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Conserved domains on  [gi|691139852|ref|WP_032053248|]
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MULTISPECIES: SMP-30/gluconolactonase/LRE family protein [Acinetobacter]

Protein Classification

SMP-30/gluconolactonase/LRE family protein( domain architecture ID 11465288)

SMP-30/gluconolactonase/LRE family protein similar to Staphylococcus lactonase drp35 and Zymomonas mobilis gluconolactonase, which hydrolyzes the gluconolactone formed by glucose-fructose oxidoreductase to form gluconate;

CATH:  2.120.10.30
EC:  3.1.1.-
Gene Ontology:  GO:0005515|GO:0046872|GO:0016787
PubMed:  9868369
SCOP:  4003251

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
26-333 2.63e-40

Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


:

Pssm-ID: 442613 [Multi-domain]  Cd Length: 266  Bit Score: 142.34  E-value: 2.63e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852  26 PECIIAQPDHSLWVADARGG-VMHIDAQGQQTliapeievqedasfeDRYVKAQGasLPNGMAMTDEGDFIICNWGlDRI 104
Cdd:COG3386   10 GEGPVWDPDGRLYWVDIPGGrIHRYDPDGGAV---------------EVFAEPSG--RPNGLAFDPDGRLLVADHG-RGL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852 105 EKLHKNTAQVEVLYDQLnGQPLGKTNFPLIDSKGRIWFTVTTTMQPwtesinsdelDGYIGVIDENG-IRVVAEQLGGAN 183
Cdd:COG3386   72 VRFDPADGEVTVLADEY-GKPLNRPNDGVVDPDGRLYFTDMGEYLP----------TGALYRVDPDGsLRVLADGLTFPN 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852 184 EIRFDDNEEWLYVVESNVRRITRFRVVDDATLSDREV-YGPEELEGFPDGFAFDVYGNLWVTLVMVDKLIAITPEQEVVT 262
Cdd:COG3386  141 GIAFSPDGRTLYVADTGAGRIYRFDLDADGTLGNRRVfADLPDGPGGPDGLAVDADGNLWVALWGGGGVVRFDPDGELLG 220
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 691139852 263 ILDDShpeanarlnqhyktktltpeimqasrgklAPWMASITFGGADLKTVYLGSLQGTRIPF----FRSPVAGQ 333
Cdd:COG3386  221 RIELP-----------------------------ERRPTNVAFGGPDLRTLYVTTARSLPLAGalfrVRVDVPGL 266
 
Name Accession Description Interval E-value
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
26-333 2.63e-40

Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442613 [Multi-domain]  Cd Length: 266  Bit Score: 142.34  E-value: 2.63e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852  26 PECIIAQPDHSLWVADARGG-VMHIDAQGQQTliapeievqedasfeDRYVKAQGasLPNGMAMTDEGDFIICNWGlDRI 104
Cdd:COG3386   10 GEGPVWDPDGRLYWVDIPGGrIHRYDPDGGAV---------------EVFAEPSG--RPNGLAFDPDGRLLVADHG-RGL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852 105 EKLHKNTAQVEVLYDQLnGQPLGKTNFPLIDSKGRIWFTVTTTMQPwtesinsdelDGYIGVIDENG-IRVVAEQLGGAN 183
Cdd:COG3386   72 VRFDPADGEVTVLADEY-GKPLNRPNDGVVDPDGRLYFTDMGEYLP----------TGALYRVDPDGsLRVLADGLTFPN 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852 184 EIRFDDNEEWLYVVESNVRRITRFRVVDDATLSDREV-YGPEELEGFPDGFAFDVYGNLWVTLVMVDKLIAITPEQEVVT 262
Cdd:COG3386  141 GIAFSPDGRTLYVADTGAGRIYRFDLDADGTLGNRRVfADLPDGPGGPDGLAVDADGNLWVALWGGGGVVRFDPDGELLG 220
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 691139852 263 ILDDShpeanarlnqhyktktltpeimqasrgklAPWMASITFGGADLKTVYLGSLQGTRIPF----FRSPVAGQ 333
Cdd:COG3386  221 RIELP-----------------------------ERRPTNVAFGGPDLRTLYVTTARSLPLAGalfrVRVDVPGL 266
SGL pfam08450
SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in ...
83-317 6.22e-19

SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in proteins expressed by a variety of eukaryotic and prokaryotic species. These proteins include various enzymes, such as senescence marker protein 30 (SMP-30), gluconolactonase and luciferin-regenerating enzyme (LRE). SMP-30 is known to hydrolyse diisopropyl phosphorofluoridate in the liver, and has been noted as having sequence similarity, in the region described in this family, with PON1 and LRE.


Pssm-ID: 462480 [Multi-domain]  Cd Length: 246  Bit Score: 84.62  E-value: 6.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852   83 PNGM-AMTDEGDFIICNwgLDRIEKLHKNTAQVEVLYDQLNGQPLGKT-NFPLIDSKGRIWFTvttTMQpwtESINSDEL 160
Cdd:pfam08450  42 PVGAiAPRDDGGLIVAL--KDGVALLDLATGELTPLADPEDDDWPLNRfNDGKVDPDGRFWFG---TMG---DDEAPGGD 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852  161 DGYIGVIDENG-IRVVAEQLGGANEIRFDDNEEWLYVVESNVRRITRFRVVDDATLSD--REVYGPEELEGFPDGFAFDV 237
Cdd:pfam08450 114 PGALYRLDPDGkLTRVLDGLTISNGLAWSPDGRTLYFADSPARKIWAYDYDLDGGLISnrRVFADFKPGLGRPDGMAVDA 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852  238 YGNLWVTLVMVDKLIAITPEQEVVTILDdshpeanarlnqhyktktlTPeimqasrgklAPWMASITFGGADLKTVYLGS 317
Cdd:pfam08450 194 EGNVWVARWGGGKVVRFDPDGKLLREIE-------------------LP----------AKRPTSCAFGGPDLRTLYVTS 244
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
23-244 1.33e-07

NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.


Pssm-ID: 271320 [Multi-domain]  Cd Length: 269  Bit Score: 51.94  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852  23 LQRPECIIAQPDHSLWVADARGG-VMHIDAQGQQTliapeIEVQEDASFEDRYvkaqgaSLPNGMAMTDEGDFIICNWGL 101
Cdd:cd05819    7 LNNPQGIAVDSSGNIYVADTGNNrIQVFDPDGNFI-----TSFGSFGSGDGQF------NEPAGVAVDSDGNLYVADTGN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852 102 DRIEKLHKNTAQVEVLydQLNGQPLGKTNFPL---IDSKGRIWftVTTTMQPWTESINSDelDGYIGVIDENGirVVAEQ 178
Cdd:cd05819   76 HRIQKFDPDGNFLASF--GGSGDGDGEFNGPRgiaVDSSGNIY--VADTGNHRIQKFDPD--GEFLTTFGSGG--SGPGQ 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 691139852 179 LGGANEIRFDDNEEwLYVVESNVRRITRFRVVDDATLS-DREVYGPEELeGFPDGFAFDVYGNLWVT 244
Cdd:cd05819  148 FNGPTGVAVDSDGN-IYVADTGNHRIQVFDPDGNFLTTfGSTGTGPGQF-NYPTGIAVDSDGNIYVA 212
 
Name Accession Description Interval E-value
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
26-333 2.63e-40

Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442613 [Multi-domain]  Cd Length: 266  Bit Score: 142.34  E-value: 2.63e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852  26 PECIIAQPDHSLWVADARGG-VMHIDAQGQQTliapeievqedasfeDRYVKAQGasLPNGMAMTDEGDFIICNWGlDRI 104
Cdd:COG3386   10 GEGPVWDPDGRLYWVDIPGGrIHRYDPDGGAV---------------EVFAEPSG--RPNGLAFDPDGRLLVADHG-RGL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852 105 EKLHKNTAQVEVLYDQLnGQPLGKTNFPLIDSKGRIWFTVTTTMQPwtesinsdelDGYIGVIDENG-IRVVAEQLGGAN 183
Cdd:COG3386   72 VRFDPADGEVTVLADEY-GKPLNRPNDGVVDPDGRLYFTDMGEYLP----------TGALYRVDPDGsLRVLADGLTFPN 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852 184 EIRFDDNEEWLYVVESNVRRITRFRVVDDATLSDREV-YGPEELEGFPDGFAFDVYGNLWVTLVMVDKLIAITPEQEVVT 262
Cdd:COG3386  141 GIAFSPDGRTLYVADTGAGRIYRFDLDADGTLGNRRVfADLPDGPGGPDGLAVDADGNLWVALWGGGGVVRFDPDGELLG 220
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 691139852 263 ILDDShpeanarlnqhyktktltpeimqasrgklAPWMASITFGGADLKTVYLGSLQGTRIPF----FRSPVAGQ 333
Cdd:COG3386  221 RIELP-----------------------------ERRPTNVAFGGPDLRTLYVTTARSLPLAGalfrVRVDVPGL 266
SGL pfam08450
SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in ...
83-317 6.22e-19

SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in proteins expressed by a variety of eukaryotic and prokaryotic species. These proteins include various enzymes, such as senescence marker protein 30 (SMP-30), gluconolactonase and luciferin-regenerating enzyme (LRE). SMP-30 is known to hydrolyse diisopropyl phosphorofluoridate in the liver, and has been noted as having sequence similarity, in the region described in this family, with PON1 and LRE.


Pssm-ID: 462480 [Multi-domain]  Cd Length: 246  Bit Score: 84.62  E-value: 6.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852   83 PNGM-AMTDEGDFIICNwgLDRIEKLHKNTAQVEVLYDQLNGQPLGKT-NFPLIDSKGRIWFTvttTMQpwtESINSDEL 160
Cdd:pfam08450  42 PVGAiAPRDDGGLIVAL--KDGVALLDLATGELTPLADPEDDDWPLNRfNDGKVDPDGRFWFG---TMG---DDEAPGGD 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852  161 DGYIGVIDENG-IRVVAEQLGGANEIRFDDNEEWLYVVESNVRRITRFRVVDDATLSD--REVYGPEELEGFPDGFAFDV 237
Cdd:pfam08450 114 PGALYRLDPDGkLTRVLDGLTISNGLAWSPDGRTLYFADSPARKIWAYDYDLDGGLISnrRVFADFKPGLGRPDGMAVDA 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852  238 YGNLWVTLVMVDKLIAITPEQEVVTILDdshpeanarlnqhyktktlTPeimqasrgklAPWMASITFGGADLKTVYLGS 317
Cdd:pfam08450 194 EGNVWVARWGGGKVVRFDPDGKLLREIE-------------------LP----------AKRPTSCAFGGPDLRTLYVTS 244
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
17-261 4.32e-11

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 62.34  E-value: 4.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852  17 QFIGQDLQRPECIIAQPDHSLWVADARGG-VMHIDAqgqqtliapeievqEDASFEdRYVKAQGASLPNGMAMTDEGDFI 95
Cdd:COG4257   52 EYPLGGGSGPHGIAVDPDGNLWFTDNGNNrIGRIDP--------------KTGEIT-TFALPGGGSNPHGIAFDPDGNLW 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852  96 ICNWGLDRIEKLHKNTAQV-EVLYDQLNGQPLGKTnfplIDSKGRIWFTvtttmqpwtesinsDELDGYIGVID-ENG-I 172
Cdd:COG4257  117 FTDQGGNRIGRLDPATGEVtEFPLPTGGAGPYGIA----VDPDGNLWVT--------------DFGANAIGRIDpDTGtL 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852 173 RVVA--EQLGGANEIRFDDNEeWLYVVESNVRRITRFrvvDDATLSDREVYGPEeLEGFPDGFAFDVYGNLWVTLVMVDK 250
Cdd:COG4257  179 TEYAlpTPGAGPRGLAVDPDG-NLWVADTGSGRIGRF---DPKTGTVTEYPLPG-GGARPYGVAVDGDGRVWFAESGANR 253
                        250
                 ....*....|.
gi 691139852 251 LIAITPEQEVV 261
Cdd:COG4257  254 IVRFDPDTELT 264
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
23-244 1.33e-07

NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.


Pssm-ID: 271320 [Multi-domain]  Cd Length: 269  Bit Score: 51.94  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852  23 LQRPECIIAQPDHSLWVADARGG-VMHIDAQGQQTliapeIEVQEDASFEDRYvkaqgaSLPNGMAMTDEGDFIICNWGL 101
Cdd:cd05819    7 LNNPQGIAVDSSGNIYVADTGNNrIQVFDPDGNFI-----TSFGSFGSGDGQF------NEPAGVAVDSDGNLYVADTGN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852 102 DRIEKLHKNTAQVEVLydQLNGQPLGKTNFPL---IDSKGRIWftVTTTMQPWTESINSDelDGYIGVIDENGirVVAEQ 178
Cdd:cd05819   76 HRIQKFDPDGNFLASF--GGSGDGDGEFNGPRgiaVDSSGNIY--VADTGNHRIQKFDPD--GEFLTTFGSGG--SGPGQ 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 691139852 179 LGGANEIRFDDNEEwLYVVESNVRRITRFRVVDDATLS-DREVYGPEELeGFPDGFAFDVYGNLWVT 244
Cdd:cd05819  148 FNGPTGVAVDSDGN-IYVADTGNHRIQVFDPDGNFLTTfGSTGTGPGQF-NYPTGIAVDSDGNIYVA 212
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
74-274 2.07e-05

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 45.40  E-value: 2.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852  74 YVKAQGASLPNGMAMTDEGDFIICNWGLDRIEKLHKNTAQVEVLYDQLNGQPLGKTnfplIDSKGRIWFTvtttmqpwte 153
Cdd:COG4257   10 YPVPAPGSGPRDVAVDPDGAVWFTDQGGGRIGRLDPATGEFTEYPLGGGSGPHGIA----VDPDGNLWFT---------- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852 154 sinsDELDGYIGVID--ENGIRVVA--EQLGGANEIRFDDNEEwLYVVESNVRRITRFrvvDDATLSDREVYGPEElEGF 229
Cdd:COG4257   76 ----DNGNNRIGRIDpkTGEITTFAlpGGGSNPHGIAFDPDGN-LWFTDQGGNRIGRL---DPATGEVTEFPLPTG-GAG 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 691139852 230 PDGFAFDVYGNLWVTLVMVDKLIAITPEQEVVTILDDSHPEANAR 274
Cdd:COG4257  147 PYGIAVDPDGNLWVTDFGANAIGRIDPDTGTLTEYALPTPGAGPR 191
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
22-207 8.36e-03

NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.


Pssm-ID: 271320 [Multi-domain]  Cd Length: 269  Bit Score: 37.30  E-value: 8.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852  22 DLQRPECIIAQPDHSLWVADARGGVMH-IDAQGQQTLIAPEiEVQEDASFEDryvkaqgaslPNGMAMTDEGDFIICNWG 100
Cdd:cd05819  100 EFNGPRGIAVDSSGNIYVADTGNHRIQkFDPDGEFLTTFGS-GGSGPGQFNG----------PTGVAVDSDGNIYVADTG 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691139852 101 LDRIEKLHKNTAQVEVLYDQlnGQPLGKTNFPL---IDSKGRIWFtvtttmqpwTESINS--DELDGYIGVIDENG-IRV 174
Cdd:cd05819  169 NHRIQVFDPDGNFLTTFGST--GTGPGQFNYPTgiaVDSDGNIYV---------ADSGNNrvQVFDPDGAGFGGNGnFLG 237
                        170       180       190
                 ....*....|....*....|....*....|...
gi 691139852 175 VAEQLGGANEIRFDDNeEWLYVVESNVRRITRF 207
Cdd:cd05819  238 SDGQFNRPSGLAVDSD-GNLYVADTGNNRIQVF 269
 
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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