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Conserved domains on  [gi|193787261|dbj|BAG52467|]
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unnamed protein product [Homo sapiens]

Protein Classification

vWA domain-containing protein( domain architecture ID 10107205)

vWA (von Willebrand factor type A) domain-containing protein similar to Homo sapiens collagen alpha-3(VI) chain isoform 2

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
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 37-201 3.76e-85

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: 271.50  E-value: 3.76e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   37 RDIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSAL 116
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  117 YTGSALDFVRNNLFTSSAGYRAAEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSSLVF 196
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                  ....*
gi 193787261  197 IPAEF 201
Cdd:cd01481   161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 231-395 8.64e-84

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: 268.04  E-value: 8.64e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  231 RDIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSGL 310
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  311 NTGSALSYVYANHFTEAGGSRIREHVPQLLLLLTAGQSEDSYLQAANALTRAGILTFCVGASQANKAELEQIAFNPSLVY 390
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                  ....*
gi 193787261  391 LMDDF 395
Cdd:cd01481   161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 825-987 2.95e-82

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: 263.80  E-value: 2.95e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  825 RDVVFLIDGSQSAGP-EFQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQI 903
Cdd:cd01481     1 KDIVFLIDGSDNVGSgNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  904 NVGNALEYVSRNIFKRPLGSRIEEGVPQFLVLISSGKSDDEVDDPAVELKQFGVAPFTI-ARNADQEELVKISLSPEYVF 982
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIgARNADLAELQQIAFDPSFVF 160


                  ....*
gi 193787261  983 SVSTF 987
Cdd:cd01481   161 QVSDF 165
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 621-784 1.91e-69

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 cd01481:

Pssm-ID: 469594  Cd Length: 165  Bit Score: 228.75  E-value: 1.91e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  621 KDVVFLLDGSEGVRS-GFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTP 699
Cdd:cd01481     1 KDIVFLIDGSDNVGSgNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  700 NTGAALEFVLRNILVSSAGSRITEGVPQLLIVLTADRSGDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPDFAV 779
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                  ....*
gi 193787261  780 AIPTF 784
Cdd:cd01481   161 QVSDF 165
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 429-592 3.14e-59

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 cd01481:

Pssm-ID: 469594  Cd Length: 165  Bit Score: 200.24  E-value: 3.14e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  429 RDILFLFDGSANL-VGQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKAL 507
Cdd:cd01481     1 KDIVFLIDGSDNVgSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  508 NLGYALDYAQRYIFVKSAGSRIEDGVLQFLVLLVAGRSSDRVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSPAFIL 587
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                  ....*
gi 193787261  588 AAESL 592
Cdd:cd01481   161 QVSDF 165
 
Name Accession Description Interval E-value
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 37-201 3.76e-85

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: 271.50  E-value: 3.76e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   37 RDIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSAL 116
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  117 YTGSALDFVRNNLFTSSAGYRAAEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSSLVF 196
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                  ....*
gi 193787261  197 IPAEF 201
Cdd:cd01481   161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 231-395 8.64e-84

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: 268.04  E-value: 8.64e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  231 RDIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSGL 310
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  311 NTGSALSYVYANHFTEAGGSRIREHVPQLLLLLTAGQSEDSYLQAANALTRAGILTFCVGASQANKAELEQIAFNPSLVY 390
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                  ....*
gi 193787261  391 LMDDF 395
Cdd:cd01481   161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 825-987 2.95e-82

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: 263.80  E-value: 2.95e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  825 RDVVFLIDGSQSAGP-EFQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQI 903
Cdd:cd01481     1 KDIVFLIDGSDNVGSgNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  904 NVGNALEYVSRNIFKRPLGSRIEEGVPQFLVLISSGKSDDEVDDPAVELKQFGVAPFTI-ARNADQEELVKISLSPEYVF 982
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIgARNADLAELQQIAFDPSFVF 160


                  ....*
gi 193787261  983 SVSTF 987
Cdd:cd01481   161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 621-784 1.91e-69

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: 228.75  E-value: 1.91e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  621 KDVVFLLDGSEGVRS-GFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTP 699
Cdd:cd01481     1 KDIVFLIDGSDNVGSgNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  700 NTGAALEFVLRNILVSSAGSRITEGVPQLLIVLTADRSGDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPDFAV 779
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                  ....*
gi 193787261  780 AIPTF 784
Cdd:cd01481   161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 429-592 3.14e-59

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: 200.24  E-value: 3.14e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  429 RDILFLFDGSANL-VGQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKAL 507
Cdd:cd01481     1 KDIVFLIDGSDNVgSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  508 NLGYALDYAQRYIFVKSAGSRIEDGVLQFLVLLVAGRSSDRVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSPAFIL 587
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                  ....*
gi 193787261  588 AAESL 592
Cdd:cd01481   161 QVSDF 165
VWA pfam00092
von Willebrand factor type A domain;
232-404 7.49e-54

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 185.17  E-value: 7.49e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   232 DIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSGLN 311
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   312 TGSALSYVYANHFTEAGGSriREHVPQLLLLLTAGQSED-SYLQAANALTRAGILTFCVGASQANKAELEQIAFNPS--L 388
Cdd:pfam00092   81 TGKALKYALENLFSSAAGA--RPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158

                          170
                   ....*....|....*.
gi 193787261   389 VYLMDDFSSLPALPQQ 404
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
826-996 3.12e-50

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 175.16  E-value: 3.12e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   826 DVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQIN 904
Cdd:pfam00092    1 DIVFLLDGSGSIGGDnFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   905 VGNALEYVSRNIFKRPLGSRieEGVPQFLVLISSGKSDD-EVDDPAVELKQFGVAPFTIA-RNADQEELVKISLSP--EY 980
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGvGNADDEELRKIASEPgeGH 158

                          170
                   ....*....|....*.
gi 193787261   981 VFSVSTFRELPSLEQK 996
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
38-205 1.16e-49

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 173.23  E-value: 1.16e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261    38 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSALY 117
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   118 TGSALDFVRNNLFTSSAGYRaaEGIPKLLVLITGGKSLD-EISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSS--L 194
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158

                          170
                   ....*....|.
gi 193787261   195 VFIPAEFRAAP 205
Cdd:pfam00092  159 VFTVSDFEALE 169
VWA pfam00092
von Willebrand factor type A domain;
622-792 1.38e-49

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 173.23  E-value: 1.38e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   622 DVVFLLDGSEGVR-SGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTPN 700
Cdd:pfam00092    1 DIVFLLDGSGSIGgDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   701 TGAALEFVLRNILVSSAGSRitEGVPQLLIVLTADRSGD-DVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPD--F 777
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158

                          170
                   ....*....|....*
gi 193787261   778 AVAIPTFRQLGTVQQ 792
Cdd:pfam00092  159 VFTVSDFEALEDLQD 173
VWA pfam00092
von Willebrand factor type A domain;
430-601 1.36e-40

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 147.42  E-value: 1.36e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   430 DILFLFDGSANL-VGQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKALN 508
Cdd:pfam00092    1 DIVFLLDGSGSIgGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   509 LGYALDYAQRYIFVKSAGSRIedGVLQFLVLLVAGRSSD-RVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSPA--F 585
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARP--GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158

                          170
                   ....*....|....*.
gi 193787261   586 ILAAESLPKIGDLHPQ 601
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 232-390 3.07e-40

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: 146.45  E-value: 3.07e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261    232 DIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSGLN 311
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261    312 TGSALSYVYANHFTEAGGSriREHVPQLLLLLTAGQSEDS---YLQAANALTRAGILTFCVGASQA-NKAELEQIAFNPS 387
Cdd:smart00327   81 LGAALQYALENLFSKSAGS--RRGAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPG 158


                    ...
gi 193787261    388 LVY 390
Cdd:smart00327  159 GVY 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 826-993 1.16e-38

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: 141.82  E-value: 1.16e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261    826 DVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQIN 904
Cdd:smart00327    1 DVVFLLDGSGSMGGNrFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261    905 VGNALEYVSRNIFKRPLGSRieEGVPQFLVLISSGKSDD---EVDDPAVELKQFGVAPFTIA--RNADQEELVKISLSP- 978
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGvgNDVDEEELKKLASAPg 158

                           170
                    ....*....|....*.
gi 193787261    979 -EYVFSVSTFRELPSL 993
Cdd:smart00327  159 gVYVFLPELLDLLIDL 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 38-210 7.10e-38

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: 139.90  E-value: 7.10e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261     38 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSALY 117
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261    118 TGSALDFVRNNLFTSSAGYRaaEGIPKLLVLITGGKSLD---EISQPAQELKRSSIMAFAIG-NKGADQAELEEIAFDSS 193
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGvGNDVDEEELKKLASAPG 158

                           170
                    ....*....|....*..
gi 193787261    194 LVFIPAEFRAAPLQGML 210
Cdd:smart00327  159 GVYVFLPELLDLLIDLL 175
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 622-780 1.39e-34

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: 130.27  E-value: 1.39e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261    622 DVVFLLDGSEGVR-SGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTPN 700
Cdd:smart00327    1 DVVFLLDGSGSMGgNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261    701 TGAALEFVLRNILVSSAGSRitEGVPQLLIVLTADRSGD---DVRNPSVVVKRGGAVPIGIGIGNA-DITEMQTISFIPD 776
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPG 158


                    ....
gi 193787261    777 FAVA 780
Cdd:smart00327  159 GVYV 162
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 430-585 2.63e-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: 2.63e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261    430 DILFLFDGSANLVGQ-FPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKALN 508
Cdd:smart00327    1 DVVFLLDGSGSMGGNrFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261    509 LGYALDYAQRYIFVKSAGSRieDGVLQFLVLLVAGRSSD---RVDGPASNLKQSGVVPFIFQAKNA-DPAELEQIVLSPA 584
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPG 158


                    .
gi 193787261    585 F 585
Cdd:smart00327  159 G 159
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 809-975 5.11e-10

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: 61.49  E-value: 5.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  809 LQPVLQPLPSPGVGGKRDVVFLID--GSQSAGPEFQYVRTLIERLVDYLDvgfDTTRVAVIQFSDDPKVefLLNAHSSKD 886
Cdd:COG1240    77 LALALAPLALARPQRGRDVVLVVDasGSMAAENRLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEV--LLPLTRDRE 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  887 EVQNAVQRLRPKGGRQInvGNALeYVSRNIFKrplgsRIEEGVPQFLVLISSGKSDDEVDDP---AVELKQFGVAPFTIA 963
Cdd:COG1240   152 ALKRALDELPPGGGTPL--GDAL-ALALELLK-----RADPARRKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIG 223

                         170
                  ....*....|....*
gi 193787261  964 ---RNADQEELVKIS 975
Cdd:COG1240   224 vgtEAVDEGLLREIA 238
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 160-383 3.50e-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: 55.71  E-value: 3.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  160 QPAQELKRSSIMAFAIGNKGADQAELEEIAFDSSLVFIPAEFRAAPLQGMLPGLLAPLRTLSGTPEVHSNKRDIIFLLDG 239
Cdd:COG1240    22 LLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  240 SANVGKTN-FPYVRDFVMNLVNSLDignDNIRVGLVQFSDTPVTEFSLnTYQtKSDILGHLRQLQLQGGSglNTGSALSY 318
Cdd:COG1240   102 SGSMAAENrLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEVLLPL-TRD-REALKRALDELPPGGGT--PLGDALAL 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  319 VYaNHFTEAGGSRIRehvpqLLLLLTAGQ---SEDSYLQAANALTRAGILTFCV--GASQANKAELEQIA 383
Cdd:COG1240   175 AL-ELLKRADPARRK-----VIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIgvGTEAVDEGLLREIA 238
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 37-189 9.81e-06

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: 48.40  E-value: 9.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   37 RDIVFLVDGS-SALGLANFNAIRDFIAKVIQRLEIGQdliQVAVAQYADTVrpefYFNTHPT--KREVITAVRKMKPLDG 113
Cdd:COG1240    93 RDVVLVVDASgSMAAENRLEAAKGALLDFLDDYRPRD---RVGLVAFGGEA----EVLLPLTrdREALKRALDELPPGGG 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  114 SALYTG--SALDFVRnnlftssagyRAAEGIPKLLVLITGGK---SLDEISQPAQELKRSSIMAFAI--GNKGADQAELE 186
Cdd:COG1240   166 TPLGDAlaLALELLK----------RADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIgvGTEAVDEGLLR 235


                  ...
gi 193787261  187 EIA 189
Cdd:COG1240   236 EIA 238
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 613-772 1.21e-03

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 41.85  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  613 APAPVSGEKDVVFLLD--GSEGVRSGFPLLKEFVQRVVESLdvgQDRVRVAVVQYSDRTRPEFYLNSymNKQDVVNAVRQ 690
Cdd:COG1240    85 ALARPQRGRDVVLVVDasGSMAAENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTR--DREALKRALDE 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  691 LTLLGGpTPnTGAALEfvlrniLVSSAGSRITEGVPQLLIVLT---ADRSGDDVRNPSVVVKRGGA--VPIGIGIGNADI 765
Cdd:COG1240   160 LPPGGG-TP-LGDALA------LALELLKRADPARRKVIVLLTdgrDNAGRIDPLEAAELAAAAGIriYTIGVGTEAVDE 231


                  ....*..
gi 193787261  766 TEMQTIS 772
Cdd:COG1240   232 GLLREIA 238
 
Name Accession Description Interval E-value
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 37-201 3.76e-85

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: 271.50  E-value: 3.76e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   37 RDIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSAL 116
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  117 YTGSALDFVRNNLFTSSAGYRAAEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSSLVF 196
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                  ....*
gi 193787261  197 IPAEF 201
Cdd:cd01481   161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 231-395 8.64e-84

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: 268.04  E-value: 8.64e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  231 RDIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSGL 310
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  311 NTGSALSYVYANHFTEAGGSRIREHVPQLLLLLTAGQSEDSYLQAANALTRAGILTFCVGASQANKAELEQIAFNPSLVY 390
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                  ....*
gi 193787261  391 LMDDF 395
Cdd:cd01481   161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 825-987 2.95e-82

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: 263.80  E-value: 2.95e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  825 RDVVFLIDGSQSAGP-EFQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQI 903
Cdd:cd01481     1 KDIVFLIDGSDNVGSgNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  904 NVGNALEYVSRNIFKRPLGSRIEEGVPQFLVLISSGKSDDEVDDPAVELKQFGVAPFTI-ARNADQEELVKISLSPEYVF 982
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIgARNADLAELQQIAFDPSFVF 160


                  ....*
gi 193787261  983 SVSTF 987
Cdd:cd01481   161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 621-784 1.91e-69

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: 228.75  E-value: 1.91e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  621 KDVVFLLDGSEGVRS-GFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTP 699
Cdd:cd01481     1 KDIVFLIDGSDNVGSgNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  700 NTGAALEFVLRNILVSSAGSRITEGVPQLLIVLTADRSGDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPDFAV 779
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                  ....*
gi 193787261  780 AIPTF 784
Cdd:cd01481   161 QVSDF 165
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 37-201 4.97e-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: 205.15  E-value: 4.97e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   37 RDIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLdGSAL 116
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYI-GGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  117 YTGSALDFVRNNLFTSSAgyRAAEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIAFD--SSL 194
Cdd:cd01472    80 NTGKALKYVRENLFTEAS--GSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDpkELY 157


                  ....*..
gi 193787261  195 VFIPAEF 201
Cdd:cd01472   158 VFNVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 825-987 1.03e-60

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: 204.38  E-value: 1.03e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  825 RDVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGrQI 903
Cdd:cd01472     1 ADIVFLVDGSESIGLSnFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGG-GT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  904 NVGNALEYVSRNIFKRPlgSRIEEGVPQFLVLISSGKSDDEVDDPAVELKQFGVAPFTIA-RNADQEELVKISLSP--EY 980
Cdd:cd01472    80 NTGKALKYVRENLFTEA--SGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGvKNADEEELKQIASDPkeLY 157


                  ....*..
gi 193787261  981 VFSVSTF 987
Cdd:cd01472   158 VFNVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 231-395 4.35e-60

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: 202.46  E-value: 4.35e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  231 RDIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGsGL 310
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGG-GT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  311 NTGSALSYVYANHFTEAggSRIREHVPQLLLLLTAGQSEDSYLQAANALTRAGILTFCVGASQANKAELEQIAFNP--SL 388
Cdd:cd01472    80 NTGKALKYVRENLFTEA--SGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPkeLY 157


                  ....*..
gi 193787261  389 VYLMDDF 395
Cdd:cd01472   158 VFNVADF 164
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 429-592 3.14e-59

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: 200.24  E-value: 3.14e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  429 RDILFLFDGSANL-VGQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKAL 507
Cdd:cd01481     1 KDIVFLIDGSDNVgSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  508 NLGYALDYAQRYIFVKSAGSRIEDGVLQFLVLLVAGRSSDRVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSPAFIL 587
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                  ....*
gi 193787261  588 AAESL 592
Cdd:cd01481   161 QVSDF 165
VWA pfam00092
von Willebrand factor type A domain;
232-404 7.49e-54

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 185.17  E-value: 7.49e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   232 DIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSGLN 311
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   312 TGSALSYVYANHFTEAGGSriREHVPQLLLLLTAGQSED-SYLQAANALTRAGILTFCVGASQANKAELEQIAFNPS--L 388
Cdd:pfam00092   81 TGKALKYALENLFSSAAGA--RPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158

                          170
                   ....*....|....*.
gi 193787261   389 VYLMDDFSSLPALPQQ 404
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 621-775 1.93e-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: 178.19  E-value: 1.93e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  621 KDVVFLLDGSEGV-RSGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTp 699
Cdd:cd01472     1 ADIVFLVDGSESIgLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGT- 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193787261  700 NTGAALEFVLRNILVSSAGSRitEGVPQLLIVLTADRSGDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIP 775
Cdd:cd01472    80 NTGKALKYVRENLFTEASGSR--EGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDP 153
VWA pfam00092
von Willebrand factor type A domain;
826-996 3.12e-50

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 175.16  E-value: 3.12e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   826 DVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQIN 904
Cdd:pfam00092    1 DIVFLLDGSGSIGGDnFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   905 VGNALEYVSRNIFKRPLGSRieEGVPQFLVLISSGKSDD-EVDDPAVELKQFGVAPFTIA-RNADQEELVKISLSP--EY 980
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGvGNADDEELRKIASEPgeGH 158

                          170
                   ....*....|....*.
gi 193787261   981 VFSVSTFRELPSLEQK 996
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
38-205 1.16e-49

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 173.23  E-value: 1.16e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261    38 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSALY 117
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   118 TGSALDFVRNNLFTSSAGYRaaEGIPKLLVLITGGKSLD-EISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSS--L 194
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158

                          170
                   ....*....|.
gi 193787261   195 VFIPAEFRAAP 205
Cdd:pfam00092  159 VFTVSDFEALE 169
VWA pfam00092
von Willebrand factor type A domain;
622-792 1.38e-49

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 173.23  E-value: 1.38e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   622 DVVFLLDGSEGVR-SGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTPN 700
Cdd:pfam00092    1 DIVFLLDGSGSIGgDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   701 TGAALEFVLRNILVSSAGSRitEGVPQLLIVLTADRSGD-DVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPD--F 777
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158

                          170
                   ....*....|....*
gi 193787261   778 AVAIPTFRQLGTVQQ 792
Cdd:pfam00092  159 VFTVSDFEALEDLQD 173
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 232-391 1.36e-46

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: 164.00  E-value: 1.36e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  232 DIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSGLN 311
Cdd:cd01450     2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGTN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  312 TGSALSYVYANHFTEaggSRIREHVPQLLLLLTAGQSEDSY--LQAANALTRAGILTFCVGASQANKAELEQIAFNPSLV 389
Cdd:cd01450    82 TGKALQYALEQLFSE---SNARENVPKVIIVLTDGRSDDGGdpKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSER 158


                  ..
gi 193787261  390 YL 391
Cdd:cd01450   159 HV 160
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 38-201 1.28e-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: 161.30  E-value: 1.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   38 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMkPLDGSALY 117
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNL-PYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  118 TGSALDFVRNNLFTSSAGYRaaEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSSL--V 195
Cdd:cd01482    81 TGKALTHVREKNFTPDAGAR--PGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSEthV 158


                  ....*.
gi 193787261  196 FIPAEF 201
Cdd:cd01482   159 FNVADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 232-395 1.61e-43

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: 1.61e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  232 DIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGsGLN 311
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGG-NTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  312 TGSALSYVYANHFTEAGGSriREHVPQLLLLLTAGQSEDSYLQAANALTRAGILTFCVGASQANKAELEQIAFNPSL--V 389
Cdd:cd01482    81 TGKALTHVREKNFTPDAGA--RPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSEthV 158


                  ....*.
gi 193787261  390 YLMDDF 395
Cdd:cd01482   159 FNVADF 164
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 38-193 3.93e-43

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: 154.37  E-value: 3.93e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   38 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSALY 117
Cdd:cd01450     2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGTN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193787261  118 TGSALDFVRNNLFTSSagyRAAEGIPKLLVLITGGKSLD--EISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSS 193
Cdd:cd01450    82 TGKALQYALEQLFSES---NARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 429-583 1.98e-42

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: 152.38  E-value: 1.98e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  429 RDILFLFDGSANlVGQ--FPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKtGKA 506
Cdd:cd01472     1 ADIVFLVDGSES-IGLsnFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYI-GGG 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193787261  507 LNLGYALDYAQRYIFVKSagSRIEDGVLQFLVLLVAGRSSDRVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSP 583
Cdd:cd01472    79 TNTGKALKYVRENLFTEA--SGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDP 153
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 826-982 1.27e-41

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: 149.75  E-value: 1.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  826 DVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQIN 904
Cdd:cd01450     2 DIVFLLDGSESVGPEnFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGTN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  905 VGNALEYVSRNIFKrplGSRIEEGVPQFLVLISSGKSDDEVD--DPAVELKQFGVAPFTIA-RNADQEELVKISLSP--E 979
Cdd:cd01450    82 TGKALQYALEQLFS---ESNARENVPKVIIVLTDGRSDDGGDpkEAAAKLKDEGIKVFVVGvGPADEEELREIASCPseR 158


                  ...
gi 193787261  980 YVF 982
Cdd:cd01450   159 HVF 161
VWA pfam00092
von Willebrand factor type A domain;
430-601 1.36e-40

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 147.42  E-value: 1.36e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   430 DILFLFDGSANL-VGQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKALN 508
Cdd:pfam00092    1 DIVFLLDGSGSIgGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   509 LGYALDYAQRYIFVKSAGSRIedGVLQFLVLLVAGRSSD-RVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSPA--F 585
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARP--GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158

                          170
                   ....*....|....*.
gi 193787261   586 ILAAESLPKIGDLHPQ 601
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 232-390 3.07e-40

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: 146.45  E-value: 3.07e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261    232 DIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSGLN 311
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261    312 TGSALSYVYANHFTEAGGSriREHVPQLLLLLTAGQSEDS---YLQAANALTRAGILTFCVGASQA-NKAELEQIAFNPS 387
Cdd:smart00327   81 LGAALQYALENLFSKSAGS--RRGAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPG 158


                    ...
gi 193787261    388 LVY 390
Cdd:smart00327  159 GVY 161
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 826-987 1.52e-39

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: 143.97  E-value: 1.52e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  826 DVVFLIDGSQSAG-PEFQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQiN 904
Cdd:cd01482     2 DIVFLVDGSWSIGrSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT-R 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  905 VGNALEYVSRNIFKRPLGSRieEGVPQFLVLISSGKSDDEVDDPAVELKQFGVAPFTIA-RNADQEELVKISLSP--EYV 981
Cdd:cd01482    81 TGKALTHVREKNFTPDAGAR--PGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGvKDADESELKMIASKPseTHV 158


                  ....*.
gi 193787261  982 FSVSTF 987
Cdd:cd01482   159 FNVADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 622-776 5.34e-39

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: 142.43  E-value: 5.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  622 DVVFLLDGSEGV-RSGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTpN 700
Cdd:cd01482     2 DIVFLVDGSWSIgRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT-R 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193787261  701 TGAALEFVLRNILVSSAGSRitEGVPQLLIVLTADRSGDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPD 776
Cdd:cd01482    81 TGKALTHVREKNFTPDAGAR--PGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPS 154
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 622-776 8.59e-39

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: 141.66  E-value: 8.59e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  622 DVVFLLDGSEGVRS-GFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTPN 700
Cdd:cd01450     2 DIVFLLDGSESVGPeNFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGTN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193787261  701 TGAALEFVLRNILVSSAGSritEGVPQLLIVLTADRS--GDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPD 776
Cdd:cd01450    82 TGKALQYALEQLFSESNAR---ENVPKVIIVLTDGRSddGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 826-993 1.16e-38

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: 141.82  E-value: 1.16e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261    826 DVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQIN 904
Cdd:smart00327    1 DVVFLLDGSGSMGGNrFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261    905 VGNALEYVSRNIFKRPLGSRieEGVPQFLVLISSGKSDD---EVDDPAVELKQFGVAPFTIA--RNADQEELVKISLSP- 978
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGvgNDVDEEELKKLASAPg 158

                           170
                    ....*....|....*.
gi 193787261    979 -EYVFSVSTFRELPSL 993
Cdd:smart00327  159 gVYVFLPELLDLLIDL 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 38-210 7.10e-38

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: 139.90  E-value: 7.10e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261     38 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSALY 117
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261    118 TGSALDFVRNNLFTSSAGYRaaEGIPKLLVLITGGKSLD---EISQPAQELKRSSIMAFAIG-NKGADQAELEEIAFDSS 193
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGvGNDVDEEELKKLASAPG 158

                           170
                    ....*....|....*..
gi 193787261    194 LVFIPAEFRAAPLQGML 210
Cdd:smart00327  159 GVYVFLPELLDLLIDLL 175
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 622-780 1.39e-34

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: 130.27  E-value: 1.39e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261    622 DVVFLLDGSEGVR-SGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTPN 700
Cdd:smart00327    1 DVVFLLDGSGSMGgNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261    701 TGAALEFVLRNILVSSAGSRitEGVPQLLIVLTADRSGD---DVRNPSVVVKRGGAVPIGIGIGNA-DITEMQTISFIPD 776
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPG 158


                    ....
gi 193787261    777 FAVA 780
Cdd:smart00327  159 GVYV 162
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 430-583 1.50e-32

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: 123.94  E-value: 1.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  430 DILFLFDGSANlVGQ--FPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKAL 507
Cdd:cd01450     2 DIVFLLDGSES-VGPenFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193787261  508 NLGYALDYAQRYIFVKsagSRIEDGVLQFLVLLVAGRSSDRVDG--PASNLKQSGVVPFIFQAKNADPAELEQIVLSP 583
Cdd:cd01450    81 NTGKALQYALEQLFSE---SNARENVPKVIIVLTDGRSDDGGDPkeAAAKLKDEGIKVFVVGVGPADEEELREIASCP 155
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 232-405 2.42e-32

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: 125.58  E-value: 2.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  232 DIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQgGSGLN 311
Cdd:cd01475     4 DLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYL-ETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  312 TGSALSYVYANHFTEAGGSR-IREHVPQLLLLLTAGQSEDSYLQAANALTRAGILTFCVGASQANKAELEQIAFNPSL-- 388
Cdd:cd01475    83 TGLAIQYAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAdh 162

                         170
                  ....*....|....*..
gi 193787261  389 VYLMDDFSSLPALPQQL 405
Cdd:cd01475   163 VFYVEDFSTIEELTKKF 179
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 38-189 1.17e-31

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: 123.65  E-value: 1.17e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   38 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLdGSALY 117
Cdd:cd01475     4 DLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYL-ETGTM 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193787261  118 TGSALDFVRNNLFTSSAGYR-AAEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIA 189
Cdd:cd01475    83 TGLAIQYAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIA 155
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 430-584 8.58e-30

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: 116.23  E-value: 8.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  430 DILFLFDGSANlVGQ--FPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKAl 507
Cdd:cd01482     2 DIVFLVDGSWS-IGRsnFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT- 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193787261  508 NLGYALDYAQRYIFVKSAGSRieDGVLQFLVLLVAGRSSDRVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSPA 584
Cdd:cd01482    80 RTGKALTHVREKNFTPDAGAR--PGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPS 154
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 430-585 2.63e-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: 2.63e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261    430 DILFLFDGSANLVGQ-FPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKALN 508
Cdd:smart00327    1 DVVFLLDGSGSMGGNrFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261    509 LGYALDYAQRYIFVKSAGSRieDGVLQFLVLLVAGRSSD---RVDGPASNLKQSGVVPFIFQAKNA-DPAELEQIVLSPA 584
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPG 158


                    .
gi 193787261    585 F 585
Cdd:smart00327  159 G 159
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 622-771 5.15e-28

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: 113.25  E-value: 5.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  622 DVVFLLDGSEGVR-SGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTpN 700
Cdd:cd01475     4 DLVFLIDSSRSVRpENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT-M 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193787261  701 TGAALEFVLRNILVSSAGSR-ITEGVPQLLIVLTADRSGDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTI 771
Cdd:cd01475    83 TGLAIQYAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREI 154
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 826-997 1.28e-26

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: 109.01  E-value: 1.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  826 DVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKgGRQIN 904
Cdd:cd01475     4 DLVFLIDSSRSVRPEnFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYL-ETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  905 VGNALEYVSRNIFKRPLGSR-IEEGVPQFLVLISSGKSDDEVDDPAVELKQFGVAPFTIA-RNADQEELVKISLSP--EY 980
Cdd:cd01475    83 TGLAIQYAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGvGRADEEELREIASEPlaDH 162

                         170
                  ....*....|....*..
gi 193787261  981 VFSVSTFRELPSLEQKL 997
Cdd:cd01475   163 VFYVEDFSTIEELTKKF 179
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 231-383 8.98e-26

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: 104.57  E-value: 8.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  231 RDIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSGL 310
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193787261  311 NTGSALSYVYANHFteaggSRIREHVPQLLLLLTAGQSEDSY---LQAANALTRAGILTFCVG-ASQANKAELEQIA 383
Cdd:cd00198    81 NIGAALRLALELLK-----SAKRPNARRVIILLTDGEPNDGPellAEAARELRKLGITVYTIGiGDDANEDELKEIA 152
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 232-398 2.76e-24

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: 100.89  E-value: 2.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  232 DIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSgLN 311
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGL-TN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  312 TGSALSYVYANHFTEAGGSriREHVPQLLLLLTAGQSEDSYL--QAANALTRAGILTFCVG---ASQANKA--ELEQIAF 384
Cdd:cd01469    81 TATAIQYVVTELFSESNGA--RKDATKVLVVITDGESHDDPLlkDVIPQAEREGIIRYAIGvggHFQRENSreELKTIAS 158

                         170
                  ....*....|....*.
gi 193787261  385 NPS--LVYLMDDFSSL 398
Cdd:cd01469   159 KPPeeHFFNVTDFAAL 174
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 825-984 4.29e-24

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: 99.56  E-value: 4.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  825 RDVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQI 903
Cdd:cd00198     1 ADIVFLLDVSGSMGGEkLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  904 NVGNALEYVSRNIFKRPLGSRieegvPQFLVLISSGKSDD---EVDDPAVELKQFGVAPFTIA--RNADQEELVKISLSP 978
Cdd:cd00198    81 NIGAALRLALELLKSAKRPNA-----RRVIILLTDGEPNDgpeLLAEAARELRKLGITVYTIGigDDANEDELKEIADKT 155


                  ....*.
gi 193787261  979 EYVFSV 984
Cdd:cd00198   156 TGGAVF 161
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 38-188 7.32e-24

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: 99.74  E-value: 7.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   38 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSAlY 117
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLT-N 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193787261  118 TGSALDFVRNNLFTSSAGYRaaEGIPKLLVLITGGKSLD--EISQPAQELKRSSIMAFAIGNKGADQAE--LEEI 188
Cdd:cd01469    81 TATAIQYVVTELFSESNGAR--KDATKVLVVITDGESHDdpLLKDVIPQAEREGIIRYAIGVGGHFQREnsREEL 153
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 621-751 4.18e-23

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: 97.08  E-value: 4.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  621 KDVVFLLDGSEGVRSGFPLLKEFVQRVVESLDVGQDRVRVAVVQYS--DRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPT 698
Cdd:cd01476     1 LDLLFVLDSSGSVRGKFEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 193787261  699 pNTGAALEFVLrNILVSSAGSRitEGVPQLLIVLTADRSGDDVRNPSVVVKRG 751
Cdd:cd01476    81 -ATGAAIEVAL-QQLDPSEGRR--EGIPKVVVVLTDGRSHDDPEKQARILRAV 129
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 826-993 6.99e-23

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: 96.66  E-value: 6.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  826 DVVFLIDGSQSAGP-EFQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQiN 904
Cdd:cd01469     2 DIVFVLDGSGSIYPdDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLT-N 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  905 VGNALEYVSRNIFKRPLGSRieEGVPQFLVLISSGKSDDEVDDPAV--ELKQFGVAPFTIA------RNADQEELVKISL 976
Cdd:cd01469    81 TATAIQYVVTELFSESNGAR--KDATKVLVVITDGESHDDPLLKDVipQAEREGIIRYAIGvgghfqRENSREELKTIAS 158

                         170
                  ....*....|....*....
gi 193787261  977 SP--EYVFSVSTFRELPSL 993
Cdd:cd01469   159 KPpeEHFFNVTDFAALKDI 177
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 232-399 4.46e-22

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: 94.76  E-value: 4.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  232 DIIFLLDGSANVGKTN-FPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTY-----QTKSDILGHLRQLQLQ 305
Cdd:cd01471     2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPnstnkDLALNAIRALLSLYYP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  306 GGSgLNTGSALSYVYANHFTEAGGsriREHVPQLLLLLTAGQSEDSY--LQAANALTRAG--ILTFCVGASqANKAEleq 381
Cdd:cd01471    82 NGS-TNTTSALLVVEKHLFDTRGN---RENAPQLVIIMTDGIPDSKFrtLKEARKLRERGviIAVLGVGQG-VNHEE--- 153

                         170
                  ....*....|....*...
gi 193787261  382 iafNPSLVYLMDDFSSLP 399
Cdd:cd01471   154 ---NRSLVGCDPDDSPCP 168
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 622-776 1.38e-21

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: 93.19  E-value: 1.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  622 DVVFLLDGSEGVR-SGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTpN 700
Cdd:cd01469     2 DIVFVLDGSGSIYpDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLT-N 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  701 TGAALEFVLRNILVSSAGSRitEGVPQLLIVLTADRSGDDVRNPSVV--VKRGGAVPIGIGIGNA-----DITEMQTISF 773
Cdd:cd01469    81 TATAIQYVVTELFSESNGAR--KDATKVLVVITDGESHDDPLLKDVIpqAEREGIIRYAIGVGGHfqrenSREELKTIAS 158


                  ...
gi 193787261  774 IPD 776
Cdd:cd01469   159 KPP 161
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 37-189 4.49e-20

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: 88.39  E-value: 4.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   37 RDIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSAL 116
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193787261  117 YTGSALDFVRNNLFTssagyRAAEGIPKLLVLITGGKSLD---EISQPAQELKRSSIMAFAIG-NKGADQAELEEIA 189
Cdd:cd00198    81 NIGAALRLALELLKS-----AKRPNARRVIILLTDGEPNDgpeLLAEAARELRKLGITVYTIGiGDDANEDELKEIA 152
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 38-198 9.48e-20

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: 87.45  E-value: 9.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   38 DIVFLVDGSSALGlANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYA--DTVRPEFYFNTHPTKREVITAVRKMKPLDGSA 115
Cdd:cd01476     2 DLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  116 lYTGSALDFVrNNLFTSSAGYRaaEGIPKLLVLITGGKSLDEISQPAQELKR---SSIMAFAIGNKGA-DQAELEEIAFD 191
Cdd:cd01476    81 -ATGAAIEVA-LQQLDPSEGRR--EGIPKVVVVLTDGRSHDDPEKQARILRAvpnIETFAVGTGDPGTvDTEELHSITGN 156


                  ....*..
gi 193787261  192 SSLVFIP 198
Cdd:cd01476   157 EDHIFTD 163
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 622-772 2.50e-19

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: 86.08  E-value: 2.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  622 DVVFLLDGSEGVRSG-FPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTPN 700
Cdd:cd00198     2 DIVFLLDVSGSMGGEkLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGTN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193787261  701 TGAALEFVLRNILvssagSRITEGVPQLLIVLT---ADRSGDDVRNPSVVVKRGGAVPIGIGIGN-ADITEMQTIS 772
Cdd:cd00198    82 IGAALRLALELLK-----SAKRPNARRVIILLTdgePNDGPELLAEAARELRKLGITVYTIGIGDdANEDELKEIA 152
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 826-982 4.20e-18

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: 82.45  E-value: 4.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  826 DVVFLIDGSQSAGPEFQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPK--VEFLLNAHSSKDEVQNAVQRLRPKGGrQI 903
Cdd:cd01476     2 DLLFVLDSSGSVRGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGG-TT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  904 NVGNALEYVSrNIFKRPLGSRieEGVPQFLVLISSGKSDDEVDDPAVELK-QFGVAPFTIAR----NADQEELVKISLSP 978
Cdd:cd01476    81 ATGAAIEVAL-QQLDPSEGRR--EGIPKVVVVLTDGRSHDDPEKQARILRaVPNIETFAVGTgdpgTVDTEELHSITGNE 157


                  ....
gi 193787261  979 EYVF 982
Cdd:cd01476   158 DHIF 161
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 430-583 1.11e-17

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: 83.20  E-value: 1.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  430 DILFLFDGSANLVGQ-FPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMK-IKTGKAl 507
Cdd:cd01475     4 DLVFLIDSSRSVRPEnFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEyLETGTM- 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193787261  508 nLGYALDYAQRYIFVKSAGSR-IEDGVLQFLVLLVAGRSSDRVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSP 583
Cdd:cd01475    83 -TGLAIQYAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEP 158
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 232-386 9.29e-16

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: 75.90  E-value: 9.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  232 DIIFLLDGSANVGKTnFPYVRDFVMNLVNSLDIGNDNIRVGLVQFS--DTPVTEFSLNTYQTKSDILGHLRQLQLQGGSg 309
Cdd:cd01476     2 DLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGT- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  310 LNTGSALSYVyANHFTEAGGSriREHVPQLLLLLTAGQSEDSYLQAANALTR-AGILTFCVGA---SQANKAELEQIAFN 385
Cdd:cd01476    80 TATGAAIEVA-LQQLDPSEGR--REGIPKVVVVLTDGRSHDDPEKQARILRAvPNIETFAVGTgdpGTVDTEELHSITGN 156


                  .
gi 193787261  386 P 386
Cdd:cd01476   157 E 157
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 429-580 2.75e-13

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: 68.75  E-value: 2.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  429 RDILFLFDGSANLVGQ-FPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKAL 507
Cdd:cd00198     1 ADIVFLLDVSGSMGGEkLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193787261  508 NLGYALDYAQRYIFvksagSRIEDGVLQFLVLLVAGRSSDRVDGP---ASNLKQSGVVPFIFQAKN-ADPAELEQIV 580
Cdd:cd00198    81 NIGAALRLALELLK-----SAKRPNARRVIILLTDGEPNDGPELLaeaARELRKLGITVYTIGIGDdANEDELKEIA 152
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 622-758 5.38e-13

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: 68.57  E-value: 5.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  622 DVVFLLDGSEGV-RSGFPLLKEFVQRVVESL------DVGQDRVRVAVVQYSDRTRPEF-YLNSYMNKQDVVNAVRQLTL 693
Cdd:cd01480     4 DITFVLDSSESVgLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNLEY 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193787261  694 LGGPTpNTGAALEFVLRNILVSSAGsriteGVPQLLIVLTADRS-GDDVRNPSVVVKRGGAVPIGI 758
Cdd:cd01480    84 IGGGT-FTDCALKYATEQLLEGSHQ-----KENKFLLVITDGHSdGSPDGGIEKAVNEADHLGIKI 143
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 232-398 9.54e-13

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: 67.80  E-value: 9.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  232 DIIFLLDGSANVGKTNFPYVRDFVMNLVNSL------DIGNDNIRVGLVQFSDTPVTEF-SLNTYQTKSDILGHLRQLQL 304
Cdd:cd01480     4 DITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNLEY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  305 QGGsGLNTGSALSYVYanhfteaggSRIREHVPQL----LLLLTAGQS----EDSYLQAANALTRAGILTFCVGASQANK 376
Cdd:cd01480    84 IGG-GTFTDCALKYAT---------EQLLEGSHQKenkfLLVITDGHSdgspDGGIEKAVNEADHLGIKIFFVAVGSQNE 153

                         170       180
                  ....*....|....*....|..
gi 193787261  377 AELEQIAFNPSLVYLMDDFSSL 398
Cdd:cd01480   154 EPLSRIACDGKSALYRENFAEL 175
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 622-761 9.63e-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: 67.80  E-value: 9.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  622 DVVFLLD--GSEGVRSGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSY--MNKQ---DVVNAVRQLTLL 694
Cdd:cd01471     2 DLYLLVDgsGSIGYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPnsTNKDlalNAIRALLSLYYP 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193787261  695 GGPTpNTGAALEFVlRNILVSSAGSRitEGVPQLLIVLTADRSGDDVRNPSVVVK---RGGAVP-IGIGIG 761
Cdd:cd01471    82 NGST-NTTSALLVV-EKHLFDTRGNR--ENAPQLVIIMTDGIPDSKFRTLKEARKlreRGVIIAvLGVGQG 148
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 38-182 7.79e-12

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: 65.10  E-value: 7.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   38 DIVFLVDGSSALGLANFNAIRDFIAKVIQRL------EIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVIT-AVRKMKP 110
Cdd:cd01480     4 DITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTSLKeAVDNLEY 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193787261  111 LDGsALYTGSALDFVRNNLFTSSAGyraaeGIPKLLVLITGGKSLDE----ISQPAQELKRSSI--MAFAIGNKGADQ 182
Cdd:cd01480    84 IGG-GTFTDCALKYATEQLLEGSHQ-----KENKFLLVITDGHSDGSpdggIEKAVNEADHLGIkiFFVAVGSQNEEP 155
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 826-978 8.99e-12

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: 65.10  E-value: 8.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  826 DVVFLIDGSQSAGPE-FQYVRTLIERLVD------YLDVGFDTTRVAVIQFSDDPKVEF-LLNAHSSKDEVQNAVQRLRP 897
Cdd:cd01480     4 DITFVLDSSESVGLQnFDITKNFVKRVAErflkdyYRKDPAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNLEY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  898 KGGrQINVGNALEYVSRNIFKRPLGsrieeGVPQFLVLISSGKSDDEVD----DPAVELKQFGVAPFTIARNADQEE-LV 972
Cdd:cd01480    84 IGG-GTFTDCALKYATEQLLEGSHQ-----KENKFLLVITDGHSDGSPDggieKAVNEADHLGIKIFFVAVGSQNEEpLS 157


                  ....*.
gi 193787261  973 KISLSP 978
Cdd:cd01480   158 RIACDG 163
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 430-571 1.01e-11

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 64.68  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  430 DILFLFDGSANLV-GQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVK---RMKIKTGK 505
Cdd:cd01469     2 DIVFVLDGSGSIYpDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKhisQLLGLTNT 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193787261  506 ALnlgyALDYAQRYIFVKSAGSRieDGVLQFLVLLVAGRSSDRVDGPAsNLKQS---GVVPFI------FQAKNA 571
Cdd:cd01469    82 AT----AIQYVVTELFSESNGAR--KDATKVLVVITDGESHDDPLLKD-VIPQAereGIIRYAigvgghFQRENS 149
VWA_2 pfam13519
von Willebrand factor type A domain;
827-924 3.62e-11

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 60.77  E-value: 3.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   827 VVFLIDGSQSAGP------EFQYVRTLIERLVDYLDvgfdTTRVAVIQFSDDPKVEFLLNahSSKDEVQNAVQRLRPKGG 900
Cdd:pfam13519    1 LVFVLDTSGSMRNgdygptRLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                           90       100
                   ....*....|....*....|....
gi 193787261   901 rQINVGNALEYVSRNIFKRPLGSR 924
Cdd:pfam13519   75 -GTNLAAALQLARAALKHRRKNQP 97
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 38-176 4.72e-11

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: 62.79  E-value: 4.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   38 DIVFLVDGSSALGLAN-FNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTK-----REVITAVRKMkPL 111
Cdd:cd01471     2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTnkdlaLNAIRALLSL-YY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  112 DGSALYTGSALDFVRNNLFTsSAGYRaaEGIPKLLVLITGGKSlDEISQP---AQELK-RSSIMA-FAIG 176
Cdd:cd01471    81 PNGSTNTTSALLVVEKHLFD-TRGNR--ENAPQLVIIMTDGIP-DSKFRTlkeARKLReRGVIIAvLGVG 146
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 430-579 7.42e-11

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: 61.65  E-value: 7.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  430 DILFLFDGSANLVGQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVK--VESRFDEHQSKPEILNLVKRMKIKTGKAl 507
Cdd:cd01476     2 DLLFVLDSSGSVRGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGGTT- 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193787261  508 NLGYALDYAQRYiFVKSAGSRieDGVLQFLVLLVAGRSSDRVDGPASNLkQSGVVPFIFQAKNADP-----AELEQI 579
Cdd:cd01476    81 ATGAAIEVALQQ-LDPSEGRR--EGIPKVVVVLTDGRSHDDPEKQARIL-RAVPNIETFAVGTGDPgtvdtEELHSI 153
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 809-975 5.11e-10

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: 61.49  E-value: 5.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  809 LQPVLQPLPSPGVGGKRDVVFLID--GSQSAGPEFQYVRTLIERLVDYLDvgfDTTRVAVIQFSDDPKVefLLNAHSSKD 886
Cdd:COG1240    77 LALALAPLALARPQRGRDVVLVVDasGSMAAENRLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEV--LLPLTRDRE 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  887 EVQNAVQRLRPKGGRQInvGNALeYVSRNIFKrplgsRIEEGVPQFLVLISSGKSDDEVDDP---AVELKQFGVAPFTIA 963
Cdd:COG1240   152 ALKRALDELPPGGGTPL--GDAL-ALALELLK-----RADPARRKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIG 223

                         170
                  ....*....|....*
gi 193787261  964 ---RNADQEELVKIS 975
Cdd:COG1240   224 vgtEAVDEGLLREIA 238
VWA_2 pfam13519
von Willebrand factor type A domain;
623-732 3.45e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 54.99  E-value: 3.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   623 VVFLLDGSEGVRSG------FPLLKEFVQRVVESLDvgqdRVRVAVVQYSDRTRPEFYLNSymNKQDVVNAVRQLTLLGG 696
Cdd:pfam13519    1 LVFVLDTSGSMRNGdygptrLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 193787261   697 PTpNTGAALEFVLRNIlvssagSRITEGVPQLLIVL 732
Cdd:pfam13519   75 GT-NLAAALQLARAAL------KHRRKNQPRRIVLI 103
VWA_2 pfam13519
von Willebrand factor type A domain;
233-321 1.51e-08

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 53.45  E-value: 1.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   233 IIFLLDGSA-----NVGKTNFPYVRDFVMNLVNSldigNDNIRVGLVQFSDTPVTEFSLNTyqTKSDILGHLRQLQLQGG 307
Cdd:pfam13519    1 LVFVLDTSGsmrngDYGPTRLEAAKDAVLALLKS----LPGDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                           90
                   ....*....|....
gi 193787261   308 sGLNTGSALSYVYA 321
Cdd:pfam13519   75 -GTNLAAALQLARA 87
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 160-383 3.50e-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: 55.71  E-value: 3.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  160 QPAQELKRSSIMAFAIGNKGADQAELEEIAFDSSLVFIPAEFRAAPLQGMLPGLLAPLRTLSGTPEVHSNKRDIIFLLDG 239
Cdd:COG1240    22 LLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  240 SANVGKTN-FPYVRDFVMNLVNSLDignDNIRVGLVQFSDTPVTEFSLnTYQtKSDILGHLRQLQLQGGSglNTGSALSY 318
Cdd:COG1240   102 SGSMAAENrLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEVLLPL-TRD-REALKRALDELPPGGGT--PLGDALAL 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  319 VYaNHFTEAGGSRIRehvpqLLLLLTAGQ---SEDSYLQAANALTRAGILTFCV--GASQANKAELEQIA 383
Cdd:COG1240   175 AL-ELLKRADPARRK-----VIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIgvGTEAVDEGLLREIA 238
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 232-410 7.19e-08

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: 53.67  E-value: 7.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  232 DIIFLLDGSANVGKtNFPYVRDFVMNLVNSLDigNDNIRVGLVQFSDTPVTEFSLNTYqtKSDILGHLRQLQLQGGSGLN 311
Cdd:cd01474     6 DLYFVLDKSGSVAA-NWIEIYDFVEQLVDRFN--SPGLRFSFITFSTRATKILPLTDD--SSAIIKGLEVLKKVTPSGQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  312 -TGSALSYVYANHFTEAGGSRIREHVpqlLLLLTAGQ-SEDSYLQA---ANALTRAGILTFCVGASQANKAELEQIAFNP 386
Cdd:cd01474    81 yIHEGLENANEQIFNRNGGGRETVSV---IIALTDGQlLLNGHKYPeheAKLSRKLGAIVYCVGVTDFLKSQLINIADSK 157

                         170       180
                  ....*....|....*....|....*
gi 193787261  387 SLVYLMDD-FSSLpalpQQLIQPLT 410
Cdd:cd01474   158 EYVFPVTSgFQAL----SGIIESVV 178
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 826-943 1.94e-07

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: 52.39  E-value: 1.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  826 DVVFLIDGSQSAGPE--FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSS--KDEVQNAVQRLR----P 897
Cdd:cd01471     2 DLYLLVDGSGSIGYSnwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNStnKDLALNAIRALLslyyP 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 193787261  898 KGgrQINVGNALEYVSRNIFKRPlGSRieEGVPQFLVLISSGKSDD 943
Cdd:cd01471    82 NG--STNTTSALLVVEKHLFDTR-GNR--ENAPQLVIIMTDGIPDS 122
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 232-383 3.05e-07

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: 51.93  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  232 DIIFLLDGSANVGKTNF-PYVRDFVMNLVNSLDIGNDNIRVGLVQFSD--TPVTEFSLNTYQTKSDILGHLRQLQ--LQG 306
Cdd:cd01473     2 DLTLILDESASIGYSNWrKDVIPFTEKIINNLNISKDKVHVGILLFAEknRDVVPFSDEERYDKNELLKKINDLKnsYRS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  307 GSGLNTGSALSYVYANHFteaGGSRIREHVPQLLLLLTAGQ---SEDSYLQAANAL-TRAGILTFCVGASQANKAELEQI 382
Cdd:cd01473    82 GGETYIVEALKYGLKNYT---KHGNRRKDAPKVTMLFTDGNdtsASKKELQDISLLyKEENVKLLVVGVGAASENKLKLL 158


                  .
gi 193787261  383 A 383
Cdd:cd01473   159 A 159
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 823-1009 4.29e-07

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: 51.36  E-value: 4.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  823 GKRDVVFLIDGSQSAG---PE-FQYVRTLIERLVDyldvgfDTTRVAVIQFSDDPKVEFLLNAHSSKdEVQNA--VQRLR 896
Cdd:cd01474     3 GHFDLYFVLDKSGSVAanwIEiYDFVEQLVDRFNS------PGLRFSFITFSTRATKILPLTDDSSA-IIKGLevLKKVT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  897 PKGgrQINVGNALEYVSRNIFKRPLGSRIEEGVpqfLVLISSGKSDDEV----DDPAVELKQFGVAPFTIA-RNADQEEL 971
Cdd:cd01474    76 PSG--QTYIHEGLENANEQIFNRNGGGRETVSV---IIALTDGQLLLNGhkypEHEAKLSRKLGAIVYCVGvTDFLKSQL 150

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 193787261  972 VKISLSPEYVFSV-STFRELpsleQKLLTPITTLTSEQI 1009
Cdd:cd01474   151 INIADSKEYVFPVtSGFQAL----SGIIESVVKKACIEI 185
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 430-551 7.83e-07

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: 50.46  E-value: 7.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  430 DILFLFDGSANlVG--QFPVVRDFLYKIIDELN----VKPE--GTRIAVAQYSDDVKVESRFDEH-QSKPEILNLVKRMK 500
Cdd:cd01480     4 DITFVLDSSES-VGlqNFDITKNFVKRVAERFLkdyyRKDPagSWRVGVVQYSDQQEVEAGFLRDiRNYTSLKEAVDNLE 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 193787261  501 IkTGKALNLGYALDYAQRYIFVKSAGsriedGVLQFLVLLVAGRSSDRVDG 551
Cdd:cd01480    83 Y-IGGGTFTDCALKYATEQLLEGSHQ-----KENKFLLVITDGHSDGSPDG 127
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 37-189 9.81e-06

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: 48.40  E-value: 9.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   37 RDIVFLVDGS-SALGLANFNAIRDFIAKVIQRLEIGQdliQVAVAQYADTVrpefYFNTHPT--KREVITAVRKMKPLDG 113
Cdd:COG1240    93 RDVVLVVDASgSMAAENRLEAAKGALLDFLDDYRPRD---RVGLVAFGGEA----EVLLPLTrdREALKRALDELPPGGG 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  114 SALYTG--SALDFVRnnlftssagyRAAEGIPKLLVLITGGK---SLDEISQPAQELKRSSIMAFAI--GNKGADQAELE 186
Cdd:COG1240   166 TPLGDAlaLALELLK----------RADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIgvGTEAVDEGLLR 235


                  ...
gi 193787261  187 EIA 189
Cdd:COG1240   236 EIA 238
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 825-975 1.51e-05

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 48.17  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  825 RDVVFLIDGSQS-AGPEFQYVRTLIERLVDYLDvgfDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGrqI 903
Cdd:COG2304    92 LNLVFVIDVSGSmSGDKLELAKEAAKLLVDQLR---PGDRVSIVTFAGDARVLLPPTPATDRAKILAAIDRLQAGGG--T 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  904 NVGNALEYVsrniFKRPLGSRIEEGVPQfLVLISSGKSDDEVDDPAV------ELKQFGVAPFTIA--RNADQEELVKIS 975
Cdd:COG2304   167 ALGAGLELA----YELARKHFIPGRVNR-VILLTDGDANVGITDPEEllklaeEAREEGITLTTLGvgSDYNEDLLERLA 241
VWA_2 pfam13519
von Willebrand factor type A domain;
39-138 2.57e-05

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 44.21  E-value: 2.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261    39 IVFLVDGS-----SALGLANFNAIRDFIAKVIQRLEIGQdliqVAVAQYADTVRPEFYFNTHPTKreVITAVRKMKPLDG 113
Cdd:pfam13519    1 LVFVLDTSgsmrnGDYGPTRLEAAKDAVLALLKSLPGDR----VGLVTFGDGPEVLIPLTKDRAK--ILRALRRLEPKGG 74

                           90       100
                   ....*....|....*....|....*
gi 193787261   114 SAlYTGSALDFVRNNLFTSSAGYRA 138
Cdd:pfam13519   75 GT-NLAAALQLARAALKHRRKNQPR 98
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 232-348 6.34e-04

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: 42.27  E-value: 6.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  232 DIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTP-----VTEFSLNtyqTKSDILGHLRQLQLQ- 305
Cdd:cd01470     2 NIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPkeivsIRDFNSN---DADDVIKRLEDFNYDd 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 193787261  306 --GGSGLNTGSALSYVY----------ANHFteaggSRIReHVpqlLLLLTAGQS 348
Cdd:cd01470    79 hgDKTGTNTAAALKKVYermalekvrnKEAF-----NETR-HV---IILFTDGKS 124
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 613-772 1.21e-03

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 41.85  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  613 APAPVSGEKDVVFLLD--GSEGVRSGFPLLKEFVQRVVESLdvgQDRVRVAVVQYSDRTRPEFYLNSymNKQDVVNAVRQ 690
Cdd:COG1240    85 ALARPQRGRDVVLVVDasGSMAAENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTR--DREALKRALDE 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  691 LTLLGGpTPnTGAALEfvlrniLVSSAGSRITEGVPQLLIVLT---ADRSGDDVRNPSVVVKRGGA--VPIGIGIGNADI 765
Cdd:COG1240   160 LPPGGG-TP-LGDALA------LALELLKRADPARRKVIVLLTdgrDNAGRIDPLEAAELAAAAGIriYTIGVGTEAVDE 231


                  ....*..
gi 193787261  766 TEMQTIS 772
Cdd:COG1240   232 GLLREIA 238
VWA_2 pfam13519
von Willebrand factor type A domain;
431-521 2.39e-03

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 38.43  E-value: 2.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261   431 ILFLFDGSANLVGQ------FPVVRDFLYKIIDELNvkpeGTRIAVAQYSDDVKVESRFDEHQSKpeILNLVKRMKIKTG 504
Cdd:pfam13519    1 LVFVLDTSGSMRNGdygptrLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLTKDRAK--ILRALRRLEPKGG 74

                           90
                   ....*....|....*..
gi 193787261   505 KAlNLGYALDYAQRYIF 521
Cdd:pfam13519   75 GT-NLAAALQLARAALK 90
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 430-548 3.22e-03

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: 39.68  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  430 DILFLFDGS-----ANLVGQfpvVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRF--DEHQSKPEILNL---VKRM 499
Cdd:cd01471     2 DLYLLVDGSgsigySNWVTH---VVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLssPNSTNKDLALNAiraLLSL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 193787261  500 KIKTGKAlNLGYALDYAQRYIFvKSAGSRieDGVLQFLVLLVAGRSSDR 548
Cdd:cd01471    79 YYPNGST-NTTSALLVVEKHLF-DTRGNR--ENAPQLVIIMTDGIPDSK 123
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
826-990 5.64e-03

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 39.14  E-value: 5.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  826 DVVFLIDGSQS-AGPEFQYV----RTLIERLVDYLDVGfDTTRVAVIQFSDDPKVEFLLnahSSKDEVQnaVQRLRPKGG 900
Cdd:COG4245     7 PVYLLLDTSGSmSGEPIEALneglQALIDELRQDPYAL-ETVEVSVITFDGEAKVLLPL---TDLEDFQ--PPDLSASGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787261  901 rqINVGNALEYVsRNIFKRPLGSRIEEGVPQF---LVLISSGK-SDDEVDDPAVELKQFGVAP----FTIA--RNADQEE 970
Cdd:COG4245    81 --TPLGAALELL-LDLIERRVQKYTAEGKGDWrpvVFLITDGEpTDSDWEAALQRLKDGEAAKkaniFAIGvgPDADTEV 157

                         170       180
                  ....*....|....*....|...
gi 193787261  971 LVKISlSPEYVFSVS---TFREL 990
Cdd:COG4245   158 LKQLT-DPVRALDALdglDFREF 179
 
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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