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Conserved domains on  [gi|392902088|ref|NP_001255892|]
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5'-nucleotidase [Caenorhabditis elegans]

Protein Classification

5'-nucleotidase( domain architecture ID 11576270)

5'-nucleotidase is a HAD (haloacid dehalogenase) family protein similar to cytosolic 5'-nucleotidases 3A and 3B, which are 7-methylguanosine phosphate-specific 5'-nucleotidases

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HAD_5NT cd07504
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to human cytosolic IIIA and IIIB; 5 ...
20-296 8.11e-152

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to human cytosolic IIIA and IIIB; 5'-nucleotidases dephosphorylate nucleoside 5prime-monophosphates. This family includes human 5'-nucleotidase, cytosolic IIIA (cN-IIIA, previously called cN-III; NT5C3A) the main pyrimidine 5'-nucleotidase in erythrocytes which dephosphorylates the pyrimidine nucleotides CMP, UMP, TMP, and the purine 7-methylguanosine monophosphate (m7GM), and possesses phosphotransferase activity. It also includes human 5'-nucleotidase, cytosolic IIIB (cN-IIIB; NT5C3B) which has a strong preference for m7GMP, dephosphorylates CMP and UMP and, with significantly lower efficiency, GMP and AMP, and can also act as a phosphotransferase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


:

Pssm-ID: 319807 [Multi-domain]  Cd Length: 273  Bit Score: 425.96  E-value: 8.11e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902088  20 DIKSLTDKLQNIVSGGADQLMVISDFDFTLSRFADKSGnRCSSCYCVFDSAVGtNNPEWCRKFVGLYHKYGPIEHDHSLS 99
Cdd:cd07504    1 DPTRVEEKICGLVKGGADKLQIISDFDMTLSRFRYNGG-RCPTCHNIFDNCKL-LTEECRAKLVQLKEKYYPIEIDPHLT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902088 100 IEEKVPFMEAWWQQSHGLIIQGGFKKQAIDDYVAHCNIQLRDNADIMMKKMTNHAVPFIIFSAGIGTIIEMYLRHKFGRv 179
Cdd:cd07504   79 IEEKVPYMEEWWTKSHELLIEQGFQKDAIDQIVAESDIALRDGYEEFFEKLQQHGIPVLIFSAGLGDIIEEVLRQAGVY- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902088 180 ESNTHVVSNMMGFDDDGYVNSFSDPLIHVFCKNSSVMpADRTFSEQIEGRKNVILLGDSVGDAFMDVGVEEEQVSLKIGF 259
Cdd:cd07504  158 HPNVKVVSNFMDFDDNGVLTGFKGPLIHVFNKNESAL-KNTDYFKQLKGRTNIILLGDSIGDLRMADGVPNVEHILKIGF 236
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 392902088 260 VNHDADKLVDKYLNYFDIVLVDDQSMDIPNQILEAIY 296
Cdd:cd07504  237 LNDKVEELLEKYMDSYDIVLVNDETLDVPNSILQKIL 273
 
Name Accession Description Interval E-value
HAD_5NT cd07504
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to human cytosolic IIIA and IIIB; 5 ...
20-296 8.11e-152

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to human cytosolic IIIA and IIIB; 5'-nucleotidases dephosphorylate nucleoside 5prime-monophosphates. This family includes human 5'-nucleotidase, cytosolic IIIA (cN-IIIA, previously called cN-III; NT5C3A) the main pyrimidine 5'-nucleotidase in erythrocytes which dephosphorylates the pyrimidine nucleotides CMP, UMP, TMP, and the purine 7-methylguanosine monophosphate (m7GM), and possesses phosphotransferase activity. It also includes human 5'-nucleotidase, cytosolic IIIB (cN-IIIB; NT5C3B) which has a strong preference for m7GMP, dephosphorylates CMP and UMP and, with significantly lower efficiency, GMP and AMP, and can also act as a phosphotransferase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319807 [Multi-domain]  Cd Length: 273  Bit Score: 425.96  E-value: 8.11e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902088  20 DIKSLTDKLQNIVSGGADQLMVISDFDFTLSRFADKSGnRCSSCYCVFDSAVGtNNPEWCRKFVGLYHKYGPIEHDHSLS 99
Cdd:cd07504    1 DPTRVEEKICGLVKGGADKLQIISDFDMTLSRFRYNGG-RCPTCHNIFDNCKL-LTEECRAKLVQLKEKYYPIEIDPHLT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902088 100 IEEKVPFMEAWWQQSHGLIIQGGFKKQAIDDYVAHCNIQLRDNADIMMKKMTNHAVPFIIFSAGIGTIIEMYLRHKFGRv 179
Cdd:cd07504   79 IEEKVPYMEEWWTKSHELLIEQGFQKDAIDQIVAESDIALRDGYEEFFEKLQQHGIPVLIFSAGLGDIIEEVLRQAGVY- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902088 180 ESNTHVVSNMMGFDDDGYVNSFSDPLIHVFCKNSSVMpADRTFSEQIEGRKNVILLGDSVGDAFMDVGVEEEQVSLKIGF 259
Cdd:cd07504  158 HPNVKVVSNFMDFDDNGVLTGFKGPLIHVFNKNESAL-KNTDYFKQLKGRTNIILLGDSIGDLRMADGVPNVEHILKIGF 236
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 392902088 260 VNHDADKLVDKYLNYFDIVLVDDQSMDIPNQILEAIY 296
Cdd:cd07504  237 LNDKVEELLEKYMDSYDIVLVNDETLDVPNSILQKIL 273
UMPH-1 pfam05822
Pyrimidine 5'-nucleotidase (UMPH-1); This family consists of several eukaryotic pyrimidine 5 ...
47-296 4.10e-139

Pyrimidine 5'-nucleotidase (UMPH-1); This family consists of several eukaryotic pyrimidine 5'-nucleotidase proteins. P5'N-1, also known as uridine monophosphate hydrolase-1 (UMPH-1), is a member of a large functional group of enzymes, characterized by the ability to dephosphorylate nucleic acids. P5'N-1 catalyzes the dephosphorylation of pyrimidine nucleoside monophosphates to the corresponding nucleosides. Deficiencies in this proteins function can lead to several different disorders in humans.


Pssm-ID: 310424 [Multi-domain]  Cd Length: 246  Bit Score: 392.49  E-value: 4.10e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902088   47 FTLSRFADkSGNRCSSCYCVFDSAvGTNNPEWCRKFVGLYHKYGPIEHDHSLSIEEKVPFMEAWWQQSHGLIIQGGFKKQ 126
Cdd:pfam05822   1 MTLSKFRV-NGERCPSSHGIFDNC-KSIPEECRKKLRELYHKYYPIEIDPHMPIEEKVPYMVEWWTKSHALLIGQGLQKE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902088  127 AIDDYVAHCNIQLRDNADIMMKKMTNHAVPFIIFSAGIGTIIEMYLRHKfGRVESNTHVVSNMMGFDDDGYVNSFSDPLI 206
Cdd:pfam05822  79 AIAEVVAESDIMLRDGTHEFFDDLQQLNVPVLIFSAGLGDVLEEVLRQA-NVMHPNVKVVSNFMDFDDDGVLNGFKGPLI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902088  207 HVFCKNSSVMPaDRTFSEQIEGRKNVILLGDSVGDAFMDVGVEEEQVSLKIGFVNHDADKLVDKYLNYFDIVLVDDQSMD 286
Cdd:pfam05822 158 HTFNKNETVLD-GTEYFDQLHTRDNIILLGDSLGDLGMADGVPSVEHILKIGFLNDKVEENLDKYMDAFDIVLVDDQTMD 236
                         250
                  ....*....|
gi 392902088  287 IPNQILEAIY 296
Cdd:pfam05822 237 VPNAILEMIL 246
HAD-SF-IE TIGR01544
haloacid dehalogenase superfamily, subfamily IE hydrolase, TIGR01544; This model represents a ...
15-295 3.66e-96

haloacid dehalogenase superfamily, subfamily IE hydrolase, TIGR01544; This model represents a small group of metazoan sequences. The sequences from mouse are annotated as Pyrimidine 5'-nucleotidases, aparrently in reference to HSPC233, the human homolog. However, no such annotation can currently be found for this gene. This group of sequences was found during searches for members of the haloacid dehalogenase (HAD) superfamily. All of the conserved catalytic motifs are found. The placement of the variable domain between motifs 1 and 2 indicates membership in subfamily I of the superfamily, but these sequences are sufficiently different from any of the branches (IA, TIGR01493, TIGR01509, TIGR01549; IB, TIGR01488; IC, TIGR01494; ID, TIGR01658; IF TIGR01545) of that subfamily as to constitute a separate branch to now be called IE. Considering that the closest identifiable hit outside of the noise range is to a phosphoserine phosphatase, this group may be considered to be most closely allied to subfamily IB.


Pssm-ID: 273683 [Multi-domain]  Cd Length: 283  Bit Score: 285.21  E-value: 3.66e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902088   15 QVHVKDIKSLTDKLQNIVSGGADQLMVISDFDFTLSRFADKSGNRCSSCYCVFDsAVGTNNPEWCRKFVGLYHKYGPIEH 94
Cdd:TIGR01544   5 HCRMRDPTEVERIINEFVIGGAEKMQIISDFDYTLSRFRTEDGGRVPTSHGIFD-ACQSLPEEFKAKTDKLKHKYYPIEI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902088   95 DHSLSIEEKVPFMEAWWQQSHGLIIQGGFKKQAIDDYVAHCNIQLRDNADIMMKKMTNHAVPFIIFSAGIGTIIEMYLRH 174
Cdd:TIGR01544  84 DPHLTIEEKVPYMIEWWTKSHELTVGFPFDKSEIDQIVSKSTHALKDGTEEFFADLQRHGIPTLIFSAGIGNSVESVLRQ 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902088  175 KfGRVESNTHVVSNMMGFDDDGYVNSFSDPLIHVFCKNSSVMPADRTFSEQIEGRKNVILLGDSVGDAFMDVGVEEEQVS 254
Cdd:TIGR01544 164 A-NVLHPNVKVVSNFLQFDEDGLLDGFQQPLIHTFNKNETVLNETTEYFDLVHTRDNIILLGDSIGDADMASGVPASSHI 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 392902088  255 LKIGFVNHDADKLVDKYLNYFDIVLVDDQSMDIPNQILEAI 295
Cdd:TIGR01544 243 LKIGYLNDHVDANLKKYMDTYDIVLVDDQTLDVARTILSLI 283
 
Name Accession Description Interval E-value
HAD_5NT cd07504
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to human cytosolic IIIA and IIIB; 5 ...
20-296 8.11e-152

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to human cytosolic IIIA and IIIB; 5'-nucleotidases dephosphorylate nucleoside 5prime-monophosphates. This family includes human 5'-nucleotidase, cytosolic IIIA (cN-IIIA, previously called cN-III; NT5C3A) the main pyrimidine 5'-nucleotidase in erythrocytes which dephosphorylates the pyrimidine nucleotides CMP, UMP, TMP, and the purine 7-methylguanosine monophosphate (m7GM), and possesses phosphotransferase activity. It also includes human 5'-nucleotidase, cytosolic IIIB (cN-IIIB; NT5C3B) which has a strong preference for m7GMP, dephosphorylates CMP and UMP and, with significantly lower efficiency, GMP and AMP, and can also act as a phosphotransferase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319807 [Multi-domain]  Cd Length: 273  Bit Score: 425.96  E-value: 8.11e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902088  20 DIKSLTDKLQNIVSGGADQLMVISDFDFTLSRFADKSGnRCSSCYCVFDSAVGtNNPEWCRKFVGLYHKYGPIEHDHSLS 99
Cdd:cd07504    1 DPTRVEEKICGLVKGGADKLQIISDFDMTLSRFRYNGG-RCPTCHNIFDNCKL-LTEECRAKLVQLKEKYYPIEIDPHLT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902088 100 IEEKVPFMEAWWQQSHGLIIQGGFKKQAIDDYVAHCNIQLRDNADIMMKKMTNHAVPFIIFSAGIGTIIEMYLRHKFGRv 179
Cdd:cd07504   79 IEEKVPYMEEWWTKSHELLIEQGFQKDAIDQIVAESDIALRDGYEEFFEKLQQHGIPVLIFSAGLGDIIEEVLRQAGVY- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902088 180 ESNTHVVSNMMGFDDDGYVNSFSDPLIHVFCKNSSVMpADRTFSEQIEGRKNVILLGDSVGDAFMDVGVEEEQVSLKIGF 259
Cdd:cd07504  158 HPNVKVVSNFMDFDDNGVLTGFKGPLIHVFNKNESAL-KNTDYFKQLKGRTNIILLGDSIGDLRMADGVPNVEHILKIGF 236
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 392902088 260 VNHDADKLVDKYLNYFDIVLVDDQSMDIPNQILEAIY 296
Cdd:cd07504  237 LNDKVEELLEKYMDSYDIVLVNDETLDVPNSILQKIL 273
UMPH-1 pfam05822
Pyrimidine 5'-nucleotidase (UMPH-1); This family consists of several eukaryotic pyrimidine 5 ...
47-296 4.10e-139

Pyrimidine 5'-nucleotidase (UMPH-1); This family consists of several eukaryotic pyrimidine 5'-nucleotidase proteins. P5'N-1, also known as uridine monophosphate hydrolase-1 (UMPH-1), is a member of a large functional group of enzymes, characterized by the ability to dephosphorylate nucleic acids. P5'N-1 catalyzes the dephosphorylation of pyrimidine nucleoside monophosphates to the corresponding nucleosides. Deficiencies in this proteins function can lead to several different disorders in humans.


Pssm-ID: 310424 [Multi-domain]  Cd Length: 246  Bit Score: 392.49  E-value: 4.10e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902088   47 FTLSRFADkSGNRCSSCYCVFDSAvGTNNPEWCRKFVGLYHKYGPIEHDHSLSIEEKVPFMEAWWQQSHGLIIQGGFKKQ 126
Cdd:pfam05822   1 MTLSKFRV-NGERCPSSHGIFDNC-KSIPEECRKKLRELYHKYYPIEIDPHMPIEEKVPYMVEWWTKSHALLIGQGLQKE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902088  127 AIDDYVAHCNIQLRDNADIMMKKMTNHAVPFIIFSAGIGTIIEMYLRHKfGRVESNTHVVSNMMGFDDDGYVNSFSDPLI 206
Cdd:pfam05822  79 AIAEVVAESDIMLRDGTHEFFDDLQQLNVPVLIFSAGLGDVLEEVLRQA-NVMHPNVKVVSNFMDFDDDGVLNGFKGPLI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902088  207 HVFCKNSSVMPaDRTFSEQIEGRKNVILLGDSVGDAFMDVGVEEEQVSLKIGFVNHDADKLVDKYLNYFDIVLVDDQSMD 286
Cdd:pfam05822 158 HTFNKNETVLD-GTEYFDQLHTRDNIILLGDSLGDLGMADGVPSVEHILKIGFLNDKVEENLDKYMDAFDIVLVDDQTMD 236
                         250
                  ....*....|
gi 392902088  287 IPNQILEAIY 296
Cdd:pfam05822 237 VPNAILEMIL 246
HAD-SF-IE TIGR01544
haloacid dehalogenase superfamily, subfamily IE hydrolase, TIGR01544; This model represents a ...
15-295 3.66e-96

haloacid dehalogenase superfamily, subfamily IE hydrolase, TIGR01544; This model represents a small group of metazoan sequences. The sequences from mouse are annotated as Pyrimidine 5'-nucleotidases, aparrently in reference to HSPC233, the human homolog. However, no such annotation can currently be found for this gene. This group of sequences was found during searches for members of the haloacid dehalogenase (HAD) superfamily. All of the conserved catalytic motifs are found. The placement of the variable domain between motifs 1 and 2 indicates membership in subfamily I of the superfamily, but these sequences are sufficiently different from any of the branches (IA, TIGR01493, TIGR01509, TIGR01549; IB, TIGR01488; IC, TIGR01494; ID, TIGR01658; IF TIGR01545) of that subfamily as to constitute a separate branch to now be called IE. Considering that the closest identifiable hit outside of the noise range is to a phosphoserine phosphatase, this group may be considered to be most closely allied to subfamily IB.


Pssm-ID: 273683 [Multi-domain]  Cd Length: 283  Bit Score: 285.21  E-value: 3.66e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902088   15 QVHVKDIKSLTDKLQNIVSGGADQLMVISDFDFTLSRFADKSGNRCSSCYCVFDsAVGTNNPEWCRKFVGLYHKYGPIEH 94
Cdd:TIGR01544   5 HCRMRDPTEVERIINEFVIGGAEKMQIISDFDYTLSRFRTEDGGRVPTSHGIFD-ACQSLPEEFKAKTDKLKHKYYPIEI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902088   95 DHSLSIEEKVPFMEAWWQQSHGLIIQGGFKKQAIDDYVAHCNIQLRDNADIMMKKMTNHAVPFIIFSAGIGTIIEMYLRH 174
Cdd:TIGR01544  84 DPHLTIEEKVPYMIEWWTKSHELTVGFPFDKSEIDQIVSKSTHALKDGTEEFFADLQRHGIPTLIFSAGIGNSVESVLRQ 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902088  175 KfGRVESNTHVVSNMMGFDDDGYVNSFSDPLIHVFCKNSSVMPADRTFSEQIEGRKNVILLGDSVGDAFMDVGVEEEQVS 254
Cdd:TIGR01544 164 A-NVLHPNVKVVSNFLQFDEDGLLDGFQQPLIHTFNKNETVLNETTEYFDLVHTRDNIILLGDSIGDADMASGVPASSHI 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 392902088  255 LKIGFVNHDADKLVDKYLNYFDIVLVDDQSMDIPNQILEAI 295
Cdd:TIGR01544 243 LKIGYLNDHVDANLKKYMDTYDIVLVDDQTLDVARTILSLI 283
 
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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