|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00120 |
PRK00120 |
dITP/XTP pyrophosphatase; Reviewed |
3-183 |
1.08e-108 |
|
dITP/XTP pyrophosphatase; Reviewed
Pssm-ID: 234648 [Multi-domain] Cd Length: 196 Bit Score: 309.32 E-value: 1.08e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 3 KTLVLATGNPGKVKELANMLSSLNINVVPQSDFNVSEVAETGTTFVENAIIKARHAAKITGMAAIADDSGLEVDGLNGAP 82
Cdd:PRK00120 1 MKIVLASHNAGKLRELKALLAPFGIEVVSQGELGVPEPEETGTTFVENALIKARHAAKATGLPALADDSGLCVDALGGAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 83 GVYSARFAGPGASDQDNIDKLLVDLGNNPI--RSARFWCVLVLMRHadDPTPLICSASWEGEITLTQNGNGGFGYDPVFF 160
Cdd:PRK00120 81 GVYSARYAGEGASDAANNEKLLEELKGVPDedRRARFVCVLVLVRP--DPTPLVAEGRWEGEILWEPRGENGFGYDPIFF 158
|
170 180
....*....|....*....|...
gi 1887645430 161 VAEKNCTSAELTKEQKNAVSHRG 183
Cdd:PRK00120 159 PPGYGKTFAELTPEEKNAISHRG 181
|
|
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
4-183 |
9.95e-102 |
|
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];
Pssm-ID: 439897 [Multi-domain] Cd Length: 191 Bit Score: 291.58 E-value: 9.95e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 4 TLVLATGNPGKVKELANMLSSLNINVVPQSDFNVSEVAETGTTFVENAIIKARHAAKITGMAAIADDSGLEVDGLNGAPG 83
Cdd:COG0127 1 KLVFATGNAGKLREIRALLAPLGIEVVSLSDLGLPEPEETGDTFEENALIKARAAAKATGLPALADDSGLEVDALGGAPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 84 VYSARFAGPGASDQDNIDKLLVDLGNNPI-RSARFWCVLVLMRHadDPTPLICSASWEGEITLTQNGNGGFGYDPVFFVA 162
Cdd:COG0127 81 VYSARYAGEGADDEANNEKLLKLLEGVDEdRRARFVCVLALADP--DGEPLVFEGEVEGEIAEEPRGEGGFGYDPIFIPD 158
|
170 180
....*....|....*....|.
gi 1887645430 163 EKNCTSAELTKEQKNAVSHRG 183
Cdd:COG0127 159 GYGKTFAELSPEEKNAISHRG 179
|
|
| Ham1p_like |
pfam01725 |
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ... |
5-183 |
3.22e-87 |
|
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: 254.68 E-value: 3.22e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 5 LVLATGNPGKVKELANMLSSLnINVVPQSDF-NVSEVAETGTTFVENAIIKARHAAKiTGMAAIADDSGLEVDGLNGAPG 83
Cdd:pfam01725 1 IVFATGNAGKLRELKAILADG-IEVLSLKDLgELPEIEETGGTFEENALIKARAAAK-TGLPVLADDSGLEVDALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 84 VYSARFAGPGASDQDNIDKLLVDLGNNPI-RSARFWCVLVLMRHadDPTPLICSASWEGEITLTQNGNGGFGYDPVFFVA 162
Cdd:pfam01725 79 VYSARFAGEGGDDEANNAKLLEELEVPDEdRSARFVCVIALADP--GGPELVFEGEVEGEIVEEPRGEGGFGYDPIFIPP 156
|
170 180
....*....|....*....|.
gi 1887645430 163 EKNCTSAELTKEQKNAVSHRG 183
Cdd:pfam01725 157 EGGKTFAELSPEEKNAISHRG 177
|
|
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
5-183 |
1.84e-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: 245.12 E-value: 1.84e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 5 LVLATGNPGKVKELANMLSSLNINVVPQSDfnVSEVAETGTTFVENAIIKARHAAKITGMAAIADDSGLEVDGLNGAPGV 84
Cdd:cd00515 1 IVFATGNKGKLKEFKEILAPFGIEVVSLKD--IIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 85 YSARFAGPGaSDQDNIDKLLVDLGNNPIRSARFWCVLVLMRHadDPTPLICSASWEGEITLTQNGNGGFGYDPVFFVAEK 164
Cdd:cd00515 79 YSARFAGEH-DDAENNEKLLELLEGDEDRSAYFVCVIALVDP--DGEPLVFEGEVEGKIVTEPRGTGGFGYDPIFIPEGY 155
|
170
....*....|....*....
gi 1887645430 165 NCTSAELTKEQKNAVSHRG 183
Cdd:cd00515 156 GKTFAEMSPEEKNAISHRG 174
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
4-183 |
1.85e-71 |
|
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: 214.54 E-value: 1.85e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 4 TLVLATGNPGKVKELANMLSSLNINVVPQSDFNVSEvaETGTTFVENAIIKARHAAKITGMAAIADDSGLEVDGLNGAPG 83
Cdd:TIGR00042 1 KIVFATGNPGKLKEVQSILSDLGDNEIEQLDLGYPE--ETGLTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 84 VYSARFAGpgaSDQDNIDKLLVDLGNNPIRSARFWCVLVLMRHADDptPLICSASWEGEITLTQNGNGGFGYDPVFFVAE 163
Cdd:TIGR00042 79 IYSARYQG---TDIGNLEKILKLLEGVENRQAYFVCVIGYCDPNGE--PLVFEGIVKGKITREPRGTYGFGYDPIFIPPE 153
|
170 180
....*....|....*....|
gi 1887645430 164 KNCTSAELTKEQKNAVSHRG 183
Cdd:TIGR00042 154 EGKTFAELTTEEKNKISHRG 173
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00120 |
PRK00120 |
dITP/XTP pyrophosphatase; Reviewed |
3-183 |
1.08e-108 |
|
dITP/XTP pyrophosphatase; Reviewed
Pssm-ID: 234648 [Multi-domain] Cd Length: 196 Bit Score: 309.32 E-value: 1.08e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 3 KTLVLATGNPGKVKELANMLSSLNINVVPQSDFNVSEVAETGTTFVENAIIKARHAAKITGMAAIADDSGLEVDGLNGAP 82
Cdd:PRK00120 1 MKIVLASHNAGKLRELKALLAPFGIEVVSQGELGVPEPEETGTTFVENALIKARHAAKATGLPALADDSGLCVDALGGAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 83 GVYSARFAGPGASDQDNIDKLLVDLGNNPI--RSARFWCVLVLMRHadDPTPLICSASWEGEITLTQNGNGGFGYDPVFF 160
Cdd:PRK00120 81 GVYSARYAGEGASDAANNEKLLEELKGVPDedRRARFVCVLVLVRP--DPTPLVAEGRWEGEILWEPRGENGFGYDPIFF 158
|
170 180
....*....|....*....|...
gi 1887645430 161 VAEKNCTSAELTKEQKNAVSHRG 183
Cdd:PRK00120 159 PPGYGKTFAELTPEEKNAISHRG 181
|
|
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
4-183 |
9.95e-102 |
|
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];
Pssm-ID: 439897 [Multi-domain] Cd Length: 191 Bit Score: 291.58 E-value: 9.95e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 4 TLVLATGNPGKVKELANMLSSLNINVVPQSDFNVSEVAETGTTFVENAIIKARHAAKITGMAAIADDSGLEVDGLNGAPG 83
Cdd:COG0127 1 KLVFATGNAGKLREIRALLAPLGIEVVSLSDLGLPEPEETGDTFEENALIKARAAAKATGLPALADDSGLEVDALGGAPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 84 VYSARFAGPGASDQDNIDKLLVDLGNNPI-RSARFWCVLVLMRHadDPTPLICSASWEGEITLTQNGNGGFGYDPVFFVA 162
Cdd:COG0127 81 VYSARYAGEGADDEANNEKLLKLLEGVDEdRRARFVCVLALADP--DGEPLVFEGEVEGEIAEEPRGEGGFGYDPIFIPD 158
|
170 180
....*....|....*....|.
gi 1887645430 163 EKNCTSAELTKEQKNAVSHRG 183
Cdd:COG0127 159 GYGKTFAELSPEEKNAISHRG 179
|
|
| Ham1p_like |
pfam01725 |
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ... |
5-183 |
3.22e-87 |
|
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: 254.68 E-value: 3.22e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 5 LVLATGNPGKVKELANMLSSLnINVVPQSDF-NVSEVAETGTTFVENAIIKARHAAKiTGMAAIADDSGLEVDGLNGAPG 83
Cdd:pfam01725 1 IVFATGNAGKLRELKAILADG-IEVLSLKDLgELPEIEETGGTFEENALIKARAAAK-TGLPVLADDSGLEVDALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 84 VYSARFAGPGASDQDNIDKLLVDLGNNPI-RSARFWCVLVLMRHadDPTPLICSASWEGEITLTQNGNGGFGYDPVFFVA 162
Cdd:pfam01725 79 VYSARFAGEGGDDEANNAKLLEELEVPDEdRSARFVCVIALADP--GGPELVFEGEVEGEIVEEPRGEGGFGYDPIFIPP 156
|
170 180
....*....|....*....|.
gi 1887645430 163 EKNCTSAELTKEQKNAVSHRG 183
Cdd:pfam01725 157 EGGKTFAELSPEEKNAISHRG 177
|
|
| PRK14822 |
PRK14822 |
XTP/dITP diphosphatase; |
3-183 |
1.14e-85 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184835 [Multi-domain] Cd Length: 200 Bit Score: 251.35 E-value: 1.14e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 3 KTLVLATGNPGKVKELANMLSSLNINVVPQSDF-NVSEVAETGTTFVENAIIKARHAAKITGMAAIADDSGLEVDGLNGA 81
Cdd:PRK14822 2 KEIVIATKNKGKVREFKEIFEKFDIEVKSLADFpPIPEVEETGTTFEENAILKAEAAAKALNKPVIADDSGLEVDALNGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 82 PGVYSARFAGPGASDQDNIDKLLVDLGNNPI--RSARFWCVLVLMRhADDPTpLICSASWEGEITLTQNGNGGFGYDPVF 159
Cdd:PRK14822 82 PGVYSARYAGEAKDDAANNEKLLKELGGVPFekRTARFHCVIAVAF-PGGET-KTVEGTCEGEILEEPRGENGFGYDPLF 159
|
170 180
....*....|....*....|....
gi 1887645430 160 FVAEKNCTSAELTKEQKNAVSHRG 183
Cdd:PRK14822 160 YVPEKGKTMAELSSEEKNAISHRG 183
|
|
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
5-183 |
1.84e-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: 245.12 E-value: 1.84e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 5 LVLATGNPGKVKELANMLSSLNINVVPQSDfnVSEVAETGTTFVENAIIKARHAAKITGMAAIADDSGLEVDGLNGAPGV 84
Cdd:cd00515 1 IVFATGNKGKLKEFKEILAPFGIEVVSLKD--IIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 85 YSARFAGPGaSDQDNIDKLLVDLGNNPIRSARFWCVLVLMRHadDPTPLICSASWEGEITLTQNGNGGFGYDPVFFVAEK 164
Cdd:cd00515 79 YSARFAGEH-DDAENNEKLLELLEGDEDRSAYFVCVIALVDP--DGEPLVFEGEVEGKIVTEPRGTGGFGYDPIFIPEGY 155
|
170
....*....|....*....
gi 1887645430 165 NCTSAELTKEQKNAVSHRG 183
Cdd:cd00515 156 GKTFAEMSPEEKNAISHRG 174
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
4-183 |
1.85e-71 |
|
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: 214.54 E-value: 1.85e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 4 TLVLATGNPGKVKELANMLSSLNINVVPQSDFNVSEvaETGTTFVENAIIKARHAAKITGMAAIADDSGLEVDGLNGAPG 83
Cdd:TIGR00042 1 KIVFATGNPGKLKEVQSILSDLGDNEIEQLDLGYPE--ETGLTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 84 VYSARFAGpgaSDQDNIDKLLVDLGNNPIRSARFWCVLVLMRHADDptPLICSASWEGEITLTQNGNGGFGYDPVFFVAE 163
Cdd:TIGR00042 79 IYSARYQG---TDIGNLEKILKLLEGVENRQAYFVCVIGYCDPNGE--PLVFEGIVKGKITREPRGTYGFGYDPIFIPPE 153
|
170 180
....*....|....*....|
gi 1887645430 164 KNCTSAELTKEQKNAVSHRG 183
Cdd:TIGR00042 154 EGKTFAELTTEEKNKISHRG 173
|
|
| PRK14826 |
PRK14826 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
2-183 |
9.06e-57 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173287 Cd Length: 222 Bit Score: 178.71 E-value: 9.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 2 TKTLVLATGNPGKVKELANMLSSLN--INVVPQSDFNVS-EVAETGTTFVENAIIKARH-----AAKITGMAAIADDSGL 73
Cdd:PRK14826 8 TITIVLATGNRDKVRELRPLLEHISplFSVRSLADLGVEvDIEETEETLEGNALLKADAifellSDRFPFLIALADDTGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 74 EVDGLNGAPGVYSARFA----GPGASDQDNIDKLLVDLGNNPIRSARFWCVLVL---MRHADDPT--PLICSASWEGEIT 144
Cdd:PRK14826 88 EVDALGGAPGVYSARFApvpeGEKPTYEDNVRHLLSEMEGKTERSARFRTVIALkgrLPGKNGAFefEETAEGVVEGSIT 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 1887645430 145 LTQNGNGGFGYDPVFFVAEKNCTSAELTKEQKNAVSHRG 183
Cdd:PRK14826 168 TEKKGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRA 206
|
|
| PRK02491 |
PRK02491 |
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; ... |
4-183 |
4.66e-56 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed
Pssm-ID: 179431 [Multi-domain] Cd Length: 328 Bit Score: 180.01 E-value: 4.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 4 TLVLATGNPGKVKELANMLSSLNINVVPQSDF-NVSEVAETGTTFVENAIIKARHAAKITGMAAIADDSGLEVDGLNGAP 82
Cdd:PRK02491 129 TILIATRNEGKTKEFRKLFGKLGYKVENLNDYpDLPEVAETGMTFEENARLKAETISRLTGKMVLADDSGLKVDALGGLP 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 83 GVYSARFAGPGASDQDNIDKLLVDLG---NNPIRSARFWCVLVLMrhADDPTPLICSASWEGEITLTQNGNGGFGYDPVF 159
Cdd:PRK02491 209 GVWSARFSGPDATDAENNAKLLHELAmvfDLKDRSAQFHTTLVVA--APNKDSLVVEADWPGYIATEPKGENGFGYDPLF 286
|
170 180
....*....|....*....|....
gi 1887645430 160 FVAEKNCTSAELTKEQKNAVSHRG 183
Cdd:PRK02491 287 LVGETGRHAAELTAEEKNQLSHRG 310
|
|
| PRK14823 |
PRK14823 |
putative deoxyribonucleoside-triphosphatase; Provisional |
5-183 |
1.48e-49 |
|
putative deoxyribonucleoside-triphosphatase; Provisional
Pssm-ID: 237823 [Multi-domain] Cd Length: 191 Bit Score: 159.08 E-value: 1.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 5 LVLATGNPGKVKELANMLSSlNINVVPQSDFNVSE-VAETGTTFVENAIIKARHAAKITGMAAIADDSGLEVDGLNGAPG 83
Cdd:PRK14823 3 LVFATNNKHKLEEIRSILPE-KIELLSLSDIGCHEdIPETADTLEGNALLKAEYVYKKYGYDCFADDTGLEVEALNGAPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 84 VYSARFAGPGASDQDNIDKLLVDLGNNPIRSARFWCVLVLMrhaDDPTPLICSASWEGEITLTQNGNGGFGYDPVFFVAE 163
Cdd:PRK14823 82 VYSARYAGGEHNAEANMRKLLEELEGKDNRKAQFRTVIALI---LDGKEHLFEGIIKGEIIKEKRGDSGFGYDPIFVPEG 158
|
170 180
....*....|....*....|
gi 1887645430 164 KNCTSAELTKEQKNAVSHRG 183
Cdd:PRK14823 159 YDKTFAELGLEIKNQISHRA 178
|
|
| PRK14824 |
PRK14824 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
5-183 |
3.25e-47 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 237824 [Multi-domain] Cd Length: 201 Bit Score: 153.76 E-value: 3.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 5 LVLATGNPGKVKELANMLSSLNINVVpqSDFNVSEVAETGTTFVENAIIKARHAAKITGMAAIADDSGLEVDGLNGAPGV 84
Cdd:PRK14824 3 ILLATTNEGKVREIKRLLSDLGIEVL--SPDKKIEVEEDGETFLENAYLKARAYAEFYKIPVLADDSGLEVPALEGYPGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 85 YSARFAG---------PGASDQDNIDKLLVDLGNNPIRSARFWCVLVLmrhADDPTPLICSASWEGEITLTQNGNGGFGY 155
Cdd:PRK14824 81 YSSRFYQiefggkeevVESKDEANIRKLLRLLEGKQNRKARFVAFVVL---YFGDWGIWTEGECRGKIAEEPRGSGGFGY 157
|
170 180
....*....|....*....|....*...
gi 1887645430 156 DPVFFVAEKNCTSAELTKEQKNAVSHRG 183
Cdd:PRK14824 158 DPVFIPEGYNKTMAELSPEEKNKISHRG 185
|
|
| PRK14821 |
PRK14821 |
XTP/dITP diphosphatase; |
5-183 |
2.19e-29 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184834 [Multi-domain] Cd Length: 184 Bit Score: 107.35 E-value: 2.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 5 LVLATGNPGKVKELANMLSSLNINVVP--------QSDfNVSEVAETGttfvenaiikARHAAKITGMAAIADDSGLEVD 76
Cdd:PRK14821 3 IYFATGNKGKVEEAKIILKPLGIEVEQikieypeiQAD-TLEEVAAFG----------AKWVYNKLNRPVIVEDSGLFIE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 77 GLNGAPGVYSA----RFAGPGasdqdnIDKLLVDLGNnpiRSARFWCVLVLmrHADDPTPLIcSASWEGEITLTQNGNGG 152
Cdd:PRK14821 72 ALNGFPGPYSAfvykTLGNEG------ILKLLEGEEN---RRAYFKSVIGY--CDPGGEKLF-TGIVEGKIANEIRGKGG 139
|
170 180 190
....*....|....*....|....*....|.
gi 1887645430 153 FGYDPVFFVAEKNCTSAELTKEQKNAVSHRG 183
Cdd:PRK14821 140 FGYDPIFIPEGEEKTFAEMTTEEKNKISHRK 170
|
|
| Maf_Ham1 |
cd00985 |
Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum ... |
5-143 |
1.72e-28 |
|
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: 103.35 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 5 LVLATGNPGKVKELANMLSslnINVVPQSdfnvSEVAETG------TTFVENAIIKARHAAKITGMA-AIADDSGLEVDg 77
Cdd:cd00985 1 LILASGSPRRLEELKQIGG---IEFEVLP----SDIDETGlkgepeDTVEELALLKARAVAERLPDApVIADDTGLVVD- 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1887645430 78 lnGAPGVYSARFAGPgasdqdniDKLLVDLGNnpiRSARFWCVLVLMRHadDPTPLICSASWEGEI 143
Cdd:cd00985 73 --GRPGGKPARFAEA--------LEMLRGLSG---RTAEFVTAVALVDP--DGKIITFEGETEGKI 123
|
|
| PRK14825 |
PRK14825 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
3-183 |
4.65e-27 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173286 Cd Length: 199 Bit Score: 101.94 E-value: 4.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 3 KTLVLATGNPGKVKELANMLSSLNINVVPQSDFNVSevaETGTTFVENAIIKARHAAKITG--MAAIADDSGLEVDGLNG 80
Cdd:PRK14825 2 KTLFFATTNINKINEVKQILDIPNIKIEIPQNFDIK---ETGKTFKENSLLKAKALFEILNnkQPVFSEDSGLCIEALNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887645430 81 APGVYSARFagpgasDQDNIDK---------LLVDL-GNNPIRSARFWCVLVLMrhADDPTPLICSASWEGEITLTQN-- 148
Cdd:PRK14825 79 EPGIYSKRY------DQYKLGKklstneknhLIIDLmKNEKNRTAYFICNISYI--SKDGTILNFEGIIKGTIALSIDdy 150
|
170 180 190
....*....|....*....|....*....|....*
gi 1887645430 149 GNGGFGYDPVFFVAeKNCTSAELTKEQKNAVSHRG 183
Cdd:PRK14825 151 KKNGFGYDPIFLTK-NNKRLSELTLEEKNKISHRG 184
|
|
| |
