NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|10835057|ref|NP_003482|]
View 

N-alpha-acetyltransferase 10 isoform 1 [Homo sapiens]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11418877)

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:  27367672|26818562|15581578|10940244
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
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 54-152 3.01e-17

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 73.92  E-value: 3.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835057  54 GYVLAKMEEDPDdvpHGHITSLAVKRSHRRLGLAQKLMDQASRAMIENfNAKYVSLHVRKSNRAALHLYSNtLNFQISEV 133
Cdd:COG0456   1 GFALLGLVDGGD---EAEIEDLAVDPEYRGRGIGRALLEAALERARER-GARRLRLEVREDNEAAIALYEK-LGFEEVGE 75

                        90
                ....*....|....*....
gi 10835057 134 EPKYYADgeDAYAMKRDLT 152
Cdd:COG0456  76 RPNYYGD--DALVMEKELA 92
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 54-152 3.01e-17

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 73.92  E-value: 3.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835057  54 GYVLAKMEEDPDdvpHGHITSLAVKRSHRRLGLAQKLMDQASRAMIENfNAKYVSLHVRKSNRAALHLYSNtLNFQISEV 133
Cdd:COG0456   1 GFALLGLVDGGD---EAEIEDLAVDPEYRGRGIGRALLEAALERARER-GARRLRLEVREDNEAAIALYEK-LGFEEVGE 75

                        90
                ....*....|....*....
gi 10835057 134 EPKYYADgeDAYAMKRDLT 152
Cdd:COG0456  76 RPNYYGD--DALVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 28-122 1.03e-16

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: 73.32  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835057    28 MKYYFYHGLSWPQLSYIAEDENGKIVGYVLAKMeeDPDDVPHGHITSLAVKRSHRRLGLAQKLMDQASRAMIEnFNAKYV 107
Cdd:pfam00583  20 PLDLLEDWDEDASEGFFVAEEDGELVGFASLSI--IDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARE-RGCERI 96

                          90
                  ....*....|....*
gi 10835057   108 SLHVRKSNRAALHLY 122
Cdd:pfam00583  97 FLEVAADNLAAIALY 111
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 42-110 6.69e-10

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: 53.43  E-value: 6.69e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10835057  42 SYIAEDEnGKIVGYVLAKMEEDPDDvpHGHITSLAVKRSHRRLGLAQKLMDQASRAMIENfNAKYVSLH 110
Cdd:cd04301   1 FLVAEDD-GEIVGFASLSPDGSGGD--TAYIGDLAVLPEYRGKGIGSALLEAAEEEARER-GAKRLRLE 65
PRK03624 PRK03624
putative acetyltransferase; Provisional
 39-133 2.16e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 45.69  E-value: 2.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835057   39 PQLSYIAEDeNGKIVGYVLAKMeedpdDVPHGHITSLAVKRSHRRLGLAQKLMDQASRAMIENFNAKyVSLHVRKSNRAA 118
Cdd:PRK03624  44 PSLFLVAEV-GGEVVGTVMGGY-----DGHRGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPK-INLQVREDNDAV 116

                         90
                 ....*....|....*
gi 10835057  119 LHLYSnTLNFQISEV 133
Cdd:PRK03624 117 LGFYE-ALGYEEQDR 130
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 54-152 3.01e-17

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 73.92  E-value: 3.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835057  54 GYVLAKMEEDPDdvpHGHITSLAVKRSHRRLGLAQKLMDQASRAMIENfNAKYVSLHVRKSNRAALHLYSNtLNFQISEV 133
Cdd:COG0456   1 GFALLGLVDGGD---EAEIEDLAVDPEYRGRGIGRALLEAALERARER-GARRLRLEVREDNEAAIALYEK-LGFEEVGE 75

                        90
                ....*....|....*....
gi 10835057 134 EPKYYADgeDAYAMKRDLT 152
Cdd:COG0456  76 RPNYYGD--DALVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 28-122 1.03e-16

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: 73.32  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835057    28 MKYYFYHGLSWPQLSYIAEDENGKIVGYVLAKMeeDPDDVPHGHITSLAVKRSHRRLGLAQKLMDQASRAMIEnFNAKYV 107
Cdd:pfam00583  20 PLDLLEDWDEDASEGFFVAEEDGELVGFASLSI--IDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARE-RGCERI 96

                          90
                  ....*....|....*
gi 10835057   108 SLHVRKSNRAALHLY 122
Cdd:pfam00583  97 FLEVAADNLAAIALY 111
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-151 1.40e-12

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 62.80  E-value: 1.40e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835057   3 IRNARPEDLMNMQHCNLLCLPENYQMKY-YFYHGLSWPQLSYIAEDeNGKIVGYVLAKMEEDPDDVPHGHITSLAVKRSH 81
Cdd:COG3153   1 IRPATPEDAEAIAALLRAAFGPGREAELvDRLREDPAAGLSLVAED-DGEIVGHVALSPVDIDGEGPALLLGPLAVDPEY 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835057  82 RRLGLAQKLMDQASRAMIENfNAKYVSLHvrkSNRAALHLYSNtLNFQisEVEPKYYADGEDAYAMKRDL 151
Cdd:COG3153  80 RGQGIGRALMRAALEAARER-GARAVVLL---GDPSLLPFYER-FGFR--PAGELGLTLGPDEVFLAKEL 142
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-151 5.92e-10

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: 55.38  E-value: 5.92e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835057   1 MNIRNARPEDLMNMQHcnlLCLPENYQMKYYFYhglswpqlsYIAEdENGKIVGYV-LAKMEEDpddvpHGHITSLAVKR 79
Cdd:COG1246   1 MTIRPATPDDVPAILE---LIRPYALEEEIGEF---------WVAE-EDGEIVGCAaLHPLDED-----LAELRSLAVHP 62

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10835057  80 SHRRLGLAQKLMDQA-SRAmiENFNAKYVSLHvrkSNRAALHLYSNtLNFQISEVE--PKYYADGEDAYAMKRDL 151
Cdd:COG1246  63 DYRGRGIGRRLLEALlAEA--RELGLKRLFLL---TTSAAIHFYEK-LGFEEIDKEdlPYAKVWQRDSVVMEKDL 131
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 42-110 6.69e-10

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: 53.43  E-value: 6.69e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10835057  42 SYIAEDEnGKIVGYVLAKMEEDPDDvpHGHITSLAVKRSHRRLGLAQKLMDQASRAMIENfNAKYVSLH 110
Cdd:cd04301   1 FLVAEDD-GEIVGFASLSPDGSGGD--TAYIGDLAVLPEYRGKGIGSALLEAAEEEARER-GAKRLRLE 65
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-151 8.05e-10

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 55.77  E-value: 8.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835057   1 MNIRNARPEDLMNMQHCNLLCLPENY-----------QMKYYFYHGLSWPQLSYIAEdENGKIVGYVLAKMEEDPDDVPH 69
Cdd:COG1247   2 MTIRPATPEDAPAIAAIYNEAIAEGTatfeteppseeEREAWFAAILAPGRPVLVAE-EDGEVVGFASLGPFRPRPAYRG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835057  70 GHITSLAVKRSHRRLGLAQKLMDQASRAMIENfNAKYVSLHVRKSNRAALHLYSNtLNFQISEVEPK-YYADGE--DAYA 146
Cdd:COG1247  81 TAEESIYVDPDARGRGIGRALLEALIERARAR-GYRRLVAVVLADNEASIALYEK-LGFEEVGTLPEvGFKFGRwlDLVL 158


                ....*
gi 10835057 147 MKRDL 151
Cdd:COG1247 159 MQKRL 163
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 43-122 9.03e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 50.92  E-value: 9.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835057    43 YIAEDeNGKIVGYVLAKMEEDPDDVPHGHItslAVKRSHRRLGLAQKLMDQASRAMienfNAKYVSLHVRKSNRAALHLY 122
Cdd:pfam13508   6 FVAED-DGKIVGFAALLPLDDEGALAELRL---AVHPEYRGQGIGRALLEAAEAAA----KEGGIKLLELETTNRAAAFY 77
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
56-122 1.57e-07

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 47.60  E-value: 1.57e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10835057  56 VLAKMEEDPDDVPHGHITSLAVKRSHRRLGLAQKLMDQASRAMIENfNAKYVSLHVRKSNRAALHLY 122
Cdd:COG3393   2 LVAMAGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALAR-GARTPFLYVDADNPAARRLY 67
PRK03624 PRK03624
putative acetyltransferase; Provisional
 39-133 2.16e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 45.69  E-value: 2.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835057   39 PQLSYIAEDeNGKIVGYVLAKMeedpdDVPHGHITSLAVKRSHRRLGLAQKLMDQASRAMIENFNAKyVSLHVRKSNRAA 118
Cdd:PRK03624  44 PSLFLVAEV-GGEVVGTVMGGY-----DGHRGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPK-INLQVREDNDAV 116

                         90
                 ....*....|....*
gi 10835057  119 LHLYSnTLNFQISEV 133
Cdd:PRK03624 117 LGFYE-ALGYEEQDR 130
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
48-152 3.71e-06

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 45.18  E-value: 3.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835057  48 ENGKIVGY--VLakmeedPDDVPHGHITSLAVKRSHRRLGLAQKLMdQASRAMIENFNAKYVSLHVRKSnraALHLYSNt 125
Cdd:COG2153  41 DDGELVATarLL------PPGDGEAKIGRVAVLPEYRGQGLGRALM-EAAIEEARERGARRIVLSAQAH---AVGFYEK- 109

                        90       100
                ....*....|....*....|....*...
gi 10835057 126 LNFQ-ISEVepkYYADGEDAYAMKRDLT 152
Cdd:COG2153 110 LGFVpVGEE---FLEAGIPHIDMRKPLS 134
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 75-147 1.08e-05

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 44.15  E-value: 1.08e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10835057   75 LAVKRSHRRLGLAQKLMdqasRAMIENFNAKYVS---LHVRKSNRAALHLYSNtLNFQISEVEPKYY--ADG-EDAYAM 147
Cdd:PRK09491  69 IAVDPDYQRQGLGRALL----EHLIDELEKRGVAtlwLEVRASNAAAIALYES-LGFNEVTIRRNYYptADGrEDAIIM 142
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 47-110 3.04e-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: 39.56  E-value: 3.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10835057    47 DENGKIVGYVLAKMeedpddvpHGHITSLAVKRSHRRLGLAQKLMDQA-SRAMIENFNAKYVSLH 110
Cdd:pfam13673  37 FEGGQIVGVIALRD--------RGHISLLFVDPDYQGQGIGKALLEAVeDYAEKDGIKLSELTVN 93
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 68-129 3.57e-04

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 38.46  E-value: 3.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10835057    68 PHGHITSLAVKRSHRRLGLAQKLMDQASRAMIEnfNAKYVSLHVRKSNRAALHLYSNtLNFQ 129
Cdd:pfam08445  20 PGGELGALQTLPEHRRRGLGSRLVAALARGIAE--RGITPFAVVVAGNTPSRRLYEK-LGFR 78
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 44-122 4.63e-04

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: 39.60  E-value: 4.63e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10835057  44 IAEDENGKIVGYVLAkMEEDPDDvPHGHItSLAVKRSHRRLGLAQKLMDQASRAMIENFNAKYVSLHVRKSNRAALHLY 122
Cdd:COG1670  65 IEDKEDGELIGVVGL-YDIDRAN-RSAEI-GYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVL 140
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
44-122 2.90e-03

dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;


Pssm-ID: 182877  Cd Length: 194  Bit Score: 37.60  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10835057   44 IAEDENGKIVGYVLAKMEEDPDdvphGHITSLAVKRSHRRLGLAQKLMdQASRAMIENFNAKyvSLHV--RKSNRAALHL 121
Cdd:PRK10975 105 LLRDASGQIQGFVTLRELNDTD----ARIGLLAVFPGAQGRGIGARLM-QAALNWCQARGLT--RLRVatQMGNLAALRL 177


                 .
gi 10835057  122 Y 122
Cdd:PRK10975 178 Y 178
 
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