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Conserved domains on  [gi|62460540|ref|NP_001014922|]
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protein-lysine methyltransferase METTL21E [Bos taurus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 77-243 7.57e-37

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.).


The actual alignment was detected with superfamily member pfam10294:

Pssm-ID: 473071  Cd Length: 172  Bit Score: 128.99  E-value: 7.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460540    77 FAGHEIRINEAT--DCyGAVVWPSALVLCYFLETNVKQ----YNLVDKNVIEIGAGTGLVSIVASLL--GAHVTATDLPE 148
Cdd:pfam10294   2 LDNPGLRIEEDTgnGI-GGHVWDAAVVLSKYLEMKIFKelgaNNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460540   149 LLGNLQYNISRN-TKTKAkhlpQVKELSWGVALDKNFPRASiNFDYILAADVVYAHPFLEELLVTFDHLCKETTVILWVM 227
Cdd:pfam10294  81 ALELLKKNIELNaLSSKV----VVKVLDWGENLPPDLFDGH-PVDLILAADCVYNEDSFPLLEKTLKDLLGKESVILVAY 155

                         170
                  ....*....|....*.
gi 62460540   228 KFRLEKENKFVDRFEQ 243
Cdd:pfam10294 156 KKRREAEKKFFKLLER 171
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 77-243 7.57e-37

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 128.99  E-value: 7.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460540    77 FAGHEIRINEAT--DCyGAVVWPSALVLCYFLETNVKQ----YNLVDKNVIEIGAGTGLVSIVASLL--GAHVTATDLPE 148
Cdd:pfam10294   2 LDNPGLRIEEDTgnGI-GGHVWDAAVVLSKYLEMKIFKelgaNNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460540   149 LLGNLQYNISRN-TKTKAkhlpQVKELSWGVALDKNFPRASiNFDYILAADVVYAHPFLEELLVTFDHLCKETTVILWVM 227
Cdd:pfam10294  81 ALELLKKNIELNaLSSKV----VVKVLDWGENLPPDLFDGH-PVDLILAADCVYNEDSFPLLEKTLKDLLGKESVILVAY 155

                         170
                  ....*....|....*.
gi 62460540   228 KFRLEKENKFVDRFEQ 243
Cdd:pfam10294 156 KKRREAEKKFFKLLER 171
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
112-199 2.66e-07

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 50.54  E-value: 2.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460540  112 QYNLVDKNVIEIGAGTGLVSIVASLLGA-HVTATDLPEL-LGNLQYNISRNtktkakhlpqvkelswGVALDKNFPRASI 189
Cdd:PRK00517 115 KLVLPGKTVLDVGCGSGILAIAAAKLGAkKVLAVDIDPQaVEAARENAELN----------------GVELNVYLPQGDL 178

                         90
                 ....*....|...
gi 62460540  190 NFDYILA---ADV 199
Cdd:PRK00517 179 KADVIVAnilANP 191
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 106-218 6.93e-06

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: 44.62  E-value: 6.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460540 106 LETNVKQYNLVDKNVIEIGAGTGLVSIVASLLGAHVTATDL-PELLGNLQynisrntktkaKHLPQVK-ELSWGVALDKN 183
Cdd:COG2227  14 LAALLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDIsPEALEIAR-----------ERAAELNvDFVQGDLEDLP 82

                        90       100       110
                ....*....|....*....|....*....|....*
gi 62460540 184 FPRASinFDYILAADVVYaHpfLEELLVTFDHLCK 218
Cdd:COG2227  83 LEDGS--FDLVICSEVLE-H--LPDPAALLRELAR 112
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 114-162 1.93e-04

HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 41.38  E-value: 1.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 62460540   114 NLVD---KNVIEIGAGTGLVSIVASLLGAHVTATDL-PELLGNLQYNISRNTK 162
Cdd:TIGR00537  14 NLRElkpDDVLEIGAGTGLVAIRLKGKGKCILTTDInPFAVKELRENAKLNNV 66
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 119-229 6.14e-03

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: 35.87  E-value: 6.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460540 119 NVIEIGAGTGLVSI-VASLLGAHVTATDL-PELLGNLQYNISRNTKTKAKHLPQvkelSWGVALDKNFPRasinFDYILA 196
Cdd:cd02440   1 RVLDLGCGTGALALaLASGPGARVTGVDIsPVALELARKAAAALLADNVEVLKG----DAEELPPEADES----FDVIIS 72

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 62460540 197 ADVVYA-----HPFLEELLvtfDHLCKETTVILWVMKF 229
Cdd:cd02440  73 DPPLHHlvedlARFLEEAR---RLLKPGGVLVLTLVLA 107
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 77-243 7.57e-37

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 128.99  E-value: 7.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460540    77 FAGHEIRINEAT--DCyGAVVWPSALVLCYFLETNVKQ----YNLVDKNVIEIGAGTGLVSIVASLL--GAHVTATDLPE 148
Cdd:pfam10294   2 LDNPGLRIEEDTgnGI-GGHVWDAAVVLSKYLEMKIFKelgaNNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460540   149 LLGNLQYNISRN-TKTKAkhlpQVKELSWGVALDKNFPRASiNFDYILAADVVYAHPFLEELLVTFDHLCKETTVILWVM 227
Cdd:pfam10294  81 ALELLKKNIELNaLSSKV----VVKVLDWGENLPPDLFDGH-PVDLILAADCVYNEDSFPLLEKTLKDLLGKESVILVAY 155

                         170
                  ....*....|....*.
gi 62460540   228 KFRLEKENKFVDRFEQ 243
Cdd:pfam10294 156 KKRREAEKKFFKLLER 171
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
112-199 2.66e-07

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 50.54  E-value: 2.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460540  112 QYNLVDKNVIEIGAGTGLVSIVASLLGA-HVTATDLPEL-LGNLQYNISRNtktkakhlpqvkelswGVALDKNFPRASI 189
Cdd:PRK00517 115 KLVLPGKTVLDVGCGSGILAIAAAKLGAkKVLAVDIDPQaVEAARENAELN----------------GVELNVYLPQGDL 178

                         90
                 ....*....|...
gi 62460540  190 NFDYILA---ADV 199
Cdd:PRK00517 179 KADVIVAnilANP 191
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 106-218 6.93e-06

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: 44.62  E-value: 6.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460540 106 LETNVKQYNLVDKNVIEIGAGTGLVSIVASLLGAHVTATDL-PELLGNLQynisrntktkaKHLPQVK-ELSWGVALDKN 183
Cdd:COG2227  14 LAALLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDIsPEALEIAR-----------ERAAELNvDFVQGDLEDLP 82

                        90       100       110
                ....*....|....*....|....*....|....*
gi 62460540 184 FPRASinFDYILAADVVYaHpfLEELLVTFDHLCK 218
Cdd:COG2227  83 LEDGS--FDLVICSEVLE-H--LPDPAALLRELAR 112
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 101-160 1.52e-05

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 45.72  E-value: 1.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62460540   101 VLC-YFLETNVKQynlvDKNVIEIGAGTGLVSIVASLLGA-HVTATDLPEL-LGNLQYNISRN 160
Cdd:pfam06325 149 KLClEALERLVKP----GESVLDVGCGSGILAIAALKLGAkKVVGVDIDPVaVRAAKENAELN 207
PRK14968 PRK14968
putative methyltransferase; Provisional
 114-146 2.97e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 43.73  E-value: 2.97e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 62460540  114 NLVDKN---VIEIGAGTGLVSIVASLLGAHVTATDL 146
Cdd:PRK14968  18 NAVDKKgdrVLEVGTGSGIVAIVAAKNGKKVVGVDI 53
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
112-160 5.96e-05

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 43.62  E-value: 5.96e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 62460540 112 QYNLVDKNVIEIGAGTGLVSIVASLLGA-HVTATDL-PELLGNLQYNISRN 160
Cdd:COG2264 144 KLLKPGKTVLDVGCGSGILAIAAAKLGAkRVLAVDIdPVAVEAARENAELN 194
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 114-162 1.93e-04

HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 41.38  E-value: 1.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 62460540   114 NLVD---KNVIEIGAGTGLVSIVASLLGAHVTATDL-PELLGNLQYNISRNTK 162
Cdd:TIGR00537  14 NLRElkpDDVLEIGAGTGLVAIRLKGKGKCILTTDInPFAVKELRENAKLNNV 66
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 120-199 8.78e-04

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 37.93  E-value: 8.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460540   120 VIEIGAGTGLVSI-VASLLGAHVTATDL-PELLgnlqynisRNTKTKAKHLPQVKELSWGVALDKNFPRASinFDYILAA 197
Cdd:pfam13649   1 VLDLGCGTGRLTLaLARRGGARVTGVDLsPEML--------ERARERAAEAGLNVEFVQGDAEDLPFPDGS--FDLVVSS 70


                  ..
gi 62460540   198 DV 199
Cdd:pfam13649  71 GV 72
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 117-201 1.35e-03

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: 38.44  E-value: 1.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460540 117 DKNVIEIGAGTGLVSIVASLLGAHVTATDL-PELLgnlqynisRNTKTKAKHLPQVKELSWGVALDKNFPRASinFDYIL 195
Cdd:COG2226  23 GARVLDLGCGTGRLALALAERGARVTGVDIsPEML--------ELARERAAEAGLNVEFVVGDAEDLPFPDGS--FDLVI 92


                ....*.
gi 62460540 196 AADVVY 201
Cdd:COG2226  93 SSFVLH 98
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
117-216 3.52e-03

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 36.34  E-value: 3.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460540 117 DKNVIEIGAGTGLVS--IVASLLGAHVTATDL-PELLGNLQynisrntktkaKHLPQVkELSWGVALDKNFPRasiNFDY 193
Cdd:COG4106   2 PRRVLDLGCGTGRLTalLAERFPGARVTGVDLsPEMLARAR-----------ARLPNV-RFVVADLRDLDPPE---PFDL 66

                        90       100
                ....*....|....*....|...
gi 62460540 194 ILAADVVYahpFLEELLVTFDHL 216
Cdd:COG4106  67 VVSNAALH---WLPDHAALLARL 86
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 119-229 6.14e-03

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: 35.87  E-value: 6.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460540 119 NVIEIGAGTGLVSI-VASLLGAHVTATDL-PELLGNLQYNISRNTKTKAKHLPQvkelSWGVALDKNFPRasinFDYILA 196
Cdd:cd02440   1 RVLDLGCGTGALALaLASGPGARVTGVDIsPVALELARKAAAALLADNVEVLKG----DAEELPPEADES----FDVIIS 72

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 62460540 197 ADVVYA-----HPFLEELLvtfDHLCKETTVILWVMKF 229
Cdd:cd02440  73 DPPLHHlvedlARFLEEAR---RLLKPGGVLVLTLVLA 107
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 121-218 7.19e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 35.42  E-value: 7.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62460540   121 IEIGAGTG--LVSIVASLLGAHVTATDL-PELLGNLQynisrnTKTKAKHLPQVKELSWGVALDKNFPRASinFDYILAA 197
Cdd:pfam08242   1 LEIGCGTGtlLRALLEALPGLEYTGLDIsPAALEAAR------ERLAALGLLNAVRVELFQLDLGELDPGS--FDVVVAS 72

                          90       100
                  ....*....|....*....|.
gi 62460540   198 DVVYAHPFLEELLVTFDHLCK 218
Cdd:pfam08242  73 NVLHHLADPRAVLRNIRRLLK 93
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
117-159 9.28e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 36.42  E-value: 9.28e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 62460540 117 DKNVIEIGAGTGLVSIVASLLGA-HVTATDL-PELLGNLQYNISR 159
Cdd:COG2263  46 GKTVLDLGCGTGMLAIGAALLGAkKVVGVDIdPEALEIARENAER 90
 
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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