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Conserved domains on  [gi|17560426|ref|NP_504602|]
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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 ...
 481-684 1.20e-61

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: 203.77  E-value: 1.20e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 481 LPIDLMFLVDTSSSIGINNFDIQKNFICEILKD------VDIAPGRSRIAMIQYSQDPSVVFGFDQ-YYSYESVRRGVMR 553
Cdd:cd01480   1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERflkdyyRKDPAGSWRVGVVQYSDQQEVEAGFLRdIRNYTSLKEAVDN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 554 LSYTGGATMLSKALAFAGGIMYHeqnlkkttkkhqylpTPKHDRLQVLCLVSDG---YSDDNADKESVNLHDHLHVKIFA 630
Cdd:cd01480  81 LEYIGGGTFTDCALKYATEQLLE---------------GSHQKENKFLLVITDGhsdGSPDGGIEKAVNEADHLGIKIFF 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17560426 631 VVTRSFNKDKLAPITRFDGSvftVHQRESVAIWLWrqqriwaehySAFIEKEKK 684
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 ...
 481-684 1.20e-61

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: 203.77  E-value: 1.20e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 481 LPIDLMFLVDTSSSIGINNFDIQKNFICEILKD------VDIAPGRSRIAMIQYSQDPSVVFGFDQ-YYSYESVRRGVMR 553
Cdd:cd01480   1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERflkdyyRKDPAGSWRVGVVQYSDQQEVEAGFLRdIRNYTSLKEAVDN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 554 LSYTGGATMLSKALAFAGGIMYHeqnlkkttkkhqylpTPKHDRLQVLCLVSDG---YSDDNADKESVNLHDHLHVKIFA 630
Cdd:cd01480  81 LEYIGGGTFTDCALKYATEQLLE---------------GSHQKENKFLLVITDGhsdGSPDGGIEKAVNEADHLGIKIFF 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17560426 631 VVTRSFNKDKLAPITRFDGSvftVHQRESVAIWLWrqqriwaehySAFIEKEKK 684
Cdd:cd01480 146 VAVGSQNEEPLSRIACDGKS---ALYRENFAELLW----------SFFIDDETA 186
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 484-654 1.46e-29

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: 1.46e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426    484 DLMFLVDTSSSIGINNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYSYESVRRGVMRLSYT-GGATM 562
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426    563 LSKALAFAggimyhEQNLKKTTKKHQYlptpkhDRLQVLCLVSDGYSDD---NADKESVNLHDHlHVKIFAV-VTRSFNK 638
Cdd:smart00327  81 LGAALQYA------LENLFSKSAGSRR------GAPKVVILITDGESNDgpkDLLKAAKELKRS-GVKVFVVgVGNDVDE 147

                          170
                   ....*....|....*.
gi 17560426    639 DKLAPITRFDGSVFTV 654
Cdd:smart00327 148 EELKKLASAPGGVYVF 163
VWA pfam00092
von Willebrand factor type A domain;
484-631 5.69e-23

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 96.19  E-value: 5.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426   484 DLMFLVDTSSSIGINNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYSYESVRRGVMRLSY-TGGATM 562
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYlGGGTTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17560426   563 LSKALAFAggimyhEQNLKKTTKKHqylptpKHDRLQVLCLVSDGYSDDNADKESVNLHDHLHVKIFAV 631
Cdd:pfam00092  81 TGKALKYA------LENLFSSAAGA------RPGAPKVVVLLTDGRSQDGDPEEVARELKSAGVTVFAV 137
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 423-661 1.30e-08

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: 1.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 423 PIPSPVHNGSDGKDDATSSGTPESIESSGSDVTETTEDDLEELNRRTHLPRDHPARKLLPIDLMFLVDTSSSIGINN-FD 501
Cdd:COG1240  33 PLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLE 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 502 IQKNFICEILKDvdiAPGRSRIAMIQYSQDPSVVFGFDqyYSYESVRRGVMRLSyTGGATMLSKALAFAggimyheqnlk 581
Cdd:COG1240 113 AAKGALLDFLDD---YRPRDRVGLVAFGGEAEVLLPLT--RDREALKRALDELP-PGGGTPLGDALALA----------- 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 582 kttkkHQYLPTPKHDRLQVLCLVSDGysDDNADKES----VNLHDHLHVKIFAV--VTRSFNKDKLAPITRF-DGSVFTV 654
Cdd:COG1240 176 -----LELLKRADPARRKVIVLLTDG--RDNAGRIDpleaAELAAAAGIRIYTIgvGTEAVDEGLLREIAEAtGGRYFRA 248


                ....*..
gi 17560426 655 HQRESVA 661
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 ...
 481-684 1.20e-61

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: 203.77  E-value: 1.20e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 481 LPIDLMFLVDTSSSIGINNFDIQKNFICEILKD------VDIAPGRSRIAMIQYSQDPSVVFGFDQ-YYSYESVRRGVMR 553
Cdd:cd01480   1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERflkdyyRKDPAGSWRVGVVQYSDQQEVEAGFLRdIRNYTSLKEAVDN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 554 LSYTGGATMLSKALAFAGGIMYHeqnlkkttkkhqylpTPKHDRLQVLCLVSDG---YSDDNADKESVNLHDHLHVKIFA 630
Cdd:cd01480  81 LEYIGGGTFTDCALKYATEQLLE---------------GSHQKENKFLLVITDGhsdGSPDGGIEKAVNEADHLGIKIFF 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17560426 631 VVTRSFNKDKLAPITRFDGSvftVHQRESVAIWLWrqqriwaehySAFIEKEKK 684
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 ...
 483-663 2.54e-51

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: 2.54e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 483 IDLMFLVDTSSSIGINNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYSYESVRRGVMRLSYTGGATM 562
Cdd:cd01472   1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 563 LSKALAFAGGIMYHEQnlkkttkkhqylPTPKHDRLQVLCLVSDGYSDDNADKESVNLHDhLHVKIFAVVTRSFNKDKLA 642
Cdd:cd01472  81 TGKALKYVRENLFTEA------------SGSREGVPKVLVVITDGKSQDDVEEPAVELKQ-AGIEVFAVGVKNADEEELK 147

                       170       180
                ....*....|....*....|.
gi 17560426 643 PITRFDGSvftvHQRESVAIW 663
Cdd:cd01472 148 QIASDPKE----LYVFNVADF 164
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 483-645 5.06e-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: 130.10  E-value: 5.06e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 483 IDLMFLVDTSSSIGINNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYSYESVRRGVMRLSY-TGGAT 561
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYlGGGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 562 MLSKALAFAGGIMYHEQNLKKTTKKhqylptpkhdrlqVLCLVSDGYSDDNAD--KESVNLHDHlHVKIFAVVTRSFNKD 639
Cdd:cd01450  81 NTGKALQYALEQLFSESNARENVPK-------------VIIVLTDGRSDDGGDpkEAAAKLKDE-GIKVFVVGVGPADEE 146


                ....*.
gi 17560426 640 KLAPIT 645
Cdd:cd01450 147 ELREIA 152
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 484-654 1.46e-29

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: 1.46e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426    484 DLMFLVDTSSSIGINNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYSYESVRRGVMRLSYT-GGATM 562
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426    563 LSKALAFAggimyhEQNLKKTTKKHQYlptpkhDRLQVLCLVSDGYSDD---NADKESVNLHDHlHVKIFAV-VTRSFNK 638
Cdd:smart00327  81 LGAALQYA------LENLFSKSAGSRR------GAPKVVILITDGESNDgpkDLLKAAKELKRS-GVKVFVVgVGNDVDE 147

                          170
                   ....*....|....*.
gi 17560426    639 DKLAPITRFDGSVFTV 654
Cdd:smart00327 148 EELKKLASAPGGVYVF 163
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 484-631 2.08e-26

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: 105.83  E-value: 2.08e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 484 DLMFLVDTSSSIGINNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYSYESVRRGVMRLSYTGGATML 563
Cdd:cd01482   2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17560426 564 SKALAFAggimyHEQNLKKTTKKHQYLPtpkhdrlQVLCLVSDGYSDDNADKESVNLHDhLHVKIFAV 631
Cdd:cd01482  82 GKALTHV-----REKNFTPDAGARPGVP-------KVVILITDGKSQDDVELPARVLRN-LGVNVFAV 136
VWA pfam00092
von Willebrand factor type A domain;
484-631 5.69e-23

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 96.19  E-value: 5.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426   484 DLMFLVDTSSSIGINNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYSYESVRRGVMRLSY-TGGATM 562
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYlGGGTTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17560426   563 LSKALAFAggimyhEQNLKKTTKKHqylptpKHDRLQVLCLVSDGYSDDNADKESVNLHDHLHVKIFAV 631
Cdd:pfam00092  81 TGKALKYA------LENLFSSAAGA------RPGAPKVVVLLTDGRSQDGDPEEVARELKSAGVTVFAV 137
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 483-654 3.66e-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: 82.23  E-value: 3.66e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 483 IDLMFLVDTSSSIGINNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYSYESVRRGVMRLSYT-GGAT 561
Cdd:cd00198   1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 562 MLSKALAFAggimyhEQNLKKTTKKHQYlptpkhdrlQVLCLVSDGYSDD---NADKESVNLHDhLHVKIFAV-VTRSFN 637
Cdd:cd00198  81 NIGAALRLA------LELLKSAKRPNAR---------RVIILLTDGEPNDgpeLLAEAARELRK-LGITVYTIgIGDDAN 144

                       170
                ....*....|....*..
gi 17560426 638 KDKLAPITRFDGSVFTV 654
Cdd:cd00198 145 EDELKEIADKTTGGAVF 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 484-653 7.65e-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: 72.82  E-value: 7.65e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 484 DLMFLVDTSSSIGiNNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPS--VVFGFDQYYSYESVRRGVMRLSYTGGAT 561
Cdd:cd01476   2 DLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 562 MLSKALAFAGGIMYHEQNLKKTTKKhqylptpkhdrlqVLCLVSDGYSDDNADKESVNLHDHLHVKIFAVVT---RSFNK 638
Cdd:cd01476  81 ATGAAIEVALQQLDPSEGRREGIPK-------------VVVVLTDGRSHDDPEKQARILRAVPNIETFAVGTgdpGTVDT 147

                       170
                ....*....|....*
gi 17560426 639 DKLAPITRFDGSVFT 653
Cdd:cd01476 148 EELHSITGNEDHIFT 162
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 483-618 1.03e-13

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: 69.69  E-value: 1.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 483 IDLMFLVDTSSSIGINNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYSYESVRRGVMRLSYTGGATM 562
Cdd:cd01469   1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17560426 563 LSKALAFAGGIMYHEQN--LKKTTKkhqylptpkhdrlqVLCLVSDGYSDDNADKESV 618
Cdd:cd01469  81 TATAIQYVVTELFSESNgaRKDATK--------------VLVVITDGESHDDPLLKDV 124
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 482-570 5.21e-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: 5.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 482 PIDLMFLVDTSSSIGINNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYSYESVRRGVMRLSYTGGAT 561
Cdd:cd01475   2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81


                ....*....
gi 17560426 562 MLSKALAFA 570
Cdd:cd01475  82 MTGLAIQYA 90
VWA_2 pfam13519
von Willebrand factor type A domain;
485-582 1.63e-12

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 64.24  E-value: 1.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426   485 LMFLVDTSSSI-----GINNFDIQKNFICEILKDVDiapgRSRIAMIQYSQDPSVVFGFDQyySYESVRRGVMRLSYTGG 559
Cdd:pfam13519   1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                          90       100
                  ....*....|....*....|...
gi 17560426   560 ATMLSKALAFAGGIMYHEQNLKK 582
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 ...
 484-654 9.77e-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: 9.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 484 DLMFLVDTSSSIGINNFDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYSYESVRRGVMRLSYTGGATM- 562
Cdd:cd01481   2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLn 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 563 LSKALAF--------AGGIMYHEQnlkkttkkhqyLPtpkhdrlQVLCLVSDGYSDDNADKESVNLhDHLHVKIFAVVTR 634
Cdd:cd01481  82 TGSALDYvvknlftkSAGSRIEEG-----------VP-------QFLVLITGGKSQDDVERPAVAL-KRAGIVPFAIGAR 142

                       170       180
                ....*....|....*....|.
gi 17560426 635 SFNKDKLAPITrFDGS-VFTV 654
Cdd:cd01481 143 NADLAELQQIA-FDPSfVFQV 162
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 423-661 1.30e-08

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: 1.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 423 PIPSPVHNGSDGKDDATSSGTPESIESSGSDVTETTEDDLEELNRRTHLPRDHPARKLLPIDLMFLVDTSSSIGINN-FD 501
Cdd:COG1240  33 PLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLE 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 502 IQKNFICEILKDvdiAPGRSRIAMIQYSQDPSVVFGFDqyYSYESVRRGVMRLSyTGGATMLSKALAFAggimyheqnlk 581
Cdd:COG1240 113 AAKGALLDFLDD---YRPRDRVGLVAFGGEAEVLLPLT--RDREALKRALDELP-PGGGTPLGDALALA----------- 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 582 kttkkHQYLPTPKHDRLQVLCLVSDGysDDNADKES----VNLHDHLHVKIFAV--VTRSFNKDKLAPITRF-DGSVFTV 654
Cdd:COG1240 176 -----LELLKRADPARRKVIVLLTDG--RDNAGRIDpleaAELAAAAGIRIYTIgvGTEAVDEGLLREIAEAtGGRYFRA 248


                ....*..
gi 17560426 655 HQRESVA 661
Cdd:COG1240 249 DDLSELA 255
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 483-638 6.53e-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: 6.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 483 IDLMFLVDTSSSIGINN-FDIQKNFICEILKDVDIAPGRSRIAMIQYSQDPSVVFGFDQYYS-----YESVRRGVMRLSY 556
Cdd:cd01471   1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNStnkdlALNAIRALLSLYY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 557 TGGATMLSKALAFAggimyhEQNLKKTTKKHQYLPtpkhdrlQVLCLVSDGYSDDNAD--KESVNLHDhLHVKI--FAV- 631
Cdd:cd01471  81 PNGSTNTTSALLVV------EKHLFDTRGNRENAP-------QLVIIMTDGIPDSKFRtlKEARKLRE-RGVIIavLGVg 146


                ....*....
gi 17560426 632 --VTRSFNK 638
Cdd:cd01471 147 qgVNHEENR 155
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
477-633 4.55e-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: 4.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 477 ARKLLPIdlMFLVDTSSSI-GIN----NFDIQKnFICEILKDvDIAPGRSRIAMIQYSQDPSVVFGF---DQYYsyesvr 548
Cdd:COG4245   2 PMRRLPV--YLLLDTSGSMsGEPiealNEGLQA-LIDELRQD-PYALETVEVSVITFDGEAKVLLPLtdlEDFQ------ 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 549 rgVMRLSyTGGATMLSKALAFAGGIMyheqnlkkTTKKHQYLPTPKHDRLQVLCLVSDGYSDDNADKESVN-LHDHLHVK 627
Cdd:COG4245  72 --PPDLS-ASGGTPLGAALELLLDLI--------ERRVQKYTAEGKGDWRPVVFLITDGEPTDSDWEAALQrLKDGEAAK 140


                ....*.
gi 17560426 628 IFAVVT 633
Cdd:COG4245 141 KANIFA 146
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 484-654 9.59e-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: 9.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 484 DLMFLVDTSSSIGINNFDIQkNFIcEILKDVDIAPGrSRIAMIQYSQDPSVVFGFDQYYSYESvrrgvmrlsytGGATML 563
Cdd:cd01474   6 DLYFVLDKSGSVAANWIEIY-DFV-EQLVDRFNSPG-LRFSFITFSTRATKILPLTDDSSAII-----------KGLEVL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17560426 564 SKALafAGGIMYHEQNLKKTTKKHQYLPTPKHDRLQVLCLVSDGYSDDN----ADKESvNLHDHLHVKIFAVVTRSFNKD 639
Cdd:cd01474  72 KKVT--PSGQTYIHEGLENANEQIFNRNGGGRETVSVIIALTDGQLLLNghkyPEHEA-KLSRKLGAIVYCVGVTDFLKS 148

                       170
                ....*....|....*
gi 17560426 640 KLAPITRFDGSVFTV 654
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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