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Conserved domains on  [gi|2326314|emb|CAA04232|]
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infection responsive serine protease like protein [Anopheles gambiae]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
341-583 9.74e-70

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  Cd Length: 232  Bit Score: 224.85  E-value: 9.74e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314  341 AEYGEFPWMVALfQLPEQRYCCNGALIDPKAILTTAHCVTNCGgrAANIMVRFGEWNMSSTHEmaiPREDIGVKSVHQHP 420
Cdd:cd00190   7 AKIGSFPWQVSL-QYTGGRHFCGGSLISPRWVLTAAHCVYSSA--PSNYTVRLGSHDLSSNEG---GGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314  421 RYSPSALLNNIAVLELAHPVQYQATIQPVCLPSANQPLRAMENMIATGWGRvMEENAPPTQILKRLDLQRMEPSICREAL 500
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGR-TSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314  501 RrvrrpYPFILDSSFVCSTTNHGDQeRPCDGDAGAPVVVELPGttnRYYLHGLVSWGYGCHQKQIPyTVLTKVVHFREWI 580
Cdd:cd00190 160 S-----YGGTITDNMLCAGGLEGGK-DACQGDSGGPLVCNDNG---RGVLVGIVSWGSGCARPNYP-GVYTRVSSYLDWI 229

                ...
gi 2326314  581 DRI 583
Cdd:cd00190 230 QKT 232
motB super family cl32828
flagellar motor protein MotB; Reviewed
186-305 5.35e-04

flagellar motor protein MotB; Reviewed


The actual alignment was detected with superfamily member PRK12799:

Pssm-ID: 183756 [Multi-domain]  Cd Length: 421  Bit Score: 42.78  E-value: 5.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314   186 TTPVSATTANSLGTSLDAQSIEGTGASEPTKLPIPLR--PITPDQQ---TVESSGVNNTTDSIEKS-AKPTTNTSDAQLE 259
Cdd:PRK12799 298 TVPVAAVTPSSAVTQSSAITPSSAAIPSPAVIPSSVTtqSATTTQAsavALSSAGVLPSDVTLPGTvALPAAEPVNMQPQ 377
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 2326314   260 LTSSSESNDLVTSIIDTAlvddnslQETDTTTIPVIPPNAADPPPT 305
Cdd:PRK12799 378 PMSTTETQQSSTGNITST-------ANGPTTSLPAAPASNIPVSPT 416
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
341-583 9.74e-70

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  Cd Length: 232  Bit Score: 224.85  E-value: 9.74e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314  341 AEYGEFPWMVALfQLPEQRYCCNGALIDPKAILTTAHCVTNCGgrAANIMVRFGEWNMSSTHEmaiPREDIGVKSVHQHP 420
Cdd:cd00190   7 AKIGSFPWQVSL-QYTGGRHFCGGSLISPRWVLTAAHCVYSSA--PSNYTVRLGSHDLSSNEG---GGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314  421 RYSPSALLNNIAVLELAHPVQYQATIQPVCLPSANQPLRAMENMIATGWGRvMEENAPPTQILKRLDLQRMEPSICREAL 500
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGR-TSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314  501 RrvrrpYPFILDSSFVCSTTNHGDQeRPCDGDAGAPVVVELPGttnRYYLHGLVSWGYGCHQKQIPyTVLTKVVHFREWI 580
Cdd:cd00190 160 S-----YGGTITDNMLCAGGLEGGK-DACQGDSGGPLVCNDNG---RGVLVGIVSWGSGCARPNYP-GVYTRVSSYLDWI 229

                ...
gi 2326314  581 DRI 583
Cdd:cd00190 230 QKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
341-580 3.85e-67

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: 217.93  E-value: 3.85e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314     341 AEYGEFPWMVALfQLPEQRYCCNGALIDPKAILTTAHCVTNCggRAANIMVRFGEWNMSSTHEMaiprEDIGVKSVHQHP 420
Cdd:smart00020   8 ANIGSFPWQVSL-QYGGGRHFCGGSLISPRWVLTAAHCVRGS--DPSNIRVRLGSHDLSSGEEG----QVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314     421 RYSPSALLNNIAVLELAHPVQYQATIQPVCLPSANQPLRAMENMIATGWGRVMEENAPPTQILKRLDLQRMEPSICREAl 500
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314     501 rrvrRPYPFILDSSFVCSTTNHGDQErPCDGDAGAPVVVELpgttNRYYLHGLVSWGYGCHQKQIPyTVLTKVVHFREWI 580
Cdd:smart00020 160 ----YSGGGAITDNMLCAGGLEGGKD-ACQGDSGGPLVCND----GRWVLVGIVSWGSGCARPGKP-GVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
339-580 2.43e-40

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 146.05  E-value: 2.43e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314    339 FRAEYGEFPWMVALfQLPEQRYCCNGALIDPKAILTTAHCVTNcggrAANIMVRFGEWNMSSTHEMAiprEDIGVKSVHQ 418
Cdd:pfam00089   5 DEAQPGSFPWQVSL-QLSSGKHFCGGSLISENWVLTAAHCVSG----ASDVKVVLGAHNIVLREGGE---QKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314    419 HPRYSPSALLNNIAVLELAHPVQYQATIQPVCLPSANQPLRAMENMIATGWGRVMEENAPptQILKRLDLQRMEPSICre 498
Cdd:pfam00089  77 HPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPS--DTLQEVTVPVVSRETC-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314    499 alrrvRRPYPFILDSSFVCSTTNHGDqerPCDGDAGAPVVVELPgttnryYLHGLVSWGYGCHQKQIPyTVLTKVVHFRE 578
Cdd:pfam00089 153 -----RSAYGGTVTDTMICAGAGGKD---ACQGDSGGPLVCSDG------ELIGIVSWGYGCASGNYP-GVYTPVSSYLD 217

                  ..
gi 2326314    579 WI 580
Cdd:pfam00089 218 WI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
341-587 4.02e-13

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 71.45  E-value: 4.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314  341 AEYGEFPWMVALF---QLPEQRYCCNGALIDPKAILTTAHCVTncGGRAANIMVRFGEWNMSSTHEMaiprEDIGVKSVH 417
Cdd:COG5640  39 ANAGEYPSLVALVdriSDYVSGTFCGGSKLGGRYVLTAAHCAD--ASSPISSDVNRVVVDLNDSSQA----ERGHVRTIY 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314  418 QHPRYSPSALLNNIAVLELAHPvqyqATIQPVCLPSANQP------LRAMENMIATGWG-RVM---EENAPPTQILKRLD 487
Cdd:COG5640 113 VHEFYSPGNLGNDIAVLELARA----ASLPRVKITSFDASdtflnsVTTVSPMTNGTFGvTTPsdvPRSSPKGTILHEVA 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314  488 LQRMEPSICRealrrvRRPYPFILDSSFVCSTTNHGDQER--PCDGDAGAPVVVElpGTTNRYYLhGLVSWGYGCHQKQI 565
Cdd:COG5640 189 VLFVPLSTCA------QYKGCANASDGATGLTGFCAGRPPkdACQGDSGGPIFHK--GEEGRVQR-GVVSWGDGGCGGTL 259
                       250       260
                ....*....|....*....|..
gi 2326314  566 PYTVLTKVVHFREWIDRIVLGF 587
Cdd:COG5640 260 IPGVYTNVSNYQDWIAAMTNGL 281
motB PRK12799
flagellar motor protein MotB; Reviewed
186-305 5.35e-04

flagellar motor protein MotB; Reviewed


Pssm-ID: 183756 [Multi-domain]  Cd Length: 421  Bit Score: 42.78  E-value: 5.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314   186 TTPVSATTANSLGTSLDAQSIEGTGASEPTKLPIPLR--PITPDQQ---TVESSGVNNTTDSIEKS-AKPTTNTSDAQLE 259
Cdd:PRK12799 298 TVPVAAVTPSSAVTQSSAITPSSAAIPSPAVIPSSVTtqSATTTQAsavALSSAGVLPSDVTLPGTvALPAAEPVNMQPQ 377
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 2326314   260 LTSSSESNDLVTSIIDTAlvddnslQETDTTTIPVIPPNAADPPPT 305
Cdd:PRK12799 378 PMSTTETQQSSTGNITST-------ANGPTTSLPAAPASNIPVSPT 416
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
341-583 9.74e-70

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  Cd Length: 232  Bit Score: 224.85  E-value: 9.74e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314  341 AEYGEFPWMVALfQLPEQRYCCNGALIDPKAILTTAHCVTNCGgrAANIMVRFGEWNMSSTHEmaiPREDIGVKSVHQHP 420
Cdd:cd00190   7 AKIGSFPWQVSL-QYTGGRHFCGGSLISPRWVLTAAHCVYSSA--PSNYTVRLGSHDLSSNEG---GGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314  421 RYSPSALLNNIAVLELAHPVQYQATIQPVCLPSANQPLRAMENMIATGWGRvMEENAPPTQILKRLDLQRMEPSICREAL 500
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGR-TSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314  501 RrvrrpYPFILDSSFVCSTTNHGDQeRPCDGDAGAPVVVELPGttnRYYLHGLVSWGYGCHQKQIPyTVLTKVVHFREWI 580
Cdd:cd00190 160 S-----YGGTITDNMLCAGGLEGGK-DACQGDSGGPLVCNDNG---RGVLVGIVSWGSGCARPNYP-GVYTRVSSYLDWI 229

                ...
gi 2326314  581 DRI 583
Cdd:cd00190 230 QKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
341-580 3.85e-67

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: 217.93  E-value: 3.85e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314     341 AEYGEFPWMVALfQLPEQRYCCNGALIDPKAILTTAHCVTNCggRAANIMVRFGEWNMSSTHEMaiprEDIGVKSVHQHP 420
Cdd:smart00020   8 ANIGSFPWQVSL-QYGGGRHFCGGSLISPRWVLTAAHCVRGS--DPSNIRVRLGSHDLSSGEEG----QVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314     421 RYSPSALLNNIAVLELAHPVQYQATIQPVCLPSANQPLRAMENMIATGWGRVMEENAPPTQILKRLDLQRMEPSICREAl 500
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314     501 rrvrRPYPFILDSSFVCSTTNHGDQErPCDGDAGAPVVVELpgttNRYYLHGLVSWGYGCHQKQIPyTVLTKVVHFREWI 580
Cdd:smart00020 160 ----YSGGGAITDNMLCAGGLEGGKD-ACQGDSGGPLVCND----GRWVLVGIVSWGSGCARPGKP-GVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
339-580 2.43e-40

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 146.05  E-value: 2.43e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314    339 FRAEYGEFPWMVALfQLPEQRYCCNGALIDPKAILTTAHCVTNcggrAANIMVRFGEWNMSSTHEMAiprEDIGVKSVHQ 418
Cdd:pfam00089   5 DEAQPGSFPWQVSL-QLSSGKHFCGGSLISENWVLTAAHCVSG----ASDVKVVLGAHNIVLREGGE---QKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314    419 HPRYSPSALLNNIAVLELAHPVQYQATIQPVCLPSANQPLRAMENMIATGWGRVMEENAPptQILKRLDLQRMEPSICre 498
Cdd:pfam00089  77 HPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPS--DTLQEVTVPVVSRETC-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314    499 alrrvRRPYPFILDSSFVCSTTNHGDqerPCDGDAGAPVVVELPgttnryYLHGLVSWGYGCHQKQIPyTVLTKVVHFRE 578
Cdd:pfam00089 153 -----RSAYGGTVTDTMICAGAGGKD---ACQGDSGGPLVCSDG------ELIGIVSWGYGCASGNYP-GVYTPVSSYLD 217

                  ..
gi 2326314    579 WI 580
Cdd:pfam00089 218 WI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
341-587 4.02e-13

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 71.45  E-value: 4.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314  341 AEYGEFPWMVALF---QLPEQRYCCNGALIDPKAILTTAHCVTncGGRAANIMVRFGEWNMSSTHEMaiprEDIGVKSVH 417
Cdd:COG5640  39 ANAGEYPSLVALVdriSDYVSGTFCGGSKLGGRYVLTAAHCAD--ASSPISSDVNRVVVDLNDSSQA----ERGHVRTIY 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314  418 QHPRYSPSALLNNIAVLELAHPvqyqATIQPVCLPSANQP------LRAMENMIATGWG-RVM---EENAPPTQILKRLD 487
Cdd:COG5640 113 VHEFYSPGNLGNDIAVLELARA----ASLPRVKITSFDASdtflnsVTTVSPMTNGTFGvTTPsdvPRSSPKGTILHEVA 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314  488 LQRMEPSICRealrrvRRPYPFILDSSFVCSTTNHGDQER--PCDGDAGAPVVVElpGTTNRYYLhGLVSWGYGCHQKQI 565
Cdd:COG5640 189 VLFVPLSTCA------QYKGCANASDGATGLTGFCAGRPPkdACQGDSGGPIFHK--GEEGRVQR-GVVSWGDGGCGGTL 259
                       250       260
                ....*....|....*....|..
gi 2326314  566 PYTVLTKVVHFREWIDRIVLGF 587
Cdd:COG5640 260 IPGVYTNVSNYQDWIAAMTNGL 281
motB PRK12799
flagellar motor protein MotB; Reviewed
186-305 5.35e-04

flagellar motor protein MotB; Reviewed


Pssm-ID: 183756 [Multi-domain]  Cd Length: 421  Bit Score: 42.78  E-value: 5.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2326314   186 TTPVSATTANSLGTSLDAQSIEGTGASEPTKLPIPLR--PITPDQQ---TVESSGVNNTTDSIEKS-AKPTTNTSDAQLE 259
Cdd:PRK12799 298 TVPVAAVTPSSAVTQSSAITPSSAAIPSPAVIPSSVTtqSATTTQAsavALSSAGVLPSDVTLPGTvALPAAEPVNMQPQ 377
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 2326314   260 LTSSSESNDLVTSIIDTAlvddnslQETDTTTIPVIPPNAADPPPT 305
Cdd:PRK12799 378 PMSTTETQQSSTGNITST-------ANGPTTSLPAAPASNIPVSPT 416
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
307-381 3.70e-03

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


Pssm-ID: 226119  Cd Length: 251  Bit Score: 39.29  E-value: 3.70e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2326314  307 ALTAQFSPESFsyqdcGQLNLNGVVQRTINEDFRAEYGE---FPW-MVALFQLPEQRYCCNGALIDPKAILTTAHCVTN 381
Cdd:COG3591  12 ALTILTSAAGV-----GATAVEEPQQTASAEDDRTQVTDttqFPYsAVVQFEAATGRLCTAATLIGPNTVLTAGHCIYS 85
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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