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Conserved domains on  [gi|197100526|ref|NP_001124537|]
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Rieske domain-containing protein isoform 1 [Homo sapiens]

Protein Classification

Rieske (2Fe-2S) protein( domain architecture ID 10005408)

Rieske (2Fe-2S) protein contains a [2Fe-2S] cluster, which is involved in electron transfer, and is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs

CATH:  2.102.10.10
Gene Ontology:  GO:0051537|GO:0046872

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 69-187 4.46e-20

Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 441749 [Multi-domain]  Cd Length: 103  Bit Score: 81.04  E-value: 4.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100526  69 SSVCVGREDDIKKSERMTAVVHDREVVIFYHKGEYHAMDIRCYHSGGPLHLGDIEDFdgrpCIVCPWHKYKITLATGEGL 148
Cdd:COG2146    2 SEVKVCALDDLPEGGGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLSEGIVDGG----VVTCPLHGARFDLRTGECL 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 197100526 149 yqsinpKDPSAKPkwcskgikQRIHTVTVDNGNIYVTLS 187
Cdd:COG2146   78 ------GGPATEP--------LKTYPVRVEDGDVYVDLP 102
 
Name Accession Description Interval E-value
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 69-187 4.46e-20

Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441749 [Multi-domain]  Cd Length: 103  Bit Score: 81.04  E-value: 4.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100526  69 SSVCVGREDDIKKSERMTAVVHDREVVIFYHKGEYHAMDIRCYHSGGPLHLGDIEDFdgrpCIVCPWHKYKITLATGEGL 148
Cdd:COG2146    2 SEVKVCALDDLPEGGGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLSEGIVDGG----VVTCPLHGARFDLRTGECL 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 197100526 149 yqsinpKDPSAKPkwcskgikQRIHTVTVDNGNIYVTLS 187
Cdd:COG2146   78 ------GGPATEP--------LKTYPVRVEDGDVYVDLP 102
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 71-149 6.37e-20

Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron oxygenase (RO) systems such as naphthalene and biphenyl dioxygenases, as well as in plant/cyanobacterial chloroplast b6f and mitochondrial cytochrome bc(1) complexes. The Rieske domain can be divided into two subdomains, with an incomplete six-stranded, antiparallel beta-barrel at one end, and an iron-sulfur cluster binding subdomain at the other. The Rieske iron-sulfur center contains a [2Fe-2S] cluster, which is involved in electron transfer, and is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In RO systems, the N-terminal Rieske domain of the alpha subunit acts as an electron shuttle that accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron in the alpha subunit C-terminal domain to be used for catalysis.


Pssm-ID: 239550 [Multi-domain]  Cd Length: 98  Bit Score: 80.61  E-value: 6.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100526  71 VCVGREDDIKKSERMTAVVHDREVVIFYHK-GEYHAMDIRCYHSGGPLHLGDIEDfdgrPCIVCPWHKYKITLATGEGLY 149
Cdd:cd03467    2 VVVGALSELPPGGGRVVVVGGGPVVVVRREgGEVYALSNRCTHQGCPLSEGEGED----GCIVCPCHGSRFDLRTGEVVS 77
Rieske_2 pfam13806
Rieske-like [2Fe-2S] domain;
71-184 4.03e-10

Rieske-like [2Fe-2S] domain;


Pssm-ID: 433491 [Multi-domain]  Cd Length: 103  Bit Score: 54.87  E-value: 4.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100526   71 VCVGREDDIKKSERMTAVVHDREVVIF-YHKGEYHAMDIRCYHSG-GPLHLGDIEDFDGRPCIVCPWHKYKITLATGEGL 148
Cdd:pfam13806   2 TPVCALDDLPPGTGVCALVGGRQVAVFrLEDGQVYAIDNRDPFSGaNVLSRGIVGDLGGELVVASPLYKQHFDLKTGECL 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 197100526  149 yqsinpKDPSakpkwcskgIKQRIHTVTVDNGNIYV 184
Cdd:pfam13806  82 ------EDPE---------VSVPVYPVRVRDGNVEV 102
PRK09965 PRK09965
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional
 88-189 2.86e-08

3-phenylpropionate dioxygenase ferredoxin subunit; Provisional


Pssm-ID: 170182 [Multi-domain]  Cd Length: 106  Bit Score: 50.16  E-value: 2.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100526  88 VVHDREVVIFYHKGEYHAMDIRCYHSGGPLHLGDIEDfdgrPCIV-CPWHKYKITLATGEglyqsinPKDPSAKpkwcsk 166
Cdd:PRK09965  20 VDTSPVIALFNVGGEFYAIDDRCSHGNASLSEGYLED----DATVeCPLHAASFCLRTGK-------ALCLPAT------ 82

                         90       100
                 ....*....|....*....|...
gi 197100526 167 gIKQRIHTVTVDNGNIYVTLSNE 189
Cdd:PRK09965  83 -DPLRTYPVHVEGGDIFIDLPEA 104
 
Name Accession Description Interval E-value
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 69-187 4.46e-20

Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441749 [Multi-domain]  Cd Length: 103  Bit Score: 81.04  E-value: 4.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100526  69 SSVCVGREDDIKKSERMTAVVHDREVVIFYHKGEYHAMDIRCYHSGGPLHLGDIEDFdgrpCIVCPWHKYKITLATGEGL 148
Cdd:COG2146    2 SEVKVCALDDLPEGGGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLSEGIVDGG----VVTCPLHGARFDLRTGECL 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 197100526 149 yqsinpKDPSAKPkwcskgikQRIHTVTVDNGNIYVTLS 187
Cdd:COG2146   78 ------GGPATEP--------LKTYPVRVEDGDVYVDLP 102
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 71-149 6.37e-20

Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron oxygenase (RO) systems such as naphthalene and biphenyl dioxygenases, as well as in plant/cyanobacterial chloroplast b6f and mitochondrial cytochrome bc(1) complexes. The Rieske domain can be divided into two subdomains, with an incomplete six-stranded, antiparallel beta-barrel at one end, and an iron-sulfur cluster binding subdomain at the other. The Rieske iron-sulfur center contains a [2Fe-2S] cluster, which is involved in electron transfer, and is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In RO systems, the N-terminal Rieske domain of the alpha subunit acts as an electron shuttle that accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron in the alpha subunit C-terminal domain to be used for catalysis.


Pssm-ID: 239550 [Multi-domain]  Cd Length: 98  Bit Score: 80.61  E-value: 6.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100526  71 VCVGREDDIKKSERMTAVVHDREVVIFYHK-GEYHAMDIRCYHSGGPLHLGDIEDfdgrPCIVCPWHKYKITLATGEGLY 149
Cdd:cd03467    2 VVVGALSELPPGGGRVVVVGGGPVVVVRREgGEVYALSNRCTHQGCPLSEGEGED----GCIVCPCHGSRFDLRTGEVVS 77
Rieske_NirD_small_Bacillus cd03530
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar ...
 73-184 3.32e-14

Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar to the Bacillus subtilis small subunit of assimilatory nitrite reductase containing a Rieske domain. The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. Assimilatory nitrate and nitrite reductases convert nitrate through nitrite to ammonium.


Pssm-ID: 239606 [Multi-domain]  Cd Length: 98  Bit Score: 65.70  E-value: 3.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100526  73 VGREDDIKKSERMTAVVHDREVVIF-YHKGEYHAMDIRCYHSGGPLHLGDIEDfdgrPCIVCPWHKYKITLATGEGLYqs 151
Cdd:cd03530    4 IGALEDIPPRGARKVQTGGGEIAVFrTADDEVFALENRCPHKGGPLSEGIVHG----EYVTCPLHNWVIDLETGEAQG-- 77

                         90       100       110
                 ....*....|....*....|....*....|...
gi 197100526 152 inPKDPSAKPkwcskgikqriHTVTVDNGNIYV 184
Cdd:cd03530   78 --PDEGCVRT-----------FPVKVEDGRVYL 97
Rieske_AIFL_N cd03478
AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family ...
 73-183 2.94e-10

AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family show similarity to human AIFL, containing an N-terminal Rieske domain and a C-terminal pyridine nucleotide-disulfide oxidoreductase domain (Pyr_redox). The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. AIFL shares 35% homology with human AIF (apoptosis-inducing factor), mainly in the Pyr_redox domain. AIFL is predominantly localized to the mitochondria. AIFL induces apoptosis in a caspase-dependent manner.


Pssm-ID: 239560 [Multi-domain]  Cd Length: 95  Bit Score: 54.94  E-value: 2.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100526  73 VGREDDIKKSERMTAVVHDREVVIFYHKGEYHAMDIRCYHSGGPLHLGDIEdfDGRpcIVCPWHKYKITLATGEglyqSI 152
Cdd:cd03478    3 VCRLSDLGDGEMKEVDVGDGKVLLVRQGGEVHAIGAKCPHYGAPLAKGVLT--DGR--IRCPWHGACFNLRTGD----IE 74

                         90       100       110
                 ....*....|....*....|....*....|.
gi 197100526 153 NPKDPSAKPKWcskgikqrihTVTVDNGNIY 183
Cdd:cd03478   75 DAPALDSLPCY----------EVEVEDGRVY 95
Rieske_2 pfam13806
Rieske-like [2Fe-2S] domain;
71-184 4.03e-10

Rieske-like [2Fe-2S] domain;


Pssm-ID: 433491 [Multi-domain]  Cd Length: 103  Bit Score: 54.87  E-value: 4.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100526   71 VCVGREDDIKKSERMTAVVHDREVVIF-YHKGEYHAMDIRCYHSG-GPLHLGDIEDFDGRPCIVCPWHKYKITLATGEGL 148
Cdd:pfam13806   2 TPVCALDDLPPGTGVCALVGGRQVAVFrLEDGQVYAIDNRDPFSGaNVLSRGIVGDLGGELVVASPLYKQHFDLKTGECL 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 197100526  149 yqsinpKDPSakpkwcskgIKQRIHTVTVDNGNIYV 184
Cdd:pfam13806  82 ------EDPE---------VSVPVYPVRVRDGNVEV 102
Rieske_RO_ferredoxin cd03528
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ...
 71-184 5.62e-10

Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the Rieske ferredoxin component of some three-component RO systems including biphenyl dioxygenase (BPDO) and carbazole 1,9a-dioxygenase (CARDO). The RO family comprise a large class of aromatic ring-hydroxylating dioxygenases found predominantly in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth. ROs consist of two or three components: reductase, oxygenase, and ferredoxin (in some cases) components. The ferredoxin component contains either a plant-type or Rieske-type [2Fe-2S] cluster. The Rieske ferredoxin component in this family carries an electron from the RO reductase component to the terminal RO oxygenase component. BPDO degrades biphenyls and polychlorinated biphenyls. BPDO ferredoxin (BphF) has structural features consistent with a minimal and perhaps archetypical Rieske protein in that the insertions that give other Rieske proteins unique structural features are missing. CARDO catalyzes dihydroxylation at the C1 and C9a positions of carbazole. Rieske ferredoxins are found as subunits of membrane oxidase complexes, cis-dihydrodiol-forming aromatic dioxygenases, bacterial assimilatory nitrite reductases, and arsenite oxidase. Rieske ferredoxins are also found as soluble electron carriers in bacterial dioxygenase and monooxygenase complexes.


Pssm-ID: 239604 [Multi-domain]  Cd Length: 98  Bit Score: 54.42  E-value: 5.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100526  71 VCVGREDDIKKSERMTAVVHDREVVIFYHKGEYHAMDIRCYHSGGPLHLGDIEDFdgrpCIVCPWHKYKITLATGEglyq 150
Cdd:cd03528    2 VRVCAVDELPEGEPKRVDVGGRPIAVYRVDGEFYATDDLCTHGDASLSEGYVEGG----VIECPLHGGRFDLRTGK---- 73

                         90       100       110
                 ....*....|....*....|....*....|....
gi 197100526 151 sinpkdPSAKPkwCSKGIKqrIHTVTVDNGNIYV 184
Cdd:cd03528   74 ------ALSLP--ATEPLK--TYPVKVEDGDVYV 97
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 71-137 4.27e-09

Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines coordinate one Fe ion, while the other Fe ion is coordinated by two conserved histidines. In hyperthermophilic archaea there is a SKTPCX(2-3)C motif at the C-terminus. The cysteines in this motif form a disulphide bridge, which stabilizes the protein.


Pssm-ID: 425632 [Multi-domain]  Cd Length: 89  Bit Score: 51.58  E-value: 4.27e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 197100526   71 VCVGREDDIKKSERMTAVVHDREVVIF-YHKGEYHAMDIRCYHSGGPLHLGDIedfDGRPCIVCPWHK 137
Cdd:pfam00355   3 YPVCHSSELPEGEPKVVEVGGEPLVVFrDEDGELYALEDRCPHRGAPLSEGKV---NGGGRLECPYHG 67
PRK09965 PRK09965
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional
 88-189 2.86e-08

3-phenylpropionate dioxygenase ferredoxin subunit; Provisional


Pssm-ID: 170182 [Multi-domain]  Cd Length: 106  Bit Score: 50.16  E-value: 2.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100526  88 VVHDREVVIFYHKGEYHAMDIRCYHSGGPLHLGDIEDfdgrPCIV-CPWHKYKITLATGEglyqsinPKDPSAKpkwcsk 166
Cdd:PRK09965  20 VDTSPVIALFNVGGEFYAIDDRCSHGNASLSEGYLED----DATVeCPLHAASFCLRTGK-------ALCLPAT------ 82

                         90       100
                 ....*....|....*....|...
gi 197100526 167 gIKQRIHTVTVDNGNIYVTLSNE 189
Cdd:PRK09965  83 -DPLRTYPVHVEGGDIFIDLPEA 104
Rieske_NirD cd03529
Assimilatory nitrite reductase (NirD) family, Rieske domain; Assimilatory nitrate and nitrite ...
 73-184 7.73e-06

Assimilatory nitrite reductase (NirD) family, Rieske domain; Assimilatory nitrate and nitrite reductases convert nitrate through nitrite to ammonium. Members include bacterial and fungal proteins. The bacterial NirD contains a single Rieske domain while fungal proteins have a C-terminal Rieske domain in addition to several other domains. The fungal NirD is involved in nutrient acquisition, functioning at the soil/fungus interface to control nutrient exchange between the fungus and the host plant. The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. The Rieske [2Fe-2S] cluster is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In this family, only a few members contain these residues. Other members may have lost the ability to bind the Rieske [2Fe-2S] cluster.


Pssm-ID: 239605 [Multi-domain]  Cd Length: 103  Bit Score: 43.27  E-value: 7.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100526  73 VGREDDIKKSERMTAVVHDREVVIFY-HKGEYHAMDIRCYHSGGP-LHLGDIEDFDGRPCIVCPWHKYKITLATGEGLyq 150
Cdd:cd03529    4 VCALDDLPPGSGVAALVGDTQIAIFRlPGREVYAVQNMDPHSRANvLSRGIVGDIGGEPVVASPLYKQHFSLKTGRCL-- 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 197100526 151 sinpKDPSAKPKWcskgikqriHTVTVDNGNIYV 184
Cdd:cd03529   82 ----EDEDVSVAT---------FPVRVEDGEVYV 102
Rieske_CMP_Neu5Ac_hydrolase_N cd03473
Cytidine monophosphate-N-acetylneuraminic acid (CMP Neu5Ac) hydroxylase family, N-terminal ...
 92-156 1.39e-04

Cytidine monophosphate-N-acetylneuraminic acid (CMP Neu5Ac) hydroxylase family, N-terminal Rieske domain; The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. CMP Neu5Ac hydroxylase is the key enzyme for the synthesis of N-glycolylneuraminic acid (NeuGc) from N-acetylneuraminic acid (Neu5Ac), NeuGc and Neu5Ac are members of a family of cell surface sugars called sialic acids. All mammals except humans have both NeuGc variants on their cell surfaces. In humans, the gene encoding CMP Neu5Ac hydroxylase has a mutation within its coding region that abolishes NeuGc production.


Pssm-ID: 239555  Cd Length: 107  Bit Score: 39.78  E-value: 1.39e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 197100526  92 REVVIFYHKGEYHAMDIRCYHSGGpLHLGDIEDFDGRpCIVCPWHKYKITLATgeglYQSINPKD 156
Cdd:cd03473   31 KKYIIYKSKSELKACKNQCKHQGG-LFIKDIEDLDGR-TVRCTKHNWKLDVST----MKYVNPPD 89
Rieske_RO_Alpha_N cd03469
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ...
 71-136 2.12e-03

Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha subunit; The RO family comprise a large class of aromatic ring-hydroxylating dioxygenases found predominantly in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth. ROs consist of two or three components: reductase, oxygenase, and ferredoxin (in some cases) components. The oxygenase component may contain alpha and beta subunits, with the beta subunit having a purely structural function. Some oxygenase components contain only an alpha subunit. The oxygenase alpha subunit has two domains, an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from the reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. Reduced pyridine nucleotide is used as the initial source of two electrons for dioxygen activation.


Pssm-ID: 239551 [Multi-domain]  Cd Length: 118  Bit Score: 36.80  E-value: 2.12e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 197100526  71 VCVGREDDIKKSER-MTAVVHDREVVIFYHK-GEYHAMDIRCYHSGGPLHLGDIedfDGRPCIVCPWH 136
Cdd:cd03469    2 YFVGHSSELPEPGDyVTLELGGEPLVLVRDRdGEVRAFHNVCPHRGARLCEGRG---GNAGRLVCPYH 66
 
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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