|
Name |
Accession |
Description |
Interval |
E-value |
| Dut |
COG0756 |
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ... |
173-304 |
5.50e-32 |
|
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP pyrophosphatase (dUTPase) is part of the Pathway/BioSystem: Thymidylate biosynthesis
Pssm-ID: 440519 [Multi-domain] Cd Length: 143 Bit Score: 115.88 E-value: 5.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 173 EVQLPTRAYSDDAGLDLF--VTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKKGL-LVN-PGIIDAGYRGEL 248
Cdd:COG0756 10 DAPLPAYATPGSAGLDLRaaLDEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGItLLNsPGTIDSDYRGEI 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2027880700 249 FSGVQNMTSKPVHVEAGERIAQLIIigngTR--QIEPVLVPELNSHARGKNGFGSSGK 304
Cdd:COG0756 90 KVILINLGDEPFTIERGDRIAQLVI----APvvQAEFEEVEELDETERGAGGFGSTGR 143
|
|
| dUTPase |
pfam00692 |
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate. |
172-303 |
1.11e-30 |
|
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
Pssm-ID: 395562 [Multi-domain] Cd Length: 129 Bit Score: 112.00 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 172 AEVQLPTRAYSDDAGLDLFVTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSStLRKKGLLVNPGIIDAGYRGELFSG 251
Cdd:pfam00692 1 DEAEIPTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSG-LAAKGLIVVPGVIDSDYRGEVKVV 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2027880700 252 VQNMTSKPVHVEAGERIAQLIIIGNGTRQIEPVLvpELNSHARGKNGFGSSG 303
Cdd:pfam00692 80 LFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVE--TLDNTDRGDGGFGSSG 129
|
|
| dut |
TIGR00576 |
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ... |
163-304 |
9.64e-27 |
|
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is in maintaining the levels of dUTP in the cell to prevent dUTP incorporation into DNA during DNA replication. Pol proteins in viruses are very similar to this protein family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Changed role from 132 to 123. RTD [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
Pssm-ID: 273149 [Multi-domain] Cd Length: 142 Bit Score: 101.93 E-value: 9.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 163 TLQFAPVDgAEVQLPTRAYSDDAGLDLFVTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKKG--LLVNPGII 240
Cdd:TIGR00576 1 KLKFVKLS-PNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGvtIDNSPGVI 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2027880700 241 DAGYRGELFSGVQNMTSKPVHVEAGERIAQLII--IGngtRQIEPVLVPELNSHARGKNGFGSSGK 304
Cdd:TIGR00576 80 DADYRGEIKVILINLGKEDFTVKKGDRIAQLVVekIV---TEVEFEEVEELDETERGEGGFGSTGV 142
|
|
| trimeric_dUTPase |
cd07557 |
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ... |
185-273 |
1.55e-24 |
|
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common family of dUTPase, found in bacteria, eukaryotes, and archaea. They catalyze the hydrolysis of the dUTP-Mg complex (dUTP-Mg) into dUMP and pyrophosphate. This reaction is crucial for the preservation of chromosomal integrity as it removes dUTP and therefore reduces the cellular dUTP/dTTP ratio, and prevents dUTP from being incorporated into DNA. It also provides dUMP as the precursor for dTTP synthesis via the thymidylate synthase pathway. dUTPases are homotrimeric, except some monomeric viral dUTPases, which have been shown to mimic a trimer. Active sites are located at the subunit interface.
Pssm-ID: 143638 [Multi-domain] Cd Length: 92 Bit Score: 94.48 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 185 AGLDLFVTED---TWVPANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKkGLLV-NPGIIDAGYRGELFSGVQNMTSKPV 260
Cdd:cd07557 1 AGYDLRLGEDfegIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLARK-GITVhNAGVIDPGYRGEITLELYNLGPEPV 79
|
90
....*....|...
gi 2027880700 261 HVEAGERIAQLII 273
Cdd:cd07557 80 VIKKGDRIAQLVF 92
|
|
| dut |
PRK00601 |
dUTP diphosphatase; |
171-304 |
1.40e-22 |
|
dUTP diphosphatase;
Pssm-ID: 234802 [Multi-domain] Cd Length: 150 Bit Score: 91.38 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 171 GAEVQLPTRAYSDDAGLDLFVTEDTWV--PANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKKGL-LVN-PGIIDAGYRG 246
Cdd:PRK00601 14 GKEFPLPAYATEGSAGLDLRACLDEPVtlAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIvLGNlPGTIDSDYRG 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2027880700 247 ELFSGVQNMTSKPVHVEAGERIAQLIIIgnGTRQIEPVLVPELNSHARGKNGFGSSGK 304
Cdd:PRK00601 94 ELKVSLWNRGQEPFTIEPGERIAQLVIV--PVVQAEFEEVEEFDETERGAGGFGSTGR 149
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Dut |
COG0756 |
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ... |
173-304 |
5.50e-32 |
|
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP pyrophosphatase (dUTPase) is part of the Pathway/BioSystem: Thymidylate biosynthesis
Pssm-ID: 440519 [Multi-domain] Cd Length: 143 Bit Score: 115.88 E-value: 5.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 173 EVQLPTRAYSDDAGLDLF--VTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKKGL-LVN-PGIIDAGYRGEL 248
Cdd:COG0756 10 DAPLPAYATPGSAGLDLRaaLDEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGItLLNsPGTIDSDYRGEI 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2027880700 249 FSGVQNMTSKPVHVEAGERIAQLIIigngTR--QIEPVLVPELNSHARGKNGFGSSGK 304
Cdd:COG0756 90 KVILINLGDEPFTIERGDRIAQLVI----APvvQAEFEEVEELDETERGAGGFGSTGR 143
|
|
| dUTPase |
pfam00692 |
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate. |
172-303 |
1.11e-30 |
|
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
Pssm-ID: 395562 [Multi-domain] Cd Length: 129 Bit Score: 112.00 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 172 AEVQLPTRAYSDDAGLDLFVTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSStLRKKGLLVNPGIIDAGYRGELFSG 251
Cdd:pfam00692 1 DEAEIPTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSG-LAAKGLIVVPGVIDSDYRGEVKVV 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2027880700 252 VQNMTSKPVHVEAGERIAQLIIIGNGTRQIEPVLvpELNSHARGKNGFGSSG 303
Cdd:pfam00692 80 LFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVE--TLDNTDRGDGGFGSSG 129
|
|
| dut |
TIGR00576 |
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ... |
163-304 |
9.64e-27 |
|
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is in maintaining the levels of dUTP in the cell to prevent dUTP incorporation into DNA during DNA replication. Pol proteins in viruses are very similar to this protein family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Changed role from 132 to 123. RTD [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
Pssm-ID: 273149 [Multi-domain] Cd Length: 142 Bit Score: 101.93 E-value: 9.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 163 TLQFAPVDgAEVQLPTRAYSDDAGLDLFVTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKKG--LLVNPGII 240
Cdd:TIGR00576 1 KLKFVKLS-PNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGvtIDNSPGVI 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2027880700 241 DAGYRGELFSGVQNMTSKPVHVEAGERIAQLII--IGngtRQIEPVLVPELNSHARGKNGFGSSGK 304
Cdd:TIGR00576 80 DADYRGEIKVILINLGKEDFTVKKGDRIAQLVVekIV---TEVEFEEVEELDETERGEGGFGSTGV 142
|
|
| trimeric_dUTPase |
cd07557 |
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ... |
185-273 |
1.55e-24 |
|
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common family of dUTPase, found in bacteria, eukaryotes, and archaea. They catalyze the hydrolysis of the dUTP-Mg complex (dUTP-Mg) into dUMP and pyrophosphate. This reaction is crucial for the preservation of chromosomal integrity as it removes dUTP and therefore reduces the cellular dUTP/dTTP ratio, and prevents dUTP from being incorporated into DNA. It also provides dUMP as the precursor for dTTP synthesis via the thymidylate synthase pathway. dUTPases are homotrimeric, except some monomeric viral dUTPases, which have been shown to mimic a trimer. Active sites are located at the subunit interface.
Pssm-ID: 143638 [Multi-domain] Cd Length: 92 Bit Score: 94.48 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 185 AGLDLFVTED---TWVPANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKkGLLV-NPGIIDAGYRGELFSGVQNMTSKPV 260
Cdd:cd07557 1 AGYDLRLGEDfegIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLARK-GITVhNAGVIDPGYRGEITLELYNLGPEPV 79
|
90
....*....|...
gi 2027880700 261 HVEAGERIAQLII 273
Cdd:cd07557 80 VIKKGDRIAQLVF 92
|
|
| dut |
PRK00601 |
dUTP diphosphatase; |
171-304 |
1.40e-22 |
|
dUTP diphosphatase;
Pssm-ID: 234802 [Multi-domain] Cd Length: 150 Bit Score: 91.38 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 171 GAEVQLPTRAYSDDAGLDLFVTEDTWV--PANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKKGL-LVN-PGIIDAGYRG 246
Cdd:PRK00601 14 GKEFPLPAYATEGSAGLDLRACLDEPVtlAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIvLGNlPGTIDSDYRG 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2027880700 247 ELFSGVQNMTSKPVHVEAGERIAQLIIIgnGTRQIEPVLVPELNSHARGKNGFGSSGK 304
Cdd:PRK00601 94 ELKVSLWNRGQEPFTIEPGERIAQLVIV--PVVQAEFEEVEEFDETERGAGGFGSTGR 149
|
|
| PLN02547 |
PLN02547 |
dUTP pyrophosphatase |
176-303 |
8.59e-19 |
|
dUTP pyrophosphatase
Pssm-ID: 215302 Cd Length: 157 Bit Score: 81.38 E-value: 8.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 176 LPTRAYSDDAGLDLFVTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKKGLLVNPGIIDAGYRGELFSGVQNM 255
Cdd:PLN02547 28 LPSRGSALAAGYDLSSAYDTVVPARGKALVPTDLSIAIPEGTYARIAPRSGLAWKHSIDVGAGVIDADYRGPVGVILFNH 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2027880700 256 TSKPVHVEAGERIAQLIIigngtRQI---EPVLVPELNSHARGKNGFGSSG 303
Cdd:PLN02547 108 SDVDFEVKVGDRIAQLIL-----EKIvtpEVVEVEDLDATVRGAGGFGSTG 153
|
|
| PTZ00143 |
PTZ00143 |
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional |
181-304 |
3.65e-18 |
|
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
Pssm-ID: 240288 [Multi-domain] Cd Length: 155 Bit Score: 79.78 E-value: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 181 YSDDAGLDLFVTEDTWVPANGFVDIRSHIKV----------QLPDWSWgFLVGRSSTLRKKGLLVNP-GIIDAGYRGELF 249
Cdd:PTZ00143 23 HEGDSGLDLFIVKDQTIKPGETAFIKLGIKAaafqkdedgsDGKNVSW-LLFPRSSISKTPLRLANSiGLIDAGYRGELI 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2027880700 250 SGVQNMTSKPVHVEAGERIAQLIIIgNGtRQIEPVLVPELNSHARGKNGFGSSGK 304
Cdd:PTZ00143 102 AAVDNIKDEPYTIKKGDRLVQLVSF-DG-EPITFELVDELDETTRGEGGFGSTGR 154
|
|
| PHA03094 |
PHA03094 |
dUTPase; Provisional |
176-303 |
1.02e-15 |
|
dUTPase; Provisional
Pssm-ID: 165376 [Multi-domain] Cd Length: 144 Bit Score: 72.88 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 176 LPTRAYSDDAGLDLFVTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKKGLLVNPGIIDAGYRGELFSGVQNM 255
Cdd:PHA03094 17 IPTRSSPKSAGYDLYSAYDYTVPPKERILVKTDISLSIPKFCYGRIAPRSGLSLNYGIDIGGGVIDEDYRGNIGVIFINN 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2027880700 256 TSKPVHVEAGERIAQLIIIGNGTRQIEPVLvpELNSHARGKNGFGSSG 303
Cdd:PHA03094 97 GKCTFNIKTGDRIAQIIFERIEYPELKEVQ--SLDSTDRGDQGFGSSG 142
|
|
| PHA02703 |
PHA02703 |
ORF007 dUTPase; Provisional |
176-303 |
1.03e-15 |
|
ORF007 dUTPase; Provisional
Pssm-ID: 165079 Cd Length: 165 Bit Score: 73.09 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 176 LPTRAYSDDAGLDLFVTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKKGLLVNPGIIDAGYRGELFSGVQNM 255
Cdd:PHA02703 25 IPTRGSPGAAGLDLCSACDCIVPAGCRCVVFTDLLIKLPDGCYGRIAPRSGLAVKHFIDVGAGVIDADYRGNVGVVLFNF 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2027880700 256 TSKPVHVEAGERIAQLIIigngTRQIEPVL--VPELNSHARGKNGFGSSG 303
Cdd:PHA02703 105 GHNDFEVKKGDRIAQLIC----ERAAFPAVeeVACLDDTDRGAGGFGSTG 150
|
|
| dut |
PRK13956 |
dUTP diphosphatase; |
176-304 |
1.30e-14 |
|
dUTP diphosphatase;
Pssm-ID: 184417 [Multi-domain] Cd Length: 147 Bit Score: 69.82 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 176 LPTRAYSDDAGLDLFVTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKKGL-LVNP-GIIDAGY------RGE 247
Cdd:PRK13956 18 LPKRETAHAAGYDLKVAERTVIAPGEIKLVPTGVKAYMQPGEVLYLYDRSSNPRKKGLvLINSvGVIDGDYygnpanEGH 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2027880700 248 LFSGVQNMTSKPVHVEAGERIAQLIIIgngtrqiePVLVPElNSHARGK--NGFGSSGK 304
Cdd:PRK13956 98 IFAQMKNITDQEVVLEVGERIVQGVFM--------PFLIAD-GDQADGErtGGFGSTGK 147
|
|
| Dcd |
COG0717 |
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ... |
192-272 |
3.53e-11 |
|
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway/BioSystem: Thymidylate biosynthesis
Pssm-ID: 440481 Cd Length: 180 Bit Score: 60.99 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 192 TEDTWV-PANGFVDIRSHIKVQLPDWSWGFLVGRSSTLRKkGLLVNP--GIIDAGYRGELFSGVQNMTSKPVHVEAGERI 268
Cdd:COG0717 66 PGDGFIlPPGEFYLARTLEYVRLPDDLVAFLEGRSSLARL-GLFVHTtaGVIDPGFEGRITLELSNTGPLPIKLYPGMRI 144
|
....
gi 2027880700 269 AQLI 272
Cdd:COG0717 145 AQLV 148
|
|
| dCTP_deam |
TIGR02274 |
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ... |
197-272 |
1.26e-09 |
|
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli monofunctional deoxycytidine triphosphate deaminase (dCTP deaminase) and a Methanocaldococcus jannaschii bifunctional dCTP deaminase (3.5.4.13)/dUTP diphosphatase (EC 3.6.1.23), which has the EC number 3.5.4.30 for the overall operation. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
Pssm-ID: 274062 Cd Length: 179 Bit Score: 56.55 E-value: 1.26e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2027880700 197 VPANGFVDIRSHIKVQLPDWSWGFLVGRSStLRKKGLLVNP--GIIDAGYRGELFSGVQNMTSKPVHVEAGERIAQLI 272
Cdd:TIGR02274 73 IPPGEFALATTLEYVKLPDDVVGFLEGRSS-LARLGLFIHVtaGRIDPGFEGNITLELFNAGKLPVKLRPGMRIAQLV 149
|
|
| PHA03130 |
PHA03130 |
dUTPase; Provisional |
176-275 |
3.75e-08 |
|
dUTPase; Provisional
Pssm-ID: 222995 [Multi-domain] Cd Length: 368 Bit Score: 54.14 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 176 LPTRAysDDAGLDLFVTEDTWVPANGFVDIRSHIKVQLPDWSWG--FLVGRSStLRKKGLLVNPGIIDAGyRGELFSgVQ 253
Cdd:PHA03130 207 LPKRA--EDAGIDIVVHKRVEVPAGGTVVIQPSLRVLLAAGGPEayYVLGRSS-LNARGVLVTPTRWLPG-RQCAFS-VH 281
|
90 100
....*....|....*....|..
gi 2027880700 254 NMTSKPVHVEAGERIAQLIIIG 275
Cdd:PHA03130 282 NITGAPVTLEAGSKVAQLLVAG 303
|
|
| PHA03124 |
PHA03124 |
dUTPase; Provisional |
182-304 |
4.73e-07 |
|
dUTPase; Provisional
Pssm-ID: 165396 [Multi-domain] Cd Length: 418 Bit Score: 50.71 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 182 SDDAGLDLFVTEDTWVPANGFVDIRSHIKVQLPDWSWGFLVGRSStLRKKGLLVNP-GIIDAGYRGelFSgVQNMTSKPV 260
Cdd:PHA03124 288 AEDAGYDIRAPEDCTILPGGSTRIILPQKLACGKFRAAFILGRSS-MNLKGLLVDPeHVQDDDWIS--FN-ITNIRDAAA 363
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2027880700 261 HVEAGERIAQLIIIGNGT-----------RQIEPVLVPELNSHARGKNGFGSSGK 304
Cdd:PHA03124 364 FFHAGDRIAQLIALEDKLeflgepdalpwKIVNSVQDEKKNLSSRGDGGFGSSGK 418
|
|
| PHA03123 |
PHA03123 |
dUTPase; Provisional |
183-281 |
2.34e-06 |
|
dUTPase; Provisional
Pssm-ID: 165395 [Multi-domain] Cd Length: 402 Bit Score: 48.45 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 183 DDAGLDLFVTEDTWVPANGFvdirshIKVQLP---DWSW------GFLVGRSSTLRKkGLLVNPGIIDAGYRGELFsgVQ 253
Cdd:PHA03123 243 EDAGYDICAPFEITLKANEF------IKITLPfiqDLDLnhpnidAYIFGRSSKNRI-GIIVCPTAWIAGEHCEFY--IF 313
|
90 100
....*....|....*....|....*...
gi 2027880700 254 NMTSKPVHVEAGERIAQLIIIGNGTRQI 281
Cdd:PHA03123 314 NATGDDIIIKPGDKIAQVLLIDHNNQSI 341
|
|
| PHA03127 |
PHA03127 |
dUTPase; Provisional |
133-303 |
3.10e-06 |
|
dUTPase; Provisional
Pssm-ID: 222993 [Multi-domain] Cd Length: 322 Bit Score: 48.07 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 133 WQFATIEAMDWLADQKLPSFAKGNPARERktLQFAPVD-----GAEVQLPTRAY-----SDDAGLDLFVTEDTWVPANGF 202
Cdd:PHA03127 115 WAPPCIETIPEAGLALRLTLARLAKTTPR--LAACDDTaragqGAGVEVPFFETfapkrDEDAGYDIAMPYTAVLAPGEN 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 203 VDIRSHIkVQLPD--WSWGFLVGRSStLRKKGLLVNPGIIDAGYRGELFsgVQNMTSKPVHVEAGERIAQLIIIgngtrq 280
Cdd:PHA03127 193 LHVRLPV-AYAAGahAAAPYVFGRSS-LNLRGIVVLPTAWPPGEPCRFV--IRNVTQEPVVAAAGQRVAQLLLL------ 262
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2027880700 281 IEPV--LVPELNSH----------------------------------ARGKNGFGSSG 303
Cdd:PHA03127 263 EEPLewLPTELNDRepfpttpraappapmahrlrwrfvadfaavapssARGDRGFGSTG 321
|
|
| dut |
PHA01707 |
2'-deoxyuridine 5'-triphosphatase |
211-287 |
4.08e-05 |
|
2'-deoxyuridine 5'-triphosphatase
Pssm-ID: 107053 Cd Length: 158 Bit Score: 43.00 E-value: 4.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2027880700 211 VQLPDWSWGFLVGRSsTLRKKGLLVNPGIIDAGYRGELFSGVQNmTSKPVHVEAGERIAQLIIigngTRQIEPVLVP 287
Cdd:PHA01707 71 IKLPNDIIAFCNLRS-TFARKGLLIPPTIVDAGFEGQLTIELVG-SSIPVKLKSGERFLHLIF----ARTLTPVEKP 141
|
|
| PHA03131 |
PHA03131 |
dUTPase; Provisional |
181-274 |
3.51e-04 |
|
dUTPase; Provisional
Pssm-ID: 222996 [Multi-domain] Cd Length: 286 Bit Score: 41.52 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 181 YSDDAGLDLFVTEDTWVP---ANGF-------VDIRSHIKVqlpdwswgfLVGRSStLRKKGLLVNPgiidAGYRGELFS 250
Cdd:PHA03131 129 YPDDAGFDVSLPQDLVIFpttTFTFtlslccpPISPHFVPV---------IFGRSG-LASKGLTVKP----TKWRRSGLQ 194
|
90 100
....*....|....*....|....*
gi 2027880700 251 -GVQNMTSKPVHVEAGERIAQLIII 274
Cdd:PHA03131 195 lKLYNYTDETIFLPAGSRICQVVFM 219
|
|
| PHA03129 |
PHA03129 |
dUTPase; Provisional |
178-274 |
3.03e-03 |
|
dUTPase; Provisional
Pssm-ID: 222994 [Multi-domain] Cd Length: 436 Bit Score: 39.09 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027880700 178 TRAYSDDAGLDLFVTEDTWVPANGFVDIRSHIKVQLPDWS---WGFlvGRSStLRKKGLLVNPGIIDAGyrGELFSGVQN 254
Cdd:PHA03129 281 NPKRLEDAGYDIPAPRDIELEPLSSTTIKIQQRYNCKDSSvipCIF--GRSS-MNLRGLIVLPSRWLPN--SWLTLTICN 355
|
90 100
....*....|....*....|
gi 2027880700 255 MTSKPVHVEAGERIAQLIII 274
Cdd:PHA03129 356 LTEKTVFIKAGDRIAQLLLV 375
|
|
| PRK02253 |
PRK02253 |
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional |
211-274 |
8.78e-03 |
|
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
Pssm-ID: 179395 Cd Length: 167 Bit Score: 36.47 E-value: 8.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2027880700 211 VQLPDWSWGFLVGRSSTLRKkGLLVNPGIIDAGY--RGELFSGVQNmtSKPVHVEAGERIAQLIII 274
Cdd:PRK02253 87 VNIPEDHVGFAYPRSSLLRN-GCTLETAVWDAGYegRGEGLLVVHN--PHGIRLERGARIAQLVFA 149
|
|
|