|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14822 |
PRK14822 |
XTP/dITP diphosphatase; |
1-195 |
7.45e-118 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184835 [Multi-domain] Cd Length: 200 Bit Score: 332.24 E-value: 7.45e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 1 MKEIVIASNNQGKINDFKVIF--PDYHVIGISELIPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNG 78
Cdd:PRK14822 1 MKEIVIATKNKGKVREFKEIFekFDIEVKSLADFPPIPEVEETGTTFEENAILKAEAAAKALNKPVIADDSGLEVDALNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 79 EPGIYSARYAGENKSDEANIEKLLNKLGNT--TDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFY 156
Cdd:PRK14822 81 APGVYSARYAGEAKDDAANNEKLLKELGGVpfEKRTARFHCVIAVAFPGGETKTVEGTCEGEILEEPRGENGFGYDPLFY 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 446581969 157 VPKLDKTMAQLSKEEKGQISHRRNAINLLEAYLAGDQHV 195
Cdd:PRK14822 161 VPEKGKTMAELSSEEKNAISHRGKALKKLEAELPEWLKV 199
|
|
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
3-191 |
1.72e-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: 1.72e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 3 EIVIASNNQGKINDFKVIFPDYH--VIGISELiPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEP 80
Cdd:COG0127 1 KLVFATGNAGKLREIRALLAPLGieVVSLSDL-GLPEPEETGDTFEENALIKARAAAKATGLPALADDSGLEVDALGGAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 81 GIYSARYAGENKSDEANIEKLLNKLGNT-TDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFYVPK 159
Cdd:COG0127 80 GVYSARYAGEGADDEANNEKLLKLLEGVdEDRRARFVCVLALADPDGEPLVFEGEVEGEIAEEPRGEGGFGYDPIFIPDG 159
|
170 180 190
....*....|....*....|....*....|..
gi 446581969 160 LDKTMAQLSKEEKGQISHRRNAINLLEAYLAG 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 |
5.99e-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: 261.23 E-value: 5.99e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 4 IVIASNNQGKINDFKVIF-PDYHVIGISELIPDFDVEETGSTFEENAILKSEAAAKaLNKTVIADDSGLEVFALNGEPGI 82
Cdd:pfam01725 1 IVFATGNAGKLRELKAILaDGIEVLSLKDLGELPEIEETGGTFEENALIKARAAAK-TGLPVLADDSGLEVDALNGFPGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 83 YSARYAGENKSDEANIEKLLNKL-GNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFYVPKLD 161
Cdd:pfam01725 80 YSARFAGEGGDDEANNAKLLEELeVPDEDRSARFVCVIALADPGGPELVFEGEVEGEIVEEPRGEGGFGYDPIFIPPEGG 159
|
170 180
....*....|....*....|....*..
gi 446581969 162 KTMAQLSKEEKGQISHRRNAINLLEAY 188
Cdd:pfam01725 160 KTFAELSPEEKNAISHRGKALRKLKEF 186
|
|
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
4-188 |
5.52e-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: 253.60 E-value: 5.52e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 4 IVIASNNQGKINDFKVIFPDYhVIGISELIPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEPGIY 83
Cdd:cd00515 1 IVFATGNKGKLKEFKEILAPF-GIEVVSLKDIIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 84 SARYAGENkSDEANIEKLLNKLGNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFYVPKLDKT 163
Cdd:cd00515 80 SARFAGEH-DDAENNEKLLELLEGDEDRSAYFVCVIALVDPDGEPLVFEGEVEGKIVTEPRGTGGFGYDPIFIPEGYGKT 158
|
170 180
....*....|....*....|....*
gi 446581969 164 MAQLSKEEKGQISHRRNAINLLEAY 188
Cdd:cd00515 159 FAEMSPEEKNAISHRGKALRKLKEF 183
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
3-189 |
3.58e-68 |
|
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: 206.06 E-value: 3.58e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 3 EIVIASNNQGKINDFKVIFPDYHVIGISELIPDFdVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEPGI 82
Cdd:TIGR00042 1 KIVFATGNPGKLKEVQSILSDLGDNEIEQLDLGY-PEETGLTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 83 YSARYAGenkSDEANIEKLLNKLGNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFYVPKLDK 162
Cdd:TIGR00042 80 YSARYQG---TDIGNLEKILKLLEGVENRQAYFVCVIGYCDPNGEPLVFEGIVKGKITREPRGTYGFGYDPIFIPPEEGK 156
|
170 180
....*....|....*....|....*..
gi 446581969 163 TMAQLSKEEKGQISHRRNAINLLEAYL 189
Cdd:TIGR00042 157 TFAELTTEEKNKISHRGKAFKKFKKFL 183
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14822 |
PRK14822 |
XTP/dITP diphosphatase; |
1-195 |
7.45e-118 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184835 [Multi-domain] Cd Length: 200 Bit Score: 332.24 E-value: 7.45e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 1 MKEIVIASNNQGKINDFKVIF--PDYHVIGISELIPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNG 78
Cdd:PRK14822 1 MKEIVIATKNKGKVREFKEIFekFDIEVKSLADFPPIPEVEETGTTFEENAILKAEAAAKALNKPVIADDSGLEVDALNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 79 EPGIYSARYAGENKSDEANIEKLLNKLGNT--TDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFY 156
Cdd:PRK14822 81 APGVYSARYAGEAKDDAANNEKLLKELGGVpfEKRTARFHCVIAVAFPGGETKTVEGTCEGEILEEPRGENGFGYDPLFY 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 446581969 157 VPKLDKTMAQLSKEEKGQISHRRNAINLLEAYLAGDQHV 195
Cdd:PRK14822 161 VPEKGKTMAELSSEEKNAISHRGKALKKLEAELPEWLKV 199
|
|
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
3-191 |
1.72e-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: 1.72e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 3 EIVIASNNQGKINDFKVIFPDYH--VIGISELiPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEP 80
Cdd:COG0127 1 KLVFATGNAGKLREIRALLAPLGieVVSLSDL-GLPEPEETGDTFEENALIKARAAAKATGLPALADDSGLEVDALGGAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 81 GIYSARYAGENKSDEANIEKLLNKLGNT-TDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFYVPK 159
Cdd:COG0127 80 GVYSARYAGEGADDEANNEKLLKLLEGVdEDRRARFVCVLALADPDGEPLVFEGEVEGEIAEEPRGEGGFGYDPIFIPDG 159
|
170 180 190
....*....|....*....|....*....|..
gi 446581969 160 LDKTMAQLSKEEKGQISHRRNAINLLEAYLAG 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 |
5.99e-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: 261.23 E-value: 5.99e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 4 IVIASNNQGKINDFKVIF-PDYHVIGISELIPDFDVEETGSTFEENAILKSEAAAKaLNKTVIADDSGLEVFALNGEPGI 82
Cdd:pfam01725 1 IVFATGNAGKLRELKAILaDGIEVLSLKDLGELPEIEETGGTFEENALIKARAAAK-TGLPVLADDSGLEVDALNGFPGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 83 YSARYAGENKSDEANIEKLLNKL-GNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFYVPKLD 161
Cdd:pfam01725 80 YSARFAGEGGDDEANNAKLLEELeVPDEDRSARFVCVIALADPGGPELVFEGEVEGEIVEEPRGEGGFGYDPIFIPPEGG 159
|
170 180
....*....|....*....|....*..
gi 446581969 162 KTMAQLSKEEKGQISHRRNAINLLEAY 188
Cdd:pfam01725 160 KTFAELSPEEKNAISHRGKALRKLKEF 186
|
|
| PRK00120 |
PRK00120 |
dITP/XTP pyrophosphatase; Reviewed |
2-189 |
1.63e-88 |
|
dITP/XTP pyrophosphatase; Reviewed
Pssm-ID: 234648 [Multi-domain] Cd Length: 196 Bit Score: 258.09 E-value: 1.63e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 2 KEIVIASNNQGKINDFKVIFPDYH--VIGISELiPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGE 79
Cdd:PRK00120 1 MKIVLASHNAGKLRELKALLAPFGieVVSQGEL-GVPEPEETGTTFVENALIKARHAAKATGLPALADDSGLCVDALGGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 80 PGIYSARYAGENKSDEANIEKLLNKLGNT--TDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFYV 157
Cdd:PRK00120 80 PGVYSARYAGEGASDAANNEKLLEELKGVpdEDRRARFVCVLVLVRPDPTPLVAEGRWEGEILWEPRGENGFGYDPIFFP 159
|
170 180 190
....*....|....*....|....*....|..
gi 446581969 158 PKLDKTMAQLSKEEKGQISHRRNAINLLEAYL 189
Cdd:PRK00120 160 PGYGKTFAELTPEEKNAISHRGKALKLLLEAL 191
|
|
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
4-188 |
5.52e-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: 253.60 E-value: 5.52e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 4 IVIASNNQGKINDFKVIFPDYhVIGISELIPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEPGIY 83
Cdd:cd00515 1 IVFATGNKGKLKEFKEILAPF-GIEVVSLKDIIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 84 SARYAGENkSDEANIEKLLNKLGNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFYVPKLDKT 163
Cdd:cd00515 80 SARFAGEH-DDAENNEKLLELLEGDEDRSAYFVCVIALVDPDGEPLVFEGEVEGKIVTEPRGTGGFGYDPIFIPEGYGKT 158
|
170 180
....*....|....*....|....*
gi 446581969 164 MAQLSKEEKGQISHRRNAINLLEAY 188
Cdd:cd00515 159 FAEMSPEEKNAISHRGKALRKLKEF 183
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
3-189 |
3.58e-68 |
|
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: 206.06 E-value: 3.58e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 3 EIVIASNNQGKINDFKVIFPDYHVIGISELIPDFdVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEPGI 82
Cdd:TIGR00042 1 KIVFATGNPGKLKEVQSILSDLGDNEIEQLDLGY-PEETGLTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 83 YSARYAGenkSDEANIEKLLNKLGNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFYVPKLDK 162
Cdd:TIGR00042 80 YSARYQG---TDIGNLEKILKLLEGVENRQAYFVCVIGYCDPNGEPLVFEGIVKGKITREPRGTYGFGYDPIFIPPEEGK 156
|
170 180
....*....|....*....|....*..
gi 446581969 163 TMAQLSKEEKGQISHRRNAINLLEAYL 189
Cdd:TIGR00042 157 TFAELTTEEKNKISHRGKAFKKFKKFL 183
|
|
| PRK14823 |
PRK14823 |
putative deoxyribonucleoside-triphosphatase; Provisional |
2-189 |
8.74e-60 |
|
putative deoxyribonucleoside-triphosphatase; Provisional
Pssm-ID: 237823 [Multi-domain] Cd Length: 191 Bit Score: 184.88 E-value: 8.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 2 KEIVIASNNQGKINDFKVIFPDY-HVIGISELIPDFDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEP 80
Cdd:PRK14823 1 MKLVFATNNKHKLEEIRSILPEKiELLSLSDIGCHEDIPETADTLEGNALLKAEYVYKKYGYDCFADDTGLEVEALNGAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 81 GIYSARYAGENKSDEANIEKLLNKLGNTTDRRAQFVCVISMSgPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFYVPKL 160
Cdd:PRK14823 81 GVYSARYAGGEHNAEANMRKLLEELEGKDNRKAQFRTVIALI-LDGKEHLFEGIIKGEIIKEKRGDSGFGYDPIFVPEGY 159
|
170 180
....*....|....*....|....*....
gi 446581969 161 DKTMAQLSKEEKGQISHRRNAINLLEAYL 189
Cdd:PRK14823 160 DKTFAELGLEIKNQISHRAKAVQKLIDFL 188
|
|
| PRK14826 |
PRK14826 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
4-191 |
7.83e-54 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173287 Cd Length: 222 Bit Score: 171.00 E-value: 7.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 4 IVIASNNQGKINDFK----VIFPDYHVIGISELIPDFDVEETGSTFEENAILKSEA-----AAKALNKTVIADDSGLEVF 74
Cdd:PRK14826 11 IVLATGNRDKVRELRplleHISPLFSVRSLADLGVEVDIEETEETLEGNALLKADAifellSDRFPFLIALADDTGLEVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 75 ALNGEPGIYSARYA----GENKSDEANIEKLLNKLGNTTDRRAQFVCVISMSG--PDMETKVF-----KGTVSGEIADGK 143
Cdd:PRK14826 91 ALGGAPGVYSARFApvpeGEKPTYEDNVRHLLSEMEGKTERSARFRTVIALKGrlPGKNGAFEfeetaEGVVEGSITTEK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446581969 144 YGDNGFGYDPIFYVPKLDKTMAQLSKEEKGQISHR----RNAINLLEAYLAG 191
Cdd:PRK14826 171 KGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRalavQKAVKFLRTILSQ 222
|
|
| PRK14824 |
PRK14824 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
4-185 |
1.76e-51 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 237824 [Multi-domain] Cd Length: 201 Bit Score: 164.16 E-value: 1.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 4 IVIASNNQGKINDFKVIFPDYhviGISELIPD--FDVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEPG 81
Cdd:PRK14824 3 ILLATTNEGKVREIKRLLSDL---GIEVLSPDkkIEVEEDGETFLENAYLKARAYAEFYKIPVLADDSGLEVPALEGYPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 82 IYSAR-----YAGENK----SDEANIEKLLNKLGNTTDRRAQFVCVISMSGPDMETKVfKGTVSGEIADGKYGDNGFGYD 152
Cdd:PRK14824 80 VYSSRfyqieFGGKEEvvesKDEANIRKLLRLLEGKQNRKARFVAFVVLYFGDWGIWT-EGECRGKIAEEPRGSGGFGYD 158
|
170 180 190
....*....|....*....|....*....|...
gi 446581969 153 PIFYVPKLDKTMAQLSKEEKGQISHRRNAINLL 185
Cdd:PRK14824 159 PVFIPEGYNKTMAELSPEEKNKISHRGKAVRKL 191
|
|
| PRK02491 |
PRK02491 |
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; ... |
4-188 |
4.67e-49 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed
Pssm-ID: 179431 [Multi-domain] Cd Length: 328 Bit Score: 161.90 E-value: 4.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 4 IVIASNNQGKINDFKVIFPD--YHVIGISELiPDF-DVEETGSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEP 80
Cdd:PRK02491 130 ILIATRNEGKTKEFRKLFGKlgYKVENLNDY-PDLpEVAETGMTFEENARLKAETISRLTGKMVLADDSGLKVDALGGLP 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 81 GIYSARYAGENKSDEANIEKLLNKLG---NTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIADGKYGDNGFGYDPIFYV 157
Cdd:PRK02491 209 GVWSARFSGPDATDAENNAKLLHELAmvfDLKDRSAQFHTTLVVAAPNKDSLVVEADWPGYIATEPKGENGFGYDPLFLV 288
|
170 180 190
....*....|....*....|....*....|..
gi 446581969 158 PKLDKTMAQLSKEEKGQISHRRNAI-NLLEAY 188
Cdd:PRK02491 289 GETGRHAAELTAEEKNQLSHRGQAVkKLMEVF 320
|
|
| PRK14825 |
PRK14825 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
1-189 |
2.09e-34 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173286 Cd Length: 199 Bit Score: 120.43 E-value: 2.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 1 MKEIVIASNNQGKINDFKVIFpdyHVIGISELIP-DFDVEETGSTFEENAILKSEAAAKALNKT--VIADDSGLEVFALN 77
Cdd:PRK14825 1 MKTLFFATTNINKINEVKQIL---DIPNIKIEIPqNFDIKETGKTFKENSLLKAKALFEILNNKqpVFSEDSGLCIEALN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 78 GEPGIYSARY----AGENKSDEANIEKLLNKLGNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIA--DGKYGDNGFGY 151
Cdd:PRK14825 78 LEPGIYSKRYdqykLGKKLSTNEKNHLIIDLMKNEKNRTAYFICNISYISKDGTILNFEGIIKGTIAlsIDDYKKNGFGY 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 446581969 152 DPIFyVPKLDKTMAQLSKEEKGQISHRRNAINLLEAYL 189
Cdd:PRK14825 158 DPIF-LTKNNKRLSELTLEEKNKISHRGIAFDKFKKFL 194
|
|
| PRK14821 |
PRK14821 |
XTP/dITP diphosphatase; |
3-189 |
3.18e-34 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184834 [Multi-domain] Cd Length: 184 Bit Score: 119.67 E-value: 3.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 3 EIVIASNNQGKINDFKVIFPDYHVIGISELIPDFDVEEtgSTFEENAILKSEAAAKALNKTVIADDSGLEVFALNGEPGI 82
Cdd:PRK14821 2 KIYFATGNKGKVEEAKIILKPLGIEVEQIKIEYPEIQA--DTLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 83 YSArYAGENksdeANIEKLLNKLGNTTDRRAQFVCVISMSGPDMEtKVFKGTVSGEIADGKYGDNGFGYDPIFYVPKLDK 162
Cdd:PRK14821 80 YSA-FVYKT----LGNEGILKLLEGEENRRAYFKSVIGYCDPGGE-KLFTGIVEGKIANEIRGKGGFGYDPIFIPEGEEK 153
|
170 180
....*....|....*....|....*..
gi 446581969 163 TMAQLSKEEKGQISHRRNAINLLEAYL 189
Cdd:PRK14821 154 TFAEMTTEEKNKISHRKRAFDEFKEWL 180
|
|
| Maf_Ham1 |
cd00985 |
Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum ... |
4-140 |
1.55e-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: 1.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446581969 4 IVIASNNQGKINDFKVIFpdyhviGISELIPDFDVEETGS------TFEENAILKSEAAAKALNKT-VIADDSGLEVfal 76
Cdd:cd00985 1 LILASGSPRRLEELKQIG------GIEFEVLPSDIDETGLkgepedTVEELALLKARAVAERLPDApVIADDTGLVV--- 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446581969 77 NGEPGIYSARYAGEnksdeanieklLNKLGNTTDRRAQFVCVISMSGPDMETKVFKGTVSGEIA 140
Cdd:cd00985 72 DGRPGGKPARFAEA-----------LEMLRGLSGRTAEFVTAVALVDPDGKIITFEGETEGKIA 124
|
|
|