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Conserved domains on  [gi|71984760|ref|NP_001023671|]
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VWFA domain-containing protein [Caenorhabditis elegans]

Protein Classification

VWA domain-containing protein( domain architecture ID 10442346)

VWA (von Willebrand factor type A) domain-containing protein

PubMed:  10830113|12579041

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWA pfam00092
von Willebrand factor type A domain;
35-185 6.00e-26

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 103.12  E-value: 6.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760    35 DIVIVVDASNAYDQVTFEQIRTFLLNFVSSLTVSPLDSQVALYAYGSSAQTVASLNDGSSLGSIQAKINtTLKYQGSAER 114
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVD-NLRYLGGGTT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71984760   115 NLFQALTKVQAEV-SSMSGMRSGDYKKVLVILSGDSWTGNtvigSSVLTQLKQKFNV-IMSVGFGAKALANLN 185
Cdd:pfam00092  80 NTGKALKYALENLfSSAAGARPGAPKVVVLLTDGRSQDGD----PEEVARELKSAGVtVFAVGVGNADDEELR 148
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 250-409 2.20e-17

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: 78.87  E-value: 2.20e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760 250 YDVYLIVDVSNKASAADFAAMKTAIHNFVAPFAIGDLGTSFALVTTGiDSQLFFTNFKNGQSRGDVLTAVDGLLQDDVPG 329
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYS-DDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760 330 QTLNLALSAIQGYLAQPTSAS---KKIMAYFTSTTAWD-VSPISTMNSLKSKY-SLSPVAVqwgASASTSDLTNLVGGAN 404
Cdd:cd01450  80 TNTGKALQYALEQLFSESNARenvPKVIIVLTDGRSDDgGDPKEAAAKLKDEGiKVFVVGV---GPADEEELREIASCPS 156


                ....*
gi 71984760 405 CVNVV 409
Cdd:cd01450 157 ERHVF 161
 
Name Accession Description Interval E-value
VWA pfam00092
von Willebrand factor type A domain;
35-185 6.00e-26

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 103.12  E-value: 6.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760    35 DIVIVVDASNAYDQVTFEQIRTFLLNFVSSLTVSPLDSQVALYAYGSSAQTVASLNDGSSLGSIQAKINtTLKYQGSAER 114
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVD-NLRYLGGGTT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71984760   115 NLFQALTKVQAEV-SSMSGMRSGDYKKVLVILSGDSWTGNtvigSSVLTQLKQKFNV-IMSVGFGAKALANLN 185
Cdd:pfam00092  80 NTGKALKYALENLfSSAAGARPGAPKVVVLLTDGRSQDGD----PEEVARELKSAGVtVFAVGVGNADDEELR 148
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 35-186 6.95e-23

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: 94.28  E-value: 6.95e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760  35 DIVIVVDASNAYDQVTFEQIRTFLLNFVSSLTVSPLDSQVALYAYGSSAQTVASLNDGSSLGSIQAKINtTLKYQGSAER 114
Cdd:cd01450   2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVK-NLKYLGGGGT 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71984760 115 NLFQALTKVQAEVSSMSGMRSGDYKKVLVILSGDSWTGNTVIGSSVltQLKQKFNVIMSVGFGAKALANLNS 186
Cdd:cd01450  81 NTGKALQYALEQLFSESNARENVPKVIIVLTDGRSDDGGDPKEAAA--KLKDEGIKVFVVGVGPADEEELRE 150
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 35-191 6.73e-22

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: 92.13  E-value: 6.73e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760     35 DIVIVVDASNAYDQVTFEQIRTFLLNFVSSLTVSPLDSQVALYAYGSSAQTVASLNDGSSLGSIQAKINtTLKYQGSAER 114
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALA-SLSYKLGGGT 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71984760    115 NLFQALTKVQAEV-SSMSGMRSGDYKKVLVILSGDSWTGNTVIGSSVLTQLKQKFNVImSVGFGAkalANLNSQLPQI 191
Cdd:smart00327  80 NLGAALQYALENLfSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVF-VVGVGN---DVDEEELKKL 153
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 250-409 2.20e-17

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: 78.87  E-value: 2.20e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760 250 YDVYLIVDVSNKASAADFAAMKTAIHNFVAPFAIGDLGTSFALVTTGiDSQLFFTNFKNGQSRGDVLTAVDGLLQDDVPG 329
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYS-DDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760 330 QTLNLALSAIQGYLAQPTSAS---KKIMAYFTSTTAWD-VSPISTMNSLKSKY-SLSPVAVqwgASASTSDLTNLVGGAN 404
Cdd:cd01450  80 TNTGKALQYALEQLFSESNARenvPKVIIVLTDGRSDDgGDPKEAAAKLKDEGiKVFVVGV---GPADEEELREIASCPS 156


                ....*
gi 71984760 405 CVNVV 409
Cdd:cd01450 157 ERHVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 251-415 6.28e-15

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: 72.49  E-value: 6.28e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760    251 DVYLIVDVSNKASAADFAAMKTAIHNFVAPFAIGDLGTSFALVTTGIDSQLFFtNFKNGQSRGDVLTAVDGLLQDDVPGQ 330
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLF-PLNDSRSKDALLEALASLSYKLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760    331 TLNLALSAIQGYLAQPTSAS----KKIMAYFTSTTAWD-VSPISTMNSLKSKYSLSPVAVQWGASASTSDLTNLVGGANC 405
Cdd:smart00327  80 NLGAALQYALENLFSKSAGSrrgaPKVVILITDGESNDgPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                          170
                   ....*....|
gi 71984760    406 VNVVSNKAAS 415
Cdd:smart00327 160 VYVFLPELLD 169
VWA pfam00092
von Willebrand factor type A domain;
251-386 7.64e-09

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 54.97  E-value: 7.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760   251 DVYLIVDVSNKASAADFAAMKTAIHNFVAPFAIGDLGTSFALVTTGIDSQLFFtNFKNGQSRGDVLTAVDGLLQDDVPGQ 330
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEF-PLNDYSSKEELLSAVDNLRYLGGGTT 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71984760   331 TLNLALSAIQGYLAQPTSAS----KKIMAYFTSTTAWDVSPISTMNSLKS-KYSLSPVAVQ 386
Cdd:pfam00092  80 NTGKALKYALENLFSSAAGArpgaPKVVVLLTDGRSQDGDPEEVARELKSaGVTVFAVGVG 140
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 35-181 5.35e-03

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 38.38  E-value: 5.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760  35 DIVIVVDAS---NAYDQvtFEQIRTFLLNFVSSLtvsPLDSQVALYAYGSSAQTVASLndGSSLGSIQAKINtTLKYQGS 111
Cdd:COG1240  94 DVVLVVDASgsmAAENR--LEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPL--TRDREALKRALD-ELPPGGG 165

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71984760 112 AerNLFQALTKVQAEVSSmsgmRSGDYKKVLVILS-GDswtgNTVIGSSVLTQLK--QKFNV-IMSVGFGAKAL 181
Cdd:COG1240 166 T--PLGDALALALELLKR----ADPARRKVIVLLTdGR----DNAGRIDPLEAAElaAAAGIrIYTIGVGTEAV 229
 
Name Accession Description Interval E-value
VWA pfam00092
von Willebrand factor type A domain;
35-185 6.00e-26

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 103.12  E-value: 6.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760    35 DIVIVVDASNAYDQVTFEQIRTFLLNFVSSLTVSPLDSQVALYAYGSSAQTVASLNDGSSLGSIQAKINtTLKYQGSAER 114
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVD-NLRYLGGGTT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71984760   115 NLFQALTKVQAEV-SSMSGMRSGDYKKVLVILSGDSWTGNtvigSSVLTQLKQKFNV-IMSVGFGAKALANLN 185
Cdd:pfam00092  80 NTGKALKYALENLfSSAAGARPGAPKVVVLLTDGRSQDGD----PEEVARELKSAGVtVFAVGVGNADDEELR 148
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 35-186 6.95e-23

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: 94.28  E-value: 6.95e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760  35 DIVIVVDASNAYDQVTFEQIRTFLLNFVSSLTVSPLDSQVALYAYGSSAQTVASLNDGSSLGSIQAKINtTLKYQGSAER 114
Cdd:cd01450   2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVK-NLKYLGGGGT 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71984760 115 NLFQALTKVQAEVSSMSGMRSGDYKKVLVILSGDSWTGNTVIGSSVltQLKQKFNVIMSVGFGAKALANLNS 186
Cdd:cd01450  81 NTGKALQYALEQLFSESNARENVPKVIIVLTDGRSDDGGDPKEAAA--KLKDEGIKVFVVGVGPADEEELRE 150
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 35-191 6.73e-22

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: 92.13  E-value: 6.73e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760     35 DIVIVVDASNAYDQVTFEQIRTFLLNFVSSLTVSPLDSQVALYAYGSSAQTVASLNDGSSLGSIQAKINtTLKYQGSAER 114
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALA-SLSYKLGGGT 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71984760    115 NLFQALTKVQAEV-SSMSGMRSGDYKKVLVILSGDSWTGNTVIGSSVLTQLKQKFNVImSVGFGAkalANLNSQLPQI 191
Cdd:smart00327  80 NLGAALQYALENLfSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVF-VVGVGN---DVDEEELKKL 153
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 250-409 2.20e-17

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: 78.87  E-value: 2.20e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760 250 YDVYLIVDVSNKASAADFAAMKTAIHNFVAPFAIGDLGTSFALVTTGiDSQLFFTNFKNGQSRGDVLTAVDGLLQDDVPG 329
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYS-DDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760 330 QTLNLALSAIQGYLAQPTSAS---KKIMAYFTSTTAWD-VSPISTMNSLKSKY-SLSPVAVqwgASASTSDLTNLVGGAN 404
Cdd:cd01450  80 TNTGKALQYALEQLFSESNARenvPKVIIVLTDGRSDDgGDPKEAAAKLKDEGiKVFVVGV---GPADEEELREIASCPS 156


                ....*
gi 71984760 405 CVNVV 409
Cdd:cd01450 157 ERHVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 251-415 6.28e-15

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: 72.49  E-value: 6.28e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760    251 DVYLIVDVSNKASAADFAAMKTAIHNFVAPFAIGDLGTSFALVTTGIDSQLFFtNFKNGQSRGDVLTAVDGLLQDDVPGQ 330
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLF-PLNDSRSKDALLEALASLSYKLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760    331 TLNLALSAIQGYLAQPTSAS----KKIMAYFTSTTAWD-VSPISTMNSLKSKYSLSPVAVQWGASASTSDLTNLVGGANC 405
Cdd:smart00327  80 NLGAALQYALENLFSKSAGSrrgaPKVVILITDGESNDgPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                          170
                   ....*....|
gi 71984760    406 VNVVSNKAAS 415
Cdd:smart00327 160 VYVFLPELLD 169
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 35-180 2.43e-14

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: 70.29  E-value: 2.43e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760  35 DIVIVVDASNAYDQVTFEQIRTFLLNFVSSLTVSPLDSQVALYAYGSSAQTVASLNDGSSLGSIQAKINtTLKYQGSAER 114
Cdd:cd00198   2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAID-ALKKGLGGGT 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71984760 115 NLFQALTKVQAEVSSmsgMRSGDYKKVLVILSGDSWTGNTVIGSSVLTQLKQKFNVIMSVGFGAKA 180
Cdd:cd00198  81 NIGAALRLALELLKS---AKRPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDA 143
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 34-156 4.85e-12

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: 64.30  E-value: 4.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760  34 SDIVIVVDASNAYDQVTFEQIRTFLLNFVSSLTVSPLDSQVALYAYGSSAQTVASLNDGSSLGSIQAKINTTLKYQGSAe 113
Cdd:cd01469   1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLT- 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 71984760 114 rNLFQALTKVQAEVSSMS-GMRSgDYKKVLVIL----SGDSWTGNTVI 156
Cdd:cd01469  80 -NTATAIQYVVTELFSESnGARK-DATKVLVVItdgeSHDDPLLKDVI 125
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 35-191 1.49e-10

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: 59.55  E-value: 1.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760  35 DIVIVVDASNAYDQVTFEQIRTFLLNFVSSLTVSPLDSQVALYAYGSSAQTVASLNDGSSLGSIQAKINtTLKYQGSAEr 114
Cdd:cd01472   2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVK-NLRYIGGGT- 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71984760 115 NLFQALTKVQAEV-SSMSGMRSGdYKKVLVILSgDSWTGNTVIGSSVltQLKQKFNVIMSVGFGakalANLNSQLPQI 191
Cdd:cd01472  80 NTGKALKYVRENLfTEASGSREG-VPKVLVVIT-DGKSQDDVEEPAV--ELKQAGIEVFAVGVK----NADEEELKQI 149
VWA pfam00092
von Willebrand factor type A domain;
251-386 7.64e-09

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 54.97  E-value: 7.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760   251 DVYLIVDVSNKASAADFAAMKTAIHNFVAPFAIGDLGTSFALVTTGIDSQLFFtNFKNGQSRGDVLTAVDGLLQDDVPGQ 330
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEF-PLNDYSSKEELLSAVDNLRYLGGGTT 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71984760   331 TLNLALSAIQGYLAQPTSAS----KKIMAYFTSTTAWDVSPISTMNSLKS-KYSLSPVAVQ 386
Cdd:pfam00092  80 NTGKALKYALENLFSSAAGArpgaPKVVVLLTDGRSQDGDPEEVARELKSaGVTVFAVGVG 140
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 35-149 5.53e-07

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: 49.21  E-value: 5.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760  35 DIVIVVDASNAYDQVTFEQIRTFLLNFVSSLTVSPLDSQVALYAYGSSAQTVASLNDGSSLGSIQAKINtTLKYQGSAER 114
Cdd:cd01482   2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIK-NLPYKGGNTR 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 71984760 115 NlFQALTKVQAEV-SSMSGMRSGDYKKVLVILSGDS 149
Cdd:cd01482  81 T-GKALTHVREKNfTPDAGARPGVPKVVILITDGKS 115
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 35-191 1.17e-06

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: 48.09  E-value: 1.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760  35 DIVIVVDASNAYDQVTFEQIRTFLLNFVSSLTVSPLDSQVALYAYGSSAQTVASLNDGSSLGSIQAKINtTLKYQGSAER 114
Cdd:cd01481   2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVR-RLRLRGGSQL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760 115 NLFQALTKVQAEV---SSMSGMRSGdYKKVLVILSGDSWTGNTVIGSSVLTQlkqkfNVIMSVGFGAKAlANLNsQLPQI 191
Cdd:cd01481  81 NTGSALDYVVKNLftkSAGSRIEEG-VPQFLVLITGGKSQDDVERPAVALKR-----AGIVPFAIGARN-ADLA-ELQQI 152
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 250-409 3.95e-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: 46.79  E-value: 3.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760 250 YDVYLIVDVSNKASAADFAAMKTAIHNFVAPFAIGDLGTSFALVTTGiDSQLFFTNFKNGQSRGDVLTAVDGLLQDDVPG 329
Cdd:cd00198   1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFG-SNARVVLPLTTDTDKADLLEAIDALKKGLGGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760 330 QTLNLALS-AIQGYLAQPTSASKKIMAYFTS--TTAWDVSPISTMNSLKS-KYSLSPVAVqwGASASTSDLTNLVGGANC 405
Cdd:cd00198  80 TNIGAALRlALELLKSAKRPNARRVIILLTDgePNDGPELLAEAARELRKlGITVYTIGI--GDDANEDELKEIADKTTG 157


                ....
gi 71984760 406 VNVV 409
Cdd:cd00198 158 GAVF 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 34-151 4.28e-06

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: 46.62  E-value: 4.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760  34 SDIVIVVDASNAYDQVtFEQIRTFLLNFVSSLTVSPLDSQVALYAYGSSAQTVASLNDGSSL--GSIQAKINTTLKYQGS 111
Cdd:cd01476   1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQRVRFNLPKHNdgEELLEKVDNLRFIGGT 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 71984760 112 AERNlfQALTKVQAEVSSMSGMRSGdYKKVLVILSgDSWT 151
Cdd:cd01476  80 TATG--AAIEVALQQLDPSEGRREG-IPKVVVVLT-DGRS 115
VWA_2 pfam13519
von Willebrand factor type A domain;
36-145 5.15e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 44.98  E-value: 5.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760    36 IVIVVDASN-----AYDQVTFEQIRTFLLNFVSSLTvsplDSQVALYAYGSSAQTVASLNDGssLGSIQAKINTTLKYQG 110
Cdd:pfam13519   1 LVFVLDTSGsmrngDYGPTRLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLTKD--RAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 71984760   111 saERNLFQALTKVQAEVSSmsgmRSGDYKKVLVIL 145
Cdd:pfam13519  75 --GTNLAAALQLARAALKH----RRKNQPRRIVLI 103
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 35-89 7.31e-06

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: 46.99  E-value: 7.31e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71984760  35 DIVIVVDASNAYDQVTFEQIRTFLLNFVSSLTVSPLDSQVALYAYGSSAQTVASL 89
Cdd:cd01475   4 DLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPL 58
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 251-324 4.21e-03

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: 38.11  E-value: 4.21e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71984760 251 DVYLIVDVSNKASAADFAAMKTAIHNFVAPFAIGDLGTSFALVTTGIDSQLFFtNFKNGQSRGDVLTAVDGLLQ 324
Cdd:cd01469   2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEF-TLNEYRTKEEPLSLVKHISQ 74
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 35-181 5.35e-03

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 38.38  E-value: 5.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984760  35 DIVIVVDAS---NAYDQvtFEQIRTFLLNFVSSLtvsPLDSQVALYAYGSSAQTVASLndGSSLGSIQAKINtTLKYQGS 111
Cdd:COG1240  94 DVVLVVDASgsmAAENR--LEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPL--TRDREALKRALD-ELPPGGG 165

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71984760 112 AerNLFQALTKVQAEVSSmsgmRSGDYKKVLVILS-GDswtgNTVIGSSVLTQLK--QKFNV-IMSVGFGAKAL 181
Cdd:COG1240 166 T--PLGDALALALELLKR----ADPARRKVIVLLTdGR----DNAGRIDPLEAAElaAAAGIrIYTIGVGTEAV 229
 
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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