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Conserved domains on  [gi|488432666|ref|WP_002502051|]
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MULTISPECIES: dUTP diphosphatase [Bacilli]

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 ...
4-140 7.99e-52

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: 160.95  E-value: 7.99e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432666   4 ELEIKLLSENATMPKRANSTDSGLDLY--VSEATTIKVGETKAVKTDVAINLPHGYEAQVRPRSGKSLKTKLRV--ALGT 79
Cdd:COG0756    1 KVKIKRLDEDAPLPAYATPGSAGLDLRaaLDEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLlnSPGT 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488432666  80 IDQTYNKEIGIITDNIGDEDITVEKGERLAQLVVVPVIYPTPKQVNWFEnESDRGA--YGSTG 140
Cdd:COG0756   81 IDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELD-ETERGAggFGSTG 142
 
Name Accession Description Interval E-value
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
4-140 7.99e-52

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: 160.95  E-value: 7.99e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432666   4 ELEIKLLSENATMPKRANSTDSGLDLY--VSEATTIKVGETKAVKTDVAINLPHGYEAQVRPRSGKSLKTKLRV--ALGT 79
Cdd:COG0756    1 KVKIKRLDEDAPLPAYATPGSAGLDLRaaLDEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLlnSPGT 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488432666  80 IDQTYNKEIGIITDNIGDEDITVEKGERLAQLVVVPVIYPTPKQVNWFEnESDRGA--YGSTG 140
Cdd:COG0756   81 IDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELD-ETERGAggFGSTG 142
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
4-141 4.45e-45

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: 143.91  E-value: 4.45e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432666    4 ELEIKLLSENATMPKRANSTDSGLDLYVSEATTIKVGETKAVKTDVAINLPHGYEAQVRPRSGKSLK--TKLRVALGTID 81
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKhgVTIDNSPGVID 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488432666   82 QTYNKEIGIITDNIGDEDITVEKGERLAQLVVVPVIY-PTPKQVNWFEnESDRGA--YGSTGE 141
Cdd:TIGR00576  81 ADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELD-ETERGEggFGSTGV 142
dut PRK00601
dUTP diphosphatase;
2-140 4.17e-42

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 136.45  E-value: 4.17e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432666   2 SKELEIKLL----SENATMPKRANSTDSGLDLY--VSEATTIKVGETKAVKTDVAINLPHGYEAQVRPRSGKSLKTKLRV 75
Cdd:PRK00601   1 MKKIDVKILdprlGKEFPLPAYATEGSAGLDLRacLDEPVTLAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIVL 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488432666  76 --ALGTIDQTYNKEIGIITDNIGDEDITVEKGERLAQLVVVPVIYPTPKQVNWFEnESDRGA--YGSTG 140
Cdd:PRK00601  81 gnLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFD-ETERGAggFGSTG 148
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
12-140 5.59e-30

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 105.06  E-value: 5.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432666   12 ENATMPKRANSTDSGLDLYVSEATTIKVGETKAVKTDVAINLPHGYEAQVRPRSGKSLKtKLRVALGTIDQTYNKEIGII 91
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAK-GLIVVPGVIDSDYRGEVKVV 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 488432666   92 TDNIGDEDITVEKGERLAQLVVVPVIYPTPKQVNWFENeSDRGA--YGSTG 140
Cdd:pfam00692  80 LFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDN-TDRGDggFGSSG 129
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
25-113 2.68e-23

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: 86.78  E-value: 2.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432666  25 SGLDLYVSE---ATTIKVGETKAVKTDVAINLPHGYEAQVRPRSGKSLKtKLRVA-LGTIDQTYNKEIGIITDNIGDEDI 100
Cdd:cd07557    1 AGYDLRLGEdfeGIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLARK-GITVHnAGVIDPGYRGEITLELYNLGPEPV 79
                         90
                 ....*....|...
gi 488432666 101 TVEKGERLAQLVV 113
Cdd:cd07557   80 VIKKGDRIAQLVF 92
 
Name Accession Description Interval E-value
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
4-140 7.99e-52

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: 160.95  E-value: 7.99e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432666   4 ELEIKLLSENATMPKRANSTDSGLDLY--VSEATTIKVGETKAVKTDVAINLPHGYEAQVRPRSGKSLKTKLRV--ALGT 79
Cdd:COG0756    1 KVKIKRLDEDAPLPAYATPGSAGLDLRaaLDEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLlnSPGT 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488432666  80 IDQTYNKEIGIITDNIGDEDITVEKGERLAQLVVVPVIYPTPKQVNWFEnESDRGA--YGSTG 140
Cdd:COG0756   81 IDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELD-ETERGAggFGSTG 142
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
4-141 4.45e-45

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: 143.91  E-value: 4.45e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432666    4 ELEIKLLSENATMPKRANSTDSGLDLYVSEATTIKVGETKAVKTDVAINLPHGYEAQVRPRSGKSLK--TKLRVALGTID 81
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKhgVTIDNSPGVID 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488432666   82 QTYNKEIGIITDNIGDEDITVEKGERLAQLVVVPVIY-PTPKQVNWFEnESDRGA--YGSTGE 141
Cdd:TIGR00576  81 ADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELD-ETERGEggFGSTGV 142
dut PRK00601
dUTP diphosphatase;
2-140 4.17e-42

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 136.45  E-value: 4.17e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432666   2 SKELEIKLL----SENATMPKRANSTDSGLDLY--VSEATTIKVGETKAVKTDVAINLPHGYEAQVRPRSGKSLKTKLRV 75
Cdd:PRK00601   1 MKKIDVKILdprlGKEFPLPAYATEGSAGLDLRacLDEPVTLAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIVL 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488432666  76 --ALGTIDQTYNKEIGIITDNIGDEDITVEKGERLAQLVVVPVIYPTPKQVNWFEnESDRGA--YGSTG 140
Cdd:PRK00601  81 gnLPGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFD-ETERGAggFGSTG 148
PLN02547 PLN02547
dUTP pyrophosphatase
1-140 2.92e-30

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 106.80  E-value: 2.92e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432666   1 MSKELEIKLLSENATMPKRANSTDSGLDLYVSEATTIKVGETKAVKTDVAINLPHGYEAQVRPRSGKSLKTKLRVALGTI 80
Cdd:PLN02547  13 PSPLLRVKKLSEKATLPSRGSALAAGYDLSSAYDTVVPARGKALVPTDLSIAIPEGTYARIAPRSGLAWKHSIDVGAGVI 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488432666  81 DQTYNKEIGIITDNIGDEDITVEKGERLAQLVVVPVIYPTPKQVNWFEnESDRGA--YGSTG 140
Cdd:PLN02547  93 DADYRGPVGVILFNHSDVDFEVKVGDRIAQLILEKIVTPEVVEVEDLD-ATVRGAggFGSTG 153
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
12-140 5.59e-30

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 105.06  E-value: 5.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432666   12 ENATMPKRANSTDSGLDLYVSEATTIKVGETKAVKTDVAINLPHGYEAQVRPRSGKSLKtKLRVALGTIDQTYNKEIGII 91
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAK-GLIVVPGVIDSDYRGEVKVV 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 488432666   92 TDNIGDEDITVEKGERLAQLVVVPVIYPTPKQVNWFENeSDRGA--YGSTG 140
Cdd:pfam00692  80 LFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDN-TDRGDggFGSSG 129
PHA02703 PHA02703
ORF007 dUTPase; Provisional
5-140 4.50e-26

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 96.21  E-value: 4.50e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432666   5 LEIKLLSENATMPKRANSTDSGLDLYVSEATTIKVGETKAVKTDVAINLPHGYEAQVRPRSGKSLKTKLRVALGTIDQTY 84
Cdd:PHA02703  14 LRVVRLSPNATIPTRGSPGAAGLDLCSACDCIVPAGCRCVVFTDLLIKLPDGCYGRIAPRSGLAVKHFIDVGAGVIDADY 93
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488432666  85 NKEIGIITDNIGDEDITVEKGERLAQLVVVPVIYPTPKQVNWFEnESDRGA--YGSTG 140
Cdd:PHA02703  94 RGNVGVVLFNFGHNDFEVKKGDRIAQLICERAAFPAVEEVACLD-DTDRGAggFGSTG 150
PHA03094 PHA03094
dUTPase; Provisional
10-140 2.50e-24

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 90.98  E-value: 2.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432666  10 LSENATMPKRANSTDSGLDLYVSEATTIKVGETKAVKTDVAINLPHGYEAQVRPRSGKSLKTKLRVALGTIDQTYNKEIG 89
Cdd:PHA03094  11 LSNFAKIPTRSSPKSAGYDLYSAYDYTVPPKERILVKTDISLSIPKFCYGRIAPRSGLSLNYGIDIGGGVIDEDYRGNIG 90
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488432666  90 IITDNIGDEDITVEKGERLAQLVVVPVIYPTPKQVNWFENeSDRG--AYGSTG 140
Cdd:PHA03094  91 VIFINNGKCTFNIKTGDRIAQIIFERIEYPELKEVQSLDS-TDRGdqGFGSSG 142
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
25-113 2.68e-23

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: 86.78  E-value: 2.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432666  25 SGLDLYVSE---ATTIKVGETKAVKTDVAINLPHGYEAQVRPRSGKSLKtKLRVA-LGTIDQTYNKEIGIITDNIGDEDI 100
Cdd:cd07557    1 AGYDLRLGEdfeGIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLARK-GITVHnAGVIDPGYRGEITLELYNLGPEPV 79
                         90
                 ....*....|...
gi 488432666 101 TVEKGERLAQLVV 113
Cdd:cd07557   80 VIKKGDRIAQLVF 92
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
24-140 3.30e-15

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 67.84  E-value: 3.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432666  24 DSGLDLYVSEATTIKVGETKAVKTDV---AINLPHGYEAQVR------PRSGKSlKTKLRVA--LGTIDQTYNKEIGIIT 92
Cdd:PTZ00143  26 DSGLDLFIVKDQTIKPGETAFIKLGIkaaAFQKDEDGSDGKNvswllfPRSSIS-KTPLRLAnsIGLIDAGYRGELIAAV 104
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488432666  93 DNIGDEDITVEKGERLAQLVVV---PVIYPTPKQVNwfENESDRGAYGSTG 140
Cdd:PTZ00143 105 DNIKDEPYTIKKGDRLVQLVSFdgePITFELVDELD--ETTRGEGGFGSTG 153
dut PRK13956
dUTP diphosphatase;
16-140 1.12e-09

dUTP diphosphatase;


Pssm-ID: 184417 [Multi-domain]  Cd Length: 147  Bit Score: 53.26  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432666  16 MPKRANSTDSGLDLYVSEATTIKVGETKAVKTDVAINLPHGYEAQVRPRSGKSLKTKLRV--ALGTIDQTY----NKEIG 89
Cdd:PRK13956  18 LPKRETAHAAGYDLKVAERTVIAPGEIKLVPTGVKAYMQPGEVLYLYDRSSNPRKKGLVLinSVGVIDGDYygnpANEGH 97
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488432666  90 IITD--NIGDEDITVEKGERLAQLVVVPVIYPTPKQvnwfENESDRGAYGSTG 140
Cdd:PRK13956  98 IFAQmkNITDQEVVLEVGERIVQGVFMPFLIADGDQ----ADGERTGGFGSTG 146
PHA03124 PHA03124
dUTPase; Provisional
17-114 6.11e-03

dUTPase; Provisional


Pssm-ID: 165396 [Multi-domain]  Cd Length: 418  Bit Score: 35.69  E-value: 6.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432666  17 PKRANstDSGLDLYVSEATTIKVGETKAVKTDVAINLPHGYEAQVRPRSGKSLKTKLRVALGTIDqtyNKEIGIITDNIG 96
Cdd:PHA03124 285 PKEAE--DAGYDIRAPEDCTILPGGSTRIILPQKLACGKFRAAFILGRSSMNLKGLLVDPEHVQD---DDWISFNITNIR 359
                         90
                 ....*....|....*...
gi 488432666  97 DEDITVEKGERLAQLVVV 114
Cdd:PHA03124 360 DAAAFFHAGDRIAQLIAL 377
 
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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