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Conserved domains on  [gi|198443661|gb|ACH88059|]
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von Willebrand Factor, partial [Chironectes minimus]

Protein Classification

VWA domain-containing protein( domain architecture ID 11264677)

VWA (von Willebrand factor type A) domain-containing protein similar to mammalian von Willebrand factor that plays an essential role in the formation of a platelet plug, to stop bleeding, by anchoring blood platelets to the damaged vessel wall under conditions of high shear stress

PubMed:  10830113|12579041

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWA pfam00092
von Willebrand factor type A domain;
211-319 2.32e-34

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 123.54  E-value: 2.32e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661  211 DVVFVLEGSDKIGEANFNKTKEFMEQVIQRMDVRQGSIHISILQYSYTVSVEFSFNETQSKRHILERIQQIHYRGGNGTN 290
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                          90       100
                  ....*....|....*....|....*....
gi 198443661  291 TGKALQYLSENTFSSNQGTRKQAPQLVYM 319
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVL 109
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 3-163 3.68e-20

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: 85.97  E-value: 3.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661     3 SEAEFEVLKAFVVGVMERLHISQRRIRVAVVEYHDGCHSYIQLKDRKRPSELRRIASSVRYPGSNMASTSEVLKFALFHV 82
Cdd:smart00327  13 GGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTNLGAALQYALENL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661    83 FGKAD--RPEASRIALLLTAnEEPLPMAKGIELYARGLKKKKVIVIPVGLGPHASLKQIRLIEQKAPENKAFLLSGVNEL 160
Cdd:smart00327  93 FSKSAgsRRGAPKVVILITD-GESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGGVYVFLPELLDLL 171


                   ...
gi 198443661   161 EQR 163
Cdd:smart00327 172 IDL 174
 
Name Accession Description Interval E-value
VWA pfam00092
von Willebrand factor type A domain;
211-319 2.32e-34

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 123.54  E-value: 2.32e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661  211 DVVFVLEGSDKIGEANFNKTKEFMEQVIQRMDVRQGSIHISILQYSYTVSVEFSFNETQSKRHILERIQQIHYRGGNGTN 290
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                          90       100
                  ....*....|....*....|....*....
gi 198443661  291 TGKALQYLSENTFSSNQGTRKQAPQLVYM 319
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVL 109
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 210-317 4.07e-33

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: 119.70  E-value: 4.07e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661 210 LDVVFVLEGSDKIGEANFNKTKEFMEQVIQRMDVRQGSIHISILQYSYTVSVEFSFNETQSKRHILERIQQIHYRGGNGT 289
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                         90       100
                 ....*....|....*....|....*...
gi 198443661 290 NTGKALQYLSENTFSSNQgTRKQAPQLV 317
Cdd:cd01450   81 NTGKALQYALEQLFSESN-ARENVPKVI 107
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 211-319 6.70e-32

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: 117.17  E-value: 6.70e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661   211 DVVFVLEGSDKIGEANFNKTKEFMEQVIQRMDVRQGSIHISILQYSYTVSVEFSFNETQSKRHILERIQQIHYRGGNGTN 290
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100
                   ....*....|....*....|....*....
gi 198443661   291 TGKALQYLSENTFSSNQGTRKQAPQLVYM 319
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVIL 109
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 3-163 3.68e-20

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: 85.97  E-value: 3.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661     3 SEAEFEVLKAFVVGVMERLHISQRRIRVAVVEYHDGCHSYIQLKDRKRPSELRRIASSVRYPGSNMASTSEVLKFALFHV 82
Cdd:smart00327  13 GGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTNLGAALQYALENL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661    83 FGKAD--RPEASRIALLLTAnEEPLPMAKGIELYARGLKKKKVIVIPVGLGPHASLKQIRLIEQKAPENKAFLLSGVNEL 160
Cdd:smart00327  93 FSKSAgsRRGAPKVVILITD-GESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGGVYVFLPELLDLL 171


                   ...
gi 198443661   161 EQR 163
Cdd:smart00327 172 IDL 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 2-152 1.36e-18

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 81.18  E-value: 1.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661   2 LSEAEFEVLKAFVVGVMERLHISQRRIRVAVVEYHDGCHSYIQLKDRKRPSELRRIASSVRYPGSNMASTSEVLKFALFH 81
Cdd:cd01450   13 VGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGTNTGKALQYALEQ 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 198443661  82 VF-GKADRPEASRIALLLTANEEplPMAKGIELYARGLKKKKVIVIPVGLGPhASLKQIRLIEQKAPENKAF 152
Cdd:cd01450   93 LFsESNARENVPKVIIVLTDGRS--DDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSERHVF 161
VWA pfam00092
von Willebrand factor type A domain;
2-162 3.25e-14

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 69.61  E-value: 3.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661    2 LSEAEFEVLKAFVVGVMERLHISQRRIRVAVVEYHDGCHSYIQLKDRKRPSELRRIASSVRYPGSNMASTSEVLKFALFH 81
Cdd:pfam00092  12 IGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTNTGKALKYALEN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661   82 VFGKA--DRPEASRIALLLTANEeplPMAKGIELYARGLKKKKVIVIPVGLGPhASLKQIRLIEQKAPENKAFLLSGVNE 159
Cdd:pfam00092  92 LFSSAagARPGAPKVVVLLTDGR---SQDGDPEEVARELKSAGVTVFAVGVGN-ADDEELRKIASEPGEGHVFTVSDFEA 167


                  ...
gi 198443661  160 LEQ 162
Cdd:pfam00092 168 LED 170
 
Name Accession Description Interval E-value
VWA pfam00092
von Willebrand factor type A domain;
211-319 2.32e-34

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 123.54  E-value: 2.32e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661  211 DVVFVLEGSDKIGEANFNKTKEFMEQVIQRMDVRQGSIHISILQYSYTVSVEFSFNETQSKRHILERIQQIHYRGGNGTN 290
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                          90       100
                  ....*....|....*....|....*....
gi 198443661  291 TGKALQYLSENTFSSNQGTRKQAPQLVYM 319
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVL 109
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 210-317 4.07e-33

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: 119.70  E-value: 4.07e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661 210 LDVVFVLEGSDKIGEANFNKTKEFMEQVIQRMDVRQGSIHISILQYSYTVSVEFSFNETQSKRHILERIQQIHYRGGNGT 289
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                         90       100
                 ....*....|....*....|....*...
gi 198443661 290 NTGKALQYLSENTFSSNQgTRKQAPQLV 317
Cdd:cd01450   81 NTGKALQYALEQLFSESN-ARENVPKVI 107
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 211-317 9.63e-33

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: 118.87  E-value: 9.63e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661 211 DVVFVLEGSDKIGEANFNKTKEFMEQVIQRMDVRQGSIHISILQYSYTVSVEFSFNETQSKRHILERIQQIHYRGGNgTN 290
Cdd:cd01472    2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGG-TN 80

                         90       100
                 ....*....|....*....|....*..
gi 198443661 291 TGKALQYLSENTFSSNQGTRKQAPQLV 317
Cdd:cd01472   81 TGKALKYVRENLFTEASGSREGVPKVL 107
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 211-319 6.70e-32

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: 117.17  E-value: 6.70e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661   211 DVVFVLEGSDKIGEANFNKTKEFMEQVIQRMDVRQGSIHISILQYSYTVSVEFSFNETQSKRHILERIQQIHYRGGNGTN 290
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100
                   ....*....|....*....|....*....
gi 198443661   291 TGKALQYLSENTFSSNQGTRKQAPQLVYM 319
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVIL 109
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 211-310 5.63e-27

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: 103.94  E-value: 5.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661 211 DVVFVLEGSDKIGEANFNKTKEFMEQVIQRMDVRQGSIHISILQYSYTVSVEFSFNETQSKRHILERIQQIHYRGGNGTN 290
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                         90       100
                 ....*....|....*....|
gi 198443661 291 TGKALQYLSENTFSSNQGTR 310
Cdd:cd01481   82 TGSALDYVVKNLFTKSAGSR 101
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 211-317 3.95e-25

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: 98.90  E-value: 3.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661 211 DVVFVLEGSDKIGEANFNKTKEFMEQVIQRMDVRQGSIHISILQYSYTVSVEFSFNETQSKRHILERIQQIHYRGGNgTN 290
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGN-TR 80

                         90       100
                 ....*....|....*....|....*..
gi 198443661 291 TGKALQYLSENTFSSNQGTRKQAPQLV 317
Cdd:cd01482   81 TGKALTHVREKNFTPDAGARPGVPKVV 107
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 210-313 1.71e-20

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: 86.64  E-value: 1.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661 210 LDVVFVLEGSDKIGEANFNKTKEFMEQVIQRMDVRQGSIHISILQYSYTVSVEFSFNETQSKRHILERIQQIHYRGGNgT 289
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGL-T 79

                         90       100
                 ....*....|....*....|....
gi 198443661 290 NTGKALQYLSENTFSSNQGTRKQA 313
Cdd:cd01469   80 NTATAIQYVVTELFSESNGARKDA 103
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 3-163 3.68e-20

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: 85.97  E-value: 3.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661     3 SEAEFEVLKAFVVGVMERLHISQRRIRVAVVEYHDGCHSYIQLKDRKRPSELRRIASSVRYPGSNMASTSEVLKFALFHV 82
Cdd:smart00327  13 GGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTNLGAALQYALENL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661    83 FGKAD--RPEASRIALLLTAnEEPLPMAKGIELYARGLKKKKVIVIPVGLGPHASLKQIRLIEQKAPENKAFLLSGVNEL 160
Cdd:smart00327  93 FSKSAgsRRGAPKVVILITD-GESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGGVYVFLPELLDLL 171


                   ...
gi 198443661   161 EQR 163
Cdd:smart00327 172 IDL 174
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 210-314 1.26e-19

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: 85.51  E-value: 1.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661 210 LDVVFVLEGSDKIGEANFNKTKEFMEQVIQRMDVRQGSIHISILQYSYTVSVEFSFNETQSKRHILERIQQIHYRgGNGT 289
Cdd:cd01475    3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYL-ETGT 81

                         90       100
                 ....*....|....*....|....*
gi 198443661 290 NTGKALQYLSENTFSSNQGTRKQAP 314
Cdd:cd01475   82 MTGLAIQYAMNNAFSEAEGARPGSE 106
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 2-152 1.36e-18

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 81.18  E-value: 1.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661   2 LSEAEFEVLKAFVVGVMERLHISQRRIRVAVVEYHDGCHSYIQLKDRKRPSELRRIASSVRYPGSNMASTSEVLKFALFH 81
Cdd:cd01450   13 VGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGTNTGKALQYALEQ 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 198443661  82 VF-GKADRPEASRIALLLTANEEplPMAKGIELYARGLKKKKVIVIPVGLGPhASLKQIRLIEQKAPENKAF 152
Cdd:cd01450   93 LFsESNARENVPKVIIVLTDGRS--DDGGDPKEAAAKLKDEGIKVFVVGVGP-ADEEELREIASCPSERHVF 161
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 210-319 6.47e-18

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 79.53  E-value: 6.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661 210 LDVVFVLEGSDKIGEANFNKTKEFMEQVIQRMDVRQGSIHISILQYSYTVSVEFSFNETQSKRHILERIQQIHYRGGNGT 289
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 198443661 290 NTGKALQYLSENTFSSNqgtRKQAPQLVYM 319
Cdd:cd00198   81 NIGAALRLALELLKSAK---RPNARRVIIL 107
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 210-313 1.57e-14

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: 70.49  E-value: 1.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661 210 LDVVFVLEGSDKIGEANFNKTKEFMEQVIQRM------DVRQGSIHISILQYSYTVSVEFSFNETQSKRHILER-IQQIH 282
Cdd:cd01480    3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTSLKEaVDNLE 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 198443661 283 YRGGnGTNTGKALQYLSENTF-SSNQGTRKQA 313
Cdd:cd01480   83 YIGG-GTFTDCALKYATEQLLeGSHQKENKFL 113
VWA pfam00092
von Willebrand factor type A domain;
2-162 3.25e-14

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 69.61  E-value: 3.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661    2 LSEAEFEVLKAFVVGVMERLHISQRRIRVAVVEYHDGCHSYIQLKDRKRPSELRRIASSVRYPGSNMASTSEVLKFALFH 81
Cdd:pfam00092  12 IGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTNTGKALKYALEN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661   82 VFGKA--DRPEASRIALLLTANEeplPMAKGIELYARGLKKKKVIVIPVGLGPhASLKQIRLIEQKAPENKAFLLSGVNE 159
Cdd:pfam00092  92 LFSSAagARPGAPKVVVLLTDGR---SQDGDPEEVARELKSAGVTVFAVGVGN-ADDEELRKIASEPGEGHVFTVSDFEA 167


                  ...
gi 198443661  160 LEQ 162
Cdd:pfam00092 168 LED 170
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 7-152 6.95e-11

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: 59.89  E-value: 6.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661   7 FEVLKAFVVGVMERLHISQRRIRVAVVEYHDGCHSYIQLKDRKRPSELRRIASSVRYPGSNMASTSEVLKFALfHVFGKA 86
Cdd:cd00198   18 LDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGTNIGAALRLAL-ELLKSA 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 198443661  87 DRPEASRIALLLTaNEEPLPMAKGIELYARGLKKKKVIVIPVGLGPHASLKQIRLIEQKAPENKAF 152
Cdd:cd00198   97 KRPNARRVIILLT-DGEPNDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIADKTTGGAVF 161
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 210-317 9.30e-10

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: 57.01  E-value: 9.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661 210 LDVVFVLEGSDKIGEAN-FNKTKEFMEQVIQRMDVRQGSIHISILQYSYTVSVEFSFNETQSK-----RHILERIQQIHY 283
Cdd:cd01471    1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTnkdlaLNAIRALLSLYY 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 198443661 284 RGGNgTNTGKALQYLSENTFSSnQGTRKQAPQLV 317
Cdd:cd01471   81 PNGS-TNTTSALLVVEKHLFDT-RGNRENAPQLV 112
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 211-314 4.87e-08

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: 52.32  E-value: 4.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661 211 DVVFVLEGSDKIGEANFNK-TKEFMEQVIQRMDVRQGSIHISILQYSYTVS--VEFSFNETQSKRHILERIQQI--HYRG 285
Cdd:cd01473    2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEKNRdvVPFSDEERYDKNELLKKINDLknSYRS 81

                         90       100
                 ....*....|....*....|....*....
gi 198443661 286 GNGTNTGKALQYLSENtFSSNQGTRKQAP 314
Cdd:cd01473   82 GGETYIVEALKYGLKN-YTKHGNRRKDAP 109
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 210-318 1.50e-07

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: 50.48  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661 210 LDVVFVLEGSDKIGEAnFNKTKEFMEQVIQRMDVRQGSIHISILQYS--YTVSVEFSFNETQSKRHILERIQQIHYRGGN 287
Cdd:cd01476    1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 198443661 288 gTNTGKALQYlSENTFSSNQGTRKQAPQLVY 318
Cdd:cd01476   80 -TATGAAIEV-ALQQLDPSEGRREGIPKVVV 108
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 4-139 3.24e-07

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: 50.46  E-value: 3.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661   4 EAEFEVLKAFVVGVMERLHISQRRIRVAVVEYHDGCHSYIQLKDRKRPSELRRIASSVRYPGS-NMasTSEVLKFALFHV 82
Cdd:cd01475   17 PENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETgTM--TGLAIQYAMNNA 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661  83 FGKAD--RPEA---SRIALLLTAN------EEPLPMAK--GIELYARGlkkkkvivipVGLGPHASLKQI 139
Cdd:cd01475   95 FSEAEgaRPGServPRVGIVVTDGrpqddvSEVAAKARalGIEMFAVG----------VGRADEEELREI 154
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 210-296 5.82e-07

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


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 49.21  E-value: 5.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661 210 LDVVFVLEGSDKIGEANFNKTKEFMEQVIQRMDVRQGSIHISILQYSYTVSVEFS---FNEtQSKRHILERIQQIHYR-- 284
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSirdFNS-NDADDVIKRLEDFNYDdh 79

                         90
                 ....*....|...
gi 198443661 285 -GGNGTNTGKALQ 296
Cdd:cd01470   80 gDKTGTNTAAALK 92
VWA_2 pfam13519
von Willebrand factor type A domain;
212-312 5.83e-07

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 47.29  E-value: 5.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661  212 VVFVLEGSDKIGEANFNKT-----KEFMEQVIQRMDVRQgsihISILQYSYTVSVEFSFneTQSKRHILERIQQIHYRGG 286
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTrleaaKDAVLALLKSLPGDR----VGLVTFGDGPEVLIPL--TKDRAKILRALRRLEPKGG 74

                          90       100
                  ....*....|....*....|....*.
gi 198443661  287 nGTNTGKALQYLSeNTFSSNQGTRKQ 312
Cdd:pfam13519  75 -GTNLAAALQLAR-AALKHRRKNQPR 98
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 7-120 1.11e-06

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: 47.67  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661   7 FEVLKAFVVGVMERLHISQRRIRVAVVEYHDGCHSYIQLKDRKRPSELRRIASSVRYPGSNmASTSEVLKFALFHVFGKA 86
Cdd:cd01482   18 FNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGN-TRTGKALTHVREKNFTPD 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 198443661  87 D--RPEASRIALLLT------ANEEPLPMAK--GIELYARGLKK 120
Cdd:cd01482   97 AgaRPGVPKVVILITdgksqdDVELPARVLRnlGVNVFAVGVKD 140
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 5-139 1.08e-05

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: 44.91  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661   5 AEFEVLKAFVVGVMERLHISQRRIRVAVVEYHDGCHSYIQLKDRKRPSELRRIASSVRYPGSNMAsTSEVLKFALFHVFG 84
Cdd:cd01472   16 SNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN-TGKALKYVRENLFT 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 198443661  85 KADRPEAS--RIALLLTANEEPlpmaKGIELYARGLKKKKVIVIPVGLGPHAS--LKQI 139
Cdd:cd01472   95 EASGSREGvpKVLVVITDGKSQ----DDVEEPAVELKQAGIEVFAVGVKNADEeeLKQI 149
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 7-131 8.52e-05

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 42.76  E-value: 8.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661   7 FEVLKAFVVGVMERLHISQRRIRVAVVEYHDGCHSYIQLKD--RKRPSELRRIASSVR---YPGSNmASTSEVLKFALFH 81
Cdd:cd01471   19 VTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpnSTNKDLALNAIRALLslyYPNGS-TNTTSALLVVEKH 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 198443661  82 VF-GKADRPEASRIALLLT---ANEEPLPMAKgielyARGLKKKKVIVIPVGLG 131
Cdd:cd01471   98 LFdTRGNRENAPQLVIIMTdgiPDSKFRTLKE-----ARKLRERGVIIAVLGVG 146
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 6-155 1.66e-03

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 38.88  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661   6 EFEVLKAFVVGVMERLHISQRRIRVAVVEYHDGCHSYIQLKD-RKRPSELRRIASSVRYPG-SNMASTSEVLKFALFHvF 83
Cdd:cd01469   17 DFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEyRTKEEPLSLVKHISQLLGlTNTATAIQYVVTELFS-E 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198443661  84 GKADRPEASRIALLLT--------ANEEPLPMAK--GIELYArglkkkkvivipVGLGPH----ASLKQIRLIEQKAPEN 149
Cdd:cd01469   96 SNGARKDATKVLVVITdgeshddpLLKDVIPQAEreGIIRYA------------IGVGGHfqreNSREELKTIASKPPEE 163


                 ....*.
gi 198443661 150 KAFLLS 155
Cdd:cd01469  164 HFFNVT 169
 
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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