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Conserved domains on  [gi|156616288|ref|NP_766515|]
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collagen alpha-6(VI) chain isoform 2 precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 620-783 4.66e-49

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


:

Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 171.64  E-value: 4.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  620 ADIMFLVDSSGSIGPENFSKMKMFMKNLVSKSQIGADRVQIGVVQFSHENKEEFQLNTFMSQSDIANAIDRMTHIGETTL 699
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  700 TGSALTFVS-QYFSPDKGARPNVRKFLILITDGEAQDIVRDPAIALRKEGVIIYSVGVFGSNVTQLEEISGKPEmVFYVE 778
Cdd:cd01472    81 TGKALKYVReNLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPK-ELYVF 159


                  ....*
gi 156616288  779 NFDIL 783
Cdd:cd01472   160 NVADF 164
VWA pfam00092
von Willebrand factor type A domain;
435-604 2.12e-43

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 155.51  E-value: 2.12e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   435 DIYLLIDGSGSTQPTDFHEMKTFLSEVVGMFNIAPHKVRVGAVQYADTWDLEFEISKYSNKPDLGKAIENIRQMGGNT-N 513
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   514 TGAALNFTLKLLQRAKKERGSKVPCHLVVLTNGMSRD-SVLGPAHKLREENIRVHAIGVKEANQTQLREIAGE--EKRVY 590
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEpgEGHVF 160

                          170
                   ....*....|....
gi 156616288   591 YVHEFDALRNIRNQ 604
Cdd:pfam00092  161 TVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
999-1166 1.78e-40

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 147.42  E-value: 1.78e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   999 DLVFLMDGSNSIHPDDFQKMKGFLVSVVQDFDVSLNRVRIGVAQFSDSYRSEFLLGTFTGEREISTQIEGIQQIF-GYTH 1077
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGgGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  1078 IGDALRKV-KYYFQPDMGSRINAgtPQVLLVLTDGRSQD-EVAQAAEELRHKGVDIYSVGIGDVDDQELVQITGTAEKKL 1155
Cdd:pfam00092   81 TGKALKYAlENLFSSAAGARPGA--PKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGH 158

                          170
                   ....*....|...
gi 156616288  1156 --TVHNFDELKKV 1166
Cdd:pfam00092  159 vfTVSDFEALEDL 171
VWA pfam00092
von Willebrand factor type A domain;
808-980 4.64e-39

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 143.18  E-value: 4.64e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   808 DVVFVIDSSGSIDYQEYNIMKDFMIGLVKKADVGKNQVRFGALKYADDPEVLFYLDELGTKLEVVSVLQNDHPMGGNT-Y 886
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   887 TAEALAF-SDHMFTEARGSRlhKGVPQVLIVITDGESHDAEkLNTTAKALRDKGILVLAVGIAGANSWELLAMAGSSDK- 964
Cdd:pfam00092   81 TGKALKYaLENLFSSAAGAR--PGAPKVVVLLTDGRSQDGD-PEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEg 157

                          170
                   ....*....|....*..
gi 156616288   965 -YYFVETFGGLKGIFSD 980
Cdd:pfam00092  158 hVFTVSDFEALEDLQDQ 174
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 25-179 9.21e-37

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


The actual alignment was detected with superfamily member cd01472:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 164  Bit Score: 136.20  E-value: 9.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   25 ADVVFLVDSSDHLGLKSFPLVKTFIHKMISSLPIEANKYRVALAQYSDALHNEFQLGTFKNRNPMLNHLkKNFGFIGGSL 104
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAV-KNLRYIGGGT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156616288  105 KIGNALQEAHRTYFSAPTngRDKKQFPPILVVLASAESEDDVEEAAKALREDGVKIISVGVQKASEENLKAMATS 179
Cdd:cd01472    80 NTGKALKYVRENLFTEAS--GSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASD 152
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 227-392 7.38e-35

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


The actual alignment was detected with superfamily member cd01472:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 164  Bit Score: 130.81  E-value: 7.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  227 ADVVFLLDmainGS----QEDLDHLKAFLGESISALDIKENCMRVGLVTYSNETRVISSLSTGNNKTEVLQRIQDLSPQV 302
Cdd:cd01472     1 ADIVFLVD----GSesigLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  303 GQAYTGAALRKTRKEIFSAQRGSRKnqGVPQIAVLVTHRASEDNVTKAAVNLRREGVTIFTMGIEGANPDELEKIASHPA 382
Cdd:cd01472    77 GGTNTGKALKYVRENLFTEASGSRE--GVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPK 154

                         170
                  ....*....|
gi 156616288  383 EQFTSKLGNF 392
Cdd:cd01472   155 ELYVFNVADF 164
 
Name Accession Description Interval E-value
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 620-783 4.66e-49

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 171.64  E-value: 4.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  620 ADIMFLVDSSGSIGPENFSKMKMFMKNLVSKSQIGADRVQIGVVQFSHENKEEFQLNTFMSQSDIANAIDRMTHIGETTL 699
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  700 TGSALTFVS-QYFSPDKGARPNVRKFLILITDGEAQDIVRDPAIALRKEGVIIYSVGVFGSNVTQLEEISGKPEmVFYVE 778
Cdd:cd01472    81 TGKALKYVReNLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPK-ELYVF 159


                  ....*
gi 156616288  779 NFDIL 783
Cdd:cd01472   160 NVADF 164
VWA pfam00092
von Willebrand factor type A domain;
621-789 7.24e-49

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 171.30  E-value: 7.24e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   621 DIMFLVDSSGSIGPENFSKMKMFMKNLVSKSQIGADRVQIGVVQFSHENKEEFQLNTFMSQSDIANAIDRMTHI-GETTL 699
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   700 TGSALTFV-SQYFSPDKGARPNVRKFLILITDGEAQDI-VRDPAIALRKEGVIIYSVGVFGSNVTQLEEISGKP--EMVF 775
Cdd:pfam00092   81 TGKALKYAlENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPgeGHVF 160

                          170
                   ....*....|....
gi 156616288   776 YVENFDILQHIEDD 789
Cdd:pfam00092  161 TVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
435-604 2.12e-43

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 155.51  E-value: 2.12e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   435 DIYLLIDGSGSTQPTDFHEMKTFLSEVVGMFNIAPHKVRVGAVQYADTWDLEFEISKYSNKPDLGKAIENIRQMGGNT-N 513
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   514 TGAALNFTLKLLQRAKKERGSKVPCHLVVLTNGMSRD-SVLGPAHKLREENIRVHAIGVKEANQTQLREIAGE--EKRVY 590
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEpgEGHVF 160

                          170
                   ....*....|....
gi 156616288   591 YVHEFDALRNIRNQ 604
Cdd:pfam00092  161 TVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
999-1166 1.78e-40

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 147.42  E-value: 1.78e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   999 DLVFLMDGSNSIHPDDFQKMKGFLVSVVQDFDVSLNRVRIGVAQFSDSYRSEFLLGTFTGEREISTQIEGIQQIF-GYTH 1077
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGgGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  1078 IGDALRKV-KYYFQPDMGSRINAgtPQVLLVLTDGRSQD-EVAQAAEELRHKGVDIYSVGIGDVDDQELVQITGTAEKKL 1155
Cdd:pfam00092   81 TGKALKYAlENLFSSAAGARPGA--PKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGH 158

                          170
                   ....*....|...
gi 156616288  1156 --TVHNFDELKKV 1166
Cdd:pfam00092  159 vfTVSDFEALEDL 171
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 434-595 1.99e-40

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: 146.60  E-value: 1.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  434 ADIYLLIDGSGSTQPTDFHEMKTFLSEVVGMFNIAPHKVRVGAVQYADTWDLEFEISKYSNKPDLGKAIENIRQMGGNTN 513
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  514 TGAALNFTLKLLQRAKKERGSKVPCHLVVLTNGMSRDSVLGPAHKLREENIRVHAIGVKEANQTQLREIA--GEEKRVYY 591
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIAsdPKELYVFN 160


                  ....
gi 156616288  592 VHEF 595
Cdd:cd01472   161 VADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 998-1163 2.13e-39

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: 143.91  E-value: 2.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  998 VDLVFLMDGSNSIHPDDFQKMKGFLVSVVQDFDVSLNRVRIGVAQFSDSYRSEFLLGTFTGEREISTQIEGIQQIFGYTH 1077
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288 1078 IGDALRKV-KYYFQPDMGSRinAGTPQVLLVLTDGRSQDEVAQAAEELRHKGVDIYSVGIGDVDDQELVQITGTAeKKLT 1156
Cdd:cd01472    81 TGKALKYVrENLFTEASGSR--EGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDP-KELY 157


                  ....*..
gi 156616288 1157 VHNFDEL 1163
Cdd:cd01472   158 VFNVADF 164
VWA pfam00092
von Willebrand factor type A domain;
808-980 4.64e-39

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 143.18  E-value: 4.64e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   808 DVVFVIDSSGSIDYQEYNIMKDFMIGLVKKADVGKNQVRFGALKYADDPEVLFYLDELGTKLEVVSVLQNDHPMGGNT-Y 886
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   887 TAEALAF-SDHMFTEARGSRlhKGVPQVLIVITDGESHDAEkLNTTAKALRDKGILVLAVGIAGANSWELLAMAGSSDK- 964
Cdd:pfam00092   81 TGKALKYaLENLFSSAAGAR--PGAPKVVVLLTDGRSQDGD-PEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEg 157

                          170
                   ....*....|....*..
gi 156616288   965 -YYFVETFGGLKGIFSD 980
Cdd:pfam00092  158 hVFTVSDFEALEDLQDQ 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 807-968 2.97e-38

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: 140.50  E-value: 2.97e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  807 LDVVFVIDSSGSIDYQEYNIMKDFMIGLVKKADVGKNQVRFGALKYADDPEVLFYLDELGTKLEVVSVLQNDHPMGGN-T 885
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  886 YTAEALAF-SDHMFTEargSRLHKGVPQVLIVITDGESHDAEKLNTTAKALRDKGILVLAVGIAGANSWELLAMAGSSDK 964
Cdd:cd01450    81 NTGKALQYaLEQLFSE---SNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSE 157


                  ....
gi 156616288  965 YYFV 968
Cdd:cd01450   158 RHVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 621-790 1.80e-37

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: 138.74  E-value: 1.80e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288    621 DIMFLVDSSGSIGPENFSKMKMFMKNLVSKSQIGADRVQIGVVQFSHENKEEFQLNTFMSQSDIANAIDRMTHI-GETTL 699
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288    700 TGSALTFVSQY-FSPDKGARPNVRKFLILITDGEAQD---IVRDPAIALRKEGVIIYSVGV-FGSNVTQLEEISGKPeMV 774
Cdd:smart00327   81 LGAALQYALENlFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAP-GG 159

                           170
                    ....*....|....*.
gi 156616288    775 FYVENFDILQHIEDDL 790
Cdd:smart00327  160 VYVFLPELLDLLIDLL 175
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 25-179 9.21e-37

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: 136.20  E-value: 9.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   25 ADVVFLVDSSDHLGLKSFPLVKTFIHKMISSLPIEANKYRVALAQYSDALHNEFQLGTFKNRNPMLNHLkKNFGFIGGSL 104
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAV-KNLRYIGGGT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156616288  105 KIGNALQEAHRTYFSAPTngRDKKQFPPILVVLASAESEDDVEEAAKALREDGVKIISVGVQKASEENLKAMATS 179
Cdd:cd01472    80 NTGKALKYVRENLFTEAS--GSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASD 152
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 227-392 7.38e-35

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: 130.81  E-value: 7.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  227 ADVVFLLDmainGS----QEDLDHLKAFLGESISALDIKENCMRVGLVTYSNETRVISSLSTGNNKTEVLQRIQDLSPQV 302
Cdd:cd01472     1 ADIVFLVD----GSesigLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  303 GQAYTGAALRKTRKEIFSAQRGSRKnqGVPQIAVLVTHRASEDNVTKAAVNLRREGVTIFTMGIEGANPDELEKIASHPA 382
Cdd:cd01472    77 GGTNTGKALKYVRENLFTEASGSRE--GVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPK 154

                         170
                  ....*....|
gi 156616288  383 EQFTSKLGNF 392
Cdd:cd01472   155 ELYVFNVADF 164
VWA pfam00092
von Willebrand factor type A domain;
228-397 1.07e-34

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 130.86  E-value: 1.07e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   228 DVVFLLDMAINGSQEDLDHLKAFLGESISALDIKENCMRVGLVTYSNETRVISSLSTGNNKTEVLQRIQDLSPQ-VGQAY 306
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   307 TGAALRKTRKEIFSAQRGSRKNqgVPQIAVLVTHRASED-NVTKAAVNLRREGVTIFTMGIEGANPDELEKIASHPAEQF 385
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPG--APKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGH 158

                          170
                   ....*....|..
gi 156616288   386 TSKLGNFSELAT 397
Cdd:pfam00092  159 VFTVSDFEALED 170
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 999-1162 8.82e-33

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: 125.26  E-value: 8.82e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288    999 DLVFLMDGSNSIHPDDFQKMKGFLVSVVQDFDVSLNRVRIGVAQFSDSYRSEFLLGTFTGEREISTQIEGIQQIF-GYTH 1077
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLgGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   1078 IGDALRKV-KYYFQPDMGSRINAgtPQVLLVLTDGRSQD---EVAQAAEELRHKGVDIYSVGIG-DVDDQELVQItgtAE 1152
Cdd:smart00327   81 LGAALQYAlENLFSKSAGSRRGA--PKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGnDVDEEELKKL---AS 155

                           170
                    ....*....|
gi 156616288   1153 KKLTVHNFDE 1162
Cdd:smart00327  156 APGGVYVFLP 165
VWA pfam00092
von Willebrand factor type A domain;
26-191 1.03e-32

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 125.08  E-value: 1.03e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288    26 DVVFLVDSSDHLGLKSFPLVKTFIHKMISSLPIEANKYRVALAQYSDALHNEFQLGTFKNRNPMLNHLKKNFGFIGGSLK 105
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   106 IGNALQEAHRTYFSAPTNGRdkKQFPPILVVLASAESED-DVEEAAKALREDGVKIISVGVQKASEENLKAMATS---QF 181
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEpgeGH 158

                          170
                   ....*....|
gi 156616288   182 HFNLRTARDL 191
Cdd:pfam00092  159 VFTVSDFEAL 168
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 808-971 1.11e-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: 124.87  E-value: 1.11e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288    808 DVVFVIDSSGSIDYQEYNIMKDFMIGLVKKADVGKNQVRFGALKYADDPEVLFYLDELGTKLEVVSVLQNDHP-MGGNTY 886
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288    887 TAEALAF-SDHMFTEARGSRlhKGVPQVLIVITDGESHDAEK-LNTTAKALRDKGILVLAVGIAGANSWELL---AMAGS 961
Cdd:smart00327   81 LGAALQYaLENLFSKSAGSR--RGAPKVVILITDGESNDGPKdLLKAAKELKRSGVKVFVVGVGNDVDEEELkklASAPG 158

                           170
                    ....*....|
gi 156616288    962 SDKYYFVETF 971
Cdd:smart00327  159 GVYVFLPELL 168
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 435-592 4.09e-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: 120.64  E-value: 4.09e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288    435 DIYLLIDGSGSTQPTDFHEMKTFLSEVVGMFNIAPHKVRVGAVQYADTWDLEFEISKYSNKPDLGKAIENIR-QMGGNTN 513
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288    514 TGAALNFTLKLLQRAKKERGSKVPCHLVVLTNGMSRDS---VLGPAHKLREENIRVHAIGVKEA-NQTQLREIAGEEKRV 589
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160


                    ...
gi 156616288    590 YYV 592
Cdd:smart00327  161 YVF 163
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 228-397 8.56e-27

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: 108.31  E-value: 8.56e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288    228 DVVFLLDMAINGSQEDLDHLKAFLGESISALDIKENCMRVGLVTYSNETRVISSLSTGNNKTEVLQRIQDLSPQ-VGQAY 306
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288    307 TGAALRKTRKEIFSAQRGSRKnqGVPQIAVLVT---HRASEDNVTKAAVNLRREGVTIFTMGIEGA-NPDELEKIASHPA 382
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRR--GAPKVVILITdgeSNDGPKDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPG 158

                           170
                    ....*....|....*
gi 156616288    383 EQFTSKLGNFSELAT 397
Cdd:smart00327  159 GVYVFLPELLDLLID 173
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 26-192 1.46e-26

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: 107.54  E-value: 1.46e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288     26 DVVFLVDSSDHLGLKSFPLVKTFIHKMISSLPIEANKYRVALAQYSDALHNEFQLGTFKNRNPMLNHLKKNFGFIGGSLK 105
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288    106 IGNALQEAHRTYFSAPTNGRdkKQFPPILVVLASAESED---DVEEAAKALREDGVKIISVGV-QKASEENLKAMA---T 178
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLAsapG 158

                           170
                    ....*....|....
gi 156616288    179 SQFHFNLRTARDLS 192
Cdd:smart00327  159 GVYVFLPELLDLLI 172
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 432-601 7.20e-15

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 76.13  E-value: 7.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  432 EEADIYLLIDGSGSTQPTD-FHEMKTFLSEVVGMFniaPHKVRVGAVQYADTWDLEFEISkySNKPDLGKAIENIrQMGG 510
Cdd:COG1240    91 RGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLT--RDREALKRALDEL-PPGG 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  511 NTNTGAALNFTLKLLQRAKKERgskvPCHLVVLTNGMSRDSVLGP---AHKLREENIRVHAIGV--KEANQTQLREIAGE 585
Cdd:COG1240   165 GTPLGDALALALELLKRADPAR----RKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVgtEAVDEGLLREIAEA 240

                         170
                  ....*....|....*..
gi 156616288  586 EK-RVYYVHEFDALRNI 601
Cdd:COG1240   241 TGgRYFRADDLSELAAI 257
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 620-786 1.16e-14

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 75.36  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  620 ADIMFLVDSSGSIGPEN-FSKMKMFMKNLVSKSQigaDRVQIGVVQFSHENKEEFQLNTfmSQSDIANAIDRMThIGETT 698
Cdd:COG1240    93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEVLLPLTR--DREALKRALDELP-PGGGT 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  699 LTGSALTFVSQYFspdKGARPNVRKFLILITDGEAQDIVRDP---AIALRKEGVIIYSVGVFGSNV--TQLEEIS----G 769
Cdd:COG1240   167 PLGDALALALELL---KRADPARRKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVGTEAVdeGLLREIAeatgG 243

                         170
                  ....*....|....*..
gi 156616288  770 KpemVFYVENFDILQHI 786
Cdd:COG1240   244 R---YFRADDLSELAAI 257
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 998-1147 5.64e-14

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 73.43  E-value: 5.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  998 VDLVFLMDGSNSIH-PDDFQKMKGFLVSVVQDFdvsLNRVRIGVAQFSDsyRSEFLLGtFTGERE-ISTQIEGIQqIFGY 1075
Cdd:COG1240    93 RDVVLVVDASGSMAaENRLEAAKGALLDFLDDY---RPRDRVGLVAFGG--EAEVLLP-LTRDREaLKRALDELP-PGGG 165

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156616288 1076 THIGDALRKVKyyfqpDMGSRINAGTPQVLLVLTDGR---SQDEVAQAAEELRHKGVDIYSVGIGD--VDDQELVQI 1147
Cdd:COG1240   166 TPLGDALALAL-----ELLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTeaVDEGLLREI 237
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 807-981 6.17e-12

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 67.27  E-value: 6.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  807 LDVVFVIDSSGSIDYQE-YNIMKDFMIGLVKKADVGknqVRFGALKYADDPEVLFyldELGTKLEVVSVLQNDHPMGGNT 885
Cdd:COG1240    93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPR---DRVGLVAFGGEAEVLL---PLTRDREALKRALDELPPGGGT 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  886 YTAEALAFSDHMFteargSRLHKGVPQVLIVITDGESHD-AEKLNTTAKALRDKGI--LVLAVGIAGANSWELLAMAGSS 962
Cdd:COG1240   167 PLGDALALALELL-----KRADPARRKVIVLLTDGRDNAgRIDPLEAAELAAAAGIriYTIGVGTEAVDEGLLREIAEAT 241

                         170       180
                  ....*....|....*....|
gi 156616288  963 D-KYYFVETFGGLKGIFSDV 981
Cdd:COG1240   242 GgRYFRADDLSELAAIYREI 261
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 213-378 9.91e-12

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 66.89  E-value: 9.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  213 ADDIIVEACQGPSVADVVFLLD----MAingSQEDLDHLKAFLGESISALDIKEncmRVGLVTYSNETRVISSLSTgnNK 288
Cdd:COG1240    79 LALAPLALARPQRGRDVVLVVDasgsMA---AENRLEAAKGALLDFLDDYRPRD---RVGLVAFGGEAEVLLPLTR--DR 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  289 TEVLQRIQDLSPQvGQAYTGAALRKtrkeifSAQRGSRKNQGVPQIAVLVT---HRASEDNVTKAAVNLRREGVTIFT-- 363
Cdd:COG1240   151 EALKRALDELPPG-GGTPLGDALAL------ALELLKRADPARRKVIVLLTdgrDNAGRIDPLEAAELAAAAGIRIYTig 223

                         170
                  ....*....|....*
gi 156616288  364 MGIEGANPDELEKIA 378
Cdd:COG1240   224 VGTEAVDEGLLREIA 238
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 603-756 8.21e-07

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 53.04  E-value: 8.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  603 NQVVQEI-CAEEACRDmKADIMFLVDSSGSIGPENF--SKMKMFMKnLVSKSQIGADRVQIGVVQFSHENKEEFQLNTFM 679
Cdd:PTZ00441   26 NKIVDEVkYREEVCNE-EVDLYLLVDGSGSIGYHNWitHVIPMLMG-LIQQLNLSDDAINLYMSLFSNNTTELIRLGSGA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  680 SQsDIANAIDRMTHI-------GETTLTgSALTFVSQYFSpDKGARPNVRKFLILITDGEAQDIVR--DPAIALRKEGVI 750
Cdd:PTZ00441  104 SK-DKEQALIIVKSLrktylpyGKTNMT-DALLEVRKHLN-DRVNRENAIQLVILMTDGIPNSKYRalEESRKLKDRNVK 180


                  ....*.
gi 156616288  751 IYSVGV 756
Cdd:PTZ00441  181 LAVIGI 186
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 982-1137 4.32e-06

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 50.73  E-value: 4.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  982 SASVCNsskvdceiEKVDLVFLMDGSNSI-HPDDFQKMKGFLVSVVQDFDVSLNRVRIGVAQFSDSYRSEFLLGTFTGER 1060
Cdd:PTZ00441   35 REEVCN--------EEVDLYLLVDGSGSIgYHNWITHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASKD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288 1061 E-----ISTQIEGIQQIFGYTHIGDALRKVKYYFQpDMGSRINAGtpQVLLVLTDG--RSQDEVAQAAEELRHKGVDIYS 1133
Cdd:PTZ00441  107 KeqaliIVKSLRKTYLPYGKTNMTDALLEVRKHLN-DRVNRENAI--QLVILMTDGipNSKYRALEESRKLKDRNVKLAV 183


                  ....
gi 156616288 1134 VGIG 1137
Cdd:PTZ00441  184 IGIG 187
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 18-192 1.82e-04

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 44.54  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   18 QDSGPEYADVVFLVDSSDHLGLKS-FPLVKTFIHKMISSLPIEAnkyRVALAQYSD----ALHNEFQLGTFKNRnpmLNH 92
Cdd:COG1240    86 LARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRD---RVGLVAFGGeaevLLPLTRDREALKRA---LDE 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   93 LKknfgfIGGSLKIGNALQEAHRTYFSAPTNGRdkkqfpPILVVL---ASAESEDDVEEAAKALREDGVKI--ISVGVQK 167
Cdd:COG1240   160 LP-----PGGGTPLGDALALALELLKRADPARR------KVIVLLtdgRDNAGRIDPLEAAELAAAAGIRIytIGVGTEA 228

                         170       180
                  ....*....|....*....|....*...
gi 156616288  168 ASEENLKAMATS---QFhFNLRTARDLS 192
Cdd:COG1240   229 VDEGLLREIAEAtggRY-FRADDLSELA 255
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 1000-1141 7.02e-04

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 43.06  E-value: 7.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  1000 LVFLMDGSNSIHPD-DF--QKMKGFLVSVVQDFDvslnrvRIGVAQFSDsyrSEFLLGTFTGE-REISTQIEGIQ----- 1070
Cdd:TIGR03436   56 VGLVIDTSGSMRNDlDRarAAAIRFLKTVLRPND------RVFVVTFNT---RLRLLQDFTSDpRLLEAALNRLKpplrt 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  1071 -----QIFGYTHIGDALRKVKYYFQPDMGSRINAGTP--QVLLVLTDG---RSQDEVAQAAEELRHKGVDIYSVGIGDVD 1140
Cdd:TIGR03436  127 dynssGAFVRDGGGTALYDAITLAALEQLANALAGIPgrKALIVISDGgdnRSRDTLERAIDAAQRADVAIYSIDARGLR 206


                   .
gi 156616288  1141 D 1141
Cdd:TIGR03436  207 A 207
 
Name Accession Description Interval E-value
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 620-783 4.66e-49

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 171.64  E-value: 4.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  620 ADIMFLVDSSGSIGPENFSKMKMFMKNLVSKSQIGADRVQIGVVQFSHENKEEFQLNTFMSQSDIANAIDRMTHIGETTL 699
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  700 TGSALTFVS-QYFSPDKGARPNVRKFLILITDGEAQDIVRDPAIALRKEGVIIYSVGVFGSNVTQLEEISGKPEmVFYVE 778
Cdd:cd01472    81 TGKALKYVReNLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPK-ELYVF 159


                  ....*
gi 156616288  779 NFDIL 783
Cdd:cd01472   160 NVADF 164
VWA pfam00092
von Willebrand factor type A domain;
621-789 7.24e-49

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 171.30  E-value: 7.24e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   621 DIMFLVDSSGSIGPENFSKMKMFMKNLVSKSQIGADRVQIGVVQFSHENKEEFQLNTFMSQSDIANAIDRMTHI-GETTL 699
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   700 TGSALTFV-SQYFSPDKGARPNVRKFLILITDGEAQDI-VRDPAIALRKEGVIIYSVGVFGSNVTQLEEISGKP--EMVF 775
Cdd:pfam00092   81 TGKALKYAlENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPgeGHVF 160

                          170
                   ....*....|....
gi 156616288   776 YVENFDILQHIEDD 789
Cdd:pfam00092  161 TVSDFEALEDLQDQ 174
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 620-780 9.11e-46

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: 162.07  E-value: 9.11e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  620 ADIMFLVDSSGSIGPENFSKMKMFMKNLVSKSQIGADRVQIGVVQFSHENKEEFQLNTFMSQSDIANAIDRMTHIGETTL 699
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  700 TGSALTFVSQ-YFSPDKGARPNVRKFLILITDGEAQDIVRDPAIALRKEGVIIYSVGVFGSNVTQLEEISGKP--EMVFY 776
Cdd:cd01482    81 TGKALTHVREkNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPseTHVFN 160


                  ....
gi 156616288  777 VENF 780
Cdd:cd01482   161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
435-604 2.12e-43

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 155.51  E-value: 2.12e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   435 DIYLLIDGSGSTQPTDFHEMKTFLSEVVGMFNIAPHKVRVGAVQYADTWDLEFEISKYSNKPDLGKAIENIRQMGGNT-N 513
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   514 TGAALNFTLKLLQRAKKERGSKVPCHLVVLTNGMSRD-SVLGPAHKLREENIRVHAIGVKEANQTQLREIAGE--EKRVY 590
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEpgEGHVF 160

                          170
                   ....*....|....
gi 156616288   591 YVHEFDALRNIRNQ 604
Cdd:pfam00092  161 TVSDFEALEDLQDQ 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 620-775 3.38e-42

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: 151.68  E-value: 3.38e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  620 ADIMFLVDSSGSIGPENFSKMKMFMKNLVSKSQIGADRVQIGVVQFSHENKEEFQLNTFMSQSDIANAIDRMTHI-GETT 698
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLgGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  699 LTGSALTFVSQYFSPDKGARPNVRKFLILITDGEAQD--IVRDPAIALRKEGVIIYSVGVFGSNVTQLEEISGKP--EMV 774
Cdd:cd01450    81 NTGKALQYALEQLFSESNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPseRHV 160


                  .
gi 156616288  775 F 775
Cdd:cd01450   161 F 161
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 620-801 1.26e-41

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: 152.54  E-value: 1.26e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  620 ADIMFLVDSSGSIGPENFSKMKMFMKNLVSKSQIGADRVQIGVVQFSHENKEEFQLNTFMSQSDIANAIDRMTHIGETTL 699
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  700 TGSALTF-VSQYFSPDKGARP---NVRKFLILITDGEAQDIVRDPAIALRKEGVIIYSVGVFGSNVTQLEEISGKP--EM 773
Cdd:cd01475    83 TGLAIQYaMNNAFSEAEGARPgseRVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPlaDH 162

                         170       180
                  ....*....|....*....|....*...
gi 156616288  774 VFYVENFDILQHIEDDLVLGICSPREEC 801
Cdd:cd01475   163 VFYVEDFSTIEELTKKFQGKICVVPDLC 190
VWA pfam00092
von Willebrand factor type A domain;
999-1166 1.78e-40

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 147.42  E-value: 1.78e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   999 DLVFLMDGSNSIHPDDFQKMKGFLVSVVQDFDVSLNRVRIGVAQFSDSYRSEFLLGTFTGEREISTQIEGIQQIF-GYTH 1077
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGgGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  1078 IGDALRKV-KYYFQPDMGSRINAgtPQVLLVLTDGRSQD-EVAQAAEELRHKGVDIYSVGIGDVDDQELVQITGTAEKKL 1155
Cdd:pfam00092   81 TGKALKYAlENLFSSAAGARPGA--PKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGH 158

                          170
                   ....*....|...
gi 156616288  1156 --TVHNFDELKKV 1166
Cdd:pfam00092  159 vfTVSDFEALEDL 171
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 434-595 1.99e-40

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: 146.60  E-value: 1.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  434 ADIYLLIDGSGSTQPTDFHEMKTFLSEVVGMFNIAPHKVRVGAVQYADTWDLEFEISKYSNKPDLGKAIENIRQMGGNTN 513
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  514 TGAALNFTLKLLQRAKKERGSKVPCHLVVLTNGMSRDSVLGPAHKLREENIRVHAIGVKEANQTQLREIA--GEEKRVYY 591
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIAsdPKELYVFN 160


                  ....
gi 156616288  592 VHEF 595
Cdd:cd01472   161 VADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 998-1163 2.13e-39

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: 143.91  E-value: 2.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  998 VDLVFLMDGSNSIHPDDFQKMKGFLVSVVQDFDVSLNRVRIGVAQFSDSYRSEFLLGTFTGEREISTQIEGIQQIFGYTH 1077
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288 1078 IGDALRKV-KYYFQPDMGSRinAGTPQVLLVLTDGRSQDEVAQAAEELRHKGVDIYSVGIGDVDDQELVQITGTAeKKLT 1156
Cdd:cd01472    81 TGKALKYVrENLFTEASGSR--EGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDP-KELY 157


                  ....*..
gi 156616288 1157 VHNFDEL 1163
Cdd:cd01472   158 VFNVADF 164
VWA pfam00092
von Willebrand factor type A domain;
808-980 4.64e-39

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 143.18  E-value: 4.64e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   808 DVVFVIDSSGSIDYQEYNIMKDFMIGLVKKADVGKNQVRFGALKYADDPEVLFYLDELGTKLEVVSVLQNDHPMGGNT-Y 886
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   887 TAEALAF-SDHMFTEARGSRlhKGVPQVLIVITDGESHDAEkLNTTAKALRDKGILVLAVGIAGANSWELLAMAGSSDK- 964
Cdd:pfam00092   81 TGKALKYaLENLFSSAAGAR--PGAPKVVVLLTDGRSQDGD-PEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEg 157

                          170
                   ....*....|....*..
gi 156616288   965 -YYFVETFGGLKGIFSD 980
Cdd:pfam00092  158 hVFTVSDFEALEDLQDQ 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 807-968 2.97e-38

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: 140.50  E-value: 2.97e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  807 LDVVFVIDSSGSIDYQEYNIMKDFMIGLVKKADVGKNQVRFGALKYADDPEVLFYLDELGTKLEVVSVLQNDHPMGGN-T 885
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  886 YTAEALAF-SDHMFTEargSRLHKGVPQVLIVITDGESHDAEKLNTTAKALRDKGILVLAVGIAGANSWELLAMAGSSDK 964
Cdd:cd01450    81 NTGKALQYaLEQLFSE---SNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSE 157


                  ....
gi 156616288  965 YYFV 968
Cdd:cd01450   158 RHVF 161
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 998-1153 6.25e-38

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: 139.35  E-value: 6.25e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  998 VDLVFLMDGSNSIHPDDFQKMKGFLVSVVQDFDVSLNRVRIGVAQFSDSYRSEFLLGTFTGEREISTQIEGIQQIFG-YT 1076
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288 1077 HIGDALRKV-KYYFQPdmgSRINAGTPQVLLVLTDGRSQD--EVAQAAEELRHKGVDIYSVGIGDVDDQELVQITGTAEK 1153
Cdd:cd01450    81 NTGKALQYAlEQLFSE---SNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSE 157
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 434-595 6.61e-38

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: 139.73  E-value: 6.61e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  434 ADIYLLIDGSGSTQPTDFHEMKTFLSEVVGMFNIAPHKVRVGAVQYADTWDLEFEISKYSNKPDLGKAIENIRQMGGNTN 513
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  514 TGAALNFTL-KLLQRAKKERgSKVPCHLVVLTNGMSRDSVLGPAHKLREENIRVHAIGVKEANQTQLREIAGE--EKRVY 590
Cdd:cd01482    81 TGKALTHVReKNFTPDAGAR-PGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKpsETHVF 159


                  ....*
gi 156616288  591 YVHEF 595
Cdd:cd01482   160 NVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 808-972 1.63e-37

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: 138.51  E-value: 1.63e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  808 DVVFVIDSSGSIDYQEYNIMKDFMIGLVKKADVGKNQVRFGALKYADDPEVLFYLDELGTKLEVVSVLQNDHPMGGNTYT 887
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  888 AEALAF-SDHMFTEARGSRlhKGVPQVLIVITDGESHDaeKLNTTAKALRDKGILVLAVGIAGANSWELLAMAgSSDKYY 966
Cdd:cd01472    82 GKALKYvRENLFTEASGSR--EGVPKVLVVITDGKSQD--DVEEPAVELKQAGIEVFAVGVKNADEEELKQIA-SDPKEL 156


                  ....*.
gi 156616288  967 FVETFG 972
Cdd:cd01472   157 YVFNVA 162
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 621-790 1.80e-37

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: 138.74  E-value: 1.80e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288    621 DIMFLVDSSGSIGPENFSKMKMFMKNLVSKSQIGADRVQIGVVQFSHENKEEFQLNTFMSQSDIANAIDRMTHI-GETTL 699
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288    700 TGSALTFVSQY-FSPDKGARPNVRKFLILITDGEAQD---IVRDPAIALRKEGVIIYSVGV-FGSNVTQLEEISGKPeMV 774
Cdd:smart00327   81 LGAALQYALENlFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAP-GG 159

                           170
                    ....*....|....*.
gi 156616288    775 FYVENFDILQHIEDDL 790
Cdd:smart00327  160 VYVFLPELLDLLIDLL 175
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 25-179 9.21e-37

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: 136.20  E-value: 9.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   25 ADVVFLVDSSDHLGLKSFPLVKTFIHKMISSLPIEANKYRVALAQYSDALHNEFQLGTFKNRNPMLNHLkKNFGFIGGSL 104
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAV-KNLRYIGGGT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156616288  105 KIGNALQEAHRTYFSAPTngRDKKQFPPILVVLASAESEDDVEEAAKALREDGVKIISVGVQKASEENLKAMATS 179
Cdd:cd01472    80 NTGKALKYVRENLFTEAS--GSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASD 152
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 620-780 1.98e-36

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: 135.53  E-value: 1.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  620 ADIMFLVDSSGSIGPENFSKMKMFMKNLVSKSQIGADRVQIGVVQFSHENKEEFQLNTFMSQSDIANAIDRMTHIGETTL 699
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  700 -TGSALTFVSQ-YFSPDKGAR--PNVRKFLILITDGEAQDIVRDPAIALRKEGVIIYSVGVFGSNVTQLEEISGKPEMVF 775
Cdd:cd01481    81 nTGSALDYVVKnLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                  ....*
gi 156616288  776 YVENF 780
Cdd:cd01481   161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 25-187 8.72e-36

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: 133.60  E-value: 8.72e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   25 ADVVFLVDSSDHLGLKSFPLVKTFIHKMISSLPIEANKYRVALAQYSDALHNEFQLGTFKNRNPMLNHLKKnFGFIGGS- 103
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRR-LRLRGGSq 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  104 LKIGNALQEAHRTYFSAPTNGRDKKQFPPILVVLASAESEDDVEEAAKALREDGVKIISVGVQKASEENLKAMATS-QFH 182
Cdd:cd01481    80 LNTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDpSFV 159


                  ....*
gi 156616288  183 FNLRT 187
Cdd:cd01481   160 FQVSD 164
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 434-592 1.55e-35

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 132.80  E-value: 1.55e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  434 ADIYLLIDGSGSTQPTDFHEMKTFLSEVVGMFNIAPHKVRVGAVQYADTWDLEFEISKYSNKPDLGKAIENIRQMGGN-T 512
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  513 NTGAALNFTLKLLQRaKKERGSKVPCHLVVLTNGMSRD--SVLGPAHKLREENIRVHAIGVKEANQTQLREIAGEEKRVY 590
Cdd:cd01450    81 NTGKALQYALEQLFS-ESNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSERH 159


                  ..
gi 156616288  591 YV 592
Cdd:cd01450   160 VF 161
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 227-392 7.38e-35

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: 130.81  E-value: 7.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  227 ADVVFLLDmainGS----QEDLDHLKAFLGESISALDIKENCMRVGLVTYSNETRVISSLSTGNNKTEVLQRIQDLSPQV 302
Cdd:cd01472     1 ADIVFLVD----GSesigLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  303 GQAYTGAALRKTRKEIFSAQRGSRKnqGVPQIAVLVTHRASEDNVTKAAVNLRREGVTIFTMGIEGANPDELEKIASHPA 382
Cdd:cd01472    77 GGTNTGKALKYVRENLFTEASGSRE--GVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPK 154

                         170
                  ....*....|
gi 156616288  383 EQFTSKLGNF 392
Cdd:cd01472   155 ELYVFNVADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 999-1163 8.27e-35

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: 130.87  E-value: 8.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  999 DLVFLMDGSNSIHPDDFQKMKGFLVSVVQDFDVSLNRVRIGVAQFSDSYRSEFLLGTFTGEREISTQIEGIQQIFGYTHI 1078
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288 1079 GDALRKV-KYYFQPDMGSRinAGTPQVLLVLTDGRSQDEVAQAAEELRHKGVDIYSVGIGDVDDQELVQITGTAEkKLTV 1157
Cdd:cd01482    82 GKALTHVrEKNFTPDAGAR--PGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPS-ETHV 158


                  ....*.
gi 156616288 1158 HNFDEL 1163
Cdd:cd01482   159 FNVADF 164
VWA pfam00092
von Willebrand factor type A domain;
228-397 1.07e-34

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 130.86  E-value: 1.07e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   228 DVVFLLDMAINGSQEDLDHLKAFLGESISALDIKENCMRVGLVTYSNETRVISSLSTGNNKTEVLQRIQDLSPQ-VGQAY 306
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   307 TGAALRKTRKEIFSAQRGSRKNqgVPQIAVLVTHRASED-NVTKAAVNLRREGVTIFTMGIEGANPDELEKIASHPAEQF 385
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPG--APKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGH 158

                          170
                   ....*....|..
gi 156616288   386 TSKLGNFSELAT 397
Cdd:pfam00092  159 VFTVSDFEALED 170
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 621-786 5.00e-34

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 129.01  E-value: 5.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  621 DIMFLVDSSGSIGPENFSKMKMFMKNLVSKSQIGADRVQIGVVQFSHENKEEFQLNTFMSQSDIANAIDRMTHIGETTLT 700
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  701 GSALTFV-SQYFSPDKGARPNVRKFLILITDGEAQDIVRDPAI--ALRKEGVIIYSVGVFG-----SNVTQLEEISGKP- 771
Cdd:cd01469    82 ATAIQYVvTELFSESNGARKDATKVLVVITDGESHDDPLLKDVipQAEREGIIRYAIGVGGhfqreNSREELKTIASKPp 161

                         170
                  ....*....|....*.
gi 156616288  772 -EMVFYVENFDILQHI 786
Cdd:cd01469   162 eEHFFNVTDFAALKDI 177
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 999-1160 2.43e-33

VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238758  Cd Length: 165  Bit Score: 126.67  E-value: 2.43e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  999 DLVFLMDGSNSIHPDDFQKMKGFLVSVVQDFDVSLNRVRIGVAQFSDSYRSEFLLGTFTGEREISTQIEGIQQIFGY-TH 1077
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSqLN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288 1078 IGDALRKV-KYYFQPDMGSRINAGTPQVLLVLTDGRSQDEVAQAAEELRHKGVDIYSVGIGDVDDQELVQITGTAEKKLT 1156
Cdd:cd01481    82 TGSALDYVvKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVFQ 161


                  ....
gi 156616288 1157 VHNF 1160
Cdd:cd01481   162 VSDF 165
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 999-1162 8.82e-33

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: 125.26  E-value: 8.82e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288    999 DLVFLMDGSNSIHPDDFQKMKGFLVSVVQDFDVSLNRVRIGVAQFSDSYRSEFLLGTFTGEREISTQIEGIQQIF-GYTH 1077
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLgGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   1078 IGDALRKV-KYYFQPDMGSRINAgtPQVLLVLTDGRSQD---EVAQAAEELRHKGVDIYSVGIG-DVDDQELVQItgtAE 1152
Cdd:smart00327   81 LGAALQYAlENLFSKSAGSRRGA--PKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGnDVDEEELKKL---AS 155

                           170
                    ....*....|
gi 156616288   1153 KKLTVHNFDE 1162
Cdd:smart00327  156 APGGVYVFLP 165
VWA pfam00092
von Willebrand factor type A domain;
26-191 1.03e-32

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 125.08  E-value: 1.03e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288    26 DVVFLVDSSDHLGLKSFPLVKTFIHKMISSLPIEANKYRVALAQYSDALHNEFQLGTFKNRNPMLNHLKKNFGFIGGSLK 105
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   106 IGNALQEAHRTYFSAPTNGRdkKQFPPILVVLASAESED-DVEEAAKALREDGVKIISVGVQKASEENLKAMATS---QF 181
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEpgeGH 158

                          170
                   ....*....|
gi 156616288   182 HFNLRTARDL 191
Cdd:pfam00092  159 VFTVSDFEAL 168
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 808-971 1.09e-32

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: 124.71  E-value: 1.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  808 DVVFVIDSSGSIDYQEYNIMKDFMIGLVKKADVGKNQVRFGALKYADDPEVLFYLDELGTKLEVVSVLQNDHPMGGNTYT 887
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  888 AEALAF-SDHMFTEARGSRlhKGVPQVLIVITDGESHDAekLNTTAKALRDKGILVLAVGIAGANSWELLAMAG--SSDK 964
Cdd:cd01482    82 GKALTHvREKNFTPDAGAR--PGVPKVVILITDGKSQDD--VELPARVLRNLGVNVFAVGVKDADESELKMIASkpSETH 157


                  ....*..
gi 156616288  965 YYFVETF 971
Cdd:cd01482   158 VFNVADF 164
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 808-971 1.11e-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: 124.87  E-value: 1.11e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288    808 DVVFVIDSSGSIDYQEYNIMKDFMIGLVKKADVGKNQVRFGALKYADDPEVLFYLDELGTKLEVVSVLQNDHP-MGGNTY 886
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288    887 TAEALAF-SDHMFTEARGSRlhKGVPQVLIVITDGESHDAEK-LNTTAKALRDKGILVLAVGIAGANSWELL---AMAGS 961
Cdd:smart00327   81 LGAALQYaLENLFSKSAGSR--RGAPKVVILITDGESNDGPKdLLKAAKELKRSGVKVFVVGVGNDVDEEELkklASAPG 158

                           170
                    ....*....|
gi 156616288    962 SDKYYFVETF 971
Cdd:smart00327  159 GVYVFLPELL 168
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 998-1175 3.73e-32

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 125.19  E-value: 3.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  998 VDLVFLMDGSNSIHPDDFQKMKGFLVSVVQDFDVSLNRVRIGVAQFSDSYRSEFLLGTFTGEREISTQIEGIQQIFGYTH 1077
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288 1078 IGDALR-KVKYYFQPDMGSR-INAGTPQVLLVLTDGRSQDEVAQAAEELRHKGVDIYSVGIGDVDDQELVQITG--TAEK 1153
Cdd:cd01475    83 TGLAIQyAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASepLADH 162

                         170       180
                  ....*....|....*....|..
gi 156616288 1154 KLTVHNFDELKKVKKRIVRNIC 1175
Cdd:cd01475   163 VFYVEDFSTIEELTKKFQGKIC 184
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 620-777 4.23e-32

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 122.67  E-value: 4.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  620 ADIMFLVDSSGSIGPENFSKMKMFMKNLVSKSQIGADRVQIGVVQFSHENKEEFQLNTFMSQSDIANAIDRMTH-IGETT 698
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  699 LTGSALTFVSQYFspDKGARPNVRKFLILITDGEAQD---IVRDPAIALRKEGVIIYSVGV-FGSNVTQLEEISGKPEMV 774
Cdd:cd00198    81 NIGAALRLALELL--KSAKRPNARRVIILLTDGEPNDgpeLLAEAARELRKLGITVYTIGIgDDANEDELKEIADKTTGG 158


                  ...
gi 156616288  775 FYV 777
Cdd:cd00198   159 AVF 161
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 807-977 4.65e-32

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 123.23  E-value: 4.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  807 LDVVFVIDSSGSIDYQEYNIMKDFMIGLVKKADVGKNQVRFGALKYADDPEVLFYLDELGTKLEVVSVLQNDHPMGGNTY 886
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  887 TAEALAFS-DHMFTEARGSRlhKGVPQVLIVITDGESHDAEKLNTTAKALRDKGILVLAVGIAGA----NSWELLAMAGS 961
Cdd:cd01469    81 TATAIQYVvTELFSESNGAR--KDATKVLVVITDGESHDDPLLKDVIPQAEREGIIRYAIGVGGHfqreNSREELKTIAS 158

                         170
                  ....*....|....*....
gi 156616288  962 --SDKYYF-VETFGGLKGI 977
Cdd:cd01469   159 kpPEEHFFnVTDFAALKDI 177
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 25-181 2.22e-31

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: 120.85  E-value: 2.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   25 ADVVFLVDSSDHLGLKSFPLVKTFIHKMISSLPIEANKYRVALAQYSDALHNEFQLGTFKNRNPMLNHLkKNFGFIGGSL 104
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAI-KNLPYKGGNT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156616288  105 KIGNALQEAHRTYFSAPTNGRdkKQFPPILVVLASAESEDDVEEAAKALREDGVKIISVGVQKASEENLKAMATSQF 181
Cdd:cd01482    80 RTGKALTHVREKNFTPDAGAR--PGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPS 154
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 435-592 4.09e-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: 120.64  E-value: 4.09e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288    435 DIYLLIDGSGSTQPTDFHEMKTFLSEVVGMFNIAPHKVRVGAVQYADTWDLEFEISKYSNKPDLGKAIENIR-QMGGNTN 513
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288    514 TGAALNFTLKLLQRAKKERGSKVPCHLVVLTNGMSRDS---VLGPAHKLREENIRVHAIGVKEA-NQTQLREIAGEEKRV 589
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160


                    ...
gi 156616288    590 YYV 592
Cdd:smart00327  161 YVF 163
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 808-971 6.33e-31

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: 119.74  E-value: 6.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  808 DVVFVIDSSGSIDYQEYNIMKDFMIGLVKKADVGKNQVRFGALKYADDPEVLFYLDELGTKLEVVSVLQNDHPMGGN-TY 886
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSqLN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  887 TAEALAF-SDHMFTEARGSRLHKGVPQVLIVITDGESHDAekLNTTAKALRDKGILVLAVGIAGANSWELLAMAGSSDKY 965
Cdd:cd01481    82 TGSALDYvVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDD--VERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFV 159


                  ....*.
gi 156616288  966 YFVETF 971
Cdd:cd01481   160 FQVSDF 165
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 227-385 7.05e-31

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 119.32  E-value: 7.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  227 ADVVFLLDMAINGSQEDLDHLKAFLGESISALDIKENCMRVGLVTYSNETRVISSLSTGNNKTEVLQRIQDLSPQVGQA- 305
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGt 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  306 YTGAALRKTRKEIFSaqrGSRKNQGVPQIAVLVT--HRASEDNVTKAAVNLRREGVTIFTMGIEGANPDELEKIASHPAE 383
Cdd:cd01450    81 NTGKALQYALEQLFS---ESNARENVPKVIIVLTdgRSDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSE 157


                  ..
gi 156616288  384 QF 385
Cdd:cd01450   158 RH 159
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 434-595 2.16e-30

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: 118.20  E-value: 2.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  434 ADIYLLIDGSGSTQPTDFHEMKTFLSEVVGMFNIAPHKVRVGAVQYADTWDLEFEISKYSNKPDLGKAIENIRQMGGN-T 512
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSqL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  513 NTGAALNFTLKLLqrAKKERGSK----VPCHLVVLTNGMSRDSVLGPAHKLREENIRVHAIGVKEANQTQLREIAGEEKR 588
Cdd:cd01481    81 NTGSALDYVVKNL--FTKSAGSRieegVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSF 158


                  ....*..
gi 156616288  589 VYYVHEF 595
Cdd:cd01481   159 VFQVSDF 165
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 227-392 2.69e-30

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 117.77  E-value: 2.69e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  227 ADVVFLLDMAINGSQEDLDHLKAFLGESISALDIKENCMRVGLVTYSNETRVISSLSTGNNKTEVLQRIQDLSPQVGQAY 306
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  307 TGAALRKTRKEIFSAQRGSRKnqGVPQIAVLVTHRASEDNVTKAAVNLRREGVTIFTMGIEGANPDELEKIASHPAEQFT 386
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARP--GVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHV 158


                  ....*.
gi 156616288  387 SKLGNF 392
Cdd:cd01482   159 FNVADF 164
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 227-386 8.45e-30

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: 116.27  E-value: 8.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  227 ADVVFLLDMAINGSQEDLDHLKAFLGESISALDIKENCMRVGLVTYSNETRVISSLSTGNNKTEVLQRIQDLSPQVG-QA 305
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGsQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  306 YTGAALRKTRKEIFSAQRGSRKNQGVPQIAVLVTHRASEDNVTKAAVNLRREGVTIFTMGIEGANPDELEKIASHPAEQF 385
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                  .
gi 156616288  386 T 386
Cdd:cd01481   161 Q 161
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 434-613 4.81e-29

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: 116.33  E-value: 4.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  434 ADIYLLIDGSGSTQPTDFHEMKTFLSEVVGMFNIAPHKVRVGAVQYADTWDLEFEISKYSNKPDLGKAIENIRQMGGNTN 513
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  514 TGAALNFtlkLLQRAKKE------RGSKVPCHLVVLTNGMSRDSVLGPAHKLREENIRVHAIGVKEANQTQLREIAGE-- 585
Cdd:cd01475    83 TGLAIQY---AMNNAFSEaegarpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEpl 159

                         170       180
                  ....*....|....*....|....*...
gi 156616288  586 EKRVYYVHEFDALRNIRNQVVQEICAEE 613
Cdd:cd01475   160 ADHVFYVEDFSTIEELTKKFQGKICVVP 187
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 434-592 1.65e-27

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: 109.58  E-value: 1.65e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  434 ADIYLLIDGSGSTQPTDFHEMKTFLSEVVGMFNIAPHKVRVGAVQYADTWDLEFEISKYSNKPDLGKAIENIR-QMGGNT 512
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKkGLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  513 NTGAALNFTLKLLQRAKKERGSKVpchLVVLTNGMSRDSVLGP---AHKLREENIRVHAIGVK-EANQTQLREIAGEEKR 588
Cdd:cd00198    81 NIGAALRLALELLKSAKRPNARRV---IILLTDGEPNDGPELLaeaARELRKLGITVYTIGIGdDANEDELKEIADKTTG 157


                  ....
gi 156616288  589 VYYV 592
Cdd:cd00198   158 GAVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 228-397 8.56e-27

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: 108.31  E-value: 8.56e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288    228 DVVFLLDMAINGSQEDLDHLKAFLGESISALDIKENCMRVGLVTYSNETRVISSLSTGNNKTEVLQRIQDLSPQ-VGQAY 306
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288    307 TGAALRKTRKEIFSAQRGSRKnqGVPQIAVLVT---HRASEDNVTKAAVNLRREGVTIFTMGIEGA-NPDELEKIASHPA 382
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRR--GAPKVVILITdgeSNDGPKDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPG 158

                           170
                    ....*....|....*
gi 156616288    383 EQFTSKLGNFSELAT 397
Cdd:smart00327  159 GVYVFLPELLDLLID 173
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 26-192 1.46e-26

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: 107.54  E-value: 1.46e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288     26 DVVFLVDSSDHLGLKSFPLVKTFIHKMISSLPIEANKYRVALAQYSDALHNEFQLGTFKNRNPMLNHLKKNFGFIGGSLK 105
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288    106 IGNALQEAHRTYFSAPTNGRdkKQFPPILVVLASAESED---DVEEAAKALREDGVKIISVGV-QKASEENLKAMA---T 178
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLAsapG 158

                           170
                    ....*....|....
gi 156616288    179 SQFHFNLRTARDLS 192
Cdd:smart00327  159 GVYVFLPELLDLLI 172
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 435-601 1.59e-26

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: 107.44  E-value: 1.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  435 DIYLLIDGSGSTQPTDFHEMKTFLSEVVGMFNIAPHKVRVGAVQYADTWDLEFEISKYSNKPDLGKAIENIRQMGGNTNT 514
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  515 GAALNFTLKLLQRAkkERGS-----KVpchLVVLTNGMSRDSVLGPA--HKLREENIRVHAIGVKEANQT-----QLREI 582
Cdd:cd01469    82 ATAIQYVVTELFSE--SNGArkdatKV---LVVITDGESHDDPLLKDviPQAEREGIIRYAIGVGGHFQRensreELKTI 156

                         170       180
                  ....*....|....*....|.
gi 156616288  583 AGE--EKRVYYVHEFDALRNI 601
Cdd:cd01469   157 ASKppEEHFFNVTDFAALKDI 177
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 25-179 3.82e-26

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 105.84  E-value: 3.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   25 ADVVFLVDSSDHLGLKSFPLVKTFIHKMISSLPIEANKYRVALAQYSDALHNEFQLGTFKNRNPMLNHLkKNFGFIGGSL 104
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAV-KNLKYLGGGG 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156616288  105 -KIGNALQEAHRTYFSaPTNGRdkKQFPPILVVLASAESED--DVEEAAKALREDGVKIISVGVQKASEENLKAMATS 179
Cdd:cd01450    80 tNTGKALQYALEQLFS-ESNAR--ENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASC 154
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 998-1153 4.47e-26

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 105.73  E-value: 4.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  998 VDLVFLMDGSNSIHPDDFQKMKGFLVSVVQDFDVSLNRVRIGVAQFSDSYRSEFLLGTFTGEREISTQIEGIQ-QIFGYT 1076
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKkGLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288 1077 HIGDALRKVKYYFQpdmgSRINAGTPQVLLVLTDGRSQD---EVAQAAEELRHKGVDIYSVGIGD-VDDQELVQITGTAE 1152
Cdd:cd00198    81 NIGAALRLALELLK----SAKRPNARRVIILLTDGEPNDgpeLLAEAARELRKLGITVYTIGIGDdANEDELKEIADKTT 156


                  .
gi 156616288 1153 K 1153
Cdd:cd00198   157 G 157
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 807-986 1.46e-25

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: 106.32  E-value: 1.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  807 LDVVFVIDSSGSIDYQEYNIMKDFMIGLVKKADVGKNQVRFGALKYADDPEVLFYLDELGTKLEVVSVLQNDHPMGGNTY 886
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  887 TAEALAFS-DHMFTEARGSR-LHKGVPQVLIVITDGESHDaeKLNTTAKALRDKGILVLAVGIAGANSWELLAMAG--SS 962
Cdd:cd01475    83 TGLAIQYAmNNAFSEAEGARpGSERVPRVGIVVTDGRPQD--DVSEVAAKARALGIEMFAVGVGRADEEELREIASepLA 160

                         170       180
                  ....*....|....*....|....
gi 156616288  963 DKYYFVETFGGLKGIFSDVSASVC 986
Cdd:cd01475   161 DHVFYVEDFSTIEELTKKFQGKIC 184
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 807-968 6.70e-25

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: 102.26  E-value: 6.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  807 LDVVFVIDSSGSIDYQEYNIMKDFMIGLVKKADVGKNQVRFGALKYADDPEVLFYLDELGTKLEVVSVLQN-DHPMGGNT 885
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDAlKKGLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  886 YTAEALAFSDHMFTEARgsrlHKGVPQVLIVITDGESHDA-EKLNTTAKALRDKGILVLAVGI-AGANSWELLAMAGSSD 963
Cdd:cd00198    81 NIGAALRLALELLKSAK----RPNARRVIILLTDGEPNDGpELLAEAARELRKLGITVYTIGIgDDANEDELKEIADKTT 156


                  ....*
gi 156616288  964 KYYFV 968
Cdd:cd00198   157 GGAVF 161
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 25-178 8.38e-25

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: 104.00  E-value: 8.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   25 ADVVFLVDSSDHLGLKSFPLVKTFIHKMISSLPIEANKYRVALAQYSDALHNEFQLGTFKNRNPMLNHLKKNFGFIGGSL 104
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156616288  105 KiGNALQEAHRTYFSAPTNGRDKKQFPP-ILVVLASAESEDDVEEAAKALREDGVKIISVGVQKASEENLKAMAT 178
Cdd:cd01475    83 T-GLAIQYAMNNAFSEAEGARPGSERVPrVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIAS 156
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 620-775 2.96e-24

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 100.55  E-value: 2.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  620 ADIMFLVDSSGSIGPEnFSKMKMFMKNLVSKSQIGADRVQIGVVQFSHENKE--EFQLNTFMSQSDIANAIDRMTHIGET 697
Cdd:cd01476     1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  698 TLTGSALTFVSQYFSPDKGARPNVRKFLILITDGEAQDIVRDPAIALRKE-GVIIYSVGV---FGSNVTQLEEISGKPEM 773
Cdd:cd01476    80 TATGAAIEVALQQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTgdpGTVDTEELHSITGNEDH 159


                  ..
gi 156616288  774 VF 775
Cdd:cd01476   160 IF 161
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 998-1138 5.24e-24

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 100.12  E-value: 5.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  998 VDLVFLMDGSNSIHPDDFQKMKGFLVSVVQDFDVSLNRVRIGVAQFSDSYRSEFLLGTFTGEREISTQIEGIQQIFGYTH 1077
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156616288 1078 IGDALRKV-KYYFQPDMGSRINAgtPQVLLVLTDGRSQD-----EVAQAAEelrHKGVDIYSVGIGD 1138
Cdd:cd01469    81 TATAIQYVvTELFSESNGARKDA--TKVLVVITDGESHDdpllkDVIPQAE---REGIIRYAIGVGG 142
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 227-431 7.81e-24

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: 101.31  E-value: 7.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  227 ADVVFLLDMAINGSQEDLDHLKAFLGESISALDIKENCMRVGLVTYSNETRVISSLSTGNNKTEVLQRIQDLSPQVGQAY 306
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  307 TGAALRKTRKEIFSAQRGSRK-NQGVPQIAVLVTHRASEDNVTKAAVNLRREGVTIFTMGIEGANPDELEKIASHPAEQF 385
Cdd:cd01475    83 TGLAIQYAMNNAFSEAEGARPgSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLADH 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 156616288  386 TSKLGNFSELathnQTFLKKLRNQITHTVSVFSERTETLKSACVDT 431
Cdd:cd01475   163 VFYVEDFSTI----EELTKKFQGKICVVPDLCATLSHVCQQVCIST 204
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 434-590 2.32e-23

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 97.85  E-value: 2.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  434 ADIYLLIDGSGSTQPTdFHEMKTFLSEVVGMFNIAPHKVRVGAVQYA--DTWDLEFEISKYSNKPDLGKAIENIRQMGGN 511
Cdd:cd01476     1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  512 TNTGAALNFTLKLLQRAKKERgSKVPCHLVVLTNGMSRDSVLGPAHKLREE-NIRVHAIGVKE---ANQTQLREIAGEEK 587
Cdd:cd01476    80 TATGAAIEVALQQLDPSEGRR-EGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGDpgtVDTEELHSITGNED 158


                  ...
gi 156616288  588 RVY 590
Cdd:cd01476   159 HIF 161
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 620-783 1.93e-21

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: 93.22  E-value: 1.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  620 ADIMFLVDSSGSIGPENFSKMKMFMKNLVS------KSQIGADRVQIGVVQFSHENKEEFQLNTFM-SQSDIANAIDRMT 692
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAErflkdyYRKDPAGSWRVGVVQYSDQQEVEAGFLRDIrNYTSLKEAVDNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  693 HIGETTLTGSALTFVSQYFSpdKGARPNVRKFLILITDGEAqDIVRDPAI--AL---RKEGVIIYSVGVFGSNVTQLEEI 767
Cdd:cd01480    83 YIGGGTFTDCALKYATEQLL--EGSHQKENKFLLVITDGHS-DGSPDGGIekAVneaDHLGIKIFFVAVGSQNEEPLSRI 159

                         170
                  ....*....|....*.
gi 156616288  768 SGKPEMVFYVENFDIL 783
Cdd:cd01480   160 ACDGKSALYRENFAEL 175
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 999-1156 4.01e-20

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 88.61  E-value: 4.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  999 DLVFLMDGSNSIHpDDFQKMKGFLVSVVQDFDVSLNRVRIGVAQFSDSYRS--EFLLGTFTGEREISTQIEGIQQIFGYT 1076
Cdd:cd01476     2 DLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288 1077 HIGDALRKVKYYFQPDMGSRinAGTPQVLLVLTDGRSQDEVAQAAEELR-HKGVDIYSVGIGD---VDDQELVQITGTAE 1152
Cdd:cd01476    81 ATGAAIEVALQQLDPSEGRR--EGIPKVVVVLTDGRSHDDPEKQARILRaVPNIETFAVGTGDpgtVDTEELHSITGNED 158


                  ....
gi 156616288 1153 KKLT 1156
Cdd:cd01476   159 HIFT 162
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 807-965 6.17e-20

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: 88.60  E-value: 6.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  807 LDVVFVIDSSGSIDYQ-EYNIMKDFMIGLVKKADVGKNQVRFGALKYADDPEVLFYLDELGTK-----LEVVSVLQNDHP 880
Cdd:cd01471     1 LDLYLLVDGSGSIGYSnWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTnkdlaLNAIRALLSLYY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  881 MGGNTYTAEALAFSDHMFTEARGSRLHkgVPQVLIVITDGESHDAEKLNTTAKALRDKG--ILVLAVGiAGANSWELLAM 958
Cdd:cd01471    81 PNGSTNTTSALLVVEKHLFDTRGNREN--APQLVIIMTDGIPDSKFRTLKEARKLRERGviIAVLGVG-QGVNHEENRSL 157


                  ....*..
gi 156616288  959 AGSSDKY 965
Cdd:cd01471   158 VGCDPDD 164
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 227-379 8.01e-20

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 87.62  E-value: 8.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  227 ADVVFLLDMAINGSQEDLDHLKAFLGESISALDIKENCMRVGLVTYSNETRVISSLSTGNNKTEVLQRIQDLSPQV-GQA 305
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLgGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156616288  306 YTGAALRKTRKEIFSAQRGSRKnqgvpQIAVLVT---HRASEDNVTKAAVNLRREGVTIFTMGI-EGANPDELEKIAS 379
Cdd:cd00198    81 NIGAALRLALELLKSAKRPNAR-----RVIILLTdgePNDGPELLAEAARELRKLGITVYTIGIgDDANEDELKEIAD 153
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 621-756 2.17e-19

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 87.06  E-value: 2.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  621 DIMFLVDSSGSIGPEN-FSKMKMFMKNLVSKSQIGADRVQIGVVQFSHENKEEFQLNTFMSQS-----DIANAIDRMTHI 694
Cdd:cd01471     2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNkdlalNAIRALLSLYYP 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156616288  695 GETTLTGSALTFVSQYFSPDKGARPNVRKFLILITDGEAQDIVR--DPAIALRKEGVIIYSVGV 756
Cdd:cd01471    82 NGSTNTTSALLVVEKHLFDTRGNRENAPQLVIIMTDGIPDSKFRtlKEARKLRERGVIIAVLGV 145
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 228-397 1.70e-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: 84.33  E-value: 1.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  228 DVVFLLDMAINGSQEDLDHLKAFLGESISALDIKENCMRVGLVTYSNETRVISSLSTGNNKTEVLQRIQDLSPQVGQAYT 307
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  308 GAALRKTRKEIFSAQRGSRKnqGVPQIAVLVTHRASEDN-----VTKAAvnlRREGVTIFTMGIEGA--NPD---ELEKI 377
Cdd:cd01469    82 ATAIQYVVTELFSESNGARK--DATKVLVVITDGESHDDpllkdVIPQA---EREGIIRYAIGVGGHfqRENsreELKTI 156

                         170       180
                  ....*....|....*....|
gi 156616288  378 ASHPAEQFTSKLGNFSELAT 397
Cdd:cd01469   157 ASKPPEEHFFNVTDFAALKD 176
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 25-178 5.95e-17

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: 5.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   25 ADVVFLVDSSDHLGLKSFPLVKTFIHKMISSLPIEANKYRVALAQYSDALHNEFQLGTFKNRNPMLNHLKKNFGFIGGSL 104
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156616288  105 KIGNALQEAHRTYFSAPTNGRdkkqfPPILVVLASAESEDD---VEEAAKALREDGVKIISVGV-QKASEENLKAMAT 178
Cdd:cd00198    81 NIGAALRLALELLKSAKRPNA-----RRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIgDDANEDELKEIAD 153
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 998-1163 1.70e-16

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: 78.97  E-value: 1.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  998 VDLVFLMDGSNSIHPDDFQKMKGFLVSVVQDF-------DVSLnRVRIGVAQFSDSYRSEFLLGTFTGERE-ISTQIEGI 1069
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrkDPAG-SWRVGVVQYSDQQEVEAGFLRDIRNYTsLKEAVDNL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288 1070 QQIFGYTHIGDALRKVKYYFQPDMGSrinaGTPQVLLVLTDGRSQDEVA----QAAEELRHKGVDIYSVGIGDVDDQELV 1145
Cdd:cd01480    82 EYIGGGTFTDCALKYATEQLLEGSHQ----KENKFLLVITDGHSDGSPDggieKAVNEADHLGIKIFFVAVGSQNEEPLS 157

                         170
                  ....*....|....*...
gi 156616288 1146 QITGTAEKKLTVHNFDEL 1163
Cdd:cd01480   158 RIACDGKSALYRENFAEL 175
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 807-967 3.61e-16

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 77.05  E-value: 3.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  807 LDVVFVIDSSGSIDyQEYNIMKDFMIGLVKKADVGKNQVRFGALKYADDPE--VLFYLDELGTKLEVVSVLQNDHPMGGN 884
Cdd:cd01476     1 LDLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  885 TYTAEALAFSDHMFTEARGSRlhKGVPQVLIVITDGESHDAEKlnTTAKALR-DKGILVLAVGI---AGANSWELLAMAG 960
Cdd:cd01476    80 TATGAAIEVALQQLDPSEGRR--EGIPKVVVVLTDGRSHDDPE--KQARILRaVPNIETFAVGTgdpGTVDTEELHSITG 155


                  ....*..
gi 156616288  961 SSDKYYF 967
Cdd:cd01476   156 NEDHIFT 162
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 620-791 5.94e-15

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 74.47  E-value: 5.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  620 ADIMFLVDSSGSIG---PENFSkmkmFMKNLVSKsqIGADRVQIGVVQFSHENKEEFQLNTFMSQ-SDIANAIDRMTHIG 695
Cdd:cd01474     5 FDLYFVLDKSGSVAanwIEIYD----FVEQLVDR--FNSPGLRFSFITFSTRATKILPLTDDSSAiIKGLEVLKKVTPSG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  696 ETTLtGSALTFVSQYFSPDKGARPNVRKFLILITDGE-AQDIVRDP---AIALRKEGVIIYSVGVFGSNVTQLEEISGKP 771
Cdd:cd01474    79 QTYI-HEGLENANEQIFNRNGGGRETVSVIIALTDGQlLLNGHKYPeheAKLSRKLGAIVYCVGVTDFLKSQLINIADSK 157

                         170       180
                  ....*....|....*....|.
gi 156616288  772 EMVFYV-ENFDILQHIEDDLV 791
Cdd:cd01474   158 EYVFPVtSGFQALSGIIESVV 178
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 432-601 7.20e-15

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 76.13  E-value: 7.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  432 EEADIYLLIDGSGSTQPTD-FHEMKTFLSEVVGMFniaPHKVRVGAVQYADTWDLEFEISkySNKPDLGKAIENIrQMGG 510
Cdd:COG1240    91 RGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLT--RDREALKRALDEL-PPGG 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  511 NTNTGAALNFTLKLLQRAKKERgskvPCHLVVLTNGMSRDSVLGP---AHKLREENIRVHAIGV--KEANQTQLREIAGE 585
Cdd:COG1240   165 GTPLGDALALALELLKRADPAR----RKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVgtEAVDEGLLREIAEA 240

                         170
                  ....*....|....*..
gi 156616288  586 EK-RVYYVHEFDALRNI 601
Cdd:COG1240   241 TGgRYFRADDLSELAAI 257
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 620-786 1.16e-14

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 75.36  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  620 ADIMFLVDSSGSIGPEN-FSKMKMFMKNLVSKSQigaDRVQIGVVQFSHENKEEFQLNTfmSQSDIANAIDRMThIGETT 698
Cdd:COG1240    93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEVLLPLTR--DREALKRALDELP-PGGGT 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  699 LTGSALTFVSQYFspdKGARPNVRKFLILITDGEAQDIVRDP---AIALRKEGVIIYSVGVFGSNV--TQLEEIS----G 769
Cdd:COG1240   167 PLGDALALALELL---KRADPARRKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVGTEAVdeGLLREIAeatgG 243

                         170
                  ....*....|....*..
gi 156616288  770 KpemVFYVENFDILQHI 786
Cdd:COG1240   244 R---YFRADDLSELAAI 257
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 807-959 3.68e-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: 72.03  E-value: 3.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  807 LDVVFVIDSSGSIDYQEYNIMKDFMIGLVK--KADVGKN----QVRFGALKYADDPEVLFYLDELGTKLEVV-SVLQNDH 879
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAErfLKDYYRKdpagSWRVGVVQYSDQQEVEAGFLRDIRNYTSLkEAVDNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  880 PMGGNTYTAEALAFSDHMFTEARgsrlHKGVPQVLIVITDGEShDAEKLNTTAKALRDK---GILVLAVGIAGANSWELL 956
Cdd:cd01480    83 YIGGGTFTDCALKYATEQLLEGS----HQKENKFLLVITDGHS-DGSPDGGIEKAVNEAdhlGIKIFFVAVGSQNEEPLS 157


                  ...
gi 156616288  957 AMA 959
Cdd:cd01480   158 RIA 160
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 25-165 4.68e-14

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: 71.28  E-value: 4.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   25 ADVVFLVDSSDHLGLKsFPLVKTFIHKMISSLPIEANKYRVALAQYSDAL--HNEFQLGTFKNRNPMLNHLkKNFGFIGG 102
Cdd:cd01476     1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGrqRVRFNLPKHNDGEELLEKV-DNLRFIGG 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156616288  103 SLKIGNALQEAhrTYFSAPTNGRdKKQFPPILVVLASAESEDDVEEAAKALRED-GVKIISVGV 165
Cdd:cd01476    79 TTATGAAIEVA--LQQLDPSEGR-REGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGT 139
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 998-1147 5.64e-14

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 73.43  E-value: 5.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  998 VDLVFLMDGSNSIH-PDDFQKMKGFLVSVVQDFdvsLNRVRIGVAQFSDsyRSEFLLGtFTGERE-ISTQIEGIQqIFGY 1075
Cdd:COG1240    93 RDVVLVVDASGSMAaENRLEAAKGALLDFLDDY---RPRDRVGLVAFGG--EAEVLLP-LTRDREaLKRALDELP-PGGG 165

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156616288 1076 THIGDALRKVKyyfqpDMGSRINAGTPQVLLVLTDGR---SQDEVAQAAEELRHKGVDIYSVGIGD--VDDQELVQI 1147
Cdd:COG1240   166 TPLGDALALAL-----ELLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTeaVDEGLLREI 237
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 801-986 7.44e-14

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 71.00  E-value: 7.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  801 CKRIevLDVVFVIDSSGSIDYQEYNIMkDFMIGLVKKadVGKNQVRFGALKYADDPEVLFYL-DELGTKLEVVSVLQNDH 879
Cdd:cd01474     1 CAGH--FDLYFVLDKSGSVAANWIEIY-DFVEQLVDR--FNSPGLRFSFITFSTRATKILPLtDDSSAIIKGLEVLKKVT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  880 PmGGNTYTAEALAF-SDHMFTEARGSRLhkgVPQVLIVITDGESH-----DAEKlntTAKALRDKGILVLAVGIAGANSW 953
Cdd:cd01474    76 P-SGQTYIHEGLENaNEQIFNRNGGGRE---TVSVIIALTDGQLLlnghkYPEH---EAKLSRKLGAIVYCVGVTDFLKS 148

                         170       180       190
                  ....*....|....*....|....*....|....
gi 156616288  954 ELLAMAGSSDKYYFV-ETFGGLKGIFSDVSASVC 986
Cdd:cd01474   149 QLINIADSKEYVFPVtSGFQALSGIIESVVKKAC 182
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 435-584 1.22e-13

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 70.49  E-value: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  435 DIYLLIDGSGSTQPTD-FHEMKTFLSEVVGMFNIAPHKVRVGAVQYADT----WDLefEISKYSNKPDLGKAIENIRQM- 508
Cdd:cd01471     2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNakelIRL--SSPNSTNKDLALNAIRALLSLy 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  509 --GGNTNTGAALNFTLKLLQRAKKERgSKVPCHLVVLTNGMSRD--SVLGPAHKLREENIRVHAIGVKEA-NQTQLREIA 583
Cdd:cd01471    80 ypNGSTNTTSALLVVEKHLFDTRGNR-ENAPQLVIIMTDGIPDSkfRTLKEARKLRERGVIIAVLGVGQGvNHEENRSLV 158


                  .
gi 156616288  584 G 584
Cdd:cd01471   159 G 159
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 434-599 2.56e-13

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 69.72  E-value: 2.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  434 ADIYLLIDGSGSTQPTDFHEMKTFLSEVVGMF------NIAPHKVRVGAVQYADTWDLEF-EISKYSNKPDLGKAIENIR 506
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  507 QMGGNTNTGAALNFTLKLLQRAkkeRGSKVPCHLVVLTNGMSR----DSVLGPAHKLREENIRVHAIGVKEANQTQLREI 582
Cdd:cd01480    83 YIGGGTFTDCALKYATEQLLEG---SHQKENKFLLVITDGHSDgspdGGIEKAVNEADHLGIKIFFVAVGSQNEEPLSRI 159

                         170
                  ....*....|....*..
gi 156616288  583 AGEEKRVYYVHEFDALR 599
Cdd:cd01480   160 ACDGKSALYRENFAELL 176
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 26-185 9.57e-13

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 67.77  E-value: 9.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   26 DVVFLVDSSDHLGLKSFPLVKTFIHKMISSLPIEANKYRVALAQYSDALHNEFQLGTFKNRNPMLNhLKKNFGFIGGSLK 105
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLS-LVKHISQLLGLTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  106 IGNALQEAHRTYFSAPTNGRdkKQFPPILVVLASAESEDDVEEAA--KALREDGVKIISVGVQKA-----SEENLKAMA- 177
Cdd:cd01469    81 TATAIQYVVTELFSESNGAR--KDATKVLVVITDGESHDDPLLKDviPQAEREGIIRYAIGVGGHfqrenSREELKTIAs 158

                         170
                  ....*....|
gi 156616288  178 --TSQFHFNL 185
Cdd:cd01469   159 kpPEEHFFNV 168
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 807-981 6.17e-12

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 67.27  E-value: 6.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  807 LDVVFVIDSSGSIDYQE-YNIMKDFMIGLVKKADVGknqVRFGALKYADDPEVLFyldELGTKLEVVSVLQNDHPMGGNT 885
Cdd:COG1240    93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPR---DRVGLVAFGGEAEVLL---PLTRDREALKRALDELPPGGGT 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  886 YTAEALAFSDHMFteargSRLHKGVPQVLIVITDGESHD-AEKLNTTAKALRDKGI--LVLAVGIAGANSWELLAMAGSS 962
Cdd:COG1240   167 PLGDALALALELL-----KRADPARRKVIVLLTDGRDNAgRIDPLEAAELAAAAGIriYTIGVGTEAVDEGLLREIAEAT 241

                         170       180
                  ....*....|....*....|
gi 156616288  963 D-KYYFVETFGGLKGIFSDV 981
Cdd:COG1240   242 GgRYFRADDLSELAAIYREI 261
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 213-378 9.91e-12

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 66.89  E-value: 9.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  213 ADDIIVEACQGPSVADVVFLLD----MAingSQEDLDHLKAFLGESISALDIKEncmRVGLVTYSNETRVISSLSTgnNK 288
Cdd:COG1240    79 LALAPLALARPQRGRDVVLVVDasgsMA---AENRLEAAKGALLDFLDDYRPRD---RVGLVAFGGEAEVLLPLTR--DR 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  289 TEVLQRIQDLSPQvGQAYTGAALRKtrkeifSAQRGSRKNQGVPQIAVLVT---HRASEDNVTKAAVNLRREGVTIFT-- 363
Cdd:COG1240   151 EALKRALDELPPG-GGTPLGDALAL------ALELLKRADPARRKVIVLLTdgrDNAGRIDPLEAAELAAAAGIRIYTig 223

                         170
                  ....*....|....*
gi 156616288  364 MGIEGANPDELEKIA 378
Cdd:COG1240   224 VGTEAVDEGLLREIA 238
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 25-199 1.63e-11

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: 64.33  E-value: 1.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   25 ADVVFLVDSSDHLGLKSFPLVKTFIHKMISSL------PIEANKYRVALAQYSDALHNEFQLGTFKNRNPMLNHLKKNFG 98
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTSLKEAVDNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   99 FIGGSLKIGNALQEAHRTYFSAPTNGRDKkqfppILVVLASAES--EDD--VEEAAKALREDGVKIISVGVQKASEENLK 174
Cdd:cd01480    83 YIGGGTFTDCALKYATEQLLEGSHQKENK-----FLLVITDGHSdgSPDggIEKAVNEADHLGIKIFFVAVGSQNEEPLS 157

                         170       180
                  ....*....|....*....|....*...
gi 156616288  175 AMAT---SQFHFNLRTARDLSVFAPNMT 199
Cdd:cd01480   158 RIACdgkSALYRENFAELLWSFFIDDET 185
VWA_2 pfam13519
von Willebrand factor type A domain;
436-536 5.57e-11

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 60.38  E-value: 5.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   436 IYLLIDGSGS-----TQPTDFHEMKTFLSEVVGMFNIaphkVRVGAVQYADTWDLEFEISKysNKPDLGKAIENIRQMGG 510
Cdd:pfam13519    1 LVFVLDTSGSmrngdYGPTRLEAAKDAVLALLKSLPG----DRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                           90       100
                   ....*....|....*....|....*.
gi 156616288   511 NTNTGAALNFTLKLLQRAKKERGSKV 536
Cdd:pfam13519   75 GTNLAAALQLARAALKHRRKNQPRRI 100
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 228-366 1.23e-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: 62.02  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  228 DVVFLLDMA--InGSQEDLDHLKAFLGESISALDIKENCMRVGLVTYSNETRVISSLSTGN--NKTEVLQRIQDL---SP 300
Cdd:cd01471     2 DLYLLVDGSgsI-GYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNstNKDLALNAIRALlslYY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156616288  301 QVGQAYTGAALRKTRKEIFSAqRGSRKNqgVPQIAVLVTHRASED--NVTKAAVNLRREGVTIFTMGI 366
Cdd:cd01471    81 PNGSTNTTSALLVVEKHLFDT-RGNREN--APQLVIIMTDGIPDSkfRTLKEARKLRERGVIIAVLGV 145
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 999-1177 1.62e-10

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 61.37  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  999 DLVFLMDGSNSIHpDDFQKMKGFLVSVVQDFdVSLNrVRIGVAQFSDsyRSEFLLGTFTGEREISTQIEGIQQIF--GYT 1076
Cdd:cd01474     6 DLYFVLDKSGSVA-ANWIEIYDFVEQLVDRF-NSPG-LRFSFITFST--RATKILPLTDDSSAIIKGLEVLKKVTpsGQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288 1077 HIGDALRKVK-YYFQPDMGSRInagTPQVLLVLTDGRSQDEVAQAAEE----LRHKGVDIYSVGIGDVDDQELVQITGTA 1151
Cdd:cd01474    81 YIHEGLENANeQIFNRNGGGRE---TVSVIIALTDGQLLLNGHKYPEHeaklSRKLGAIVYCVGVTDFLKSQLINIADSK 157

                         170       180
                  ....*....|....*....|....*..
gi 156616288 1152 EKKLTVHN-FDELKKVKKRIVRNICTS 1177
Cdd:cd01474   158 EYVFPVTSgFQALSGIIESVVKKACIE 184
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 808-960 2.05e-10

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: 61.18  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  808 DVVFVIDSSGSIDYqeYNIMKDFM---IGLVKKADVGKNQVRFGALKYADDPEVL--FYLDELGTK---LEVVSVLQNDH 879
Cdd:cd01473     2 DLTLILDESASIGY--SNWRKDVIpftEKIINNLNISKDKVHVGILLFAEKNRDVvpFSDEERYDKnelLKKINDLKNSY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  880 PMGGNTYTAEALAFSDHMFTEARGSRlhKGVPQVLIVITDGESHDAEK--LNTTAKALRDKGILVLAVGIAGANSWELLA 957
Cdd:cd01473    80 RSGGETYIVEALKYGLKNYTKHGNRR--KDAPKVTMLFTDGNDTSASKkeLQDISLLYKEENVKLLVVGVGAASENKLKL 157


                  ...
gi 156616288  958 MAG 960
Cdd:cd01473   158 LAG 160
VWA_2 pfam13519
von Willebrand factor type A domain;
622-728 2.31e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 58.84  E-value: 2.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   622 IMFLVDSSGSI-----GPENFSKMKMFMKNLVSKsqigADRVQIGVVQFSHENKEEFQLNTfmSQSDIANAIDRMTHIGE 696
Cdd:pfam13519    1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKS----LPGDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|..
gi 156616288   697 TTLTGSALTFVSQYFspdKGARPNVRKFLILI 728
Cdd:pfam13519   75 GTNLAAALQLARAAL---KHRRKNQPRRIVLI 103
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 26-177 6.01e-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: 59.71  E-value: 6.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   26 DVVFLVDSSDHLGLKS-FPLVKTFIHKMISSLPIEANKYRVALAQYSDALHNEFQLGTFKNRNP-----MLNHLKKNFgF 99
Cdd:cd01471     2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKdlalnAIRALLSLY-Y 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  100 IGGSLKIGNALQEAHRTYFSaptnGRDKKQFPPILVVLASAESEDDVE---EAAKALREDGVKI--ISVGVQKASEENlK 174
Cdd:cd01471    81 PNGSTNTTSALLVVEKHLFD----TRGNRENAPQLVIIMTDGIPDSKFrtlKEARKLRERGVIIavLGVGQGVNHEEN-R 155


                  ...
gi 156616288  175 AMA 177
Cdd:cd01471   156 SLV 158
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 790-980 1.17e-09

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 60.89  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  790 LVLGICSPREECKRIEVLDVVFVIDSSGSidyqeyniMKDFMIGLVKKA-----DVGKNQVRFGALKYADDPEVLFYLDE 864
Cdd:COG2304    75 LLVGLQPPKAAAEERPPLNLVFVIDVSGS--------MSGDKLELAKEAakllvDQLRPGDRVSIVTFAGDARVLLPPTP 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  865 LGTKLEVVSVLQNDHPmGGNTYTAEALAFSdhmFTEARGSRLHKGVPQVlIVITDGE----SHDAEKLNTTAKALRDKGI 940
Cdd:COG2304   147 ATDRAKILAAIDRLQA-GGGTALGAGLELA---YELARKHFIPGRVNRV-ILLTDGDanvgITDPEELLKLAEEAREEGI 221

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 156616288  941 LVLAVGI-AGANSWELLAMAGSSD-KYYFVETFGGLKGIFSD 980
Cdd:COG2304   222 TLTTLGVgSDYNEDLLERLADAGGgNYYYIDDPEEAEKVFVR 263
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 998-1137 1.50e-09

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: 58.55  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  998 VDLVFLMDGSNSI-HPDDFQKMKGFLVSVVQDFDVSLNRVRIGVAQFS---------DSYRS---EFLLGTFTGEREIST 1064
Cdd:cd01471     1 LDLYLLVDGSGSIgYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFStnakelirlSSPNStnkDLALNAIRALLSLYY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156616288 1065 QiegiqqiFGYTHIGDALRKVKYYFQPDMGSRINAgtPQVLLVLTDGRSQD--EVAQAAEELRHKGVDIYSVGIG 1137
Cdd:cd01471    81 P-------NGSTNTTSALLVVEKHLFDTRGNRENA--PQLVIIMTDGIPDSkfRTLKEARKLRERGVIIAVLGVG 146
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 227-387 2.60e-09

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: 57.41  E-value: 2.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  227 ADVVFLLDmaingSQEDLDHL----KAFLGESISALDIKENCMRVGLVTYSNETR--VISSLSTGNNKTEVLQRIQDLSP 300
Cdd:cd01476     1 LDLLFVLD-----SSGSVRGKfekyKKYIERIVEGLEIGPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  301 QVGQAYTGAALRKTrKEIFSAQRGSRKnqGVPQIAVLVTHRASEDNVTKAAVNLRRE-GVTIFTMGI---EGANPDELEK 376
Cdd:cd01476    76 IGGTTATGAAIEVA-LQQLDPSEGRRE--GIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTgdpGTVDTEELHS 152

                         170
                  ....*....|.
gi 156616288  377 IASHPAEQFTS 387
Cdd:cd01476   153 ITGNEDHIFTD 163
VWA_2 pfam13519
von Willebrand factor type A domain;
1000-1108 7.59e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 54.22  E-value: 7.59e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  1000 LVFLMDGSNSIHPDD-----FQKMKGFLVSVVQdfdvSLNRVRIGVAQFSDSYRsefLLGTFTGERE-ISTQIEGIQQIF 1073
Cdd:pfam13519    1 LVFVLDTSGSMRNGDygptrLEAAKDAVLALLK----SLPGDRVGLVTFGDGPE---VLIPLTKDRAkILRALRRLEPKG 73

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 156616288  1074 GYTHIGDALRKVKYYFQpdmgsRINAGTPQVLLVL 1108
Cdd:pfam13519   74 GGTNLAAALQLARAALK-----HRRKNQPRRIVLI 103
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 265-395 1.35e-08

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 55.98  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  265 MRVGLVTYSNETRVISSLsTGNNKTEV--LQRIQDLSPQvGQAYTGAALRKTRKEIFSAQRGSRKnqgVPQIAVLVTHRA 342
Cdd:cd01474    40 LRFSFITFSTRATKILPL-TDDSSAIIkgLEVLKKVTPS-GQTYIHEGLENANEQIFNRNGGGRE---TVSVIIALTDGQ 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 156616288  343 SEDNV----TKAAVNLRREGVTIFTMGIEGANPDELEKIASHPAEQFTSKlGNFSEL 395
Cdd:cd01474   115 LLLNGhkypEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYVFPVT-SGFQAL 170
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 434-583 2.39e-08

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 57.03  E-value: 2.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  434 ADIYLLIDGSGSTQPTDFHEMKTFLSEVVGMFNiapHKVRVGAVQYADTWDLEFEISKYSNKPDLGKAIENIrQMGGNTN 513
Cdd:COG2304    92 LNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLR---PGDRVSIVTFAGDARVLLPPTPATDRAKILAAIDRL-QAGGGTA 167

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156616288  514 TGAALNFTLKLLQRAKKERGSKvpcHLVVLTNGM------SRDSVLGPAHKLREENIRVHAIGV-KEANQTQLREIA 583
Cdd:COG2304   168 LGAGLELAYELARKHFIPGRVN---RVILLTDGDanvgitDPEELLKLAEEAREEGITLTTLGVgSDYNEDLLERLA 241
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 434-612 4.17e-08

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 54.44  E-value: 4.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  434 ADIYLLIDGSGSTQpTDFHEMKTFLSEVVGMFNiAPhKVRVGAVQYADTWDLEFEISKYSNKpdLGKAIENIRQM--GGN 511
Cdd:cd01474     5 FDLYFVLDKSGSVA-ANWIEIYDFVEQLVDRFN-SP-GLRFSFITFSTRATKILPLTDDSSA--IIKGLEVLKKVtpSGQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  512 TNTGAALNFTlKLLQRAKKERGSKVPCHLVVLTNG-MSRDSVLGPAH---KLREENIRVHAIGVKEANQTQLREIAGEEK 587
Cdd:cd01474    80 TYIHEGLENA-NEQIFNRNGGGRETVSVIIALTDGqLLLNGHKYPEHeakLSRKLGAIVYCVGVTDFLKSQLINIADSKE 158

                         170       180
                  ....*....|....*....|....*.
gi 156616288  588 RVYYVHE-FDALRNIRNQVVQEICAE 612
Cdd:cd01474   159 YVFPVTSgFQALSGIIESVVKKACIE 184
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 621-795 6.36e-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: 53.86  E-value: 6.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  621 DIMFLVDSSGSIGPENFSKMKM-FMKNLVSKSQIGADRVQIGVVQFSHEN--------KEEFQLNTFMSQsdiANAIDRM 691
Cdd:cd01473     2 DLTLILDESASIGYSNWRKDVIpFTEKIINNLNISKDKVHVGILLFAEKNrdvvpfsdEERYDKNELLKK---INDLKNS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  692 THIGETTLTGSALTFVSQYFSPDKGARPNVRKFLILITDG----EAQDIVRDPAIALRKEGVIIYSVGVFGSNVTQLEEI 767
Cdd:cd01473    79 YRSGGETYIVEALKYGLKNYTKHGNRRKDAPKVTMLFTDGndtsASKKELQDISLLYKEENVKLLVVGVGAASENKLKLL 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 156616288  768 SG-------KPEMVFYveNFDILQHIEDDLVLGIC 795
Cdd:cd01473   159 AGcdinndnCPNVIKT--EWNNLNGISKFLTDKIC 191
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 808-959 6.96e-08

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 55.07  E-value: 6.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  808 DVVFVIDSSGSIDYQEYNIMKDFMIGLVKKAdvgKNQVRFGALKYADDPEVLFYLDELGTKLEVVSVLQNDHPMGGnTYT 887
Cdd:COG2425   120 PVVLCVDTSGSMAGSKEAAAKAAALALLRAL---RPNRRFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLFAGGG-TDI 195

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156616288  888 AEALAFSDHMFTEARGSRlhkgvpQVLIVITDGESH-DAEKLNTTAKAlRDKGILVLAVGIAGANSWELLAMA 959
Cdd:COG2425   196 APALRAALELLEEPDYRN------ADIVLITDGEAGvSPEELLREVRA-KESGVRLFTVAIGDAGNPGLLEAL 261
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 620-770 7.34e-08

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 55.49  E-value: 7.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  620 ADIMFLVDSSGSIGPENFSKMKMFMKNLVskSQIGA-DRVqiGVVQFSHENKEEFQLNTFMSQSDIANAIDRMTHIGETT 698
Cdd:COG2304    92 LNLVFVIDVSGSMSGDKLELAKEAAKLLV--DQLRPgDRV--SIVTFAGDARVLLPPTPATDRAKILAAIDRLQAGGGTA 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  699 LTGS---ALTFVSQYFSPDkgaRPNVrkfLILITDGEAQDIVRDPAI------ALRKEGVIIYSVGvFGSNVTQ--LEEI 767
Cdd:COG2304   168 LGAGlelAYELARKHFIPG---RVNR---VILLTDGDANVGITDPEEllklaeEAREEGITLTTLG-VGSDYNEdlLERL 240


                  ...
gi 156616288  768 SGK 770
Cdd:COG2304   241 ADA 243
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 227-405 8.24e-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: 53.54  E-value: 8.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  227 ADVVFLLD----MAINGSQEDLDHLKAFLGE--SISALDIKENCMRVGLVTYSNETRVIS-SLSTGNNKTEVLQRIQDLS 299
Cdd:cd01480     3 VDITFVLDssesVGLQNFDITKNFVKRVAERflKDYYRKDPAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  300 PQVGQAYTGAALRKTRKEIfsaQRGSRknQGVPQIAVLVT---HRASEDNVTKAAVNL-RREGVTIFTMGIEGANPDELE 375
Cdd:cd01480    83 YIGGGTFTDCALKYATEQL---LEGSH--QKENKFLLVITdghSDGSPDGGIEKAVNEaDHLGIKIFFVAVGSQNEEPLS 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 156616288  376 KIAS--HPAEQFTsklgNFSELatHNQTFLKK 405
Cdd:cd01480   158 RIACdgKSALYRE----NFAEL--LWSFFIDD 183
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 227-378 9.54e-08

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


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 53.05  E-value: 9.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  227 ADVVFLLDmaINGS--QEDLDHLKAFLGESISALDIKEncmRVGLVTYSNETRVISSLSTGNNKTEVLQRIQDLSPQVGQ 304
Cdd:cd01465     1 LNLVFVID--RSGSmdGPKLPLVKSALKLLVDQLRPDD---RLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTAGGST 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  305 AyTGAALRKTRKEifsAQRGSRKnQGVPQIaVLVTH------RASEDNVTKAAVNLRREGVTIFTMGIEGA-NPDELEKI 377
Cdd:cd01465    76 A-GGAGIQLGYQE---AQKHFVP-GGVNRI-LLATDgdfnvgETDPDELARLVAQKRESGITLSTLGFGDNyNEDLMEAI 149


                  .
gi 156616288  378 A 378
Cdd:cd01465   150 A 150
VWA_2 pfam13519
von Willebrand factor type A domain;
229-327 5.19e-07

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 49.21  E-value: 5.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   229 VVFLLDM-----AINGSQEDLDHLKAFLGESISALDIkencMRVGLVTYSNETRVISSLSTGNNKteVLQRIQDLSPQVG 303
Cdd:pfam13519    1 LVFVLDTsgsmrNGDYGPTRLEAAKDAVLALLKSLPG----DRVGLVTFGDGPEVLIPLTKDRAK--ILRALRRLEPKGG 74

                           90       100
                   ....*....|....*....|....
gi 156616288   304 QAYTGAALRKTRKEIFSAQRGSRK 327
Cdd:pfam13519   75 GTNLAAALQLARAALKHRRKNQPR 98
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 611-767 6.72e-07

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 51.99  E-value: 6.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  611 AEEACRDMKADIMFLVDSSGSIGPENFSKMKMFMKNLVSKSqigADRVQIGVVQFSHENKEEFQLNTFMSQSDIANAIDR 690
Cdd:COG2425   110 ASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRAL---RPNRRFGVILFDTEVVEDLPLTADDGLEDAIEFLSG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  691 MTHIGETTLTgSALTFVSQYFSPDKGArpnvRKFLILITDGEAQ----DIVRdpAIALRKEGVIIYSVGVFGSNVTQLEE 766
Cdd:COG2425   187 LFAGGGTDIA-PALRAALELLEEPDYR----NADIVLITDGEAGvspeELLR--EVRAKESGVRLFTVAIGDAGNPGLLE 259


                  .
gi 156616288  767 I 767
Cdd:COG2425   260 A 260
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 603-756 8.21e-07

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 53.04  E-value: 8.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  603 NQVVQEI-CAEEACRDmKADIMFLVDSSGSIGPENF--SKMKMFMKnLVSKSQIGADRVQIGVVQFSHENKEEFQLNTFM 679
Cdd:PTZ00441   26 NKIVDEVkYREEVCNE-EVDLYLLVDGSGSIGYHNWitHVIPMLMG-LIQQLNLSDDAINLYMSLFSNNTTELIRLGSGA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  680 SQsDIANAIDRMTHI-------GETTLTgSALTFVSQYFSpDKGARPNVRKFLILITDGEAQDIVR--DPAIALRKEGVI 750
Cdd:PTZ00441  104 SK-DKEQALIIVKSLrktylpyGKTNMT-DALLEVRKHLN-DRVNRENAIQLVILMTDGIPNSKYRalEESRKLKDRNVK 180


                  ....*.
gi 156616288  751 IYSVGV 756
Cdd:PTZ00441  181 LAVIGI 186
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 620-788 9.95e-07

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 50.41  E-value: 9.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  620 ADIMFLVDSSGSIGPENFSKMKMF--MKNLVSK--SQIGADRvqIGVVQFShenKEEFQLNTF----MSQSDIANAIDRM 691
Cdd:cd01467     3 RDIMIALDVSGSMLAQDFVKPSRLeaAKEVLSDfiDRRENDR--IGLVVFA---GAAFTQAPLtldrESLKELLEDIKIG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  692 ThIGETTLTGSALTFVSQYFSPDKGarpnVRKFLILITDGE--AQDIVRDPAIALRKE-GVIIYSVGVfGSNVTQLEEIS 768
Cdd:cd01467    78 L-AGQGTAIGDAIGLAIKRLKNSEA----KERVIVLLTDGEnnAGEIDPATAAELAKNkGVRIYTIGV-GKSGSGPKPDG 151

                         170       180
                  ....*....|....*....|
gi 156616288  769 GkpemvfYVENFDILQHIED 788
Cdd:cd01467   152 S------TILDEDSLVEIAD 165
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 435-600 3.19e-06

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: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  435 DIYLLIDGSGSTQPTDFHEMKTFLS---EVVGMFNIAPhkvRVGAVQYADTWDLEFEISK-YSNKPD-----LGKAIENI 505
Cdd:cd01470     2 NIYIALDASDSIGEEDFDEAKNAIKtliEKISSYEVSP---RYEIISYASDPKEIVSIRDfNSNDADdvikrLEDFNYDD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  506 RQMGGNTNTGAALNF---TLKLLQRAKKERGSKVPCHLVVLTNGMS-------------RDSVL--GPAHKLREENIRVH 567
Cdd:cd01470    79 HGDKTGTNTAAALKKvyeRMALEKVRNKEAFNETRHVIILFTDGKSnmggsplptvdkiKNLVYknNKSDNPREDYLDVY 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 156616288  568 AIGV-KEANQTQLREIA---GEEKRVYYVHEFDALRN 600
Cdd:cd01470   159 VFGVgDDVNKEELNDLAskkDNERHFFKLKDYEDLQE 195
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 996-1146 3.24e-06

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 48.86  E-value: 3.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  996 EKVDLVFLMDGSNSIHPDDFQKMKGFLVS--VVQDFDVSLNRVRIGVAQFSDSyrsEFLLGTFTGERE-ISTQIEGIQQI 1072
Cdd:cd01467     1 EGRDIMIALDVSGSMLAQDFVKPSRLEAAkeVLSDFIDRRENDRIGLVVFAGA---AFTQAPLTLDREsLKELLEDIKIG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156616288 1073 F--GYTHIGDALRKVKYYFQPDMGSRinagtpQVLLVLTDGRS-QDEV--AQAAEELRHKGVDIYSVGIGDVDDQELVQ 1146
Cdd:cd01467    78 LagQGTAIGDAIGLAIKRLKNSEAKE------RVIVLLTDGENnAGEIdpATAAELAKNKGVRIYTIGVGKSGSGPKPD 150
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 982-1137 4.32e-06

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 50.73  E-value: 4.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  982 SASVCNsskvdceiEKVDLVFLMDGSNSI-HPDDFQKMKGFLVSVVQDFDVSLNRVRIGVAQFSDSYRSEFLLGTFTGER 1060
Cdd:PTZ00441   35 REEVCN--------EEVDLYLLVDGSGSIgYHNWITHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASKD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288 1061 E-----ISTQIEGIQQIFGYTHIGDALRKVKYYFQpDMGSRINAGtpQVLLVLTDG--RSQDEVAQAAEELRHKGVDIYS 1133
Cdd:PTZ00441  107 KeqaliIVKSLRKTYLPYGKTNMTDALLEVRKHLN-DRVNRENAI--QLVILMTDGipNSKYRALEESRKLKDRNVKLAV 183


                  ....
gi 156616288 1134 VGIG 1137
Cdd:PTZ00441  184 IGIG 187
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 622-768 4.84e-06

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


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 48.11  E-value: 4.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  622 IMFLVDSSGSIGPENFSKM----KMFMKNLvSKSQIGADRVQIGVVQFSHENKEEFQLNTFMSQsdianaIDRMTHIGET 697
Cdd:cd01464     6 IYLLLDTSGSMAGEPIEALnqglQMLQSEL-RQDPYALESVEISVITFDSAARVIVPLTPLESF------QPPRLTASGG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  698 TLTGSALTF--------VSQYFSPDKGA-RPNVrkflILITDGEAQDIVRDPAIALRKEG-----VIIYSVGVfGSNVTQ 763
Cdd:cd01464    79 TSMGAALELaldcidrrVQRYRADQKGDwRPWV----FLLTDGEPTDDLTAAIERIKEARdskgrIVACAVGP-KADLDT 153


                  ....*
gi 156616288  764 LEEIS 768
Cdd:cd01464   154 LKQIT 158
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 433-579 5.11e-06

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 49.29  E-value: 5.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  433 EADIYLLIDGSGSTQPTDFHEMKTFLSEVVGMFNiapHKVRVGAVQYADTWDLEFEISKYSNKPDLGKAIENIRQMGGnT 512
Cdd:COG2425   118 EGPVVLCVDTSGSMAGSKEAAAKAAALALLRALR---PNRRFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLFAGGG-T 193

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156616288  513 NTGAALNFTLKLLQRAKKERGskvpcHLVVLTNGMSRDSVLGPAHKLREE--NIRVHAIGVKEANQTQL 579
Cdd:COG2425   194 DIAPALRAALELLEEPDYRNA-----DIVLITDGEAGVSPEELLREVRAKesGVRLFTVAIGDAGNPGL 257
VWA_2 pfam13519
von Willebrand factor type A domain;
809-917 7.26e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 45.75  E-value: 7.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   809 VVFVIDSSGSIDYQEYN-----IMKDFMIGLVKKAdvgkNQVRFGALKYADDPEVLFYL-DELGTKLEVVSVLQndhPMG 882
Cdd:pfam13519    1 LVFVLDTSGSMRNGDYGptrleAAKDAVLALLKSL----PGDRVGLVTFGDGPEVLIPLtKDRAKILRALRRLE---PKG 73

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 156616288   883 GNTYTAEALAF-SDHMFTEArgsrlhKGVPQVLIVI 917
Cdd:pfam13519   74 GGTNLAAALQLaRAALKHRR------KNQPRRIVLI 103
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 807-968 3.61e-05

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


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 45.34  E-value: 3.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  807 LDVVFVIDSSGSIDYQEYNIMKDFMIGLVKKADvgkNQVRFGALKYADDPEVLFYLDELGTKLEVVSVLQNDHPmGGNTY 886
Cdd:cd01465     1 LNLVFVIDRSGSMDGPKLPLVKSALKLLVDQLR---PDDRLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTA-GGSTA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  887 TAEALAFSDHMFTEARGSRlhkGVPQVLIvITDGESH----DAEKLNTTAKALRDKGILVLAVGIAGANSWELL-AMAGS 961
Cdd:cd01465    77 GGAGIQLGYQEAQKHFVPG---GVNRILL-ATDGDFNvgetDPDELARLVAQKRESGITLSTLGFGDNYNEDLMeAIADA 152


                  ....*..
gi 156616288  962 SDKYYFV 968
Cdd:cd01465   153 GNGNTAY 159
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 435-573 5.44e-05

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


Pssm-ID: 238739 [Multi-domain]  Cd Length: 152  Bit Score: 44.65  E-value: 5.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  435 DIYLLIDGSGStqptdfheMKTFLSEV-----VGMFNIAPHK-VRVGAVQYadtwDLEFEISKYSNKPDLGKAIENIR-- 506
Cdd:cd01462     2 PVILLVDQSGS--------MYGAPEEVakavaLALLRIALAEnRDTYLILF----DSEFQTKIVDKTDDLEEPVEFLSgv 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  507 QMGGNTNTGAALNFTLKLLQRAKKERgskvpCHLVVLTNGM---SRDSVLGPAHKLREENIRVHAIGVKE 573
Cdd:cd01462    70 QLGGGTDINKALRYALELIERRDPRK-----ADIVLITDGYeggVSDELLREVELKRSRVARFVALALGD 134
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 999-1175 6.22e-05

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: 45.39  E-value: 6.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  999 DLVFLMDGSNSIHPDDFQK-MKGFLVSVVQDFDVSLNRVRIGVAQFSDSYRSeflLGTFTGE-----REISTQIEGIQQI 1072
Cdd:cd01473     2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEKNRD---VVPFSDEerydkNELLKKINDLKNS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288 1073 F---GYTHIGDALRKVKYYFQPDMGSRINAgtPQVLLVLTDG----RSQDEVAQAAEELRHKGVDIYSVGIGDVDDQELV 1145
Cdd:cd01473    79 YrsgGETYIVEALKYGLKNYTKHGNRRKDA--PKVTMLFTDGndtsASKKELQDISLLYKEENVKLLVVGVGAASENKLK 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 156616288 1146 QITGTAEK-----KLTVHNFDELKKVKKRIVRNIC 1175
Cdd:cd01473   157 LLAGCDINndncpNVIKTEWNNLNGISKFLTDKIC 191
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 624-760 9.02e-05

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


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 44.19  E-value: 9.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  624 FLVDSSGSIGPENFSKMKMFMKNLVSKSQIgADRVqiGVVQFSHENKEEFQLNTFMSQSDIANAIDRMTHIGETTL-TGS 702
Cdd:cd01465     5 FVIDRSGSMDGPKLPLVKSALKLLVDQLRP-DDRL--AIVTYDGAAETVLPATPVRDKAAILAAIDRLTAGGSTAGgAGI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156616288  703 ALTF--VSQYFSPDKGARpnvrkfLILITDGEAQ------DIVRDPAIALRKEGVIIYSVGvFGSN 760
Cdd:cd01465    82 QLGYqeAQKHFVPGGVNR------ILLATDGDFNvgetdpDELARLVAQKRESGITLSTLG-FGDN 140
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
621-779 1.01e-04

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 44.53  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  621 DIMFLVDSSGSIGPENFSKMK----MFMKNLvSKSQIGADRVQIGVVQFSHENK--------EEFQLNTFMSQSdianai 688
Cdd:COG4245     7 PVYLLLDTSGSMSGEPIEALNeglqALIDEL-RQDPYALETVEVSVITFDGEAKvllpltdlEDFQPPDLSASG------ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  689 drmthigeTTLTGSALTFVSQYFSPDKGA-----RPNVRKFLILITDGEAQDIVRDPAIA-----LRKEGVIIYSVGV-F 757
Cdd:COG4245    80 --------GTPLGAALELLLDLIERRVQKytaegKGDWRPVVFLITDGEPTDSDWEAALQrlkdgEAAKKANIFAIGVgP 151

                         170       180
                  ....*....|....*....|..
gi 156616288  758 GSNVTQLEEISGkPEMVFYVEN 779
Cdd:COG4245   152 DADTEVLKQLTD-PVRALDALD 172
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
807-990 1.15e-04

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 44.53  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  807 LDVVFVIDSSGSIDYQEYNIMKD---FMIGLVKKADVGKNQVRFGALKYADDPEVL--------FYLDELgtklevvsvl 875
Cdd:COG4245     6 LPVYLLLDTSGSMSGEPIEALNEglqALIDELRQDPYALETVEVSVITFDGEAKVLlpltdledFQPPDL---------- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  876 qndhPMGGNTYTAEALAF------SDHMFTEARGSRLHKgvpQVLIVITDGESHDAEkLNTTAKALRD----KGILVLAV 945
Cdd:COG4245    76 ----SASGGTPLGAALELlldlieRRVQKYTAEGKGDWR---PVVFLITDGEPTDSD-WEAALQRLKDgeaaKKANIFAI 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 156616288  946 GI-AGANswelLAMAGS-SDKYYFVET--FGGLKGIFSDVSASVCNSSK 990
Cdd:COG4245   148 GVgPDAD----TEVLKQlTDPVRALDAldGLDFREFFKWLSASVSSVSR 192
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 18-192 1.82e-04

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 44.54  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   18 QDSGPEYADVVFLVDSSDHLGLKS-FPLVKTFIHKMISSLPIEAnkyRVALAQYSD----ALHNEFQLGTFKNRnpmLNH 92
Cdd:COG1240    86 LARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRD---RVGLVAFGGeaevLLPLTRDREALKRA---LDE 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   93 LKknfgfIGGSLKIGNALQEAHRTYFSAPTNGRdkkqfpPILVVL---ASAESEDDVEEAAKALREDGVKI--ISVGVQK 167
Cdd:COG1240   160 LP-----PGGGTPLGDALALALELLKRADPARR------KVIVLLtdgRDNAGRIDPLEAAELAAAAGIRIytIGVGTEA 228

                         170       180
                  ....*....|....*....|....*...
gi 156616288  168 ASEENLKAMATS---QFhFNLRTARDLS 192
Cdd:COG1240   229 VDEGLLREIAEAtggRY-FRADDLSELA 255
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 807-968 2.30e-04

VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. The members of this subgroup lack the MIDAS motif. This subgroup is found only in C. elegans and the members identified thus far are always found fused to a C-Lectin type domain. Biochemical function thus far has not be attributed to any of the members of this subgroup.


Pssm-ID: 238754 [Multi-domain]  Cd Length: 193  Bit Score: 43.57  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  807 LDVVFVIDSS-GSIDYQEYNIMKDF--MIGLVKKADVGKNQ---VRFGALKYADDPEVLFYLDELGTKLEVVSVLQ---N 877
Cdd:cd01477    20 LDIVFVVDNSkGMTQGGLWQVRATIssLFGSSSQIGTDYDDprsTRVGLVTYNSNATVVADLNDLQSFDDLYSQIQgslT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  878 DHPMGGNTYTAEALAFSDHMF-TEARGSRLHkgVPQVLIVIT----DGESHDAEKLnttAKALRDKGILVLAVGIAGANS 952
Cdd:cd01477   100 DVSSTNASYLDTGLQAAEQMLaAGKRTSREN--YKKVVIVFAsdynDEGSNDPRPI---AARLKSTGIAIITVAFTQDES 174

                         170
                  ....*....|....*...
gi 156616288  953 WELLAMAG--SSDKYYFV 968
Cdd:cd01477   175 SNLLDKLGkiASPGMNFT 192
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 435-610 2.47e-04

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 43.46  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  435 DIYLLIDGSGSTQPTDF-HEMKTFLSEVVGMFNIAPHKVRVGAVQYAD---TWDLEFEISKYsNKPDLGKAIENIRQ--- 507
Cdd:cd01473     2 DLTLILDESASIGYSNWrKDVIPFTEKIINNLNISKDKVHVGILLFAEknrDVVPFSDEERY-DKNELLKKINDLKNsyr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  508 MGGNTNTGAALNFTLKLLQRaKKERGSKVPCHLVVLTNG---MSRDSVLGPAHKL-REENIRVHAIGVKEANQTQLREIA 583
Cdd:cd01473    81 SGGETYIVEALKYGLKNYTK-HGNRRKDAPKVTMLFTDGndtSASKKELQDISLLyKEENVKLLVVGVGAASENKLKLLA 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 156616288  584 GEEK------RVYYVhEFDALRNIRNQVVQEIC 610
Cdd:cd01473   160 GCDInndncpNVIKT-EWNNLNGISKFLTDKIC 191
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 438-584 2.47e-04

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


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 43.03  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  438 LLIDGSGSTQPTDFHEMKTFLSEVVGMFNIAPhkvRVGAVQYADTWDLEFEISKYSNKPDLGKAIENIRQmGGNTNTGAA 517
Cdd:cd01465     5 FVIDRSGSMDGPKLPLVKSALKLLVDQLRPDD---RLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTA-GGSTAGGAG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156616288  518 LNFTLKLLQRAKKERGSKvpcHLVVLTNG------MSRDSVLGPAHKLREENIRVHAIGV-KEANQTQLREIAG 584
Cdd:cd01465    81 IQLGYQEAQKHFVPGGVN---RILLATDGdfnvgeTDPDELARLVAQKRESGITLSTLGFgDNYNEDLMEAIAD 151
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 621-775 2.82e-04

VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. The members of this subgroup lack the MIDAS motif. This subgroup is found only in C. elegans and the members identified thus far are always found fused to a C-Lectin type domain. Biochemical function thus far has not be attributed to any of the members of this subgroup.


Pssm-ID: 238754 [Multi-domain]  Cd Length: 193  Bit Score: 43.18  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  621 DIMFLVDSSGSIGPENFSKMKMFMKNLVSKS-QIGAD-----RVQIGVVQFSHENKEEFQLNTFMSQSDIANAIDR-MTH 693
Cdd:cd01477    21 DIVFVVDNSKGMTQGGLWQVRATISSLFGSSsQIGTDyddprSTRVGLVTYNSNATVVADLNDLQSFDDLYSQIQGsLTD 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  694 IGETTLT--GSALTFVSQYFSPDK-GARPNVRKFLILIT---DGEAQDIVRDPAIALRKEGVIIYSVGVFGSNVTQLEEI 767
Cdd:cd01477   101 VSSTNASylDTGLQAAEQMLAAGKrTSRENYKKVVIVFAsdyNDEGSNDPRPIAARLKSTGIAIITVAFTQDESSNLLDK 180

                         170
                  ....*....|.
gi 156616288  768 SGK---PEMVF 775
Cdd:cd01477   181 LGKiasPGMNF 191
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
435-589 3.10e-04

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 43.37  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  435 DIYLLIDGSGSTQPTDFHEMKTFLSEVVGMFNIAPH---KVRVGAVQYADT--W-----DLE-FEIskysnkPDLgkaie 503
Cdd:COG4245     7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYaleTVEVSVITFDGEakVllpltDLEdFQP------PDL----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  504 nirQMGGNTNTGAALNFTLKLLQRAK-KERGSKVPCH---LVVLTNGMSRDSVLGPA-----HKLREENIRVHAIGV-KE 573
Cdd:COG4245    76 ---SASGGTPLGAALELLLDLIERRVqKYTAEGKGDWrpvVFLITDGEPTDSDWEAAlqrlkDGEAAKKANIFAIGVgPD 152

                         170
                  ....*....|....*.
gi 156616288  574 ANQTQLREIAGEEKRV 589
Cdd:COG4245   153 ADTEVLKQLTDPVRAL 168
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 48-177 3.45e-04

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 43.07  E-value: 3.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288   48 FIHKMISSLPIEANKYRVALAQYSDAL--HNEFQLGTFKNRNPML---NHLKKNFgFIGGSLKIGNALQEAHRTYFSAPT 122
Cdd:cd01473    25 FTEKIINNLNISKDKVHVGILLFAEKNrdVVPFSDEERYDKNELLkkiNDLKNSY-RSGGETYIVEALKYGLKNYTKHGN 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 156616288  123 NgrdKKQFPPILVVLA----SAESEDDVEEAAKALREDGVKIISVGVQKASEENLKAMA 177
Cdd:cd01473   104 R---RKDAPKVTMLFTdgndTSASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLA 159
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 1000-1141 7.02e-04

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 43.06  E-value: 7.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  1000 LVFLMDGSNSIHPD-DF--QKMKGFLVSVVQDFDvslnrvRIGVAQFSDsyrSEFLLGTFTGE-REISTQIEGIQ----- 1070
Cdd:TIGR03436   56 VGLVIDTSGSMRNDlDRarAAAIRFLKTVLRPND------RVFVVTFNT---RLRLLQDFTSDpRLLEAALNRLKpplrt 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  1071 -----QIFGYTHIGDALRKVKYYFQPDMGSRINAGTP--QVLLVLTDG---RSQDEVAQAAEELRHKGVDIYSVGIGDVD 1140
Cdd:TIGR03436  127 dynssGAFVRDGGGTALYDAITLAALEQLANALAGIPgrKALIVISDGgdnRSRDTLERAIDAAQRADVAIYSIDARGLR 206


                   .
gi 156616288  1141 D 1141
Cdd:TIGR03436  207 A 207
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 807-922 2.98e-03

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: 40.35  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  807 LDVVFVIDSSGSIDYQEYNIMKDFMIGLVKKADVGKNQVRFGALKYADDP-EVLFYLDELGTKL-EVVSVLQN----DHP 880
Cdd:cd01470     1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPkEIVSIRDFNSNDAdDVIKRLEDfnydDHG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 156616288  881 MGGNTYTAEAL-AFSDHMFTEARGSRLH-KGVPQVLIVITDGES 922
Cdd:cd01470    81 DKTGTNTAAALkKVYERMALEKVRNKEAfNETRHVIILFTDGKS 124
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 228-378 8.35e-03

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


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 38.14  E-value: 8.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616288  228 DVVFLLDMAINGSQEDLDHLKAFLGESISALDIKEncmRVGLVTYSNETRVISSLS--TGNNKTEVLQRIQDLspqvgQA 305
Cdd:cd01466     2 DLVAVLDVSGSMAGDKLQLVKHALRFVISSLGDAD---RLSIVTFSTSAKRLSPLRrmTAKGKRSAKRVVDGL-----QA 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156616288  306 YTGAALRKTRKEIFSAQRGSRKNQGVPQIAVLVThraSEDNVTKAAVNLRREGVTIFTMGIEGAN-PDELEKIA 378
Cdd:cd01466    74 GGGTNVVGGLKKALKVLGDRRQKNPVASIMLLSD---GQDNHGAVVLRADNAPIPIHTFGLGASHdPALLAFIA 144
 
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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