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Conserved domains on  [gi|392885356|ref|NP_491364|]
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Peptidase S1 domain-containing protein [Caenorhabditis elegans]

Protein Classification

DUF316 superfamily-containing protein( domain architecture ID 710881)

DUF316 superfamily-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUF316 super family cl27238
Nematode trypsin-6-like family; This is a family of trypsin-6-like proteins found in nematodes ...
16-313 7.36e-21

Nematode trypsin-6-like family; This is a family of trypsin-6-like proteins found in nematodes that are part of the chymotrypsin family S1, ie a serine peptidase. The C. elegans sequence UniProt:O01566 is trypsin-6: all the active site residues are present (His90, Asp168, Ser267).


The actual alignment was detected with superfamily member pfam03761:

Pssm-ID: 367641  Cd Length: 281  Bit Score: 90.95  E-value: 7.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356   16 SVSSAQKLSKEENSKRKITCGqglKLKSGYGRKVLNGLRTKIEDAPWNVAIEIE--TKDVGLCTGTLISTRHVITarhcF 93
Cdd:pfam03761  12 GFVSFRKLTEKENQQRLSSCG---NKTLPLPSQNINGIYLEKSEYPWLVKAAFQngNQKNYKPPATFISTRHILT----S 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356   94 AHLMDYGYVSIGKNQLIHGCENDNDEDLVLHGNLTNSFRIYTgTGCGYRKYCKGMNstsvgIKKIILPKVCDDKQLDFDD 173
Cdd:pfam03761  85 SRLFLNGKSLNWKNTGDNDTCSGGLGHLEVPPEVLDKFDIMD-LSKKKGKNSFRDN-----ITRAYVLNGCANTKSKFDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356  174 FA---IVELSESLKMSrkDRFICVNhEDSNLFNENNRMQLFGfgidpsagnqsagpLRSETVKAEKCFTTTGKAFCTKSI 250
Cdd:pfam03761 159 SAkpmLVELEGPLEPN--ISYPCLA-DESTSLEKGDAVDVYG--------------IDSSGELKHRKLNIVNCYSNDLSI 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392885356  251 SKNQLACTGDSGGGVVQLINDRVTVVGViyeGVTCEASTTDEQDYVANVAYYSDDICRYAGIC 313
Cdd:pfam03761 222 GTDQYLCKGDDGGPLIKNVSGKNTVIGF---GATGNMECNANDFKFFNIKNLSKEICELTGIC 281
 
Name Accession Description Interval E-value
DUF316 pfam03761
Nematode trypsin-6-like family; This is a family of trypsin-6-like proteins found in nematodes ...
16-313 7.36e-21

Nematode trypsin-6-like family; This is a family of trypsin-6-like proteins found in nematodes that are part of the chymotrypsin family S1, ie a serine peptidase. The C. elegans sequence UniProt:O01566 is trypsin-6: all the active site residues are present (His90, Asp168, Ser267).


Pssm-ID: 367641  Cd Length: 281  Bit Score: 90.95  E-value: 7.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356   16 SVSSAQKLSKEENSKRKITCGqglKLKSGYGRKVLNGLRTKIEDAPWNVAIEIE--TKDVGLCTGTLISTRHVITarhcF 93
Cdd:pfam03761  12 GFVSFRKLTEKENQQRLSSCG---NKTLPLPSQNINGIYLEKSEYPWLVKAAFQngNQKNYKPPATFISTRHILT----S 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356   94 AHLMDYGYVSIGKNQLIHGCENDNDEDLVLHGNLTNSFRIYTgTGCGYRKYCKGMNstsvgIKKIILPKVCDDKQLDFDD 173
Cdd:pfam03761  85 SRLFLNGKSLNWKNTGDNDTCSGGLGHLEVPPEVLDKFDIMD-LSKKKGKNSFRDN-----ITRAYVLNGCANTKSKFDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356  174 FA---IVELSESLKMSrkDRFICVNhEDSNLFNENNRMQLFGfgidpsagnqsagpLRSETVKAEKCFTTTGKAFCTKSI 250
Cdd:pfam03761 159 SAkpmLVELEGPLEPN--ISYPCLA-DESTSLEKGDAVDVYG--------------IDSSGELKHRKLNIVNCYSNDLSI 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392885356  251 SKNQLACTGDSGGGVVQLINDRVTVVGViyeGVTCEASTTDEQDYVANVAYYSDDICRYAGIC 313
Cdd:pfam03761 222 GTDQYLCKGDDGGPLIKNVSGKNTVIGF---GATGNMECNANDFKFFNIKNLSKEICELTGIC 281
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
48-285 2.17e-17

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 80.03  E-value: 2.17e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356    48 KVLNGLRTKIEDAPWNVAIEIETKDVgLCTGTLISTRHVITARHCFahlmdygyvsigknqlihgcendndedlvlHGNL 127
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRH-FCGGSLISPRWVLTAAHCV------------------------------RGSD 49
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356   128 TNSFRIYTGTgcgYRKYcKGMNSTSVGIKKIILPKVCDDKQLDFDdFAIVELSESLKMSRKDRFICVnHEDSNLFNENNR 207
Cdd:smart00020  50 PSNIRVRLGS---HDLS-SGEEGQVIKVSKVIIHPNYNPSTYDND-IALLKLKEPVTLSDNVRPICL-PSSNYNVPAGTT 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356   208 MQLFGFGIDPSAGNQSAGPLRSETVKA---EKC-------FTTTGKAFCTKSISKNQLACTGDSGGGVVQLiNDRVTVVG 277
Cdd:smart00020 124 CTVSGWGRTSEGAGSLPDTLQEVNVPIvsnATCrraysggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVG 202

                   ....*...
gi 392885356   278 VIYEGVTC 285
Cdd:smart00020 203 IVSWGSGC 210
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
49-285 1.38e-16

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 77.70  E-value: 1.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356  49 VLNGLRTKIEDAPWNVAIEIeTKDVGLCTGTLISTRHVITARHCFahlmdygyvsigknqlihgcendndedlvlHGNLT 128
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY-TGGRHFCGGSLISPRWVLTAAHCV------------------------------YSSAP 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356 129 NSFRIYTGTGCGYRKYCKGMNstsVGIKKIILPKVCDDKQLDFDdFAIVELSESLKMSRKDRFICVNHEDSNLFNeNNRM 208
Cdd:cd00190   50 SNYTVRLGSHDLSSNEGGGQV---IKVKKVIVHPNYNPSTYDND-IALLKLKRPVTLSDNVRPICLPSSGYNLPA-GTTC 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356 209 QLFGFGiDPSAGNQSAGPLRSETVKA---EKC-------FTTTGKAFCTKSISKNQLACTGDSGGGVVQLINDRVTVVGV 278
Cdd:cd00190  125 TVSGWG-RTSEGGPLPDVLQEVNVPIvsnAECkraysygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGI 203

                 ....*..
gi 392885356 279 IYEGVTC 285
Cdd:cd00190  204 VSWGSGC 210
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
48-306 3.99e-16

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 77.00  E-value: 3.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356  48 KVLNGLRTKIEDAPWNVAIEIETKDVG-LCTGTLISTRHVITARHCFahlmdygyvsigknqlihgcENDNDEDL-VLHG 125
Cdd:COG5640   30 AIVGGTPATVGEYPWMVALQSSNGPSGqFCGGTLIAPRWVLTAAHCV--------------------DGDGPSDLrVVIG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356 126 NLTNSfriyTGTGcgyrkyckgmnsTSVGIKKIILPKVCDDKQLDfDDFAIVELSESLKMSRkdrFICVNhEDSNLFNEN 205
Cdd:COG5640   90 STDLS----TSGG------------TVVKVARIVVHPDYDPATPG-NDIALLKLATPVPGVA---PAPLA-TSADAAAPG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356 206 NRMQLFGFG-IDPSAGNQSAGpLRSETVK---AEKCFTT----TGKAFCTKSISKNQLACTGDSGGGVVQLINDRVTVVG 277
Cdd:COG5640  149 TPATVAGWGrTSEGPGSQSGT-LRKADVPvvsDATCAAYggfdGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVG 227
                        250       260       270
                 ....*....|....*....|....*....|
gi 392885356 278 VI-YEGVTCEASTTdeqDYVANVAYYSDDI 306
Cdd:COG5640  228 VVsWGGGPCAAGYP---GVYTRVSAYRDWI 254
 
Name Accession Description Interval E-value
DUF316 pfam03761
Nematode trypsin-6-like family; This is a family of trypsin-6-like proteins found in nematodes ...
16-313 7.36e-21

Nematode trypsin-6-like family; This is a family of trypsin-6-like proteins found in nematodes that are part of the chymotrypsin family S1, ie a serine peptidase. The C. elegans sequence UniProt:O01566 is trypsin-6: all the active site residues are present (His90, Asp168, Ser267).


Pssm-ID: 367641  Cd Length: 281  Bit Score: 90.95  E-value: 7.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356   16 SVSSAQKLSKEENSKRKITCGqglKLKSGYGRKVLNGLRTKIEDAPWNVAIEIE--TKDVGLCTGTLISTRHVITarhcF 93
Cdd:pfam03761  12 GFVSFRKLTEKENQQRLSSCG---NKTLPLPSQNINGIYLEKSEYPWLVKAAFQngNQKNYKPPATFISTRHILT----S 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356   94 AHLMDYGYVSIGKNQLIHGCENDNDEDLVLHGNLTNSFRIYTgTGCGYRKYCKGMNstsvgIKKIILPKVCDDKQLDFDD 173
Cdd:pfam03761  85 SRLFLNGKSLNWKNTGDNDTCSGGLGHLEVPPEVLDKFDIMD-LSKKKGKNSFRDN-----ITRAYVLNGCANTKSKFDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356  174 FA---IVELSESLKMSrkDRFICVNhEDSNLFNENNRMQLFGfgidpsagnqsagpLRSETVKAEKCFTTTGKAFCTKSI 250
Cdd:pfam03761 159 SAkpmLVELEGPLEPN--ISYPCLA-DESTSLEKGDAVDVYG--------------IDSSGELKHRKLNIVNCYSNDLSI 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392885356  251 SKNQLACTGDSGGGVVQLINDRVTVVGViyeGVTCEASTTDEQDYVANVAYYSDDICRYAGIC 313
Cdd:pfam03761 222 GTDQYLCKGDDGGPLIKNVSGKNTVIGF---GATGNMECNANDFKFFNIKNLSKEICELTGIC 281
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
48-285 2.17e-17

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 80.03  E-value: 2.17e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356    48 KVLNGLRTKIEDAPWNVAIEIETKDVgLCTGTLISTRHVITARHCFahlmdygyvsigknqlihgcendndedlvlHGNL 127
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRH-FCGGSLISPRWVLTAAHCV------------------------------RGSD 49
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356   128 TNSFRIYTGTgcgYRKYcKGMNSTSVGIKKIILPKVCDDKQLDFDdFAIVELSESLKMSRKDRFICVnHEDSNLFNENNR 207
Cdd:smart00020  50 PSNIRVRLGS---HDLS-SGEEGQVIKVSKVIIHPNYNPSTYDND-IALLKLKEPVTLSDNVRPICL-PSSNYNVPAGTT 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356   208 MQLFGFGIDPSAGNQSAGPLRSETVKA---EKC-------FTTTGKAFCTKSISKNQLACTGDSGGGVVQLiNDRVTVVG 277
Cdd:smart00020 124 CTVSGWGRTSEGAGSLPDTLQEVNVPIvsnATCrraysggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVG 202

                   ....*...
gi 392885356   278 VIYEGVTC 285
Cdd:smart00020 203 IVSWGSGC 210
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
49-285 1.38e-16

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 77.70  E-value: 1.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356  49 VLNGLRTKIEDAPWNVAIEIeTKDVGLCTGTLISTRHVITARHCFahlmdygyvsigknqlihgcendndedlvlHGNLT 128
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY-TGGRHFCGGSLISPRWVLTAAHCV------------------------------YSSAP 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356 129 NSFRIYTGTGCGYRKYCKGMNstsVGIKKIILPKVCDDKQLDFDdFAIVELSESLKMSRKDRFICVNHEDSNLFNeNNRM 208
Cdd:cd00190   50 SNYTVRLGSHDLSSNEGGGQV---IKVKKVIVHPNYNPSTYDND-IALLKLKRPVTLSDNVRPICLPSSGYNLPA-GTTC 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356 209 QLFGFGiDPSAGNQSAGPLRSETVKA---EKC-------FTTTGKAFCTKSISKNQLACTGDSGGGVVQLINDRVTVVGV 278
Cdd:cd00190  125 TVSGWG-RTSEGGPLPDVLQEVNVPIvsnAECkraysygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGI 203

                 ....*..
gi 392885356 279 IYEGVTC 285
Cdd:cd00190  204 VSWGSGC 210
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
48-306 3.99e-16

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 77.00  E-value: 3.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356  48 KVLNGLRTKIEDAPWNVAIEIETKDVG-LCTGTLISTRHVITARHCFahlmdygyvsigknqlihgcENDNDEDL-VLHG 125
Cdd:COG5640   30 AIVGGTPATVGEYPWMVALQSSNGPSGqFCGGTLIAPRWVLTAAHCV--------------------DGDGPSDLrVVIG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356 126 NLTNSfriyTGTGcgyrkyckgmnsTSVGIKKIILPKVCDDKQLDfDDFAIVELSESLKMSRkdrFICVNhEDSNLFNEN 205
Cdd:COG5640   90 STDLS----TSGG------------TVVKVARIVVHPDYDPATPG-NDIALLKLATPVPGVA---PAPLA-TSADAAAPG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356 206 NRMQLFGFG-IDPSAGNQSAGpLRSETVK---AEKCFTT----TGKAFCTKSISKNQLACTGDSGGGVVQLINDRVTVVG 277
Cdd:COG5640  149 TPATVAGWGrTSEGPGSQSGT-LRKADVPvvsDATCAAYggfdGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVG 227
                        250       260       270
                 ....*....|....*....|....*....|
gi 392885356 278 VI-YEGVTCEASTTdeqDYVANVAYYSDDI 306
Cdd:COG5640  228 VVsWGGGPCAAGYP---GVYTRVSAYRDWI 254
Trypsin pfam00089
Trypsin;
51-304 1.91e-12

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 65.93  E-value: 1.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356   51 NGLRTKIEDAPWNVAIEIETKDVgLCTGTLISTRHVITARHCFAHLMDYGyVSIGKNQlihgcendndedlvLHGNLTNS 130
Cdd:pfam00089   3 GGDEAQPGSFPWQVSLQLSSGKH-FCGGSLISENWVLTAAHCVSGASDVK-VVLGAHN--------------IVLREGGE 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356  131 FRIYtgtgcgyrkyckgmnstsvgIKKIILPKVCDDKQLDFdDFAIVELSESLKMSRKDRFICVNHEDSNLfNENNRMQL 210
Cdd:pfam00089  67 QKFD--------------------VEKIIVHPNYNPDTLDN-DIALLKLESPVTLGDTVRPICLPDASSDL-PVGTTCTV 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885356  211 FGFGIDpsAGNQSAGPLRSETVKA---EKCFTTTGKA-----FCTKSISKNqlACTGDSGGGvvqLINDRVTVVGVIYEG 282
Cdd:pfam00089 125 SGWGNT--KTLGPSDTLQEVTVPVvsrETCRSAYGGTvtdtmICAGAGGKD--ACQGDSGGP---LVCSDGELIGIVSWG 197
                         250       260
                  ....*....|....*....|..
gi 392885356  283 VTCeaSTTDEQDYVANVAYYSD 304
Cdd:pfam00089 198 YGC--ASGNYPGVYTPVSSYLD 217
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
74-93 5.79e-05

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 43.51  E-value: 5.79e-05
                         10        20
                 ....*....|....*....|
gi 392885356  74 GLCTGTLISTRHVITARHCF 93
Cdd:COG3591   12 GVCTGTLIGPNLVLTAGHCV 31
 
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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