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Conserved domains on  [gi|1059520729|gb|AOG14216|]
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von Willebrand factor, partial [Alexandromys evoronensis]

Protein Classification

VWA domain-containing protein; VWA domain-containing protein; vWA domain-containing protein( domain architecture ID 11069210)

VWA (von Willebrand factor type A) domain-containing protein; VWA (von Willebrand factor type A) domain-containing protein; VWA (von Willebrand factor type A) domain-containing protein similar to Alicyclobacillus acidocaldarius protein Aaci_0196; VWA (von Willebrand factor type A) domain-containing protein; VWA (von Willebrand factor type A) domain-containing protein similar to Dictyostelium discoideum integrin beta-like proteins, C, D and E, and mammalian von Willebrand factor; VWA (von Willebrand factor type A) domain-containing protein similar to Dictyostelium discoideum integrin beta-like proteins, C, D and E, and mammalian von Willebrand factor; VWA (von Willebrand factor type A) domain-containing protein similar to mammalian von Willebrand factor that plays an essential role in the formation of a platelet plug, to stop bleeding, by anchoring blood platelets to the damaged vessel wall under conditions of high shear stress; VWA (von Willebrand factor type A) domain-containing protein similar to mammalian von Willebrand factor that plays an essential role in the formation of a platelet plug, to stop bleeding, by anchoring blood platelets to the damaged vessel wall under conditions of high shear stress; VWA (von Willebrand factor type A) domain-containing protein with a Flp pilus assembly protein TadE/TadG-like domain; von Willebrand factor type A (vWA) domain containing protein, often found at C-terminus of CalY family proteins; VWA (von Willebrand factor type A) domain-containing protein; VWA (von Willebrand factor type A) domain-containing protein similar to mammalian von Willebrand factor that plays an essential role in the formation of a platelet plug, to stop bleeding, by anchoring blood platelets to the damaged vessel wall under conditions of high shear stress

PubMed:  10830113|12579041

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWA pfam00092
von Willebrand factor type A domain;
265-425 2.14e-43

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 150.12  E-value: 2.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 265 DVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQEGIHISVLQYSYKVTVEYTFNEAQ*KDDVLRHVREIRYHGGNRTN 344
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 345 TAQALQYLSEHSFSPSQGDRKQAPNLVYMVT-GNP-------ASDEIKRmpGDIQVVPIGVGPhANPQELERIGWPHAPI 416
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSqdgdpeeVARELKS--AGVTVFAVGVGN-ADDEELRKIASEPGEG 157

                         170
                  ....*....|..
gi 1059520729 417 FI---RDFETLP 425
Cdd:pfam00092 158 HVftvSDFEALE 169
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 44-216 1.05e-27

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: 108.31  E-value: 1.05e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729   44 DLVFLLDGSSRLSEAEFEVLKTFVVGMMERLHISQRRIRVAVVEYHDGSHAY*DL*ARKRPSELRRIASQVKYAGSQVAS 123
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729  124 TSEVLKYTMFQIFGKVD--RPEASRIALLLTaSQEPPRLARNLVRYVQGLKKKKVIVIPVGIGPHASLKQIRLIEKQAPE 201
Cdd:smart00327  81 LGAALQYALENLFSKSAgsRRGAPKVVILIT-DGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                          170
                   ....*....|....*
gi 1059520729  202 NKAFLLSGVDELEQR 216
Cdd:smart00327 160 VYVFLPELLDLLIDL 174
VWA_N2 super family cl24671
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1-43 2.77e-21

VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to the N-terminus of the first VWA domain (pfam00092).


The actual alignment was detected with superfamily member pfam16164:

Pssm-ID: 465038  Cd Length: 79  Bit Score: 87.34  E-value: 2.77e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1059520729   1 CEACREPGGLVVPPTDAPVSSTTPYVEDTPEPPLHSFYCSKLL 43
Cdd:pfam16164  37 CEACSKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
 
Name Accession Description Interval E-value
VWA pfam00092
von Willebrand factor type A domain;
265-425 2.14e-43

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 150.12  E-value: 2.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 265 DVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQEGIHISVLQYSYKVTVEYTFNEAQ*KDDVLRHVREIRYHGGNRTN 344
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 345 TAQALQYLSEHSFSPSQGDRKQAPNLVYMVT-GNP-------ASDEIKRmpGDIQVVPIGVGPhANPQELERIGWPHAPI 416
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSqdgdpeeVARELKS--AGVTVFAVGVGN-ADDEELRKIASEPGEG 157

                         170
                  ....*....|..
gi 1059520729 417 FI---RDFETLP 425
Cdd:pfam00092 158 HVftvSDFEALE 169
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 264-415 7.02e-40

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: 140.12  E-value: 7.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 264 LDVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQEGIHISVLQYSYKVTVEYTFNEAQ*KDDVLRHVREIRYHGGNRT 343
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 344 NTAQALQYLSEHSFSPSQgDRKQAPNLVYMVT-GNP--------ASDEIKRMpgDIQVVPIGVGPhANPQELERIGWPHA 414
Cdd:cd01450    81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTdGRSddggdpkeAAAKLKDE--GIKVFVVGVGP-ADEEELREIASCPS 156


                  .
gi 1059520729 415 P 415
Cdd:cd01450   157 E 157
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 265-432 1.01e-37

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: 134.89  E-value: 1.01e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729  265 DVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQEGIHISVLQYSYKVTVEYTFNEAQ*KDDVLRHVREIRYHGGNRTN 344
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729  345 TAQALQYLSEHSFSPSQGDRKQAPNLVYMVT-GNP---------ASDEIKRMPgdIQVVPIGVGPHANPQELERIGwpHA 414
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITdGESndgpkdllkAAKELKRSG--VKVFVVGVGNDVDEEELKKLA--SA 156

                          170
                   ....*....|....*...
gi 1059520729  415 PIFIRDFetLPREAPDLV 432
Cdd:smart00327 157 PGGVYVF--LPELLDLLI 172
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 44-216 1.05e-27

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: 108.31  E-value: 1.05e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729   44 DLVFLLDGSSRLSEAEFEVLKTFVVGMMERLHISQRRIRVAVVEYHDGSHAY*DL*ARKRPSELRRIASQVKYAGSQVAS 123
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729  124 TSEVLKYTMFQIFGKVD--RPEASRIALLLTaSQEPPRLARNLVRYVQGLKKKKVIVIPVGIGPHASLKQIRLIEKQAPE 201
Cdd:smart00327  81 LGAALQYALENLFSKSAgsRRGAPKVVILIT-DGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                          170
                   ....*....|....*
gi 1059520729  202 NKAFLLSGVDELEQR 216
Cdd:smart00327 160 VYVFLPELLDLLIDL 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 43-205 3.14e-26

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: 103.53  E-value: 3.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729  43 LDLVFLLDGSSRLSEAEFEVLKTFVVGMMERLHISQRRIRVAVVEYHDGSHAY*DL*ARKRPSELRRIASQVKYAGSQVA 122
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 123 STSEVLKYTMFQIF-GKVDRPEASRIALLLTASQepPRLARNLVRYVQGLKKKKVIVIPVGIGPhASLKQIRLIEKQAPE 201
Cdd:cd01450    81 NTGKALQYALEQLFsESNARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                  ....
gi 1059520729 202 NKAF 205
Cdd:cd01450   158 RHVF 161
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1-43 2.77e-21

VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to the N-terminus of the first VWA domain (pfam00092).


Pssm-ID: 465038  Cd Length: 79  Bit Score: 87.34  E-value: 2.77e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1059520729   1 CEACREPGGLVVPPTDAPVSSTTPYVEDTPEPPLHSFYCSKLL 43
Cdd:pfam16164  37 CEACSKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
VWA pfam00092
von Willebrand factor type A domain;
44-215 3.00e-19

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 84.63  E-value: 3.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729  44 DLVFLLDGSSRLSEAEFEVLKTFVVGMMERLHISQRRIRVAVVEYHDGSHAY*DL*ARKRPSELRRIASQVKYAGSQVAS 123
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 124 TSEVLKYTMFQIFGKV--DRPEASRIALLLTA----SQEPPRLARNlvryvqgLKKKKVIVIPVGIGPhASLKQIRLIEK 197
Cdd:pfam00092  81 TGKALKYALENLFSSAagARPGAPKVVVLLTDgrsqDGDPEEVARE-------LKSAGVTVFAVGVGN-ADDEELRKIAS 152

                         170
                  ....*....|....*...
gi 1059520729 198 QAPENKAFLLSGVDELEQ 215
Cdd:pfam00092 153 EPGEGHVFTVSDFEALED 170
 
Name Accession Description Interval E-value
VWA pfam00092
von Willebrand factor type A domain;
265-425 2.14e-43

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 150.12  E-value: 2.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 265 DVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQEGIHISVLQYSYKVTVEYTFNEAQ*KDDVLRHVREIRYHGGNRTN 344
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 345 TAQALQYLSEHSFSPSQGDRKQAPNLVYMVT-GNP-------ASDEIKRmpGDIQVVPIGVGPhANPQELERIGWPHAPI 416
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSqdgdpeeVARELKS--AGVTVFAVGVGN-ADDEELRKIASEPGEG 157

                         170
                  ....*....|..
gi 1059520729 417 FI---RDFETLP 425
Cdd:pfam00092 158 HVftvSDFEALE 169
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 264-415 7.02e-40

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: 140.12  E-value: 7.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 264 LDVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQEGIHISVLQYSYKVTVEYTFNEAQ*KDDVLRHVREIRYHGGNRT 343
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 344 NTAQALQYLSEHSFSPSQgDRKQAPNLVYMVT-GNP--------ASDEIKRMpgDIQVVPIGVGPhANPQELERIGWPHA 414
Cdd:cd01450    81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTdGRSddggdpkeAAAKLKDE--GIKVFVVGVGP-ADEEELREIASCPS 156


                  .
gi 1059520729 415 P 415
Cdd:cd01450   157 E 157
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 265-432 1.01e-37

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: 134.89  E-value: 1.01e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729  265 DVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQEGIHISVLQYSYKVTVEYTFNEAQ*KDDVLRHVREIRYHGGNRTN 344
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729  345 TAQALQYLSEHSFSPSQGDRKQAPNLVYMVT-GNP---------ASDEIKRMPgdIQVVPIGVGPHANPQELERIGwpHA 414
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITdGESndgpkdllkAAKELKRSG--VKVFVVGVGNDVDEEELKKLA--SA 156

                          170
                   ....*....|....*...
gi 1059520729  415 PIFIRDFetLPREAPDLV 432
Cdd:smart00327 157 PGGVYVF--LPELLDLLI 172
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 265-409 1.25e-36

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: 131.58  E-value: 1.25e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 265 DVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQEGIHISVLQYSYKVTVEYTFNEAQ*KDDVLRHVREIRYHGGNrTN 344
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGG-TN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 345 TAQALQYLSEHSFSPSQGDRKQAPNLVYMVTGNPASDEIKRMPG-----DIQVVPIGVGPhANPQELERI 409
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVelkqaGIEVFAVGVKN-ADEEELKQI 149
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 265-410 1.02e-32

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: 121.24  E-value: 1.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 265 DVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQEGIHISVLQYSYKVTVEYTFNEAQ*KDDVLRHVREIRYHGGNrTN 344
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGN-TR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1059520729 345 TAQALQYLSEHSFSPSQGDRKQAPNLVYMVTGNPASDEIkRMPGD------IQVVPIGVgPHANPQELERIG 410
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDV-ELPARvlrnlgVNVFAVGV-KDADESELKMIA 150
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 265-421 2.53e-30

VWA_collagen alpha 3(VI) like: 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: 238758  Cd Length: 165  Bit Score: 114.73  E-value: 2.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 265 DVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQEGIHISVLQYSYKVTVEYTFNEAQ*KDDVLRHVREIRYHGGNRTN 344
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 345 TAQALQYLSEHSFSPSQGDR--KQAPNLVYMVTGNPASDEIKRMPGDIQ---VVPIGVGP-HANPQELERIGwpHAPIFI 418
Cdd:cd01481    82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKragIVPFAIGArNADLAELQQIA--FDPSFV 159


                  ....*.
gi 1059520729 419 ---RDF 421
Cdd:cd01481   160 fqvSDF 165
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 44-216 1.05e-27

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: 108.31  E-value: 1.05e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729   44 DLVFLLDGSSRLSEAEFEVLKTFVVGMMERLHISQRRIRVAVVEYHDGSHAY*DL*ARKRPSELRRIASQVKYAGSQVAS 123
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729  124 TSEVLKYTMFQIFGKVD--RPEASRIALLLTaSQEPPRLARNLVRYVQGLKKKKVIVIPVGIGPHASLKQIRLIEKQAPE 201
Cdd:smart00327  81 LGAALQYALENLFSKSAgsRRGAPKVVILIT-DGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                          170
                   ....*....|....*
gi 1059520729  202 NKAFLLSGVDELEQR 216
Cdd:smart00327 160 VYVFLPELLDLLIDL 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 43-205 3.14e-26

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: 103.53  E-value: 3.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729  43 LDLVFLLDGSSRLSEAEFEVLKTFVVGMMERLHISQRRIRVAVVEYHDGSHAY*DL*ARKRPSELRRIASQVKYAGSQVA 122
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 123 STSEVLKYTMFQIF-GKVDRPEASRIALLLTASQepPRLARNLVRYVQGLKKKKVIVIPVGIGPhASLKQIRLIEKQAPE 201
Cdd:cd01450    81 NTGKALQYALEQLFsESNARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                  ....
gi 1059520729 202 NKAF 205
Cdd:cd01450   158 RHVF 161
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 264-409 6.53e-24

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: 97.81  E-value: 6.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 264 LDVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQEGIHISVLQYSYKVTVEYTFNEAQ*KDDVLRHVREIRYHGGnRT 343
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLG-LT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1059520729 344 NTAQALQYLSEHSFSPSQGDRKQAPNLVYMVT-----GNPASDEIKRMP--GDIQVVPIGVGPHANP----QELERI 409
Cdd:cd01469    80 NTATAIQYVVTELFSESNGARKDATKVLVVITdgeshDDPLLKDVIPQAerEGIIRYAIGVGGHFQRensrEELKTI 156
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 264-409 3.60e-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: 95.33  E-value: 3.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 264 LDVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQEGIHISVLQYSYKVTVEYTFNEAQ*KDDVLRHVREIRYHGGNRT 343
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1059520729 344 NTAQALQYLSEHSFSPsqgDRKQAPNLVYMVT-GNP---------ASDEIKRMpgDIQVVPIGVGPHANPQELERI 409
Cdd:cd00198    81 NIGAALRLALELLKSA---KRPNARRVIILLTdGEPndgpellaeAARELRKL--GITVYTIGIGDDANEDELKEI 151
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1-43 2.77e-21

VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to the N-terminus of the first VWA domain (pfam00092).


Pssm-ID: 465038  Cd Length: 79  Bit Score: 87.34  E-value: 2.77e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1059520729   1 CEACREPGGLVVPPTDAPVSSTTPYVEDTPEPPLHSFYCSKLL 43
Cdd:pfam16164  37 CEACSKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 264-410 3.12e-21

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 91.68  E-value: 3.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 264 LDVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQEGIHISVLQYSYKVTVEYTFNEAQ*KDDVLRHVREIRYHGGNrT 343
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG-T 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1059520729 344 NTAQALQYLSEHSFSPSQGDRKQAPNL---VYMVTGNPASDEIK------RMPGdIQVVPIGVGpHANPQELERIG 410
Cdd:cd01475    82 MTGLAIQYAMNNAFSEAEGARPGSERVprvGIVVTDGRPQDDVSevaakaRALG-IEMFAVGVG-RADEEELREIA 155
VWA pfam00092
von Willebrand factor type A domain;
44-215 3.00e-19

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 84.63  E-value: 3.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729  44 DLVFLLDGSSRLSEAEFEVLKTFVVGMMERLHISQRRIRVAVVEYHDGSHAY*DL*ARKRPSELRRIASQVKYAGSQVAS 123
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 124 TSEVLKYTMFQIFGKV--DRPEASRIALLLTA----SQEPPRLARNlvryvqgLKKKKVIVIPVGIGPhASLKQIRLIEK 197
Cdd:pfam00092  81 TGKALKYALENLFSSAagARPGAPKVVVLLTDgrsqDGDPEEVARE-------LKSAGVTVFAVGVGN-ADDEELRKIAS 152

                         170
                  ....*....|....*...
gi 1059520729 198 QAPENKAFLLSGVDELEQ 215
Cdd:pfam00092 153 EPGEGHVFTVSDFEALED 170
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 264-405 3.90e-18

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: 82.05  E-value: 3.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 264 LDVVFVLEGSDEIGEAN-FNKSKEFLEEVIQRMDVGQEGIHISVLQYSYKVTVEYTFNE--AQ*KD---DVLRHVREIRY 337
Cdd:cd01471     1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpnSTNKDlalNAIRALLSLYY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1059520729 338 HGGNrTNTAQALQYLSEHSFSpSQGDRKQAPNLVYMVT-GNPASD--------EIKRMPGDIQVvpIGVGPHANPQE 405
Cdd:cd01471    81 PNGS-TNTTSALLVVEKHLFD-TRGNRENAPQLVIIMTdGIPDSKfrtlkearKLRERGVIIAV--LGVGQGVNHEE 153
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 43-205 2.07e-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: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 76.45  E-value: 2.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729  43 LDLVFLLDGSSRLSEAEFEVLKTFVVGMMERLHISQRRIRVAVVEYHDGSHAY*DL*ARKRPSELRRIASQVKYAGSQVA 122
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 123 STSEVLKYTMfQIFGKVDRPEASRIALLLT--ASQEPPRLARNLVRYvqgLKKKKVIVIPVGIGPHASLKQIRLIEKQAP 200
Cdd:cd00198    81 NIGAALRLAL-ELLKSAKRPNARRVIILLTdgEPNDGPELLAEAARE---LRKLGITVYTIGIGDDANEDELKEIADKTT 156


                  ....*
gi 1059520729 201 ENKAF 205
Cdd:cd00198   157 GGAVF 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 264-410 2.90e-16

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 75.90  E-value: 2.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 264 LDVVFVLEGSDEIGEAnFNKSKEFLEEVIQRMDVGQEGIHISVLQYS--YKVTVEYTFNEAQ*KDDVLRHVREIRYHGGN 341
Cdd:cd01476     1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1059520729 342 rTNTAQALQYLSEHsFSPSQGDRKQAPNLVYMVTGNPASDEIKRM-------PGdIQVVPIGVGPHANP--QELERIG 410
Cdd:cd01476    80 -TATGAAIEVALQQ-LDPSEGRREGIPKVVVVLTDGRSHDDPEKQarilravPN-IETFAVGTGDPGTVdtEELHSIT 154
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 44-192 6.00e-14

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: 69.18  E-value: 6.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729  44 DLVFLLDGSSRLSEAEFEVLKTFVVGMMERLHISQRRIRVAVVEYHDGSHAY*DL*ARKRPSELRRIASQVKYAGSQVAs 123
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN- 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1059520729 124 TSEVLKYTMFQIFGKVDRPEAS--RIALLLTASQEPPRLARNLVRyvqgLKKKKVIVIPVGIGPHAS--LKQI 192
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGvpKVLVVITDGKSQDDVEEPAVE----LKQAGIEVFAVGVKNADEeeLKQI 149
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 44-155 6.61e-11

VWA_collagen alpha 3(VI) like: 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: 238758  Cd Length: 165  Bit Score: 60.42  E-value: 6.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729  44 DLVFLLDGSSRLSEAEFEVLKTFVVGMMERLHISQRRIRVAVVEYHDGSHAY*DL*ARKRPSELRRIASQVKYAGSQVAS 123
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1059520729 124 TSEVLKYTMFQIFgkvDRPEASRIA-------LLLTASQ 155
Cdd:cd01481    82 TGSALDYVVKNLF---TKSAGSRIEegvpqflVLITGGK 117
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 43-152 3.46e-10

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 59.71  E-value: 3.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729  43 LDLVFLLDGSSRLSEAEFEVLKTFVVGMMERLHISQRRIRVAVVEYHDGSHAY*DL*ARKRPSELRRIASQVKYAgSQVA 122
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYL-ETGT 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1059520729 123 STSEVLKYTMFQIFGKVD--RPEA---SRIALLLT 152
Cdd:cd01475    82 MTGLAIQYAMNNAFSEAEgaRPGServPRVGIVVT 116
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 44-192 1.35e-09

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: 56.91  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729  44 DLVFLLDGSSRLSEAEFEVLKTFVVGMMERLHISQRRIRVAVVEYHDGSHAY*DL*ARKRPSELRRIASQVKYAGSQvAS 123
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGN-TR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1059520729 124 TSEVLKYTMFQIF--GKVDRPEASRIALLLT--ASQEPPRLArnlvryVQGLKKKKVIVIPVGIGPH--ASLKQI 192
Cdd:cd01482    81 TGKALTHVREKNFtpDAGARPGVPKVVILITdgKSQDDVELP------ARVLRNLGVNVFAVGVKDAdeSELKMI 149
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 264-366 6.63e-09

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: 55.08  E-value: 6.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 264 LDVVFVLEGSDEIGEANFNKSKEFLEEVIQRM------DVGQEGIHISVLQYSYKVTVEYTFNEAQ*KDDVLRH-VREIR 336
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTSLKEaVDNLE 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1059520729 337 YHGGNrTNTAQALQYLSEHSFSPSQGDRKQ 366
Cdd:cd01480    83 YIGGG-TFTDCALKYATEQLLEGSHQKENK 111
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 43-208 6.41e-08

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: 52.36  E-value: 6.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729  43 LDLVFLLDGSSRLSEAEFEVLKTFVVGMMERLHISQRRIRVAVVEYHDGSHAY*DL*ARKRPSELRRIASQVKYAGSqVA 122
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLG-LT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 123 STSEVLKYTMFQIF--GKVDRPEASRIALLLT--ASQEPPRLARNLvryvQGLKKKKVIVIPVGIGPH----ASLKQIRL 194
Cdd:cd01469    80 NTATAIQYVVTELFseSNGARKDATKVLVVITdgESHDDPLLKDVI----PQAEREGIIRYAIGVGGHfqreNSREELKT 155

                         170
                  ....*....|....
gi 1059520729 195 IEKQAPENKAFLLS 208
Cdd:cd01469   156 IASKPPEEHFFNVT 169
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 264-355 3.23e-07

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: 50.36  E-value: 3.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 264 LDVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQEGIHISVLQYSYKVTVE---YTFNEAQ*KDDVLRHVREIRY--H 338
Cdd:cd01470     1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIvsiRDFNSND-ADDVIKRLEDFNYddH 79

                          90
                  ....*....|....*...
gi 1059520729 339 GGNR-TNTAQALQYLSEH 355
Cdd:cd01470    80 GDKTgTNTAAALKKVYER 97
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 43-184 5.76e-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: 5.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729  43 LDLVFLLDGSSRLSEA-EFEVLKTFVVGMMERLHISQRRIRVAVVEYHDGSHAY*DL*A--RKRPSELRRIASQVK---Y 116
Cdd:cd01471     1 LDLYLLVDGSGSIGYSnWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpnSTNKDLALNAIRALLslyY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 117 AGSQVASTSEVLKYTMFQIFGKVDRPEASRIALLLT--ASQEPPRlARNLVRyvqGLKKKKVIVIPVGIG 184
Cdd:cd01471    81 PNGSTNTTSALLVVEKHLFDTRGNRENAPQLVIIMTdgIPDSKFR-TLKEAR---KLRERGVIIAVLGVG 146
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 265-387 2.49e-06

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 47.70  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 265 DVVFVLEGSDEIGEANFNKS-KEFLEEVIQRMDVGQEGIHISVLQYSYKVTVEYTF--NEAQ*KDDVLRHVREIR--YHG 339
Cdd:cd01473     2 DLTLILDESASIGYSNWRKDvIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFsdEERYDKNELLKKINDLKnsYRS 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1059520729 340 GNRTNTAQALQYlSEHSFSPSQGDRKQAPNLVYMVT-GNPASDEIKRMP 387
Cdd:cd01473    82 GGETYIVEALKY-GLKNYTKHGNRRKDAPKVTMLFTdGNDTSASKKELQ 129
VWA_2 pfam13519
von Willebrand factor type A domain;
266-374 5.91e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 44.59  E-value: 5.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729 266 VVFVLEGS-----DEIGEANFNKSKEFLEEVIQRMDvgqeGIHISVLQYSYKVTVEYTFNeaQ*KDDVLRHVREIRYHGG 340
Cdd:pfam13519   1 LVFVLDTSgsmrnGDYGPTRLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1059520729 341 NrTNTAQALQYLSEHsfspSQGDRKQAPNLVYMV 374
Cdd:pfam13519  75 G-TNLAAALQLARAA----LKHRRKNQPRRIVLI 103
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 43-188 1.85e-05

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: 45.07  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059520729  43 LDLVFLLDGSSRLSEAEFEVLKTFVVGMMERLH------ISQRRIRVAVVEY-HDGSHAY*DL*ARKRPSELRRIASQVK 115
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFLkdyyrkDPAGSWRVGVVQYsDQQEVEAGFLRDIRNYTSLKEAVDNLE 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1059520729 116 YAGsQVASTSEVLKYTMFQIFgKVDRPEASRIALLLTASQEPPRLARNLVRYVQGLKKKKVIVIPVGIGPHAS 188
Cdd:cd01480    83 YIG-GGTFTDCALKYATEQLL-EGSHQKENKFLLVITDGHSDGSPDGGIEKAVNEADHLGIKIFFVAVGSQNE 153
 
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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