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Conserved domains on  [gi|446818750|ref|WP_000896006|]
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MULTISPECIES: class II aldolase/adducin family protein [Bacillus]

Protein Classification

class II aldolase/adducin head domain-containing protein; L-fuculose-phosphate aldolase( domain architecture ID 10012807)

class II aldolase/adducin head domain-containing protein involved in catalyzing central steps of carbohydrate metabolism; it promotes carbon-carbon bond cleavage and stabilizes enolate intermediates using divalent cations| L-fuculose-phosphate aldolase catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and L-lactaldehyde; Also able to catalyze the reversible cleavage of D-ribulose 1-phosphate, but FucA has a higher affinity for L-fuculose 1-phosphate and L-lactaldehyde than for D-ribulose 1-phosphate and glycolaldehyde, respectively

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK06755 PRK06755
hypothetical protein; Validated
1-209 1.50e-148

hypothetical protein; Validated


:

Pssm-ID: 102532  Cd Length: 209  Bit Score: 410.96  E-value: 1.50e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750   1 MLFFLKKWNELKDVKSELALRDWFYGTKISLSLCTSKEPLTFLVNVEGRDKGLFSEEDFIVVNCMCESVFENEEKPAAES 80
Cdd:PRK06755   1 MLFFLKKWNELKDVKSELALRDWFYGTKISLSLCTSKEPLTFLVNVEGRDKGLFSEEDFIVVNCMCEPVFENEEKPAAES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750  81 FMHADIYKKSSAGCILQVQTVDSHLISELYGEEGEVTFDKRSVERVFGKEGITEMTIPIVEDEKKFADLLESNVPNFIEG 160
Cdd:PRK06755  81 FMHADIYKKSSAECILQVQTVDSHLISELYGEEGEVTFDKRSVERVFGKEGITEMTIPIVEDEKKFADLLENNVPNFIEG 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446818750 161 GGVVLVHNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKLLMIKGARSSVI 209
Cdd:PRK06755 161 GGVVLVHNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKLLMIKGAKSSVI 209
 
Name Accession Description Interval E-value
PRK06755 PRK06755
hypothetical protein; Validated
1-209 1.50e-148

hypothetical protein; Validated


Pssm-ID: 102532  Cd Length: 209  Bit Score: 410.96  E-value: 1.50e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750   1 MLFFLKKWNELKDVKSELALRDWFYGTKISLSLCTSKEPLTFLVNVEGRDKGLFSEEDFIVVNCMCESVFENEEKPAAES 80
Cdd:PRK06755   1 MLFFLKKWNELKDVKSELALRDWFYGTKISLSLCTSKEPLTFLVNVEGRDKGLFSEEDFIVVNCMCEPVFENEEKPAAES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750  81 FMHADIYKKSSAGCILQVQTVDSHLISELYGEEGEVTFDKRSVERVFGKEGITEMTIPIVEDEKKFADLLESNVPNFIEG 160
Cdd:PRK06755  81 FMHADIYKKSSAECILQVQTVDSHLISELYGEEGEVTFDKRSVERVFGKEGITEMTIPIVEDEKKFADLLENNVPNFIEG 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446818750 161 GGVVLVHNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKLLMIKGARSSVI 209
Cdd:PRK06755 161 GGVVLVHNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKLLMIKGAKSSVI 209
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
11-199 5.28e-31

methylthioribulose-1-phosphate dehydratase; Members of this family are the methylthioribulose-1-phosphate dehydratase of the methionine salvage pathway. This pathway allows methylthioadenosine, left over from polyamine biosynthesis, to be recycled to methionine. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 274521 [Multi-domain]  Cd Length: 192  Bit Score: 111.97  E-value: 5.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750   11 LKDVKSELALRDWFYGTKISLSLCTSkePLTFLVNVEGRDKGLFSEEDFIVVNcMCESVFENEEKPAAESFMHADIYKKS 90
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARLD--EDEILITPSGVDKGRLTPEDFLVVD-LQGKPVSGGLKPSAETLLHTQLYRLT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750   91 SAGCILQVQTVDSHLISELYGEEGEVTFDKRSVERVFgkEGIT----EMTIPIVEDEKKFADLLESnVPNFIEGG---GV 163
Cdd:TIGR03328  78 GAGAVLHTHSVEATVLSRLYPSNGGFELEGYEMLKGL--PGITthedTLVVPIIENTQDIARLADS-VAPALNAYpdvPG 154
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 446818750  164 VLVHNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKLL 199
Cdd:TIGR03328 155 VLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEML 190
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
10-205 4.66e-23

5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440005 [Multi-domain]  Cd Length: 208  Bit Score: 91.82  E-value: 4.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750  10 ELKDVKSELALRDWFYGTKISLSLCTSKEplTFLVNVEGRDKGLFSEEDFIVVNCMCESVfENEEKPAAESFMHADIYKK 89
Cdd:COG0235    9 ELAAAGRRLARRGLVDGTAGNISVRLDDD--RFLITPSGVDFGELTPEDLVVVDLDGNVV-EGDLKPSSETPLHLAIYRA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750  90 -SSAGCILQVQTVDSHLISELygeegEVTFDKRSVE--RVFGKEgitemtIPIVEDEKKFADLLESNVPNFIEGGGVVLV 166
Cdd:COG0235   86 rPDVGAVVHTHSPYATALSAL-----GEPLPPLEQTeaAAFLGD------VPVVPYAGPGTEELAEAIAEALGDRPAVLL 154
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446818750 167 HNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKLLMIKGAR 205
Cdd:COG0235  155 RNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGPL 193
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
17-191 5.44e-22

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 214970 [Multi-domain]  Cd Length: 185  Bit Score: 88.46  E-value: 5.44e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750    17 ELALRDWFYGTKISLSLCTsKEPLTFLVNVEGRDKGLFSEEDFIVVNCMCESVF-ENEEKPAAESFMHADIYKK-SSAGC 94
Cdd:smart01007   7 LLARRGLVEGTGGNISARV-GEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEgGGGPKPSSETPLHLAIYRArPDVGA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750    95 ILQVQTVDSHLISeLYGEEGEVTFDKRSVERVFGKEGITEMTIPIVEDEKKFADLLESNVPNFiEGGGVVLVHNYGMIVW 174
Cdd:smart01007  86 VVHTHSPYATALA-ALGKPLPLLPTEQAAAFLGGEIPYAPYAGPGTELAEEGAELAEALAEAL-PDRPAVLLRNHGLLVW 163
                          170
                   ....*....|....*..
gi 446818750   175 GKTPEEAKKWLEGIEYL 191
Cdd:smart01007 164 GKTLEEAFDLAEELEEA 180
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
17-191 2.50e-17

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 76.05  E-value: 2.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750   17 ELALRDWFYGT--KISLSLctskEPLTFLVNVEGRDKGLFSEEDFIVVNCMCESVfENEEKPAAESFMHADIYKK-SSAG 93
Cdd:pfam00596   9 LLARRGLVEGTggNISVRL----PGDGFLITPSGVDFGELTPEDLVVVDLDGNVV-EGGLKPSSETPLHLAIYRArPDAG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750   94 CILQVQTVDSHLISELYGEEGEVTFDkrsVERVFGKEgitemtIPIVEDEKKFADLLESNVPNFIEGGG-VVLVHNYGMI 172
Cdd:pfam00596  84 AVVHTHSPYATALSLAKEGLPPITQE---AADFLGGD------IPIIPYYTPGTEELGERIAEALGGDRkAVLLRNHGLL 154
                         170
                  ....*....|....*....
gi 446818750  173 VWGKTPEEAKKWLEGIEYL 191
Cdd:pfam00596 155 VWGKTLEEAFYLAEELERA 173
 
Name Accession Description Interval E-value
PRK06755 PRK06755
hypothetical protein; Validated
1-209 1.50e-148

hypothetical protein; Validated


Pssm-ID: 102532  Cd Length: 209  Bit Score: 410.96  E-value: 1.50e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750   1 MLFFLKKWNELKDVKSELALRDWFYGTKISLSLCTSKEPLTFLVNVEGRDKGLFSEEDFIVVNCMCESVFENEEKPAAES 80
Cdd:PRK06755   1 MLFFLKKWNELKDVKSELALRDWFYGTKISLSLCTSKEPLTFLVNVEGRDKGLFSEEDFIVVNCMCEPVFENEEKPAAES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750  81 FMHADIYKKSSAGCILQVQTVDSHLISELYGEEGEVTFDKRSVERVFGKEGITEMTIPIVEDEKKFADLLESNVPNFIEG 160
Cdd:PRK06755  81 FMHADIYKKSSAECILQVQTVDSHLISELYGEEGEVTFDKRSVERVFGKEGITEMTIPIVEDEKKFADLLENNVPNFIEG 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446818750 161 GGVVLVHNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKLLMIKGARSSVI 209
Cdd:PRK06755 161 GGVVLVHNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKLLMIKGAKSSVI 209
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
1-204 3.86e-66

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 202.20  E-value: 3.86e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750   1 MLFFLKKWNELKDVKSELALRDWFYGTKISLSLCTSKEPLTFLVNVEGRDKGLFSEEDFIVVNCMCESVFENEEKPAAES 80
Cdd:PRK06754   1 MKQLQRRWNELAEIKKELAARDWFPATSGNLSIKVSDDPLTFLVTASGKDKRKTTPEDFLLVDHDGKPVEETELKPSAET 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750  81 FMHADIYKKSSAGCILQVQTVDSHLISELYGEEGEVTFDKRSVERVFG--KEGiTEMTIPIVEDekkFADL--LESNVPN 156
Cdd:PRK06754  81 LLHTHIYNNTNAGCVLHVHTVDNNVISELYGDDGAVTFQGQEIIKALGiwEEN-AEIHIPIIEN---HADIptLAEEFAK 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446818750 157 FIEGG-GVVLVHNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKLLMIKGA 204
Cdd:PRK06754 157 HIQGDsGAVLIRNHGITVWGRDAFEAKKHLEAYEFLFSYHIKLLSIQGG 205
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
11-199 5.28e-31

methylthioribulose-1-phosphate dehydratase; Members of this family are the methylthioribulose-1-phosphate dehydratase of the methionine salvage pathway. This pathway allows methylthioadenosine, left over from polyamine biosynthesis, to be recycled to methionine. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 274521 [Multi-domain]  Cd Length: 192  Bit Score: 111.97  E-value: 5.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750   11 LKDVKSELALRDWFYGTKISLSLCTSkePLTFLVNVEGRDKGLFSEEDFIVVNcMCESVFENEEKPAAESFMHADIYKKS 90
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARLD--EDEILITPSGVDKGRLTPEDFLVVD-LQGKPVSGGLKPSAETLLHTQLYRLT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750   91 SAGCILQVQTVDSHLISELYGEEGEVTFDKRSVERVFgkEGIT----EMTIPIVEDEKKFADLLESnVPNFIEGG---GV 163
Cdd:TIGR03328  78 GAGAVLHTHSVEATVLSRLYPSNGGFELEGYEMLKGL--PGITthedTLVVPIIENTQDIARLADS-VAPALNAYpdvPG 154
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 446818750  164 VLVHNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKLL 199
Cdd:TIGR03328 155 VLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEML 190
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
10-205 4.66e-23

5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440005 [Multi-domain]  Cd Length: 208  Bit Score: 91.82  E-value: 4.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750  10 ELKDVKSELALRDWFYGTKISLSLCTSKEplTFLVNVEGRDKGLFSEEDFIVVNCMCESVfENEEKPAAESFMHADIYKK 89
Cdd:COG0235    9 ELAAAGRRLARRGLVDGTAGNISVRLDDD--RFLITPSGVDFGELTPEDLVVVDLDGNVV-EGDLKPSSETPLHLAIYRA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750  90 -SSAGCILQVQTVDSHLISELygeegEVTFDKRSVE--RVFGKEgitemtIPIVEDEKKFADLLESNVPNFIEGGGVVLV 166
Cdd:COG0235   86 rPDVGAVVHTHSPYATALSAL-----GEPLPPLEQTeaAAFLGD------VPVVPYAGPGTEELAEAIAEALGDRPAVLL 154
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446818750 167 HNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKLLMIKGAR 205
Cdd:COG0235  155 RNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGPL 193
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
17-191 5.44e-22

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 214970 [Multi-domain]  Cd Length: 185  Bit Score: 88.46  E-value: 5.44e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750    17 ELALRDWFYGTKISLSLCTsKEPLTFLVNVEGRDKGLFSEEDFIVVNCMCESVF-ENEEKPAAESFMHADIYKK-SSAGC 94
Cdd:smart01007   7 LLARRGLVEGTGGNISARV-GEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEgGGGPKPSSETPLHLAIYRArPDVGA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750    95 ILQVQTVDSHLISeLYGEEGEVTFDKRSVERVFGKEGITEMTIPIVEDEKKFADLLESNVPNFiEGGGVVLVHNYGMIVW 174
Cdd:smart01007  86 VVHTHSPYATALA-ALGKPLPLLPTEQAAAFLGGEIPYAPYAGPGTELAEEGAELAEALAEAL-PDRPAVLLRNHGLLVW 163
                          170
                   ....*....|....*..
gi 446818750   175 GKTPEEAKKWLEGIEYL 191
Cdd:smart01007 164 GKTLEEAFDLAEELEEA 180
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
17-191 2.50e-17

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 76.05  E-value: 2.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750   17 ELALRDWFYGT--KISLSLctskEPLTFLVNVEGRDKGLFSEEDFIVVNCMCESVfENEEKPAAESFMHADIYKK-SSAG 93
Cdd:pfam00596   9 LLARRGLVEGTggNISVRL----PGDGFLITPSGVDFGELTPEDLVVVDLDGNVV-EGGLKPSSETPLHLAIYRArPDAG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750   94 CILQVQTVDSHLISELYGEEGEVTFDkrsVERVFGKEgitemtIPIVEDEKKFADLLESNVPNFIEGGG-VVLVHNYGMI 172
Cdd:pfam00596  84 AVVHTHSPYATALSLAKEGLPPITQE---AADFLGGD------IPIIPYYTPGTEELGERIAEALGGDRkAVLLRNHGLL 154
                         170
                  ....*....|....*....
gi 446818750  173 VWGKTPEEAKKWLEGIEYL 191
Cdd:pfam00596 155 VWGKTLEEAFYLAEELERA 173
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
43-191 5.60e-13

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 64.96  E-value: 5.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446818750  43 LVNVEGRDKGLFSEEDFIVVNCMCESVfENEEKPAAESFMHADIYKKS-SAGCILQVQTVDSHLISeLYGEEGEVTFDKR 121
Cdd:PRK09220  40 AITVSGKDKGSLTAEDFLQVDIAGNAV-PSGRKPSAETLLHTQLYRLFpEIGAVLHTHSVNATVLS-RVEKSDALVLEGY 117
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446818750 122 SVERVFgkEGIT--EMTIPI-VEDEKKFADLLESNVPNFIEGGGVV---LVHNYGMIVWGKTPEEAKKWLEGIEYL 191
Cdd:PRK09220 118 ELQKAF--AGQTthETAVVVpIFDNDQDIARLAARVAPYLDAQPLRygyLIRGHGLYCWGRDMAEARRHLEGLEFL 191
 
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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