|
Name |
Accession |
Description |
Interval |
E-value |
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
10-188 |
4.92e-81 |
|
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: 238.57 E-value: 4.92e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 10 IVFVTGNAKKLEEVIQILGDnFPCTLEAQK--IDLPEYQGEPDEISIQKCREAARQVQGPVLVEDTCLCFNALGGLPGPY 87
Cdd:cd00515 1 IVFATGNKGKLKEFKEILAP-FGIEVVSLKdiIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 88 IKWFLQ----KLKPEGLHQLLAGFEDKSAYALCTFALStgDPSQPVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQ 162
Cdd:cd00515 80 SARFAGehddAENNEKLLELLEGDEDRSAYFVCVIALV--DPDGEPLVFEGEVEGKIVTePRGTGGFGYDPIFIPEGYGK 157
|
170 180
....*....|....*....|....*.
gi 1039759159 163 TYAEMPKSEKNTISHRFRALHKLQEY 188
Cdd:cd00515 158 TFAEMSPEEKNAISHRGKALRKLKEF 183
|
|
| Ham1p_like |
pfam01725 |
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ... |
10-188 |
2.96e-75 |
|
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: 224.25 E-value: 2.96e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 10 IVFVTGNAKKLEEVIQILGDNFPCTLEAQK---IDLPEYQGEPDEISIQKCREAARQvQGPVLVEDTCLCFNALGGLPGP 86
Cdd:pfam01725 1 IVFATGNAGKLRELKAILADGIEVLSLKDLgelPEIEETGGTFEENALIKARAAAKT-GLPVLADDSGLEVDALNGFPGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 87 YIKWFLQKLKP--EGLHQLLAGF----EDKSAYALCTFALStgDPSQPVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDG 159
Cdd:pfam01725 80 YSARFAGEGGDdeANNAKLLEELevpdEDRSARFVCVIALA--DPGGPELVFEGEVEGEIVEePRGEGGFGYDPIFIPPE 157
|
170 180
....*....|....*....|....*....
gi 1039759159 160 YEQTYAEMPKSEKNTISHRFRALHKLQEY 188
Cdd:pfam01725 158 GGKTFAELSPEEKNAISHRGKALRKLKEF 186
|
|
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
9-189 |
3.03e-61 |
|
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];
Pssm-ID: 439897 [Multi-domain] Cd Length: 191 Bit Score: 188.73 E-value: 3.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 9 KIVFVTGNAKKLEEVIQILGDnFPCTLEAQK-IDLPE--YQGE-PDEISIQKCREAARQVQGPVLVEDTCLCFNALGGLP 84
Cdd:COG0127 1 KLVFATGNAGKLREIRALLAP-LGIEVVSLSdLGLPEpeETGDtFEENALIKARAAAKATGLPALADDSGLEVDALGGAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 85 GPYIKWFL-----QKLKPEGLHQLLAGF-EDKSAYALCTFALSTGDPSqpVLLFRGQTSGQIVM-PRGSRDFGWDPCFQP 157
Cdd:COG0127 80 GVYSARYAgegadDEANNEKLLKLLEGVdEDRRARFVCVLALADPDGE--PLVFEGEVEGEIAEePRGEGGFGYDPIFIP 157
|
170 180 190
....*....|....*....|....*....|..
gi 1039759159 158 DGYEQTYAEMPKSEKNTISHRFRALHKLQEYF 189
Cdd:COG0127 158 DGYGKTFAELSPEEKNAISHRGRALRKLAEWL 189
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
9-188 |
4.96e-50 |
|
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: 160.22 E-value: 4.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 9 KIVFVTGNAKKLEEVIQILGDNFPCTLEAQKIDLPEYQGEP-DEISIQKCREAARQVQGPVLVEDTCLCFNALGGLPGPY 87
Cdd:TIGR00042 1 KIVFATGNPGKLKEVQSILSDLGDNEIEQLDLGYPEETGLTfEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 88 IKWFLQKLK--PEGLHQLLAGFEDKSAYALCTFALStgDPSQPVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQTY 164
Cdd:TIGR00042 81 SARYQGTDIgnLEKILKLLEGVENRQAYFVCVIGYC--DPNGEPLVFEGIVKGKITRePRGTYGFGYDPIFIPPEEGKTF 158
|
170 180
....*....|....*....|....
gi 1039759159 165 AEMPKSEKNTISHRFRALHKLQEY 188
Cdd:TIGR00042 159 AELTTEEKNKISHRGKAFKKFKKF 182
|
|
| PRK14821 |
PRK14821 |
XTP/dITP diphosphatase; |
9-190 |
4.83e-43 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184834 [Multi-domain] Cd Length: 184 Bit Score: 142.40 E-value: 4.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 9 KIVFVTGNAKKLEEVIQILGDnFPCTLEAQKIDLPEYQ-GEPDEISIQKCREAARQVQGPVLVEDTCLCFNALGGLPGPY 87
Cdd:PRK14821 2 KIYFATGNKGKVEEAKIILKP-LGIEVEQIKIEYPEIQaDTLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 88 IKWFLQKLKPEGLHQLLAGFEDKSAY-----ALCtfalstgDPSQpVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYE 161
Cdd:PRK14821 81 SAFVYKTLGNEGILKLLEGEENRRAYfksviGYC-------DPGG-EKLFTGIVEGKIANeIRGKGGFGYDPIFIPEGEE 152
|
170 180
....*....|....*....|....*....
gi 1039759159 162 QTYAEMPKSEKNTISHRFRALHKLQEYFS 190
Cdd:PRK14821 153 KTFAEMTTEEKNKISHRKRAFDEFKEWLK 181
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
10-188 |
4.92e-81 |
|
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: 238.57 E-value: 4.92e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 10 IVFVTGNAKKLEEVIQILGDnFPCTLEAQK--IDLPEYQGEPDEISIQKCREAARQVQGPVLVEDTCLCFNALGGLPGPY 87
Cdd:cd00515 1 IVFATGNKGKLKEFKEILAP-FGIEVVSLKdiIDIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGVY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 88 IKWFLQ----KLKPEGLHQLLAGFEDKSAYALCTFALStgDPSQPVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQ 162
Cdd:cd00515 80 SARFAGehddAENNEKLLELLEGDEDRSAYFVCVIALV--DPDGEPLVFEGEVEGKIVTePRGTGGFGYDPIFIPEGYGK 157
|
170 180
....*....|....*....|....*.
gi 1039759159 163 TYAEMPKSEKNTISHRFRALHKLQEY 188
Cdd:cd00515 158 TFAEMSPEEKNAISHRGKALRKLKEF 183
|
|
| Ham1p_like |
pfam01725 |
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ... |
10-188 |
2.96e-75 |
|
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: 224.25 E-value: 2.96e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 10 IVFVTGNAKKLEEVIQILGDNFPCTLEAQK---IDLPEYQGEPDEISIQKCREAARQvQGPVLVEDTCLCFNALGGLPGP 86
Cdd:pfam01725 1 IVFATGNAGKLRELKAILADGIEVLSLKDLgelPEIEETGGTFEENALIKARAAAKT-GLPVLADDSGLEVDALNGFPGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 87 YIKWFLQKLKP--EGLHQLLAGF----EDKSAYALCTFALStgDPSQPVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDG 159
Cdd:pfam01725 80 YSARFAGEGGDdeANNAKLLEELevpdEDRSARFVCVIALA--DPGGPELVFEGEVEGEIVEePRGEGGFGYDPIFIPPE 157
|
170 180
....*....|....*....|....*....
gi 1039759159 160 YEQTYAEMPKSEKNTISHRFRALHKLQEY 188
Cdd:pfam01725 158 GGKTFAELSPEEKNAISHRGKALRKLKEF 186
|
|
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
9-189 |
3.03e-61 |
|
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];
Pssm-ID: 439897 [Multi-domain] Cd Length: 191 Bit Score: 188.73 E-value: 3.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 9 KIVFVTGNAKKLEEVIQILGDnFPCTLEAQK-IDLPE--YQGE-PDEISIQKCREAARQVQGPVLVEDTCLCFNALGGLP 84
Cdd:COG0127 1 KLVFATGNAGKLREIRALLAP-LGIEVVSLSdLGLPEpeETGDtFEENALIKARAAAKATGLPALADDSGLEVDALGGAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 85 GPYIKWFL-----QKLKPEGLHQLLAGF-EDKSAYALCTFALSTGDPSqpVLLFRGQTSGQIVM-PRGSRDFGWDPCFQP 157
Cdd:COG0127 80 GVYSARYAgegadDEANNEKLLKLLEGVdEDRRARFVCVLALADPDGE--PLVFEGEVEGEIAEePRGEGGFGYDPIFIP 157
|
170 180 190
....*....|....*....|....*....|..
gi 1039759159 158 DGYEQTYAEMPKSEKNTISHRFRALHKLQEYF 189
Cdd:COG0127 158 DGYGKTFAELSPEEKNAISHRGRALRKLAEWL 189
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
9-188 |
4.96e-50 |
|
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: 160.22 E-value: 4.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 9 KIVFVTGNAKKLEEVIQILGDNFPCTLEAQKIDLPEYQGEP-DEISIQKCREAARQVQGPVLVEDTCLCFNALGGLPGPY 87
Cdd:TIGR00042 1 KIVFATGNPGKLKEVQSILSDLGDNEIEQLDLGYPEETGLTfEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPGIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 88 IKWFLQKLK--PEGLHQLLAGFEDKSAYALCTFALStgDPSQPVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYEQTY 164
Cdd:TIGR00042 81 SARYQGTDIgnLEKILKLLEGVENRQAYFVCVIGYC--DPNGEPLVFEGIVKGKITRePRGTYGFGYDPIFIPPEEGKTF 158
|
170 180
....*....|....*....|....
gi 1039759159 165 AEMPKSEKNTISHRFRALHKLQEY 188
Cdd:TIGR00042 159 AELTTEEKNKISHRGKAFKKFKKF 182
|
|
| PRK14821 |
PRK14821 |
XTP/dITP diphosphatase; |
9-190 |
4.83e-43 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184834 [Multi-domain] Cd Length: 184 Bit Score: 142.40 E-value: 4.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 9 KIVFVTGNAKKLEEVIQILGDnFPCTLEAQKIDLPEYQ-GEPDEISIQKCREAARQVQGPVLVEDTCLCFNALGGLPGPY 87
Cdd:PRK14821 2 KIYFATGNKGKVEEAKIILKP-LGIEVEQIKIEYPEIQaDTLEEVAAFGAKWVYNKLNRPVIVEDSGLFIEALNGFPGPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 88 IKWFLQKLKPEGLHQLLAGFEDKSAY-----ALCtfalstgDPSQpVLLFRGQTSGQIVM-PRGSRDFGWDPCFQPDGYE 161
Cdd:PRK14821 81 SAFVYKTLGNEGILKLLEGEENRRAYfksviGYC-------DPGG-EKLFTGIVEGKIANeIRGKGGFGYDPIFIPEGEE 152
|
170 180
....*....|....*....|....*....
gi 1039759159 162 QTYAEMPKSEKNTISHRFRALHKLQEYFS 190
Cdd:PRK14821 153 KTFAEMTTEEKNKISHRKRAFDEFKEWLK 181
|
|
| PRK00120 |
PRK00120 |
dITP/XTP pyrophosphatase; Reviewed |
8-188 |
7.52e-38 |
|
dITP/XTP pyrophosphatase; Reviewed
Pssm-ID: 234648 [Multi-domain] Cd Length: 196 Bit Score: 129.43 E-value: 7.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 8 KKIVFVTGNAKKLEEVIQILGDnFPCTLEAQKiDLPEYqgEPDEI-------SIQKCREAARQVQGPVLVEDTCLCFNAL 80
Cdd:PRK00120 1 MKIVLASHNAGKLRELKALLAP-FGIEVVSQG-ELGVP--EPEETgttfvenALIKARHAAKATGLPALADDSGLCVDAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 81 GGLPGPY--------------IKWFLQKLKPEGlhqllagFEDKSAYALCTFALSTGDPSqpVLLFRGQTSGQIVM-PRG 145
Cdd:PRK00120 77 GGAPGVYsaryagegasdaanNEKLLEELKGVP-------DEDRRARFVCVLVLVRPDPT--PLVAEGRWEGEILWePRG 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039759159 146 SRDFGWDPCFQPDGYEQTYAEMPKSEKNTISHRFRALHKLQEY 188
Cdd:PRK00120 148 ENGFGYDPIFFPPGYGKTFAELTPEEKNAISHRGKALKLLLEA 190
|
|
| PRK14822 |
PRK14822 |
XTP/dITP diphosphatase; |
8-189 |
2.31e-32 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184835 [Multi-domain] Cd Length: 200 Bit Score: 115.37 E-value: 2.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 8 KKIVFVTGNAKKLEEVIQILGDnFPCTLE--AQKIDLPEYQ--GEP-DEISIQKCREAARQVQGPVLVEDTCLCFNALGG 82
Cdd:PRK14822 2 KEIVIATKNKGKVREFKEIFEK-FDIEVKslADFPPIPEVEetGTTfEENAILKAEAAAKALNKPVIADDSGLEVDALNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 83 LPGPY--------------IKWFLQKLkpEGLHQllagfEDKSAYALCTFALSTgdPSQPVLLFRGQTSGQIV-MPRGSR 147
Cdd:PRK14822 81 APGVYsaryageakddaanNEKLLKEL--GGVPF-----EKRTARFHCVIAVAF--PGGETKTVEGTCEGEILeEPRGEN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1039759159 148 DFGWDPCFQPDGYEQTYAEMPKSEKNTISHRFRALHKLQEYF 189
Cdd:PRK14822 152 GFGYDPLFYVPEKGKTMAELSSEEKNAISHRGKALKKLEAEL 193
|
|
| PRK14824 |
PRK14824 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
9-187 |
4.63e-28 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 237824 [Multi-domain] Cd Length: 201 Bit Score: 104.46 E-value: 4.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 9 KIVFVTGNAKKLEEVIQILGDnfpctLEAQKIDLPEY-QGEPD-----EISIQKCREAARQVQGPVLVEDTCLCFNALGG 82
Cdd:PRK14824 2 KILLATTNEGKVREIKRLLSD-----LGIEVLSPDKKiEVEEDgetflENAYLKARAYAEFYKIPVLADDSGLEVPALEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 83 LPGPYIKWFLQ--------------KLKPEGLHQLLAGFEDKSAYALCTFALSTGDPSqpvLLFRGQTSGQIVM-PRGSR 147
Cdd:PRK14824 77 YPGVYSSRFYQiefggkeevveskdEANIRKLLRLLEGKQNRKARFVAFVVLYFGDWG---IWTEGECRGKIAEePRGSG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1039759159 148 DFGWDPCFQPDGYEQTYAEMPKSEKNTISHRFRALHKLQE 187
Cdd:PRK14824 154 GFGYDPVFIPEGYNKTMAELSPEEKNKISHRGKAVRKLVE 193
|
|
| PRK14823 |
PRK14823 |
putative deoxyribonucleoside-triphosphatase; Provisional |
8-190 |
2.07e-27 |
|
putative deoxyribonucleoside-triphosphatase; Provisional
Pssm-ID: 237823 [Multi-domain] Cd Length: 191 Bit Score: 102.45 E-value: 2.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 8 KKIVFVTGNAKKLEEVIQILGDNFPcTLEAQKI----DLPEYQGEPDEISIQKCREAARQVQGPVLVEDTCLCFNALGGL 83
Cdd:PRK14823 1 MKLVFATNNKHKLEEIRSILPEKIE-LLSLSDIgcheDIPETADTLEGNALLKAEYVYKKYGYDCFADDTGLEVEALNGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 84 PGPYIKWF----------LQKLkpegLHQLlAGFEDKSAYALCTFALSTgDPSQpvLLFRGQTSGQIVM-PRGSRDFGWD 152
Cdd:PRK14823 80 PGVYSARYaggehnaeanMRKL----LEEL-EGKDNRKAQFRTVIALIL-DGKE--HLFEGIIKGEIIKeKRGDSGFGYD 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 1039759159 153 PCFQPDGYEQTYAEMPKSEKNTISHRFRALHKLQEYFS 190
Cdd:PRK14823 152 PIFVPEGYDKTFAELGLEIKNQISHRAKAVQKLIDFLS 189
|
|
| Maf_Ham1 |
cd00985 |
Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum ... |
10-140 |
6.12e-26 |
|
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: 96.80 E-value: 6.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 10 IVFVTGNAKKLEEVIQILGDNFpctlEAQKIDLPEYQGE------PDEISIQKCREAARQVQG-PVLVEDTCLCFNalgG 82
Cdd:cd00985 1 LILASGSPRRLEELKQIGGIEF----EVLPSDIDETGLKgepedtVEELALLKARAVAERLPDaPVIADDTGLVVD---G 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039759159 83 LPGPYIKWFlqklkpEGLHQLLAGFEDKSAYALCTFALStgDPSQPVLLFRGQTSGQI 140
Cdd:cd00985 74 RPGGKPARF------AEALEMLRGLSGRTAEFVTAVALV--DPDGKIITFEGETEGKI 123
|
|
| PRK02491 |
PRK02491 |
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; ... |
6-189 |
4.90e-14 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed
Pssm-ID: 179431 [Multi-domain] Cd Length: 328 Bit Score: 69.07 E-value: 4.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 6 VGKKIVFVTGNAKKLEEVIQILGD---------NFPctleaqkiDLPEYQ--GEPDEISIQKCREAARQVQGP-VLVEDT 73
Cdd:PRK02491 126 FGDTILIATRNEGKTKEFRKLFGKlgykvenlnDYP--------DLPEVAetGMTFEENARLKAETISRLTGKmVLADDS 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 74 CLCFNALGGLPGPYIKWFL------QKLKPEGLHQLLAGFE--DKSAYALCTFALSTgdPSQPVLLFRGQTSGQIVM-PR 144
Cdd:PRK02491 198 GLKVDALGGLPGVWSARFSgpdatdAENNAKLLHELAMVFDlkDRSAQFHTTLVVAA--PNKDSLVVEADWPGYIATePK 275
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039759159 145 GSRDFGWDPCFQPDGYEQTYAEMPKSEKNTISHRFRALHKLQEYF 189
Cdd:PRK02491 276 GENGFGYDPLFLVGETGRHAAELTAEEKNQLSHRGQAVKKLMEVF 320
|
|
| PRK14826 |
PRK14826 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
69-190 |
5.95e-14 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173287 Cd Length: 222 Bit Score: 67.38 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 69 LVEDTCLCFNALGGLPGPYIKWFL---QKLKP---EGLHQLL---AGFEDKSAYALCTFALSTGDPS-QPVLLFR----G 134
Cdd:PRK14826 81 LADDTGLEVDALGGAPGVYSARFApvpEGEKPtyeDNVRHLLsemEGKTERSARFRTVIALKGRLPGkNGAFEFEetaeG 160
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039759159 135 QTSGQIVM-PRGSRDFGWDPCFQPDGYEQTYAEMPKSEKNTISHRFRALHK----LQEYFS 190
Cdd:PRK14826 161 VVEGSITTeKKGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRALAVQKavkfLRTILS 221
|
|
| PRK14825 |
PRK14825 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
8-189 |
6.41e-10 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173286 Cd Length: 199 Bit Score: 56.10 E-value: 6.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 8 KKIVFVTGNAKKLEEVIQILgDNFPCTLE-AQKIDLPEYQGEPDEISIQKCREAARQV--QGPVLVEDTCLCFNALGGLP 84
Cdd:PRK14825 2 KTLFFATTNINKINEVKQIL-DIPNIKIEiPQNFDIKETGKTFKENSLLKAKALFEILnnKQPVFSEDSGLCIEALNLEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759159 85 GPYIKWFLQ-----KLKPEGLHQLLAGF----EDKSAYALCTFALSTGDPSqpVLLFRGQTSGQIVMP---RGSRDFGWD 152
Cdd:PRK14825 81 GIYSKRYDQyklgkKLSTNEKNHLIIDLmkneKNRTAYFICNISYISKDGT--ILNFEGIIKGTIALSiddYKKNGFGYD 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039759159 153 PCFQPDGyEQTYAEMPKSEKNTISHRFRALHKLQEYF 189
Cdd:PRK14825 159 PIFLTKN-NKRLSELTLEEKNKISHRGIAFDKFKKFL 194
|
|
|