NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|118918379|ref|NP_001073145|]
View 

monoacylglycerol lipase ABHD2 [Danio rerio]

Protein Classification

alpha/beta fold hydrolase family protein( domain architecture ID 1903474)

alpha/beta fold hydrolase catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad; similar to monoacylglycerol lipase ABHD2

CATH:  3.40.50.1820
EC:  3.1.1.-
Gene Ontology:  GO:0016787
SCOP:  3000102

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
YheT super family cl43141
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
69-406 4.14e-56

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


The actual alignment was detected with superfamily member COG0429:

Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 187.66  E-value: 4.14e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379  69 TKEYIPPLlWGKSGHLQTaLYGKIGRvKSPKPCGLRKFLPMQDGATATFDLFEPQGVHSTgddiTMVICPGIGNHSEKHY 148
Cdd:COG0429    6 TSPFRPPW-WLRNGHLQT-IYPSLFR-RRPALPYRRERLELPDGDFVDLDWSDPPAPSKP----LVVLLHGLEGSSDSHY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379 149 IRTFVDYSQKQGYRCAVLNHLGA--LPNielTSPRMFTYGCTWEFSAMVGFIKRTFPQTQLIVVGFSLGGNIACKYLGEN 226
Cdd:COG0429   79 ARGLARALYARGWDVVRLNFRGCggEPN---LLPRLYHSGDTEDLVWVLAHLRARYPYAPLYAVGFSLGGNLLLKYLGEQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379 227 PANQERVLCCVSVCQGY---SALRAQETFLQwdqcrRLY--NFLmaDNMKKIILSHRgSLFGmnssrmEFADLSRLYTAT 301
Cdd:COG0429  156 GDDAPPLKAAVAVSPPLdlaASADRLERGFN-----RLYqrYFL--RSLKRKLRRKL-ALFP------GLIDLEALKRIR 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379 302 SLMQIDDNIMRKFHGHNSLKEYYEKESCVHYIHNISVPLLLVNSSDDPLVHQSllTIPRtLAEKKQNVIFALTLHGGHLG 381
Cdd:COG0429  222 TLREFDDAYTAPLHGFKDAEDYYQRASALPFLPQIRVPTLILNAADDPFLPPE--CLPE-AAELNPNVTLELTKHGGHVG 298
                        330       340
                 ....*....|....*....|....*
gi 118918379 382 FFEGAvlFPQPLSWMDKVIVSYANA 406
Cdd:COG0429  299 FISGK--SPGRRYWLERRILEFLDA 321
 
Name Accession Description Interval E-value
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
69-406 4.14e-56

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 187.66  E-value: 4.14e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379  69 TKEYIPPLlWGKSGHLQTaLYGKIGRvKSPKPCGLRKFLPMQDGATATFDLFEPQGVHSTgddiTMVICPGIGNHSEKHY 148
Cdd:COG0429    6 TSPFRPPW-WLRNGHLQT-IYPSLFR-RRPALPYRRERLELPDGDFVDLDWSDPPAPSKP----LVVLLHGLEGSSDSHY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379 149 IRTFVDYSQKQGYRCAVLNHLGA--LPNielTSPRMFTYGCTWEFSAMVGFIKRTFPQTQLIVVGFSLGGNIACKYLGEN 226
Cdd:COG0429   79 ARGLARALYARGWDVVRLNFRGCggEPN---LLPRLYHSGDTEDLVWVLAHLRARYPYAPLYAVGFSLGGNLLLKYLGEQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379 227 PANQERVLCCVSVCQGY---SALRAQETFLQwdqcrRLY--NFLmaDNMKKIILSHRgSLFGmnssrmEFADLSRLYTAT 301
Cdd:COG0429  156 GDDAPPLKAAVAVSPPLdlaASADRLERGFN-----RLYqrYFL--RSLKRKLRRKL-ALFP------GLIDLEALKRIR 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379 302 SLMQIDDNIMRKFHGHNSLKEYYEKESCVHYIHNISVPLLLVNSSDDPLVHQSllTIPRtLAEKKQNVIFALTLHGGHLG 381
Cdd:COG0429  222 TLREFDDAYTAPLHGFKDAEDYYQRASALPFLPQIRVPTLILNAADDPFLPPE--CLPE-AAELNPNVTLELTKHGGHVG 298
                        330       340
                 ....*....|....*....|....*
gi 118918379 382 FFEGAvlFPQPLSWMDKVIVSYANA 406
Cdd:COG0429  299 FISGK--SPGRRYWLERRILEFLDA 321
PLN02511 PLN02511
hydrolase
58-407 7.82e-35

hydrolase


Pssm-ID: 215282 [Multi-domain]  Cd Length: 388  Bit Score: 132.98  E-value: 7.82e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379  58 NHYLLKSCPVLTKEYIP-PLLwgKSGHLQTALYGKIGRVksPKPCGLRKFLPMQDGATATFDLfePQGVHST--GDDITM 134
Cdd:PLN02511  30 RDSFLPKFKSLERPYDAfPLL--GNRHVETIFASFFRSL--PAVRYRRECLRTPDGGAVALDW--VSGDDRAlpADAPVL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379 135 VICPGIGNHSEKHYIRTFVDYSQKQGYRCAVLNHLGAlPNIELTSPRMFTYGCTWEFSAMVGFIKRTFPQTQLIVVGFSL 214
Cdd:PLN02511 104 ILLPGLTGGSDDSYVRHMLLRARSKGWRVVVFNSRGC-ADSPVTTPQFYSASFTGDLRQVVDHVAGRYPSANLYAAGWSL 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379 215 GGNIACKYLGENPANQeRVLCCVSVCQGYSALRAQETFLQwdQCRRLYNFLMADNMKKIILSHRGSLFGMNSsrmEFaDL 294
Cdd:PLN02511 183 GANILVNYLGEEGENC-PLSGAVSLCNPFDLVIADEDFHK--GFNNVYDKALAKALRKIFAKHALLFEGLGG---EY-NI 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379 295 SRLYTATSLMQIDDNIMRKFHGHNSLKEYYEKESCVHYIHNISVPLLLVNSSDDPLVHQSllTIPRTLAEKKQNVIFALT 374
Cdd:PLN02511 256 PLVANAKTVRDFDDGLTRVSFGFKSVDAYYSNSSSSDSIKHVRVPLLCIQAANDPIAPAR--GIPREDIKANPNCLLIVT 333
                        330       340       350
                 ....*....|....*....|....*....|...
gi 118918379 375 LHGGHLGFFEGAVLfPQPLSWMDKVIVSYANAV 407
Cdd:PLN02511 334 PSGGHLGWVAGPEA-PFGAPWTDPVVMEFLEAL 365
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
133-386 2.94e-29

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 114.14  E-value: 2.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379  133 TMVICPGIGNHSekHYIRTFVDYSQKQGYRCAVLNHLGALPNIELTSPRMFtygCTWEFSAMVGFIKRTFPQTQLIVVGF 212
Cdd:pfam00561   2 PVLLLHGLPGSS--DLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDY---RTDDLAEDLEYILEALGLEKVNLVGH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379  213 SLGGNIACKYLGENPanqERVLCCVSVCqgysalrAQETFLQWDQCRRLYNFLMADNMKKIILS----HRGSLFGMNS-- 286
Cdd:pfam00561  77 SMGGLIALAYAAKYP---DRVKALVLLG-------ALDPPHELDEADRFILALFPGFFDGFVADfapnPLGRLVAKLLal 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379  287 --SRMEFADLSRLYTATSLMQIDDNIMRKFHGHNSLKEYYEKESCVHYIHNISVPLLLVNSSDDPLV-HQSLLTIPRTLA 363
Cdd:pfam00561 147 llLRLRLLKALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVpPQALEKLAQLFP 226
                         250       260
                  ....*....|....*....|...
gi 118918379  364 EKKQNVIFaltlHGGHLGFFEGA 386
Cdd:pfam00561 227 NARLVVIP----DAGHFAFLEGP 245
 
Name Accession Description Interval E-value
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
69-406 4.14e-56

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 187.66  E-value: 4.14e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379  69 TKEYIPPLlWGKSGHLQTaLYGKIGRvKSPKPCGLRKFLPMQDGATATFDLFEPQGVHSTgddiTMVICPGIGNHSEKHY 148
Cdd:COG0429    6 TSPFRPPW-WLRNGHLQT-IYPSLFR-RRPALPYRRERLELPDGDFVDLDWSDPPAPSKP----LVVLLHGLEGSSDSHY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379 149 IRTFVDYSQKQGYRCAVLNHLGA--LPNielTSPRMFTYGCTWEFSAMVGFIKRTFPQTQLIVVGFSLGGNIACKYLGEN 226
Cdd:COG0429   79 ARGLARALYARGWDVVRLNFRGCggEPN---LLPRLYHSGDTEDLVWVLAHLRARYPYAPLYAVGFSLGGNLLLKYLGEQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379 227 PANQERVLCCVSVCQGY---SALRAQETFLQwdqcrRLY--NFLmaDNMKKIILSHRgSLFGmnssrmEFADLSRLYTAT 301
Cdd:COG0429  156 GDDAPPLKAAVAVSPPLdlaASADRLERGFN-----RLYqrYFL--RSLKRKLRRKL-ALFP------GLIDLEALKRIR 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379 302 SLMQIDDNIMRKFHGHNSLKEYYEKESCVHYIHNISVPLLLVNSSDDPLVHQSllTIPRtLAEKKQNVIFALTLHGGHLG 381
Cdd:COG0429  222 TLREFDDAYTAPLHGFKDAEDYYQRASALPFLPQIRVPTLILNAADDPFLPPE--CLPE-AAELNPNVTLELTKHGGHVG 298
                        330       340
                 ....*....|....*....|....*
gi 118918379 382 FFEGAvlFPQPLSWMDKVIVSYANA 406
Cdd:COG0429  299 FISGK--SPGRRYWLERRILEFLDA 321
PLN02511 PLN02511
hydrolase
58-407 7.82e-35

hydrolase


Pssm-ID: 215282 [Multi-domain]  Cd Length: 388  Bit Score: 132.98  E-value: 7.82e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379  58 NHYLLKSCPVLTKEYIP-PLLwgKSGHLQTALYGKIGRVksPKPCGLRKFLPMQDGATATFDLfePQGVHST--GDDITM 134
Cdd:PLN02511  30 RDSFLPKFKSLERPYDAfPLL--GNRHVETIFASFFRSL--PAVRYRRECLRTPDGGAVALDW--VSGDDRAlpADAPVL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379 135 VICPGIGNHSEKHYIRTFVDYSQKQGYRCAVLNHLGAlPNIELTSPRMFTYGCTWEFSAMVGFIKRTFPQTQLIVVGFSL 214
Cdd:PLN02511 104 ILLPGLTGGSDDSYVRHMLLRARSKGWRVVVFNSRGC-ADSPVTTPQFYSASFTGDLRQVVDHVAGRYPSANLYAAGWSL 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379 215 GGNIACKYLGENPANQeRVLCCVSVCQGYSALRAQETFLQwdQCRRLYNFLMADNMKKIILSHRGSLFGMNSsrmEFaDL 294
Cdd:PLN02511 183 GANILVNYLGEEGENC-PLSGAVSLCNPFDLVIADEDFHK--GFNNVYDKALAKALRKIFAKHALLFEGLGG---EY-NI 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379 295 SRLYTATSLMQIDDNIMRKFHGHNSLKEYYEKESCVHYIHNISVPLLLVNSSDDPLVHQSllTIPRTLAEKKQNVIFALT 374
Cdd:PLN02511 256 PLVANAKTVRDFDDGLTRVSFGFKSVDAYYSNSSSSDSIKHVRVPLLCIQAANDPIAPAR--GIPREDIKANPNCLLIVT 333
                        330       340       350
                 ....*....|....*....|....*....|...
gi 118918379 375 LHGGHLGFFEGAVLfPQPLSWMDKVIVSYANAV 407
Cdd:PLN02511 334 PSGGHLGWVAGPEA-PFGAPWTDPVVMEFLEAL 365
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
133-386 2.94e-29

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 114.14  E-value: 2.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379  133 TMVICPGIGNHSekHYIRTFVDYSQKQGYRCAVLNHLGALPNIELTSPRMFtygCTWEFSAMVGFIKRTFPQTQLIVVGF 212
Cdd:pfam00561   2 PVLLLHGLPGSS--DLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDY---RTDDLAEDLEYILEALGLEKVNLVGH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379  213 SLGGNIACKYLGENPanqERVLCCVSVCqgysalrAQETFLQWDQCRRLYNFLMADNMKKIILS----HRGSLFGMNS-- 286
Cdd:pfam00561  77 SMGGLIALAYAAKYP---DRVKALVLLG-------ALDPPHELDEADRFILALFPGFFDGFVADfapnPLGRLVAKLLal 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379  287 --SRMEFADLSRLYTATSLMQIDDNIMRKFHGHNSLKEYYEKESCVHYIHNISVPLLLVNSSDDPLV-HQSLLTIPRTLA 363
Cdd:pfam00561 147 llLRLRLLKALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVpPQALEKLAQLFP 226
                         250       260
                  ....*....|....*....|...
gi 118918379  364 EKKQNVIFaltlHGGHLGFFEGA 386
Cdd:pfam00561 227 NARLVVIP----DAGHFAFLEGP 245
PRK10985 PRK10985
putative hydrolase; Provisional
198-403 3.12e-15

putative hydrolase; Provisional


Pssm-ID: 182883  Cd Length: 324  Bit Score: 76.15  E-value: 3.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379 198 IKRTFPQTQLIVVGFSLGGNIACKYLGENPANqervlCCVSVCQGYSA--------LRAQETFLQWDQcRRLYNFLMADN 269
Cdd:PRK10985 124 LQREFGHVPTAAVGYSLGGNMLACLLAKEGDD-----LPLDAAVIVSAplmleacsYRMEQGFSRVYQ-RYLLNLLKANA 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379 270 MKKIILSHrGSLFgmnssrmefADLSRLYTATSLMQIDDNIMRKFHGHNSLKEYYEKESCVHYIHNISVPLLLVNSSDDP 349
Cdd:PRK10985 198 ARKLAAYP-GTLP---------INLAQLKSVRRLREFDDLITARIHGFADAIDYYRQCSALPLLNQIRKPTLIIHAKDDP 267
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 118918379 350 LVHQSLLTIPRTLAEkkqNVIFALTLHGGHLGFFEGAVLFPQPlsWMDKVIVSY 403
Cdd:PRK10985 268 FMTHEVIPKPESLPP---NVEYQLTEHGGHVGFVGGTLLKPQM--WLEQRIPDW 316
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
106-228 6.77e-07

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 50.00  E-value: 6.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379 106 FLPMQDGATATFDLFEPQGVHSTgddiTMVICPGIGNHSEKHyiRTFVDYSQKQGYRCAVLNHL--GAlpnieltSPRMF 183
Cdd:COG2267    7 TLPTRDGLRLRGRRWRPAGSPRG----TVVLVHGLGEHSGRY--AELAEALAAAGYAVLAFDLRghGR-------SDGPR 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 118918379 184 TYGCTWE-----FSAMVGFIKRTfPQTQLIVVGFSLGGNIACKYLGENPA 228
Cdd:COG2267   74 GHVDSFDdyvddLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPD 122
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
133-352 2.37e-06

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 48.36  E-value: 2.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379  133 TMVICPGIGNHSEKhYIRtFVDYSQKQGYRCAVLNHLGA---------LPNIEltspRMFTygctwEFSAMVGFIKRTFP 203
Cdd:pfam12146   6 VVVLVHGLGEHSGR-YAH-LADALAAQGFAVYAYDHRGHgrsdgkrghVPSFD----DYVD-----DLDTFVDKIREEHP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118918379  204 QTQLIVVGFSLGGNIACKYLGENPANQER-VLCCvsvcqgySALRAQETFLQWDQcrRLYNFLMADNMKKIILSHRGsLF 282
Cdd:pfam12146  75 GLPLFLLGHSMGGLIAALYALRYPDKVDGlILSA-------PALKIKPYLAPPIL--KLLAKLLGKLFPRLRVPNNL-LP 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118918379  283 GMNSSRMEFAdlsRLYTATSLMqiddnimrkfHGHNSLKEYYE----KESCVHYIHNISVPLLLVNSSDDPLVH 352
Cdd:pfam12146 145 DSLSRDPEVV---AAYAADPLV----------HGGISARTLYElldaGERLLRRAAAITVPLLLLHGGADRVVD 205
 
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