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Conserved domains on  [gi|446868849|ref|WP_000946105|]
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MULTISPECIES: phosphoadenosine phosphosulfate reductase family protein [Enterobacteriaceae]

Protein Classification

adenine nucleotide alpha hydrolase family protein( domain architecture ID 188)

AANH (adenine nucleotide alpha hydrolase) family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AANH_superfamily super family cl00292
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ...
 50-278 9.40e-11

Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase (AANH) superfamily includes N-type ATP PPases, ATP sulfurylases, universal stress response proteins (USPs), and electron transfer flavoproteins (ETFs). The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


The actual alignment was detected with superfamily member cd23947:

Pssm-ID: 469708 [Multi-domain]  Cd Length: 206  Bit Score: 60.87  E-value: 9.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446868849  50 YDHIIVCLSGGKDSIAAYL--RLVDMGVDKsKVEFWHHDvdgqegsSLMDWAFMRDYCRQLGQELGIpmffswleggfeg 127
Cdd:cd23947   12 FDPVIVSFSGGKDSLVLLHlaLEALRRLRK-DVYVVFID-------TGIEFPETIDFVEKLAETLGL------------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446868849 128 emlkenayshphRVETPEGLLVLPRDHKRSKPGTRLRFPQQSPSLQTRWCSSALKIDVGRRALNNQdrfKGKKILFITGE 207
Cdd:cd23947   71 ------------DVEAARPPLFLEWLTSNFQPQWDPIWDNPPPPRDYRWCCDELKLEPFTKWLKEK---KPEGVLLLVGI 135

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446868849 208 RREESANRSRYNQLEahacdRRYGKTARLVDAW---RPVLHWTEEEVWEVIERHRILAPVPYRLGWNRSSCMTC 278
Cdd:cd23947  136 RADESLNRAKRPRVY-----RKYGWRNSTLPGQivaYPIKDWSVEDVWLYILRHGLPYNPLYDLGFDRGGCLVC 204
 
Name Accession Description Interval E-value
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 50-278 9.40e-11

uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to Escherichia coli YbdN; This subgroup contains Escherichia coli YbdN and other phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8)-like proteins. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP).


Pssm-ID: 467512 [Multi-domain]  Cd Length: 206  Bit Score: 60.87  E-value: 9.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446868849  50 YDHIIVCLSGGKDSIAAYL--RLVDMGVDKsKVEFWHHDvdgqegsSLMDWAFMRDYCRQLGQELGIpmffswleggfeg 127
Cdd:cd23947   12 FDPVIVSFSGGKDSLVLLHlaLEALRRLRK-DVYVVFID-------TGIEFPETIDFVEKLAETLGL------------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446868849 128 emlkenayshphRVETPEGLLVLPRDHKRSKPGTRLRFPQQSPSLQTRWCSSALKIDVGRRALNNQdrfKGKKILFITGE 207
Cdd:cd23947   71 ------------DVEAARPPLFLEWLTSNFQPQWDPIWDNPPPPRDYRWCCDELKLEPFTKWLKEK---KPEGVLLLVGI 135

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446868849 208 RREESANRSRYNQLEahacdRRYGKTARLVDAW---RPVLHWTEEEVWEVIERHRILAPVPYRLGWNRSSCMTC 278
Cdd:cd23947  136 RADESLNRAKRPRVY-----RKYGWRNSTLPGQivaYPIKDWSVEDVWLYILRHGLPYNPLYDLGFDRGGCLVC 204
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 175-278 8.21e-09

3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439945 [Multi-domain]  Cd Length: 232  Bit Score: 55.62  E-value: 8.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446868849 175 RWCSSALKIDVGRRALNNQDRfkgkkILFITGERREESANRSRYNQLEAhacDRRYGKTaRLvdawRPVLHWTEEEVWEV 254
Cdd:COG0175  115 RWCCKIRKVEPLKRALAGYDF-----DAWITGLRRDESPTRAKEPVVEW---DPVGGLI-KV----NPLADWTELDVWAY 181

                         90       100
                 ....*....|....*....|....*.
gi 446868849 255 IERHRIlaPVP--YRLGWNRSSCMTC 278
Cdd:COG0175  182 IRREDL--PYNplYDQGYPSIGCAPC 205
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 153-279 4.27e-07

Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine phosphosulfate (PAPS) reductase enzymes or PAPS sulfotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). It is also found in NodP nodulation protein P from Rhizobium which has ATP sulfurylase activity (sulfate adenylate transferase).


Pssm-ID: 396201 [Multi-domain]  Cd Length: 173  Bit Score: 49.60  E-value: 4.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446868849  153 DHKRSKPGTRLRFPQQSPSLQTRWCSSALKIDVGRRALNNQDRfkgkkILFITGERREESANRSRYNQLEAhacDRRYGK 232
Cdd:pfam01507  57 VYLPEDSFAEGINPEGIPSSLYRRCCRLRKVEPLKRALKELGF-----DAWFTGLRRDESPSRAKLPIVSI---DGDFPK 128

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 446868849  233 TARlvdaWRPVLHWTEEEVWEVIERHRILAPVPYRLGWNRSSCMTCI 279
Cdd:pfam01507 129 VIK----VFPLLNWTETDVWQYILANNVPYNPLYDQGYRSIGCYPCT 171
PRK08557 PRK08557
hypothetical protein; Provisional
 170-308 2.73e-06

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 48.98  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446868849 170 PSLQTRWCSSALKIDVGRRALnnQDRFKGKKILFITGERREESANRSRYNqleahacdrrYGKTARLVDAWR---PVLHW 246
Cdd:PRK08557 255 PTKDNRWCNSACKLMPLKEYL--KKKYGNKKVLTIDGSRKYESFTRANLD----------YERKSGFIDFQTnvfPILDW 322

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446868849 247 TEEEVWEVIERHRILAPVPYRLGWNRSSCMTC--IYNSQriWSTIRHYWPDRAGKIAQYEQTFG 308
Cdd:PRK08557 323 NSLDIWSYIYLNDILYNPLYDKGFERIGCYLCpsALNSE--FLRVKELYPELFNRWVKYLKKYG 384
 
Name Accession Description Interval E-value
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 50-278 9.40e-11

uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to Escherichia coli YbdN; This subgroup contains Escherichia coli YbdN and other phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8)-like proteins. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP).


Pssm-ID: 467512 [Multi-domain]  Cd Length: 206  Bit Score: 60.87  E-value: 9.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446868849  50 YDHIIVCLSGGKDSIAAYL--RLVDMGVDKsKVEFWHHDvdgqegsSLMDWAFMRDYCRQLGQELGIpmffswleggfeg 127
Cdd:cd23947   12 FDPVIVSFSGGKDSLVLLHlaLEALRRLRK-DVYVVFID-------TGIEFPETIDFVEKLAETLGL------------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446868849 128 emlkenayshphRVETPEGLLVLPRDHKRSKPGTRLRFPQQSPSLQTRWCSSALKIDVGRRALNNQdrfKGKKILFITGE 207
Cdd:cd23947   71 ------------DVEAARPPLFLEWLTSNFQPQWDPIWDNPPPPRDYRWCCDELKLEPFTKWLKEK---KPEGVLLLVGI 135

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446868849 208 RREESANRSRYNQLEahacdRRYGKTARLVDAW---RPVLHWTEEEVWEVIERHRILAPVPYRLGWNRSSCMTC 278
Cdd:cd23947  136 RADESLNRAKRPRVY-----RKYGWRNSTLPGQivaYPIKDWSVEDVWLYILRHGLPYNPLYDLGFDRGGCLVC 204
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 175-278 8.21e-09

3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439945 [Multi-domain]  Cd Length: 232  Bit Score: 55.62  E-value: 8.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446868849 175 RWCSSALKIDVGRRALNNQDRfkgkkILFITGERREESANRSRYNQLEAhacDRRYGKTaRLvdawRPVLHWTEEEVWEV 254
Cdd:COG0175  115 RWCCKIRKVEPLKRALAGYDF-----DAWITGLRRDESPTRAKEPVVEW---DPVGGLI-KV----NPLADWTELDVWAY 181

                         90       100
                 ....*....|....*....|....*.
gi 446868849 255 IERHRIlaPVP--YRLGWNRSSCMTC 278
Cdd:COG0175  182 IRREDL--PYNplYDQGYPSIGCAPC 205
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 153-279 4.27e-07

Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine phosphosulfate (PAPS) reductase enzymes or PAPS sulfotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). It is also found in NodP nodulation protein P from Rhizobium which has ATP sulfurylase activity (sulfate adenylate transferase).


Pssm-ID: 396201 [Multi-domain]  Cd Length: 173  Bit Score: 49.60  E-value: 4.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446868849  153 DHKRSKPGTRLRFPQQSPSLQTRWCSSALKIDVGRRALNNQDRfkgkkILFITGERREESANRSRYNQLEAhacDRRYGK 232
Cdd:pfam01507  57 VYLPEDSFAEGINPEGIPSSLYRRCCRLRKVEPLKRALKELGF-----DAWFTGLRRDESPSRAKLPIVSI---DGDFPK 128

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 446868849  233 TARlvdaWRPVLHWTEEEVWEVIERHRILAPVPYRLGWNRSSCMTCI 279
Cdd:pfam01507 129 VIK----VFPLLNWTETDVWQYILANNVPYNPLYDQGYRSIGCYPCT 171
PRK08557 PRK08557
hypothetical protein; Provisional
 170-308 2.73e-06

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 48.98  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446868849 170 PSLQTRWCSSALKIDVGRRALnnQDRFKGKKILFITGERREESANRSRYNqleahacdrrYGKTARLVDAWR---PVLHW 246
Cdd:PRK08557 255 PTKDNRWCNSACKLMPLKEYL--KKKYGNKKVLTIDGSRKYESFTRANLD----------YERKSGFIDFQTnvfPILDW 322

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446868849 247 TEEEVWEVIERHRILAPVPYRLGWNRSSCMTC--IYNSQriWSTIRHYWPDRAGKIAQYEQTFG 308
Cdd:PRK08557 323 NSLDIWSYIYLNDILYNPLYDKGFERIGCYLCpsALNSE--FLRVKELYPELFNRWVKYLKKYG 384
PRK13794 PRK13794
hypothetical protein; Provisional
 170-278 3.22e-06

hypothetical protein; Provisional


Pssm-ID: 237509 [Multi-domain]  Cd Length: 479  Bit Score: 48.90  E-value: 3.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446868849 170 PSLQTRWCSSALKIDVGRRALNNqdRFKGKKILFItGERREESANRSrynqleahacdrrygKTARLvdaWR-------- 241
Cdd:PRK13794 322 PARDNRWCSEVCKLEPLGKLIDE--KYEGECLSFV-GQRKYESFNRS---------------KKPRI---WRnpyikkqi 380

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446868849 242 ---PVLHWTEEEVWEVIERHRilAP--VPYRLGWNRSSCMTC 278
Cdd:PRK13794 381 laaPILHWTAMHVWIYLFREK--APynKLYEQGFDRIGCFMC 420
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 47-109 1.42e-05

tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439807 [Multi-domain]  Cd Length: 235  Bit Score: 45.98  E-value: 1.42e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446868849  47 LSRYDHIIVCLSGGKDSIA-AYLrLVDMgVDKSKVEF----WHHdvdGQEGSSLMDWAFMRDYCRQLG 109
Cdd:COG0037   12 LEPGDRILVAVSGGKDSLAlLHL-LAKL-RRRLGFELvavhVDH---GLREESDEDAEFVAELCEELG 74
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
187-266 1.10e-04

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 43.29  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446868849 187 RRALnnqdrfKGKKIlFITGERREESANRsryNQLEAHACDRRYGKtarlvdaWRPVLHWTEEEVWEVIERHRilapVPY 266
Cdd:PRK02090 136 NRAL------AGLDA-WITGLRREQSGTR---ANLPVLEIDGGRFK-------INPLADWTNEDVWAYLKEHD----LPY 194
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 182-266 1.86e-04

Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8) is part of the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP).


Pssm-ID: 467510 [Multi-domain]  Cd Length: 183  Bit Score: 41.81  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446868849 182 KIDVGRRALNNQdrfkGKKILfITGERREESANRsryNQLEAHACDRRYGKtarlvDAWRPVLHWTEEEVWEVIERHRil 261
Cdd:cd23945  104 KRKPFPLALALL----GVKAW-ITGRRRDQSPTR---ANLPIVEVDEEGGL-----VKINPLADWTWEDVWAYIREHD-- 168


                 ....*
gi 446868849 262 apVPY 266
Cdd:cd23945  169 --LPY 171
PRK06850 PRK06850
hypothetical protein; Provisional
 169-253 1.29e-03

hypothetical protein; Provisional


Pssm-ID: 235877 [Multi-domain]  Cd Length: 507  Bit Score: 40.73  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446868849 169 SPSLQTRWCSSALKIDVGRRALNNQDRFKGKKILfITGERREESANRSryNQLEAHACDR-RYGKTARLVDAW--RPVLH 245
Cdd:PRK06850 130 APRRKFRWCTERLKIDPSNDFIKDKVSEFGEVIV-VLGVRKAESAARA--QVMAKHEIEGsRLSRHTTLPNAFvyTPIED 206


                 ....*...
gi 446868849 246 WTEEEVWE 253
Cdd:PRK06850 207 WSNDDVWK 214
TtcA-like cd24138
tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) ...
 51-112 1.30e-03

tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) 2-sulfurtransferase, also called two-thiocytidine biosynthesis protein A or tRNA 2-thiocytidine biosynthesis protein TtcA, catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). TtcA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467514 [Multi-domain]  Cd Length: 187  Bit Score: 39.56  E-value: 1.30e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446868849  51 DHIIVCLSGGKDSIAAYLRLVDM---GVDKSKVEFWHhdVDGQEGSSLMDWAFMRDYCRQLGQEL 112
Cdd:cd24138    9 DRILVGLSGGKDSLTLLHLLEELkrrAPIKFELVAVT--VDPGYPGYRPPREELAEILEELGEIL 71
 
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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