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Conserved domains on  [gi|2460609916|gb|WEQ50486|]
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von Willebrand Factor, partial [Microtus ochrogaster]

Protein Classification

vWA domain-containing protein( domain architecture ID 10442343)

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

CATH:  3.40.50.410
PubMed:  10830113|12579041|12388743
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWA pfam00092
von Willebrand factor type A domain;
5-165 2.25e-45

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 147.04  E-value: 2.25e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916   5 DVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQQGIHISVLQYSYKVTVEYTFNEAQTKDDVLRHVREIRYHGGNRTN 84
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916  85 TAQALQYLSEHSFSPSQGDRKQAPNLVYMVT-GNP-------ASDEIKRmpGDIQVVPIGVGPhANPQELERIGWPHAPI 156
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSqdgdpeeVARELKS--AGVTVFAVGVGN-ADDEELRKIASEPGEG 157

                         170
                  ....*....|..
gi 2460609916 157 FI---RDFETLP 165
Cdd:pfam00092 158 HVftvSDFEALE 169
 
Name Accession Description Interval E-value
VWA pfam00092
von Willebrand factor type A domain;
5-165 2.25e-45

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 147.04  E-value: 2.25e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916   5 DVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQQGIHISVLQYSYKVTVEYTFNEAQTKDDVLRHVREIRYHGGNRTN 84
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916  85 TAQALQYLSEHSFSPSQGDRKQAPNLVYMVT-GNP-------ASDEIKRmpGDIQVVPIGVGPhANPQELERIGWPHAPI 156
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSqdgdpeeVARELKS--AGVTVFAVGVGN-ADDEELRKIASEPGEG 157

                         170
                  ....*....|..
gi 2460609916 157 FI---RDFETLP 165
Cdd:pfam00092 158 HVftvSDFEALE 169
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 4-155 9.83e-42

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: 137.42  E-value: 9.83e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916   4 LDVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQQGIHISVLQYSYKVTVEYTFNEAQTKDDVLRHVREIRYHGGNRT 83
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916  84 NTAQALQYLSEHSFSPSQgDRKQAPNLVYMVT-GNP--------ASDEIKRMpgDIQVVPIGVGPhANPQELERIGWPHA 154
Cdd:cd01450    81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTdGRSddggdpkeAAAKLKDE--GIKVFVVGVGP-ADEEELREIASCPS 156


                  .
gi 2460609916 155 P 155
Cdd:cd01450   157 E 157
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 5-149 4.25e-40

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: 133.73  E-value: 4.25e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916    5 DVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQQGIHISVLQYSYKVTVEYTFNEAQTKDDVLRHVREIRYHGGNRTN 84
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2460609916   85 TAQALQYLSEHSFSPSQGDRKQAPNLVYMVT-GNP---------ASDEIKRMPgdIQVVPIGVGPHANPQELERI 149
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITdGESndgpkdllkAAKELKRSG--VKVFVVGVGNDVDEEELKKL 153
 
Name Accession Description Interval E-value
VWA pfam00092
von Willebrand factor type A domain;
5-165 2.25e-45

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 147.04  E-value: 2.25e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916   5 DVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQQGIHISVLQYSYKVTVEYTFNEAQTKDDVLRHVREIRYHGGNRTN 84
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916  85 TAQALQYLSEHSFSPSQGDRKQAPNLVYMVT-GNP-------ASDEIKRmpGDIQVVPIGVGPhANPQELERIGWPHAPI 156
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTdGRSqdgdpeeVARELKS--AGVTVFAVGVGN-ADDEELRKIASEPGEG 157

                         170
                  ....*....|..
gi 2460609916 157 FI---RDFETLP 165
Cdd:pfam00092 158 HVftvSDFEALE 169
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 4-155 9.83e-42

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: 137.42  E-value: 9.83e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916   4 LDVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQQGIHISVLQYSYKVTVEYTFNEAQTKDDVLRHVREIRYHGGNRT 83
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916  84 NTAQALQYLSEHSFSPSQgDRKQAPNLVYMVT-GNP--------ASDEIKRMpgDIQVVPIGVGPhANPQELERIGWPHA 154
Cdd:cd01450    81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTdGRSddggdpkeAAAKLKDE--GIKVFVVGVGP-ADEEELREIASCPS 156


                  .
gi 2460609916 155 P 155
Cdd:cd01450   157 E 157
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 5-149 4.25e-40

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: 133.73  E-value: 4.25e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916    5 DVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQQGIHISVLQYSYKVTVEYTFNEAQTKDDVLRHVREIRYHGGNRTN 84
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2460609916   85 TAQALQYLSEHSFSPSQGDRKQAPNLVYMVT-GNP---------ASDEIKRMPgdIQVVPIGVGPHANPQELERI 149
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITdGESndgpkdllkAAKELKRSG--VKVFVVGVGNDVDEEELKKL 153
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 5-149 1.21e-39

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: 131.97  E-value: 1.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916   5 DVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQQGIHISVLQYSYKVTVEYTFNEAQTKDDVLRHVREIRYHGGNrTN 84
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGG-TN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916  85 TAQALQYLSEHSFSPSQGDRKQAPNLVYMVTGNPASDEIKRMPG-----DIQVVPIGVGPhANPQELERI 149
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 ...
 5-150 4.29e-35

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: 120.47  E-value: 4.29e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916   5 DVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQQGIHISVLQYSYKVTVEYTFNEAQTKDDVLRHVREIRYHGGNrTN 84
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGN-TR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2460609916  85 TAQALQYLSEHSFSPSQGDRKQAPNLVYMVTGNPASDEIkRMPGD------IQVVPIGVGpHANPQELERIG 150
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDV-ELPARvlrnlgVNVFAVGVK-DADESELKMIA 150
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 5-158 1.61e-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: 116.27  E-value: 1.61e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916   5 DVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQQGIHISVLQYSYKVTVEYTFNEAQTKDDVLRHVREIRYHGGNRTN 84
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916  85 TAQALQYLSEHSFSPSQGDR--KQAPNLVYMVTGNPASDEIKRMPGDIQ---VVPIGVGP-HANPQELERIGwpHAPIFI 158
Cdd:cd01481    82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKragIVPFAIGArNADLAELQQIA--FDPSFV 159
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 4-148 9.09e-26

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: 97.04  E-value: 9.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916   4 LDVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQQGIHISVLQYSYKVTVEYTFNEAQTKDDVLRHVREIRYHGGnRT 83
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLG-LT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2460609916  84 NTAQALQYLSEHSFSPSQGDRKQAPNLVYMVT-----GNPASDEIKRMP--GDIQVVPIGVGPHANPQELER 148
Cdd:cd01469    80 NTATAIQYVVTELFSESNGARKDATKVLVVITdgeshDDPLLKDVIPQAerEGIIRYAIGVGGHFQRENSRE 151
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 4-149 2.92e-25

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: 2.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916   4 LDVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQQGIHISVLQYSYKVTVEYTFNEAQTKDDVLRHVREIRYHGGNRT 83
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2460609916  84 NTAQALQYLSEHSFSPsqgDRKQAPNLVYMVT-GNP---------ASDEIKRMpgDIQVVPIGVGPHANPQELERI 149
Cdd:cd00198    81 NIGAALRLALELLKSA---KRPNARRVIILLTdGEPndgpellaeAARELRKL--GITVYTIGIGDDANEDELKEI 151
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 4-150 7.53e-24

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: 93.22  E-value: 7.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916   4 LDVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQQGIHISVLQYSYKVTVEYTFNEAQTKDDVLRHVREIRYHGGNrT 83
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG-T 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2460609916  84 NTAQALQYLSEHSFSPSQGDRKQAPNL---VYMVTGNPASDEIK------RMPGdIQVVPIGVGpHANPQELERIG 150
Cdd:cd01475    82 MTGLAIQYAMNNAFSEAEGARPGSERVprvGIVVTDGRPQDDVSevaakaRALG-IEMFAVGVG-RADEEELREIA 155
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 4-145 7.66e-20

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: 81.66  E-value: 7.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916   4 LDVVFVLEGSDEIGEAN-FNKSKEFLEEVIQRMDVGQQGIHISVLQYSYKVTVEYTFNE--AQTKD---DVLRHVREIRY 77
Cdd:cd01471     1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpnSTNKDlalNAIRALLSLYY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2460609916  78 HGGNrTNTAQALQYLSEHSFSpSQGDRKQAPNLVYMVT-GNPASD--------EIKRMPGDIQVvpIGVGPHANPQE 145
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 ...
 4-150 2.99e-17

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: 74.36  E-value: 2.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916   4 LDVVFVLEGSDEIGEAnFNKSKEFLEEVIQRMDVGQQGIHISVLQYS--YKVTVEYTFNEAQTKDDVLRHVREIRYHGGN 81
Cdd:cd01476     1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2460609916  82 rTNTAQALQYLSEHsFSPSQGDRKQAPNLVYMVTGNPASDEIKRM-------PGdIQVVPIGVGPHANP--QELERIG 150
Cdd:cd01476    80 -TATGAAIEVALQQ-LDPSEGRREGIPKVVVVLTDGRSHDDPEKQarilravPN-IETFAVGTGDPGTVdtEELHSIT 154
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 4-106 3.30e-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: 56.24  E-value: 3.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916   4 LDVVFVLEGSDEIGEANFNKSKEFLEEVIQRM------DVGQQGIHISVLQYSYKVTVEYTFNEAQTKDDVLRH-VREIR 76
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTSLKEaVDNLE 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 2460609916  77 YHGGNrTNTAQALQYLSEHSFSPSQGDRKQ 106
Cdd:cd01480    83 YIGGG-TFTDCALKYATEQLLEGSHQKENK 111
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 4-95 1.11e-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: 49.21  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916   4 LDVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQQGIHISVLQYSYKVTVE---YTFNEAQtKDDVLRHVREIRY--H 78
Cdd:cd01470     1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIvsiRDFNSND-ADDVIKRLEDFNYddH 79

                          90
                  ....*....|....*...
gi 2460609916  79 GGNR-TNTAQALQYLSEH 95
Cdd:cd01470    80 GDKTgTNTAAALKKVYER 97
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 5-127 6.58e-07

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: 47.31  E-value: 6.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916   5 DVVFVLEGSDEIGEANFNKS-KEFLEEVIQRMDVGQQGIHISVLQYSYKVTVEYTF--NEAQTKDDVLRHVREIR--YHG 79
Cdd:cd01473     2 DLTLILDESASIGYSNWRKDvIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFsdEERYDKNELLKKINDLKnsYRS 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2460609916  80 GNRTNTAQALQYlSEHSFSPSQGDRKQAPNLVYMVT-GNPASDEIKRMP 127
Cdd:cd01473    82 GGETYIVEALKY-GLKNYTKHGNRRKDAPKVTMLFTdGNDTSASKKELQ 129
VWA_2 pfam13519
von Willebrand factor type A domain;
6-114 1.22e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 44.98  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2460609916   6 VVFVLEGS-----DEIGEANFNKSKEFLEEVIQRMDvgqqGIHISVLQYSYKVTVEYTFNeaQTKDDVLRHVREIRYHGG 80
Cdd:pfam13519   1 LVFVLDTSgsmrnGDYGPTRLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2460609916  81 NrTNTAQALQYLSEHsfspSQGDRKQAPNLVYMV 114
Cdd:pfam13519  75 G-TNLAAALQLARAA----LKHRRKNQPRRIVLI 103
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 4-68 7.44e-03

VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. The members of this subgroup lack the MIDAS motif. This subgroup is found only in C. elegans and the members identified thus far are always found fused to a C-Lectin type domain. Biochemical function thus far has not be attributed to any of the members of this subgroup.


Pssm-ID: 238754 [Multi-domain]  Cd Length: 193  Bit Score: 35.48  E-value: 7.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2460609916   4 LDVVFVLEGSDEIGEANFNKSKEFLEEVIQRMDVGQQG------IHISVLQYSYKVTVEYTFNEAQTKDDV 68
Cdd:cd01477    20 LDIVFVVDNSKGMTQGGLWQVRATISSLFGSSSQIGTDyddprsTRVGLVTYNSNATVVADLNDLQSFDDL 90
 
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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