NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|18653860|ref|NP_570794|]
View 

dUTPase [Macacine gammaherpesvirus 5]

Protein Classification

PHA03131 family protein( domain architecture ID 11476167)

PHA03131 family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PHA03131 PHA03131
dUTPase; Provisional
 2-290 3.03e-152

dUTPase; Provisional


:

Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 427.10  E-value: 3.03e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860    2 AEVTAHTVPYAFDSCKFEIIPKNNSSRIALRNKFPVVVKPGEPLVVPLGLKIIRAPQCAFFLSGAPTDEVYYHTGLIDQG 81
Cdd:PHA03131   1 RMAQRPEVYYAFEPSKFLITSPAEESRLTLVNKTPILVRPGEPTVVPLGLYIRRPPGFAFILWGSTSKNVTCHTGLIDPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860   82 YRGEIKLIVLNKTKQVVTLYRGEVNVSLIAFMYASPGPLKCPILNLPHYSLDAGFDVTSPHAMTIPPTDRTPFTLSLYYk 161
Cdd:PHA03131  81 YRGELKLILLNKTKYNVTLRPGELKVSLLAFTYATPILTDDSLLNPPQYPDDAGFDVSLPQDLVIFPTTTFTFTLSLCC- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860  162 sPQLSTPHVPLIVGRSGLATKGLTVDATKWTQSLVHLRFYNFTKEPIDIPANSRICQVVFIHEDHVPSGWNILRSRVQLG 241
Cdd:PHA03131 160 -PPISPHFVPVIFGRSGLASKGLTVKPTKWRRSGLQLKLYNYTDETIFLPAGSRICQVVFMHKDHLPSFFNPLLSARCLG 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 18653860  242 STLQISWAKIRFTDVATLPKTHPLNSRHTQsQTEPETARGAKGLGSSGL 290
Cdd:PHA03131 239 PRILFRWARVSFEDIPKDPCTSSKTLRQSE-DGDSDPSRGTKGFGSSGL 286
 
Name Accession Description Interval E-value
PHA03131 PHA03131
dUTPase; Provisional
 2-290 3.03e-152

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 427.10  E-value: 3.03e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860    2 AEVTAHTVPYAFDSCKFEIIPKNNSSRIALRNKFPVVVKPGEPLVVPLGLKIIRAPQCAFFLSGAPTDEVYYHTGLIDQG 81
Cdd:PHA03131   1 RMAQRPEVYYAFEPSKFLITSPAEESRLTLVNKTPILVRPGEPTVVPLGLYIRRPPGFAFILWGSTSKNVTCHTGLIDPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860   82 YRGEIKLIVLNKTKQVVTLYRGEVNVSLIAFMYASPGPLKCPILNLPHYSLDAGFDVTSPHAMTIPPTDRTPFTLSLYYk 161
Cdd:PHA03131  81 YRGELKLILLNKTKYNVTLRPGELKVSLLAFTYATPILTDDSLLNPPQYPDDAGFDVSLPQDLVIFPTTTFTFTLSLCC- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860  162 sPQLSTPHVPLIVGRSGLATKGLTVDATKWTQSLVHLRFYNFTKEPIDIPANSRICQVVFIHEDHVPSGWNILRSRVQLG 241
Cdd:PHA03131 160 -PPISPHFVPVIFGRSGLASKGLTVKPTKWRRSGLQLKLYNYTDETIFLPAGSRICQVVFMHKDHLPSFFNPLLSARCLG 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 18653860  242 STLQISWAKIRFTDVATLPKTHPLNSRHTQsQTEPETARGAKGLGSSGL 290
Cdd:PHA03131 239 PRILFRWARVSFEDIPKDPCTSSKTLRQSE-DGDSDPSRGTKGFGSSGL 286
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 124-228 5.23e-19

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 80.80  E-value: 5.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860   124 ILNLPHYSLDAGFDVTSPHAMTIPPTDRTPFTLSLYYKSPQlstPHVPLIVGRSGLATKGLTV---DATKWTQSLVHLRF 200
Cdd:pfam00692   4 EIPTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPD---GTYGRIFPRSGLAAKGLIVvpgVIDSDYRGEVKVVL 80

                          90       100
                  ....*....|....*....|....*...
gi 18653860   201 YNFTKEPIDIPANSRICQVVFIHEDHVP 228
Cdd:pfam00692  81 FNLGKSDFTIKKGDRIAQLIFEPILHPE 108
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 134-221 1.85e-09

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: 53.65  E-value: 1.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860 134 AGFDVTSPH---AMTIPPTDRTPFTLSLYYKSPQlstPHVPLIVGRSGLATKGLTVDATKWTQS----LVHLRFYNFTKE 206
Cdd:cd07557   1 AGYDLRLGEdfeGIVLPPGETVLVPTGEAIELPE---GYVGLVFPRSSLARKGITVHNAGVIDPgyrgEITLELYNLGPE 77

                        90
                ....*....|....*
gi 18653860 207 PIDIPANSRICQVVF 221
Cdd:cd07557  78 PVVIKKGDRIAQLVF 92
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 36-104 6.16e-08

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: 50.79  E-value: 6.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860  36 PVVVKPGEPLVVPLGLKIIRAPQCAFFL---SG-----------APtdevyyhtGLIDQGYRGEIKLIVLNKTKQVVTLY 101
Cdd:COG0756  33 PVTLKPGERALVPTGLAIALPPGYEAQVrprSGlalkhgitllnSP--------GTIDSDYRGEIKVILINLGDEPFTIE 104


                ...
gi 18653860 102 RGE 104
Cdd:COG0756 105 RGD 107
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 20-104 1.79e-05

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: 43.76  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860    20 IIPKNNSSRIA---LRNKFPVVVKPGEPLVVPLGLKIIRAPQCAFFL---SGAPT---DEVYYHTGLIDQGYRGEIKLIV 90
Cdd:TIGR00576  12 PLPTYATEGAAgydLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVaprSGLALkhgVTIDNSPGVIDADYRGEIKVIL 91

                          90
                  ....*....|....
gi 18653860    91 LNKTKQVVTLYRGE 104
Cdd:TIGR00576  92 INLGKEDFTVKKGD 105
 
Name Accession Description Interval E-value
PHA03131 PHA03131
dUTPase; Provisional
 2-290 3.03e-152

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 427.10  E-value: 3.03e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860    2 AEVTAHTVPYAFDSCKFEIIPKNNSSRIALRNKFPVVVKPGEPLVVPLGLKIIRAPQCAFFLSGAPTDEVYYHTGLIDQG 81
Cdd:PHA03131   1 RMAQRPEVYYAFEPSKFLITSPAEESRLTLVNKTPILVRPGEPTVVPLGLYIRRPPGFAFILWGSTSKNVTCHTGLIDPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860   82 YRGEIKLIVLNKTKQVVTLYRGEVNVSLIAFMYASPGPLKCPILNLPHYSLDAGFDVTSPHAMTIPPTDRTPFTLSLYYk 161
Cdd:PHA03131  81 YRGELKLILLNKTKYNVTLRPGELKVSLLAFTYATPILTDDSLLNPPQYPDDAGFDVSLPQDLVIFPTTTFTFTLSLCC- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860  162 sPQLSTPHVPLIVGRSGLATKGLTVDATKWTQSLVHLRFYNFTKEPIDIPANSRICQVVFIHEDHVPSGWNILRSRVQLG 241
Cdd:PHA03131 160 -PPISPHFVPVIFGRSGLASKGLTVKPTKWRRSGLQLKLYNYTDETIFLPAGSRICQVVFMHKDHLPSFFNPLLSARCLG 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 18653860  242 STLQISWAKIRFTDVATLPKTHPLNSRHTQsQTEPETARGAKGLGSSGL 290
Cdd:PHA03131 239 PRILFRWARVSFEDIPKDPCTSSKTLRQSE-DGDSDPSRGTKGFGSSGL 286
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 124-228 5.23e-19

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 80.80  E-value: 5.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860   124 ILNLPHYSLDAGFDVTSPHAMTIPPTDRTPFTLSLYYKSPQlstPHVPLIVGRSGLATKGLTV---DATKWTQSLVHLRF 200
Cdd:pfam00692   4 EIPTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPD---GTYGRIFPRSGLAAKGLIVvpgVIDSDYRGEVKVVL 80

                          90       100
                  ....*....|....*....|....*...
gi 18653860   201 YNFTKEPIDIPANSRICQVVFIHEDHVP 228
Cdd:pfam00692  81 FNLGKSDFTIKKGDRIAQLIFEPILHPE 108
PHA03127 PHA03127
dUTPase; Provisional
 45-290 7.55e-15

dUTPase; Provisional


Pssm-ID: 222993 [Multi-domain]  Cd Length: 322  Bit Score: 73.49  E-value: 7.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860   45 LVVPLGLKIIRAPQCAfflSGAPTDEVYYHTGLIDQGYRGEIKLIVLNK----------TKQVVTLYRGEVNVSLIAF-- 112
Cdd:PHA03127  72 AAAPGGYAILMSQMCS---GQTPSRPPAVAVGIVDSGYRGILRAIVWAPpcietipeagLALRLTLARLAKTTPRLAAcd 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860  113 --MYASPG-PLKCPILNL--PHYSLDAGFDVTSPHAMTIPPTDRTPFTLSLYYKSPqlSTPHVPLIVGRSGLATKGLTVD 187
Cdd:PHA03127 149 dtARAGQGaGVEVPFFETfaPKRDEDAGYDIAMPYTAVLAPGENLHVRLPVAYAAG--AHAAAPYVFGRSSLNLRGIVVL 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860  188 ATKWtQSLVHLRFY--NFTKEPIDIPANSRICQVVFIHEdhvPSGW--NILRSRVQLGSTLQISwakirftdvATLPKTH 263
Cdd:PHA03127 227 PTAW-PPGEPCRFVirNVTQEPVVAAAGQRVAQLLLLEE---PLEWlpTELNDREPFPTTPRAA---------PPAPMAH 293

                        250       260
                 ....*....|....*....|....*....
gi 18653860  264 PLNSRHTQ--SQTEPETARGAKGLGSSGL 290
Cdd:PHA03127 294 RLRWRFVAdfAAVAPSSARGDRGFGSTGL 322
PHA03126 PHA03126
dUTPase; Provisional
 67-290 5.07e-11

dUTPase; Provisional


Pssm-ID: 165398 [Multi-domain]  Cd Length: 326  Bit Score: 62.35  E-value: 5.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860   67 PTDEVYYHT--GLIDQGYRGEIKLI-------------VLNKTKQVVTLYRGEVNVSLIAfmyaSPGPLKCPILNL---- 127
Cdd:PHA03126  94 PGNSAKYYTayGIVDSGYRGVVKAVqfapgvntsvppgQMSLGLVLVKLATETIHVTSIG----STEDGRSSEANLfydy 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860  128 --PHYSLDAGFDVTSPHAMTIPPTDRTPFTLSLYYKSpqlSTPHV-PLIVGRSGLATKGLTVDATKWTQSLVHLRF-YNF 203
Cdd:PHA03126 170 faPKRVEDAGYDISAPTDATIEPDESHFVDLPIVFAS---SNPAVtPCIFGRSSMNRRGLIVLPTRWVAGRTCCFFiLNV 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860  204 TKEPIDIPANSRICQVVF---IHEDHVPSGWNilrsrvqlgstLQISWAKIRFTDVATLPKThPLNSRHTQS--QTEPET 278
Cdd:PHA03126 247 NKYPVSITKGQRVAQLLLtedIDDALIPTTVN-----------YDTPFPTYSPTGATKAPQS-PVLWKFTTDfdREAPSS 314

                        250
                 ....*....|..
gi 18653860  279 ARGAKGLGSSGL 290
Cdd:PHA03126 315 LRADGGFGSTGL 326
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 134-221 1.85e-09

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: 53.65  E-value: 1.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860 134 AGFDVTSPH---AMTIPPTDRTPFTLSLYYKSPQlstPHVPLIVGRSGLATKGLTVDATKWTQS----LVHLRFYNFTKE 206
Cdd:cd07557   1 AGYDLRLGEdfeGIVLPPGETVLVPTGEAIELPE---GYVGLVFPRSSLARKGITVHNAGVIDPgyrgEITLELYNLGPE 77

                        90
                ....*....|....*
gi 18653860 207 PIDIPANSRICQVVF 221
Cdd:cd07557  78 PVVIKKGDRIAQLVF 92
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 36-104 6.16e-08

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: 50.79  E-value: 6.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860  36 PVVVKPGEPLVVPLGLKIIRAPQCAFFL---SG-----------APtdevyyhtGLIDQGYRGEIKLIVLNKTKQVVTLY 101
Cdd:COG0756  33 PVTLKPGERALVPTGLAIALPPGYEAQVrprSGlalkhgitllnSP--------GTIDSDYRGEIKVILINLGDEPFTIE 104


                ...
gi 18653860 102 RGE 104
Cdd:COG0756 105 RGD 107
PHA03129 PHA03129
dUTPase; Provisional
 128-225 9.12e-08

dUTPase; Provisional


Pssm-ID: 222994 [Multi-domain]  Cd Length: 436  Bit Score: 52.95  E-value: 9.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860  128 PHYSLDAGFDVTSPHAMTIPPTDRTPFTLSLYYKSPQLSTphVPLIVGRSGLATKGLTVDATKWTQ-SLVHLRFYNFTKE 206
Cdd:PHA03129 282 PKRLEDAGYDIPAPRDIELEPLSSTTIKIQQRYNCKDSSV--IPCIFGRSSMNLRGLIVLPSRWLPnSWLTLTICNLTEK 359

                         90
                 ....*....|....*....
gi 18653860  207 PIDIPANSRICQVVFIHED 225
Cdd:PHA03129 360 TVFIKAGDRIAQLLLVDQD 378
Dcd COG0717
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ...
 169-230 4.35e-07

dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway/BioSystem: Thymidylate biosynthesis


Pssm-ID: 440481  Cd Length: 180  Bit Score: 49.05  E-value: 4.35e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18653860 169 HVPLIVGRSGLATKGLTVDAT----------KWTqslvhLRFYNFTKEPIDIPANSRICQVVFIHEDHVPSG 230
Cdd:COG0717  92 LVAFLEGRSSLARLGLFVHTTagvidpgfegRIT-----LELSNTGPLPIKLYPGMRIAQLVFFRLSGPAER 158
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 36-104 1.11e-06

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: 45.95  E-value: 1.11e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18653860  36 PVVVKPGEPLVVPLGLKIIRAPQCAFFL---SGAPTDEVYYHT-GLIDQGYRGEIKLIVLNKTKQVVTLYRGE 104
Cdd:cd07557  13 GIVLPPGETVLVPTGEAIELPEGYVGLVfprSSLARKGITVHNaGVIDPGYRGEITLELYNLGPEPVVIKKGD 85
dut PRK00601
dUTP diphosphatase;
36-104 1.72e-06

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 46.70  E-value: 1.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860   36 PVVVKPGEPLVVPLGLKIIRAPQ-CAFFL--SG-----------APtdevyyhtGLIDQGYRGEIKLIVLNKTKQVVTLY 101
Cdd:PRK00601  39 PVTLAPGERALVPTGLAIHIPDGyEAQILprSGlahkhgivlgnLP--------GTIDSDYRGELKVSLWNRGQEPFTIE 110


                 ...
gi 18653860  102 RGE 104
Cdd:PRK00601 111 PGE 113
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 20-104 1.79e-05

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: 43.76  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860    20 IIPKNNSSRIA---LRNKFPVVVKPGEPLVVPLGLKIIRAPQCAFFL---SGAPT---DEVYYHTGLIDQGYRGEIKLIV 90
Cdd:TIGR00576  12 PLPTYATEGAAgydLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVaprSGLALkhgVTIDNSPGVIDADYRGEIKVIL 91

                          90
                  ....*....|....
gi 18653860    91 LNKTKQVVTLYRGE 104
Cdd:TIGR00576  92 INLGKEDFTVKKGD 105
dCTP_deam TIGR02274
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ...
 175-222 3.67e-05

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: 43.46  E-value: 3.67e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 18653860   175 GRSGLATKGLTVDATK------WTQSLVhLRFYNFTKEPIDIPANSRICQVVFI 222
Cdd:TIGR02274  99 GRSSLARLGLFIHVTAgridpgFEGNIT-LELFNAGKLPVKLRPGMRIAQLVFE 151
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 36-104 5.45e-05

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 41.89  E-value: 5.45e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18653860    36 PVVVKPGEPLVVPLGLKIIRAPQCAFFL---SGAPTDEVYYHTGLIDQGYRGEIKLIVLNKTKQVVTLYRGE 104
Cdd:pfam00692  23 DLTVKPGGTVLVPTDISIPLPDGTYGRIfprSGLAAKGLIVVPGVIDSDYRGEVKVVLFNLGKSDFTIKKGD 94
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 38-112 2.50e-04

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 40.49  E-value: 2.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860   38 VVKPGEPLVVPLGLKIIRAPQCAFFLSGAPTDEVYY--------------HTGLIDQGYRGEIKLIVLNKTKQVVTLYRG 103
Cdd:PTZ00143  38 TIKPGETAFIKLGIKAAAFQKDEDGSDGKNVSWLLFprssisktplrlanSIGLIDAGYRGELIAAVDNIKDEPYTIKKG 117


                 ....*....
gi 18653860  104 EVNVSLIAF 112
Cdd:PTZ00143 118 DRLVQLVSF 126
PHA03130 PHA03130
dUTPase; Provisional
 26-228 3.66e-04

dUTPase; Provisional


Pssm-ID: 222995 [Multi-domain]  Cd Length: 368  Bit Score: 41.42  E-value: 3.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860   26 SSRIALRNKFPVVVKPGEPLV-------VPLGLK---------IIRAPQcaffLSGAPtdevyYHT--GLIDQGYRGEIK 87
Cdd:PHA03130  34 SVRLSLANRREVAFTPAGGGAsgwavgrVPLDLRvamptdfcaVVHAPP----TAGAP-----YRValGLIDSGYRGTVQ 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860   88 LIVL--NKTKQVVTlyrGEVNVSLI--------------AFMYASPGPLKCP---------------------------- 123
Cdd:PHA03130 105 AVVLapGETRRFAP---GELRVDLTflrvsgsplgltepAFLCSFPGLKRPRrtepgaphanpwlgralaargarrrggs 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860  124 ----------------------ILNLPHYSLDAGFDVTSPHAMTIPPTDRTPFTLSLYYKSPQlSTPHVPLIVGRSGLAT 181
Cdd:PHA03130 182 vtyagelreeapgehgdgaveaPAFLPKRAEDAGIDIVVHKRVEVPAGGTVVIQPSLRVLLAA-GGPEAYYVLGRSSLNA 260

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 18653860  182 KGLTVDATKWTQSLV-HLRFYNFTKEPIDIPANSRICQVVFIHEDHVP 228
Cdd:PHA03130 261 RGVLVTPTRWLPGRQcAFSVHNITGAPVTLEAGSKVAQLLVAGSDALP 308
PHA03123 PHA03123
dUTPase; Provisional
 133-226 1.04e-03

dUTPase; Provisional


Pssm-ID: 165395 [Multi-domain]  Cd Length: 402  Bit Score: 40.36  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860  133 DAGFDVTSPHAMTIPPTD----RTPFTLSLYYKSPQLSTphvpLIVGRSGLATKGLTVDATKWTQ-SLVHLRFYNFTKEP 207
Cdd:PHA03123 244 DAGYDICAPFEITLKANEfikiTLPFIQDLDLNHPNIDA----YIFGRSSKNRIGIIVCPTAWIAgEHCEFYIFNATGDD 319

                         90
                 ....*....|....*....
gi 18653860  208 IDIPANSRICQVVFIheDH 226
Cdd:PHA03123 320 IIIKPGDKIAQVLLI--DH 336
PHA03124 PHA03124
dUTPase; Provisional
 133-289 2.30e-03

dUTPase; Provisional


Pssm-ID: 165396 [Multi-domain]  Cd Length: 418  Bit Score: 39.16  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860  133 DAGFDVTSPHAMTIPPTDRTPFTLslyyksPQ---LSTPHVPLIVGRSGLATKGLTVDATKWTQS-LVHLRFYNFTKEPI 208
Cdd:PHA03124 290 DAGYDIRAPEDCTILPGGSTRIIL------PQklaCGKFRAAFILGRSSMNLKGLLVDPEHVQDDdWISFNITNIRDAAA 363

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18653860  209 DIPANSRICQVVfihedhvpsgwnILRSRVQ-LGSTLQISWaKIrftdvatlpkthpLNSrhTQSQTEPETARGAKGLGS 287
Cdd:PHA03124 364 FFHAGDRIAQLI------------ALEDKLEfLGEPDALPW-KI-------------VNS--VQDEKKNLSSRGDGGFGS 415


                 ..
gi 18653860  288 SG 289
Cdd:PHA03124 416 SG 417
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH