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Conserved domains on  [gi|47168593]
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Chain A, Complement factor B

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 16-213 3.98e-112

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


:

Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 319.23  E-value: 3.98e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  16 MNIYLVLDGSDSIGASNFTGAKKSLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHK 95
Cdd:cd01470   1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  96 LKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVF 175
Cdd:cd01470  81 DKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYLDVYVF 160

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 47168593 176 GVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFY 213
Cdd:cd01470 161 GVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 16-213 3.98e-112

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 319.23  E-value: 3.98e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  16 MNIYLVLDGSDSIGASNFTGAKKSLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHK 95
Cdd:cd01470   1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  96 LKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVF 175
Cdd:cd01470  81 DKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYLDVYVF 160

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 47168593 176 GVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFY 213
Cdd:cd01470 161 GVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
VWA pfam00092
von Willebrand factor type A domain;
17-214 2.50e-32

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 115.45  E-value: 2.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593    17 NIYLVLDGSDSIGASNFTGAKKSLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSeaDSSNADWVTKQLNEINYEDHKL 96
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLN--DYSSKEELLSAVDNLRYLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593    97 KS-GTNTKKALQAVYSMMSWPDDvppegwnRTRHVIILMTDGlHNMGGDPITVIDEIRDllyigkdrknpreDYLDVYVF 175
Cdd:pfam00092  79 TNtGKALKYALENLFSSAAGARP-------GAPKVVVLLTDG-RSQDGDPEEVARELKS-------------AGVTVFAV 137

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 47168593   176 GVGPLVNQvNINALASKKDnEQHVFKVKDMENLEDVFYQ 214
Cdd:pfam00092 138 GVGNADDE-ELRKIASEPG-EGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 17-210 4.00e-28

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 104.46  E-value: 4.00e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593     17 NIYLVLDGSDSIGASNFTGAKKSLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSeaDSSNADWVTKQLNEINYedhKL 96
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLN--DSRSKDALLEALASLSY---KL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593     97 KSGTNTKKALQAVYSMMSwpddVPPEGWNR-TRHVIILMTDGLHNMGGDPItvIDEIRDLlyigkdrknpREDYLDVYVF 175
Cdd:smart00327  76 GGGTNLGAALQYALENLF----SKSAGSRRgAPKVVILITDGESNDGPKDL--LKAAKEL----------KRSGVKVFVV 139

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 47168593    176 GVGPLVNQVNINALASKKDNEqHVFKVKDMENLED 210
Cdd:smart00327 140 GVGNDVDEEELKKLASAPGGV-YVFLPELLDLLID 173
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 11-212 3.74e-10

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 58.03  E-value: 3.74e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  11 DPSGSMNIYLVLDGSDSIGASN-FTGAKKSLVNLIEkvaSYGVKPRYGLVTYATYPKIWVKVSeadsSNADWVTKQLNEI 89
Cdd:COG1240  88 RPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLD---DYRPRDRVGLVAFGGEAEVLLPLT----RDREALKRALDEL 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  90 nyedhKLKSGTNTKKALQAVYSMMswpDDVPPEGwnrtRHVIILMTDGLHNMG-GDPITVIDEIrdllyigkdrknpRED 168
Cdd:COG1240 161 -----PPGGGTPLGDALALALELL---KRADPAR----RKVIVLLTDGRDNAGrIDPLEAAELA-------------AAA 215

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 47168593 169 YLDVYVFGVG-PLVNQVNINALAskkdnEQ---HVFKVKDMENLEDVF 212
Cdd:COG1240 216 GIRIYTIGVGtEAVDEGLLREIA-----EAtggRYFRADDLSELAAIY 258
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 16-213 3.98e-112

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 319.23  E-value: 3.98e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  16 MNIYLVLDGSDSIGASNFTGAKKSLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHK 95
Cdd:cd01470   1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  96 LKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVF 175
Cdd:cd01470  81 DKTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSDNPREDYLDVYVF 160

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 47168593 176 GVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFY 213
Cdd:cd01470 161 GVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 16-200 3.23e-38

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 130.10  E-value: 3.23e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  16 MNIYLVLDGSDSIGASNFTGAKKSLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSeaDSSNADWVTKQLNEINYEDHk 95
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLN--DYKSKDDLLKAVKNLKYLGG- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  96 lkSGTNTKKALQAVYSMMSWPDdvppEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLlyigkdrknpredYLDVYVF 175
Cdd:cd01450  78 --GGTNTGKALQYALEQLFSES----NARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDE-------------GIKVFVV 138

                       170       180
                ....*....|....*....|....*
gi 47168593 176 GVGPlVNQVNINALASKKdNEQHVF 200
Cdd:cd01450 139 GVGP-ADEEELREIASCP-SERHVF 161
VWA pfam00092
von Willebrand factor type A domain;
17-214 2.50e-32

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 115.45  E-value: 2.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593    17 NIYLVLDGSDSIGASNFTGAKKSLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSeaDSSNADWVTKQLNEINYEDHKL 96
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLN--DYSSKEELLSAVDNLRYLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593    97 KS-GTNTKKALQAVYSMMSWPDDvppegwnRTRHVIILMTDGlHNMGGDPITVIDEIRDllyigkdrknpreDYLDVYVF 175
Cdd:pfam00092  79 TNtGKALKYALENLFSSAAGARP-------GAPKVVVLLTDG-RSQDGDPEEVARELKS-------------AGVTVFAV 137

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 47168593   176 GVGPLVNQvNINALASKKDnEQHVFKVKDMENLEDVFYQ 214
Cdd:pfam00092 138 GVGNADDE-ELRKIASEPG-EGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 17-210 4.00e-28

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 104.46  E-value: 4.00e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593     17 NIYLVLDGSDSIGASNFTGAKKSLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSeaDSSNADWVTKQLNEINYedhKL 96
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLN--DSRSKDALLEALASLSY---KL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593     97 KSGTNTKKALQAVYSMMSwpddVPPEGWNR-TRHVIILMTDGLHNMGGDPItvIDEIRDLlyigkdrknpREDYLDVYVF 175
Cdd:smart00327  76 GGGTNLGAALQYALENLF----SKSAGSRRgAPKVVILITDGESNDGPKDL--LKAAKEL----------KRSGVKVFVV 139

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 47168593    176 GVGPLVNQVNINALASKKDNEqHVFKVKDMENLED 210
Cdd:smart00327 140 GVGNDVDEEELKKLASAPGGV-YVFLPELLDLLID 173
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 17-200 6.78e-23

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 90.70  E-value: 6.78e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  17 NIYLVLDGSDSIGASNFTGAKKSLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSnadwvTKQLNEINYEDHKL 96
Cdd:cd00198   2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDK-----ADLLEAIDALKKGL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  97 KSGTNTKKALQAVYSMMSWPDDvppegwNRTRHVIILMTDGLHNmgGDPITVIDEIRDLlyigkdrknpREDYLDVYVFG 176
Cdd:cd00198  77 GGGTNIGAALRLALELLKSAKR------PNARRVIILLTDGEPN--DGPELLAEAAREL----------RKLGITVYTIG 138

                       170       180
                ....*....|....*....|....
gi 47168593 177 VGPLVNQVNINALASkKDNEQHVF 200
Cdd:cd00198 139 IGDDANEDELKEIAD-KTTGGAVF 161
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 11-212 3.74e-10

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 58.03  E-value: 3.74e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  11 DPSGSMNIYLVLDGSDSIGASN-FTGAKKSLVNLIEkvaSYGVKPRYGLVTYATYPKIWVKVSeadsSNADWVTKQLNEI 89
Cdd:COG1240  88 RPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLD---DYRPRDRVGLVAFGGEAEVLLPLT----RDREALKRALDEL 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  90 nyedhKLKSGTNTKKALQAVYSMMswpDDVPPEGwnrtRHVIILMTDGLHNMG-GDPITVIDEIrdllyigkdrknpRED 168
Cdd:COG1240 161 -----PPGGGTPLGDALALALELL---KRADPAR----RKVIVLLTDGRDNAGrIDPLEAAELA-------------AAA 215

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 47168593 169 YLDVYVFGVG-PLVNQVNINALAskkdnEQ---HVFKVKDMENLEDVF 212
Cdd:COG1240 216 GIRIYTIGVGtEAVDEGLLREIA-----EAtggRYFRADDLSELAAIY 258
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 16-211 2.24e-09

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 54.67  E-value: 2.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  16 MNIYLVLDGSDSIGASNFTGAKKSLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSE-ADSSNADWVTKQLneinyedH 94
Cdd:cd01469   1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEyRTKEEPLSLVKHI-------S 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  95 KLKSGTNTKKALQAVYSmmswpddvppEGWNRTR-------HVIILMTDGLHNMGGDPITVIDEirdllyigkdrknPRE 167
Cdd:cd01469  74 QLLGLTNTATAIQYVVT----------ELFSESNgarkdatKVLVVITDGESHDDPLLKDVIPQ-------------AER 130

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 47168593 168 DYLDVYVFGVGPLVNQVN----INALASKKDnEQHVFKVKDMENLEDV 211
Cdd:cd01469 131 EGIIRYAIGVGGHFQRENsreeLKTIASKPP-EEHFFNVTDFAALKDI 177
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 8-212 9.13e-09

Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 54.34  E-value: 9.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593   8 IVLDPSGSMNiylvldgSDSIGAsnftgAKKSLVNLIEKVasygvKP--RYGLVTYATYPKIWVKVSEADSsnadwVTKQ 85
Cdd:COG2304  96 FVIDVSGSMS-------GDKLEL-----AKEAAKLLVDQL-----RPgdRVSIVTFAGDARVLLPPTPATD-----RAKI 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  86 LNEINyedhKLKSG--TNTKKALQAVYSMmswPDDVPPEGWNRtrhVIILMTDGLHNMGgdpITVIDEIRDLLyigkdrK 163
Cdd:COG2304 154 LAAID----RLQAGggTALGAGLELAYEL---ARKHFIPGRVN---RVILLTDGDANVG---ITDPEELLKLA------E 214

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 47168593 164 NPREDYLDVYVFGVGPLVNQVNINALASKKDNEqhVFKVKDMENLEDVF 212
Cdd:COG2304 215 EAREEGITLTTLGVGSDYNEDLLERLADAGGGN--YYYIDDPEEAEKVF 261
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 16-182 8.35e-08

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 50.46  E-value: 8.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  16 MNIYLVLDGSDSIGASN-FTGAKKSLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNAD---WVTKQLNEINY 91
Cdd:cd01471   1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKDlalNAIRALLSLYY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  92 EdhklKSGTNTKKALQAV----YSMMSWPDDVPpegwnrtrHVIILMTDGLHNMGGDPITVIDEIRDLLYIgkdrknpre 167
Cdd:cd01471  81 P----NGSTNTTSALLVVekhlFDTRGNRENAP--------QLVIIMTDGIPDSKFRTLKEARKLRERGVI--------- 139

                       170
                ....*....|....*
gi 47168593 168 dyldVYVFGVGPLVN 182
Cdd:cd01471 140 ----IAVLGVGQGVN 150
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 17-137 2.38e-07

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 48.76  E-value: 2.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  17 NIYLVLDGSDSIGASNFTGAKKSLVNLIEKVASYGVKPRYGLVTYATYPKIwvkvsEADS---SNADWVTKQLNEINYed 93
Cdd:cd01472   2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRT-----EFYLntyRSKDDVLEAVKNLRY-- 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 47168593  94 hkLKSGTNTKKALQAVYSMMSWPDDVPPEGWNRtrhVIILMTDG 137
Cdd:cd01472  75 --IGGGTNTGKALKYVRENLFTEASGSREGVPK---VLVVITDG 113
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 14-197 3.47e-07

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 48.92  E-value: 3.47e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  14 GSMNIYLVLDGSDSIGASNFTGAKKSLVNLIEKVAS-YGVKP-----RYGLVTYATYPKIwVKVSEADSSNADWVTKQLN 87
Cdd:cd01480   1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKdYYRKDpagswRVGVVQYSDQQEV-EAGFLRDIRNYTSLKEAVD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  88 EINYedhkLKSGTNTKKALQAVYSMMSwpdDVPPEGWNRtrhVIILMTDGlHNMGGDPITVIDEIRDLLYIGkdrknpre 167
Cdd:cd01480  80 NLEY----IGGGTFTDCALKYATEQLL---EGSHQKENK---FLLVITDG-HSDGSPDGGIEKAVNEADHLG-------- 140

                       170       180       190
                ....*....|....*....|....*....|
gi 47168593 168 dyLDVYVFGVGPLVNQVNINALASKKDNEQ 197
Cdd:cd01480 141 --IKIFFVAVGSQNEEPLSRIACDGKSALY 168
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 18-204 2.20e-05

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 43.43  E-value: 2.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  18 IYLVLDGSDSIGASNFTGAKKSLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSeADSSNADwVTKQLNEINYedhklK 97
Cdd:cd01482   3 IVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLN-AYTSKED-VLAAIKNLPY-----K 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593  98 SG-TNTKKALQAVYSMMSWPDDVPPEGwnrTRHVIILMTDGLHNmggdpitviDEIRDllyIGKDRKNpredyLDVYVFG 176
Cdd:cd01482  76 GGnTRTGKALTHVREKNFTPDAGARPG---VPKVVILITDGKSQ---------DDVEL---PARVLRN-----LGVNVFA 135

                       170       180       190
                ....*....|....*....|....*....|
gi 47168593 177 VGplVNQVNINALAS--KKDNEQHVFKVKD 204
Cdd:cd01482 136 VG--VKDADESELKMiaSKPSETHVFNVAD 163
VWA_2 pfam13519
von Willebrand factor type A domain;
8-133 5.65e-05

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 40.74  E-value: 5.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47168593     8 IVLDPSGSMniylvldGSDSIGASNFTGAKKSLVNLIEKVAsyGVkpRYGLVTYATYPKIWVKVseadSSNADWVTKQLN 87
Cdd:pfam13519   3 FVLDTSGSM-------RNGDYGPTRLEAAKDAVLALLKSLP--GD--RVGLVTFGDGPEVLIPL----TKDRAKILRALR 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 47168593    88 EINYEDhklkSGTNTKKALQAVYSMMswpddvpPEGWNRTRHVIIL 133
Cdd:pfam13519  68 RLEPKG----GGTNLAAALQLARAAL-------KHRRKNQPRRIVL 102
 
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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