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Conserved domains on  [gi|1777141686|gb|QGM12339|]
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protective antigen [Bacillus anthracis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Binary_toxB_2 super family cl38748
Clostridial binary toxin B/anthrax toxin PA domain 2; This domain forms the middle beta ...
 289-506 4.57e-131

Clostridial binary toxin B/anthrax toxin PA domain 2; This domain forms the middle beta sandwish domain in anthrax toxin.


The actual alignment was detected with superfamily member pfam17475:

Pssm-ID: 435917  Cd Length: 198  Bit Score: 387.31  E-value: 4.57e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777141686 289 PIVHVDMENIILSKNEDQSTQNTDSETRTISKNTSTSRTHTSEVHgnaevhasffdiggsvsagfSNSNSSTVAIDHSLS 368
Cdd:pfam17475   1 PIVHVDMENIILSKNEDQSTQNTDSQTRTISKNTSTSRTHTSEPG--------------------SNSNSSTVAIDHSLS 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777141686 369 LAGERTWAETMGLNTADTARLNANIRYVNTGTAPIYNVLPTTSLVLGKNQTLATIKAKENQLSQILAPNNYYPSKNLAPI 448
Cdd:pfam17475  61 LAGERTWAETMGLNTADTARLNANIRYVNTGTAPIYNVLPTTSLVLGKNQTLATIKAKENQLSQILAPNNYYPSKNLAPI 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1777141686 449 ALNAQDDFSSTPITMNYNQFLELEKTKQLRLDTDQVYGNIATYNFENGRVRVDTGSNW 506
Cdd:pfam17475 141 ALNAQDDFSSTPITMNYNQFLELEKTKQLRLDTDQVYGNIATYNFENGRVRVDTGSNW 198
Binary_toxB_3 pfam17476
Clostridial binary toxin B/anthrax toxin PA domain 3; This entry represents the beta-grasp ...
 509-610 1.14e-49

Clostridial binary toxin B/anthrax toxin PA domain 3; This entry represents the beta-grasp domain in anthrax protective antigen.


:

Pssm-ID: 375198  Cd Length: 102  Bit Score: 169.24  E-value: 1.14e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777141686 509 VLPQIQETTARIIFNGKDLNLVERRIAAVNPSDPLETTKPDMTLKEALKIAFGFNEPNGNLQYQGKDITEFDFNFDQQTS 588
Cdd:pfam17476   1 YIPQIEETTARIIIDIKDGPMVERRIAAVDPDDPNELTKPDLTLGEALEKAFGFYEPNGNLYYQGKDIDEFHFIFDRRTE 80

                          90       100
                  ....*....|....*....|..
gi 1777141686 589 QNIKNQLAELNATNIYTVLDKI 610
Cdd:pfam17476  81 QNIKKQLEGNKNKNIYDVTIRP 102
Binary_toxB pfam03495
Clostridial binary toxin B/anthrax toxin PA Ca-binding domain; This domain is a calcium ...
 205-286 1.63e-42

Clostridial binary toxin B/anthrax toxin PA Ca-binding domain; This domain is a calcium binding domain in the anthrax toxin protective antigen.


:

Pssm-ID: 367526 [Multi-domain]  Cd Length: 78  Bit Score: 148.78  E-value: 1.63e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777141686 205 PDRDNDGIPDSLEVEGYTVDvknkRTFLSPWISNIHEKKGLTKYKSSPEKWSTASDPYSDFEKVTGRIDKNVSPEARHPL 284
Cdd:pfam03495   1 PDRDGDGIPDDLEINGYTVD----KTLLVPWIDKLHAKKGFTKYVSDPNEWSTAGDPYSDFEKVSGMIDRGIHKEARHPL 76


                  ..
gi 1777141686 285 VA 286
Cdd:pfam03495  77 VA 78
PA14 pfam07691
PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other ...
 44-179 2.46e-31

PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins, including anthrax protective antigen (PA). The domain also occurs in a Dictyostelium prespore-cell-inducing factor Psi and in fibrocystin, the mammalian protein whose mutation leads to polycystic kidney and hepatic disease. The crystal structure of PA shows that this domain (named PA14 after its location in the PA20 pro-peptide) has a beta-barrel structure. The PA14 domain sequence suggests a binding function, rather than a catalytic role. The PA14 domain distribution is compatible with carbohydrate binding.


:

Pssm-ID: 400161 [Multi-domain]  Cd Length: 141  Bit Score: 119.39  E-value: 2.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777141686  44 SSQGLLGYYFSDLNFQAPMVVTSsTTGDLSIPSSELENIPSENQYFQSAIWSGFIKVKKSDEYTFATSADNHVTMWVDDQ 123
Cdd:pfam07691   1 GKPGLTGIYFNDADFSGDPVLID-TDPDNTFYWDTDVPGFGEAPGDFSARWTGYLLPPESGTYTFGVASDDGARLWIDGE 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1777141686 124 EVIN---------KASNSNKIRLEKGRLYQIKIQYQRENPTEKGldfKLYWTDSQNKKEVISSDN 179
Cdd:pfam07691  80 LVIDnwgqhppdaSPEESNTLYLVAGKLYPIRIEYFHAGTGGSV---QLSWTSPDGGGEEIDEDG 141
 
Name Accession Description Interval E-value
Binary_toxB_2 pfam17475
Clostridial binary toxin B/anthrax toxin PA domain 2; This domain forms the middle beta ...
 289-506 4.57e-131

Clostridial binary toxin B/anthrax toxin PA domain 2; This domain forms the middle beta sandwish domain in anthrax toxin.


Pssm-ID: 435917  Cd Length: 198  Bit Score: 387.31  E-value: 4.57e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777141686 289 PIVHVDMENIILSKNEDQSTQNTDSETRTISKNTSTSRTHTSEVHgnaevhasffdiggsvsagfSNSNSSTVAIDHSLS 368
Cdd:pfam17475   1 PIVHVDMENIILSKNEDQSTQNTDSQTRTISKNTSTSRTHTSEPG--------------------SNSNSSTVAIDHSLS 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777141686 369 LAGERTWAETMGLNTADTARLNANIRYVNTGTAPIYNVLPTTSLVLGKNQTLATIKAKENQLSQILAPNNYYPSKNLAPI 448
Cdd:pfam17475  61 LAGERTWAETMGLNTADTARLNANIRYVNTGTAPIYNVLPTTSLVLGKNQTLATIKAKENQLSQILAPNNYYPSKNLAPI 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1777141686 449 ALNAQDDFSSTPITMNYNQFLELEKTKQLRLDTDQVYGNIATYNFENGRVRVDTGSNW 506
Cdd:pfam17475 141 ALNAQDDFSSTPITMNYNQFLELEKTKQLRLDTDQVYGNIATYNFENGRVRVDTGSNW 198
Binary_toxB_3 pfam17476
Clostridial binary toxin B/anthrax toxin PA domain 3; This entry represents the beta-grasp ...
 509-610 1.14e-49

Clostridial binary toxin B/anthrax toxin PA domain 3; This entry represents the beta-grasp domain in anthrax protective antigen.


Pssm-ID: 375198  Cd Length: 102  Bit Score: 169.24  E-value: 1.14e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777141686 509 VLPQIQETTARIIFNGKDLNLVERRIAAVNPSDPLETTKPDMTLKEALKIAFGFNEPNGNLQYQGKDITEFDFNFDQQTS 588
Cdd:pfam17476   1 YIPQIEETTARIIIDIKDGPMVERRIAAVDPDDPNELTKPDLTLGEALEKAFGFYEPNGNLYYQGKDIDEFHFIFDRRTE 80

                          90       100
                  ....*....|....*....|..
gi 1777141686 589 QNIKNQLAELNATNIYTVLDKI 610
Cdd:pfam17476  81 QNIKKQLEGNKNKNIYDVTIRP 102
Binary_toxB pfam03495
Clostridial binary toxin B/anthrax toxin PA Ca-binding domain; This domain is a calcium ...
 205-286 1.63e-42

Clostridial binary toxin B/anthrax toxin PA Ca-binding domain; This domain is a calcium binding domain in the anthrax toxin protective antigen.


Pssm-ID: 367526 [Multi-domain]  Cd Length: 78  Bit Score: 148.78  E-value: 1.63e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777141686 205 PDRDNDGIPDSLEVEGYTVDvknkRTFLSPWISNIHEKKGLTKYKSSPEKWSTASDPYSDFEKVTGRIDKNVSPEARHPL 284
Cdd:pfam03495   1 PDRDGDGIPDDLEINGYTVD----KTLLVPWIDKLHAKKGFTKYVSDPNEWSTAGDPYSDFEKVSGMIDRGIHKEARHPL 76


                  ..
gi 1777141686 285 VA 286
Cdd:pfam03495  77 VA 78
PA14 pfam07691
PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other ...
 44-179 2.46e-31

PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins, including anthrax protective antigen (PA). The domain also occurs in a Dictyostelium prespore-cell-inducing factor Psi and in fibrocystin, the mammalian protein whose mutation leads to polycystic kidney and hepatic disease. The crystal structure of PA shows that this domain (named PA14 after its location in the PA20 pro-peptide) has a beta-barrel structure. The PA14 domain sequence suggests a binding function, rather than a catalytic role. The PA14 domain distribution is compatible with carbohydrate binding.


Pssm-ID: 400161 [Multi-domain]  Cd Length: 141  Bit Score: 119.39  E-value: 2.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777141686  44 SSQGLLGYYFSDLNFQAPMVVTSsTTGDLSIPSSELENIPSENQYFQSAIWSGFIKVKKSDEYTFATSADNHVTMWVDDQ 123
Cdd:pfam07691   1 GKPGLTGIYFNDADFSGDPVLID-TDPDNTFYWDTDVPGFGEAPGDFSARWTGYLLPPESGTYTFGVASDDGARLWIDGE 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1777141686 124 EVIN---------KASNSNKIRLEKGRLYQIKIQYQRENPTEKGldfKLYWTDSQNKKEVISSDN 179
Cdd:pfam07691  80 LVIDnwgqhppdaSPEESNTLYLVAGKLYPIRIEYFHAGTGGSV---QLSWTSPDGGGEEIDEDG 141
PA14 smart00758
domain in bacterial beta-glucosidases other glycosidases, glycosyltransferases, proteases, ...
 46-178 2.62e-26

domain in bacterial beta-glucosidases other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins;


Pssm-ID: 214807 [Multi-domain]  Cd Length: 136  Bit Score: 104.79  E-value: 2.62e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777141686   46 QGLLGYYFSDLNFQAPMVVtSSTTGDLSIPSSELENIPSENQYFQSAIWSGFIKVKKSDEYTFATSADNHVTMWVDDQEV 125
Cdd:smart00758   1 PGLTGYYFENEKFSGLPEI-IDTDPLNTFYWDSDKFGEGEKADNFSVRWTGYLKPPEDGEYTFSITSDDGARLWIDGKLV 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777141686  126 I-------NKASNSNKIRLEKGRLYQIKIQYQRENPtekGLDFKLYWTDSQNKKEVISSD 178
Cdd:smart00758  80 IdnwgkheARPSTSSTLYLLAGGTYPIRIEYFEAGT---GGLLKLGWTTPDAAKEAIDDE 136
PFM_jacalin-like cd20231
pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin ...
 303-391 5.63e-05

pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin domain, and similar aerolysin-type beta-barrel pore-forming proteins; Jacalin-like lectins are sugar-binding protein domains. Proteins having these lectin domains may bind mono- or oligosaccharides with high specificity. 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: 380801 [Multi-domain]  Cd Length: 150  Bit Score: 43.88  E-value: 5.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777141686 303 NEDQSTQNTDSETRTISKNTSTSRTHTSEVHGNAEVHASFFDIGGSVSAGFSNSNSSTVAIDHSLSLAGERTWAETMGLN 382
Cdd:cd20231    16 STDYTWTFSGSRTKTTSRTWSQSSTSGFELSVSVSVSAGIPEIGEAVTTSAGWSLSATSSESETETTTDELGWSVSGTLP 95


                  ....*....
gi 1777141686 383 TADTARLNA 391
Cdd:cd20231    96 PGEGVKCRA 104
 
Name Accession Description Interval E-value
Binary_toxB_2 pfam17475
Clostridial binary toxin B/anthrax toxin PA domain 2; This domain forms the middle beta ...
 289-506 4.57e-131

Clostridial binary toxin B/anthrax toxin PA domain 2; This domain forms the middle beta sandwish domain in anthrax toxin.


Pssm-ID: 435917  Cd Length: 198  Bit Score: 387.31  E-value: 4.57e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777141686 289 PIVHVDMENIILSKNEDQSTQNTDSETRTISKNTSTSRTHTSEVHgnaevhasffdiggsvsagfSNSNSSTVAIDHSLS 368
Cdd:pfam17475   1 PIVHVDMENIILSKNEDQSTQNTDSQTRTISKNTSTSRTHTSEPG--------------------SNSNSSTVAIDHSLS 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777141686 369 LAGERTWAETMGLNTADTARLNANIRYVNTGTAPIYNVLPTTSLVLGKNQTLATIKAKENQLSQILAPNNYYPSKNLAPI 448
Cdd:pfam17475  61 LAGERTWAETMGLNTADTARLNANIRYVNTGTAPIYNVLPTTSLVLGKNQTLATIKAKENQLSQILAPNNYYPSKNLAPI 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1777141686 449 ALNAQDDFSSTPITMNYNQFLELEKTKQLRLDTDQVYGNIATYNFENGRVRVDTGSNW 506
Cdd:pfam17475 141 ALNAQDDFSSTPITMNYNQFLELEKTKQLRLDTDQVYGNIATYNFENGRVRVDTGSNW 198
Binary_toxB_3 pfam17476
Clostridial binary toxin B/anthrax toxin PA domain 3; This entry represents the beta-grasp ...
 509-610 1.14e-49

Clostridial binary toxin B/anthrax toxin PA domain 3; This entry represents the beta-grasp domain in anthrax protective antigen.


Pssm-ID: 375198  Cd Length: 102  Bit Score: 169.24  E-value: 1.14e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777141686 509 VLPQIQETTARIIFNGKDLNLVERRIAAVNPSDPLETTKPDMTLKEALKIAFGFNEPNGNLQYQGKDITEFDFNFDQQTS 588
Cdd:pfam17476   1 YIPQIEETTARIIIDIKDGPMVERRIAAVDPDDPNELTKPDLTLGEALEKAFGFYEPNGNLYYQGKDIDEFHFIFDRRTE 80

                          90       100
                  ....*....|....*....|..
gi 1777141686 589 QNIKNQLAELNATNIYTVLDKI 610
Cdd:pfam17476  81 QNIKKQLEGNKNKNIYDVTIRP 102
Binary_toxB pfam03495
Clostridial binary toxin B/anthrax toxin PA Ca-binding domain; This domain is a calcium ...
 205-286 1.63e-42

Clostridial binary toxin B/anthrax toxin PA Ca-binding domain; This domain is a calcium binding domain in the anthrax toxin protective antigen.


Pssm-ID: 367526 [Multi-domain]  Cd Length: 78  Bit Score: 148.78  E-value: 1.63e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777141686 205 PDRDNDGIPDSLEVEGYTVDvknkRTFLSPWISNIHEKKGLTKYKSSPEKWSTASDPYSDFEKVTGRIDKNVSPEARHPL 284
Cdd:pfam03495   1 PDRDGDGIPDDLEINGYTVD----KTLLVPWIDKLHAKKGFTKYVSDPNEWSTAGDPYSDFEKVSGMIDRGIHKEARHPL 76


                  ..
gi 1777141686 285 VA 286
Cdd:pfam03495  77 VA 78
PA14 pfam07691
PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other ...
 44-179 2.46e-31

PA14 domain; This domain forms an insert in bacterial beta-glucosidases and is found in other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins, including anthrax protective antigen (PA). The domain also occurs in a Dictyostelium prespore-cell-inducing factor Psi and in fibrocystin, the mammalian protein whose mutation leads to polycystic kidney and hepatic disease. The crystal structure of PA shows that this domain (named PA14 after its location in the PA20 pro-peptide) has a beta-barrel structure. The PA14 domain sequence suggests a binding function, rather than a catalytic role. The PA14 domain distribution is compatible with carbohydrate binding.


Pssm-ID: 400161 [Multi-domain]  Cd Length: 141  Bit Score: 119.39  E-value: 2.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777141686  44 SSQGLLGYYFSDLNFQAPMVVTSsTTGDLSIPSSELENIPSENQYFQSAIWSGFIKVKKSDEYTFATSADNHVTMWVDDQ 123
Cdd:pfam07691   1 GKPGLTGIYFNDADFSGDPVLID-TDPDNTFYWDTDVPGFGEAPGDFSARWTGYLLPPESGTYTFGVASDDGARLWIDGE 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1777141686 124 EVIN---------KASNSNKIRLEKGRLYQIKIQYQRENPTEKGldfKLYWTDSQNKKEVISSDN 179
Cdd:pfam07691  80 LVIDnwgqhppdaSPEESNTLYLVAGKLYPIRIEYFHAGTGGSV---QLSWTSPDGGGEEIDEDG 141
PA14 smart00758
domain in bacterial beta-glucosidases other glycosidases, glycosyltransferases, proteases, ...
 46-178 2.62e-26

domain in bacterial beta-glucosidases other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins;


Pssm-ID: 214807 [Multi-domain]  Cd Length: 136  Bit Score: 104.79  E-value: 2.62e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777141686   46 QGLLGYYFSDLNFQAPMVVtSSTTGDLSIPSSELENIPSENQYFQSAIWSGFIKVKKSDEYTFATSADNHVTMWVDDQEV 125
Cdd:smart00758   1 PGLTGYYFENEKFSGLPEI-IDTDPLNTFYWDSDKFGEGEKADNFSVRWTGYLKPPEDGEYTFSITSDDGARLWIDGKLV 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777141686  126 I-------NKASNSNKIRLEKGRLYQIKIQYQRENPtekGLDFKLYWTDSQNKKEVISSD 178
Cdd:smart00758  80 IdnwgkheARPSTSSTLYLLAGGTYPIRIEYFEAGT---GGLLKLGWTTPDAAKEAIDDE 136
PFM_jacalin-like cd20231
pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin ...
 303-391 5.63e-05

pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin domain, and similar aerolysin-type beta-barrel pore-forming proteins; Jacalin-like lectins are sugar-binding protein domains. Proteins having these lectin domains may bind mono- or oligosaccharides with high specificity. 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: 380801 [Multi-domain]  Cd Length: 150  Bit Score: 43.88  E-value: 5.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777141686 303 NEDQSTQNTDSETRTISKNTSTSRTHTSEVHGNAEVHASFFDIGGSVSAGFSNSNSSTVAIDHSLSLAGERTWAETMGLN 382
Cdd:cd20231    16 STDYTWTFSGSRTKTTSRTWSQSSTSGFELSVSVSVSAGIPEIGEAVTTSAGWSLSATSSESETETTTDELGWSVSGTLP 95


                  ....*....
gi 1777141686 383 TADTARLNA 391
Cdd:cd20231    96 PGEGVKCRA 104
 
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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