NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|499284122|ref|WP_010977182|]
View 

MULTISPECIES: dUTP diphosphatase [spotted fever group]

Protein Classification

dUTP diphosphatase( domain architecture ID 10792031)

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
Gene Ontology:  GO:0046872|GO:0004170

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
1-148 5.60e-89

dUTP diphosphatase;


:

Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 255.47  E-value: 5.60e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499284122   1 MTITQVKIKKLENFSG-SLPEYATEHSAGMDLIAANEQPITIKAAAIQLIPTGIAIALPDSFEAQIRPRSGLAVKHGITV 79
Cdd:PRK00601   1 MKKIDVKILDPRLGKEfPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIVL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499284122  80 ANSPGTIDADYRGEIKVILINLGKEDFIIEKGMRIAQMIIAKYERILWEESSSLMETMRGSGGFGSTGV 148
Cdd:PRK00601  81 GNLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGR 149
 
Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
1-148 5.60e-89

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 255.47  E-value: 5.60e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499284122   1 MTITQVKIKKLENFSG-SLPEYATEHSAGMDLIAANEQPITIKAAAIQLIPTGIAIALPDSFEAQIRPRSGLAVKHGITV 79
Cdd:PRK00601   1 MKKIDVKILDPRLGKEfPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIVL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499284122  80 ANSPGTIDADYRGEIKVILINLGKEDFIIEKGMRIAQMIIAKYERILWEESSSLMETMRGSGGFGSTGV 148
Cdd:PRK00601  81 GNLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGR 149
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 5-148 4.21e-87

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: 250.32  E-value: 4.21e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499284122   5 QVKIKKLENfSGSLPEYATEHSAGMDLIAANEQPITIKAAAIQLIPTGIAIALPDSFEAQIRPRSGLAVKHGITVANSPG 84
Cdd:COG0756    1 KVKIKRLDE-DAPLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLLNSPG 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499284122  85 TIDADYRGEIKVILINLGKEDFIIEKGMRIAQMIIAKYERILWEESSSLMETMRGSGGFGSTGV 148
Cdd:COG0756   80 TIDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTGR 143
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 6-148 1.66e-68

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: 203.62  E-value: 1.66e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499284122    6 VKIKKLENfSGSLPEYATEHSAGMDLIAAneQPITIKAAAIQLIPTGIAIALPDSFEAQIRPRSGLAVKHGITVANSPGT 85
Cdd:TIGR00576   2 LKFVKLSP-NAPLPTYATEGAAGYDLRAA--EDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGVTIDNSPGV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499284122   86 IDADYRGEIKVILINLGKEDFIIEKGMRIAQMIIAKYER-ILWEESSSLMETMRGSGGFGSTGV 148
Cdd:TIGR00576  79 IDADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 16-147 4.04e-40

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 131.26  E-value: 4.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499284122   16 GSLPEYATEHSAGMDLIAAneQPITIKAAAIQLIPTGIAIALPDSFEAQIRPRSGLAVKHGITVansPGTIDADYRGEIK 95
Cdd:pfam00692   3 AEIPTPGSPGDAGYDLYAP--YDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAKGLIVV---PGVIDSDYRGEVK 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 499284122   96 VILINLGKEDFIIEKGMRIAQMIIAKYERILWEESSSLMETMRGSGGFGSTG 147
Cdd:pfam00692  78 VVLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 27-119 7.15e-35

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: 116.44  E-value: 7.15e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499284122  27 AGMDLIAANE-QPITIKAAAIQLIPTGIAIALPDSFEAQIRPRSGLAvKHGITVANsPGTIDADYRGEIKVILINLGKED 105
Cdd:cd07557    1 AGYDLRLGEDfEGIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGEITLELYNLGPEP 78

                         90
                 ....*....|....
gi 499284122 106 FIIEKGMRIAQMII 119
Cdd:cd07557   79 VVIKKGDRIAQLVF 92
 
Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
1-148 5.60e-89

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 255.47  E-value: 5.60e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499284122   1 MTITQVKIKKLENFSG-SLPEYATEHSAGMDLIAANEQPITIKAAAIQLIPTGIAIALPDSFEAQIRPRSGLAVKHGITV 79
Cdd:PRK00601   1 MKKIDVKILDPRLGKEfPLPAYATEGSAGLDLRACLDEPVTLAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIVL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499284122  80 ANSPGTIDADYRGEIKVILINLGKEDFIIEKGMRIAQMIIAKYERILWEESSSLMETMRGSGGFGSTGV 148
Cdd:PRK00601  81 GNLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTGR 149
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 5-148 4.21e-87

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: 250.32  E-value: 4.21e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499284122   5 QVKIKKLENfSGSLPEYATEHSAGMDLIAANEQPITIKAAAIQLIPTGIAIALPDSFEAQIRPRSGLAVKHGITVANSPG 84
Cdd:COG0756    1 KVKIKRLDE-DAPLPAYATPGSAGLDLRAALDEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLLNSPG 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499284122  85 TIDADYRGEIKVILINLGKEDFIIEKGMRIAQMIIAKYERILWEESSSLMETMRGSGGFGSTGV 148
Cdd:COG0756   80 TIDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTGR 143
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 6-148 1.66e-68

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: 203.62  E-value: 1.66e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499284122    6 VKIKKLENfSGSLPEYATEHSAGMDLIAAneQPITIKAAAIQLIPTGIAIALPDSFEAQIRPRSGLAVKHGITVANSPGT 85
Cdd:TIGR00576   2 LKFVKLSP-NAPLPTYATEGAAGYDLRAA--EDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGVTIDNSPGV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499284122   86 IDADYRGEIKVILINLGKEDFIIEKGMRIAQMIIAKYER-ILWEESSSLMETMRGSGGFGSTGV 148
Cdd:TIGR00576  79 IDADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 16-147 4.04e-40

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 131.26  E-value: 4.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499284122   16 GSLPEYATEHSAGMDLIAAneQPITIKAAAIQLIPTGIAIALPDSFEAQIRPRSGLAVKHGITVansPGTIDADYRGEIK 95
Cdd:pfam00692   3 AEIPTPGSPGDAGYDLYAP--YDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAKGLIVV---PGVIDSDYRGEVK 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 499284122   96 VILINLGKEDFIIEKGMRIAQMIIAKYERILWEESSSLMETMRGSGGFGSTG 147
Cdd:pfam00692  78 VVLFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
PLN02547 PLN02547
dUTP pyrophosphatase
 5-148 4.98e-38

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 126.83  E-value: 4.98e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499284122   5 QVKIKKLENfSGSLPEYATEHSAGMDLIAANEqpITIKAAAIQLIPTGIAIALPDSFEAQIRPRSGLAVKHGITVAnsPG 84
Cdd:PLN02547  16 LLRVKKLSE-KATLPSRGSALAAGYDLSSAYD--TVVPARGKALVPTDLSIAIPEGTYARIAPRSGLAWKHSIDVG--AG 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499284122  85 TIDADYRGEIKVILINLGKEDFIIEKGMRIAQMIIakyERILW---EESSSLMETMRGSGGFGSTGV 148
Cdd:PLN02547  91 VIDADYRGPVGVILFNHSDVDFEVKVGDRIAQLIL---EKIVTpevVEVEDLDATVRGAGGFGSTGV 154
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 27-119 7.15e-35

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: 116.44  E-value: 7.15e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499284122  27 AGMDLIAANE-QPITIKAAAIQLIPTGIAIALPDSFEAQIRPRSGLAvKHGITVANsPGTIDADYRGEIKVILINLGKED 105
Cdd:cd07557    1 AGYDLRLGEDfEGIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLA-RKGITVHN-AGVIDPGYRGEITLELYNLGPEP 78

                         90
                 ....*....|....
gi 499284122 106 FIIEKGMRIAQMII 119
Cdd:cd07557   79 VVIKKGDRIAQLVF 92
PHA03094 PHA03094
dUTPase; Provisional
 1-148 3.04e-33

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 114.09  E-value: 3.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499284122   1 MTITQVKIKKLENFSgSLPEYATEHSAGMDLIAANEqpITIKAAAIQLIPTGIAIALPDSFEAQIRPRSGLAVKHGITVA 80
Cdd:PHA03094   1 MSNSPVRCVKLSNFA-KIPTRSSPKSAGYDLYSAYD--YTVPPKERILVKTDISLSIPKFCYGRIAPRSGLSLNYGIDIG 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499284122  81 NspGTIDADYRGEIKVILINLGKEDFIIEKGMRIAQMIIAKYERILWEESSSLMETMRGSGGFGSTGV 148
Cdd:PHA03094  78 G--GVIDEDYRGNIGVIFINNGKCTFNIKTGDRIAQIIFERIEYPELKEVQSLDSTDRGDQGFGSSGL 143
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 15-148 4.28e-30

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 106.61  E-value: 4.28e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499284122  15 SGSLPEYATEHSAGMDLIAANEqpITIKAAAIQLIPTGIAIALPDSFEAQIRPRSGLAVKHGITVAnsPGTIDADYRGEI 94
Cdd:PHA02703  22 NATIPTRGSPGAAGLDLCSACD--CIVPAGCRCVVFTDLLIKLPDGCYGRIAPRSGLAVKHFIDVG--AGVIDADYRGNV 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499284122  95 KVILINLGKEDFIIEKGMRIAQMIIAKYERILWEESSSLMETMRGSGGFGSTGV 148
Cdd:PHA02703  98 GVVLFNFGHNDFEVKKGDRIAQLICERAAFPAVEEVACLDDTDRGAGGFGSTGS 151
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 24-148 7.12e-20

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 80.16  E-value: 7.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499284122  24 EHSAGMDLIAANEQpiTIKAAAIQLIPTGI-AIAL-PDSFEAQIR-------PRSGLAvKHGITVANSPGTIDADYRGEI 94
Cdd:PTZ00143  24 EGDSGLDLFIVKDQ--TIKPGETAFIKLGIkAAAFqKDEDGSDGKnvswllfPRSSIS-KTPLRLANSIGLIDAGYRGEL 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499284122  95 KVILINLGKEDFIIEKGMRIAQMIIAKYERILWEESSSLMETMRGSGGFGSTGV 148
Cdd:PTZ00143 101 IAAVDNIKDEPYTIKKGDRLVQLVSFDGEPITFELVDELDETTRGEGGFGSTGR 154
dut PRK13956
dUTP diphosphatase;
18-148 3.23e-15

dUTP diphosphatase;


Pssm-ID: 184417 [Multi-domain]  Cd Length: 147  Bit Score: 67.90  E-value: 3.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499284122  18 LPEYATEHSAGMDLIAANEqpITIKAAAIQLIPTGIAIALPDSFEAQIRPRSGLAVKHGITVANSPGTIDADY------R 91
Cdd:PRK13956  18 LPKRETAHAAGYDLKVAER--TVIAPGEIKLVPTGVKAYMQPGEVLYLYDRSSNPRKKGLVLINSVGVIDGDYygnpanE 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499284122  92 GEIKVILINLGKEDFIIEKGMRIAQMIIAKYERILWEESSSlmetMRgSGGFGSTGV 148
Cdd:PRK13956  96 GHIFAQMKNITDQEVVLEVGERIVQGVFMPFLIADGDQADG----ER-TGGFGSTGK 147
Dcd COG0717
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ...
 55-121 1.35e-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: 50.98  E-value: 1.35e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499284122  55 IALPDSFEAQIRPRSGLAvKHGITVANSPGTIDADYRGEIKVILINLGKEDFIIEKGMRIAQMIIAK 121
Cdd:COG0717   86 VRLPDDLVAFLEGRSSLA-RLGLFVHTTAGVIDPGFEGRITLELSNTGPLPIKLYPGMRIAQLVFFR 151
dCTP_deam TIGR02274
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ...
 19-121 7.52e-07

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: 46.15  E-value: 7.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499284122   19 PEYATEHsagmDLIAANEQPITIKAAAIQLIPTGIAIALPDSFEAQIRPRSGLAvKHGITVANSPGTIDADYRGEIKVIL 98
Cdd:TIGR02274  55 PKEAVSY----LFEVEEGEEFVIPPGEFALATTLEYVKLPDDVVGFLEGRSSLA-RLGLFIHVTAGRIDPGFEGNITLEL 129

                          90       100
                  ....*....|....*....|...
gi 499284122   99 INLGKEDFIIEKGMRIAQMIIAK 121
Cdd:TIGR02274 130 FNAGKLPVKLRPGMRIAQLVFER 152
PHA03131 PHA03131
dUTPase; Provisional
 35-111 1.08e-04

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 40.75  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499284122  35 NEQPITIKAAAIQLIPTGIaialpdsfeaQIRPRSGLA-VKHGIT---VANSPGTIDADYRGEIKVILINLGKEDFIIEK 110
Cdd:PHA03131  32 NKTPILVRPGEPTVVPLGL----------YIRRPPGFAfILWGSTsknVTCHTGLIDPGYRGELKLILLNKTKYNVTLRP 101


                 .
gi 499284122 111 G 111
Cdd:PHA03131 102 G 102
PRK02253 PRK02253
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 55-121 2.14e-03

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 179395  Cd Length: 167  Bit Score: 36.47  E-value: 2.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499284122  55 IALPDSFEAQIRPRSGLaVKHGITVanSPGTIDADYRGEIKVILINLGKEDFIIEKGMRIAQMIIAK 121
Cdd:PRK02253  87 VNIPEDHVGFAYPRSSL-LRNGCTL--ETAVWDAGYEGRGEGLLVVHNPHGIRLERGARIAQLVFAT 150
 
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