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Conserved domains on  [gi|13872835|emb|CAC37587|]
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von Willebrand Factor, partial [Gerbilliscus gambianus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWA pfam00092
von Willebrand factor type A domain;
249-384 4.83e-39

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 137.41  E-value: 4.83e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835   249 VVFVLEGSDEVGEANFNKIKEFLEEAIRRMDVAHDGIHITVLQYSYTVTVEYTFNDAQSKEDVLRHVREIRYRGGNRTYT 328
Cdd:pfam00092   2 IVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTNT 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13872835   329 GQALQYLSEHSFSPMQGDREQAPNLVYLVT-GNPASDEIKRL-----PGDIQVVPIGVGPHT 384
Cdd:pfam00092  82 GKALKYALENLFSSAAGARPGAPKVVVLLTdGRSQDGDPEEVarelkSAGVTVFAVGVGNAD 143
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 26-138 9.59e-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: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 82.34  E-value: 9.59e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835  26 LDLVFLLDGSSRLSEAEFEVLKAFVVGMMETLHISQKRIRVAVVEYHDGSHSYIELKARKRPSELRRIASQVKYAGSQVA 105
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 13872835 106 STSEVLKYTMFQIF-GKVDRPEASRIALLLTASQ 138
Cdd:cd01450  81 NTGKALQYALEQLFsESNARENVPKVIIVLTDGR 114
VWA_N2 super family cl24671
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1-26 3.50e-07

VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to the N-terminus of the first VWA domain (pfam00092).


The actual alignment was detected with superfamily member pfam16164:

Pssm-ID: 465038  Cd Length: 79  Bit Score: 47.28  E-value: 3.50e-07
                          10        20
                  ....*....|....*....|....*.
gi 13872835     1 PVDSTTSYVEDTPEPPLDSFYCNRLL 26
Cdd:pfam16164  54 PVTTTTPYVEDTPEPPLHDFYCSKLL 79
 
Name Accession Description Interval E-value
VWA pfam00092
von Willebrand factor type A domain;
249-384 4.83e-39

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 137.41  E-value: 4.83e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835   249 VVFVLEGSDEVGEANFNKIKEFLEEAIRRMDVAHDGIHITVLQYSYTVTVEYTFNDAQSKEDVLRHVREIRYRGGNRTYT 328
Cdd:pfam00092   2 IVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTNT 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13872835   329 GQALQYLSEHSFSPMQGDREQAPNLVYLVT-GNPASDEIKRL-----PGDIQVVPIGVGPHT 384
Cdd:pfam00092  82 GKALKYALENLFSSAAGARPGAPKVVVLLTdGRSQDGDPEEVarelkSAGVTVFAVGVGNAD 143
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 249-383 2.39e-34

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: 124.71  E-value: 2.39e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835 249 VVFVLEGSDEVGEANFNKIKEFLEEAIRRMDVAHDGIHITVLQYSYTVTVEYTFNDAQSKEDVLRHVREIRYRGGNRTYT 328
Cdd:cd01450   3 IVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGTNT 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13872835 329 GQALQYLSEHSFSPmQGDREQAPNLVYLVT-GNP--------ASDEIKRLpgDIQVVPIGVGPH 383
Cdd:cd01450  83 GKALQYALEQLFSE-SNARENVPKVIIVLTdGRSddggdpkeAAAKLKDE--GIKVFVVGVGPA 143
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 249-383 1.77e-31

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: 117.56  E-value: 1.77e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835    249 VVFVLEGSDEVGEANFNKIKEFLEEAIRRMDVAHDGIHITVLQYSYTVTVEYTFNDAQSKEDVLRHVREIRYRGGNRTYT 328
Cdd:smart00327   2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTNL 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13872835    329 GQALQYLSEHSFSPMQGDREQAPNLVYLVT-GNP---------ASDEIKRLPgdIQVVPIGVGPH 383
Cdd:smart00327  82 GAALQYALENLFSKSAGSRRGAPKVVILITdGESndgpkdllkAAKELKRSG--VKVFVVGVGND 144
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 26-138 9.59e-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: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 82.34  E-value: 9.59e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835  26 LDLVFLLDGSSRLSEAEFEVLKAFVVGMMETLHISQKRIRVAVVEYHDGSHSYIELKARKRPSELRRIASQVKYAGSQVA 105
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 13872835 106 STSEVLKYTMFQIF-GKVDRPEASRIALLLTASQ 138
Cdd:cd01450  81 NTGKALQYALEQLFsESNARENVPKVIIVLTDGR 114
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 27-199 1.85e-18

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: 82.12  E-value: 1.85e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835     27 DLVFLLDGSSRLSEAEFEVLKAFVVGMMETLHISQKRIRVAVVEYHDGSHSYIELKARKRPSELRRIASQVKYAGSQVAS 106
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835    107 TSEVLKYTMFQIFGKVD--RPEASRIALLLTaSQEPPRTAKFLPRYAQGLKKKKVIVVPVGIG**ASL*QIRLIEKQAPE 184
Cdd:smart00327  81 LGAALQYALENLFSKSAgsRRGAPKVVILIT-DGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                          170
                   ....*....|....*
gi 13872835    185 NKAFLLSGVDELEQR 199
Cdd:smart00327 160 VYVFLPELLDLLIDL 174
VWA pfam00092
von Willebrand factor type A domain;
27-135 1.26e-13

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 68.46  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835    27 DLVFLLDGSSRLSEAEFEVLKAFVVGMMETLHISQKRIRVAVVEYHDGSHSYIELKARKRPSELRRIASQVKYAGSQVAS 106
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 13872835   107 TSEVLKYTMFQIFGKV--DRPEASRIALLLT 135
Cdd:pfam00092  81 TGKALKYALENLFSSAagARPGAPKVVVLLT 111
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1-26 3.50e-07

VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to the N-terminus of the first VWA domain (pfam00092).


Pssm-ID: 465038  Cd Length: 79  Bit Score: 47.28  E-value: 3.50e-07
                          10        20
                  ....*....|....*....|....*.
gi 13872835     1 PVDSTTSYVEDTPEPPLDSFYCNRLL 26
Cdd:pfam16164  54 PVTTTTPYVEDTPEPPLHDFYCSKLL 79
 
Name Accession Description Interval E-value
VWA pfam00092
von Willebrand factor type A domain;
249-384 4.83e-39

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 137.41  E-value: 4.83e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835   249 VVFVLEGSDEVGEANFNKIKEFLEEAIRRMDVAHDGIHITVLQYSYTVTVEYTFNDAQSKEDVLRHVREIRYRGGNRTYT 328
Cdd:pfam00092   2 IVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTNT 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13872835   329 GQALQYLSEHSFSPMQGDREQAPNLVYLVT-GNPASDEIKRL-----PGDIQVVPIGVGPHT 384
Cdd:pfam00092  82 GKALKYALENLFSSAAGARPGAPKVVVLLTdGRSQDGDPEEVarelkSAGVTVFAVGVGNAD 143
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 249-383 2.39e-34

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: 124.71  E-value: 2.39e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835 249 VVFVLEGSDEVGEANFNKIKEFLEEAIRRMDVAHDGIHITVLQYSYTVTVEYTFNDAQSKEDVLRHVREIRYRGGNRTYT 328
Cdd:cd01450   3 IVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGTNT 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13872835 329 GQALQYLSEHSFSPmQGDREQAPNLVYLVT-GNP--------ASDEIKRLpgDIQVVPIGVGPH 383
Cdd:cd01450  83 GKALQYALEQLFSE-SNARENVPKVIIVLTdGRSddggdpkeAAAKLKDE--GIKVFVVGVGPA 143
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 249-383 2.04e-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: 122.34  E-value: 2.04e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835 249 VVFVLEGSDEVGEANFNKIKEFLEEAIRRMDVAHDGIHITVLQYSYTVTVEYTFNDAQSKEDVLRHVREIRYRGGNrTYT 328
Cdd:cd01472   3 IVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGG-TNT 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13872835 329 GQALQYLSEHSFSPMQGDREQAPNLVYLVTGNPASDEIkRLPG------DIQVVPIGVGPH 383
Cdd:cd01472  82 GKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDV-EEPAvelkqaGIEVFAVGVKNA 141
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 249-383 1.77e-31

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: 117.56  E-value: 1.77e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835    249 VVFVLEGSDEVGEANFNKIKEFLEEAIRRMDVAHDGIHITVLQYSYTVTVEYTFNDAQSKEDVLRHVREIRYRGGNRTYT 328
Cdd:smart00327   2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTNL 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13872835    329 GQALQYLSEHSFSPMQGDREQAPNLVYLVT-GNP---------ASDEIKRLPgdIQVVPIGVGPH 383
Cdd:smart00327  82 GAALQYALENLFSKSAGSRRGAPKVVILITdGESndgpkdllkAAKELKRSG--VKVFVVGVGND 144
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 249-380 5.08e-29

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: 110.45  E-value: 5.08e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835 249 VVFVLEGSDEVGEANFNKIKEFLEEAIRRMDVAHDGIHITVLQYSYTVTVEYTFNDAQSKEDVLRHVREIRYRGGNrTYT 328
Cdd:cd01482   3 IVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGN-TRT 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 13872835 329 GQALQYLSEHSFSPMQGDREQAPNLVYLVTGNPASDEIkRLPGD------IQVVPIGV 380
Cdd:cd01482  82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDV-ELPARvlrnlgVNVFAVGV 138
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 249-381 5.27e-28

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: 107.79  E-value: 5.27e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835 249 VVFVLEGSDEVGEANFNKIKEFLEEAIRRMDVAHDGIHITVLQYSYTVTVEYTFNDAQSKEDVLRHVREIRYRGGNRTYT 328
Cdd:cd01481   3 IVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLNT 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 13872835 329 GQALQYLSEHSFSPMQGDR--EQAPNLVYLVTGNPASDEIKRLPGDIQ---VVPIGVG 381
Cdd:cd01481  83 GSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKragIVPFAIG 140
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 249-381 3.20e-21

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: 90.91  E-value: 3.20e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835 249 VVFVLEGSDEVGEANFNKIKEFLEEAIRRMDVAHDGIHITVLQYSYTVTVEYTFNDAQSKEDVLRHVREIRY--RGgnrT 326
Cdd:cd01475   5 LVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYleTG---T 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13872835 327 YTGQALQYLSEHSFSPMQGDR---EQAPNLVYLVTGNPASDEIK------RLPGdIQVVPIGVG 381
Cdd:cd01475  82 MTGLAIQYAMNNAFSEAEGARpgsERVPRVGIVVTDGRPQDDVSevaakaRALG-IEMFAVGVG 144
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 26-138 9.59e-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: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 82.34  E-value: 9.59e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835  26 LDLVFLLDGSSRLSEAEFEVLKAFVVGMMETLHISQKRIRVAVVEYHDGSHSYIELKARKRPSELRRIASQVKYAGSQVA 105
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 13872835 106 STSEVLKYTMFQIF-GKVDRPEASRIALLLTASQ 138
Cdd:cd01450  81 NTGKALQYALEQLFsESNARENVPKVIIVLTDGR 114
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 27-199 1.85e-18

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: 82.12  E-value: 1.85e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835     27 DLVFLLDGSSRLSEAEFEVLKAFVVGMMETLHISQKRIRVAVVEYHDGSHSYIELKARKRPSELRRIASQVKYAGSQVAS 106
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835    107 TSEVLKYTMFQIFGKVD--RPEASRIALLLTaSQEPPRTAKFLPRYAQGLKKKKVIVVPVGIG**ASL*QIRLIEKQAPE 184
Cdd:smart00327  81 LGAALQYALENLFSKSAgsRRGAPKVVILIT-DGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGG 159

                          170
                   ....*....|....*
gi 13872835    185 NKAFLLSGVDELEQR 199
Cdd:smart00327 160 VYVFLPELLDLLIDL 174
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 249-383 4.81e-18

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: 80.86  E-value: 4.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835 249 VVFVLEGSDEVGEANFNKIKEFLEEAIRRMDVAHDGIHITVLQYSYTVTVEYTFNDAQSKEDVLRHVREIRYRGGnRTYT 328
Cdd:cd01469   3 IVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLG-LTNT 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13872835 329 GQALQYLSEHSFSPMQGDREQAPNLVYLVTGNPASDEikrlPGDIQVVP-----------IGVGPH 383
Cdd:cd01469  82 ATAIQYVVTELFSESNGARKDATKVLVVITDGESHDD----PLLKDVIPqaeregiiryaIGVGGH 143
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 249-381 5.26e-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: 80.30  E-value: 5.26e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835 249 VVFVLEGSDEVGEANFNKIKEFLEEAIRRMDVAHDGIHITVLQYSYTVTVEYTFNDAQSKEDVLRHVREIRYRGGNRTYT 328
Cdd:cd00198   3 IVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGTNI 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13872835 329 GQALQYLSEHSFSPmqgDREQAPNLVYLVT-GNP---------ASDEIKRLpgDIQVVPIGVG 381
Cdd:cd00198  83 GAALRLALELLKSA---KRPNARRVIILLTdGEPndgpellaeAARELRKL--GITVYTIGIG 140
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 247-381 2.35e-14

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: 70.88  E-value: 2.35e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835 247 LGVVFVLEGSDEVGEAN-FNKIKEFLEEAIRRMDVAHDGIHITVLQYSYTVTVEYTFND--AQSKE---DVLRHVREIRY 320
Cdd:cd01471   1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpnSTNKDlalNAIRALLSLYY 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835 321 RGGNrTYTGQALQYLSEHSFSpMQGDREQAPNLVYLVT-GNPASD--------EIKRLPGDIQVVPIGVG 381
Cdd:cd01471  81 PNGS-TNTTSALLVVEKHLFD-TRGNRENAPQLVIIMTdGIPDSKfrtlkearKLRERGVIIAVLGVGQG 148
VWA pfam00092
von Willebrand factor type A domain;
27-135 1.26e-13

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 68.46  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835    27 DLVFLLDGSSRLSEAEFEVLKAFVVGMMETLHISQKRIRVAVVEYHDGSHSYIELKARKRPSELRRIASQVKYAGSQVAS 106
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 13872835   107 TSEVLKYTMFQIFGKV--DRPEASRIALLLT 135
Cdd:pfam00092  81 TGKALKYALENLFSSAagARPGAPKVVVLLT 111
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 26-135 2.11e-12

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: 65.87  E-value: 2.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835  26 LDLVFLLDGSSRLSEAEFEVLKAFVVGMMETLHISQKRIRVAVVEYHDGSHSYIELKARKRPSELRRIASQVKYAgSQVA 105
Cdd:cd01475   3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYL-ETGT 81

                        90       100       110
                ....*....|....*....|....*....|....*
gi 13872835 106 STSEVLKYTMFQIFGKVD--RPEA---SRIALLLT 135
Cdd:cd01475  82 MTGLAIQYAMNNAFSEAEgaRPGServPRVGIVVT 116
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 247-382 2.80e-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: 61.26  E-value: 2.80e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835 247 LGVVFVLEGSDEVGEAnFNKIKEFLEEAIRRMDVAHDGIHITVLQYS--YTVTVEYTFNDAQSKEDVLRHVREIRYRGGN 324
Cdd:cd01476   1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13872835 325 rTYTGQALQYLSEHsFSPMQGDREQAPNLVYLVTG-----NP--ASDEIKRLPGdIQVVPIGVGP 382
Cdd:cd01476  80 -TATGAAIEVALQQ-LDPSEGRREGIPKVVVVLTDgrshdDPekQARILRAVPN-IETFAVGTGD 141
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 27-140 8.94e-11

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: 59.93  E-value: 8.94e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835  27 DLVFLLDGSSRLSEAEFEVLKAFVVGMMETLHISQKRIRVAVVEYHDGSHSYIELKARKRPSELRRIASQVKYAGSQVAs 106
Cdd:cd01472   2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN- 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 13872835 107 TSEVLKYTMFQIFGKVDRPEAS--RIALLLTASQEP 140
Cdd:cd01472  81 TGKALKYVRENLFTEASGSREGvpKVLVVITDGKSQ 116
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 26-135 1.24e-10

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: 59.50  E-value: 1.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835  26 LDLVFLLDGSSRLSEAEFEVLKAFVVGMMETLHISQKRIRVAVVEYHDGSHSYIELKARKRPSELRRIASQVKYAGSQVA 105
Cdd:cd00198   1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                        90       100       110
                ....*....|....*....|....*....|
gi 13872835 106 STSEVLKYTMfQIFGKVDRPEASRIALLLT 135
Cdd:cd00198  81 NIGAALRLAL-ELLKSAKRPNARRVIILLT 109
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 27-135 4.41e-10

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: 58.07  E-value: 4.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835  27 DLVFLLDGSSRLSEAEFEVLKAFVVGMMETLHISQKRIRVAVVEYHDGSHSYIELKARKRPSELRRIASQVKYAGSQvAS 106
Cdd:cd01482   2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGN-TR 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 13872835 107 TSEVLKYTMFQIF--GKVDRPEASRIALLLT 135
Cdd:cd01482  81 TGKALTHVREKNFtpDAGARPGVPKVVILIT 111
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 27-138 2.76e-09

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: 55.79  E-value: 2.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835  27 DLVFLLDGSSRLSEAEFEVLKAFVVGMMETLHISQKRIRVAVVEYHDGSHSYIELKARKRPSELRRIASQVKYAGSQVAS 106
Cdd:cd01481   2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 13872835 107 TSEVLKYTMFQIFgkvDRPEASRIA-------LLLTASQ 138
Cdd:cd01481  82 TGSALDYVVKNLF---TKSAGSRIEegvpqflVLITGGK 117
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 249-337 4.44e-08

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: 52.77  E-value: 4.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835 249 VVFVLEGSDEVGEANFNKIKEFLEEAIRRM------DVAHDGIHITVLQYSYTVTVEYTF-NDAQSKEDVLRHVREIRYR 321
Cdd:cd01480   5 ITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFlRDIRNYTSLKEAVDNLEYI 84

                        90
                ....*....|....*.
gi 13872835 322 GGNrTYTGQALQYLSE 337
Cdd:cd01480  85 GGG-TFTDCALKYATE 99
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 1-26 3.50e-07

VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to the N-terminus of the first VWA domain (pfam00092).


Pssm-ID: 465038  Cd Length: 79  Bit Score: 47.28  E-value: 3.50e-07
                          10        20
                  ....*....|....*....|....*.
gi 13872835     1 PVDSTTSYVEDTPEPPLDSFYCNRLL 26
Cdd:pfam16164  54 PVTTTTPYVEDTPEPPLHDFYCSKLL 79
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 26-135 5.41e-06

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: 46.19  E-value: 5.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835  26 LDLVFLLDGSSRLSEAEFEVLKAFVVGMMETLHISQKRIRVAVVEYhdgSHSY-IEL---KARKRPSELRRIASQVKYAG 101
Cdd:cd01469   1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQY---SESFrTEFtlnEYRTKEEPLSLVKHISQLLG 77

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 13872835 102 sqVASTSEVLKYTMFQIF--GKVDRPEASRIALLLT 135
Cdd:cd01469  78 --LTNTATAIQYVVTELFseSNGARKDATKVLVVIT 111
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 270-370 1.33e-04

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 42.30  E-value: 1.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835 270 FLEEAIRRMDVAHDGIHITVLQYSYTVTVEYTFNDAQS--KEDVLRHVREIR--YRGGNRTYTGQALQY-LSEHSFSPmq 344
Cdd:cd01473  25 FTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERydKNELLKKINDLKnsYRSGGETYIVEALKYgLKNYTKHG-- 102

                        90       100
                ....*....|....*....|....*..
gi 13872835 345 GDREQAPNLVYLVT-GNPASDEIKRLP 370
Cdd:cd01473 103 NRRKDAPKVTMLFTdGNDTSASKKELQ 129
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 26-167 1.71e-04

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: 41.99  E-value: 1.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835  26 LDLVFLLDGSSRLSEA-EFEVLKAFVVGMMETLHISQKRIRVAVVEYHDGSHSYIELKA--RKRPSELRRIASQVK---Y 99
Cdd:cd01471   1 LDLYLLVDGSGSIGYSnWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpnSTNKDLALNAIRALLslyY 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835 100 AGSQVASTSEVLKYTMFQIFGKVDRPEASRIALLLT--ASQEPPRTAKflprYAQGLKKKKVIVVPVGIG 167
Cdd:cd01471  81 PNGSTNTTSALLVVEKHLFDTRGNRENAPQLVIIMTdgIPDSKFRTLK----EARKLRERGVIIAVLGVG 146
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 26-135 5.71e-03

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: 37.36  E-value: 5.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13872835  26 LDLVFLLDGSSRLSEAEFEVLKAFVVGMMETLHISQKR------IRVAVVEY-HDGSHSYIELKARKRPSELRRIASQVK 98
Cdd:cd01480   3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRkdpagsWRVGVVQYsDQQEVEAGFLRDIRNYTSLKEAVDNLE 82

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 13872835  99 YAGsQVASTSEVLKYTMFQIFgKVDRPEASRIALLLT 135
Cdd:cd01480  83 YIG-GGTFTDCALKYATEQLL-EGSHQKENKFLLVIT 117
 
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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