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Conserved domains on  [gi|13699836|ref|NP_085095|]
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matrilin-4 isoform 3 precursor [Homo sapiens]

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 ...
 260-496 2.80e-123

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 cd01475:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 224  Bit Score: 359.39  E-value: 2.80e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 260 GHVDLVLLVDGSKSVRPQNFELVKRFVNQIVDFLDVSPEGTRVGLVQFSSRVRTEFPLGRYGTAAEVKQAVLAVEYMERG 339
Cdd:cd01475   1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 340 TMTGLALRHMVEHSFSEAQGARPRALNVPRVGLVFTDGRSQDDISVWAARAKEEGIVMYAVGVGKAVEAELREIASEPAE 419
Cdd:cd01475  81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13699836 420 LHVSYAPDFGTMTHLLENLRGSICPEegisagtelRSPCECESLVEFQGRTLGALESltlnLAQLTARLEDLENQLA 496
Cdd:cd01475 161 DHVFYVEDFSTIEELTKKFQGKICVV---------PDLCATLSHVCQQVCISTPGSY----LCACTEGYALLEDNKT 224
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 31-253 1.12e-120

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 cd01475:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 224  Bit Score: 352.84  E-value: 1.12e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836  31 GPLDLVFVIDSSRSVRPFEFETMRQFLMGLLRGLNVGPNATRVGVIQYSSQVQSVFPLRAFSRREDMERAIRDLVPLAQG 110
Cdd:cd01475   1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 111 TMTGLAIQYAMNVAFSVAEGARPPEERVPRVAVIVTDGRPQDRVAEVAAQARARGIEIYAVGVQRADVGSLRAMASPPLD 190
Cdd:cd01475  81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13699836 191 EHVFLVESFDLIQEFGLQFQSRLCV-RDLCNGVDHGCEFQCVSEGLSYRCLCPEGRQLQADGKS 253
Cdd:cd01475 161 DHVFYVEDFSTIEELTKKFQGKICVvPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
 
Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 260-496 2.80e-123

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: 359.39  E-value: 2.80e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 260 GHVDLVLLVDGSKSVRPQNFELVKRFVNQIVDFLDVSPEGTRVGLVQFSSRVRTEFPLGRYGTAAEVKQAVLAVEYMERG 339
Cdd:cd01475   1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 340 TMTGLALRHMVEHSFSEAQGARPRALNVPRVGLVFTDGRSQDDISVWAARAKEEGIVMYAVGVGKAVEAELREIASEPAE 419
Cdd:cd01475  81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13699836 420 LHVSYAPDFGTMTHLLENLRGSICPEegisagtelRSPCECESLVEFQGRTLGALESltlnLAQLTARLEDLENQLA 496
Cdd:cd01475 161 DHVFYVEDFSTIEELTKKFQGKICVV---------PDLCATLSHVCQQVCISTPGSY----LCACTEGYALLEDNKT 224
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 31-253 1.12e-120

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: 352.84  E-value: 1.12e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836  31 GPLDLVFVIDSSRSVRPFEFETMRQFLMGLLRGLNVGPNATRVGVIQYSSQVQSVFPLRAFSRREDMERAIRDLVPLAQG 110
Cdd:cd01475   1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 111 TMTGLAIQYAMNVAFSVAEGARPPEERVPRVAVIVTDGRPQDRVAEVAAQARARGIEIYAVGVQRADVGSLRAMASPPLD 190
Cdd:cd01475  81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13699836 191 EHVFLVESFDLIQEFGLQFQSRLCV-RDLCNGVDHGCEFQCVSEGLSYRCLCPEGRQLQADGKS 253
Cdd:cd01475 161 DHVFYVEDFSTIEELTKKFQGKICVvPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
VWA pfam00092
von Willebrand factor type A domain;
263-437 1.72e-65

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 209.44  E-value: 1.72e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836   263 DLVLLVDGSKSVRPQNFELVKRFVNQIVDFLDVSPEGTRVGLVQFSSRVRTEFPLGRYGTAAEVKQAVLAVEYMERGTM- 341
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836   342 TGLALRHMVEHSFSEAQGARPralNVPRVGLVFTDGRSQD-DISVWAARAKEEGIVMYAVGVGKAVEAELREIASEPAEL 420
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARP---GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                         170
                  ....*....|....*..
gi 13699836   421 HVSYAPDFGTMTHLLEN 437
Cdd:pfam00092 158 HVFTVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
34-205 3.25e-59

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 192.88  E-value: 3.25e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836    34 DLVFVIDSSRSVRPFEFETMRQFLMGLLRGLNVGPNATRVGVIQYSSQVQSVFPLRAFSRREDMERAIRDLVPLAQGTM- 112
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836   113 TGLAIQYAMNVAFSVAEGARPpeeRVPRVAVIVTDGRPQD-RVAEVAAQARARGIEIYAVGVQRADVGSLRAMASPPLDE 191
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARP---GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                         170
                  ....*....|....
gi 13699836   192 HVFLVESFDLIQEF 205
Cdd:pfam00092 158 HVFTVSDFEALEDL 171
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 263-435 3.08e-50

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: 169.56  E-value: 3.08e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836    263 DLVLLVDGSKSVRPQNFELVKRFVNQIVDFLDVSPEGTRVGLVQFSSRVRTEFPLGRYGTAAEVKQAVLAVEY-MERGTM 341
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836    342 TGLALRHMVEHSFSEAQGARPralNVPRVGLVFTDGRSQD---DISVWAARAKEEGIVMYAVGVGKAV-EAELREIASEP 417
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRR---GAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVdEEELKKLASAP 157

                          170
                   ....*....|....*...
gi 13699836    418 AELHVSYAPDFGTMTHLL 435
Cdd:smart00327 158 GGVYVFLPELLDLLIDLL 175
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 34-205 2.01e-48

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: 164.55  E-value: 2.01e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836     34 DLVFVIDSSRSVRPFEFETMRQFLMGLLRGLNVGPNATRVGVIQYSSQVQSVFPLRAFSRREDMERAIRDLVPLAQG-TM 112
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGgTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836    113 TGLAIQYAMNVAFSVAEGARPpeeRVPRVAVIVTDGRPQD---RVAEVAAQARARGIEIYAVGVQRA-DVGSLRAMASPP 188
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRR---GAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAP 157

                          170
                   ....*....|....*..
gi 13699836    189 LDEHVFLVESFDLIQEF 205
Cdd:smart00327 158 GGVYVFLPELLDLLIDL 174
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 32-185 4.32e-16

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: 78.06  E-value: 4.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836  32 PLDLVFVIDSSRSVRPFE-FETMRQFLMGLLRGLNVGpnaTRVGVIQYSSQVQSVFPLRafSRREDMERAIRDLVPlAQG 110
Cdd:COG1240  92 GRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPR---DRVGLVAFGGEAEVLLPLT--RDREALKRALDELPP-GGG 165

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 111 TMTGLAIQYAMNVAFSVAEGARppeervpRVAVIVTDGRP---QDRVAEVAAQARARGIEIYAVGV--QRADVGSLRAMA 185
Cdd:COG1240 166 TPLGDALALALELLKRADPARR-------KVIVLLTDGRDnagRIDPLEAAELAAAAGIRIYTIGVgtEAVDEGLLREIA 238
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 262-416 5.55e-14

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: 71.89  E-value: 5.55e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 262 VDLVLLVDGSKSVRPQN-FELVKRFVNqivDFLDVSPEGTRVGLVQFSSRVRTEFPLGRygtaaEVKQAVLAVEYMERGT 340
Cdd:COG1240  93 RDVVLVVDASGSMAAENrLEAAKGALL---DFLDDYRPRDRVGLVAFGGEAEVLLPLTR-----DREALKRALDELPPGG 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 341 MT--GLALRHMVEHsFSEAQGARPRALnvprvgLVFTDGR---SQDDISVWAARAKEEGIVMYAVGVGKAV--EAELREI 413
Cdd:COG1240 165 GTplGDALALALEL-LKRADPARRKVI------VLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTEAvdEGLLREI 237


                ...
gi 13699836 414 ASE 416
Cdd:COG1240 238 AEA 240
 
Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 260-496 2.80e-123

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: 359.39  E-value: 2.80e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 260 GHVDLVLLVDGSKSVRPQNFELVKRFVNQIVDFLDVSPEGTRVGLVQFSSRVRTEFPLGRYGTAAEVKQAVLAVEYMERG 339
Cdd:cd01475   1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 340 TMTGLALRHMVEHSFSEAQGARPRALNVPRVGLVFTDGRSQDDISVWAARAKEEGIVMYAVGVGKAVEAELREIASEPAE 419
Cdd:cd01475  81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13699836 420 LHVSYAPDFGTMTHLLENLRGSICPEegisagtelRSPCECESLVEFQGRTLGALESltlnLAQLTARLEDLENQLA 496
Cdd:cd01475 161 DHVFYVEDFSTIEELTKKFQGKICVV---------PDLCATLSHVCQQVCISTPGSY----LCACTEGYALLEDNKT 224
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 31-253 1.12e-120

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: 352.84  E-value: 1.12e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836  31 GPLDLVFVIDSSRSVRPFEFETMRQFLMGLLRGLNVGPNATRVGVIQYSSQVQSVFPLRAFSRREDMERAIRDLVPLAQG 110
Cdd:cd01475   1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 111 TMTGLAIQYAMNVAFSVAEGARPPEERVPRVAVIVTDGRPQDRVAEVAAQARARGIEIYAVGVQRADVGSLRAMASPPLD 190
Cdd:cd01475  81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13699836 191 EHVFLVESFDLIQEFGLQFQSRLCV-RDLCNGVDHGCEFQCVSEGLSYRCLCPEGRQLQADGKS 253
Cdd:cd01475 161 DHVFYVEDFSTIEELTKKFQGKICVvPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
VWA pfam00092
von Willebrand factor type A domain;
263-437 1.72e-65

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 209.44  E-value: 1.72e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836   263 DLVLLVDGSKSVRPQNFELVKRFVNQIVDFLDVSPEGTRVGLVQFSSRVRTEFPLGRYGTAAEVKQAVLAVEYMERGTM- 341
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836   342 TGLALRHMVEHSFSEAQGARPralNVPRVGLVFTDGRSQD-DISVWAARAKEEGIVMYAVGVGKAVEAELREIASEPAEL 420
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARP---GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                         170
                  ....*....|....*..
gi 13699836   421 HVSYAPDFGTMTHLLEN 437
Cdd:pfam00092 158 HVFTVSDFEALEDLQDQ 174
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 262-428 2.42e-61

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: 198.22  E-value: 2.42e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 262 VDLVLLVDGSKSVRPQNFELVKRFVNQIVDFLDVSPEGTRVGLVQFSSRVRTEFPLGRYGTAAEVKQAVLAVEYMERGTM 341
Cdd:cd01472   1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 342 TGLALRHMVEHSFSEAQGARPralNVPRVGLVFTDGRSQDDISVWAARAKEEGIVMYAVGVGKAVEAELREIASEPAELH 421
Cdd:cd01472  81 TGKALKYVRENLFTEASGSRE---GVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELY 157


                ....*..
gi 13699836 422 VSYAPDF 428
Cdd:cd01472 158 VFNVADF 164
VWA pfam00092
von Willebrand factor type A domain;
34-205 3.25e-59

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 192.88  E-value: 3.25e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836    34 DLVFVIDSSRSVRPFEFETMRQFLMGLLRGLNVGPNATRVGVIQYSSQVQSVFPLRAFSRREDMERAIRDLVPLAQGTM- 112
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836   113 TGLAIQYAMNVAFSVAEGARPpeeRVPRVAVIVTDGRPQD-RVAEVAAQARARGIEIYAVGVQRADVGSLRAMASPPLDE 191
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARP---GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                         170
                  ....*....|....
gi 13699836   192 HVFLVESFDLIQEF 205
Cdd:pfam00092 158 HVFTVSDFEALEDL 171
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 262-422 1.04e-58

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: 190.97  E-value: 1.04e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 262 VDLVLLVDGSKSVRPQNFELVKRFVNQIVDFLDVSPEGTRVGLVQFSSRVRTEFPLGRYGTAAEVKQAVLAVEYMER-GT 340
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 341 MTGLALRHMVEHSFSEAQgarpRALNVPRVGLVFTDGRSQDDISV--WAARAKEEGIVMYAVGVGKAVEAELREIASEPA 418
Cdd:cd01450  81 NTGKALQYALEQLFSESN----ARENVPKVIIVLTDGRSDDGGDPkeAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156


                ....
gi 13699836 419 ELHV 422
Cdd:cd01450 157 ERHV 160
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 263-428 2.93e-58

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: 190.19  E-value: 2.93e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 263 DLVLLVDGSKSVRPQNFELVKRFVNQIVDFLDVSPEGTRVGLVQFSSRVRTEFPLGRYGTAAEVKQAVLAVEYMERGTMT 342
Cdd:cd01482   2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 343 GLALRHMVEHSFSEAQGARPralNVPRVGLVFTDGRSQDDISVWAARAKEEGIVMYAVGVGKAVEAELREIASEPAELHV 422
Cdd:cd01482  82 GKALTHVREKNFTPDAGARP---GVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHV 158


                ....*.
gi 13699836 423 SYAPDF 428
Cdd:cd01482 159 FNVADF 164
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 33-194 3.26e-51

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: 171.71  E-value: 3.26e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836  33 LDLVFVIDSSRSVRPFEFETMRQFLMGLLRGLNVGPNATRVGVIQYSSQVQSVFPLRAFSRREDMERAIRDLVPLA-QGT 111
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGgGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 112 MTGLAIQYAMNVAFSvaegARPPEERVPRVAVIVTDGRPQDR--VAEVAAQARARGIEIYAVGVQRADVGSLRAMASPPL 189
Cdd:cd01450  81 NTGKALQYALEQLFS----ESNARENVPKVIIVLTDGRSDDGgdPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156


                ....*
gi 13699836 190 DEHVF 194
Cdd:cd01450 157 ERHVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 263-435 3.08e-50

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: 169.56  E-value: 3.08e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836    263 DLVLLVDGSKSVRPQNFELVKRFVNQIVDFLDVSPEGTRVGLVQFSSRVRTEFPLGRYGTAAEVKQAVLAVEY-MERGTM 341
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836    342 TGLALRHMVEHSFSEAQGARPralNVPRVGLVFTDGRSQD---DISVWAARAKEEGIVMYAVGVGKAV-EAELREIASEP 417
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRR---GAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVdEEELKKLASAP 157

                          170
                   ....*....|....*...
gi 13699836    418 AELHVSYAPDFGTMTHLL 435
Cdd:smart00327 158 GGVYVFLPELLDLLIDLL 175
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 34-199 1.93e-49

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: 167.02  E-value: 1.93e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836  34 DLVFVIDSSRSVRPFEFETMRQFLMGLLRGLNVGPNATRVGVIQYSSQVQSVFPLRAFSRREDMERAIRDLVPLAQGTMT 113
Cdd:cd01472   2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 114 GLAIQYAMNVAFSVAEGARppeERVPRVAVIVTDGRPQDRVAEVAAQARARGIEIYAVGVQRADVGSLRAMASPPLDEHV 193
Cdd:cd01472  82 GKALKYVRENLFTEASGSR---EGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYV 158


                ....*.
gi 13699836 194 FLVESF 199
Cdd:cd01472 159 FNVADF 164
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 34-205 2.01e-48

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: 164.55  E-value: 2.01e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836     34 DLVFVIDSSRSVRPFEFETMRQFLMGLLRGLNVGPNATRVGVIQYSSQVQSVFPLRAFSRREDMERAIRDLVPLAQG-TM 112
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGgTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836    113 TGLAIQYAMNVAFSVAEGARPpeeRVPRVAVIVTDGRPQD---RVAEVAAQARARGIEIYAVGVQRA-DVGSLRAMASPP 188
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRR---GAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAP 157

                          170
                   ....*....|....*..
gi 13699836    189 LDEHVFLVESFDLIQEF 205
Cdd:smart00327 158 GGVYVFLPELLDLLIDL 174
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 34-199 4.40e-45

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: 155.52  E-value: 4.40e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836  34 DLVFVIDSSRSVRPFEFETMRQFLMGLLRGLNVGPNATRVGVIQYSSQVQSVFPLRAFSRREDMERAIRDLVPLAQGTMT 113
Cdd:cd01482   2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 114 GLAIQYAMNVAFSVAEGARPpeeRVPRVAVIVTDGRPQDRVAEVAAQARARGIEIYAVGVQRADVGSLRAMASPPLDEHV 193
Cdd:cd01482  82 GKALTHVREKNFTPDAGARP---GVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHV 158


                ....*.
gi 13699836 194 FLVESF 199
Cdd:cd01482 159 FNVADF 164
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 262-428 3.88e-34

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: 126.70  E-value: 3.88e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 262 VDLVLLVDGSKSVRPQNFELVKRFVNQIVDFLDVSPEGTRVGLVQFSSRVRTEFPLGRYGTAAEVKQAVLAVEYMERGTM 341
Cdd:cd01469   1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 342 TGLALRHMVEHSFSEAQGARPRALnvpRVGLVFTDGRSQDDISVWAA--RAKEEGIVMYAVGVGKAVEA-----ELREIA 414
Cdd:cd01469  81 TATAIQYVVTELFSESNGARKDAT---KVLVVITDGESHDDPLLKDVipQAEREGIIRYAIGVGGHFQRensreELKTIA 157

                       170
                ....*....|....
gi 13699836 415 SEPAELHVSYAPDF 428
Cdd:cd01469 158 SKPPEEHFFNVTDF 171
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 263-417 5.69e-33

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: 123.20  E-value: 5.69e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 263 DLVLLVDGSKSVRPQNFELVKRFVNQIVDFLDVSPEGTRVGLVQFSSRVRTEFPLGRYGTAAEVKQAVLAVEYME-RGTM 341
Cdd:cd01481   2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGgSQLN 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13699836 342 TGLALRHMVEHSFSEAQGARPRAlNVPRVGLVFTDGRSQDDISVWAARAKEEGIVMYAVGVGKAVEAELREIASEP 417
Cdd:cd01481  82 TGSALDYVVKNLFTKSAGSRIEE-GVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP 156
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 33-200 2.16e-32

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: 121.69  E-value: 2.16e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836  33 LDLVFVIDSSRSVRPFEFETMRQFLMGLLRGLNVGPNATRVGVIQYSSQVQSVFPLRAFSRREDMERAIRDLVPLAQGTM 112
Cdd:cd01469   1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 113 TGLAIQYAMNVAFSVAEGARPpeeRVPRVAVIVTDGRPQD--RVAEVAAQARARGIEIYAVGV----QRAD-VGSLRAMA 185
Cdd:cd01469  81 TATAIQYVVTELFSESNGARK---DATKVLVVITDGESHDdpLLKDVIPQAEREGIIRYAIGVgghfQRENsREELKTIA 157

                       170
                ....*....|....*
gi 13699836 186 SPPLDEHVFLVESFD 200
Cdd:cd01469 158 SKPPEEHFFNVTDFA 172
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 34-199 2.36e-32

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: 121.28  E-value: 2.36e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836  34 DLVFVIDSSRSVRPFEFETMRQFLMGLLRGLNVGPNATRVGVIQYSSQVQSVFPLRAFSRREDMERAIRDLVPL-AQGTM 112
Cdd:cd01481   2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRgGSQLN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 113 TGLAIQYAMNVAFSVAEGARpPEERVPRVAVIVTDGRPQDRVAEVAAQARARGIEIYAVGVQRADVGSLRAMASPPldEH 192
Cdd:cd01481  82 TGSALDYVVKNLFTKSAGSR-IEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP--SF 158


                ....*..
gi 13699836 193 VFLVESF 199
Cdd:cd01481 159 VFQVSDF 165
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 262-422 1.15e-31

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: 119.21  E-value: 1.15e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 262 VDLVLLVDGSKSVRPQNFELVKRFVNQIVDFLDVSPEGTRVGLVQFSSRVRTEFPLGRYGTAAEVKQAVLAVEY-MERGT 340
Cdd:cd00198   1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 341 MTGLALRHMVEHSFSEAQGarpralNVPRVGLVFTDGRSQDD---ISVWAARAKEEGIVMYAVGVG-KAVEAELREIASE 416
Cdd:cd00198  81 NIGAALRLALELLKSAKRP------NARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIGdDANEDELKEIADK 154


                ....*.
gi 13699836 417 PAELHV 422
Cdd:cd00198 155 TTGGAV 160
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 33-194 5.07e-30

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: 114.97  E-value: 5.07e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836  33 LDLVFVIDSSRSVRPFEFETMRQFLMGLLRGLNVGPNATRVGVIQYSSQVQSVFPLRAFSRREDMERAIRDLVPLA-QGT 111
Cdd:cd00198   1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLgGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 112 MTGLAIQYAMNVAFSVAEGARppeervPRVAVIVTDGRPQD---RVAEVAAQARARGIEIYAVGV-QRADVGSLRAMASP 187
Cdd:cd00198  81 NIGAALRLALELLKSAKRPNA------RRVIILLTDGEPNDgpeLLAEAARELRKLGITVYTIGIgDDANEDELKEIADK 154


                ....*..
gi 13699836 188 PLDEHVF 194
Cdd:cd00198 155 TTGGAVF 161
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 260-431 4.20e-26

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: 104.77  E-value: 4.20e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 260 GHVDLVLLVDGSKSVRPQNFELVKRFVNQIVDFL------DVSPEGTRVGLVQFSSRVRTEFPLGR-YGTAAEVKQAVLA 332
Cdd:cd01480   1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRdIRNYTSLKEAVDN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 333 VEYMERGTMTGLALRHMVEhsfsEAQGARPRALNvpRVGLVFTDGRSQ----DDISVWAARAKEEGIVMYAVGVGKAVEA 408
Cdd:cd01480  81 LEYIGGGTFTDCALKYATE----QLLEGSHQKEN--KFLLVITDGHSDgspdGGIEKAVNEADHLGIKIFFVAVGSQNEE 154

                       170       180
                ....*....|....*....|...
gi 13699836 409 ELREIASEPAELHvsYAPDFGTM 431
Cdd:cd01480 155 PLSRIACDGKSAL--YRENFAEL 175
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 33-173 6.97e-25

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: 100.55  E-value: 6.97e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836  33 LDLVFVIDSSRSVRPfEFETMRQFLMGLLRGLNVGPNATRVGVIQYSSQVQS--VFPLRAFSRREDMERAIRDLVPLAQG 110
Cdd:cd01476   1 LDLLFVLDSSGSVRG-KFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGT 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13699836 111 TMTGLAIQYAMNVaFSVAEGARppeERVPRVAVIVTDGRPQDRVAEVAAQARAR-GIEIYAVGV 173
Cdd:cd01476  80 TATGAAIEVALQQ-LDPSEGRR---EGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGT 139
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 263-414 1.34e-24

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: 99.78  E-value: 1.34e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 263 DLVLLVDGSKSVRPQnFELVKRFVNQIVDFLDVSPEGTRVGLVQFSSRVRT--EFPLGRYGTAAEVKQAVLAVEYMERGT 340
Cdd:cd01476   2 DLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13699836 341 MTGLALRHMVEHsFSEAQGARPralNVPRVGLVFTDGRSQDDISVWAARAKEE-GIVMYAVGVG---KAVEAELREIA 414
Cdd:cd01476  81 ATGAAIEVALQQ-LDPSEGRRE---GIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGdpgTVDTEELHSIT 154
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 262-414 9.59e-19

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: 83.97  E-value: 9.59e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 262 VDLVLLVDGSKSVRPQN-FELVKRFVNQIVDFLDVSPEGTRVGLVQFSSRVRTEFPLGRYG-----TAAEVKQAVLAVEY 335
Cdd:cd01471   1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNstnkdLALNAIRALLSLYY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 336 MERGTMTGLALRHMVEHSFsEAQGARPralNVPRVGLVFTDGRSQDDI-SVWAARA-KEEGIVMYAVGVGKAVE-AELRE 412
Cdd:cd01471  81 PNGSTNTTSALLVVEKHLF-DTRGNRE---NAPQLVIIMTDGIPDSKFrTLKEARKlRERGVIIAVLGVGQGVNhEENRS 156


                ..
gi 13699836 413 IA 414
Cdd:cd01471 157 LV 158
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 31-175 1.48e-18

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: 83.59  E-value: 1.48e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836  31 GPLDLVFVIDSSRSVRPFEFET----MRQFLMGLLRGLNVGPNA--TRVGVIQYSSQVQSVFP-LRAFSRREDMERAIRD 103
Cdd:cd01480   1 GPVDITFVLDSSESVGLQNFDItknfVKRVAERFLKDYYRKDPAgsWRVGVVQYSDQQEVEAGfLRDIRNYTSLKEAVDN 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13699836 104 LVPLAQGTMTGLAIQYAMNVafsVAEGARPPEErvpRVAVIVTDGRPQ---DRVAEVAAQ-ARARGIEIYAVGVQR 175
Cdd:cd01480  81 LEYIGGGTFTDCALKYATEQ---LLEGSHQKEN---KFLLVITDGHSDgspDGGIEKAVNeADHLGIKIFFVAVGS 150
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 32-185 4.32e-16

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: 78.06  E-value: 4.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836  32 PLDLVFVIDSSRSVRPFE-FETMRQFLMGLLRGLNVGpnaTRVGVIQYSSQVQSVFPLRafSRREDMERAIRDLVPlAQG 110
Cdd:COG1240  92 GRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPR---DRVGLVAFGGEAEVLLPLT--RDREALKRALDELPP-GGG 165

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 111 TMTGLAIQYAMNVAFSVAEGARppeervpRVAVIVTDGRP---QDRVAEVAAQARARGIEIYAVGV--QRADVGSLRAMA 185
Cdd:COG1240 166 TPLGDALALALELLKRADPARR-------KVIVLLTDGRDnagRIDPLEAAELAAAAGIRIYTIGVgtEAVDEGLLREIA 238
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 32-173 4.65e-16

Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 78.60  E-value: 4.65e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836  32 PLDLVFVIDSSRSVRPFEFETMRQFLMGLLRGLNVGpnaTRVGVIQYSSQVQSVFPLRAFSRREDMERAIRDLVPlAQGT 111
Cdd:COG2304  91 PLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPG---DRVSIVTFAGDARVLLPPTPATDRAKILAAIDRLQA-GGGT 166

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13699836 112 MTGLAIQYAMNVAfsvaeGARPPEERVPRVaVIVTDGRP------QDRVAEVAAQARARGIEIYAVGV 173
Cdd:COG2304 167 ALGAGLELAYELA-----RKHFIPGRVNRV-ILLTDGDAnvgitdPEELLKLAEEAREEGITLTTLGV 228
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 262-416 5.55e-14

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: 71.89  E-value: 5.55e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 262 VDLVLLVDGSKSVRPQN-FELVKRFVNqivDFLDVSPEGTRVGLVQFSSRVRTEFPLGRygtaaEVKQAVLAVEYMERGT 340
Cdd:COG1240  93 RDVVLVVDASGSMAAENrLEAAKGALL---DFLDDYRPRDRVGLVAFGGEAEVLLPLTR-----DREALKRALDELPPGG 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 341 MT--GLALRHMVEHsFSEAQGARPRALnvprvgLVFTDGR---SQDDISVWAARAKEEGIVMYAVGVGKAV--EAELREI 413
Cdd:COG1240 165 GTplGDALALALEL-LKRADPARRKVI------VLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTEAvdEGLLREI 237


                ...
gi 13699836 414 ASE 416
Cdd:COG1240 238 AEA 240
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 33-191 1.31e-13

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: 69.34  E-value: 1.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836  33 LDLVFVIDSSRSVRPF-EFETMRQFLMGLLRGLNVGPNATRVGVIQYSSQVQSVFPLRAF--SRREDMERAIRDL--VPL 107
Cdd:cd01471   1 LDLYLLVDGSGSIGYSnWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPnsTNKDLALNAIRALlsLYY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 108 AQG-TMTGLAIQYAMNVAFSvaegARPPEERVPRVAVIVTDGRPQD--RVAEVAAQARARGIEIYAVGV-QRADVGSLRA 183
Cdd:cd01471  81 PNGsTNTTSALLVVEKHLFD----TRGNRENAPQLVIIMTDGIPDSkfRTLKEARKLRERGVIIAVLGVgQGVNHEENRS 156


                ....*...
gi 13699836 184 MASPPLDE 191
Cdd:cd01471 157 LVGCDPDD 164
VWA_2 pfam13519
von Willebrand factor type A domain;
264-365 6.46e-13

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 64.62  E-value: 6.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836   264 LVLLVDGSKSVR-----PQNFELVKRFVNQIVDFLDvspeGTRVGLVQFSSRVRTEFPLGRygTAAEVKQAVLAVEYMER 338
Cdd:pfam13519   1 LVFVLDTSGSMRngdygPTRLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                          90       100
                  ....*....|....*....|....*..
gi 13699836   339 GTMTGLALRHMVEHSFSEAQGARPRAL 365
Cdd:pfam13519  75 GTNLAAALQLARAALKHRRKNQPRRIV 101
VWA_2 pfam13519
von Willebrand factor type A domain;
35-133 7.88e-12

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 61.54  E-value: 7.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836    35 LVFVIDSSRSVR-----PFEFETMRQFLMGLLRGLNvgpnATRVGVIQYSSQVQSVFPLRafSRREDMERAIRDLVPLAQ 109
Cdd:pfam13519   1 LVFVLDTSGSMRngdygPTRLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                          90       100
                  ....*....|....*....|....
gi 13699836   110 GTMTGLAIQYAMNVAFSVAEGARP 133
Cdd:pfam13519  75 GTNLAAALQLARAALKHRRKNQPR 98
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 257-417 1.10e-10

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: 60.60  E-value: 1.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 257 CReGHVDLVLLVDGSKSVRPQNFELVKrFVNQIVDFLdVSPeGTRVGLVQFSSRVRTEFPLGRYGTA----AEVKQAVLA 332
Cdd:cd01474   1 CA-GHFDLYFVLDKSGSVAANWIEIYD-FVEQLVDRF-NSP-GLRFSFITFSTRATKILPLTDDSSAiikgLEVLKKVTP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 333 V--EYMERGtmtglaLRHMVEHSFSEAQGARpralNVPRVGLVFTDGRSQDDISVW----AARAKEEGIVMYAVGVGKAV 406
Cdd:cd01474  77 SgqTYIHEG------LENANEQIFNRNGGGR----ETVSVIIALTDGQLLLNGHKYpeheAKLSRKLGAIVYCVGVTDFL 146

                       170
                ....*....|.
gi 13699836 407 EAELREIASEP 417
Cdd:cd01474 147 KSQLINIADSK 157
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
32-187 5.55e-10

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 58.78  E-value: 5.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836  32 PLDLVFVIDSSRSVRPFEFETMRQFLMGLLRGLNVGPNAT---RVGVIQYSSQVQSVFPLrafSRREDMEraIRDLVplA 108
Cdd:COG4245   5 RLPVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYALetvEVSVITFDGEAKVLLPL---TDLEDFQ--PPDLS--A 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 109 QG-TMTGLAIQYAMN-----VAFSVAEGARPpeerVPRVAVIVTDGRPQDRVAEVAAQA-----RARGIEIYAVGVQR-A 176
Cdd:COG4245  78 SGgTPLGAALELLLDlierrVQKYTAEGKGD----WRPVVFLITDGEPTDSDWEAALQRlkdgeAAKKANIFAIGVGPdA 153

                       170
                ....*....|.
gi 13699836 177 DVGSLRAMASP 187
Cdd:COG4245 154 DTEVLKQLTDP 164
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 219-254 8.22e-10

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 53.79  E-value: 8.22e-10
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 13699836   219 CNGVDHGCEFQCVSEGLSYRCLCPEGRQLQADGKSC 254
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 33-173 1.59e-08

VWA subgroup: 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. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known.


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 54.20  E-value: 1.59e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836  33 LDLVFVIDSSRSVRPFEFETMRQFLMGLLRGLNvgpNATRVGVIQYSSQVQSVFPLRAFSRREDMERAIRDLVPlAQGTM 112
Cdd:cd01465   1 LNLVFVIDRSGSMDGPKLPLVKSALKLLVDQLR---PDDRLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTA-GGSTA 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13699836 113 TGLAIQYAMNVAfsvAEGARPpeERVPRVaVIVTDGRPQ------DRVAEVAAQARARGIEIYAVGV 173
Cdd:cd01465  77 GGAGIQLGYQEA---QKHFVP--GGVNRI-LLATDGDFNvgetdpDELARLVAQKRESGITLSTLGF 137
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 262-403 9.56e-08

VWA subgroup: 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. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known.


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 51.89  E-value: 9.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 262 VDLVLLVDGSKSVRPQNFELVKRFVNQIVDFLDvspEGTRVGLVQFSSRVRTEFPlgryGTAAEVKQAVL-AVEYMERGT 340
Cdd:cd01465   1 LNLVFVIDRSGSMDGPKLPLVKSALKLLVDQLR---PDDRLAIVTYDGAAETVLP----ATPVRDKAAILaAIDRLTAGG 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 341 MTGLALRhmVEHSFSEAQ-GARPRALNvpRVgLVFTDGRSQDDISVW------AARAKEEGIVMYAVGVG 403
Cdd:cd01465  74 STAGGAG--IQLGYQEAQkHFVPGGVN--RI-LLATDGDFNVGETDPdelarlVAQKRESGITLSTLGFG 138
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 263-422 2.06e-07

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 51.52  E-value: 2.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 263 DLVLLVDGSKSVRPQNFELVKRFVNQIVDFL---DVSPegtRVGLVQFSSRVR-----TEFplgRYGTAAEVKQAVLAVE 334
Cdd:cd01470   2 NIYIALDASDSIGEEDFDEAKNAIKTLIEKIssyEVSP---RYEIISYASDPKeivsiRDF---NSNDADDVIKRLEDFN 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 335 YME----RGTMTGLALrHMVEHSFSEAQGARPRALNVPR-VGLVFTDGRSQ---------DDI------SVWAARAKEEG 394
Cdd:cd01470  76 YDDhgdkTGTNTAAAL-KKVYERMALEKVRNKEAFNETRhVIILFTDGKSNmggsplptvDKIknlvykNNKSDNPREDY 154

                       170       180       190
                ....*....|....*....|....*....|
gi 13699836 395 IVMYAVGVGKAVEA-ELREIASE-PAELHV 422
Cdd:cd01470 155 LDVYVFGVGDDVNKeELNDLASKkDNERHF 184
Matrilin_ccoil pfam10393
Trimeric coiled-coil oligomerization domain of matrilin; This short domain is a coiled coil ...
 457-495 4.37e-07

Trimeric coiled-coil oligomerization domain of matrilin; This short domain is a coiled coil structure and has a single cysteine residue at the start which is likely to form a di-sulfide bridge with a corresponding cysteine in an upstream EGF (pfam00008) domain thereby spanning a VWA (pfam00092) domain. All three domains can be associated together as in the cartilage matrix protein matrilin, where this domain is likely to be responsible for oligomerization.


Pssm-ID: 463070  Cd Length: 43  Bit Score: 46.19  E-value: 4.37e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 13699836   457 PCECESLVEFQGRTLGALESLTLNLAQLTARLEDLENQL 495
Cdd:pfam10393   5 PCKCEAIVAFQTKVESEIQALTTKLEEVTKRIEALENRL 43
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 262-442 1.73e-06

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 48.48  E-value: 1.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 262 VDLVLLVDGSKSVRPQNFELVKRF--VNQIV-DFLDvSPEGTRVGLVQFSSRVRTEFPLGRYGTAAEVKQAVLAVEYMER 338
Cdd:cd01467   3 RDIMIALDVSGSMLAQDFVKPSRLeaAKEVLsDFID-RRENDRIGLVVFAGAAFTQAPLTLDRESLKELLEDIKIGLAGQ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 339 GTMTG----LALRHMVEhsfSEAQGarpralnvpRVGLVFTDGRS-QDDIS-VWAAR-AKEEGIVMYAVGVGKaveaelr 411
Cdd:cd01467  82 GTAIGdaigLAIKRLKN---SEAKE---------RVIVLLTDGENnAGEIDpATAAElAKNKGVRIYTIGVGK------- 142

                       170       180       190
                ....*....|....*....|....*....|..
gi 13699836 412 eiaSEPAELHV-SYAPDFGTMTHLLENLRGSI 442
Cdd:cd01467 143 ---SGSGPKPDgSTILDEDSLVEIADKTGGRI 171
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 34-173 5.08e-05

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 43.86  E-value: 5.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836  34 DLVFVIDSSRS------VRPFEFETMRQFLMGLLRGLNvgpnATRVGVIQYSSQVQSVFPLRAfsRREDMERAIRDLVP- 106
Cdd:cd01467   4 DIMIALDVSGSmlaqdfVKPSRLEAAKEVLSDFIDRRE----NDRIGLVVFAGAAFTQAPLTL--DRESLKELLEDIKIg 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13699836 107 -LAQGTMTGLAIQYAMNVaFSVAEGarppeerVPRVAVIVTDGR------PQDRVAEVAAqarARGIEIYAVGV 173
Cdd:cd01467  78 lAGQGTAIGDAIGLAIKR-LKNSEA-------KERVIVLLTDGEnnageiDPATAAELAK---NKGVRIYTIGV 140
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 31-203 5.76e-05

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: 44.04  E-value: 5.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836  31 GPLDLVFVIDSSRSVRPFEFEtMRQFLMGLLRGLNvGPNaTRVGVIQYSSQVQSVFPLRAFSRREDME-RAIRDLVPLAQ 109
Cdd:cd01474   3 GHFDLYFVLDKSGSVAANWIE-IYDFVEQLVDRFN-SPG-LRFSFITFSTRATKILPLTDDSSAIIKGlEVLKKVTPSGQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 110 gTMTGLAIQYAMNVAFSVAEGARppeeRVPRVAVIVTDGRPQDRV----AEVAAQARARGIEIYAVGVQRADVGSLRAMA 185
Cdd:cd01474  80 -TYIHEGLENANEQIFNRNGGGR----ETVSVIIALTDGQLLLNGhkypEHEAKLSRKLGAIVYCVGVTDFLKSQLINIA 154

                       170
                ....*....|....*....
gi 13699836 186 SPPldEHVFLV-ESFDLIQ 203
Cdd:cd01474 155 DSK--EYVFPVtSGFQALS 171
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 259-420 1.10e-04

VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 43.10  E-value: 1.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 259 EGHVDLVLLVDGSKSVRPQNFELVKRFVNQIVDFLDVSP---EGTRVGLVQFSSRVRTEFPLgrygTAAEvKQAVLAVEy 335
Cdd:cd01464   1 MRRLPIYLLLDTSGSMAGEPIEALNQGLQMLQSELRQDPyalESVEISVITFDSAARVIVPL----TPLE-SFQPPRLT- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 336 MERGTMTGLALR---HMVEHSFSEAQGA-----RPralnvprvgLVF--TDGRSQDDISVWAARAKEEG---IVMYAVGV 402
Cdd:cd01464  75 ASGGTSMGAALElalDCIDRRVQRYRADqkgdwRP---------WVFllTDGEPTDDLTAAIERIKEARdskGRIVACAV 145

                       170
                ....*....|....*....
gi 13699836 403 GKAVEAE-LREIASEPAEL 420
Cdd:cd01464 146 GPKADLDtLKQITEGVPLL 164
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 263-414 1.23e-04

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 43.07  E-value: 1.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 263 DLVLLVDGSKSVRPQNFEL-VKRFVNQIVDFLDVSPEGTRVGLVQFSSRVRTEFPLG---RYgtaaEVKQAVLAVEYMER 338
Cdd:cd01473   2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSdeeRY----DKNELLKKINDLKN 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 339 GTMTGL------ALRHMVEHSFseaqGARPRALNVPRVGLVFTDG----RSQDDISVWAARAKEEGIVMYAVGVGKAVEA 408
Cdd:cd01473  78 SYRSGGetyiveALKYGLKNYT----KHGNRRKDAPKVTMLFTDGndtsASKKELQDISLLYKEENVKLLVVGVGAASEN 153


                ....*.
gi 13699836 409 ELREIA 414
Cdd:cd01473 154 KLKLLA 159
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 33-201 1.30e-04

VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 42.71  E-value: 1.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836  33 LDLVFVIDSSRSVRPFEFETMRQFLMGLLRGLNVGPNATR---VGVIQYSSQVQSVFPLrafsrrEDMERAIRDLVPLAQ 109
Cdd:cd01464   4 LPIYLLLDTSGSMAGEPIEALNQGLQMLQSELRQDPYALEsveISVITFDSAARVIVPL------TPLESFQPPRLTASG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836 110 GTMTGLAIQYAM-----NVAFSVAEGA---RPpeervprVAVIVTDGRPQDRV---AEVAAQARARGIEIYAVGV-QRAD 177
Cdd:cd01464  78 GTSMGAALELALdcidrRVQRYRADQKgdwRP-------WVFLLTDGEPTDDLtaaIERIKEARDSKGRIVACAVgPKAD 150

                       170       180
                ....*....|....*....|....*.
gi 13699836 178 VGSLRAMAS--PPLDEHVFLVESFDL 201
Cdd:cd01464 151 LDTLKQITEgvPLLDDALSGLNFFKW 176
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 33-172 7.12e-04

VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known.


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 40.07  E-value: 7.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13699836  33 LDLVFVIDSSRSVRPFEFETMRQFLMGLLRGLNvgpNATRVGVIQYSSQVQSVFPLR---AFSRREDmERAIRDLVPlAQ 109
Cdd:cd01466   1 VDLVAVLDVSGSMAGDKLQLVKHALRFVISSLG---DADRLSIVTFSTSAKRLSPLRrmtAKGKRSA-KRVVDGLQA-GG 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13699836 110 GTMTGLAIQYAMnvafSVAEGARppeERVPRVAVIV-TDGRPQDrvAEVAAQARARGIEIYAVG 172
Cdd:cd01466  76 GTNVVGGLKKAL----KVLGDRR---QKNPVASIMLlSDGQDNH--GAVVLRADNAPIPIHTFG 130
 
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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