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Conserved domains on  [gi|2079609743|gb|QYU73402|]
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von Willebrand factor, partial [Crocidura orientalis lawuana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 17-98 2.86e-13

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


The actual alignment was detected with superfamily member cd01450:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 161  Bit Score: 65.39  E-value: 2.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079609743  17 LDLVFLLDGSNKLSEAEFQVLKAFVVGTMERLHISQKRIRVALVEYHDGSHAYLGLHDRKRPSELRRVASQVRYAGSDVA 96
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80


                  ..
gi 2079609743  97 ST 98
Cdd:cd01450    81 NT 82
VWA_N2 super family cl24671
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1-17 1.18e-04

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: 39.58  E-value: 1.18e-04
                          10
                  ....*....|....*..
gi 2079609743   1 EDTPEPPLHDFFCSKLL 17
Cdd:pfam16164  63 EDTPEPPLHDFYCSKLL 79
 
Name Accession Description Interval E-value
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 17-98 2.86e-13

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 65.39  E-value: 2.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079609743  17 LDLVFLLDGSNKLSEAEFQVLKAFVVGTMERLHISQKRIRVALVEYHDGSHAYLGLHDRKRPSELRRVASQVRYAGSDVA 96
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80


                  ..
gi 2079609743  97 ST 98
Cdd:cd01450    81 NT 82
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 18-99 6.08e-12

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: 62.09  E-value: 6.08e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079609743   18 DLVFLLDGSNKLSEAEFQVLKAFVVGTMERLHISQKRIRVALVEYHDGSHAYLGLHDRKRPSELRRVASQVRYAGSDVAS 97
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80


                   ..
gi 2079609743   98 TS 99
Cdd:smart00327  81 LG 82
VWA pfam00092
von Willebrand factor type A domain;
18-98 3.04e-09

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 54.59  E-value: 3.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079609743  18 DLVFLLDGSNKLSEAEFQVLKAFVVGTMERLHISQKRIRVALVEYHDGSHAYLGLHDRKRPSELRRVASQVRYAGSDVAS 97
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80


                  .
gi 2079609743  98 T 98
Cdd:pfam00092  81 T 81
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1-17 1.18e-04

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: 39.58  E-value: 1.18e-04
                          10
                  ....*....|....*..
gi 2079609743   1 EDTPEPPLHDFFCSKLL 17
Cdd:pfam16164  63 EDTPEPPLHDFYCSKLL 79
 
Name Accession Description Interval E-value
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 17-98 2.86e-13

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 65.39  E-value: 2.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079609743  17 LDLVFLLDGSNKLSEAEFQVLKAFVVGTMERLHISQKRIRVALVEYHDGSHAYLGLHDRKRPSELRRVASQVRYAGSDVA 96
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80


                  ..
gi 2079609743  97 ST 98
Cdd:cd01450    81 NT 82
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 18-99 6.08e-12

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: 62.09  E-value: 6.08e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079609743   18 DLVFLLDGSNKLSEAEFQVLKAFVVGTMERLHISQKRIRVALVEYHDGSHAYLGLHDRKRPSELRRVASQVRYAGSDVAS 97
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80


                   ..
gi 2079609743   98 TS 99
Cdd:smart00327  81 LG 82
VWA pfam00092
von Willebrand factor type A domain;
18-98 3.04e-09

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 54.59  E-value: 3.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079609743  18 DLVFLLDGSNKLSEAEFQVLKAFVVGTMERLHISQKRIRVALVEYHDGSHAYLGLHDRKRPSELRRVASQVRYAGSDVAS 97
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80


                  .
gi 2079609743  98 T 98
Cdd:pfam00092  81 T 81
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 17-90 1.48e-08

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: 53.54  E-value: 1.48e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2079609743  17 LDLVFLLDGSNKLSEAEFQVLKAFVVGTMERLHISQKRIRVALVEYHDGSHAYLGLHDRKRPSELRRVASQVRY 90
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEY 76
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 17-92 1.79e-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: 1.79e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2079609743  17 LDLVFLLDGSNKLSEAEFQVLKAFVVGTMERLHISQKRIRVALVEYHDGSHAYLGLHD-RKRPSELRRVASQVRYAG 92
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEyRTKEEPLSLVKHISQLLG 77
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 18-92 2.54e-08

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: 51.90  E-value: 2.54e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2079609743  18 DLVFLLDGSNKLSEAEFQVLKAFVVGTMERLHISQKRIRVALVEYHDGSHAYLGLHDRKRPSELRRVASQVRYAG 92
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKG 76
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 18-78 7.41e-08

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: 50.40  E-value: 7.41e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2079609743  18 DLVFLLDGSNKLSEAEFQVLKAFVVGTMERLHISQKRIRVALVEYHDGSHA--YLGLHDRKRP 78
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPefYLNTHSTKAD 64
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 18-64 8.69e-08

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: 50.30  E-value: 8.69e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2079609743  18 DLVFLLDGSNKLSEAEFQVLKAFVVGTMERLHISQKRIRVALVEYHD 64
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSD 48
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 17-93 1.86e-05

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: 43.71  E-value: 1.86e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2079609743  17 LDLVFLLDGSNKLSEAEFQVLKAFVVGTMERLHISQKRIRVALVEYHDGSHAYLGLHDRKRPSELRRVASQVRYAGS 93
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLG 77
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1-17 1.18e-04

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: 39.58  E-value: 1.18e-04
                          10
                  ....*....|....*..
gi 2079609743   1 EDTPEPPLHDFFCSKLL 17
Cdd:pfam16164  63 EDTPEPPLHDFYCSKLL 79
 
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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