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Conserved domains on  [gi|1464307100|ref|YP_009505705|]
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dUTPase [Bottlenose dolphin adenovirus 1]

Protein Classification

dCTP deaminase/dUTPase family protein( domain architecture ID 272)

dCTP deaminase/dUTPase family protein similar to archaeal deoxycytidine triphosphate (dCTP) deaminase that catalyzes the deamination of dCTP to dUTP, and to Yarrowia lipolytica deoxyuridine 5'-triphosphate (dUTP) nucleotidohydrolase that catalyzes the hydrolysis of dUTP to form dUMP

CATH:  2.70.40.10
Gene Ontology:  GO:0009165
SCOP:  3001957

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
trimeric_dUTPase super family cl00493
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 11-115 1.88e-45

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.


The actual alignment was detected with superfamily member TIGR00576:

Pssm-ID: 444938 [Multi-domain]  Cd Length: 142  Bit Score: 143.91  E-value: 1.88e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464307100  11 LKVKLLSANAKVPLRATEGAAGYDLFAASSLLLPANTRKLIPIDIALEIPDGHYGRIAPRSGLSVRHGIMV--GAGVVDC 88
Cdd:TIGR00576   2 LKFVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGVTIdnSPGVIDA 81

                          90       100
                  ....*....|....*....|....*..
gi 1464307100  89 DYRGNIHVLLFNLSNEDFHIKQGVSIC 115
Cdd:TIGR00576  82 DYRGEIKVILINLGKEDFTVKKGDRIA 108
 
Name Accession Description Interval E-value
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 11-115 1.88e-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: 1.88e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464307100  11 LKVKLLSANAKVPLRATEGAAGYDLFAASSLLLPANTRKLIPIDIALEIPDGHYGRIAPRSGLSVRHGIMV--GAGVVDC 88
Cdd:TIGR00576   2 LKFVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGVTIdnSPGVIDA 81

                          90       100
                  ....*....|....*....|....*..
gi 1464307100  89 DYRGNIHVLLFNLSNEDFHIKQGVSIC 115
Cdd:TIGR00576  82 DYRGEIKVILINLGKEDFTVKKGDRIA 108
PLN02547 PLN02547
dUTP pyrophosphatase
 9-111 1.46e-44

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 142.24  E-value: 1.46e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464307100   9 QLLKVKLLSANAKVPLRATEGAAGYDLFAASSLLLPANTRKLIPIDIALEIPDGHYGRIAPRSGLSVRHGIMVGAGVVDC 88
Cdd:PLN02547   15 PLLRVKKLSEKATLPSRGSALAAGYDLSSAYDTVVPARGKALVPTDLSIAIPEGTYARIAPRSGLAWKHSIDVGAGVIDA 94

                          90       100
                  ....*....|....*....|...
gi 1464307100  89 DYRGNIHVLLFNLSNEDFHIKQG 111
Cdd:PLN02547   95 DYRGPVGVILFNHSDVDFEVKVG 117
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 11-111 1.77e-39

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: 128.60  E-value: 1.77e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464307100  11 LKVKLLSANAKVPLRATEGAAGYDLFAA--SSLLLPANTRKLIPIDIALEIPDGHYGRIAPRSGLSVRHGIMVG--AGVV 86
Cdd:COG0756     2 VKIKRLDEDAPLPAYATPGSAGLDLRAAldEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLLnsPGTI 81

                          90       100
                  ....*....|....*....|....*
gi 1464307100  87 DCDYRGNIHVLLFNLSNEDFHIKQG 111
Cdd:COG0756    82 DSDYRGEIKVILINLGDEPFTIERG 106
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 18-115 1.77e-34

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 115.46  E-value: 1.77e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464307100  18 ANAKVPLRATEGAAGYDLFAASSLLLPANTRKLIPIDIALEIPDGHYGRIAPRSGLSVRHGIMVGaGVVDCDYRGNIHVL 97
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAKGLIVVP-GVIDSDYRGEVKVV 79

                          90
                  ....*....|....*...
gi 1464307100  98 LFNLSNEDFHIKQGVSIC 115
Cdd:pfam00692  80 LFNLGKSDFTIKKGDRIA 97
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 31-115 4.22e-27

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: 95.64  E-value: 4.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464307100  31 AGYDLFAAS---SLLLPANTRKLIPIDIALEIPDGHYGRIAPRSGLSvRHGIMVG-AGVVDCDYRGNIHVLLFNLSNEDF 106
Cdd:cd07557     1 AGYDLRLGEdfeGIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLA-RKGITVHnAGVIDPGYRGEITLELYNLGPEPV 79


                  ....*....
gi 1464307100 107 HIKQGVSIC 115
Cdd:cd07557    80 VIKKGDRIA 88
 
Name Accession Description Interval E-value
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 11-115 1.88e-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: 1.88e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464307100  11 LKVKLLSANAKVPLRATEGAAGYDLFAASSLLLPANTRKLIPIDIALEIPDGHYGRIAPRSGLSVRHGIMV--GAGVVDC 88
Cdd:TIGR00576   2 LKFVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGVTIdnSPGVIDA 81

                          90       100
                  ....*....|....*....|....*..
gi 1464307100  89 DYRGNIHVLLFNLSNEDFHIKQGVSIC 115
Cdd:TIGR00576  82 DYRGEIKVILINLGKEDFTVKKGDRIA 108
PLN02547 PLN02547
dUTP pyrophosphatase
 9-111 1.46e-44

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 142.24  E-value: 1.46e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464307100   9 QLLKVKLLSANAKVPLRATEGAAGYDLFAASSLLLPANTRKLIPIDIALEIPDGHYGRIAPRSGLSVRHGIMVGAGVVDC 88
Cdd:PLN02547   15 PLLRVKKLSEKATLPSRGSALAAGYDLSSAYDTVVPARGKALVPTDLSIAIPEGTYARIAPRSGLAWKHSIDVGAGVIDA 94

                          90       100
                  ....*....|....*....|...
gi 1464307100  89 DYRGNIHVLLFNLSNEDFHIKQG 111
Cdd:PLN02547   95 DYRGPVGVILFNHSDVDFEVKVG 117
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 11-111 1.77e-39

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: 128.60  E-value: 1.77e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464307100  11 LKVKLLSANAKVPLRATEGAAGYDLFAA--SSLLLPANTRKLIPIDIALEIPDGHYGRIAPRSGLSVRHGIMVG--AGVV 86
Cdd:COG0756     2 VKIKRLDEDAPLPAYATPGSAGLDLRAAldEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLLnsPGTI 81

                          90       100
                  ....*....|....*....|....*
gi 1464307100  87 DCDYRGNIHVLLFNLSNEDFHIKQG 111
Cdd:COG0756    82 DSDYRGEIKVILINLGDEPFTIERG 106
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 11-114 1.76e-38

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 127.02  E-value: 1.76e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464307100  11 LKVKLLSANAKVPLRATEGAAGYDLFAASSLLLPANTRKLIPIDIALEIPDGHYGRIAPRSGLSVRHGIMVGAGVVDCDY 90
Cdd:PHA02703   14 LRVVRLSPNATIPTRGSPGAAGLDLCSACDCIVPAGCRCVVFTDLLIKLPDGCYGRIAPRSGLAVKHFIDVGAGVIDADY 93

                          90       100
                  ....*....|....*....|....
gi 1464307100  91 RGNIHVLLFNLSNEDFHIKQGVSI 114
Cdd:PHA02703   94 RGNVGVVLFNFGHNDFEVKKGDRI 117
PHA03094 PHA03094
dUTPase; Provisional
 11-114 1.82e-37

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 123.72  E-value: 1.82e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464307100  11 LKVKLLSANAKVPLRATEGAAGYDLFAASSLLLPANTRKLIPIDIALEIPDGHYGRIAPRSGLSVRHGIMVGAGVVDCDY 90
Cdd:PHA03094    6 VRCVKLSNFAKIPTRSSPKSAGYDLYSAYDYTVPPKERILVKTDISLSIPKFCYGRIAPRSGLSLNYGIDIGGGVIDEDY 85

                          90       100
                  ....*....|....*....|....
gi 1464307100  91 RGNIHVLLFNLSNEDFHIKQGVSI 114
Cdd:PHA03094   86 RGNIGVIFINNGKCTFNIKTGDRI 109
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 18-115 1.77e-34

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 115.46  E-value: 1.77e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464307100  18 ANAKVPLRATEGAAGYDLFAASSLLLPANTRKLIPIDIALEIPDGHYGRIAPRSGLSVRHGIMVGaGVVDCDYRGNIHVL 97
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAKGLIVVP-GVIDSDYRGEVKVV 79

                          90
                  ....*....|....*...
gi 1464307100  98 LFNLSNEDFHIKQGVSIC 115
Cdd:pfam00692  80 LFNLGKSDFTIKKGDRIA 97
dut PRK00601
dUTP diphosphatase;
11-111 9.17e-32

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 109.48  E-value: 9.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464307100  11 LKVKLLSANAKVPL--RATEGAAGYDLFAA--SSLLLPANTRKLIPIDIALEIPDGHYGRIAPRSGLSVRHGIMVG--AG 84
Cdd:PRK00601    6 VKILDPRLGKEFPLpaYATEGSAGLDLRACldEPVTLAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIVLGnlPG 85

                          90       100
                  ....*....|....*....|....*..
gi 1464307100  85 VVDCDYRGNIHVLLFNLSNEDFHIKQG 111
Cdd:PRK00601   86 TIDSDYRGELKVSLWNRGQEPFTIEPG 112
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 31-115 4.22e-27

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: 95.64  E-value: 4.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464307100  31 AGYDLFAAS---SLLLPANTRKLIPIDIALEIPDGHYGRIAPRSGLSvRHGIMVG-AGVVDCDYRGNIHVLLFNLSNEDF 106
Cdd:cd07557     1 AGYDLRLGEdfeGIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLA-RKGITVHnAGVIDPGYRGEITLELYNLGPEPV 79


                  ....*....
gi 1464307100 107 HIKQGVSIC 115
Cdd:cd07557    80 VIKKGDRIA 88
dut PRK13956
dUTP diphosphatase;
22-93 7.91e-06

dUTP diphosphatase;


Pssm-ID: 184417 [Multi-domain]  Cd Length: 147  Bit Score: 42.09  E-value: 7.91e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1464307100  22 VPLRATEGAAGYDLFAASSLLLPANTRKLIPIDIALEIPDGHYGRIAPRSGLSVRHGIMV--GAGVVDCDYRGN 93
Cdd:PRK13956   18 LPKRETAHAAGYDLKVAERTVIAPGEIKLVPTGVKAYMQPGEVLYLYDRSSNPRKKGLVLinSVGVIDGDYYGN 91
Dcd COG0717
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ...
 57-118 1.50e-05

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


Pssm-ID: 440481  Cd Length: 180  Bit Score: 41.73  E-value: 1.50e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1464307100  57 LEIPDGHYGRIAPRSGLSvRHGIMVG--AGVVDCDYRGNIHVLLFNLSNEDFHIKQGVSIC---FFK 118
Cdd:COG0717    86 VRLPDDLVAFLEGRSSLA-RLGLFVHttAGVIDPGFEGRITLELSNTGPLPIKLYPGMRIAqlvFFR 151
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 28-111 9.12e-04

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 36.64  E-value: 9.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464307100  28 EGAAGYDLFAASSLLLPANTRKLIPIDIALEIPDGHYGR---------IAPRSGLS---VRHGIMVGagVVDCDYRGNIH 95
Cdd:PTZ00143   24 EGDSGLDLFIVKDQTIKPGETAFIKLGIKAAAFQKDEDGsdgknvswlLFPRSSISktpLRLANSIG--LIDAGYRGELI 101

                          90
                  ....*....|....*.
gi 1464307100  96 VLLFNLSNEDFHIKQG 111
Cdd:PTZ00143  102 AAVDNIKDEPYTIKKG 117
PHA03131 PHA03131
dUTPase; Provisional
 31-115 7.67e-03

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 34.58  E-value: 7.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464307100  31 AGYDLFAASSLLLPANTRKLIPIDIALEIPDGHYGRIA-PRSGLSVRhGIMVGAgvvdCDYRGN-IHVLLFNLSNEDFHI 108
Cdd:PHA03131  133 AGFDVSLPQDLVIFPTTTFTFTLSLCCPPISPHFVPVIfGRSGLASK-GLTVKP----TKWRRSgLQLKLYNYTDETIFL 207


                  ....*..
gi 1464307100 109 KQGVSIC 115
Cdd:PHA03131  208 PAGSRIC 214
dCTP_deam TIGR02274
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ...
 57-115 8.13e-03

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: 34.21  E-value: 8.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1464307100  57 LEIPDGHYGRIAPRSGLSvRHGIM--VGAGVVDCDYRGNIHVLLFNLSNEDFHIKQGVSIC 115
Cdd:TIGR02274  87 VKLPDDVVGFLEGRSSLA-RLGLFihVTAGRIDPGFEGNITLELFNAGKLPVKLRPGMRIA 146
 
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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