NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1624566572|ref|WP_136409615|]
View 

GNAT family N-acetyltransferase [Muribaculum gordoncarteri]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10456837)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
PubMed:  15581578|10940244|9175471|27367672|26818562
SCOP:  3000403

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 16-129 3.02e-12

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


:

Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 60.22  E-value: 3.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566572  16 EELIALYNASFPADERRPVDSIMALIDDHDSPFnAYVIKTDN---GFAGFITTWDFDDMLYVEHFATNPELRGQGIGSDA 92
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDWDEDASEG-FFVAEEDGelvGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1624566572  93 LNMLMELADKPVV--LEVEPEDSNPLAsrrIGFYRRHGF 129
Cdd:pfam00583  81 LQALLEWARERGCerIFLEVAADNLAA---IALYEKLGF 116
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 16-129 3.02e-12

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 60.22  E-value: 3.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566572  16 EELIALYNASFPADERRPVDSIMALIDDHDSPFnAYVIKTDN---GFAGFITTWDFDDMLYVEHFATNPELRGQGIGSDA 92
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDWDEDASEG-FFVAEEDGelvGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1624566572  93 LNMLMELADKPVV--LEVEPEDSNPLAsrrIGFYRRHGF 129
Cdd:pfam00583  81 LQALLEWARERGCerIFLEVAADNLAA---IALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
16-142 8.33e-12

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 59.71  E-value: 8.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566572  16 EELIALYNASFP-ADERRPVDSIMALIDDHDSpfnaYVIKTDNGFAGFITTWDFD-----DMLYVEHFATNPELRGQGIG 89
Cdd:COG3153    10 EAIAALLRAAFGpGREAELVDRLREDPAAGLS----LVAEDDGEIVGHVALSPVDidgegPALLLGPLAVDPEYRGQGIG 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1624566572  90 S----DALNMLMELADKPVVLEVEPedsnplasRRIGFYRRHGFMLHSDYKYIQPPY 142
Cdd:COG3153    86 RalmrAALEAARERGARAVVLLGDP--------SLLPFYERFGFRPAGELGLTLGPD 134
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 46-129 3.42e-08

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 49.63  E-value: 3.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566572  46 SPFNAYVIKTDNG-FAGFITTWDFDDMLYVEHFATNPELRGQGIGSDALNMLMELAD----KPVVLEVEPedSNPLAsrr 120
Cdd:TIGR01575  28 NYHLCYLLARIGGkVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKgrgvNEIFLEVRV--SNIAA--- 102


                  ....*....
gi 1624566572 121 IGFYRRHGF 129
Cdd:TIGR01575 103 QALYKKLGF 111
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 51-102 1.65e-07

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 46.11  E-value: 1.65e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1624566572  51 YVIKTDN---GFAGFITTWDFDDMLYVEHFATNPELRGQGIGSDALNMLMELADK 102
Cdd:cd04301     2 LVAEDDGeivGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARE 56
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 16-129 3.02e-12

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 60.22  E-value: 3.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566572  16 EELIALYNASFPADERRPVDSIMALIDDHDSPFnAYVIKTDN---GFAGFITTWDFDDMLYVEHFATNPELRGQGIGSDA 92
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDWDEDASEG-FFVAEEDGelvGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1624566572  93 LNMLMELADKPVV--LEVEPEDSNPLAsrrIGFYRRHGF 129
Cdd:pfam00583  81 LQALLEWARERGCerIFLEVAADNLAA---IALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
16-142 8.33e-12

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 59.71  E-value: 8.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566572  16 EELIALYNASFP-ADERRPVDSIMALIDDHDSpfnaYVIKTDNGFAGFITTWDFD-----DMLYVEHFATNPELRGQGIG 89
Cdd:COG3153    10 EAIAALLRAAFGpGREAELVDRLREDPAAGLS----LVAEDDGEIVGHVALSPVDidgegPALLLGPLAVDPEYRGQGIG 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1624566572  90 S----DALNMLMELADKPVVLEVEPedsnplasRRIGFYRRHGFMLHSDYKYIQPPY 142
Cdd:COG3153    86 RalmrAALEAARERGARAVVLLGDP--------SLLPFYERFGFRPAGELGLTLGPD 134
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 51-129 1.03e-10

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 55.15  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566572  51 YVIKTDNGFAGFITTWDFDDMLYVEH--FATNPELRGQGIGSDALNMLMELADKPVVLEVEPEDSNplasRRIGFYRRHG 128
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEGALAElrLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTN----RAAAFYEKLG 81


                  .
gi 1624566572 129 F 129
Cdd:pfam13508  82 F 82
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 61-129 1.55e-10

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 55.05  E-value: 1.55e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1624566572  61 GFITTW--DFDDMLYVEHFATNPELRGQGIGSDALNMLMELAD----KPVVLEVEPedSNPLAsrrIGFYRRHGF 129
Cdd:COG0456     1 GFALLGlvDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARergaRRLRLEVRE--DNEAA---IALYEKLGF 70
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 50-129 3.67e-10

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 55.06  E-value: 3.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566572  50 AYVIKTDNGFA-GFITTWDFDD-MLYVEHFATNPELRGQGIGSDALNMLMELADK--PVVLEVEPEDSNPLAsrrIGFYR 125
Cdd:COG0454    35 EFIAVDDKGEPiGFAGLRRLDDkVLELKRLYVLPEYRGKGIGKALLEALLEWARErgCTALELDTLDGNPAA---IRFYE 111


                  ....
gi 1624566572 126 RHGF 129
Cdd:COG0454   112 RLGF 115
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 34-129 2.72e-08

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 49.99  E-value: 2.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566572  34 VDSIMALIDD---HDSPFNAYVIKTDN---GFAGFITTWDfdDMLYVEHFATNPELRGQGIGSDALNMLMELAD----KP 103
Cdd:COG1246    11 VPAILELIRPyalEEEIGEFWVAEEDGeivGCAALHPLDE--DLAELRSLAVHPDYRGRGIGRRLLEALLAEARelglKR 88

                          90       100
                  ....*....|....*....|....*.
gi 1624566572 104 VVLEvepedSNPLAsrrIGFYRRHGF 129
Cdd:COG1246    89 LFLL-----TTSAA---IHFYEKLGF 106
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 46-129 3.42e-08

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 49.63  E-value: 3.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566572  46 SPFNAYVIKTDNG-FAGFITTWDFDDMLYVEHFATNPELRGQGIGSDALNMLMELAD----KPVVLEVEPedSNPLAsrr 120
Cdd:TIGR01575  28 NYHLCYLLARIGGkVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKgrgvNEIFLEVRV--SNIAA--- 102


                  ....*....
gi 1624566572 121 IGFYRRHGF 129
Cdd:TIGR01575 103 QALYKKLGF 111
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 51-102 1.65e-07

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 46.11  E-value: 1.65e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1624566572  51 YVIKTDN---GFAGFITTWDFDDMLYVEHFATNPELRGQGIGSDALNMLMELADK 102
Cdd:cd04301     2 LVAEDDGeivGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARE 56
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
58-138 8.64e-07

Predicted acetyltransferase, GNAT family [General function prediction only];


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 44.90  E-value: 8.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566572  58 GFAGFitTWDFDDMLYVEHFATNPELRGQGIGSDALNMLMELA----DKPVVLEVepEDSNPlASRRIgfYRRHGFMLHS 133
Cdd:COG3393     4 AMAGV--RAESPGVAEISGVYTHPEYRGRGLASALVAALAREAlargARTPFLYV--DADNP-AARRL--YERLGFRPVG 76


                  ....*
gi 1624566572 134 DYKYI 138
Cdd:COG3393    77 EYATV 81
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
16-129 1.20e-05

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 43.44  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566572  16 EELIALYNASFPA------DERRPVDSIMALIDDHDSPFNAYVIKTDNG-FAGFIT-----TWDFDDMLYVEHFATNPEL 83
Cdd:COG1247    13 PAIAAIYNEAIAEgtatfeTEPPSEEEREAWFAAILAPGRPVLVAEEDGeVVGFASlgpfrPRPAYRGTAEESIYVDPDA 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1624566572  84 RGQGIGSdalnMLME-LADKPV-----VLEVEPEDSNPlASRRigFYRRHGF 129
Cdd:COG1247    93 RGRGIGR----ALLEaLIERARargyrRLVAVVLADNE-ASIA--LYEKLGF 137
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 27-129 2.24e-05

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 42.68  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566572  27 PADERRPVDSIMALIDDHDSPFNAYVIKTDNGFAGFITTWDFDDML-YVE-HFATNPELRGQGIGSDALNMLMELADKP- 103
Cdd:COG1670    41 LEEARAWLERLLADWADGGALPFAIEDKEDGELIGVVGLYDIDRANrSAEiGYWLAPAYWGKGYATEALRALLDYAFEEl 120

                          90       100       110
                  ....*....|....*....|....*....|
gi 1624566572 104 ----VVLEVEPEdsNPlASRRIgfYRRHGF 129
Cdd:COG1670   121 glhrVEAEVDPD--NT-ASIRV--LEKLGF 145
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
38-90 1.67e-04

Predicted acetyltransferase, GNAT superfamily [General function prediction only];


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 38.60  E-value: 1.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1624566572  38 MALIDDHDSpfNAYVIKTDNGFAGFITTWDFDDMLYVEHFATNPELRGQGIGS 90
Cdd:COG2388     1 MEITHNEEK--GRFELEVDGELAGELTYRLEGGVIIITHTEVPPALRGQGIAS 51
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
74-134 1.82e-04

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 39.40  E-value: 1.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1624566572  74 VEHFATNPELRGQGIGSDALNMLMELA----DKPVVLEVEpedsnplaSRRIGFYRRHGFMLHSD 134
Cdd:COG2153    61 IGRVAVLPEYRGQGLGRALMEAAIEEArergARRIVLSAQ--------AHAVGFYEKLGFVPVGE 117
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 35-129 2.47e-04

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 39.18  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566572  35 DSIMALIDDHDSPFnaYVIKTDNGFAGFITTwdfDDMLYVEHFATNPELRGQGIGS----DALNMLMELADKPVVLEVep 110
Cdd:pfam13673  20 EALRERIDQGEYFF--FVAFEGGQIVGVIAL---RDRGHISLLFVDPDYQGQGIGKalleAVEDYAEKDGIKLSELTV-- 92

                          90
                  ....*....|....*....
gi 1624566572 111 eDSNPLAsrrIGFYRRHGF 129
Cdd:pfam13673  93 -NASPYA---VPFYEKLGF 107
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH