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Conserved domains on  [gi|1254045078|ref|NP_001343843|]
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VWFA domain-containing protein [Caenorhabditis elegans]

Protein Classification

vWA domain-containing protein( domain architecture ID 630)

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
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 251-454 1.71e-63

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 cd01480:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 186  Bit Score: 203.39  E-value: 1.71e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 251 LPIDLMFLVDTSSSIGINNFDIQKNFICEILKD------VDIAPGRSRIAMIQYSQDPSVVFGFDQ-YYSYESVRRGVMR 323
Cdd:cd01480     1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERflkdyyRKDPAGSWRVGVVQYSDQQEVEAGFLRdIRNYTSLKEAVDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 324 LSYTGGATMLSKALAFAGGIMYHeqnlkkttkkhqylpTPKHDRLQVLCLVSDG---YSDDNADKESVNLHDHLHVKIFA 400
Cdd:cd01480    81 LEYIGGGTFTDCALKYATEQLLE---------------GSHQKENKFLLVITDGhsdGSPDGGIEKAVNEADHLGIKIFF 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1254045078 401 VVTRSFNKDKLAPITRFDGSvftVHQRESVAIWLWrqqriwaehySAFIEKEKK 454
Cdd:cd01480   146 VAVGSQNEEPLSRIACDGKS---ALYRENFAELLW----------SFFIDDETA 186
 
Name Accession Description Interval E-value
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 251-454 1.71e-63

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: 203.39  E-value: 1.71e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 251 LPIDLMFLVDTSSSIGINNFDIQKNFICEILKD------VDIAPGRSRIAMIQYSQDPSVVFGFDQ-YYSYESVRRGVMR 323
Cdd:cd01480     1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERflkdyyRKDPAGSWRVGVVQYSDQQEVEAGFLRdIRNYTSLKEAVDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 324 LSYTGGATMLSKALAFAGGIMYHeqnlkkttkkhqylpTPKHDRLQVLCLVSDG---YSDDNADKESVNLHDHLHVKIFA 400
Cdd:cd01480    81 LEYIGGGTFTDCALKYATEQLLE---------------GSHQKENKFLLVITDGhsdGSPDGGIEKAVNEADHLGIKIFF 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1254045078 401 VVTRSFNKDKLAPITRFDGSvftVHQRESVAIWLWrqqriwaehySAFIEKEKK 454
Cdd:cd01480   146 VAVGSQNEEPLSRIACDGKS---ALYRENFAELLW----------SFFIDDETA 186
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 254-424 3.46e-30

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: 115.24  E-value: 3.46e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078  254 DLMFLVDTSSSIGINNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYSYESVRRGVMRLSYT-GGATM 332
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078  333 LSKALAFAggimyhEQNLKKTTKKHQYlptpkhDRLQVLCLVSDGYSDD---NADKESVNLHDHlHVKIFAV-VTRSFNK 408
Cdd:smart00327  81 LGAALQYA------LENLFSKSAGSRR------GAPKVVILITDGESNDgpkDLLKAAKELKRS-GVKVFVVgVGNDVDE 147

                          170
                   ....*....|....*.
gi 1254045078  409 DKLAPITRFDGSVFTV 424
Cdd:smart00327 148 EELKKLASAPGGVYVF 163
VWA pfam00092
von Willebrand factor type A domain;
254-401 2.48e-23

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 96.19  E-value: 2.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 254 DLMFLVDTSSSIGINNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYSYESVRRGVMRLSY-TGGATM 332
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYlGGGTTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1254045078 333 LSKALAFAggimyhEQNLKKTTKKHqylptpKHDRLQVLCLVSDGYSDDNADKESVNLHDHLHVKIFAV 401
Cdd:pfam00092  81 TGKALKYA------LENLFSSAAGA------RPGAPKVVVLLTDGRSQDGDPEEVARELKSAGVTVFAV 137
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 193-431 7.37e-09

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: 56.49  E-value: 7.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 193 PIPSPVHNGSDGKDDATSSGTPESIESSGSDVTETTEDDLEELNRRTHLPRDHPARKLLPIDLMFLVDTSSSIGINN-FD 271
Cdd:COG1240    33 PLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 272 IQKNFICEILKDvdiAPGRSRIAMIQYSQDPSVVFGFDqyYSYESVRRGVMRLSyTGGATMLSKALAFAggimyheqnlk 351
Cdd:COG1240   113 AAKGALLDFLDD---YRPRDRVGLVAFGGEAEVLLPLT--RDREALKRALDELP-PGGGTPLGDALALA----------- 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 352 kttkkHQYLPTPKHDRLQVLCLVSDGysDDNADKES----VNLHDHLHVKIFAV--VTRSFNKDKLAPITRF-DGSVFTV 424
Cdd:COG1240   176 -----LELLKRADPARRKVIVLLTDG--RDNAGRIDpleaAELAAAAGIRIYTIgvGTEAVDEGLLREIAEAtGGRYFRA 248


                  ....*..
gi 1254045078 425 HQRESVA 431
Cdd:COG1240   249 DDLSELA 255
 
Name Accession Description Interval E-value
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 251-454 1.71e-63

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: 203.39  E-value: 1.71e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 251 LPIDLMFLVDTSSSIGINNFDIQKNFICEILKD------VDIAPGRSRIAMIQYSQDPSVVFGFDQ-YYSYESVRRGVMR 323
Cdd:cd01480     1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERflkdyyRKDPAGSWRVGVVQYSDQQEVEAGFLRdIRNYTSLKEAVDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 324 LSYTGGATMLSKALAFAGGIMYHeqnlkkttkkhqylpTPKHDRLQVLCLVSDG---YSDDNADKESVNLHDHLHVKIFA 400
Cdd:cd01480    81 LEYIGGGTFTDCALKYATEQLLE---------------GSHQKENKFLLVITDGhsdGSPDGGIEKAVNEADHLGIKIFF 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1254045078 401 VVTRSFNKDKLAPITRFDGSvftVHQRESVAIWLWrqqriwaehySAFIEKEKK 454
Cdd:cd01480   146 VAVGSQNEEPLSRIACDGKS---ALYRENFAELLW----------SFFIDDETA 186
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 253-433 5.38e-53

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: 175.49  E-value: 5.38e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 253 IDLMFLVDTSSSIGINNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYSYESVRRGVMRLSYTGGATM 332
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 333 LSKALAFAGGIMYHEQnlkkttkkhqylPTPKHDRLQVLCLVSDGYSDDNADKESVNLHDhLHVKIFAVVTRSFNKDKLA 412
Cdd:cd01472    81 TGKALKYVRENLFTEA------------SGSREGVPKVLVVITDGKSQDDVEEPAVELKQ-AGIEVFAVGVKNADEEELK 147

                         170       180
                  ....*....|....*....|.
gi 1254045078 413 PITRFDGSvftvHQRESVAIW 433
Cdd:cd01472   148 QIASDPKE----LYVFNVADF 164
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 253-415 1.01e-35

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: 129.72  E-value: 1.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 253 IDLMFLVDTSSSIGINNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYSYESVRRGVMRLSY-TGGAT 331
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYlGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 332 MLSKALAFAGGIMYHEQNLKKTTKKhqylptpkhdrlqVLCLVSDGYSDDNAD--KESVNLHDHlHVKIFAVVTRSFNKD 409
Cdd:cd01450    81 NTGKALQYALEQLFSESNARENVPK-------------VIIVLTDGRSDDGGDpkEAAAKLKDE-GIKVFVVGVGPADEE 146


                  ....*.
gi 1254045078 410 KLAPIT 415
Cdd:cd01450   147 ELREIA 152
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 254-424 3.46e-30

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: 115.24  E-value: 3.46e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078  254 DLMFLVDTSSSIGINNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYSYESVRRGVMRLSYT-GGATM 332
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078  333 LSKALAFAggimyhEQNLKKTTKKHQYlptpkhDRLQVLCLVSDGYSDD---NADKESVNLHDHlHVKIFAV-VTRSFNK 408
Cdd:smart00327  81 LGAALQYA------LENLFSKSAGSRR------GAPKVVILITDGESNDgpkDLLKAAKELKRS-GVKVFVVgVGNDVDE 147

                          170
                   ....*....|....*.
gi 1254045078  409 DKLAPITRFDGSVFTV 424
Cdd:smart00327 148 EELKKLASAPGGVYVF 163
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 254-401 8.31e-27

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: 105.45  E-value: 8.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 254 DLMFLVDTSSSIGINNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYSYESVRRGVMRLSYTGGATML 333
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1254045078 334 SKALAFAggimyHEQNLKKTTKKHQYLPtpkhdrlQVLCLVSDGYSDDNADKESVNLHDhLHVKIFAV 401
Cdd:cd01482    82 GKALTHV-----REKNFTPDAGARPGVP-------KVVILITDGKSQDDVELPARVLRN-LGVNVFAV 136
VWA pfam00092
von Willebrand factor type A domain;
254-401 2.48e-23

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 96.19  E-value: 2.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 254 DLMFLVDTSSSIGINNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYSYESVRRGVMRLSY-TGGATM 332
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYlGGGTTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1254045078 333 LSKALAFAggimyhEQNLKKTTKKHqylptpKHDRLQVLCLVSDGYSDDNADKESVNLHDHLHVKIFAV 401
Cdd:pfam00092  81 TGKALKYA------LENLFSSAAGA------RPGAPKVVVLLTDGRSQDGDPEEVARELKSAGVTVFAV 137
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 253-424 2.39e-18

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: 81.84  E-value: 2.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 253 IDLMFLVDTSSSIGINNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYSYESVRRGVMRLSYT-GGAT 331
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 332 MLSKALAFAggimyhEQNLKKTTKKHQYlptpkhdrlQVLCLVSDGYSDD---NADKESVNLHDhLHVKIFAV-VTRSFN 407
Cdd:cd00198    81 NIGAALRLA------LELLKSAKRPNAR---------RVIILLTDGEPNDgpeLLAEAARELRK-LGITVYTIgIGDDAN 144

                         170
                  ....*....|....*..
gi 1254045078 408 KDKLAPITRFDGSVFTV 424
Cdd:cd00198   145 EDELKEIADKTTGGAVF 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 254-423 4.94e-15

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: 72.43  E-value: 4.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 254 DLMFLVDTSSSIGiNNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPS--VVFGFDQYYSYESVRRGVMRLSYTGGAT 331
Cdd:cd01476     2 DLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 332 MLSKALAFAGGIMYHEQNLKKTTKKhqylptpkhdrlqVLCLVSDGYSDDNADKESVNLHDHLHVKIFAVVT---RSFNK 408
Cdd:cd01476    81 ATGAAIEVALQQLDPSEGRREGIPK-------------VVVVLTDGRSHDDPEKQARILRAVPNIETFAVGTgdpGTVDT 147

                         170
                  ....*....|....*
gi 1254045078 409 DKLAPITRFDGSVFT 423
Cdd:cd01476   148 EELHSITGNEDHIFT 162
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 253-388 8.54e-14

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: 69.31  E-value: 8.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 253 IDLMFLVDTSSSIGINNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYSYESVRRGVMRLSYTGGATM 332
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1254045078 333 LSKALAFAGGIMYHEQN--LKKTTKkhqylptpkhdrlqVLCLVSDGYSDDNADKESV 388
Cdd:cd01469    81 TATAIQYVVTELFSESNgaRKDATK--------------VLVVITDGESHDDPLLKDV 124
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 252-340 2.98e-13

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: 68.95  E-value: 2.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 252 PIDLMFLVDTSSSIGINNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYSYESVRRGVMRLSYTGGAT 331
Cdd:cd01475     2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81


                  ....*....
gi 1254045078 332 MLSKALAFA 340
Cdd:cd01475    82 MTGLAIQYA 90
VWA_2 pfam13519
von Willebrand factor type A domain;
255-352 9.46e-13

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 64.24  E-value: 9.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 255 LMFLVDTSSSI-----GINNFDIQKNFICEILKDVDiapgRSRIAMIQYSQDPSVVFGFDQyySYESVRRGVMRLSYTGG 329
Cdd:pfam13519   1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                          90       100
                  ....*....|....*....|...
gi 1254045078 330 ATMLSKALAFAGGIMYHEQNLKK 352
Cdd:pfam13519  75 GTNLAAALQLARAALKHRRKNQP 97
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 254-424 5.94e-12

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: 63.88  E-value: 5.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 254 DLMFLVDTSSSIGINNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYSYESVRRGVMRLSYTGGATM- 332
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLn 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 333 LSKALAF--------AGGIMYHEQnlkkttkkhqyLPtpkhdrlQVLCLVSDGYSDDNADKESVNLhDHLHVKIFAVVTR 404
Cdd:cd01481    82 TGSALDYvvknlftkSAGSRIEEG-----------VP-------QFLVLITGGKSQDDVERPAVAL-KRAGIVPFAIGAR 142

                         170       180
                  ....*....|....*....|.
gi 1254045078 405 SFNKDKLAPITrFDGS-VFTV 424
Cdd:cd01481   143 NADLAELQQIA-FDPSfVFQV 162
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 193-431 7.37e-09

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: 56.49  E-value: 7.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 193 PIPSPVHNGSDGKDDATSSGTPESIESSGSDVTETTEDDLEELNRRTHLPRDHPARKLLPIDLMFLVDTSSSIGINN-FD 271
Cdd:COG1240    33 PLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 272 IQKNFICEILKDvdiAPGRSRIAMIQYSQDPSVVFGFDqyYSYESVRRGVMRLSyTGGATMLSKALAFAggimyheqnlk 351
Cdd:COG1240   113 AAKGALLDFLDD---YRPRDRVGLVAFGGEAEVLLPLT--RDREALKRALDELP-PGGGTPLGDALALA----------- 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 352 kttkkHQYLPTPKHDRLQVLCLVSDGysDDNADKES----VNLHDHLHVKIFAV--VTRSFNKDKLAPITRF-DGSVFTV 424
Cdd:COG1240   176 -----LELLKRADPARRKVIVLLTDG--RDNAGRIDpleaAELAAAAGIRIYTIgvGTEAVDEGLLREIAEAtGGRYFRA 248


                  ....*..
gi 1254045078 425 HQRESVA 431
Cdd:COG1240   249 DDLSELA 255
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 253-408 3.96e-05

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: 44.30  E-value: 3.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 253 IDLMFLVDTSSSIGINN-FDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYS-----YESVRRGVMRLSY 326
Cdd:cd01471     1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNStnkdlALNAIRALLSLYY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 327 TGGATMLSKALAFAggimyhEQNLKKTTKKHQYLPtpkhdrlQVLCLVSDGYSDDNAD--KESVNLHDhLHVKI--FAV- 401
Cdd:cd01471    81 PNGSTNTTSALLVV------EKHLFDTRGNRENAP-------QLVIIMTDGIPDSKFRtlKEARKLRE-RGVIIavLGVg 146


                  ....*....
gi 1254045078 402 --VTRSFNK 408
Cdd:cd01471   147 qgVNHEENR 155
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
247-403 2.77e-03

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 38.75  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 247 ARKLLPIdlMFLVDTSSSI-GIN----NFDIQKnFICEILKDvDIAPGRSRIAMIQYSQDPSVVFGF---DQYYsyesvr 318
Cdd:COG4245     2 PMRRLPV--YLLLDTSGSMsGEPiealNEGLQA-LIDELRQD-PYALETVEVSVITFDGEAKVLLPLtdlEDFQ------ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 319 rgVMRLSyTGGATMLSKALAFAGGIMyheqnlkkTTKKHQYLPTPKHDRLQVLCLVSDGYSDDNADKESVN-LHDHLHVK 397
Cdd:COG4245    72 --PPDLS-ASGGTPLGAALELLLDLI--------ERRVQKYTAEGKGDWRPVVFLITDGEPTDSDWEAALQrLKDGEAAK 140


                  ....*.
gi 1254045078 398 IFAVVT 403
Cdd:COG4245   141 KANIFA 146
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 254-424 5.88e-03

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 37.88  E-value: 5.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 254 DLMFLVDTSSSIGINNFDIQkNFIcEILKDVDIAPGrSRIAMIQYSQDPSVVFGFDQYYSYESvrrgvmrlsytGGATML 333
Cdd:cd01474     6 DLYFVLDKSGSVAANWIEIY-DFV-EQLVDRFNSPG-LRFSFITFSTRATKILPLTDDSSAII-----------KGLEVL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045078 334 SKALafAGGIMYHEQNLKKTTKKHQYLPTPKHDRLQVLCLVSDGYSDDN----ADKESvNLHDHLHVKIFAVVTRSFNKD 409
Cdd:cd01474    72 KKVT--PSGQTYIHEGLENANEQIFNRNGGGRETVSVIIALTDGQLLLNghkyPEHEA-KLSRKLGAIVYCVGVTDFLKS 148

                         170
                  ....*....|....*
gi 1254045078 410 KLAPITRFDGSVFTV 424
Cdd:cd01474   149 QLINIADSKEYVFPV 163
 
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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