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Conserved domains on  [gi|648456530|ref|WP_026148281|]
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bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG [Thioalkalivibrio sp. HL-Eb18]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11454890)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

EC:  2.1.1.-
Gene Ontology:  GO:0032259|GO:0008168|GO:1904047
PubMed:  12504684|12826405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 234-344 6.79e-11

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


:

Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 59.65  E-value: 6.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648456530 234 RARIAELYATLTPPGARVLDLMSSWESHLDQL--RGPEaVVGLGMNHEELA-ANEALDQALVH----DLNrqpAIPLPPA 306
Cdd:COG2227   11 DRRLAALLARLLPAGGRVLDVGCGTGRLALALarRGAD-VTGVDISPEALEiARERAAELNVDfvqgDLE---DLPLEDG 86

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 648456530 307 SFDAVVCTASVEYLTRPQAVFASVRELLRPGGVFVVTF 344
Cdd:COG2227   87 SFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLST 124
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 234-344 6.79e-11

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 59.65  E-value: 6.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648456530 234 RARIAELYATLTPPGARVLDLMSSWESHLDQL--RGPEaVVGLGMNHEELA-ANEALDQALVH----DLNrqpAIPLPPA 306
Cdd:COG2227   11 DRRLAALLARLLPAGGRVLDVGCGTGRLALALarRGAD-VTGVDISPEALEiARERAAELNVDfvqgDLE---DLPLEDG 86

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 648456530 307 SFDAVVCTASVEYLTRPQAVFASVRELLRPGGVFVVTF 344
Cdd:COG2227   87 SFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLST 124
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 271-342 5.27e-08

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 50.36  E-value: 5.27e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648456530  271 VVGLGMNHEELAANEALDQALVHDLNRQPA--IPLPPASFDAVVCTASVEYLTRPQAVFASVRELLRPGGVFVV 342
Cdd:pfam08241  21 VTGVDISPEMLELAREKAPREGLTFVVGDAedLPFPDNSFDLVLSSEVLHHVEDPERALREIARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 300-344 2.95e-04

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 40.11  E-value: 2.95e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 648456530 300 AIPLPPASFDAVVCTASVEYL-TRPQAVFASVRELLRPGGVFVVTF 344
Cdd:cd02440   59 LPPEADESFDVIISDPPLHHLvEDLARFLEEARRLLKPGGVLVLTL 104
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 301-346 4.78e-04

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 41.50  E-value: 4.78e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 648456530  301 IPLPPASFDAVVCTASVEYLTRPQAVFASVRELLRPGGVFVV-TFSD 346
Cdd:TIGR02072  92 LPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFsTFGP 138
PRK08317 PRK08317
hypothetical protein; Provisional
 300-346 7.89e-03

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 37.61  E-value: 7.89e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 648456530 300 AIPLPPASFDAVVCTASVEYLTRPQAVFASVRELLRPGGVFVVTFSD 346
Cdd:PRK08317  80 GLPFPDGSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLDTD 126
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 234-344 6.79e-11

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 59.65  E-value: 6.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648456530 234 RARIAELYATLTPPGARVLDLMSSWESHLDQL--RGPEaVVGLGMNHEELA-ANEALDQALVH----DLNrqpAIPLPPA 306
Cdd:COG2227   11 DRRLAALLARLLPAGGRVLDVGCGTGRLALALarRGAD-VTGVDISPEALEiARERAAELNVDfvqgDLE---DLPLEDG 86

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 648456530 307 SFDAVVCTASVEYLTRPQAVFASVRELLRPGGVFVVTF 344
Cdd:COG2227   87 SFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLST 124
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 231-343 1.54e-10

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 58.85  E-value: 1.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648456530 231 AEARARIAELYATLTP-PGARVLDLMSSWESHLDQLRGPEA-VVGLGMNHEELAANEALDQALVHDLNRQPA----IPLP 304
Cdd:COG2226    5 AARYDGREALLAALGLrPGARVLDLGCGTGRLALALAERGArVTGVDISPEMLELARERAAEAGLNVEFVVGdaedLPFP 84

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 648456530 305 PASFDAVVCTASVEYLTRPQAVFASVRELLRPGGVFVVT 343
Cdd:COG2226   85 DGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVV 123
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 271-342 5.27e-08

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 50.36  E-value: 5.27e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648456530  271 VVGLGMNHEELAANEALDQALVHDLNRQPA--IPLPPASFDAVVCTASVEYLTRPQAVFASVRELLRPGGVFVV 342
Cdd:pfam08241  21 VTGVDISPEMLELAREKAPREGLTFVVGDAedLPFPDNSFDLVLSSEVLHHVEDPERALREIARVLKPGGILII 94
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
280-346 1.17e-07

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 51.54  E-value: 1.17e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648456530 280 ELAANEALDQALVH-DLnrqPAIPLPPASFDAVVCTASVEYLTRPQAVFASVRELLRPGGVFVVTFSD 346
Cdd:COG4976   82 AKAREKGVYDRLLVaDL---ADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVED 146
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 279-340 4.89e-07

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 47.75  E-value: 4.89e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648456530  279 EELAANEALDQALVHDLNRQPAIPLPPaSFDAVVCTASVEYLTRPQAVFASVRELLRPGGVF 340
Cdd:pfam08242  38 ERLAALGLLNAVRVELFQLDLGELDPG-SFDVVVASNVLHHLADPRAVLRNIRRLLKPGGVL 98
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
247-344 5.22e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 47.51  E-value: 5.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648456530 247 PGARVLDLMSSWESHLDQL--RGPEA-VVGLGMNHEELA-ANEALDQA--LVHDLNRQPaiplPPASFDAVVCTASVEYL 320
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLaeRFPGArVTGVDLSPEMLArARARLPNVrfVVADLRDLD----PPEPFDLVVSNAALHWL 76

                         90       100
                 ....*....|....*....|....
gi 648456530 321 TRPQAVFASVRELLRPGGVFVVTF 344
Cdd:COG4106   77 PDHAALLARLAAALAPGGVLAVQV 100
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 300-338 1.30e-06

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 46.40  E-value: 1.30e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 648456530  300 AIPLPPASFDAVVCTASVEYLTRPQ--AVFASVRELLRPGG 338
Cdd:pfam13649  56 DLPFPDGSFDLVVSSGVLHHLPDPDleAALREIARVLKPGG 96
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 229-344 2.88e-06

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 46.85  E-value: 2.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648456530 229 LDAEARARIAELYATL-TPPGARVLDLMSSWESHLDQL--RGPEAVVGLGMNHEELA-ANEALDQALVHD---LNRQPAI 301
Cdd:COG2230   32 LEEAQEAKLDLILRKLgLKPGMRVLDIGCGWGGLALYLarRYGVRVTGVTLSPEQLEyARERAAEAGLADrveVRLADYR 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 648456530 302 PLPP-ASFDAVVCTASVEYLTRPQ--AVFASVRELLRPGGVFVVTF 344
Cdd:COG2230  112 DLPAdGQFDAIVSIGMFEHVGPENypAYFAKVARLLKPGGRLLLHT 157
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 280-406 4.56e-05

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 44.14  E-value: 4.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648456530 280 ELAANEALDQA--LVHDLNRQPaiPLPPASFDAVVCTASVEYL--TRPQAVFASVRELLRPGGVFVVTFSD---RCFPTK 352
Cdd:COG0500   67 ARAAKAGLGNVefLVADLAELD--PLPAESFDLVVAFGVLHHLppEEREALLRELARALKPGGVLLLSASDaaaALSLAR 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 648456530 353 TIAVWEPLYDFERMGLVLDLFLRAGFDDRSTLSLRGLPRPPDDPYAGRLEHADP 406
Cdd:COG0500  145 LLLLATASLLELLLLLRLLALELYLRALLAAAATEDLRSDALLESANALEYLLS 198
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 300-344 2.95e-04

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 40.11  E-value: 2.95e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 648456530 300 AIPLPPASFDAVVCTASVEYL-TRPQAVFASVRELLRPGGVFVVTF 344
Cdd:cd02440   59 LPPEADESFDVIISDPPLHHLvEDLARFLEEARRLLKPGGVLVLTL 104
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 301-346 4.78e-04

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 41.50  E-value: 4.78e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 648456530  301 IPLPPASFDAVVCTASVEYLTRPQAVFASVRELLRPGGVFVV-TFSD 346
Cdd:TIGR02072  92 LPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFsTFGP 138
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 225-343 2.94e-03

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 38.18  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648456530  225 LVHHLDAEARARIAELyATLTPPGARVLDLMS---SWESHLDQlRGPEaVVGLGMNHEelaANEALDQALVHDLNRQPAI 301
Cdd:pfam13489   1 YAHQRERLLADLLLRL-LPKLPSPGRVLDFGCgtgIFLRLLRA-QGFS-VTGVDPSPI---AIERALLNVRFDQFDEQEA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 648456530  302 PLPPASFDAVVCTASVEYLTRPQAVFASVRELLRPGGVFVVT 343
Cdd:pfam13489  75 AVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLS 116
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 300-363 6.13e-03

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 38.01  E-value: 6.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648456530  300 AIPLPPASFDAVVCTASVEYLTRPQAVFASVRELLRPGGVFVVTFsdrcFPTKTIAVWEPLYDF 363
Cdd:TIGR01934  99 ALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILE----FSKPANALLKKFYKF 158
metW TIGR02081
methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that ...
 239-344 7.10e-03

methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that acylates homoserine as a first step toward methionine biosynthesis, in many species. It appears to act in methionine biosynthesis but is not fully characterized. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273958  Cd Length: 194  Bit Score: 37.35  E-value: 7.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648456530  239 ELYATLTPPGARVLDLMSSWESHLDQLRGPEAVVGLGMNHEELAANEALDQAL-VHDLNRQPAIPL-PPASFDAVVCTAS 316
Cdd:TIGR02081   5 ESILNLIPPGSRVLDLGCGDGELLALLRDEKQVRGYGIEIDQDGVLACVARGVnVIQGDLDEGLEAfPDKSFDYVILSQT 84

                          90       100
                  ....*....|....*....|....*...
gi 648456530  317 VEYLTRPQAVfasVRELLRPGGVFVVTF 344
Cdd:TIGR02081  85 LQATRNPEEI---LDEMLRVGRHAIVSF 109
PRK08317 PRK08317
hypothetical protein; Provisional
 300-346 7.89e-03

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 37.61  E-value: 7.89e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 648456530 300 AIPLPPASFDAVVCTASVEYLTRPQAVFASVRELLRPGGVFVVTFSD 346
Cdd:PRK08317  80 GLPFPDGSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLDTD 126
 
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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