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Conserved domains on  [gi|19527406|ref|NP_599007|]
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acyl-coenzyme A thioesterase 3 isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
214-423 1.07e-120

BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C terminal of acyl-CoA thioester hydrolases and bile acid-CoA:amino acid N-acetyltransferases (BAAT).


:

Pssm-ID: 430252 [Multi-domain]  Cd Length: 211  Bit Score: 349.66  E-value: 1.07e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406   214 IHLEYFEEAVTYLLSHPQVTGSGVGVLGISKGGELGFAMASFLKNITAAVIINGSISNIGGNLQYKDETVPSVGINTKRV 293
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406   294 KRTKDGLKDIVDLLNNPLEGPDQKSLIPVERSDTAFLFLVGQDDHNWKSEFYAREASKRLQAHGKE-KPQIICYPETGHH 372
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKPDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEvEVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 19527406   373 IEPPYFPLCKASLNSLVGGPVIWGGEPRAHAMAQVDAWQQLQTFFHNHLDG 423
Cdd:pfam08840 161 IEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
27-152 5.01e-60

Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini of acyl-CoA thioester hydrolase and bile acid-CoA:amino acid N-acetyltransferase (BAAT). This region is not thought to contain the active site of either enzyme. Thioesterase isoforms have been identified in peroxisomes, cytoplasm and mitochondria, where they are thought to have distinct functions in lipid metabolism. For example, in peroxisomes, the hydrolase acts on bile-CoA esters.


:

Pssm-ID: 461422  Cd Length: 127  Bit Score: 191.68  E-value: 5.01e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406    27 DQPVHIAVRGLAPEQPVTLRSVLRDEKGALFRAHARYRADSHGELDLARTPALGGSFSGLEPMGLLWAMEPDRPFW-RLI 105
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFRpRLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 19527406   106 KRDVQ-TPFVVELEVLDGHEPDgGQRLARAVHERHFMAPGVRRVPVRE 152
Cdd:pfam04775  81 KRDVLpTPFVVTLSVYDGSEES-GKPLASVTVERWYMAPGVRRIEVRE 127
Axe1 super family cl34617
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
150-263 1.10e-06

Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];


The actual alignment was detected with superfamily member COG3458:

Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 50.19  E-value: 1.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406 150 VREGRVRATLFLPPGTGPFPGIIdLF---GIGSGLLeYRASLLAGKGFAVMAL---------------------AYNNY- 204
Cdd:COG3458  64 FGGARIYGWLLRPKGEGPLPAVV-EFhgyGGGRGLP-HEDLDWAAAGYAVLVMdtrgqgsswgdtpdpggysggALPGYm 141
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406 205 ----EDlPKD-------MDIIHleyfeeAVTYLLSHPQVTGSGVGVLGISKGGELGFAMASFLKNITAAV 263
Cdd:COG3458 142 trgiDD-PDTyyyrrvyLDAVR------AVDALRSLPEVDGKRIGVTGGSQGGGLALAAAALDPRVKAAA 204
 
Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
214-423 1.07e-120

BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C terminal of acyl-CoA thioester hydrolases and bile acid-CoA:amino acid N-acetyltransferases (BAAT).


Pssm-ID: 430252 [Multi-domain]  Cd Length: 211  Bit Score: 349.66  E-value: 1.07e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406   214 IHLEYFEEAVTYLLSHPQVTGSGVGVLGISKGGELGFAMASFLKNITAAVIINGSISNIGGNLQYKDETVPSVGINTKRV 293
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406   294 KRTKDGLKDIVDLLNNPLEGPDQKSLIPVERSDTAFLFLVGQDDHNWKSEFYAREASKRLQAHGKE-KPQIICYPETGHH 372
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKPDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEvEVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 19527406   373 IEPPYFPLCKASLNSLVGGPVIWGGEPRAHAMAQVDAWQQLQTFFHNHLDG 423
Cdd:pfam08840 161 IEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
27-152 5.01e-60

Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini of acyl-CoA thioester hydrolase and bile acid-CoA:amino acid N-acetyltransferase (BAAT). This region is not thought to contain the active site of either enzyme. Thioesterase isoforms have been identified in peroxisomes, cytoplasm and mitochondria, where they are thought to have distinct functions in lipid metabolism. For example, in peroxisomes, the hydrolase acts on bile-CoA esters.


Pssm-ID: 461422  Cd Length: 127  Bit Score: 191.68  E-value: 5.01e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406    27 DQPVHIAVRGLAPEQPVTLRSVLRDEKGALFRAHARYRADSHGELDLARTPALGGSFSGLEPMGLLWAMEPDRPFW-RLI 105
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFRpRLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 19527406   106 KRDVQ-TPFVVELEVLDGHEPDgGQRLARAVHERHFMAPGVRRVPVRE 152
Cdd:pfam04775  81 KRDVLpTPFVVTLSVYDGSEES-GKPLASVTVERWYMAPGVRRIEVRE 127
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
147-379 3.18e-16

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 77.75  E-value: 3.18e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406 147 RVPVREG-RVRATLFLPPGTGPFPGIIDLFGIGSGLLE---YRASLLAGKGFAVMALAYNNYEDLPKDMDIIHLEYFEEA 222
Cdd:COG1506   1 TFKSADGtTLPGWLYLPADGKKYPVVVYVHGGPGSRDDsflPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDVLAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406 223 VTYLLSHPQVTGSGVGVLGISKGGELGFAMASFLKNITAAVIINGSISNIGGnlqykdetvpsvgintkRVKRTKDGLKD 302
Cdd:COG1506  81 IDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRS-----------------YYGTTREYTER 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19527406 303 IVDLLNNPLEGPDQKSLIP-VERSDTAFLFLVGQDDHNWKSEfYAREASKRLQAHGKEKpQIICYPETGHHIEPPYFP 379
Cdd:COG1506 144 LMGGPWEDPEAYAARSPLAyADKLKTPLLLIHGEADDRVPPE-QAERLYEALKKAGKPV-ELLVYPGEGHGFSGAGAP 219
Axe1 COG3458
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
150-263 1.10e-06

Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 50.19  E-value: 1.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406 150 VREGRVRATLFLPPGTGPFPGIIdLF---GIGSGLLeYRASLLAGKGFAVMAL---------------------AYNNY- 204
Cdd:COG3458  64 FGGARIYGWLLRPKGEGPLPAVV-EFhgyGGGRGLP-HEDLDWAAAGYAVLVMdtrgqgsswgdtpdpggysggALPGYm 141
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406 205 ----EDlPKD-------MDIIHleyfeeAVTYLLSHPQVTGSGVGVLGISKGGELGFAMASFLKNITAAV 263
Cdd:COG3458 142 trgiDD-PDTyyyrrvyLDAVR------AVDALRSLPEVDGKRIGVTGGSQGGGLALAAAALDPRVKAAA 204
DLH pfam01738
Dienelactone hydrolase family;
156-268 5.46e-04

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 41.18  E-value: 5.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406   156 RATLFLPPGtGPFPGII---DLFGIGSGLLEYRASLlAGKGFAVMA-------LAYNNYEDLPKDMDIIH--------LE 217
Cdd:pfam01738   1 DAYLATPKN-PPWPVVVvfqEIFGVNDNIREIADRL-ADEGYVALApdlyfrqGDPNDEADAARAMFELVskrvmekvLD 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 19527406   218 YFEEAVTYLLSHPQVTGSGVGVLGISKGGELGFAMASFLKNITAAVIINGS 268
Cdd:pfam01738  79 DLEAAVNYLKSQPEVSPKKVGVVGYCMGGALAVLLAAKGPLVDAAVGFYGV 129
 
Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
214-423 1.07e-120

BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C terminal of acyl-CoA thioester hydrolases and bile acid-CoA:amino acid N-acetyltransferases (BAAT).


Pssm-ID: 430252 [Multi-domain]  Cd Length: 211  Bit Score: 349.66  E-value: 1.07e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406   214 IHLEYFEEAVTYLLSHPQVTGSGVGVLGISKGGELGFAMASFLKNITAAVIINGSISNIGGNLQYKDETVPSVGINTKRV 293
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPGIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLVYKDNPLPPLGEGMRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406   294 KRTKDGLKDIVDLLNNPLEGPDQKSLIPVERSDTAFLFLVGQDDHNWKSEFYAREASKRLQAHGKE-KPQIICYPETGHH 372
Cdd:pfam08840  81 KVNKDGLLDIRDMFNDPLSKPDPKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERLQKHGKEvEVQLVCYPGAGHL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 19527406   373 IEPPYFPLCKASLNSLVGGPVIWGGEPRAHAMAQVDAWQQLQTFFHNHLDG 423
Cdd:pfam08840 161 IEPPYFPHCGASFHALVGMPVLWGGEPKAHAKAQEDAWKKIQAFFHKHLGG 211
Bile_Hydr_Trans pfam04775
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
27-152 5.01e-60

Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini of acyl-CoA thioester hydrolase and bile acid-CoA:amino acid N-acetyltransferase (BAAT). This region is not thought to contain the active site of either enzyme. Thioesterase isoforms have been identified in peroxisomes, cytoplasm and mitochondria, where they are thought to have distinct functions in lipid metabolism. For example, in peroxisomes, the hydrolase acts on bile-CoA esters.


Pssm-ID: 461422  Cd Length: 127  Bit Score: 191.68  E-value: 5.01e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406    27 DQPVHIAVRGLAPEQPVTLRSVLRDEKGALFRAHARYRADSHGELDLARTPALGGSFSGLEPMGLLWAMEPDRPFW-RLI 105
Cdd:pfam04775   1 DEPVHIRVSGLPPGQPVTLRALLTDEKGGLFESYAVYRADENGEVDLSRDAPLGGSYTGVDPMGLFWSMKPEPGFRpRLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 19527406   106 KRDVQ-TPFVVELEVLDGHEPDgGQRLARAVHERHFMAPGVRRVPVRE 152
Cdd:pfam04775  81 KRDVLpTPFVVTLSVYDGSEES-GKPLASVTVERWYMAPGVRRIEVRE 127
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
147-379 3.18e-16

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 77.75  E-value: 3.18e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406 147 RVPVREG-RVRATLFLPPGTGPFPGIIDLFGIGSGLLE---YRASLLAGKGFAVMALAYNNYEDLPKDMDIIHLEYFEEA 222
Cdd:COG1506   1 TFKSADGtTLPGWLYLPADGKKYPVVVYVHGGPGSRDDsflPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDVLAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406 223 VTYLLSHPQVTGSGVGVLGISKGGELGFAMASFLKNITAAVIINGSISNIGGnlqykdetvpsvgintkRVKRTKDGLKD 302
Cdd:COG1506  81 IDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRS-----------------YYGTTREYTER 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19527406 303 IVDLLNNPLEGPDQKSLIP-VERSDTAFLFLVGQDDHNWKSEfYAREASKRLQAHGKEKpQIICYPETGHHIEPPYFP 379
Cdd:COG1506 144 LMGGPWEDPEAYAARSPLAyADKLKTPLLLIHGEADDRVPPE-QAERLYEALKKAGKPV-ELLVYPGEGHGFSGAGAP 219
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
153-417 2.77e-14

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 71.92  E-value: 2.77e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406 153 GRVRATLFLPPGTGPFPGIIDLFGIGsGLLEY---RASLLAGKGFAVMALAYNNYEDLPKDMDIIH-----------LEY 218
Cdd:COG0412  14 VTLPGYLARPAGGGPRPGVVVLHEIF-GLNPHirdVARRLAAAGYVVLAPDLYGRGGPGDDPDEARalmgaldpellAAD 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406 219 FEEAVTYLLSHPQVTGSGVGVLGISKGGELGFAMASFLKNITAAVIINGSisniggnlqykdetvpsvgintkrvkRTKD 298
Cdd:COG0412  93 LRAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAVSFYGG--------------------------LPAD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406 299 GLKDIVDLLNNPLegpdqkslipversdtafLFLVGQDDHNWKSEfYAREASKRLQAHGKEKpQIICYPETGHhieppyf 378
Cdd:COG0412 147 DLLDLAARIKAPV------------------LLLYGEKDPLVPPE-QVAALEAALAAAGVDV-ELHVYPGAGH------- 199
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 19527406 379 plckASLNSlvggpviwgGEPRAHAMAQVDAWQQLQTFF 417
Cdd:COG0412 200 ----GFTNP---------GRPRYDPAAAEDAWQRTLAFL 225
Axe1 COG3458
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
150-263 1.10e-06

Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 50.19  E-value: 1.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406 150 VREGRVRATLFLPPGTGPFPGIIdLF---GIGSGLLeYRASLLAGKGFAVMAL---------------------AYNNY- 204
Cdd:COG3458  64 FGGARIYGWLLRPKGEGPLPAVV-EFhgyGGGRGLP-HEDLDWAAAGYAVLVMdtrgqgsswgdtpdpggysggALPGYm 141
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406 205 ----EDlPKD-------MDIIHleyfeeAVTYLLSHPQVTGSGVGVLGISKGGELGFAMASFLKNITAAV 263
Cdd:COG3458 142 trgiDD-PDTyyyrrvyLDAVR------AVDALRSLPEVDGKRIGVTGGSQGGGLALAAAALDPRVKAAA 204
DLH pfam01738
Dienelactone hydrolase family;
156-268 5.46e-04

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 41.18  E-value: 5.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527406   156 RATLFLPPGtGPFPGII---DLFGIGSGLLEYRASLlAGKGFAVMA-------LAYNNYEDLPKDMDIIH--------LE 217
Cdd:pfam01738   1 DAYLATPKN-PPWPVVVvfqEIFGVNDNIREIADRL-ADEGYVALApdlyfrqGDPNDEADAARAMFELVskrvmekvLD 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 19527406   218 YFEEAVTYLLSHPQVTGSGVGVLGISKGGELGFAMASFLKNITAAVIINGS 268
Cdd:pfam01738  79 DLEAAVNYLKSQPEVSPKKVGVVGYCMGGALAVLLAAKGPLVDAAVGFYGV 129
 
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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