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Conserved domains on  [gi|1827608]
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Chain A, PROAEROLYSIN

Protein Classification

similar to aerolysin( domain architecture ID 10263893)

protein similar to aerolysin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Aerolysin smart00999
Aerolysin toxin; This family represents the pore forming lobe of aerolysin.
 96-454 0e+00

Aerolysin toxin; This family represents the pore forming lobe of aerolysin.


:

Pssm-ID: 198067  Cd Length: 368  Bit Score: 620.75  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608      96 GDEVDVQWRLVHDSANFIKPTSYLAHYLGYAWVGGNHSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTAIKVSNF 175
Cdd:smart00999   1 GDEVDLKWRLVHDPSNFIRPLSYLAHYLGYAWVGGNASQYVGEDMDVTRVGDGWVIQGNYNGSCSGYRCGEKTKITLSNF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608     176 AYNLDPDSFKHGDVTQSDRQLVKTVVGWAVNDSDTPQSgYDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPLVGETEL 255
Cdd:smart00999  81 AYNLNPKSFKLGDVTVSDRELVKTVTAVAYNDGDTPDT-IVVTLRYDETTSWSKTDTYSFSEKVTTKNKFEWPLIGSTEI 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608     256 SIEIAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIELYKADISYPYEFKADVSYDLTLSGFLRWGGNAWYTHPDN 335
Cdd:smart00999 160 SAEFDANQGWSESNGGSTTTSLSAQYRATMPARSKRPIKIELYKQKIDYPYESKADISYDVTFEGFLRWGGNAWHTHPTN 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608     336 RPNWNHTFVIGPYKDKASSIRYQWDKRYIPGEVKWWDWNWTIQQNGLSTMQNNLARVLRPVRAGITGDFSAESQFAGNIE 415
Cdd:smart00999 240 RPNWNHTFGMGNASNLAEDIRYQWDHRYIPGEGKWWDWNWAIQENGLSGMQWALGNILRPFHAPISGKFTAESQFAGNID 319

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1827608     416 IGAPVPLAADSKVRRARSVDGAGQG----------LRLEIPLDAQELSG 454
Cdd:smart00999 320 AGAPVPLAADSKVRRARSADTKGGGstniqvavgeVRVETPFDAQSLSG 368
APT super family cl04073
Aerolysin/Pertussis toxin (APT) domain; This family represents the N-terminal domain of ...
 1-82 1.00e-35

Aerolysin/Pertussis toxin (APT) domain; This family represents the N-terminal domain of aerolysin and pertussis toxin and has a type-C lectin like fold.


The actual alignment was detected with superfamily member pfam03440:

Pssm-ID: 367501  Cd Length: 87  Bit Score: 127.39  E-value: 1.00e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608      1 AEPVYPDQLRLFSLG--QGVCGDKYRPVNREEAQS---VKSNIVGMMGQWQISGLANgWVIMGPGYNGEIKPGTASNTWC 75
Cdd:pfam03440   1 PGIVIPPQLRLTQLGgaYGRCGNKTRALTVAELRGnaeLQSYLRNMTGGWSISGLYD-GTYLGPGYGGEIKDGTPGNTFC 79


                  ....*..
gi 1827608     76 YPTNPVT 82
Cdd:pfam03440  80 YPTTFCI 86
 
Name Accession Description Interval E-value
Aerolysin smart00999
Aerolysin toxin; This family represents the pore forming lobe of aerolysin.
 96-454 0e+00

Aerolysin toxin; This family represents the pore forming lobe of aerolysin.


Pssm-ID: 198067  Cd Length: 368  Bit Score: 620.75  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608      96 GDEVDVQWRLVHDSANFIKPTSYLAHYLGYAWVGGNHSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTAIKVSNF 175
Cdd:smart00999   1 GDEVDLKWRLVHDPSNFIRPLSYLAHYLGYAWVGGNASQYVGEDMDVTRVGDGWVIQGNYNGSCSGYRCGEKTKITLSNF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608     176 AYNLDPDSFKHGDVTQSDRQLVKTVVGWAVNDSDTPQSgYDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPLVGETEL 255
Cdd:smart00999  81 AYNLNPKSFKLGDVTVSDRELVKTVTAVAYNDGDTPDT-IVVTLRYDETTSWSKTDTYSFSEKVTTKNKFEWPLIGSTEI 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608     256 SIEIAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIELYKADISYPYEFKADVSYDLTLSGFLRWGGNAWYTHPDN 335
Cdd:smart00999 160 SAEFDANQGWSESNGGSTTTSLSAQYRATMPARSKRPIKIELYKQKIDYPYESKADISYDVTFEGFLRWGGNAWHTHPTN 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608     336 RPNWNHTFVIGPYKDKASSIRYQWDKRYIPGEVKWWDWNWTIQQNGLSTMQNNLARVLRPVRAGITGDFSAESQFAGNIE 415
Cdd:smart00999 240 RPNWNHTFGMGNASNLAEDIRYQWDHRYIPGEGKWWDWNWAIQENGLSGMQWALGNILRPFHAPISGKFTAESQFAGNID 319

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1827608     416 IGAPVPLAADSKVRRARSVDGAGQG----------LRLEIPLDAQELSG 454
Cdd:smart00999 320 AGAPVPLAADSKVRRARSADTKGGGstniqvavgeVRVETPFDAQSLSG 368
Aerolysin pfam01117
Aerolysin toxin; This family represents the pore forming lobe of aerolysin.
 96-454 0e+00

Aerolysin toxin; This family represents the pore forming lobe of aerolysin.


Pssm-ID: 366474  Cd Length: 359  Bit Score: 562.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608     96 GDEVDVQWRLVHDSANFIKPTSYLAHYLGYAWVGGNHSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTAIKVSNF 175
Cdd:pfam01117   1 QDLLDVKWRLVDDQVEFYQPLAYLAHYLGYGWCGGTRSQYVGEDFVVTRNGDSWLVEANNNGPCNGYRCDHRLKMHFSDF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608    176 AYNLDPDSFKHGDVTQSDRQLVKTVVGWAVNDSDTPQSgYDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPLVGETEL 255
Cdd:pfam01117  81 KFGVKPSSLKYGDPVISDREPYKYIVGYARNDSDTPQQ-RVLTLSYDEVTNWSKTDTYKYSEKVTIKNKYKFPLIGETEL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608    256 SIEIAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIELYKADISYPYEFKADVSYDLTLSGFLRWGGNAWYTHPDN 335
Cdd:pfam01117 160 SLELGANQSWATTNGNSSTKTISDVARVLVPANTKIPVRLKLEKARVDYPYEFNAQVSYDVTLDGFLRWGGNALGDHPNN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608    336 RPNWNHTFVIGPYKDKASSIRYQWDKRYIPGEVKWWDWNWTIQQNGLSTMQNNLARVL-RPVRAGITGDFSAESQFAGNI 414
Cdd:pfam01117 240 RPTKNYTFGDGRGSTPASTILYQYLKRHIPRGTRPWDWNWMVDRHGKDAYKWAVSLALeRPYEATLTGDFEAVSGYVANI 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1827608    415 EIGAPVPLAADSKVRRARSVDGAGQGLRLEIPLDAQELSG 454
Cdd:pfam01117 320 TYWAPVSLYGDQQVERAFRVDGSVGSARIFPKPDYEELSQ 359
PFM_aerolysin cd20218
pore-forming module of aerolysin and similar aerolysin-type beta-barrel pore-forming proteins; ...
 179-314 3.21e-68

pore-forming module of aerolysin and similar aerolysin-type beta-barrel pore-forming proteins; Aerolysin is a cytosolic bacterial toxin that forms pores in the host membrane, leading to destruction of the membrane permeability barrier and host cell death. Another member of this family is alpha-toxin from Clostridium septicum, the main virulence factor of this bacterium, known for causing non-traumatic gas gangrene. Many proteins belonging to this group have an N-terminal APT domain; an APT domain is the N-terminal domain of aerolysin and pertussis toxin and has a type-C lectin-like fold. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380788  Cd Length: 144  Bit Score: 214.49  E-value: 3.21e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608  179 LDPDSFKHGDVTQSDRQLVKTVVGWAVNDSDTPQSgYDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPLVGETELSIE 258
Cdd:cd20218   1 LDPESFSHGDITESDKELVKTITAYAINDSDIPQQ-YRVTFTYDTSTNWSKTDTYGFSQSVSVKNTFKWPLVGETELSIT 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 1827608  259 IAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIELYKADISYPyEFKADVSY 314
Cdd:cd20218  80 IGANQSWGETNGGSSSESVSRQARVTVPAHSKLPVKIELYRSDISYP-DFSAESQY 134
APT pfam03440
Aerolysin/Pertussis toxin (APT) domain; This family represents the N-terminal domain of ...
 1-82 1.00e-35

Aerolysin/Pertussis toxin (APT) domain; This family represents the N-terminal domain of aerolysin and pertussis toxin and has a type-C lectin like fold.


Pssm-ID: 367501  Cd Length: 87  Bit Score: 127.39  E-value: 1.00e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608      1 AEPVYPDQLRLFSLG--QGVCGDKYRPVNREEAQS---VKSNIVGMMGQWQISGLANgWVIMGPGYNGEIKPGTASNTWC 75
Cdd:pfam03440   1 PGIVIPPQLRLTQLGgaYGRCGNKTRALTVAELRGnaeLQSYLRNMTGGWSISGLYD-GTYLGPGYGGEIKDGTPGNTFC 79


                  ....*..
gi 1827608     76 YPTNPVT 82
Cdd:pfam03440  80 YPTTFCI 86
 
Name Accession Description Interval E-value
Aerolysin smart00999
Aerolysin toxin; This family represents the pore forming lobe of aerolysin.
 96-454 0e+00

Aerolysin toxin; This family represents the pore forming lobe of aerolysin.


Pssm-ID: 198067  Cd Length: 368  Bit Score: 620.75  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608      96 GDEVDVQWRLVHDSANFIKPTSYLAHYLGYAWVGGNHSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTAIKVSNF 175
Cdd:smart00999   1 GDEVDLKWRLVHDPSNFIRPLSYLAHYLGYAWVGGNASQYVGEDMDVTRVGDGWVIQGNYNGSCSGYRCGEKTKITLSNF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608     176 AYNLDPDSFKHGDVTQSDRQLVKTVVGWAVNDSDTPQSgYDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPLVGETEL 255
Cdd:smart00999  81 AYNLNPKSFKLGDVTVSDRELVKTVTAVAYNDGDTPDT-IVVTLRYDETTSWSKTDTYSFSEKVTTKNKFEWPLIGSTEI 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608     256 SIEIAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIELYKADISYPYEFKADVSYDLTLSGFLRWGGNAWYTHPDN 335
Cdd:smart00999 160 SAEFDANQGWSESNGGSTTTSLSAQYRATMPARSKRPIKIELYKQKIDYPYESKADISYDVTFEGFLRWGGNAWHTHPTN 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608     336 RPNWNHTFVIGPYKDKASSIRYQWDKRYIPGEVKWWDWNWTIQQNGLSTMQNNLARVLRPVRAGITGDFSAESQFAGNIE 415
Cdd:smart00999 240 RPNWNHTFGMGNASNLAEDIRYQWDHRYIPGEGKWWDWNWAIQENGLSGMQWALGNILRPFHAPISGKFTAESQFAGNID 319

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1827608     416 IGAPVPLAADSKVRRARSVDGAGQG----------LRLEIPLDAQELSG 454
Cdd:smart00999 320 AGAPVPLAADSKVRRARSADTKGGGstniqvavgeVRVETPFDAQSLSG 368
Aerolysin pfam01117
Aerolysin toxin; This family represents the pore forming lobe of aerolysin.
 96-454 0e+00

Aerolysin toxin; This family represents the pore forming lobe of aerolysin.


Pssm-ID: 366474  Cd Length: 359  Bit Score: 562.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608     96 GDEVDVQWRLVHDSANFIKPTSYLAHYLGYAWVGGNHSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTAIKVSNF 175
Cdd:pfam01117   1 QDLLDVKWRLVDDQVEFYQPLAYLAHYLGYGWCGGTRSQYVGEDFVVTRNGDSWLVEANNNGPCNGYRCDHRLKMHFSDF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608    176 AYNLDPDSFKHGDVTQSDRQLVKTVVGWAVNDSDTPQSgYDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPLVGETEL 255
Cdd:pfam01117  81 KFGVKPSSLKYGDPVISDREPYKYIVGYARNDSDTPQQ-RVLTLSYDEVTNWSKTDTYKYSEKVTIKNKYKFPLIGETEL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608    256 SIEIAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIELYKADISYPYEFKADVSYDLTLSGFLRWGGNAWYTHPDN 335
Cdd:pfam01117 160 SLELGANQSWATTNGNSSTKTISDVARVLVPANTKIPVRLKLEKARVDYPYEFNAQVSYDVTLDGFLRWGGNALGDHPNN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608    336 RPNWNHTFVIGPYKDKASSIRYQWDKRYIPGEVKWWDWNWTIQQNGLSTMQNNLARVL-RPVRAGITGDFSAESQFAGNI 414
Cdd:pfam01117 240 RPTKNYTFGDGRGSTPASTILYQYLKRHIPRGTRPWDWNWMVDRHGKDAYKWAVSLALeRPYEATLTGDFEAVSGYVANI 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1827608    415 EIGAPVPLAADSKVRRARSVDGAGQGLRLEIPLDAQELSG 454
Cdd:pfam01117 320 TYWAPVSLYGDQQVERAFRVDGSVGSARIFPKPDYEELSQ 359
PFM_aerolysin cd20218
pore-forming module of aerolysin and similar aerolysin-type beta-barrel pore-forming proteins; ...
 179-314 3.21e-68

pore-forming module of aerolysin and similar aerolysin-type beta-barrel pore-forming proteins; Aerolysin is a cytosolic bacterial toxin that forms pores in the host membrane, leading to destruction of the membrane permeability barrier and host cell death. Another member of this family is alpha-toxin from Clostridium septicum, the main virulence factor of this bacterium, known for causing non-traumatic gas gangrene. Many proteins belonging to this group have an N-terminal APT domain; an APT domain is the N-terminal domain of aerolysin and pertussis toxin and has a type-C lectin-like fold. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380788  Cd Length: 144  Bit Score: 214.49  E-value: 3.21e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608  179 LDPDSFKHGDVTQSDRQLVKTVVGWAVNDSDTPQSgYDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPLVGETELSIE 258
Cdd:cd20218   1 LDPESFSHGDITESDKELVKTITAYAINDSDIPQQ-YRVTFTYDTSTNWSKTDTYGFSQSVSVKNTFKWPLVGETELSIT 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 1827608  259 IAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIELYKADISYPyEFKADVSY 314
Cdd:cd20218  80 IGANQSWGETNGGSSSESVSRQARVTVPAHSKLPVKIELYRSDISYP-DFSAESQY 134
APT pfam03440
Aerolysin/Pertussis toxin (APT) domain; This family represents the N-terminal domain of ...
 1-82 1.00e-35

Aerolysin/Pertussis toxin (APT) domain; This family represents the N-terminal domain of aerolysin and pertussis toxin and has a type-C lectin like fold.


Pssm-ID: 367501  Cd Length: 87  Bit Score: 127.39  E-value: 1.00e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608      1 AEPVYPDQLRLFSLG--QGVCGDKYRPVNREEAQS---VKSNIVGMMGQWQISGLANgWVIMGPGYNGEIKPGTASNTWC 75
Cdd:pfam03440   1 PGIVIPPQLRLTQLGgaYGRCGNKTRALTVAELRGnaeLQSYLRNMTGGWSISGLYD-GTYLGPGYGGEIKDGTPGNTFC 79


                  ....*..
gi 1827608     76 YPTNPVT 82
Cdd:pfam03440  80 YPTTFCI 86
PFM_alpha-toxin-like cd20224
pore-forming module of Clostridium septicum alpha-toxin and similar aerolysin-type beta-barrel ...
 204-299 3.21e-20

pore-forming module of Clostridium septicum alpha-toxin and similar aerolysin-type beta-barrel pore-forming proteins; Clostridium septicum alpha-toxin is the main virulence factor of this bacterium, known for causing non-traumatic gas gangrene. Members of this family belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380794  Cd Length: 121  Bit Score: 85.89  E-value: 3.21e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608  204 AVNDSDTPQSGyDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPL----VGETELSIEIAANQSWASQNGGSTTTSLSQ 279
Cdd:cd20224   9 AENHGNTEDTG-TATFNYTESTSWSKTDNFKFSEGIKVTVKFTVGIpligGAESETEFSFNAEQGWSDSTGNTETIQQSA 87

                        90       100
                ....*....|....*....|
gi 1827608  280 SVRPTVPARSKIPVKIELYK 299
Cdd:cd20224  88 QYTATVPPRSKRTITLTAFK 107
ETX_MTX2 pfam03318
Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; This family appears to be ...
 205-333 3.75e-10

Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; This family appears to be distantly related to pfam01117.


Pssm-ID: 427241 [Multi-domain]  Cd Length: 222  Bit Score: 59.73  E-value: 3.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608    205 VNDSDTPQSGYDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPLVGET--ELSIEIAANQSWASQNGGSTTTSL---SQ 279
Cdd:pfam03318  37 TNNTDSTQTLQTQSFSKKVTTTTSTTTTHGFKIGAKASGKFGIPFVAEGgiTLSVSGEYNFSSTTTNTTSVTTTYwvpSQ 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1827608    280 SVrpTVPARSKIPVKIELYKADISYPYEFKADVS----YDLTLSGFLRwGGNAWYTHP 333
Cdd:pfam03318 117 KV--TVPPHTTVRVTLVLYKTTYSVPVDLYTTLSgtfsIEGTRSGYVE-PASYPLTAS 171
PFM_aerolysin-like cd20240
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 200-326 1.18e-09

pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized subgroup; Generally, pore-forming proteins (PFPs) are secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores detrimental to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel. Many of this family are bacterial toxins. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380810 [Multi-domain]  Cd Length: 145  Bit Score: 56.50  E-value: 1.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608  200 VVGWAV-NDSDTPQS-GYDVTLRYDTATNWSKTNtyGLSEKVTTKNKFKWPLVGETELSIEIAANQSWASQNGGSTTTSL 277
Cdd:cd20240   8 IVTWTYtNNTSIEQTmTTNFSETATETSSFSETE--GVSTTVSTSLKVGIPFIAGGEITTTTTTSQSWTYGKSETKTDTI 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 1827608  278 SQSVRPTVPARSKIPVKIEL--YKADISYPYEFKADVS-YDLTLSGflRWGG 326
Cdd:cd20240  86 SYTFPIVVPPNTTVTATAVVtkYNMDVTYVATLRGINTgKRIKIKG--KWSG 135
PFM_aerolysin-like cd20239
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 206-315 1.36e-09

pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized subgroup; Generally, pore-forming proteins (PFPs) are secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores detrimental to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel. Many of this family are bacterial toxins. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380809 [Multi-domain]  Cd Length: 145  Bit Score: 56.31  E-value: 1.36e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608  206 NDSDTPQSgYDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPLVGETELSIEIAANQS--WasqnGGSTTTS--LSQSV 281
Cdd:cd20239  11 NDSDSPAS-QTLTYSYSKSEEGTWNNTAGIELGVKVTFKAGVPFVASGELEVSVSASYShtW----GGSTTVTktVSSST 85

                        90       100       110
                ....*....|....*....|....*....|....
gi 1827608  282 RPTVPARSKIPVKIELYKADISYPYEFKADVSYD 315
Cdd:cd20239  86 TVVVPPRKKGVASVLIRKAEIDVPFTYTERITYT 119
PFM_LSL-like cd20215
pore-forming module of Laetiporus sulphureus LSL lectin and similar aerolysin-type beta-barrel ...
 206-306 7.55e-08

pore-forming module of Laetiporus sulphureus LSL lectin and similar aerolysin-type beta-barrel pore-forming proteins; LSL is a lectin, produced by the parasitic mushroom Laetiporus sulphureus, which exhibits hemolytic and hemagglutinating activities. Members of this family belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380785 [Multi-domain]  Cd Length: 164  Bit Score: 51.94  E-value: 7.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608  206 NDSDTPQSgydVTLRYD-TATNWSK-TNTYGLSEKVTTKNKFKWPLVGETELSIEIAANQ--SWASQNGGSTTTSLSQSV 281
Cdd:cd20215  32 NDTDVEQT---MSFTLTeTETHTSTfEYTAGFTITVGTSFKAGIPGVAEGKIKVDTTVSNewKWGESTTFTKTYTATFPV 108

                        90       100
                ....*....|....*....|....*
gi 1827608  282 rpTVPARSKIPVKIELYKADISYPY 306
Cdd:cd20215 109 --KAPPGSTVRAVATVTKSNLEVPF 131
PFM_epsilon-toxin-like cd20223
pore-forming module of Clostridium perfringens epsilon-toxin and similar aerolysin-type ...
 206-318 8.40e-08

pore-forming module of Clostridium perfringens epsilon-toxin and similar aerolysin-type beta-barrel pore-forming proteins; Clostridium perfringens epsilon-toxin is responsible for fatal enterotoxemia in ungulates. It forms a heptamer in the lipid rafts of Madin-Darby Canine Kidney (MDCK) cells, leading to cell death; its oligomer formation is induced by activation of neutral sphingomyelinase. This group also includes an insecticidal crystal protein Cry14-4 (encoded on plasmid pBMBt1 of Bacillus thuringiensis serovar darmstadiensis). Also included is pXO2-60 (a protein from the pathogenic pXO2 plasmid of Bacillus anthracis) which harbors a unique ubiquitin-like fold domain at the C-terminus of the aerolysin-like domain, and is involved in virulence. They belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380793 [Multi-domain]  Cd Length: 144  Bit Score: 51.08  E-value: 8.40e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608  206 NDSDTPQSG------YDVTlryDTATNwSKTNTYGLSEKVTTKNKFKWPLVGETELSIEIAANQSWASQNggSTTTSL-- 277
Cdd:cd20223  24 NDTDEEQTLktpsfsKTVT---DTVTT-TTTNGFKLGVSTSAKFKIPFPGGGSTELSAEYNFSTTNTNTT--SETKTYta 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 1827608  278 -SQSVrpTVPARSKIPVKIELYKADISYPY-EFKADVSYDLTL 318
Cdd:cd20223  98 pSQTI--KVPPGKTYKVTVYLKKVKFSGTVgTFTGVYGTDFTV 138
PFM_parasporin-2-like cd20222
pore-forming module of parasporin-2, hydralysin and similar aerolysin-type beta-barrel ...
 204-295 1.39e-07

pore-forming module of parasporin-2, hydralysin and similar aerolysin-type beta-barrel pore-forming proteins; Bacillus thuringiensis strain A1547 parasporin-2 (PS2, also named Cry46Aa1) is an anti-cancer protein which causes specific cell damage via PS2 oligomerization in the cell membrane. Glycosylphosphatidylinositol (GPI)-anchored proteins may be involved in the cytocidal action of PS2 as co-receptors for PS2's cytocidal action. This family also includes hydralysin (Hln-1) and Hln-2 produced by the green hydra Chlorohydra viridissima. Hydralysin is a paralysis-inducing protein not found in the stinging cells (nematocytes), with a cell type-selective cytolytic activity; it binds erythrocyte membranes and forms discrete pores. They belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380792  Cd Length: 147  Bit Score: 50.79  E-value: 1.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608  204 AVNDSDTPQSgyDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPLVGETELSIEIaaNQSWASQNGGSTTT--SLSQSV 281
Cdd:cd20222  22 AVNNGDEEEI--TVTYSYKVGGKWTWKTSWSSSSTTGATFSSGIPLEGVFEVGTEF--SVSGTTGESGSTSTekTLTSSV 97

                        90
                ....*....|....
gi 1827608  282 RPTVPARSKIPVKI 295
Cdd:cd20222  98 TVKVPPNSKVKITM 111
PFM_Cry51Aa-like cd20226
pore-forming module of Bacillus thuringiensis insecticidal Cry51A toxin, Bacillus ...
 205-323 2.30e-07

pore-forming module of Bacillus thuringiensis insecticidal Cry51A toxin, Bacillus thuringiensis cytotoxic parasporin-5 and similar aerolysin-type beta-barrel pore-forming proteins; Bacillus thuringiensis parasporin-5 has strong cytocidal activity against several types of cancer cells and may or may not have insecticidal activity. Cry51A toxin is toxic to coleopteran (beetle) larvae. Other members of this family include Bacillus thuringiensis Cry15Aa which is toxic to lepidopteran (butterflies and moth) larvae. They belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380796 [Multi-domain]  Cd Length: 172  Bit Score: 50.74  E-value: 2.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608  205 VNDSDTPQSGydvTLRYD---TATNWSKTN---TYGLSEKVTTKNKFKWPLVGETELSIEIAANQSWASQNGGSTTT--- 275
Cdd:cd20226  30 TNNTSVPQSQ---TVSFSektTETTSTTTTegyKIGTSIKSTTKFKVKFGFVVGGEQSIEVSVSFEYNYSTTTTYTTtte 106

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 1827608  276 ---SLSQSVrpTVPARSKIPVKIELYKADISYPYEFKADVSYDLTLSGFLR 323
Cdd:cd20226 107 klwEDTQPV--TVPPRTKVTATLIIYGGPFNVPVTLNCTISLNFKGSGTLT 155
PFM_HFR-2-like cd20216
pore-forming module of wheat HFR-2 toxin, FEM32, and similar aerolysin-type beta-barrel ...
 204-294 9.68e-06

pore-forming module of wheat HFR-2 toxin, FEM32, and similar aerolysin-type beta-barrel pore-forming proteins; HFR-2 is a wheat cytolytic toxin which may normally function in defense against certain insects or pathogens. The Hfr-2 gene is upregulated in virulent Hessian fly larval feedingdouble dagger. The HFR-2 protein may insert in plant cell membranes at the feeding sites and by forming pores provide water, ions and other small nutritive molecules to the developing larvae. This group also contains FEM32, a flower-specific lectin-like protein from the dioecious plant Rumex acetosa, which alters flower development and induces male sterility in transgenic tobacco. It has been suggested that the FEM32 gene activates some form of programmed cell death (PCD), a process that could be mediated by the action of its lectin domains for binding to specific glycoproteins on the cell membrane and facilitated by the formation of pore structures in the membranes and the subsequent leakage of the cytosolic content through its pore-forming aerolysin domain. Most proteins belonging to this group have N-terminal agglutatin (also known as amaranthin) lectin domains; most have two agglutatin domains, in combination with one aerolysin domain. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380786 [Multi-domain]  Cd Length: 152  Bit Score: 45.27  E-value: 9.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608  204 AVNDSDTPQSGyDVTLRY-DT-ATNWSKTNTYGLSEKVTTKNKFkwPLVGETElsIEIAANQSWASQNGGSTTTSLSQSV 281
Cdd:cd20216  14 ATNNTSEPQTV-TLKLSYtDTkTSTWNSSVSLKLGVKTTISAGV--PFIVDGK--IEISAEFSGSYEWGETKTETTEVET 88

                        90
                ....*....|....*
gi 1827608  282 --RPTVPARSKIPVK 294
Cdd:cd20216  89 tyTVTVPPMTKVTVT 103
PFM_aerolysin-like cd20241
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 205-305 1.17e-05

pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized subgroup; Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380811 [Multi-domain]  Cd Length: 139  Bit Score: 44.79  E-value: 1.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608  205 VNDSDTPQSgYDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPLVGETELSIEIAANQSWASQNGGSTTTSLSQSVRPT 284
Cdd:cd20241   9 RNNGNTPAT-LKANMSRSVSETGSFSFTHGFSIGVGTTIKAGIPFIVEGEIETELSTSHDFTWGKSTTVTTTVGSSVTVE 87

                        90       100
                ....*....|....*....|.
gi 1827608  285 VPARSKIPVKIELYKADISYP 305
Cdd:cd20241  88 VPPRSTQTVVGTFKRSKMTVP 108
PFM_aerolysin-like cd20242
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 204-314 4.87e-05

pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized subgroup; Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380812 [Multi-domain]  Cd Length: 144  Bit Score: 43.18  E-value: 4.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827608  204 AVNDSDTPQSgydVTLRYDTATNWSKT--NTYGLSEKVTTKNKFKWPLV--GETELSIEIAANQSWASQNGGSTTTSLSQ 279
Cdd:cd20242   9 VTNDTGQPQT---PSISGSETVTETSTweDEVGLKLGVSTSFSAGVPVVaeGKVEVSAEVHNNYTWNGSNTRSKTWSFST 85

                        90       100       110
                ....*....|....*....|....*....|....*
gi 1827608  280 SVRptVPARSKIPVKIELYKADISYPYEFKADVSY 314
Cdd:cd20242  86 PVN--VPAHSAVRATATVTESTISVPYTLTWKSIF 118
PFM_aerolysin_family cd10140
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; Pore-forming proteins ...
 272-325 8.20e-04

pore-forming module of aerolysin-type beta-barrel pore-forming proteins; Pore-forming proteins (PFPs) are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta pore-forming proteins (beta-PFPs) form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Members of this family includes enterolobin, a cytolytic, inflammatory and insecticidal protein from the Brazilian tree Enterolobium contortisiliquum.


Pssm-ID: 380782  Cd Length: 92  Bit Score: 38.68  E-value: 8.20e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 1827608  272 STTTSLSQSVRPTVPARSKIPVKIELYKADISYPY--EFKADVSYDLTLSGFLRWG 325
Cdd:cd10140  24 SETKTVSVTVTVTVPPGKTVKVTVTVTKAKIDVPYtaTLKATYSTSGTGTTGTVSG 79
 
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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