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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819905 136 ILILVDMSGSM-KNKLPTVKESLLDLSLSLNARMGHNQFSIFLFPGKKKDVEKLMDWNPRLESLSTI-FPKLTAGGITPT 213
Cdd:cd00198    3 IVFLLDVSGSMgGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIdALKKGLGGGTNI 82

                         90
                 ....*....|....*.
gi 502819905 214 GPAIKEATHYFTKKRS 229
Cdd:cd00198   83 GAALRLALELLKSAKR 98

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

                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 502819905   7 KQMLVITDGGSNTGE-DPVAMAALAKEQGISVNVIGV 42
Cdd:cd01467  104 RVIVLLTDGENNAGEiDPATAAELAKNKGVRIYTIGV 140

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.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502819905     2 KKGTLKQMLVITDGGSNTGEDPVAMAA-LAKEQGISVNVIGVmeedtIDEQSTNEIEGIAMSGGGV 66
Cdd:smart00327 100 RRGAPKVVILITDGESNDGPKDLLKAAkELKRSGVKVFVVGV-----GNDVDEEELKKLASAPGGV 160

von Willebrand factor type A domain;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502819905    1 MKKGTLKQMLVITDGGSNTGeDPVAMAALAKEQGISVNVIGVmeedtiDEQSTNEIEGIAMSGG 64
Cdd:pfam00092  99 ARPGAPKVVVLLTDGRSQDG-DPEEVARELKSAGVTVFAVGV------GNADDEELRKIASEPG 155

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

                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 502819905   7 KQMLVITDGGSNTGE-DPVAMAALAKEQGISVNVIGV 42
Cdd:cd01467  104 RVIVLLTDGENNAGEiDPATAAELAKNKGVRIYTIGV 140

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

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 502819905   1 MKKGTLKQMLVITDGGSNTGEDPVAMAALAKEQGISVNVIGV 42
Cdd:cd01450   99 ARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGIKVFVVGV 140

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819905   136 ILILVDMSGSM-KNKLPTVKESLLDLSLSLNARMGHNQFSIFLFPGkkkDVEKLMDWN--PRLESLSTIFPKL--TAGGI 210
Cdd:smart00327   2 VVFLLDGSGSMgGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSD---DARVLFPLNdsRSKDALLEALASLsyKLGGG 78

                           90
                   ....*....|....*....
gi 502819905   211 TPTGPAIKEATHYFTKKRS 229
Cdd:smart00327  79 TNLGAALQYALENLFSKSA 97

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502819905 134 LEILILVDMSGSMK-NKLPTVK--------ESLLDLSLSLNARMghnqfSIFLFPGkkkDVEKLMDWNPrLESLStiFPK 204
Cdd:COG4245    6 LPVYLLLDTSGSMSgEPIEALNeglqalidELRQDPYALETVEV-----SVITFDG---EAKVLLPLTD-LEDFQ--PPD 74

                         90
                 ....*....|....*...
gi 502819905 205 LTAGGITPTGPAIKEATH 222
Cdd:COG4245   75 LSASGGTPLGAALELLLD 92