|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00120 |
PRK00120 |
dITP/XTP pyrophosphatase; Reviewed |
2-197 |
1.92e-125 |
|
dITP/XTP pyrophosphatase; Reviewed
Pssm-ID: 234648 [Multi-domain] Cd Length: 196 Bit Score: 351.31 E-value: 1.92e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 2 QKVVLATGNAGKVRELASLLSDFGLDVVAQTDLGVDSAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVNALGGAP 81
Cdd:PRK00120 1 MKIVLASHNAGKLRELKALLAPFGIEVVSQGELGVPEPEETGTTFVENALIKARHAAKATGLPALADDSGLCVDALGGAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 82 GIYSARYSGEDATDRQNLEKLLHTLQDVPDDKRQAQFHCVLVYMRHadDPTPVVCHGSWPGIITREPAGNGGFGYDPIFF 161
Cdd:PRK00120 81 GVYSARYAGEGASDAANNEKLLEELKGVPDEDRRARFVCVLVLVRP--DPTPLVAEGRWEGEILWEPRGENGFGYDPIFF 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 740848361 162 VPTEGKTAAELTREEKSAISHRGQALKLLLDALRNG 197
Cdd:PRK00120 159 PPGYGKTFAELTPEEKNAISHRGKALKLLLEALREL 194
|
|
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
3-196 |
3.00e-113 |
|
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];
Pssm-ID: 439897 [Multi-domain] Cd Length: 191 Bit Score: 320.47 E-value: 3.00e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 3 KVVLATGNAGKVRELASLLSDFGLDVVAQTDLGVDSAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVNALGGAPG 82
Cdd:COG0127 1 KLVFATGNAGKLREIRALLAPLGIEVVSLSDLGLPEPEETGDTFEENALIKARAAAKATGLPALADDSGLEVDALGGAPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 83 IYSARYSGEDATDRQNLEKLLHTLQDVPDDkRQAQFHCVLVYMRHadDPTPVVCHGSWPGIITREPAGNGGFGYDPIFFV 162
Cdd:COG0127 81 VYSARYAGEGADDEANNEKLLKLLEGVDED-RRARFVCVLALADP--DGEPLVFEGEVEGEIAEEPRGEGGFGYDPIFIP 157
|
170 180 190
....*....|....*....|....*....|....
gi 740848361 163 PTEGKTAAELTREEKSAISHRGQALKLLLDALRN 196
Cdd:COG0127 158 DGYGKTFAELSPEEKNAISHRGRALRKLAEWLKE 191
|
|
| Ham1p_like |
pfam01725 |
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ... |
4-192 |
3.59e-95 |
|
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: 274.71 E-value: 3.59e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 4 VVLATGNAGKVRELASLLSDfGLDVVAQTDLGVDS-AEETGLTFIENAILKARHAAQiTGLPAIADDSGLAVNALGGAPG 82
Cdd:pfam01725 1 IVFATGNAGKLRELKAILAD-GIEVLSLKDLGELPeIEETGGTFEENALIKARAAAK-TGLPVLADDSGLEVDALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 83 IYSARYSGEDATDRQNLEKLLHTLQdVPDDKRQAQFHCVLVYMRHadDPTPVVCHGSWPGIITREPAGNGGFGYDPIFFV 162
Cdd:pfam01725 79 VYSARFAGEGGDDEANNAKLLEELE-VPDEDRSARFVCVIALADP--GGPELVFEGEVEGEIVEEPRGEGGFGYDPIFIP 155
|
170 180 190
....*....|....*....|....*....|
gi 740848361 163 PTEGKTAAELTREEKSAISHRGQALKLLLD 192
Cdd:pfam01725 156 PEGGKTFAELSPEEKNAISHRGKALRKLKE 185
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
3-195 |
1.23e-94 |
|
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: 273.09 E-value: 1.23e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 3 KVVLATGNAGKVRELASLLSDFGLDVVAQTDLGvdSAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVNALGGAPG 82
Cdd:TIGR00042 1 KIVFATGNPGKLKEVQSILSDLGDNEIEQLDLG--YPEETGLTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 83 IYSARYSGedaTDRQNLEKLLHTLQDVPDdkRQAQFHCVLVYMRHADDPtpVVCHGSWPGIITREPAGNGGFGYDPIFFV 162
Cdd:TIGR00042 79 IYSARYQG---TDIGNLEKILKLLEGVEN--RQAYFVCVIGYCDPNGEP--LVFEGIVKGKITREPRGTYGFGYDPIFIP 151
|
170 180 190
....*....|....*....|....*....|...
gi 740848361 163 PTEGKTAAELTREEKSAISHRGQALKLLLDALR 195
Cdd:TIGR00042 152 PEEGKTFAELTTEEKNKISHRGKAFKKFKKFLL 184
|
|
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
4-193 |
1.58e-90 |
|
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: 262.84 E-value: 1.58e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 4 VVLATGNAGKVRELASLLSDFGLDVVAQTDLGvdSAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVNALGGAPGI 83
Cdd:cd00515 1 IVFATGNKGKLKEFKEILAPFGIEVVSLKDII--DIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 84 YSARYSGEdATDRQNLEKLLHTLQDvpDDKRQAQFHCVLVYMRHadDPTPVVCHGSWPGIITREPAGNGGFGYDPIFFVP 163
Cdd:cd00515 79 YSARFAGE-HDDAENNEKLLELLEG--DEDRSAYFVCVIALVDP--DGEPLVFEGEVEGKIVTEPRGTGGFGYDPIFIPE 153
|
170 180 190
....*....|....*....|....*....|
gi 740848361 164 TEGKTAAELTREEKSAISHRGQALKLLLDA 193
Cdd:cd00515 154 GYGKTFAEMSPEEKNAISHRGKALRKLKEF 183
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00120 |
PRK00120 |
dITP/XTP pyrophosphatase; Reviewed |
2-197 |
1.92e-125 |
|
dITP/XTP pyrophosphatase; Reviewed
Pssm-ID: 234648 [Multi-domain] Cd Length: 196 Bit Score: 351.31 E-value: 1.92e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 2 QKVVLATGNAGKVRELASLLSDFGLDVVAQTDLGVDSAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVNALGGAP 81
Cdd:PRK00120 1 MKIVLASHNAGKLRELKALLAPFGIEVVSQGELGVPEPEETGTTFVENALIKARHAAKATGLPALADDSGLCVDALGGAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 82 GIYSARYSGEDATDRQNLEKLLHTLQDVPDDKRQAQFHCVLVYMRHadDPTPVVCHGSWPGIITREPAGNGGFGYDPIFF 161
Cdd:PRK00120 81 GVYSARYAGEGASDAANNEKLLEELKGVPDEDRRARFVCVLVLVRP--DPTPLVAEGRWEGEILWEPRGENGFGYDPIFF 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 740848361 162 VPTEGKTAAELTREEKSAISHRGQALKLLLDALRNG 197
Cdd:PRK00120 159 PPGYGKTFAELTPEEKNAISHRGKALKLLLEALREL 194
|
|
| RdgB |
COG0127 |
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide ... |
3-196 |
3.00e-113 |
|
Inosine/xanthosine triphosphate pyrophosphatase, all-alpha NTP-PPase family [Nucleotide transport and metabolism];
Pssm-ID: 439897 [Multi-domain] Cd Length: 191 Bit Score: 320.47 E-value: 3.00e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 3 KVVLATGNAGKVRELASLLSDFGLDVVAQTDLGVDSAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVNALGGAPG 82
Cdd:COG0127 1 KLVFATGNAGKLREIRALLAPLGIEVVSLSDLGLPEPEETGDTFEENALIKARAAAKATGLPALADDSGLEVDALGGAPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 83 IYSARYSGEDATDRQNLEKLLHTLQDVPDDkRQAQFHCVLVYMRHadDPTPVVCHGSWPGIITREPAGNGGFGYDPIFFV 162
Cdd:COG0127 81 VYSARYAGEGADDEANNEKLLKLLEGVDED-RRARFVCVLALADP--DGEPLVFEGEVEGEIAEEPRGEGGFGYDPIFIP 157
|
170 180 190
....*....|....*....|....*....|....
gi 740848361 163 PTEGKTAAELTREEKSAISHRGQALKLLLDALRN 196
Cdd:COG0127 158 DGYGKTFAELSPEEKNAISHRGRALRKLAEWLKE 191
|
|
| Ham1p_like |
pfam01725 |
Ham1 family; This family consists of the HAM1 protein and hypothetical archaeal bacterial and ... |
4-192 |
3.59e-95 |
|
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: 274.71 E-value: 3.59e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 4 VVLATGNAGKVRELASLLSDfGLDVVAQTDLGVDS-AEETGLTFIENAILKARHAAQiTGLPAIADDSGLAVNALGGAPG 82
Cdd:pfam01725 1 IVFATGNAGKLRELKAILAD-GIEVLSLKDLGELPeIEETGGTFEENALIKARAAAK-TGLPVLADDSGLEVDALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 83 IYSARYSGEDATDRQNLEKLLHTLQdVPDDKRQAQFHCVLVYMRHadDPTPVVCHGSWPGIITREPAGNGGFGYDPIFFV 162
Cdd:pfam01725 79 VYSARFAGEGGDDEANNAKLLEELE-VPDEDRSARFVCVIALADP--GGPELVFEGEVEGEIVEEPRGEGGFGYDPIFIP 155
|
170 180 190
....*....|....*....|....*....|
gi 740848361 163 PTEGKTAAELTREEKSAISHRGQALKLLLD 192
Cdd:pfam01725 156 PEGGKTFAELSPEEKNAISHRGKALRKLKE 185
|
|
| TIGR00042 |
TIGR00042 |
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Saccharomyces cerevisiae HAM1 ... |
3-195 |
1.23e-94 |
|
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: 273.09 E-value: 1.23e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 3 KVVLATGNAGKVRELASLLSDFGLDVVAQTDLGvdSAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVNALGGAPG 82
Cdd:TIGR00042 1 KIVFATGNPGKLKEVQSILSDLGDNEIEQLDLG--YPEETGLTFEENALLKAKHAAKILNKPVIAEDSGLFVDALNGFPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 83 IYSARYSGedaTDRQNLEKLLHTLQDVPDdkRQAQFHCVLVYMRHADDPtpVVCHGSWPGIITREPAGNGGFGYDPIFFV 162
Cdd:TIGR00042 79 IYSARYQG---TDIGNLEKILKLLEGVEN--RQAYFVCVIGYCDPNGEP--LVFEGIVKGKITREPRGTYGFGYDPIFIP 151
|
170 180 190
....*....|....*....|....*....|...
gi 740848361 163 PTEGKTAAELTREEKSAISHRGQALKLLLDALR 195
Cdd:TIGR00042 152 PEEGKTFAELTTEEKNKISHRGKAFKKFKKFLL 184
|
|
| PRK14822 |
PRK14822 |
XTP/dITP diphosphatase; |
1-194 |
7.74e-94 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184835 [Multi-domain] Cd Length: 200 Bit Score: 271.76 E-value: 7.74e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 1 MQKVVLATGNAGKVRELASLLSDFGLDVVAQTDLGVD-SAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVNALGG 79
Cdd:PRK14822 1 MKEIVIATKNKGKVREFKEIFEKFDIEVKSLADFPPIpEVEETGTTFEENAILKAEAAAKALNKPVIADDSGLEVDALNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 80 APGIYSARYSGEDATDRQNLEKLLHTLQDVPDDKRQAQFHCVLVyMRHADDPTPVVcHGSWPGIITREPAGNGGFGYDPI 159
Cdd:PRK14822 81 APGVYSARYAGEAKDDAANNEKLLKELGGVPFEKRTARFHCVIA-VAFPGGETKTV-EGTCEGEILEEPRGENGFGYDPL 158
|
170 180 190
....*....|....*....|....*....|....*
gi 740848361 160 FFVPTEGKTAAELTREEKSAISHRGQALKLLLDAL 194
Cdd:PRK14822 159 FYVPEKGKTMAELSSEEKNAISHRGKALKKLEAEL 193
|
|
| HAM1 |
cd00515 |
NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ ... |
4-193 |
1.58e-90 |
|
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: 262.84 E-value: 1.58e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 4 VVLATGNAGKVRELASLLSDFGLDVVAQTDLGvdSAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVNALGGAPGI 83
Cdd:cd00515 1 IVFATGNKGKLKEFKEILAPFGIEVVSLKDII--DIEETGSTFEENALLKARAAAEALGLPVLADDSGLCVDALNGFPGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 84 YSARYSGEdATDRQNLEKLLHTLQDvpDDKRQAQFHCVLVYMRHadDPTPVVCHGSWPGIITREPAGNGGFGYDPIFFVP 163
Cdd:cd00515 79 YSARFAGE-HDDAENNEKLLELLEG--DEDRSAYFVCVIALVDP--DGEPLVFEGEVEGKIVTEPRGTGGFGYDPIFIPE 153
|
170 180 190
....*....|....*....|....*....|
gi 740848361 164 TEGKTAAELTREEKSAISHRGQALKLLLDA 193
Cdd:cd00515 154 GYGKTFAEMSPEEKNAISHRGKALRKLKEF 183
|
|
| PRK02491 |
PRK02491 |
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; ... |
4-193 |
2.77e-64 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase/unknown domain fusion protein; Reviewed
Pssm-ID: 179431 [Multi-domain] Cd Length: 328 Bit Score: 201.19 E-value: 2.77e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 4 VVLATGNAGKVRELASLLSDFGLDVVAQTDL-GVDSAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVNALGGAPG 82
Cdd:PRK02491 130 ILIATRNEGKTKEFRKLFGKLGYKVENLNDYpDLPEVAETGMTFEENARLKAETISRLTGKMVLADDSGLKVDALGGLPG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 83 IYSARYSGEDATDRQNLEKLLHTLQDVPDDK-RQAQFHCVLVYMrhADDPTPVVCHGSWPGIITREPAGNGGFGYDPIFF 161
Cdd:PRK02491 210 VWSARFSGPDATDAENNAKLLHELAMVFDLKdRSAQFHTTLVVA--APNKDSLVVEADWPGYIATEPKGENGFGYDPLFL 287
|
170 180 190
....*....|....*....|....*....|..
gi 740848361 162 VPTEGKTAAELTREEKSAISHRGQALKLLLDA 193
Cdd:PRK02491 288 VGETGRHAAELTAEEKNQLSHRGQAVKKLMEV 319
|
|
| PRK14824 |
PRK14824 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
3-197 |
3.98e-55 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 237824 [Multi-domain] Cd Length: 201 Bit Score: 173.79 E-value: 3.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 3 KVVLATGNAGKVRELASLLSDFGLDVVAqTDLGVDsAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVNALGGAPG 82
Cdd:PRK14824 2 KILLATTNEGKVREIKRLLSDLGIEVLS-PDKKIE-VEEDGETFLENAYLKARAYAEFYKIPVLADDSGLEVPALEGYPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 83 IYSAR-----YSGED----ATDRQNLEKLLHTLQDVPDdkRQAQFHCVLV-YMRHADDPTPVVCHGSwpgiITREPAGNG 152
Cdd:PRK14824 80 VYSSRfyqieFGGKEevveSKDEANIRKLLRLLEGKQN--RKARFVAFVVlYFGDWGIWTEGECRGK----IAEEPRGSG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 740848361 153 GFGYDPIfFVPtEG--KTAAELTREEKSAISHRGQALKLLLDALRNG 197
Cdd:PRK14824 154 GFGYDPV-FIP-EGynKTMAELSPEEKNKISHRGKAVRKLVEILKYG 198
|
|
| PRK14826 |
PRK14826 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
4-196 |
2.81e-53 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173287 Cd Length: 222 Bit Score: 169.46 E-value: 2.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 4 VVLATGNAGKVRELASLLS--DFGLDVVAQTDLGVDSA-EETGLTFIENAILKARH-----AAQITGLPAIADDSGLAVN 75
Cdd:PRK14826 11 IVLATGNRDKVRELRPLLEhiSPLFSVRSLADLGVEVDiEETEETLEGNALLKADAifellSDRFPFLIALADDTGLEVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 76 ALGGAPGIYSARYS----GEDATDRQNLEKLLHTLQDVPDdkRQAQFHCVLVY---MRHADDPTPV--VCHGSWPGIITR 146
Cdd:PRK14826 91 ALGGAPGVYSARFApvpeGEKPTYEDNVRHLLSEMEGKTE--RSARFRTVIALkgrLPGKNGAFEFeeTAEGVVEGSITT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 740848361 147 EPAGNGGFGYDPIFFVPTEGKTAAELTREEKSAISHRGQALKLLLDALRN 196
Cdd:PRK14826 169 EKKGDGGFGYDPIFRVEATGKTFAEMSTEEKNTISHRALAVQKAVKFLRT 218
|
|
| PRK14823 |
PRK14823 |
putative deoxyribonucleoside-triphosphatase; Provisional |
3-196 |
2.23e-51 |
|
putative deoxyribonucleoside-triphosphatase; Provisional
Pssm-ID: 237823 [Multi-domain] Cd Length: 191 Bit Score: 163.70 E-value: 2.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 3 KVVLATGNAGKVRELASLLSDfGLDVVAQTDLGV-DSAEETGLTFIENAILKARHAAQITGLPAIADDSGLAVNALGGAP 81
Cdd:PRK14823 2 KLVFATNNKHKLEEIRSILPE-KIELLSLSDIGChEDIPETADTLEGNALLKAEYVYKKYGYDCFADDTGLEVEALNGAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 82 GIYSARYSGEDATDRQNLEKLLHTLQDVPDdkRQAQFHCVLVYMrhaDDPTPVVCHGSWPGIITREPAGNGGFGYDPIFF 161
Cdd:PRK14823 81 GVYSARYAGGEHNAEANMRKLLEELEGKDN--RKAQFRTVIALI---LDGKEHLFEGIIKGEIIKEKRGDSGFGYDPIFV 155
|
170 180 190
....*....|....*....|....*....|....*
gi 740848361 162 VPTEGKTAAELTREEKSAISHRGQALKLLLDALRN 196
Cdd:PRK14823 156 PEGYDKTFAELGLEIKNQISHRAKAVQKLIDFLSK 190
|
|
| PRK14821 |
PRK14821 |
XTP/dITP diphosphatase; |
3-196 |
1.19e-38 |
|
XTP/dITP diphosphatase;
Pssm-ID: 184834 [Multi-domain] Cd Length: 184 Bit Score: 130.84 E-value: 1.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 3 KVVLATGNAGKVRELASLLSDFGLDVVAQTD----LGVDSAEETgltfienAILKARHAAQITGLPAIADDSGLAVNALG 78
Cdd:PRK14821 2 KIYFATGNKGKVEEAKIILKPLGIEVEQIKIeypeIQADTLEEV-------AAFGAKWVYNKLNRPVIVEDSGLFIEALN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 79 GAPGIYSArYsgedATDRQNLEKLLHTLQDVPDdkRQAQFHCVLVYMRHADDP--TPVVChgswpGIITREPAGNGGFGY 156
Cdd:PRK14821 75 GFPGPYSA-F----VYKTLGNEGILKLLEGEEN--RRAYFKSVIGYCDPGGEKlfTGIVE-----GKIANEIRGKGGFGY 142
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 740848361 157 DPIFFVPTEGKTAAELTREEKSAISHRGQALKLLLDALRN 196
Cdd:PRK14821 143 DPIFIPEGEEKTFAEMTTEEKNKISHRKRAFDEFKEWLKE 182
|
|
| PRK14825 |
PRK14825 |
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional |
1-194 |
5.99e-26 |
|
putative deoxyribonucleotide triphosphate pyrophosphatase; Provisional
Pssm-ID: 173286 Cd Length: 199 Bit Score: 98.85 E-value: 5.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 1 MQKVVLATGNAGKVRELASLLSDFGLDVVAQTDLGVdsaEETGLTFIENAILKARHAAQITG--LPAIADDSGLAVNALG 78
Cdd:PRK14825 1 MKTLFFATTNINKINEVKQILDIPNIKIEIPQNFDI---KETGKTFKENSLLKAKALFEILNnkQPVFSEDSGLCIEALN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 79 GAPGIYSARYsgedatDRQNLEKLL------HTLQDVPDDK--RQAQFHCVLVYMrhADDPTPVVCHGSWPGIITR--EP 148
Cdd:PRK14825 78 LEPGIYSKRY------DQYKLGKKLstneknHLIIDLMKNEknRTAYFICNISYI--SKDGTILNFEGIIKGTIALsiDD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 740848361 149 AGNGGFGYDPIFFVpTEGKTAAELTREEKSAISHRGQAL----KLLLDAL 194
Cdd:PRK14825 150 YKKNGFGYDPIFLT-KNNKRLSELTLEEKNKISHRGIAFdkfkKFLMQSL 198
|
|
| Maf_Ham1 |
cd00985 |
Maf_Ham1. Maf, a nucleotide binding protein, has been implicated in inhibition of septum ... |
4-142 |
7.78e-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: 96.42 E-value: 7.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740848361 4 VVLATGNAGKVRELASLLsdfGLDVVAQtDLGVD---SAEETGLTFIENAILKARHAAQITG-LPAIADDSGLAVNalgG 79
Cdd:cd00985 1 LILASGSPRRLEELKQIG---GIEFEVL-PSDIDetgLKGEPEDTVEELALLKARAVAERLPdAPVIADDTGLVVD---G 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740848361 80 APGIYSARYSGEdatdrqnLEKLlhtlqdVPDDKRQAQFHCVLVYMRHadDPTPVVCHGSWPG 142
Cdd:cd00985 74 RPGGKPARFAEA-------LEML------RGLSGRTAEFVTAVALVDP--DGKIITFEGETEG 121
|
|
| |
