NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|347668599|gb|AEP18909|]
View 

von Willebrand factor, partial [Hystrix brachyura]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
VWA pfam00092
von Willebrand factor type A domain;
261-406 1.91e-40

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 141.64  E-value: 1.91e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599  261 DVVFVLEGSDKVGEANFNQSKEFMAEVIQRMDVGQGGVHVTVLQYSYMVTVEYTFREAQSKQDLLQHIREIHFRGGNQTN 340
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347668599  341 TGLALQYVSEHSFSASQGDREQAPNLVYMVT-GNPASDEIKRL-----PGDVQVVPIGVGpGANMQELQRIS 406
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSQDGDPEEVarelkSAGVTVFAVGVG-NADDEELRKIA 151
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 39-201 1.54e-27

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: 106.99  E-value: 1.54e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599  39 LDLVFLLDGSSRLSEAEFEVLKAFVVSVMERLHISQKRIRVAVVEYHDGSHAYLELKARKRPSELRRIASQVKYAGSQEA 118
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 119 STSEVLKYTLFQIFGRIE-RPEASRIVLLLTASSEprQMARNLVRYVQGLKKKKVILMPVGIGPhANLQQIRLIEKQAPE 197
Cdd:cd01450   81 NTGKALQYALEQLFSESNaRENVPKVIIVLTDGRS--DDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                 ....
gi 347668599 198 NKAF 201
Cdd:cd01450  158 RHVF 161
VWA_N2 super family cl24671
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1-39 9.96e-19

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: 80.02  E-value: 9.96e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 347668599    1 QEPGGLVVPPTEAPIHATTPYVEDTPEPPLHDFYCSKLL 39
Cdd:pfam16164  41 SKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
 
Name Accession Description Interval E-value
VWA pfam00092
von Willebrand factor type A domain;
261-406 1.91e-40

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 141.64  E-value: 1.91e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599  261 DVVFVLEGSDKVGEANFNQSKEFMAEVIQRMDVGQGGVHVTVLQYSYMVTVEYTFREAQSKQDLLQHIREIHFRGGNQTN 340
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347668599  341 TGLALQYVSEHSFSASQGDREQAPNLVYMVT-GNPASDEIKRL-----PGDVQVVPIGVGpGANMQELQRIS 406
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSQDGDPEEVarelkSAGVTVFAVGVG-NADDEELRKIA 151
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 260-411 5.31e-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: 5.31e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 260 LDVVFVLEGSDKVGEANFNQSKEFMAEVIQRMDVGQGGVHVTVLQYSYMVTVEYTFREAQSKQDLLQHIREIHFRGGNQT 339
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 340 NTGLALQYVSEHSFSASQgDREQAPNLVYMVT-GNP--------ASDEIKRLpgDVQVVPIGVGPgANMQELQRISWPST 410
Cdd:cd01450   81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTdGRSddggdpkeAAAKLKDE--GIKVFVVGVGP-ADEEELREIASCPS 156


                 .
gi 347668599 411 P 411
Cdd:cd01450  157 E 157
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 261-406 1.13e-35

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: 129.11  E-value: 1.13e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599   261 DVVFVLEGSDKVGEANFNQSKEFMAEVIQRMDVGQGGVHVTVLQYSYMVTVEYTFREAQSKQDLLQHIREIHFRGGNQTN 340
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 347668599   341 TGLALQYVSEHSFSASQGDREQAPNLVYMVT-GNP---------ASDEIKRLPgdVQVVPIGVGPGANMQELQRIS 406
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITdGESndgpkdllkAAKELKRSG--VKVFVVGVGNDVDEEELKKLA 154
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 39-201 1.54e-27

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: 106.99  E-value: 1.54e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599  39 LDLVFLLDGSSRLSEAEFEVLKAFVVSVMERLHISQKRIRVAVVEYHDGSHAYLELKARKRPSELRRIASQVKYAGSQEA 118
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 119 STSEVLKYTLFQIFGRIE-RPEASRIVLLLTASSEprQMARNLVRYVQGLKKKKVILMPVGIGPhANLQQIRLIEKQAPE 197
Cdd:cd01450   81 NTGKALQYALEQLFSESNaRENVPKVIIVLTDGRS--DDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                 ....
gi 347668599 198 NKAF 201
Cdd:cd01450  158 RHVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 40-212 1.57e-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: 107.54  E-value: 1.57e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599    40 DLVFLLDGSSRLSEAEFEVLKAFVVSVMERLHISQKRIRVAVVEYHDGSHAYLELKARKRPSELRRIASQVKYAGSQEAS 119
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599   120 TSEVLKYTLFQIFGRIE--RPEASRIVLLLTaSSEPRQMARNLVRYVQGLKKKKVILMPVGIGPHANLQQIRLIEKQAPE 197
Cdd:smart00327  81 LGAALQYALENLFSKSAgsRRGAPKVVILIT-DGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                          170
                   ....*....|....*
gi 347668599   198 NKAFVLSGVDELEQR 212
Cdd:smart00327 160 VYVFLPELLDLLIDL 174
VWA pfam00092
von Willebrand factor type A domain;
40-211 1.10e-19

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 85.79  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599   40 DLVFLLDGSSRLSEAEFEVLKAFVVSVMERLHISQKRIRVAVVEYhdGSHAYLE--LKARKRPSELRRIASQVKYAGSQE 117
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQY--SSDVRTEfpLNDYSSKEELLSAVDNLRYLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599  118 ASTSEVLKYTLFQIFGRIE--RPEASRIVLLLTA----SSEPRQMARNlvryvqgLKKKKVILMPVGIGPHANlQQIRLI 191
Cdd:pfam00092  79 TNTGKALKYALENLFSSAAgaRPGAPKVVVLLTDgrsqDGDPEEVARE-------LKSAGVTVFAVGVGNADD-EELRKI 150

                         170       180
                  ....*....|....*....|
gi 347668599  192 EKQAPENKAFVLSGVDELEQ 211
Cdd:pfam00092 151 ASEPGEGHVFTVSDFEALED 170
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1-39 9.96e-19

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: 80.02  E-value: 9.96e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 347668599    1 QEPGGLVVPPTEAPIHATTPYVEDTPEPPLHDFYCSKLL 39
Cdd:pfam16164  41 SKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
260-406 3.90e-05

Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 44.15  E-value: 3.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 260 LDVVFVLEGS-----DKVGEANfNQSKEFMAEVIQRmDVGQGGVHVTVLQYSYMVTVEYTFREAQSkqdllQHIREIHFR 334
Cdd:COG4245    6 LPVYLLLDTSgsmsgEPIEALN-EGLQALIDELRQD-PYALETVEVSVITFDGEAKVLLPLTDLED-----FQPPDLSAS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 335 GGnqTNTGLALQYV-----SEHSFSASQGDREQAPnLVYMVT-GNP-------ASDEIKRLPGD--VQVVPIGVGPGANM 399
Cdd:COG4245   79 GG--TPLGAALELLldlieRRVQKYTAEGKGDWRP-VVFLITdGEPtdsdweaALQRLKDGEAAkkANIFAIGVGPDADT 155


                 ....*..
gi 347668599 400 QELQRIS 406
Cdd:COG4245  156 EVLKQLT 162
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 39-188 6.17e-03

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 38.16  E-value: 6.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599  39 LDLVFLLDGSSRLSEAEFEVLKAFVVSVMERLHisqKRIRVAVVEYHDGSHAYLELKARKRPSELRRIASQVK------- 111
Cdd:COG2304   92 LNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLR---PGDRVSIVTFAGDARVLLPPTPATDRAKILAAIDRLQagggtal 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 112 YAGSQEAstsevlkytlFQIFGRIERPEASRIVLLLT---ASSEPRQMARnLVRYVQGLKKKKVILMPVGIGPHAN---L 185
Cdd:COG2304  169 GAGLELA----------YELARKHFIPGRVNRVILLTdgdANVGITDPEE-LLKLAEEAREEGITLTTLGVGSDYNedlL 237


                 ...
gi 347668599 186 QQI 188
Cdd:COG2304  238 ERL 240
 
Name Accession Description Interval E-value
VWA pfam00092
von Willebrand factor type A domain;
261-406 1.91e-40

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 141.64  E-value: 1.91e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599  261 DVVFVLEGSDKVGEANFNQSKEFMAEVIQRMDVGQGGVHVTVLQYSYMVTVEYTFREAQSKQDLLQHIREIHFRGGNQTN 340
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347668599  341 TGLALQYVSEHSFSASQGDREQAPNLVYMVT-GNPASDEIKRL-----PGDVQVVPIGVGpGANMQELQRIS 406
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSQDGDPEEVarelkSAGVTVFAVGVG-NADDEELRKIA 151
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 260-411 5.31e-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: 5.31e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 260 LDVVFVLEGSDKVGEANFNQSKEFMAEVIQRMDVGQGGVHVTVLQYSYMVTVEYTFREAQSKQDLLQHIREIHFRGGNQT 339
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 340 NTGLALQYVSEHSFSASQgDREQAPNLVYMVT-GNP--------ASDEIKRLpgDVQVVPIGVGPgANMQELQRISWPST 410
Cdd:cd01450   81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTdGRSddggdpkeAAAKLKDE--GIKVFVVGVGP-ADEEELREIASCPS 156


                 .
gi 347668599 411 P 411
Cdd:cd01450  157 E 157
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 261-406 5.75e-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: 129.66  E-value: 5.75e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 261 DVVFVLEGSDKVGEANFNQSKEFMAEVIQRMDVGQGGVHVTVLQYSYMVTVEYTFREAQSKQDLLQHIREIHFRGGNqTN 340
Cdd:cd01472    2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGG-TN 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 347668599 341 TGLALQYVSEHSFSASQGDREQAPNLVYMVTGNPASDEIkRLPG----DVQVVPIGVGPG-ANMQELQRIS 406
Cdd:cd01472   81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDV-EEPAvelkQAGIEVFAVGVKnADEEELKQIA 150
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 261-406 1.13e-35

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: 129.11  E-value: 1.13e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599   261 DVVFVLEGSDKVGEANFNQSKEFMAEVIQRMDVGQGGVHVTVLQYSYMVTVEYTFREAQSKQDLLQHIREIHFRGGNQTN 340
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 347668599   341 TGLALQYVSEHSFSASQGDREQAPNLVYMVT-GNP---------ASDEIKRLPgdVQVVPIGVGPGANMQELQRIS 406
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITdGESndgpkdllkAAKELKRSG--VKVFVVGVGNDVDEEELKKLA 154
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 261-406 2.07e-33

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: 122.82  E-value: 2.07e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 261 DVVFVLEGSDKVGEANFNQSKEFMAEVIQRMDVGQGGVHVTVLQYSYMVTVEYTFREAQSKQDLLQHIREIHFRGGNQTN 340
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347668599 341 TGLALQYVSEHSFSASQGDR--EQAPNLVYMVTGNPASDEIKRLPGDVQ---VVPIGVGP-GANMQELQRIS 406
Cdd:cd01481   82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKragIVPFAIGArNADLAELQQIA 153
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 261-411 9.51e-29

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: 110.45  E-value: 9.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 261 DVVFVLEGSDKVGEANFNQSKEFMAEVIQRMDVGQGGVHVTVLQYSYMVTVEYTFREAQSKQDLLQHIREIHFRGGNqTN 340
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGN-TR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 347668599 341 TGLALQYVSEHSFSASQGDREQAPNLVYMVTGNPASDEIkRLPGD------VQVVPIGVgPGANMQELQRISwpSTP 411
Cdd:cd01482   81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDV-ELPARvlrnlgVNVFAVGV-KDADESELKMIA--SKP 153
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 39-201 1.54e-27

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: 106.99  E-value: 1.54e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599  39 LDLVFLLDGSSRLSEAEFEVLKAFVVSVMERLHISQKRIRVAVVEYHDGSHAYLELKARKRPSELRRIASQVKYAGSQEA 118
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 119 STSEVLKYTLFQIFGRIE-RPEASRIVLLLTASSEprQMARNLVRYVQGLKKKKVILMPVGIGPhANLQQIRLIEKQAPE 197
Cdd:cd01450   81 NTGKALQYALEQLFSESNaRENVPKVIIVLTDGRS--DDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSE 157


                 ....
gi 347668599 198 NKAF 201
Cdd:cd01450  158 RHVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 40-212 1.57e-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: 107.54  E-value: 1.57e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599    40 DLVFLLDGSSRLSEAEFEVLKAFVVSVMERLHISQKRIRVAVVEYHDGSHAYLELKARKRPSELRRIASQVKYAGSQEAS 119
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599   120 TSEVLKYTLFQIFGRIE--RPEASRIVLLLTaSSEPRQMARNLVRYVQGLKKKKVILMPVGIGPHANLQQIRLIEKQAPE 197
Cdd:smart00327  81 LGAALQYALENLFSKSAgsRRGAPKVVILIT-DGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                          170
                   ....*....|....*
gi 347668599   198 NKAFVLSGVDELEQR 212
Cdd:smart00327 160 VYVFLPELLDLLIDL 174
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 260-412 2.47e-22

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: 94.37  E-value: 2.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 260 LDVVFVLEGSDKVGEANFNQSKEFMAEVIQRMDVGQGGVHVTVLQYSYMVTVEYTFREAQSKQDLLQHIREIHF--RGgn 337
Cdd:cd01475    3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYleTG-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 338 qTNTGLALQYVSEHSFSASQGDR---EQAPNLVYMVTGNPASDEIK------RLPGdVQVVPIGVGpGANMQELQRISwp 408
Cdd:cd01475   81 -TMTGLAIQYAMNNAFSEAEGARpgsERVPRVGIVVTDGRPQDDVSevaakaRALG-IEMFAVGVG-RADEEELREIA-- 155


                 ....
gi 347668599 409 STPI 412
Cdd:cd01475  156 SEPL 159
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 260-411 6.90e-22

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: 91.47  E-value: 6.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 260 LDVVFVLEGSDKVGEANFNQSKEFMAEVIQRMDVGQGGVHVTVLQYSYMVTVEYTFREAQSKQDLLQHIREIHFRGGNQT 339
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 340 NTGLALQYVSEHSFSAsqgDREQAPNLVYMVT-GNP---------ASDEIKRLpgDVQVVPIGVGPGANMQELQRISWPS 409
Cdd:cd00198   81 NIGAALRLALELLKSA---KRPNARRVIILLTdGEPndgpellaeAARELRKL--GITVYTIGIGDDANEDELKEIADKT 155


                 ..
gi 347668599 410 TP 411
Cdd:cd00198  156 TG 157
VWA pfam00092
von Willebrand factor type A domain;
40-211 1.10e-19

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 85.79  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599   40 DLVFLLDGSSRLSEAEFEVLKAFVVSVMERLHISQKRIRVAVVEYhdGSHAYLE--LKARKRPSELRRIASQVKYAGSQE 117
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQY--SSDVRTEfpLNDYSSKEELLSAVDNLRYLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599  118 ASTSEVLKYTLFQIFGRIE--RPEASRIVLLLTA----SSEPRQMARNlvryvqgLKKKKVILMPVGIGPHANlQQIRLI 191
Cdd:pfam00092  79 TNTGKALKYALENLFSSAAgaRPGAPKVVVLLTDgrsqDGDPEEVARE-------LKSAGVTVFAVGVGNADD-EELRKI 150

                         170       180
                  ....*....|....*....|
gi 347668599  192 EKQAPENKAFVLSGVDELEQ 211
Cdd:pfam00092 151 ASEPGEGHVFTVSDFEALED 170
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1-39 9.96e-19

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: 80.02  E-value: 9.96e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 347668599    1 QEPGGLVVPPTEAPIHATTPYVEDTPEPPLHDFYCSKLL 39
Cdd:pfam16164  41 SKPGTLVVPPTEGPVTTTTPYVEDTPEPPLHDFYCSKLL 79
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 39-201 2.08e-18

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: 81.84  E-value: 2.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599  39 LDLVFLLDGSSRLSEAEFEVLKAFVVSVMERLHISQKRIRVAVVEYHDGSHAYLELKARKRPSELRRIASQVKYAGSQEA 118
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 119 STSEVLKYTLfQIFGRIERPEASRIVLLLTaSSEPRQMARNLVRYVQGLKKKKVILMPVGIGPHANLQQIRLIEKQAPEN 198
Cdd:cd00198   81 NIGAALRLAL-ELLKSAKRPNARRVIILLT-DGEPNDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIADKTTGG 158


                 ...
gi 347668599 199 KAF 201
Cdd:cd00198  159 AVF 161
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 260-371 1.06e-17

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: 80.09  E-value: 1.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 260 LDVVFVLEGSDKVGEANFNQSKEFMAEVIQRMDVGQGGVHVTVLQYSYMVTVEYTFREAQSKQDLLQHIREIHFRGGnQT 339
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLG-LT 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 347668599 340 NTGLALQYVSEHSFSASQGDREQAPNLVYMVT 371
Cdd:cd01469   80 NTATAIQYVVTELFSESNGARKDATKVLVVIT 111
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 260-401 1.32e-14

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: 71.65  E-value: 1.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 260 LDVVFVLEGSDKVGEAN-FNQSKEFMAEVIQRMDVGQGGVHVTVLQYSYMVTVEYTFRE--AQSKQ---DLLQHIREIHF 333
Cdd:cd01471    1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpnSTNKDlalNAIRALLSLYY 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 347668599 334 RGGNqTNTGLALQYVSEHSFSaSQGDREQAPNLVYMVT-GNPASD--------EIKRLPGDVQVvpIGVGPGANMQE 401
Cdd:cd01471   81 PNGS-TNTTSALLVVEKHLFD-TRGNRENAPQLVIIMTdGIPDSKfrtlkearKLRERGVIIAV--LGVGQGVNHEE 153
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 260-406 3.71e-13

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: 67.04  E-value: 3.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 260 LDVVFVLEGSDKVGEAnFNQSKEFMAEVIQRMDVGQGGVHVTVLQYSYMVT--VEYTFREAQSKQDLLQHIREIHFRGGN 337
Cdd:cd01476    1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 347668599 338 qTNTGLALQYVSEHsFSASQGDREQAPNLVYMVTG-----NP--ASDEIKRLPG-DVQVVPIGVGPGANMQELQRIS 406
Cdd:cd01476   80 -TATGAAIEVALQQ-LDPSEGRREGIPKVVVVLTDgrshdDPekQARILRAVPNiETFAVGTGDPGTVDTEELHSIT 154
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 40-188 1.05e-12

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: 65.71  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599  40 DLVFLLDGSSRLSEAEFEVLKAFVVSVMERLHISQKRIRVAVVEYHDGSHAYLELKARKRPSELRRIASQVKYAGSQeAS 119
Cdd:cd01472    2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGG-TN 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 347668599 120 TSEVLKYTLFQIFGRIERPEAS--RIVLLLTASSEP---RQMARNlvryvqgLKKKKVILMPVGIGPH--ANLQQI 188
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 ...
 40-188 7.73e-12

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: 63.11  E-value: 7.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599  40 DLVFLLDGSSRLSEAEFEVLKAFVVSVMERLHISQKRIRVAVVEYHDGSHAYLELKARKRPSELRRIASQVKYAGSQEAS 119
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 347668599 120 TSEVLKYTLFQIFgriERPEASRI-------VLLLTAssepRQMARNLVRYVQGLKKKKVILMPVGIGP--HANLQQI 188
Cdd:cd01481   82 TGSALDYVVKNLF---TKSAGSRIeegvpqfLVLITG----GKSQDDVERPAVALKRAGIVPFAIGARNadLAELQQI 152
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 40-148 2.12e-11

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: 61.92  E-value: 2.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599  40 DLVFLLDGSSRLSEAEFEVLKAFVVSVMERLHISQKRIRVAVVEYHDGSHAYLELKARKRPSELRRIASQVKYAGSQeAS 119
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGN-TR 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 347668599 120 TSEVLKYTLFQIF--GRIERPEASRIVLLLT 148
Cdd:cd01482   81 TGKALTHVREKNFtpDAGARPGVPKVVILIT 111
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 39-148 7.67e-11

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: 61.63  E-value: 7.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599  39 LDLVFLLDGSSRLSEAEFEVLKAFVVSVMERLHISQKRIRVAVVEYHDGSHAYLELKARKRPSELRRIASQVKYAgSQEA 118
Cdd:cd01475    3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYL-ETGT 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 347668599 119 STSEVLKYTLFQIFGRIE--RPEA---SRIVLLLT 148
Cdd:cd01475   82 MTGLAIQYAMNNAFSEAEgaRPGServPRVGIVVT 116
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 260-362 1.10e-10

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: 60.48  E-value: 1.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 260 LDVVFVLEGSDKVGEANFNQSKEFMAEVIQRM------DVGQGGVHVTVLQYSYMVTVEYTF-REAQSKQDLLQHIREIH 332
Cdd:cd01480    3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFlRDIRNYTSLKEAVDNLE 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 347668599 333 FRGGNqTNTGLALQYVSEHSFSASQGDREQ 362
Cdd:cd01480   83 YIGGG-TFTDCALKYATEQLLEGSHQKENK 111
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 39-191 3.93e-09

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: 55.85  E-value: 3.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599  39 LDLVFLLDGSSRLSEA-EFEVLKAFVVSVMERLHISQKRIRVAVVEYHDGSHAYLELKA--RKRPSELRRIASQVKYAGS 115
Cdd:cd01471    1 LDLYLLVDGSGSIGYSnWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpnSTNKDLALNAIRALLSLYY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 116 QEAST------SEVLKYtLFQifGRIERPEASRIVLLLT-ASSEPRQMARNLVRyvqGLKKKKVILMPVGIGPHANLQQI 188
Cdd:cd01471   81 PNGSTnttsalLVVEKH-LFD--TRGNRENAPQLVIIMTdGIPDSKFRTLKEAR---KLRERGVIIAVLGVGQGVNHEEN 154


                 ...
gi 347668599 189 RLI 191
Cdd:cd01471  155 RSL 157
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 39-204 6.11e-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: 6.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599  39 LDLVFLLDGSSRLSEAEFEVLKAFVVSVMERLHISQKRIRVAVVEYHDGSHAYLELKARKRPSELRRIASQVKYAGSQeA 118
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGL-T 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 119 STSEVLKYTLFQIF--GRIERPEASRIVLLLT---ASSEPRqmarnLVRYVQGLKKKKVILMPVGIGPHAN----LQQIR 189
Cdd:cd01469   80 NTATAIQYVVTELFseSNGARKDATKVLVVITdgeSHDDPL-----LKDVIPQAEREGIIRYAIGVGGHFQrensREELK 154

                        170
                 ....*....|....*
gi 347668599 190 LIEKQAPENKAFVLS 204
Cdd:cd01469  155 TIASKPPEEHFFNVT 169
VWA_2 pfam13519
von Willebrand factor type A domain;
262-370 3.21e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 45.36  E-value: 3.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599  262 VVFVLEGS-----DKVGEANFNQSKEFMAEVIQRMDvgqgGVHVTVLQYSYMVTVEYTFReaQSKQDLLQHIREIHFRGG 336
Cdd:pfam13519   1 LVFVLDTSgsmrnGDYGPTRLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 347668599  337 NqTNTGLALQYVSehsfSASQGDREQAPNLVYMV 370
Cdd:pfam13519  75 G-TNLAAALQLAR----AALKHRRKNQPRRIVLI 103
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 39-189 1.33e-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: 45.45  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599  39 LDLVFLLDGSSRLSEAEFEVLKAFVVSVMERLHISQKR------IRVAVVEY-HDGSHAYLELKARKRPSELRRIASQVK 111
Cdd:cd01480    3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRkdpagsWRVGVVQYsDQQEVEAGFLRDIRNYTSLKEAVDNLE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 112 YAGsqEAS-TSEVLKYTLFQIfgRIERPEAS-RIVLLLTASSEPRQMARNLVRYVQGLKKKKVILMPVGIGPHANLQQIR 189
Cdd:cd01480   83 YIG--GGTfTDCALKYATEQL--LEGSHQKEnKFLLVITDGHSDGSPDGGIEKAVNEADHLGIKIFFVAVGSQNEEPLSR 158
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
260-406 3.90e-05

Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 44.15  E-value: 3.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 260 LDVVFVLEGS-----DKVGEANfNQSKEFMAEVIQRmDVGQGGVHVTVLQYSYMVTVEYTFREAQSkqdllQHIREIHFR 334
Cdd:COG4245    6 LPVYLLLDTSgsmsgEPIEALN-EGLQALIDELRQD-PYALETVEVSVITFDGEAKVLLPLTDLED-----FQPPDLSAS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 335 GGnqTNTGLALQYV-----SEHSFSASQGDREQAPnLVYMVT-GNP-------ASDEIKRLPGD--VQVVPIGVGPGANM 399
Cdd:COG4245   79 GG--TPLGAALELLldlieRRVQKYTAEGKGDWRP-VVFLITdGEPtdsdweaALQRLKDGEAAkkANIFAIGVGPDADT 155


                 ....*..
gi 347668599 400 QELQRIS 406
Cdd:COG4245  156 EVLKQLT 162
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 260-405 4.17e-03

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: 38.04  E-value: 4.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 260 LDVVFVLEGSDKVGEANFNQSKEFMAEVIQRMDVGQGGVHVTVLQYSYMVTVEYTFREAQSKQ--DLLQHIREI-HFRGG 336
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDadDVIKRLEDFnYDDHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 337 NQ--TNTGLALQYVSEHSFSASQGDRE---QAPNLVYMVT-------GNP--ASDEIKRLPG-------------DVQVv 389
Cdd:cd01470   81 DKtgTNTAAALKKVYERMALEKVRNKEafnETRHVIILFTdgksnmgGSPlpTVDKIKNLVYknnksdnpredylDVYV- 159

                        170
                 ....*....|....*.
gi 347668599 390 pIGVGPGANMQELQRI 405
Cdd:cd01470  160 -FGVGDDVNKEELNDL 174
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 39-188 6.17e-03

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 38.16  E-value: 6.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599  39 LDLVFLLDGSSRLSEAEFEVLKAFVVSVMERLHisqKRIRVAVVEYHDGSHAYLELKARKRPSELRRIASQVK------- 111
Cdd:COG2304   92 LNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLR---PGDRVSIVTFAGDARVLLPPTPATDRAKILAAIDRLQagggtal 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347668599 112 YAGSQEAstsevlkytlFQIFGRIERPEASRIVLLLT---ASSEPRQMARnLVRYVQGLKKKKVILMPVGIGPHAN---L 185
Cdd:COG2304  169 GAGLELA----------YELARKHFIPGRVNRVILLTdgdANVGITDPEE-LLKLAEEAREEGITLTTLGVGSDYNedlL 237


                 ...
gi 347668599 186 QQI 188
Cdd:COG2304  238 ERL 240
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH