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Conserved domains on  [gi|254839723|gb|ACT83450|]
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von Willebrand factor, partial [Suncus infinitesimus]

Protein Classification

vWA domain-containing protein( domain architecture ID 10646251)

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|12388743|12579041
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1-143 3.04e-17

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: 75.57  E-value: 3.04e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839723     1 MERLHISQKRIRVALVEYHDGSHAYLGLHDRKRPSELRRVASQVLYAGSEVASTSEVLKYTLFQIFSKIDRP-EAARV*L 79
Cdd:smart00327  28 VEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTNLGAALQYALENLFSKSAGSrRGAPKVV 107

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254839723    80 LLMASQEPPRLARNLVRYLQGLKKKKVAVIPVGLGPHASLKQIRLIE*QAPENRAFVLSSVDEL 143
Cdd:smart00327 108 ILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGGVYVFLPELLDLL 171
 
Name Accession Description Interval E-value
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1-143 3.04e-17

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: 75.57  E-value: 3.04e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839723     1 MERLHISQKRIRVALVEYHDGSHAYLGLHDRKRPSELRRVASQVLYAGSEVASTSEVLKYTLFQIFSKIDRP-EAARV*L 79
Cdd:smart00327  28 VEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTNLGAALQYALENLFSKSAGSrRGAPKVV 107

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254839723    80 LLMASQEPPRLARNLVRYLQGLKKKKVAVIPVGLGPHASLKQIRLIE*QAPENRAFVLSSVDEL 143
Cdd:smart00327 108 ILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGGVYVFLPELLDLL 171
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1-135 3.96e-12

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: 61.54  E-value: 3.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839723   1 MERLHISQKRIRVALVEYHDGSHAYLGLHDRKRPSELRRVASQVLYAGSEVASTSEVLKYTLFQIFSKI-DRPEAARV*L 79
Cdd:cd01450   29 VEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGTNTGKALQYALEQLFSESnARENVPKVII 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254839723  80 LLMASQ-----EPPRLARNlvrylqgLKKKKVAVIPVGLGPhASLKQIRLIE*QAPENRAF 135
Cdd:cd01450  109 VLTDGRsddggDPKEAAAK-------LKDEGIKVFVVGVGP-ADEEELREIASCPSERHVF 161
VWA pfam00092
von Willebrand factor type A domain;
1-144 2.35e-06

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 46.11  E-value: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839723    1 MERLHISQKRIRVALVEYHDGSHAYLGLHDRKRPSELRRVASQVLYAGSEVASTSEVLKYTLFQIFSKI--DRPEAARV* 78
Cdd:pfam00092  28 VESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTNTGKALKYALENLFSSAagARPGAPKVV 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839723   79 LLL----MASQEPPRLARNlvrylqgLKKKKVAVIPVGLGPhASLKQIRLIE*QAPENRAFVLSSVDELE 144
Cdd:pfam00092 108 VLLtdgrSQDGDPEEVARE-------LKSAGVTVFAVGVGN-ADDEELRKIASEPGEGHVFTVSDFEALE 169
 
Name Accession Description Interval E-value
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1-143 3.04e-17

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: 75.57  E-value: 3.04e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839723     1 MERLHISQKRIRVALVEYHDGSHAYLGLHDRKRPSELRRVASQVLYAGSEVASTSEVLKYTLFQIFSKIDRP-EAARV*L 79
Cdd:smart00327  28 VEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTNLGAALQYALENLFSKSAGSrRGAPKVV 107

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254839723    80 LLMASQEPPRLARNLVRYLQGLKKKKVAVIPVGLGPHASLKQIRLIE*QAPENRAFVLSSVDEL 143
Cdd:smart00327 108 ILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGGVYVFLPELLDLL 171
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1-135 3.96e-12

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: 61.54  E-value: 3.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839723   1 MERLHISQKRIRVALVEYHDGSHAYLGLHDRKRPSELRRVASQVLYAGSEVASTSEVLKYTLFQIFSKI-DRPEAARV*L 79
Cdd:cd01450   29 VEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGTNTGKALQYALEQLFSESnARENVPKVII 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254839723  80 LLMASQ-----EPPRLARNlvrylqgLKKKKVAVIPVGLGPhASLKQIRLIE*QAPENRAF 135
Cdd:cd01450  109 VLTDGRsddggDPKEAAAK-------LKDEGIKVFVVGVGP-ADEEELREIASCPSERHVF 161
VWA pfam00092
von Willebrand factor type A domain;
1-144 2.35e-06

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 46.11  E-value: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839723    1 MERLHISQKRIRVALVEYHDGSHAYLGLHDRKRPSELRRVASQVLYAGSEVASTSEVLKYTLFQIFSKI--DRPEAARV* 78
Cdd:pfam00092  28 VESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTNTGKALKYALENLFSSAagARPGAPKVV 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839723   79 LLL----MASQEPPRLARNlvrylqgLKKKKVAVIPVGLGPhASLKQIRLIE*QAPENRAFVLSSVDELE 144
Cdd:pfam00092 108 VLLtdgrSQDGDPEEVARE-------LKSAGVTVFAVGVGN-ADDEELRKIASEPGEGHVFTVSDFEALE 169
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1-135 3.15e-06

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: 45.63  E-value: 3.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839723   1 MERLHISQKRIRVALVEYHDGSHAYLGLHDRKRPSELRRVASQVLYAGSEVASTSEVLKYTLfQIFSKIDRPEAARV*LL 80
Cdd:cd00198   29 VSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGTNIGAALRLAL-ELLKSAKRPNARRV-II 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 254839723  81 LMASQEPPRLARNLVRYLQGLKKKKVAVIPVGLGPHASLKQIRLIE*QAPENRAF 135
Cdd:cd00198  107 LLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIADKTTGGAVF 161
 
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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