTMAQLSKEQKGQISHRRNAINLLQAFLEG 191
Cdd:COG0127 160 YGKTFAELSPEEKNAISHRGRALRKLAEWLKE 191
|
|
| Ham1p_like |
pfam01725 |
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ... |
4-188 |
7.88e-90 |
|
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: 260.85 E-value: 7.88e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 4 IVIASNNQGKINDFKVIF-PDYHVIGISELIPDFDVEETGSTFEENAILKSEAAAKaLNKTVIADDSGLEVFALNGEPGI 82
Cdd:pfam01725 1 IVFATGNAGKLRELKAILaDGIEVLSLKDLGELPEIEETGGTFEENALIKARAAAK-TGLPVLADDSGLEVDALNGFPGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 83 YSARYAGENKSDEANIEKLLNKL-GNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGENGFGYDPIFYVPKLD 161
Cdd:pfam01725 80 YSARFAGEGGDDEANNAKLLEELeVPDEDRSARFVCVIALADPGGPELVFEGEVEGEIVEEPRGEGGFGYDPIFIPPEGG 159
|
170 180
....*....|....*....|....*..
gi 577530842 162 KTMAQLSKEQKGQISHRRNAINLLQAF 188
Cdd:pfam01725 160 KTFAELSPEEKNAISHRGKALRKLKEF 186
|
|
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
4-188 |
2.88e-86 |
|
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: 252.06 E-value: 2.88e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 4 IVIASNNQGKINDFKVIFPDYhVIGISELIPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEPGIY 83
Cdd:cd00515 1 IVFATGNKGKLKEFKEILAPF-GIEVVSLKDIIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 84 SARYAGENkSDEANIEKLLNKLGNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGENGFGYDPIFYVPKLDKT 163
Cdd:cd00515 80 SARFAGEH-DDAENNEKLLELLEGDEDRSAYFVCVIALVDPDGEPLVFEGEVEGKIVTEPRGTGGFGYDPIFIPEGYGKT 158
|
170 180
....*....|....*....|....*
gi 577530842 164 MAQLSKEQKGQISHRRNAINLLQAF 188
Cdd:cd00515 159 FAEMSPEEKNAISHRGKALRKLKEF 183
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
3-190 |
7.06e-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: 7.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 3 EIVIASNNQGKINDFKVIFPDYHVIGISELIPDFdVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEPGI 82
Cdd:TIGR00042 1 KIVFATGNPGKLKEVQSILSDLGDNEIEQLDLGY-PEETGLTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 83 YSARYAGenkSDEANIEKLLNKLGNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGENGFGYDPIFYVPKLDK 162
Cdd:TIGR00042 80 YSARYQG---TDIGNLEKILKLLEGVENRQAYFVCVIGYCDPNGEPLVFEGIVKGKITREPRGTYGFGYDPIFIPPEEGK 156
|
170 180
....*....|....*....|....*...
gi 577530842 163 TMAQLSKEQKGQISHRRNAINLLQAFLE 190
Cdd:TIGR00042 157 TFAELTTEEKNKISHRGKAFKKFKKFLL 184
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14822 |
PRK14822 |
XTP/dITP diphosphatase; |
1-195 |
1.05e-116 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184835 [Multi-domain] Cd Length: 200 Bit Score: 329.54 E-value: 1.05e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 1 MKEIVIASNNQGKINDFKVIF--PDYHVIGISELIPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNG 78
Cdd:PRK14822 1 MKEIVIATKNKGKVREFKEIFekFDIEVKSLADFPPIPEVEETGTTFEENAILKAEAAAKALNKPVIADDSGLEVDALNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 79 EPGIYSARYAGENKSDEANIEKLLNKLGNT--TDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGENGFGYDPIFY 156
Cdd:PRK14822 81 APGVYSARYAGEAKDDAANNEKLLKELGGVpfEKRTARFHCVIAVAFPGGETKTVEGTCEGEILEEPRGENGFGYDPLFY 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 577530842 157 VPKLDKTMAQLSKEQKGQISHRRNAINLLQAFLEGEKNV 195
Cdd:PRK14822 161 VPEKGKTMAELSSEEKNAISHRGKALKKLEAELPEWLKV 199
|
|
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
3-191 |
1.35e-96 |
|
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];
Pssm-ID: 439897 [Multi-domain] Cd Length: 191 Bit Score: 278.10 E-value: 1.35e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 3 EIVIASNNQGKINDFKVIFPDYH--VIGISELiPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEP 80
Cdd:COG0127 1 KLVFATGNAGKLREIRALLAPLGieVVSLSDL-GLPEPEETGDTFEENALIKARAAAKATGLPALADDSGLEVDALGGAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 81 GIYSARYAGENKSDEANIEKLLNKLGNT-TDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGENGFGYDPIFYVPK 159
Cdd:COG0127 80 GVYSARYAGEGADDEANNEKLLKLLEGVdEDRRARFVCVLALADPDGEPLVFEGEVEGEIAEEPRGEGGFGYDPIFIPDG 159
|
170 180 190
....*....|....*....|....*....|..
gi 577530842 160 LDKTMAQLSKEQKGQISHRRNAINLLQAFLEG 191
Cdd:COG0127 160 YGKTFAELSPEEKNAISHRGRALRKLAEWLKE 191
|
|
| Ham1p_like |
pfam01725 |
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ... |
4-188 |
7.88e-90 |
|
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: 260.85 E-value: 7.88e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 4 IVIASNNQGKINDFKVIF-PDYHVIGISELIPDFDVEETGSTFEENAILKSEAAAKaLNKTVIADDSGLEVFALNGEPGI 82
Cdd:pfam01725 1 IVFATGNAGKLRELKAILaDGIEVLSLKDLGELPEIEETGGTFEENALIKARAAAK-TGLPVLADDSGLEVDALNGFPGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 83 YSARYAGENKSDEANIEKLLNKL-GNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGENGFGYDPIFYVPKLD 161
Cdd:pfam01725 80 YSARFAGEGGDDEANNAKLLEELeVPDEDRSARFVCVIALADPGGPELVFEGEVEGEIVEEPRGEGGFGYDPIFIPPEGG 159
|
170 180
....*....|....*....|....*..
gi 577530842 162 KTMAQLSKEQKGQISHRRNAINLLQAF 188
Cdd:pfam01725 160 KTFAELSPEEKNAISHRGKALRKLKEF 186
|
|
| PRK00120 |
PRK00120 |
dITP/XTP pyrophosphatase; Reviewed |
2-190 |
3.21e-88 |
|
dITP/XTP pyrophosphatase; Reviewed
Pssm-ID: 234648 [Multi-domain] Cd Length: 196 Bit Score: 257.32 E-value: 3.21e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 2 KEIVIASNNQGKINDFKVIFPDYH--VIGISELiPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGE 79
Cdd:PRK00120 1 MKIVLASHNAGKLRELKALLAPFGieVVSQGEL-GVPEPEETGTTFVENALIKARHAAKATGLPALADDSGLCVDALGGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 80 PGIYSARYAGENKSDEANIEKLLNKLGNT--TDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGENGFGYDPIFYV 157
Cdd:PRK00120 80 PGVYSARYAGEGASDAANNEKLLEELKGVpdEDRRARFVCVLVLVRPDPTPLVAEGRWEGEILWEPRGENGFGYDPIFFP 159
|
170 180 190
....*....|....*....|....*....|...
gi 577530842 158 PKLDKTMAQLSKEQKGQISHRRNAINLLQAFLE 190
Cdd:PRK00120 160 PGYGKTFAELTPEEKNAISHRGKALKLLLEALR 192
|
|
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
4-188 |
2.88e-86 |
|
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: 252.06 E-value: 2.88e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 4 IVIASNNQGKINDFKVIFPDYhVIGISELIPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEPGIY 83
Cdd:cd00515 1 IVFATGNKGKLKEFKEILAPF-GIEVVSLKDIIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 84 SARYAGENkSDEANIEKLLNKLGNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGENGFGYDPIFYVPKLDKT 163
Cdd:cd00515 80 SARFAGEH-DDAENNEKLLELLEGDEDRSAYFVCVIALVDPDGEPLVFEGEVEGKIVTEPRGTGGFGYDPIFIPEGYGKT 158
|
170 180
....*....|....*....|....*
gi 577530842 164 MAQLSKEQKGQISHRRNAINLLQAF 188
Cdd:cd00515 159 FAEMSPEEKNAISHRGKALRKLKEF 183
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
3-190 |
7.06e-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: 7.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 3 EIVIASNNQGKINDFKVIFPDYHVIGISELIPDFdVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEPGI 82
Cdd:TIGR00042 1 KIVFATGNPGKLKEVQSILSDLGDNEIEQLDLGY-PEETGLTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 83 YSARYAGenkSDEANIEKLLNKLGNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGENGFGYDPIFYVPKLDK 162
Cdd:TIGR00042 80 YSARYQG---TDIGNLEKILKLLEGVENRQAYFVCVIGYCDPNGEPLVFEGIVKGKITREPRGTYGFGYDPIFIPPEEGK 156
|
170 180
....*....|....*....|....*...
gi 577530842 163 TMAQLSKEQKGQISHRRNAINLLQAFLE 190
Cdd:TIGR00042 157 TFAELTTEEKNKISHRGKAFKKFKKFLL 184
|
|
| PRK14823 |
PRK14823 |
putative deoxyribonucleoside-triphosphatase; Provisional |
2-189 |
1.22e-58 |
|
putative deoxyribonucleoside-triphosphatase; Provisional
Pssm-ID: 237823 [Multi-domain] Cd Length: 191 Bit Score: 182.19 E-value: 1.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 2 KEIVIASNNQGKINDFKVIFPDY-HVIGISELIPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEP 80
Cdd:PRK14823 1 MKLVFATNNKHKLEEIRSILPEKiELLSLSDIGCHEDIPETADTLEGNALLKAEYVYKKYGYDCFADDTGLEVEALNGAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 81 GIYSARYAGENKSDEANIEKLLNKLGNTTDRRAQFVCVISMSgPDMETKVFKGTVSGEIADGKYGENGFGYDPIFYVPKL 160
Cdd:PRK14823 81 GVYSARYAGGEHNAEANMRKLLEELEGKDNRKAQFRTVIALI-LDGKEHLFEGIIKGEIIKEKRGDSGFGYDPIFVPEGY 159
|
170 180
....*....|....*....|....*....
gi 577530842 161 DKTMAQLSKEQKGQISHRRNAINLLQAFL 189
Cdd:PRK14823 160 DKTFAELGLEIKNQISHRAKAVQKLIDFL 188
|
|
| PRK14826 |
PRK14826 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
4-191 |
1.95e-52 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173287 Cd Length: 222 Bit Score: 167.54 E-value: 1.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 4 IVIASNNQGKINDFK----VIFPDYHVIGISELIPDFDVEETGSTFEENAILKSEA-----AAKALNKTVIADDSGLEVF 74
Cdd:PRK14826 11 IVLATGNRDKVRELRplleHISPLFSVRSLADLGVEVDIEETEETLEGNALLKADAifellSDRFPFLIALADDTGLEVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 75 ALNGEPGIYSARYA----GENKSDEANIEKLLNKLGNTTDRRAQFVCVISMSG--PDMETKVF-----KGTVSGEIADGK 143
Cdd:PRK14826 91 ALGGAPGVYSARFApvpeGEKPTYEDNVRHLLSEMEGKTERSARFRTVIALKGrlPGKNGAFEfeetaEGVVEGSITTEK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 577530842 144 YGENGFGYDPIFYVPKLDKTMAQLSKEQKGQISHR----RNAINLLQAFLEG 191
Cdd:PRK14826 171 KGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRalavQKAVKFLRTILSQ 222
|
|
| PRK14824 |
PRK14824 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
4-189 |
2.15e-50 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 237824 [Multi-domain] Cd Length: 201 Bit Score: 161.47 E-value: 2.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 4 IVIASNNQGKINDFKVIFPDYhviGISELIPD--FDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEPG 81
Cdd:PRK14824 3 ILLATTNEGKVREIKRLLSDL---GIEVLSPDkkIEVEEDGETFLENAYLKARAYAEFYKIPVLADDSGLEVPALEGYPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 82 IYSAR-----YAGENK----SDEANIEKLLNKLGNTTDRRAQFVCVISMSGPDMETKVfKGTVSGEIADGKYGENGFGYD 152
Cdd:PRK14824 80 VYSSRfyqieFGGKEEvvesKDEANIRKLLRLLEGKQNRKARFVAFVVLYFGDWGIWT-EGECRGKIAEEPRGSGGFGYD 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 577530842 153 PIFYVPKLDKTMAQLSKEQKGQISHRRNAINLLQAFL 189
Cdd:PRK14824 159 PVFIPEGYNKTMAELSPEEKNKISHRGKAVRKLVEIL 195
|
|
| PRK02491 |
PRK02491 |
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; ... |
4-188 |
1.52e-48 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed
Pssm-ID: 179431 [Multi-domain] Cd Length: 328 Bit Score: 160.75 E-value: 1.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 4 IVIASNNQGKINDFKVIFPD--YHVIGISELiPDF-DVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEP 80
Cdd:PRK02491 130 ILIATRNEGKTKEFRKLFGKlgYKVENLNDY-PDLpEVAETGMTFEENARLKAETISRLTGKMVLADDSGLKVDALGGLP 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 81 GIYSARYAGENKSDEANIEKLLNKLG---NTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGENGFGYDPIFYV 157
Cdd:PRK02491 209 GVWSARFSGPDATDAENNAKLLHELAmvfDLKDRSAQFHTTLVVAAPNKDSLVVEADWPGYIATEPKGENGFGYDPLFLV 288
|
170 180 190
....*....|....*....|....*....|..
gi 577530842 158 PKLDKTMAQLSKEQKGQISHRRNAI-NLLQAF 188
Cdd:PRK02491 289 GETGRHAAELTAEEKNQLSHRGQAVkKLMEVF 320
|
|
| PRK14825 |
PRK14825 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
1-189 |
8.94e-34 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173286 Cd Length: 199 Bit Score: 118.88 E-value: 8.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 1 MKEIVIASNNQGKINDFKVIFpdyHVIGISELIP-DFDVEETGSTFEENAILKSEAAAKALNKT--VIADDSGLEVFALN 77
Cdd:PRK14825 1 MKTLFFATTNINKINEVKQIL---DIPNIKIEIPqNFDIKETGKTFKENSLLKAKALFEILNNKqpVFSEDSGLCIEALN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 78 GEPGIYSARY----AGENKSDEANIEKLLNKLGNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIA--DGKYGENGFGY 151
Cdd:PRK14825 78 LEPGIYSKRYdqykLGKKLSTNEKNHLIIDLMKNEKNRTAYFICNISYISKDGTILNFEGIIKGTIAlsIDDYKKNGFGY 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 577530842 152 DPIFyVPKLDKTMAQLSKEQKGQISHRRNAINLLQAFL 189
Cdd:PRK14825 158 DPIF-LTKNNKRLSELTLEEKNKISHRGIAFDKFKKFL 194
|
|
| PRK14821 |
PRK14821 |
XTP/dITP diphosphatase; |
3-191 |
2.50e-33 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184834 [Multi-domain] Cd Length: 184 Bit Score: 117.36 E-value: 2.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 3 EIVIASNNQGKINDFKVIFPDYHVIGISELIPDFDVEEtgSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEPGI 82
Cdd:PRK14821 2 KIYFATGNKGKVEEAKIILKPLGIEVEQIKIEYPEIQA--DTLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 83 YSArYAGENksdeANIEKLLNKLGNTTDRRAQFVCVISMSGPDMEtKVFKGTVSGEIADGKYGENGFGYDPIFYVPKLDK 162
Cdd:PRK14821 80 YSA-FVYKT----LGNEGILKLLEGEENRRAYFKSVIGYCDPGGE-KLFTGIVEGKIANEIRGKGGFGYDPIFIPEGEEK 153
|
170 180
....*....|....*....|....*....
gi 577530842 163 TMAQLSKEQKGQISHRRNAINLLQAFLEG 191
Cdd:PRK14821 154 TFAEMTTEEKNKISHRKRAFDEFKEWLKE 182
|
|
| Maf_Ham1 |
cd00985 |
Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum ... |
4-140 |
1.45e-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: 100.65 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577530842 4 IVIASNNQGKINDFKVIFpdyhviGISELIPDFDVEETGS------TFEENAILKSEAAAKALNKT-VIADDSGLEVfal 76
Cdd:cd00985 1 LILASGSPRRLEELKQIG------GIEFEVLPSDIDETGLkgepedTVEELALLKARAVAERLPDApVIADDTGLVV--- 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577530842 77 NGEPGIYSARYAGEnksdeanieklLNKLGNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIA 140
Cdd:cd00985 72 DGRPGGKPARFAEA-----------LEMLRGLSGRTAEFVTAVALVDPDGKIITFEGETEGKIA 124
|
|
| |
