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Conserved domains on  [gi|499267341|ref|WP_010964734|]
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MULTISPECIES: dUTP diphosphatase [Clostridium]

Protein Classification

dUTP diphosphatase( domain architecture ID 10786453)

dUTP diphosphatase is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA

EC:  3.6.1.23
SCOP:  4002970

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
3-142 7.00e-83

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: 239.53  E-value: 7.00e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499267341   3 NLKIKKIDDAAILPECAHEGDAGLDLFSV--EEKVIKAGESALIGTGIQMELPPETEAQVRPRSGLALKHSITVLNSPGT 80
Cdd:COG0756    1 KVKIKRLDEDAPLPAYATPGSAGLDLRAAldEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLLNSPGT 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499267341  81 IDEGYRGEVKIILINHGKEDFKVEKSMKIAQMVIKPVLKVKVEEVKELSSSDRGTGGFGSTG 142
Cdd:COG0756   81 IDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTG 142
 
Name Accession Description Interval E-value
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
3-142 7.00e-83

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: 239.53  E-value: 7.00e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499267341   3 NLKIKKIDDAAILPECAHEGDAGLDLFSV--EEKVIKAGESALIGTGIQMELPPETEAQVRPRSGLALKHSITVLNSPGT 80
Cdd:COG0756    1 KVKIKRLDEDAPLPAYATPGSAGLDLRAAldEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLLNSPGT 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499267341  81 IDEGYRGEVKIILINHGKEDFKVEKSMKIAQMVIKPVLKVKVEEVKELSSSDRGTGGFGSTG 142
Cdd:COG0756   81 IDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTG 142
dut PRK00601
dUTP diphosphatase;
1-144 4.57e-79

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 230.44  E-value: 4.57e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499267341   1 MVNLKIKKIDDAAILPECAHEGDAGLDLFSVEEK--VIKAGESALIGTGIQMELPPETEAQVRPRSGLALKHSITVLNSP 78
Cdd:PRK00601   5 DVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEpvTLAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIVLGNLP 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499267341  79 GTIDEGYRGEVKIILINHGKEDFKVEKSMKIAQMVIKPVLKVKVEEVKELSSSDRGTGGFGSTGLK 144
Cdd:PRK00601  85 GTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
3-142 4.79e-70

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: 207.09  E-value: 4.79e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499267341    3 NLKIKKIDDAAILPECAHEGDAGLDLFSVEEKVIKAGESALIGTGIQMELPPETEAQVRPRSGLALKHSITVLNSPGTID 82
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGVTIDNSPGVID 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499267341   83 EGYRGEVKIILINHGKEDFKVEKSMKIAQMVIKPVLK-VKVEEVKELSSSDRGTGGFGSTG 142
Cdd:TIGR00576  81 ADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTG 141
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
11-142 2.78e-40

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 131.26  E-value: 2.78e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499267341   11 DAAILPECAHEGDAGLDLFSVEEKVIKAGESALIGTGIQMELPPETEAQVRPRSGLALKHSITVlnsPGTIDEGYRGEVK 90
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAKGLIVV---PGVIDSDYRGEVK 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 499267341   91 IILINHGKEDFKVEKSMKIAQMVIKPVLKVKVEEVKELSSSDRGTGGFGSTG 142
Cdd:pfam00692  78 VVLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
24-114 3.50e-33

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: 112.20  E-value: 3.50e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499267341  24 AGLDLFSVEEK---VIKAGESALIGTGIQMELPPETEAQVRPRSGLALKHsITVLNsPGTIDEGYRGEVKIILINHGKED 100
Cdd:cd07557    1 AGYDLRLGEDFegiVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLARKG-ITVHN-AGVIDPGYRGEITLELYNLGPEP 78
                         90
                 ....*....|....
gi 499267341 101 FKVEKSMKIAQMVI 114
Cdd:cd07557   79 VVIKKGDRIAQLVF 92
 
Name Accession Description Interval E-value
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
3-142 7.00e-83

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: 239.53  E-value: 7.00e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499267341   3 NLKIKKIDDAAILPECAHEGDAGLDLFSV--EEKVIKAGESALIGTGIQMELPPETEAQVRPRSGLALKHSITVLNSPGT 80
Cdd:COG0756    1 KVKIKRLDEDAPLPAYATPGSAGLDLRAAldEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLLNSPGT 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499267341  81 IDEGYRGEVKIILINHGKEDFKVEKSMKIAQMVIKPVLKVKVEEVKELSSSDRGTGGFGSTG 142
Cdd:COG0756   81 IDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTG 142
dut PRK00601
dUTP diphosphatase;
1-144 4.57e-79

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 230.44  E-value: 4.57e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499267341   1 MVNLKIKKIDDAAILPECAHEGDAGLDLFSVEEK--VIKAGESALIGTGIQMELPPETEAQVRPRSGLALKHSITVLNSP 78
Cdd:PRK00601   5 DVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEpvTLAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIVLGNLP 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499267341  79 GTIDEGYRGEVKIILINHGKEDFKVEKSMKIAQMVIKPVLKVKVEEVKELSSSDRGTGGFGSTGLK 144
Cdd:PRK00601  85 GTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGRH 150
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
3-142 4.79e-70

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: 207.09  E-value: 4.79e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499267341    3 NLKIKKIDDAAILPECAHEGDAGLDLFSVEEKVIKAGESALIGTGIQMELPPETEAQVRPRSGLALKHSITVLNSPGTID 82
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGVTIDNSPGVID 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499267341   83 EGYRGEVKIILINHGKEDFKVEKSMKIAQMVIKPVLK-VKVEEVKELSSSDRGTGGFGSTG 142
Cdd:TIGR00576  81 ADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTG 141
PLN02547 PLN02547
dUTP pyrophosphatase
4-145 4.24e-45

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 144.55  E-value: 4.24e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499267341   4 LKIKKIDDAAILPECAHEGDAGLDLFSVEEKVIKAGESALIGTGIQMELPPETEAQVRPRSGLALKHSITVlnSPGTIDE 83
Cdd:PLN02547  17 LRVKKLSEKATLPSRGSALAAGYDLSSAYDTVVPARGKALVPTDLSIAIPEGTYARIAPRSGLAWKHSIDV--GAGVIDA 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499267341  84 GYRGEVKIILINHGKEDFKVEKSMKIAQMVIKPVLKVKVEEVKELSSSDRGTGGFGSTGLKK 145
Cdd:PLN02547  95 DYRGPVGVILFNHSDVDFEVKVGDRIAQLILEKIVTPEVVEVEDLDATVRGAGGFGSTGVAL 156
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
11-142 2.78e-40

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 131.26  E-value: 2.78e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499267341   11 DAAILPECAHEGDAGLDLFSVEEKVIKAGESALIGTGIQMELPPETEAQVRPRSGLALKHSITVlnsPGTIDEGYRGEVK 90
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAKGLIVV---PGVIDSDYRGEVK 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 499267341   91 IILINHGKEDFKVEKSMKIAQMVIKPVLKVKVEEVKELSSSDRGTGGFGSTG 142
Cdd:pfam00692  78 VVLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
PHA02703 PHA02703
ORF007 dUTPase; Provisional
4-144 1.61e-34

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 118.16  E-value: 1.61e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499267341   4 LKIKKIDDAAILPECAHEGDAGLDLFSVEEKVIKAGESALIGTGIQMELPPETEAQVRPRSGLALKHSITVlnSPGTIDE 83
Cdd:PHA02703  14 LRVVRLSPNATIPTRGSPGAAGLDLCSACDCIVPAGCRCVVFTDLLIKLPDGCYGRIAPRSGLAVKHFIDV--GAGVIDA 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499267341  84 GYRGEVKIILINHGKEDFKVEKSMKIAQMVIKPVLKVKVEEVKELSSSDRGTGGFGSTGLK 144
Cdd:PHA02703  92 DYRGNVGVVLFNFGHNDFEVKKGDRIAQLICERAAFPAVEEVACLDDTDRGAGGFGSTGSG 152
PHA03094 PHA03094
dUTPase; Provisional
4-144 2.55e-34

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 116.79  E-value: 2.55e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499267341   4 LKIKKIDDAAILPECAHEGDAGLDLFSVEEKVIKAGESALIGTGIQMELPPETEAQVRPRSGLALKHSITVlnSPGTIDE 83
Cdd:PHA03094   6 VRCVKLSNFAKIPTRSSPKSAGYDLYSAYDYTVPPKERILVKTDISLSIPKFCYGRIAPRSGLSLNYGIDI--GGGVIDE 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499267341  84 GYRGEVKIILINHGKEDFKVEKSMKIAQMVIKPVLKVKVEEVKELSSSDRGTGGFGSTGLK 144
Cdd:PHA03094  84 DYRGNIGVIFINNGKCTFNIKTGDRIAQIIFERIEYPELKEVQSLDSTDRGDQGFGSSGLR 144
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
24-114 3.50e-33

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: 112.20  E-value: 3.50e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499267341  24 AGLDLFSVEEK---VIKAGESALIGTGIQMELPPETEAQVRPRSGLALKHsITVLNsPGTIDEGYRGEVKIILINHGKED 100
Cdd:cd07557    1 AGYDLRLGEDFegiVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLARKG-ITVHN-AGVIDPGYRGEITLELYNLGPEP 78
                         90
                 ....*....|....
gi 499267341 101 FKVEKSMKIAQMVI 114
Cdd:cd07557   79 VVIKKGDRIAQLVF 92
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
20-142 2.05e-24

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 91.72  E-value: 2.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499267341  20 HEGDAGLDLFSVEEKVIKAGESALIGTGI-----QMELPPETEAQVR----PRSGLAlKHSITVLNSPGTIDEGYRGEVK 90
Cdd:PTZ00143  23 HEGDSGLDLFIVKDQTIKPGETAFIKLGIkaaafQKDEDGSDGKNVSwllfPRSSIS-KTPLRLANSIGLIDAGYRGELI 101
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499267341  91 IILINHGKEDFKVEKSMKIAQMVIKPVLKVKVEEVKELSSSDRGTGGFGSTG 142
Cdd:PTZ00143 102 AAVDNIKDEPYTIKKGDRLVQLVSFDGEPITFELVDELDETTRGEGGFGSTG 153
dut PRK13956
dUTP diphosphatase;
6-142 3.21e-10

dUTP diphosphatase;


Pssm-ID: 184417 [Multi-domain]  Cd Length: 147  Bit Score: 54.80  E-value: 3.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499267341   6 IKKIDDAAILP--ECAHEgdAGLDLFSVEEKVIKAGESALIGTGIQMELPPETEAQVRPRSGLALKHSITVLNSPGTIDE 83
Cdd:PRK13956   9 VSSFTNENLLPkrETAHA--AGYDLKVAERTVIAPGEIKLVPTGVKAYMQPGEVLYLYDRSSNPRKKGLVLINSVGVIDG 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499267341  84 GY------RGEVKIILINHGKEDFKVEKSMKIAQMVIKPVLKVKVEEVKELSssdrgTGGFGSTG 142
Cdd:PRK13956  87 DYygnpanEGHIFAQMKNITDQEVVLEVGERIVQGVFMPFLIADGDQADGER-----TGGFGSTG 146
Dcd COG0717
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ...
32-113 2.79e-08

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


Pssm-ID: 440481  Cd Length: 180  Bit Score: 50.21  E-value: 2.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499267341  32 EEKVIKAGESALIGTGIQMELPPETEAQVRPRSGLAlKHSITVLNSPGTIDEGYRGEVKIILINHGKEDFKVEKSMKIAQ 111
Cdd:COG0717   68 DGFILPPGEFYLARTLEYVRLPDDLVAFLEGRSSLA-RLGLFVHTTAGVIDPGFEGRITLELSNTGPLPIKLYPGMRIAQ 146

                 ..
gi 499267341 112 MV 113
Cdd:COG0717  147 LV 148
PRK02253 PRK02253
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
51-113 3.41e-03

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 179395  Cd Length: 167  Bit Score: 35.70  E-value: 3.41e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499267341  51 ELPPETEAQVRPRSGLaLKHSITVLNSpgTIDEGYRGEVKIILINHGKEDFKVEKSMKIAQMV 113
Cdd:PRK02253  88 NIPEDHVGFAYPRSSL-LRNGCTLETA--VWDAGYEGRGEGLLVVHNPHGIRLERGARIAQLV 147
PHA03131 PHA03131
dUTPase; Provisional
35-95 3.88e-03

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 36.12  E-value: 3.88e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499267341  35 VIKAGESALIGTGIQMElPPETEAQVrprsgLALKHSITVLNSPGTIDEGYRGEVKIILIN 95
Cdd:PHA03131  37 LVRPGEPTVVPLGLYIR-RPPGFAFI-----LWGSTSKNVTCHTGLIDPGYRGELKLILLN 91
 
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.
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