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Conserved domains on  [gi|920604386|ref|WP_053015893|]
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MULTISPECIES: dUTP diphosphatase [Staphylococcus]

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 ...
4-139 9.81e-55

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: 168.27  E-value: 9.81e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604386   4 LPIKLLSENAILPTRANPTDSGLDLYVA--EDTTIPAHSTVVVPTHIAIDLAYGYEAQVRPRSGNSLKTKLRV--ALGTI 79
Cdd:COG0756    2 VKIKRLDEDAPLPAYATPGSAGLDLRAAldEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLlnSPGTI 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 920604386  80 DHTYNKEIGIITDNIGDEAIVVKAGTRLAQLVIAPVMLPEPTEVQEFDeESERGA--YGSTG 139
Cdd:COG0756   82 DSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELD-ETERGAggFGSTG 142
 
Name Accession Description Interval E-value
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
4-139 9.81e-55

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: 168.27  E-value: 9.81e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604386   4 LPIKLLSENAILPTRANPTDSGLDLYVA--EDTTIPAHSTVVVPTHIAIDLAYGYEAQVRPRSGNSLKTKLRV--ALGTI 79
Cdd:COG0756    2 VKIKRLDEDAPLPAYATPGSAGLDLRAAldEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLlnSPGTI 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 920604386  80 DHTYNKEIGIITDNIGDEAIVVKAGTRLAQLVIAPVMLPEPTEVQEFDeESERGA--YGSTG 139
Cdd:COG0756   82 DSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELD-ETERGAggFGSTG 142
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
6-140 1.06e-43

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: 140.45  E-value: 1.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604386    6 IKLLSENAILPTRANPTDSGLDLYVAEDTTIPAHSTVVVPTHIAIDLAYGYEAQVRPRSGNSLK--TKLRVALGTIDHTY 83
Cdd:TIGR00576   4 FVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKhgVTIDNSPGVIDADY 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 920604386   84 NKEIGIITDNIGDEAIVVKAGTRLAQLVIAPVMLPEPTEVQEFDEESERGA--YGSTGE 140
Cdd:TIGR00576  84 RGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTEVEFEEVEELDETERGEggFGSTGV 142
dut PRK00601
dUTP diphosphatase;
1-139 1.17e-42

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 137.99  E-value: 1.17e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604386   1 MSILPIKLL----SENAILPTRANPTDSGLDLYVAEDT--TIPAHSTVVVPTHIAIDLAYGYEAQVRPRSGNSLKTKLRV 74
Cdd:PRK00601   1 MKKIDVKILdprlGKEFPLPAYATEGSAGLDLRACLDEpvTLAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIVL 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 920604386  75 --ALGTIDHTYNKEIGIITDNIGDEAIVVKAGTRLAQLVIAPVMLPEPTEVQEFDeESERGA--YGSTG 139
Cdd:PRK00601  81 gnLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFD-ETERGAggFGSTG 148
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
11-139 1.33e-29

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 103.91  E-value: 1.33e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604386   11 ENAILPTRANPTDSGLDLYVAEDTTIPAHSTVVVPTHIAIDLAYGYEAQVRPRSGNSLKtKLRVALGTIDHTYNKEIGII 90
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAK-GLIVVPGVIDSDYRGEVKVV 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 920604386   91 TDNIGDEAIVVKAGTRLAQLVIAPVMLPEPTEVQEFDeESERGA--YGSTG 139
Cdd:pfam00692  80 LFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLD-NTDRGDggFGSSG 129
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
24-112 2.72e-21

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: 81.77  E-value: 2.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604386  24 SGLDLYVAED---TTIPAHSTVVVPTHIAIDLAYGYEAQVRPRSGNSLKtKLRVA-LGTIDHTYNKEIGIITDNIGDEAI 99
Cdd:cd07557    1 AGYDLRLGEDfegIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLARK-GITVHnAGVIDPGYRGEITLELYNLGPEPV 79
                         90
                 ....*....|...
gi 920604386 100 VVKAGTRLAQLVI 112
Cdd:cd07557   80 VIKKGDRIAQLVF 92
 
Name Accession Description Interval E-value
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
4-139 9.81e-55

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: 168.27  E-value: 9.81e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604386   4 LPIKLLSENAILPTRANPTDSGLDLYVA--EDTTIPAHSTVVVPTHIAIDLAYGYEAQVRPRSGNSLKTKLRV--ALGTI 79
Cdd:COG0756    2 VKIKRLDEDAPLPAYATPGSAGLDLRAAldEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLlnSPGTI 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 920604386  80 DHTYNKEIGIITDNIGDEAIVVKAGTRLAQLVIAPVMLPEPTEVQEFDeESERGA--YGSTG 139
Cdd:COG0756   82 DSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELD-ETERGAggFGSTG 142
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
6-140 1.06e-43

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: 140.45  E-value: 1.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604386    6 IKLLSENAILPTRANPTDSGLDLYVAEDTTIPAHSTVVVPTHIAIDLAYGYEAQVRPRSGNSLK--TKLRVALGTIDHTY 83
Cdd:TIGR00576   4 FVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKhgVTIDNSPGVIDADY 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 920604386   84 NKEIGIITDNIGDEAIVVKAGTRLAQLVIAPVMLPEPTEVQEFDEESERGA--YGSTGE 140
Cdd:TIGR00576  84 RGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTEVEFEEVEELDETERGEggFGSTGV 142
dut PRK00601
dUTP diphosphatase;
1-139 1.17e-42

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 137.99  E-value: 1.17e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604386   1 MSILPIKLL----SENAILPTRANPTDSGLDLYVAEDT--TIPAHSTVVVPTHIAIDLAYGYEAQVRPRSGNSLKTKLRV 74
Cdd:PRK00601   1 MKKIDVKILdprlGKEFPLPAYATEGSAGLDLRACLDEpvTLAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIVL 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 920604386  75 --ALGTIDHTYNKEIGIITDNIGDEAIVVKAGTRLAQLVIAPVMLPEPTEVQEFDeESERGA--YGSTG 139
Cdd:PRK00601  81 gnLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFD-ETERGAggFGSTG 148
PLN02547 PLN02547
dUTP pyrophosphatase
2-139 3.06e-34

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 116.82  E-value: 3.06e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604386   2 SILPIKLLSENAILPTRANPTDSGLDLYVAEDTTIPAHSTVVVPTHIAIDLAYGYEAQVRPRSGNSLKTKLRVALGTIDH 81
Cdd:PLN02547  15 PLLRVKKLSEKATLPSRGSALAAGYDLSSAYDTVVPARGKALVPTDLSIAIPEGTYARIAPRSGLAWKHSIDVGAGVIDA 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604386  82 TYNKEIGIITDNIGDEAIVVKAGTRLAQLVIAPVMLPEPTEVQEFDeESERGA--YGSTG 139
Cdd:PLN02547  95 DYRGPVGVILFNHSDVDFEVKVGDRIAQLILEKIVTPEVVEVEDLD-ATVRGAggFGSTG 153
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
11-139 1.33e-29

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 103.91  E-value: 1.33e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604386   11 ENAILPTRANPTDSGLDLYVAEDTTIPAHSTVVVPTHIAIDLAYGYEAQVRPRSGNSLKtKLRVALGTIDHTYNKEIGII 90
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAK-GLIVVPGVIDSDYRGEVKVV 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 920604386   91 TDNIGDEAIVVKAGTRLAQLVIAPVMLPEPTEVQEFDeESERGA--YGSTG 139
Cdd:pfam00692  80 LFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLD-NTDRGDggFGSSG 129
PHA02703 PHA02703
ORF007 dUTPase; Provisional
9-139 1.09e-27

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 100.44  E-value: 1.09e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604386   9 LSENAILPTRANPTDSGLDLYVAEDTTIPAHSTVVVPTHIAIDLAYGYEAQVRPRSGNSLKTKLRVALGTIDHTYNKEIG 88
Cdd:PHA02703  19 LSPNATIPTRGSPGAAGLDLCSACDCIVPAGCRCVVFTDLLIKLPDGCYGRIAPRSGLAVKHFIDVGAGVIDADYRGNVG 98
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 920604386  89 IITDNIGDEAIVVKAGTRLAQLVIAPVMLPEPTEVQEFDeESERGA--YGSTG 139
Cdd:PHA02703  99 VVLFNFGHNDFEVKKGDRIAQLICERAAFPAVEEVACLD-DTDRGAggFGSTG 150
PHA03094 PHA03094
dUTPase; Provisional
1-139 2.96e-25

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 93.29  E-value: 2.96e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604386   1 MSILPIKL--LSENAILPTRANPTDSGLDLYVAEDTTIPAHSTVVVPTHIAIDLAYGYEAQVRPRSGNSLKTKLRVALGT 78
Cdd:PHA03094   1 MSNSPVRCvkLSNFAKIPTRSSPKSAGYDLYSAYDYTVPPKERILVKTDISLSIPKFCYGRIAPRSGLSLNYGIDIGGGV 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 920604386  79 IDHTYNKEIGIITDNIGDEAIVVKAGTRLAQLVIAPVMLPEPTEVQEFDeESERG--AYGSTG 139
Cdd:PHA03094  81 IDEDYRGNIGVIFINNGKCTFNIKTGDRIAQIIFERIEYPELKEVQSLD-STDRGdqGFGSSG 142
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
24-112 2.72e-21

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: 81.77  E-value: 2.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604386  24 SGLDLYVAED---TTIPAHSTVVVPTHIAIDLAYGYEAQVRPRSGNSLKtKLRVA-LGTIDHTYNKEIGIITDNIGDEAI 99
Cdd:cd07557    1 AGYDLRLGEDfegIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLARK-GITVHnAGVIDPGYRGEITLELYNLGPEPV 79
                         90
                 ....*....|...
gi 920604386 100 VVKAGTRLAQLVI 112
Cdd:cd07557   80 VIKKGDRIAQLVF 92
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
21-139 2.03e-13

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 63.21  E-value: 2.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604386  21 PTDSGLDLYVAEDTTIPAHSTVVVPTHIAIdLAYGYEAQ----------VRPRSGNSlKTKLRVA--LGTIDHTYNKEIG 88
Cdd:PTZ00143  24 EGDSGLDLFIVKDQTIKPGETAFIKLGIKA-AAFQKDEDgsdgknvswlLFPRSSIS-KTPLRLAnsIGLIDAGYRGELI 101
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 920604386  89 IITDNIGDEAIVVKAGTRLAQLViapVMLPEPTEVQEFDE--ESERG--AYGSTG 139
Cdd:PTZ00143 102 AAVDNIKDEPYTIKKGDRLVQLV---SFDGEPITFELVDEldETTRGegGFGSTG 153
dut PRK13956
dUTP diphosphatase;
10-139 1.60e-10

dUTP diphosphatase;


Pssm-ID: 184417 [Multi-domain]  Cd Length: 147  Bit Score: 55.19  E-value: 1.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604386  10 SENAILPTRANPTDSGLDLYVAEDTTIPAHSTVVVPTHIAIDLAYGYEAQVRPRSGNSLKTKLRV--ALGTIDHTY---- 83
Cdd:PRK13956  13 TNENLLPKRETAHAAGYDLKVAERTVIAPGEIKLVPTGVKAYMQPGEVLYLYDRSSNPRKKGLVLinSVGVIDGDYygnp 92
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 920604386  84 NKEIGIITD--NIGDEAIVVKAGTRLAQLVIAPVMLPEPTEvqefdEESER-GAYGSTG 139
Cdd:PRK13956  93 ANEGHIFAQmkNITDQEVVLEVGERIVQGVFMPFLIADGDQ-----ADGERtGGFGSTG 146
PHA03124 PHA03124
dUTPase; Provisional
21-139 1.88e-05

dUTPase; Provisional


Pssm-ID: 165396 [Multi-domain]  Cd Length: 418  Bit Score: 43.01  E-value: 1.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604386  21 PTDSGLDLYVAEDTTIPAHSTVVVPTHIAIDLAYGYEAQVRPRSGNSLKTKLRVALGTIDhtyNKEIGIITDNIGDEAIV 100
Cdd:PHA03124 288 AEDAGYDIRAPEDCTILPGGSTRIILPQKLACGKFRAAFILGRSSMNLKGLLVDPEHVQD---DDWISFNITNIRDAAAF 364
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 920604386 101 VKAGTRLAQLVIAP---VMLPEP---------TEVQEFDEESERG--AYGSTG 139
Cdd:PHA03124 365 FHAGDRIAQLIALEdklEFLGEPdalpwkivnSVQDEKKNLSSRGdgGFGSSG 417
PHA03130 PHA03130
dUTPase; Provisional
13-139 2.43e-03

dUTPase; Provisional


Pssm-ID: 222995 [Multi-domain]  Cd Length: 368  Bit Score: 36.80  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604386  13 AILPTRANptDSGLDLYVAEDTTIPAHSTVVV-PTHIAIDLAYGYEA-QVRPRSG-NS---LKTKLRVALGtidhtynKE 86
Cdd:PHA03130 205 AFLPKRAE--DAGIDIVVHKRVEVPAGGTVVIqPSLRVLLAAGGPEAyYVLGRSSlNArgvLVTPTRWLPG-------RQ 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604386  87 IGIITDNIGDEAIVVKAGTRLAQLVIA----------------------------------PVMLPEPTEVQEFDEE--- 129
Cdd:PHA03130 276 CAFSVHNITGAPVTLEAGSKVAQLLVAgsdalpwvppdnvpgdgalrayprgvsparatpaPPALPCLVFTAEFDAEapp 355
                        170
                 ....*....|..
gi 920604386 130 SERGA--YGSTG 139
Cdd:PHA03130 356 SERGTggFGSTG 367
 
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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