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Conserved domains on  [gi|500092190|ref|WP_011768203|]
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MULTISPECIES: dUTP diphosphatase [Mycolicibacterium]

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

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List of domain hits

 Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
1-132 3.19e-67

dUTP diphosphatase;


:

Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 200.78  E-value: 3.19e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500092190   1 MSTSLAVLRLDRELPMPARAHDGDAGVDLFSA--RDVELAPGQRELVPTGIAVAIPHGMVGLVHPRSGLAARVGLSIVNS 78
Cdd:PRK00601   4 IDVKILDPRLGKEFPLPAYATEGSAGLDLRACldEPVTLAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIVLGNL 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 500092190  79 PGTIDAGYRGEIKVSLINLDpHAPIVIRRGDRIAQLLVQRVELPELVEVTSFDE 132
Cdd:PRK00601  84 PGTIDSDYRGELKVSLWNRG-QEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDE 136
 
Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
1-132 3.19e-67

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 200.78  E-value: 3.19e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500092190   1 MSTSLAVLRLDRELPMPARAHDGDAGVDLFSA--RDVELAPGQRELVPTGIAVAIPHGMVGLVHPRSGLAARVGLSIVNS 78
Cdd:PRK00601   4 IDVKILDPRLGKEFPLPAYATEGSAGLDLRACldEPVTLAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIVLGNL 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 500092190  79 PGTIDAGYRGEIKVSLINLDpHAPIVIRRGDRIAQLLVQRVELPELVEVTSFDE 132
Cdd:PRK00601  84 PGTIDSDYRGELKVSLWNRG-QEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDE 136
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 5-132 2.14e-66

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: 198.32  E-value: 2.14e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500092190   5 LAVLRLDRELPMPARAHDGDAGVDLFSAR--DVELAPGQRELVPTGIAVAIPHGMVGLVHPRSGLAARVGLSIVNSPGTI 82
Cdd:COG0756    2 VKIKRLDEDAPLPAYATPGSAGLDLRAALdePVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLLNSPGTI 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 500092190  83 DAGYRGEIKVSLINLDPHaPIVIRRGDRIAQLLVQRVELPELVEVTSFDE 132
Cdd:COG0756   82 DSDYRGEIKVILINLGDE-PFTIERGDRIAQLVIAPVVQAEFEEVEELDE 130
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 4-132 6.03e-55

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: 169.34  E-value: 6.03e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500092190    4 SLAVLRLDRELPMPARAHDGDAGVDLFSARDVELAPGQRELVPTGIAVAIPHGMVGLVHPRSGLAARVGLSIVNSPGTID 83
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGVTIDNSPGVID 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 500092190   84 AGYRGEIKVSLINLDpHAPIVIRRGDRIAQLLVQRVEL-PELVEVTSFDE 132
Cdd:TIGR00576  81 ADYRGEIKVILINLG-KEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDE 129
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 12-131 1.89e-33

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 114.31  E-value: 1.89e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500092190   12 RELPMPARAHDGDAGVDLFSARDVELAPGQRELVPTGIAVAIPHGMVGLVHPRSGLAARvGLSIVnsPGTIDAGYRGEIK 91
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAK-GLIVV--PGVIDSDYRGEVK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 500092190   92 VSLINLDpHAPIVIRRGDRIAQLLVQRVELPELVEVTSFD 131
Cdd:pfam00692  78 VVLFNLG-KSDFTIKKGDRIAQLIFEPILHPELEPVETLD 116
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 25-116 8.54e-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: 111.43  E-value: 8.54e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500092190  25 AGVDLFSARD---VELAPGQRELVPTGIAVAIPHGMVGLVHPRSGLaARVGLsIVNSPGTIDAGYRGEIKVSLINLDPHa 101
Cdd:cd07557    1 AGYDLRLGEDfegIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSL-ARKGI-TVHNAGVIDPGYRGEITLELYNLGPE- 77

                         90
                 ....*....|....*
gi 500092190 102 PIVIRRGDRIAQLLV 116
Cdd:cd07557   78 PVVIKKGDRIAQLVF 92
 
Name Accession Description Interval E-value
dut PRK00601
dUTP diphosphatase;
1-132 3.19e-67

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 200.78  E-value: 3.19e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500092190   1 MSTSLAVLRLDRELPMPARAHDGDAGVDLFSA--RDVELAPGQRELVPTGIAVAIPHGMVGLVHPRSGLAARVGLSIVNS 78
Cdd:PRK00601   4 IDVKILDPRLGKEFPLPAYATEGSAGLDLRACldEPVTLAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIVLGNL 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 500092190  79 PGTIDAGYRGEIKVSLINLDpHAPIVIRRGDRIAQLLVQRVELPELVEVTSFDE 132
Cdd:PRK00601  84 PGTIDSDYRGELKVSLWNRG-QEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDE 136
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 5-132 2.14e-66

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: 198.32  E-value: 2.14e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500092190   5 LAVLRLDRELPMPARAHDGDAGVDLFSAR--DVELAPGQRELVPTGIAVAIPHGMVGLVHPRSGLAARVGLSIVNSPGTI 82
Cdd:COG0756    2 VKIKRLDEDAPLPAYATPGSAGLDLRAALdePVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLLNSPGTI 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 500092190  83 DAGYRGEIKVSLINLDPHaPIVIRRGDRIAQLLVQRVELPELVEVTSFDE 132
Cdd:COG0756   82 DSDYRGEIKVILINLGDE-PFTIERGDRIAQLVIAPVVQAEFEEVEELDE 130
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 4-132 6.03e-55

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: 169.34  E-value: 6.03e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500092190    4 SLAVLRLDRELPMPARAHDGDAGVDLFSARDVELAPGQRELVPTGIAVAIPHGMVGLVHPRSGLAARVGLSIVNSPGTID 83
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGVTIDNSPGVID 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 500092190   84 AGYRGEIKVSLINLDpHAPIVIRRGDRIAQLLVQRVEL-PELVEVTSFDE 132
Cdd:TIGR00576  81 ADYRGEIKVILINLG-KEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDE 129
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 12-131 1.89e-33

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 114.31  E-value: 1.89e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500092190   12 RELPMPARAHDGDAGVDLFSARDVELAPGQRELVPTGIAVAIPHGMVGLVHPRSGLAARvGLSIVnsPGTIDAGYRGEIK 91
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAK-GLIVV--PGVIDSDYRGEVK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 500092190   92 VSLINLDpHAPIVIRRGDRIAQLLVQRVELPELVEVTSFD 131
Cdd:pfam00692  78 VVLFNLG-KSDFTIKKGDRIAQLIFEPILHPELEPVETLD 116
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 25-116 8.54e-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: 111.43  E-value: 8.54e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500092190  25 AGVDLFSARD---VELAPGQRELVPTGIAVAIPHGMVGLVHPRSGLaARVGLsIVNSPGTIDAGYRGEIKVSLINLDPHa 101
Cdd:cd07557    1 AGYDLRLGEDfegIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSL-ARKGI-TVHNAGVIDPGYRGEITLELYNLGPE- 77

                         90
                 ....*....|....*
gi 500092190 102 PIVIRRGDRIAQLLV 116
Cdd:cd07557   78 PVVIKKGDRIAQLVF 92
PHA03094 PHA03094
dUTPase; Provisional
 1-131 1.91e-29

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 104.85  E-value: 1.91e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500092190   1 MSTSLAVLRLDRELPMPARAHDGDAGVDLFSARDVELAPGQRELVPTGIAVAIPHGMVGLVHPRSGLAARVGLSIvnSPG 80
Cdd:PHA03094   2 SNSPVRCVKLSNFAKIPTRSSPKSAGYDLYSAYDYTVPPKERILVKTDISLSIPKFCYGRIAPRSGLSLNYGIDI--GGG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 500092190  81 TIDAGYRGEIKVSLINlDPHAPIVIRRGDRIAQLLVQRVELPELVEVTSFD 131
Cdd:PHA03094  80 VIDEDYRGNIGVIFIN-NGKCTFNIKTGDRIAQIIFERIEYPELKEVQSLD 129
PLN02547 PLN02547
dUTP pyrophosphatase
 1-132 6.04e-28

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 101.41  E-value: 6.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500092190   1 MSTSLAVLRLDRELPMPARAHDGDAGVDLFSARDVELAPGQRELVPTGIAVAIPHGMVGLVHPRSGLAARvgLSIVNSPG 80
Cdd:PLN02547  13 PSPLLRVKKLSEKATLPSRGSALAAGYDLSSAYDTVVPARGKALVPTDLSIAIPEGTYARIAPRSGLAWK--HSIDVGAG 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 500092190  81 TIDAGYRGEIKVSLINLDPhAPIVIRRGDRIAQLLVQRVELPELVEVTSFDE 132
Cdd:PLN02547  91 VIDADYRGPVGVILFNHSD-VDFEVKVGDRIAQLILEKIVTPEVVEVEDLDA 141
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 4-132 2.89e-23

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 89.66  E-value: 2.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500092190   4 SLAVLRLDRELPMPARAHDGDAGVDLFSARDVELAPGQRELVPTGIAVAIPHGMVGLVHPRSGLAARVGLSIvnSPGTID 83
Cdd:PHA02703  13 ALRVVRLSPNATIPTRGSPGAAGLDLCSACDCIVPAGCRCVVFTDLLIKLPDGCYGRIAPRSGLAVKHFIDV--GAGVID 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 500092190  84 AGYRGEIKVSLINLDpHAPIVIRRGDRIAQLLVQRVELPELVEVTSFDE 132
Cdd:PHA02703  91 ADYRGNVGVVLFNFG-HNDFEVKKGDRIAQLICERAAFPAVEEVACLDD 138
Dcd COG0717
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ...
 37-120 1.13e-16

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


Pssm-ID: 440481  Cd Length: 180  Bit Score: 72.55  E-value: 1.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500092190  37 LAPGQRELVPTGIAVAIPHGMVGLVHPRSGLAaRVGLSIVNSPGTIDAGYRGEIKVSLINLDPHaPIVIRRGDRIAQLLV 116
Cdd:COG0717   72 LPPGEFYLARTLEYVRLPDDLVAFLEGRSSLA-RLGLFVHTTAGVIDPGFEGRITLELSNTGPL-PIKLYPGMRIAQLVF 149


                 ....
gi 500092190 117 QRVE 120
Cdd:COG0717  150 FRLS 153
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 21-140 1.97e-16

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 71.30  E-value: 1.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500092190  21 HDGDAGVDLFSARDVELAPGQRELVPTGIAVAIPHGMVG---------LVHPRSGLAaRVGLSIVNSPGTIDAGYRGEIK 91
Cdd:PTZ00143  23 HEGDSGLDLFIVKDQTIKPGETAFIKLGIKAAAFQKDEDgsdgknvswLLFPRSSIS-KTPLRLANSIGLIDAGYRGELI 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 500092190  92 VSLINLDPHaPIVIRRGDRIAQLLVQ-----RVELPELVEVTSFDEAGLAETTR 140
Cdd:PTZ00143 102 AAVDNIKDE-PYTIKKGDRLVQLVSFdgepiTFELVDELDETTRGEGGFGSTGR 154
dut PRK13956
dUTP diphosphatase;
11-125 9.72e-12

dUTP diphosphatase;


Pssm-ID: 184417 [Multi-domain]  Cd Length: 147  Bit Score: 59.04  E-value: 9.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500092190  11 DRELpMPARAHDGDAGVDLFSARDVELAPGQRELVPTGIAVAIPHGMVGLVHPRSGLAARVGLSIVNSPGTIDAGY---- 86
Cdd:PRK13956  14 NENL-LPKRETAHAAGYDLKVAERTVIAPGEIKLVPTGVKAYMQPGEVLYLYDRSSNPRKKGLVLINSVGVIDGDYygnp 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 500092190  87 --RGEIKVSLINLDPHaPIVIRRGDRIaqllVQRVELPELV 125
Cdd:PRK13956  93 anEGHIFAQMKNITDQ-EVVLEVGERI----VQGVFMPFLI 128
dCTP_deam TIGR02274
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ...
 8-123 1.35e-11

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: 59.25  E-value: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500092190    8 LRLDRELPMPARAHDG--------DAGVDLFSARDVE---LAPGQRELVPTGIAVAIPHGMVGLVHPRSGLAaRVGLSIV 76
Cdd:TIGR02274  33 LRLGNEFRVFRNHTGAvidpenpkEAVSYLFEVEEGEefvIPPGEFALATTLEYVKLPDDVVGFLEGRSSLA-RLGLFIH 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 500092190   77 NSPGTIDAGYRGEIKVSLINLDPhAPIVIRRGDRIAQLLVQRVELPE 123
Cdd:TIGR02274 112 VTAGRIDPGFEGNITLELFNAGK-LPVKLRPGMRIAQLVFERLSSPA 157
PRK02253 PRK02253
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 51-120 1.96e-07

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 179395  Cd Length: 167  Bit Score: 47.64  E-value: 1.96e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500092190  51 VAIPHGMVGLVHPRSGLaARVGLSIvnSPGTIDAGYRGEIKVSLINLDPHApIVIRRGDRIAQLLVQRVE 120
Cdd:PRK02253  87 VNIPEDHVGFAYPRSSL-LRNGCTL--ETAVWDAGYEGRGEGLLVVHNPHG-IRLERGARIAQLVFATLD 152
PHA03131 PHA03131
dUTPase; Provisional
 21-114 4.80e-04

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 38.82  E-value: 4.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500092190  21 HDGDAGVDLFSARDVELAPGQRELVPTGIAV--AIPHgMVGLVHPRSGLAARvGLSIVNSPGTidagyRGEIKVSLINLD 98
Cdd:PHA03131 129 YPDDAGFDVSLPQDLVIFPTTTFTFTLSLCCppISPH-FVPVIFGRSGLASK-GLTVKPTKWR-----RSGLQLKLYNYT 201

                         90
                 ....*....|....*.
gi 500092190  99 PHaPIVIRRGDRIAQL 114
Cdd:PHA03131 202 DE-TIFLPAGSRICQV 216
PHA03131 PHA03131
dUTPase; Provisional
 39-109 8.56e-04

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 38.05  E-value: 8.56e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500092190  39 PGQRELVPTGIAVAIPHGMvGLVhprsgLAARVGLSIVNSPGTIDAGYRGEIKVSLINLDpHAPIVIRRGD 109
Cdd:PHA03131  40 PGEPTVVPLGLYIRRPPGF-AFI-----LWGSTSKNVTCHTGLIDPGYRGELKLILLNKT-KYNVTLRPGE 103
PHA03129 PHA03129
dUTPase; Provisional
 24-116 4.30e-03

dUTPase; Provisional


Pssm-ID: 222994 [Multi-domain]  Cd Length: 436  Bit Score: 36.39  E-value: 4.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500092190  24 DAGVDLFSARDVELAP-GQRELVPTGIAVAIPHGMVGLVHPRSGLAARvGLSIVNSPGTIDAGyrgeIKVSLINLDpHAP 102
Cdd:PHA03129 287 DAGYDIPAPRDIELEPlSSTTIKIQQRYNCKDSSVIPCIFGRSSMNLR-GLIVLPSRWLPNSW----LTLTICNLT-EKT 360

                         90
                 ....*....|....
gi 500092190 103 IVIRRGDRIAQLLV 116
Cdd:PHA03129 361 VFIKAGDRIAQLLL 374
 
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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