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Conserved domains on  [gi|723535895|ref|XP_010298082|]
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PREDICTED: anthrax toxin receptor 2-like [Balearica regulorum gibbericeps]

Protein Classification

vWA domain-containing protein( domain architecture ID 10208431)

vWA (von Willebrand factor type A) domain-containing protein may be involved in one of a wide variety of important cellular functions, including basal membrane formation, cell migration, cell differentiation, adhesion, hemostasis, signaling, chromosomal stability, malignant transformation, and immune defenses

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1-144 6.56e-69

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.


The actual alignment was detected with superfamily member cd01474:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 185  Bit Score: 211.21  E-value: 6.56e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723535895   1 MRLSFIVFSTQAHVIMPLTGDREKIKKGLKDLEEVKPAGDTYIHEGLKQANVQIAKQ--GASRFSSIIIALTDGKLDGQI 78
Cdd:cd01474   40 LRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTYIHEGLENANEQIFNRngGGRETVSVIIALTDGQLLLNG 119

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 723535895  79 PLYAEKEAKKSRELGARVYCVGVLDFVQEQLEKIADTKEQVFPVTGGFQALKGIINSVLKQSCTEI 144
Cdd:cd01474  120 HKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYVFPVTSGFQALSGIIESVVKKACIEI 185
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 139-239 4.89e-51

Anthrax receptor extracellular domain; This region is found in the putatively extracellular N-terminal half of the anthrax receptor. It is probably part of the Ig superfamily and most closely related to pfam01833 (personal obs: C Yeats).


:

Pssm-ID: 461684  Cd Length: 102  Bit Score: 162.80  E-value: 4.89e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723535895  139 QSCTEILYLEPSSVCVGEEFQVVLRGSGLTLGGKTDSVTCTYQVNGTTIH-EKPKTVESDFLLCPAPVLYKSGQTLEVLV 217
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYnEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|..
gi 723535895  218 SLNEGQSFMSSSLTITASECSS 239
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTCSD 102
 
Name Accession Description Interval E-value
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 1-144 6.56e-69

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 211.21  E-value: 6.56e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723535895   1 MRLSFIVFSTQAHVIMPLTGDREKIKKGLKDLEEVKPAGDTYIHEGLKQANVQIAKQ--GASRFSSIIIALTDGKLDGQI 78
Cdd:cd01474   40 LRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTYIHEGLENANEQIFNRngGGRETVSVIIALTDGQLLLNG 119

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 723535895  79 PLYAEKEAKKSRELGARVYCVGVLDFVQEQLEKIADTKEQVFPVTGGFQALKGIINSVLKQSCTEI 144
Cdd:cd01474  120 HKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYVFPVTSGFQALSGIIESVVKKACIEI 185
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 139-239 4.89e-51

Anthrax receptor extracellular domain; This region is found in the putatively extracellular N-terminal half of the anthrax receptor. It is probably part of the Ig superfamily and most closely related to pfam01833 (personal obs: C Yeats).


Pssm-ID: 461684  Cd Length: 102  Bit Score: 162.80  E-value: 4.89e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723535895  139 QSCTEILYLEPSSVCVGEEFQVVLRGSGLTLGGKTDSVTCTYQVNGTTIH-EKPKTVESDFLLCPAPVLYKSGQTLEVLV 217
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYnEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|..
gi 723535895  218 SLNEGQSFMSSSLTITASECSS 239
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTCSD 102
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 2-125 6.87e-16

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: 75.36  E-value: 6.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723535895   2 RLSFIVFSTQAHVIMPLTGDREKIKKGLKDLeevKPAGDTYIHEGLKQANVQIAKQGASRfSSIIIALTDGK-LDGQIPl 80
Cdd:COG1240  130 RVGLVAFGGEAEVLLPLTRDREALKRALDEL---PPGGGTPLGDALALALELLKRADPAR-RKVIVLLTDGRdNAGRID- 204

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 723535895  81 yAEKEAKKSRELGARVYCVGVLD--FVQEQLEKIADTkeqvfpvTGG 125
Cdd:COG1240  205 -PLEAAELAAAAGIRIYTIGVGTeaVDEGLLREIAEA-------TGG 243
VWA pfam00092
von Willebrand factor type A domain;
2-120 3.74e-11

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 60.37  E-value: 3.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723535895    2 RLSFIVFSTQAHVIMPLT--GDREKIKKGLKDLEeVKPAGDTYIHEGLKQA--NVQIAKQGA-SRFSSIIIALTDGKLDG 76
Cdd:pfam00092  39 RVGLVQYSSDVRTEFPLNdySSKEELLSAVDNLR-YLGGGTTNTGKALKYAleNLFSSAAGArPGAPKVVVLLTDGRSQD 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 723535895   77 QIPlyaEKEAKKSRELGARVYCVGVLDFVQEQLEKIADTKEQVF 120
Cdd:pfam00092 118 GDP---EEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGH 158
 
Name Accession Description Interval E-value
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 1-144 6.56e-69

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 211.21  E-value: 6.56e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723535895   1 MRLSFIVFSTQAHVIMPLTGDREKIKKGLKDLEEVKPAGDTYIHEGLKQANVQIAKQ--GASRFSSIIIALTDGKLDGQI 78
Cdd:cd01474   40 LRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTYIHEGLENANEQIFNRngGGRETVSVIIALTDGQLLLNG 119

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 723535895  79 PLYAEKEAKKSRELGARVYCVGVLDFVQEQLEKIADTKEQVFPVTGGFQALKGIINSVLKQSCTEI 144
Cdd:cd01474  120 HKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYVFPVTSGFQALSGIIESVVKKACIEI 185
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 139-239 4.89e-51

Anthrax receptor extracellular domain; This region is found in the putatively extracellular N-terminal half of the anthrax receptor. It is probably part of the Ig superfamily and most closely related to pfam01833 (personal obs: C Yeats).


Pssm-ID: 461684  Cd Length: 102  Bit Score: 162.80  E-value: 4.89e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723535895  139 QSCTEILYLEPSSVCVGEEFQVVLRGSGLTLGGKTDSVTCTYQVNGTTIH-EKPKTVESDFLLCPAPVLYKSGQTLEVLV 217
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYnEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|..
gi 723535895  218 SLNEGQSFMSSSLTITASECSS 239
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTCSD 102
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1-117 2.63e-16

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: 74.25  E-value: 2.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723535895   1 MRLSFIVFSTQAHVIMPLT--GDREKIKKGLKDLEEVKPAGdTYIHEGLKQANVQIAKQGASRFSS--IIIALTDGKLDG 76
Cdd:cd01450   39 TRVGLVQYSDDVRVEFSLNdyKSKDDLLKAVKNLKYLGGGG-TNTGKALQYALEQLFSESNARENVpkVIIVLTDGRSDD 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 723535895  77 QIplYAEKEAKKSRELGARVYCVGVLDFVQEQLEKIADTKE 117
Cdd:cd01450  118 GG--DPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 2-125 6.87e-16

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: 75.36  E-value: 6.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723535895   2 RLSFIVFSTQAHVIMPLTGDREKIKKGLKDLeevKPAGDTYIHEGLKQANVQIAKQGASRfSSIIIALTDGK-LDGQIPl 80
Cdd:COG1240  130 RVGLVAFGGEAEVLLPLTRDREALKRALDEL---PPGGGTPLGDALALALELLKRADPAR-RKVIVLLTDGRdNAGRID- 204

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 723535895  81 yAEKEAKKSRELGARVYCVGVLD--FVQEQLEKIADTkeqvfpvTGG 125
Cdd:COG1240  205 -PLEAAELAAAAGIRIYTIGVGTeaVDEGLLREIAEA-------TGG 243
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 2-114 1.21e-13

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: 67.21  E-value: 1.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723535895   2 RLSFIVFSTQAHVIMPLT--GDREKIKKGLKDLEeVKPAGDTYIHEGLKQANVQIAKQGASRFSSIIIALTDGKLDGQIP 79
Cdd:cd00198   40 RVGLVTFGSNARVVLPLTtdTDKADLLEAIDALK-KGLGGGTNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPE 118

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 723535895  80 LYAEkEAKKSRELGARVYCVGV-LDFVQEQLEKIAD 114
Cdd:cd00198  119 LLAE-AARELRKLGITVYTIGIgDDANEDELKEIAD 153
VWA pfam00092
von Willebrand factor type A domain;
2-120 3.74e-11

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 60.37  E-value: 3.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723535895    2 RLSFIVFSTQAHVIMPLT--GDREKIKKGLKDLEeVKPAGDTYIHEGLKQA--NVQIAKQGA-SRFSSIIIALTDGKLDG 76
Cdd:pfam00092  39 RVGLVQYSSDVRTEFPLNdySSKEELLSAVDNLR-YLGGGTTNTGKALKYAleNLFSSAAGArPGAPKVVVLLTDGRSQD 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 723535895   77 QIPlyaEKEAKKSRELGARVYCVGVLDFVQEQLEKIADTKEQVF 120
Cdd:pfam00092 118 GDP---EEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGH 158
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 2-131 7.76e-08

VWA BatA type: 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. Members of this subgroup are bacterial in origin. They are typified by the presence of a MIDAS motif.


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 51.18  E-value: 7.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723535895   2 RLSFIVFSTQAHVIMPLTGDREKIKKGLKDLeEVKPAGD-TYIHEGLKQANVQIAKQGASrfSSIIIALTDGKLD-GQI- 78
Cdd:cd01467   44 RIGLVVFAGAAFTQAPLTLDRESLKELLEDI-KIGLAGQgTAIGDAIGLAIKRLKNSEAK--ERVIVLLTDGENNaGEId 120

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 723535895  79 PLYAEKEAKksrELGARVYCVGV------------LDFVQEQLEKIADTkeqvfpvTGG--FQALKG 131
Cdd:cd01467  121 PATAAELAK---NKGVRIYTIGVgksgsgpkpdgsTILDEDSLVEIADK-------TGGriFRALDG 177
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 2-101 2.63e-07

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: 49.69  E-value: 2.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723535895   2 RLSFIVFSTQAHVIMPLTG----DREKIKKGLKDLEEV-KPAGDTYIHEGLKQANVQIAKQGASRFSSI--IIALTDGKL 74
Cdd:cd01471   41 NLYLVTFSTNAKELIRLSSpnstNKDLALNAIRALLSLyYPNGSTNTTSALLVVEKHLFDTRGNRENAPqlVIIMTDGIP 120

                         90       100
                 ....*....|....*....|....*..
gi 723535895  75 DGqiPLYAEKEAKKSRELGARVYCVGV 101
Cdd:cd01471  121 DS--KFRTLKEARKLRERGVIIAVLGV 145
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 2-114 4.01e-06

VWA subgroup: 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. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known.


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 46.11  E-value: 4.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723535895   2 RLSFIVFSTQAHVIMPLT--GDREKIKKGLkdlEEVKPAGDTYIHEGLKQANVQIAKQGASRFSSIIIALTDGKLDGQIP 79
Cdd:cd01465   37 RLAIVTYDGAAETVLPATpvRDKAAILAAI---DRLTAGGSTAGGAGIQLGYQEAQKHFVPGGVNRILLATDGDFNVGET 113

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 723535895  80 LYAEKE--AKKSRELGARVYCVGVLDFVQEQL-EKIAD 114
Cdd:cd01465  114 DPDELArlVAQKRESGITLSTLGFGDNYNEDLmEAIAD 151
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 2-73 3.77e-05

VWA C3HC4-type: 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. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known.


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 42.76  E-value: 3.77e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 723535895   2 RLSFIVFSTQAHVIMPLTGDREKIKKGLKD-LEEVKPAGDTYIHEGLKQA-NVQIAKQGASRFSSIIIaLTDGK 73
Cdd:cd01466   37 RLSIVTFSTSAKRLSPLRRMTAKGKRSAKRvVDGLQAGGGTNVVGGLKKAlKVLGDRRQKNPVASIML-LSDGQ 109
VWA_2 pfam13519
von Willebrand factor type A domain;
2-69 3.95e-05

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 41.89  E-value: 3.95e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 723535895    2 RLSFIVFSTQAHVIMPLTGDREKIKKGLKDLEEVkpAGDTYIHEGLKQANvQIAKQGASRFSSIIIAL 69
Cdd:pfam13519  39 RVGLVTFGDGPEVLIPLTKDRAKILRALRRLEPK--GGGTNLAAALQLAR-AALKHRRKNQPRRIVLI 103
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 2-123 9.42e-05

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: 41.83  E-value: 9.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723535895   2 RLSFIVFSTQAHVIMPLT--GDREKIKKGLKDLEEVkpAGDTYIHEGLKQANVQIAKQGASRFSSI---IIALTDGKL-D 75
Cdd:cd01472   40 RVGVVQYSDDPRTEFYLNtyRSKDDVLEAVKNLRYI--GGGTNTGKALKYVRENLFTEASGSREGVpkvLVVITDGKSqD 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 723535895  76 GqiplyAEKEAKKSRELGARVYCVGVLDFVQEQLEKIADTK--EQVFPVT 123
Cdd:cd01472  118 D-----VEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPkeLYVFNVA 162
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 2-96 3.47e-04

Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). In chlorophyll biosynthesis, insertion of Mg2+ into protoporphyrin IX is catalysed by magnesium chelatase in an ATP-dependent reaction. Magnesium chelatase is a three sub-unit (BchI, BchD and BchH) enzyme with a novel arrangement of domains: the C-terminal helical domain is located behind the nucleotide binding site. The BchD domain contains a AAA domain at its N-terminus and a VWA domain at its C-terminus. The VWA domain has been speculated to be involved in mediating protein-protein interactions.


Pssm-ID: 238728 [Multi-domain]  Cd Length: 178  Bit Score: 40.34  E-value: 3.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723535895   2 RLSFIVF-STQAHVIMPLTGDREKIKKGLKDLeevkPAGD-TYIHEGLKQANVQIAKQGASR-FSSIIIALTDGKLDGQI 78
Cdd:cd01451   39 KVALIAFrGTEAEVLLPPTRSVELAKRRLARL----PTGGgTPLAAGLLAAYELAAEQARDPgQRPLIVVITDGRANVGP 114

                         90       100
                 ....*....|....*....|.
gi 723535895  79 PLYAEKE---AKKSRELGARV 96
Cdd:cd01451  115 DPTADRAlaaARKLRARGISA 135
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 2-119 1.19e-03

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: 38.91  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723535895   2 RLSFIVFSTQAHVIMPLTG---DREKIKKGLKDLEEVkpAGDTYIHEGLKQANVQIAKQGASRFSSIIIALTDGKLDGQI 78
Cdd:cd01480   48 RVGVVQYSDQQEVEAGFLRdirNYTSLKEAVDNLEYI--GGGTFTDCALKYATEQLLEGSHQKENKFLLVITDGHSDGSP 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 723535895  79 PLYAEKEAKKSRELGARVYCVGVLDFVQEQLEKIADTKEQV 119
Cdd:cd01480  126 DGGIEKAVNEADHLGIKIFFVAVGSQNEEPLSRIACDGKSA 166
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 60-115 6.75e-03

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: 36.50  E-value: 6.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 723535895  60 SRFSSIIIALTDGKLDGQIplyaEKEAKKSRELGARVYCVGVLDFVQEQLEKIADT 115
Cdd:cd01482  101 PGVPKVVILITDGKSQDDV----ELPARVLRNLGVNVFAVGVKDADESELKMIASK 152
 
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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