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Conserved domains on  [gi|156523168|ref|NP_001095998|]
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matrilin-2 precursor [Bos taurus]

Protein Classification

vWA domain-containing protein( domain architecture ID 10107171)

vWA (von Willebrand factor type A) domain-containing protein may be involved in one of a wide variety of important cellular functions, including basal membrane formation, cell migration, cell differentiation, adhesion, hemostasis, signaling, chromosomal stability, malignant transformation, and immune defenses

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 56-278 5.00e-134

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: 401.38  E-value: 5.00e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  56 KRADVVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTG 135
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 136 TMTGLAIQYALNIAFSEAEGARPLRENVPRVIMIVTDGRPQDSVAEVAAKARDTGILIFAIGVGQVDFNTLKAIGSEPHE 215
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156523168 216 DHVFLVANFSQIETLTSVFQKKLC-TVHMCSILEHNCAHFCINTPGSYVCRCKQGYILNSDEKT 278
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICvVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 654-894 7.12e-118

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


The actual alignment was detected with superfamily member cd01475:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 224  Bit Score: 359.39  E-value: 7.12e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 654 GPVDLVFVIDGSKSLGEDNFEIVKQFVTGIIDSLAISPKAARVGLLQYSTLVRTEFTLRNFSSAKDMKKAVAHMKYMGKG 733
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 734 SMTGLALKHMFERSFTQVEGARPLSARVPRVAIVFTDGRAQDDVSEWASKAQASGITMYAVGVGKAIEEELQEIASEPTE 813
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 814 KHLFYAEDFSTMGEISDKLQKGICEaledsdgrQDSPAGELPKRVHQPTESEPVTInirdllscsNFAVQHRYLFEEDNL 893
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICV--------VPDLCATLSHVCQQVCISTPGSY---------LCACTEGYALLEDNK 223


                 .
gi 156523168 894 A 894
Cdd:cd01475  224 T 224
Matrilin_ccoil pfam10393
Trimeric coiled-coil oligomerization domain of matrilin; This short domain is a coiled coil ...
 913-955 7.82e-16

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


:

Pssm-ID: 463070  Cd Length: 43  Bit Score: 72.00  E-value: 7.82e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 156523168  913 EKQDQCKCENLIMFQNLANEEVRKLTQRLEEMTQRMEALENRL 955
Cdd:pfam10393   1 VEEDPCKCEAIVAFQTKVESEIQALTTKLEEVTKRIEALENRL 43
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 408-443 2.86e-08

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


:

Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 50.32  E-value: 2.86e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  408 CALNKPGCEHECINTEEGYYCRCRRGYTLDPNGKTC 443
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 326-361 7.19e-08

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


:

Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 49.16  E-value: 7.19e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  326 CASENHGCEHECVNADGSYLCRCPKGFALNPDKKTC 361
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 367-402 1.12e-07

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


:

Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 48.78  E-value: 1.12e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  367 CASPNHGCQHECVNTDDSYACRCLKGFTLNPDQKTC 402
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 563-605 3.16e-07

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


The actual alignment was detected with superfamily member cd01475:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 224  Bit Score: 52.39  E-value: 3.16e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 156523168 563 GKTCRRKDVCQAVDHGCEHACVSTGESYVCKCMEGFRLAEDGK 605
Cdd:cd01475  181 GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 531-566 3.73e-07

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


:

Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 47.24  E-value: 3.73e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  531 CALGKHGCEHLCISSGDSFVCRCFEGYILRGDGKTC 566
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 490-525 2.86e-06

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


:

Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 44.54  E-value: 2.86e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  490 CLLSRHGCEYSCVNTDRSFVCECPEGHVLRSDGKTC 525
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 613-648 3.92e-06

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


:

Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 44.16  E-value: 3.92e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  613 CKSTHHGCEHICVNRGNSYICKCSKGFILAEDGRRC 648
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 449-484 5.37e-06

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


:

Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 43.77  E-value: 5.37e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  449 CAEQDHGCEQLCLNTEDSFVCQCSEGFLINDDLKTC 484
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 285-320 1.14e-05

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


:

Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 43.00  E-value: 1.14e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  285 CAADDHGCEQLCVNLLGSFVCQCYSGYALAVDGKRC 320
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
 
Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 56-278 5.00e-134

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: 401.38  E-value: 5.00e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  56 KRADVVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTG 135
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 136 TMTGLAIQYALNIAFSEAEGARPLRENVPRVIMIVTDGRPQDSVAEVAAKARDTGILIFAIGVGQVDFNTLKAIGSEPHE 215
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156523168 216 DHVFLVANFSQIETLTSVFQKKLC-TVHMCSILEHNCAHFCINTPGSYVCRCKQGYILNSDEKT 278
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICvVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 654-894 7.12e-118

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 359.39  E-value: 7.12e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 654 GPVDLVFVIDGSKSLGEDNFEIVKQFVTGIIDSLAISPKAARVGLLQYSTLVRTEFTLRNFSSAKDMKKAVAHMKYMGKG 733
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 734 SMTGLALKHMFERSFTQVEGARPLSARVPRVAIVFTDGRAQDDVSEWASKAQASGITMYAVGVGKAIEEELQEIASEPTE 813
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 814 KHLFYAEDFSTMGEISDKLQKGICEaledsdgrQDSPAGELPKRVHQPTESEPVTInirdllscsNFAVQHRYLFEEDNL 893
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICV--------VPDLCATLSHVCQQVCISTPGSY---------LCACTEGYALLEDNK 223


                 .
gi 156523168 894 A 894
Cdd:cd01475  224 T 224
VWA pfam00092
von Willebrand factor type A domain;
657-831 2.27e-61

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 205.97  E-value: 2.27e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  657 DLVFVIDGSKSLGEDNFEIVKQFVTGIIDSLAISPKAARVGLLQYSTLVRTEFTLRNFSSAKDMKKAVAHMKYMGKGSM- 735
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  736 TGLALKHMFERSFTQVEGARPlsaRVPRVAIVFTDGRAQD-DVSEWASKAQASGITMYAVGVGKAIEEELQEIASEPTEK 814
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARP---GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                         170
                  ....*....|....*..
gi 156523168  815 HLFYAEDFSTMGEISDK 831
Cdd:pfam00092 158 HVFTVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
59-232 1.11e-60

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 204.05  E-value: 1.11e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168   59 DVVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTGTM- 137
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  138 TGLAIQYALNIAFSEAEGARPlreNVPRVIMIVTDGRPQD-SVAEVAAKARDTGILIFAIGVGQVDFNTLKAIGSEPHED 216
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARP---GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                         170
                  ....*....|....*.
gi 156523168  217 HVFLVANFSQIETLTS 232
Cdd:pfam00092 158 HVFTVSDFEALEDLQD 173
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 59-230 1.13e-45

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: 161.85  E-value: 1.13e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168    59 DVVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMR-HLSTGTM 137
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168   138 TGLAIQYALNIAFSEAEGARPlreNVPRVIMIVTDGRPQDS---VAEVAAKARDTGILIFAIGVGQ-VDFNTLKAIGSEP 213
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRR---GAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNdVDEEELKKLASAP 157

                          170
                   ....*....|....*..
gi 156523168   214 HEDHVFLVANFSQIETL 230
Cdd:smart00327 158 GGVYVFLPELLDLLIDL 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 657-829 3.11e-45

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: 160.70  E-value: 3.11e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168   657 DLVFVIDGSKSLGEDNFEIVKQFVTGIIDSLAISPKAARVGLLQYSTLVRTEFTLRNFSSAKDMKKAVAHMKY-MGKGSM 735
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168   736 TGLALKHMFERSFTQVEGARPlsaRVPRVAIVFTDGRAQD---DVSEWASKAQASGITMYAVGVGKAI-EEELQEIASEP 811
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRR---GAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVdEEELKKLASAP 157

                          170
                   ....*....|....*...
gi 156523168   812 TEKHLFYAEDFSTMGEIS 829
Cdd:smart00327 158 GGVYVFLPELLDLLIDLL 175
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 56-209 7.04e-16

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 78.83  E-value: 7.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  56 KRADVVFIIDSSRSVNTHD-YAKVKEFIvdiLQFLDIGPDVTRVGLLQYGSTVKNEFSLkTfkrkSEVERAVKRMRHLST 134
Cdd:COG1240   91 RGRDVVLVVDASGSMAAENrLEAAKGAL---LDFLDDYRPRDRVGLVAFGGEAEVLLPL-T----RDREALKRALDELPP 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 135 GTMT--GLAIQYALNIAfseaegaRPLRENVPRVIMIVTDGRPQDSVA---EVAAKARDTGILIFAIGVG--QVDFNTLK 207
Cdd:COG1240  163 GGGTplGDALALALELL-------KRADPARRKVIVLLTDGRDNAGRIdplEAAELAAAAGIRIYTIGVGteAVDEGLLR 235


                 ..
gi 156523168 208 AI 209
Cdd:COG1240  236 EI 237
Matrilin_ccoil pfam10393
Trimeric coiled-coil oligomerization domain of matrilin; This short domain is a coiled coil ...
 913-955 7.82e-16

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


Pssm-ID: 463070  Cd Length: 43  Bit Score: 72.00  E-value: 7.82e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 156523168  913 EKQDQCKCENLIMFQNLANEEVRKLTQRLEEMTQRMEALENRL 955
Cdd:pfam10393   1 VEEDPCKCEAIVAFQTKVESEIQALTTKLEEVTKRIEALENRL 43
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 655-828 4.81e-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: 4.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 655 PVDLVFVIDGSKS-LGEDNFEIVKQFVTGIIDSLaisPKAARVGLLQYSTLVRT--EFTlrnfSSAKDMKKAVAHMKYMG 731
Cdd:COG1240   92 GRDVVLVVDASGSmAAENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVllPLT----RDREALKRALDELPPGG 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 732 KGSMtGLALKHMFERsftqvegARPLSARVPRVAIVFTDGRA---QDDVSEWASKAQASGITMYAVGVGKAI--EEELQE 806
Cdd:COG1240  165 GTPL-GDALALALEL-------LKRADPARRKVIVLLTDGRDnagRIDPLEAAELAAAAGIRIYTIGVGTEAvdEGLLRE 236

                        170       180
                 ....*....|....*....|..
gi 156523168 807 IASEpTEKHLFYAEDFSTMGEI 828
Cdd:COG1240  237 IAEA-TGGRYFRADDLSELAAI 257
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 408-443 2.86e-08

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


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 50.32  E-value: 2.86e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  408 CALNKPGCEHECINTEEGYYCRCRRGYTLDPNGKTC 443
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 326-361 7.19e-08

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


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 49.16  E-value: 7.19e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  326 CASENHGCEHECVNADGSYLCRCPKGFALNPDKKTC 361
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 367-402 1.12e-07

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


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 48.78  E-value: 1.12e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  367 CASPNHGCQHECVNTDDSYACRCLKGFTLNPDQKTC 402
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 563-605 3.16e-07

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 52.39  E-value: 3.16e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 156523168 563 GKTCRRKDVCQAVDHGCEHACVSTGESYVCKCMEGFRLAEDGK 605
Cdd:cd01475  181 GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 531-566 3.73e-07

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


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 47.24  E-value: 3.73e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  531 CALGKHGCEHLCISSGDSFVCRCFEGYILRGDGKTC 566
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 522-565 1.70e-06

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 50.08  E-value: 1.70e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 156523168 522 GKTCAKLDACALGKHGCEHLCISSGDSFVCRCFEGYILRGDGKT 565
Cdd:cd01475  181 GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 490-525 2.86e-06

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


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 44.54  E-value: 2.86e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  490 CLLSRHGCEYSCVNTDRSFVCECPEGHVLRSDGKTC 525
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 613-648 3.92e-06

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


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 44.16  E-value: 3.92e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  613 CKSTHHGCEHICVNRGNSYICKCSKGFILAEDGRRC 648
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 572-607 4.16e-06

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


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 44.16  E-value: 4.16e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  572 CQAVDHGCEHACVSTGESYVCKCMEGFRLAEDGKRC 607
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 449-484 5.37e-06

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


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 43.77  E-value: 5.37e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  449 CAEQDHGCEQLCLNTEDSFVCQCSEGFLINDDLKTC 484
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 55-240 7.17e-06

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 49.96  E-value: 7.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  55 NKRADVVFIIDSSRSVNTHDY-AKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEvERAVKRMRHL- 132
Cdd:PTZ00441  40 NEEVDLYLLVDGSGSIGYHNWiTHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASKDK-EQALIIVKSLr 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 133 STGTMTGlaiQYALNIAFSEAE---GARPLRENVPRVIMIVTDGRP---QDSVaEVAAKARDTGILIFAIGVGQ---VDF 203
Cdd:PTZ00441 119 KTYLPYG---KTNMTDALLEVRkhlNDRVNRENAIQLVILMTDGIPnskYRAL-EESRKLKDRNVKLAVIGIGQginHQF 194

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 156523168 204 NTLKAiGSEPHED--HVFLVANFSQIETLTSVFQKKLCT 240
Cdd:PTZ00441 195 NRLLA-GCRPREGkcKFYSDADWEEAKNLIKPFIAKVCT 232
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 285-320 1.14e-05

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


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 43.00  E-value: 1.14e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  285 CAADDHGCEQLCVNLLGSFVCQCYSGYALAVDGKRC 320
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
405-443 1.83e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.84  E-value: 1.83e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 156523168   405 INYCALNKPgCEH--ECINTEEGYYCRCRRGYTldpNGKTC 443
Cdd:smart00179   2 IDECASGNP-CQNggTCVNTVGSYRCECPPGYT---DGRNC 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
364-402 2.12e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.84  E-value: 2.12e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 156523168   364 IDYCASPnHGCQH--ECVNTDDSYACRCLKGFTlnpDQKTC 402
Cdd:smart00179   2 IDECASG-NPCQNggTCVNTVGSYRCECPPGYT---DGRNC 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 405-443 3.44e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 36.08  E-value: 3.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 156523168 405 INYCALNKP-GCEHECINTEEGYYCRCRRGYTldpnGKTC 443
Cdd:cd00054    2 IDECASGNPcQNGGTCVNTVGSYRCSCPPGYT----GRNC 37
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 364-395 6.60e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 35.31  E-value: 6.60e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 156523168 364 IDYCASPNhGCQH--ECVNTDDSYACRCLKGFTL 395
Cdd:cd00054    2 IDECASGN-PCQNggTCVNTVGSYRCSCPPGYTG 34
EGF_CA smart00179
Calcium-binding EGF-like domain;
287-321 7.18e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 35.30  E-value: 7.18e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 156523168   287 ADDHGCEQ--LCVNLLGSFVCQCYSGYalaVDGKRCE 321
Cdd:smart00179   6 ASGNPCQNggTCVNTVGSYRCECPPGY---TDGRNCE 39
 
Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 56-278 5.00e-134

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: 401.38  E-value: 5.00e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  56 KRADVVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTG 135
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 136 TMTGLAIQYALNIAFSEAEGARPLRENVPRVIMIVTDGRPQDSVAEVAAKARDTGILIFAIGVGQVDFNTLKAIGSEPHE 215
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156523168 216 DHVFLVANFSQIETLTSVFQKKLC-TVHMCSILEHNCAHFCINTPGSYVCRCKQGYILNSDEKT 278
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICvVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 654-894 7.12e-118

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 359.39  E-value: 7.12e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 654 GPVDLVFVIDGSKSLGEDNFEIVKQFVTGIIDSLAISPKAARVGLLQYSTLVRTEFTLRNFSSAKDMKKAVAHMKYMGKG 733
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 734 SMTGLALKHMFERSFTQVEGARPLSARVPRVAIVFTDGRAQDDVSEWASKAQASGITMYAVGVGKAIEEELQEIASEPTE 813
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 814 KHLFYAEDFSTMGEISDKLQKGICEaledsdgrQDSPAGELPKRVHQPTESEPVTInirdllscsNFAVQHRYLFEEDNL 893
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICV--------VPDLCATLSHVCQQVCISTPGSY---------LCACTEGYALLEDNK 223


                 .
gi 156523168 894 A 894
Cdd:cd01475  224 T 224
VWA pfam00092
von Willebrand factor type A domain;
657-831 2.27e-61

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 205.97  E-value: 2.27e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  657 DLVFVIDGSKSLGEDNFEIVKQFVTGIIDSLAISPKAARVGLLQYSTLVRTEFTLRNFSSAKDMKKAVAHMKYMGKGSM- 735
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  736 TGLALKHMFERSFTQVEGARPlsaRVPRVAIVFTDGRAQD-DVSEWASKAQASGITMYAVGVGKAIEEELQEIASEPTEK 814
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARP---GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                         170
                  ....*....|....*..
gi 156523168  815 HLFYAEDFSTMGEISDK 831
Cdd:pfam00092 158 HVFTVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
59-232 1.11e-60

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 204.05  E-value: 1.11e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168   59 DVVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTGTM- 137
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  138 TGLAIQYALNIAFSEAEGARPlreNVPRVIMIVTDGRPQD-SVAEVAAKARDTGILIFAIGVGQVDFNTLKAIGSEPHED 216
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARP---GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                         170
                  ....*....|....*.
gi 156523168  217 HVFLVANFSQIETLTS 232
Cdd:pfam00092 158 HVFTVSDFEALEDLQD 173
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 657-822 4.55e-58

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 196.35  E-value: 4.55e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 657 DLVFVIDGSKSLGEDNFEIVKQFVTGIIDSLAISPKAARVGLLQYSTLVRTEFTLRNFSSAKDMKKAVAHMKYMGKGSMT 736
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 737 GLALKHMFERSFTQVEGARPlsaRVPRVAIVFTDGRAQDDVSEWASKAQASGITMYAVGVGKAIEEELQEIASEPTEKHL 816
Cdd:cd01482   82 GKALTHVREKNFTPDAGARP---GVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHV 158


                 ....*.
gi 156523168 817 FYAEDF 822
Cdd:cd01482  159 FNVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 656-822 7.29e-57

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: 193.21  E-value: 7.29e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 656 VDLVFVIDGSKSLGEDNFEIVKQFVTGIIDSLAISPKAARVGLLQYSTLVRTEFTLRNFSSAKDMKKAVAHMKYMGKGSM 735
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 736 TGLALKHMFERSFTQVEGARPlsaRVPRVAIVFTDGRAQDDVSEWASKAQASGITMYAVGVGKAIEEELQEIASEPTEKH 815
Cdd:cd01472   81 TGKALKYVRENLFTEASGSRE---GVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELY 157


                 ....*..
gi 156523168 816 LFYAEDF 822
Cdd:cd01472  158 VFNVADF 164
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 58-219 8.92e-55

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: 187.11  E-value: 8.92e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  58 ADVVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHL-STGT 136
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLgGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 137 MTGLAIQYALNIAFSEaegaRPLRENVPRVIMIVTDGRPQD--SVAEVAAKARDTGILIFAIGVGQVDFNTLKAIGSEPH 214
Cdd:cd01450   81 NTGKALQYALEQLFSE----SNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156


                 ....*
gi 156523168 215 EDHVF 219
Cdd:cd01450  157 ERHVF 161
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 656-817 1.05e-54

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: 187.11  E-value: 1.05e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 656 VDLVFVIDGSKSLGEDNFEIVKQFVTGIIDSLAISPKAARVGLLQYSTLVRTEFTLRNFSSAKDMKKAVAHMKYM-GKGS 734
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLgGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 735 MTGLALKHMFERSFTQvEGARPlsaRVPRVAIVFTDGRAQD--DVSEWASKAQASGITMYAVGVGKAIEEELQEIASEPT 812
Cdd:cd01450   81 NTGKALQYALEQLFSE-SNARE---NVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156


                 ....*
gi 156523168 813 EKHLF 817
Cdd:cd01450  157 ERHVF 161
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 58-224 3.98e-52

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: 179.73  E-value: 3.98e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  58 ADVVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTGTM 137
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 138 TGLAIQYALNIAFSEAEGArplRENVPRVIMIVTDGRPQDSVAEVAAKARDTGILIFAIGVGQVDFNTLKAIGSEPHEDH 217
Cdd:cd01472   81 TGKALKYVRENLFTEASGS---REGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELY 157


                 ....*..
gi 156523168 218 VFLVANF 224
Cdd:cd01472  158 VFNVADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 58-224 2.33e-49

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: 172.09  E-value: 2.33e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  58 ADVVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTGTM 137
Cdd:cd01482    1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 138 TGLAIQYALNIAFSEAEGARPlreNVPRVIMIVTDGRPQDSVAEVAAKARDTGILIFAIGVGQVDFNTLKAIGSEPHEDH 217
Cdd:cd01482   81 TGKALTHVREKNFTPDAGARP---GVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH 157


                 ....*..
gi 156523168 218 VFLVANF 224
Cdd:cd01482  158 VFNVADF 164
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 59-230 1.13e-45

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: 161.85  E-value: 1.13e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168    59 DVVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMR-HLSTGTM 137
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168   138 TGLAIQYALNIAFSEAEGARPlreNVPRVIMIVTDGRPQDS---VAEVAAKARDTGILIFAIGVGQ-VDFNTLKAIGSEP 213
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRR---GAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNdVDEEELKKLASAP 157

                          170
                   ....*....|....*..
gi 156523168   214 HEDHVFLVANFSQIETL 230
Cdd:smart00327 158 GGVYVFLPELLDLLIDL 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 657-829 3.11e-45

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: 160.70  E-value: 3.11e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168   657 DLVFVIDGSKSLGEDNFEIVKQFVTGIIDSLAISPKAARVGLLQYSTLVRTEFTLRNFSSAKDMKKAVAHMKY-MGKGSM 735
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168   736 TGLALKHMFERSFTQVEGARPlsaRVPRVAIVFTDGRAQD---DVSEWASKAQASGITMYAVGVGKAI-EEELQEIASEP 811
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRR---GAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVdEEELKKLASAP 157

                          170
                   ....*....|....*...
gi 156523168   812 TEKHLFYAEDFSTMGEIS 829
Cdd:smart00327 158 GGVYVFLPELLDLLIDLL 175
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 59-230 4.21e-40

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: 145.96  E-value: 4.21e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  59 DVVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTGTMT 138
Cdd:cd01469    2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 139 GLAIQYALNIAFSEAEGARPlreNVPRVIMIVTDGRPQDS--VAEVAAKARDTGILIFAIGVGQVdFNT------LKAIG 210
Cdd:cd01469   82 ATAIQYVVTELFSESNGARK---DATKVLVVITDGESHDDplLKDVIPQAEREGIIRYAIGVGGH-FQRensreeLKTIA 157

                        170       180
                 ....*....|....*....|
gi 156523168 211 SEPHEDHVFLVANFSQIETL 230
Cdd:cd01469  158 SKPPEEHFFNVTDFAALKDI 177
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 58-224 2.69e-38

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: 140.54  E-value: 2.69e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  58 ADVVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRhLSTGTM 137
Cdd:cd01481    1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLR-LRGGSQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 138 --TGLAIQYALNIAFSEAEGARpLRENVPRVIMIVTDGRPQDSVAEVAAKARDTGILIFAIGVGQVDFNTLKAIGSEPhe 215
Cdd:cd01481   80 lnTGSALDYVVKNLFTKSAGSR-IEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP-- 156


                 ....*....
gi 156523168 216 DHVFLVANF 224
Cdd:cd01481  157 SFVFQVSDF 165
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 656-828 4.29e-38

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: 140.18  E-value: 4.29e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 656 VDLVFVIDGSKSLGEDNFEIVKQFVTGIIDSLAISPKAARVGLLQYSTLVRTEFTLRNFSSAKDMKKAVAHMKYMGKGSM 735
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 736 TGLALKHMFERSFTQVEGARPLSArvpRVAIVFTDGRAQDDVSEWA--SKAQASGITMYAVGVGKAIE-----EELQEIA 808
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDAT---KVLVVITDGESHDDPLLKDviPQAEREGIIRYAIGVGGHFQrensrEELKTIA 157

                        170       180
                 ....*....|....*....|
gi 156523168 809 SEPTEKHLFYAEDFSTMGEI 828
Cdd:cd01469  158 SKPPEEHFFNVTDFAALKDI 177
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 657-822 1.11e-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: 127.05  E-value: 1.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 657 DLVFVIDGSKSLGEDNFEIVKQFVTGIIDSLAISPKAARVGLLQYSTLVRTEFTLRNFSSAKDMKKAVAHMKYM-GKGSM 735
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRgGSQLN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 736 TGLALKHMFERSFTQVEGARpLSARVPRVAIVFTDGRAQDDVSEWASKAQASGITMYAVGVGKAIEEELQEIASEPteKH 815
Cdd:cd01481   82 TGSALDYVVKNLFTKSAGSR-IEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP--SF 158


                 ....*..
gi 156523168 816 LFYAEDF 822
Cdd:cd01481  159 VFQVSDF 165
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 58-219 1.53e-31

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: 120.97  E-value: 1.53e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  58 ADVVFIIDSSRSVNtHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKN--EFSLKTFKRKSEVERAVKRMRHLSTG 135
Cdd:cd01476    1 LDLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 136 TMTGLAIQYALNIaFSEAEGARplrENVPRVIMIVTDGRPQDSVAEVAAKARDT-GILIFAIGVG---QVDFNTLKAIGS 211
Cdd:cd01476   80 TATGAAIEVALQQ-LDPSEGRR---EGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGdpgTVDTEELHSITG 155


                 ....*...
gi 156523168 212 EphEDHVF 219
Cdd:cd01476  156 N--EDHIF 161
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 58-219 2.26e-30

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 117.67  E-value: 2.26e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  58 ADVVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRH-LSTGT 136
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 137 MTGLAIQYALNIAFSEAegarplRENVPRVIMIVTDGRPQDS---VAEVAAKARDTGILIFAIGVG-QVDFNTLKAIGSE 212
Cdd:cd00198   81 NIGAALRLALELLKSAK------RPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIGdDANEDELKEIADK 154


                 ....*..
gi 156523168 213 PHEDHVF 219
Cdd:cd00198  155 TTGGAVF 161
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 656-817 4.71e-29

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: 113.81  E-value: 4.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 656 VDLVFVIDGSKSLGEDNFEIVKQFVTGIIDSLAISPKAARVGLLQYSTLVRTEFTLRNFSSAKDMKKAVAHMKY-MGKGS 734
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 735 MTGLALKHMFErsftqvEGARPLSARVPRVAIVFTDGRAQDD---VSEWASKAQASGITMYAVGVG-KAIEEELQEIASE 810
Cdd:cd00198   81 NIGAALRLALE------LLKSAKRPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIGdDANEDELKEIADK 154


                 ....*..
gi 156523168 811 PTEKHLF 817
Cdd:cd00198  155 TTGGAVF 161
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 654-825 9.96e-28

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: 110.94  E-value: 9.96e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 654 GPVDLVFVIDGSKSLGEDNFEIVKQFVTGIIDSL------AISPKAARVGLLQYSTLVRTEFT-LRNFSSAKDMKKAVAH 726
Cdd:cd01480    1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGfLRDIRNYTSLKEAVDN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 727 MKYMGKGSMTGLALKHMFErsftQVEGARPLSARvpRVAIVFTDGRAQ----DDVSEWASKAQASGITMYAVGVGKAIEE 802
Cdd:cd01480   81 LEYIGGGTFTDCALKYATE----QLLEGSHQKEN--KFLLVITDGHSDgspdGGIEKAVNEADHLGIKIFFVAVGSQNEE 154

                        170       180
                 ....*....|....*....|...
gi 156523168 803 ELQEIASEPTEKHlfYAEDFSTM 825
Cdd:cd01480  155 PLSRIACDGKSAL--YRENFAEL 175
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 657-817 1.74e-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: 1.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 657 DLVFVIDGSKSLGeDNFEIVKQFVTGIIDSLAISPKAARVGLLQYSTLVRT--EFTLRNFSSAKDMKKAVAHMKYMGKGS 734
Cdd:cd01476    2 DLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 735 MTGLALKHMFERsFTQVEGARPlsaRVPRVAIVFTDGRAQDDVSEWASKAQAS-GITMYAVGVG---KAIEEELQEIASe 810
Cdd:cd01476   81 ATGAAIEVALQQ-LDPSEGRRE---GIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGdpgTVDTEELHSITG- 155


                 ....*..
gi 156523168 811 pTEKHLF 817
Cdd:cd01476  156 -NEDHIF 161
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 59-200 4.72e-18

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 83.20  E-value: 4.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  59 DVVFIIDSSRSVNTHD-YAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEvERAVKRMRHLSTG-- 135
Cdd:cd01471    2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNK-DLALNAIRALLSLyy 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156523168 136 ----TMTGLAIQYALNIAFSeaegARPLRENVPRVIMIVTDG---RPQDSVAEvAAKARDTGILIFAIGVGQ 200
Cdd:cd01471   81 pngsTNTTSALLVVEKHLFD----TRGNRENAPQLVIIMTDGipdSKFRTLKE-ARKLRERGVIIAVLGVGQ 147
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 58-218 2.73e-17

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: 80.89  E-value: 2.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  58 ADVVFIIDSSRSVNTHDYAKVKEFIVDILQFL------DIGPDVTRVGLLQYGSTVKNEFSLKTFKR-KSEVERAVKRMR 130
Cdd:cd01480    3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDIRnYTSLKEAVDNLE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 131 HLSTGTMTGLAIQYALNIAFSeaegARPLRENvpRVIMIVTDGRPQDSVA----EVAAKARDTGILIFAIGVGQVDFNTL 206
Cdd:cd01480   83 YIGGGTFTDCALKYATEQLLE----GSHQKEN--KFLLVITDGHSDGSPDggieKAVNEADHLGIKIFFVAVGSQNEEPL 156

                        170
                 ....*....|..
gi 156523168 207 KAIGSEPHEDHV 218
Cdd:cd01480  157 SRIACDGKSALY 168
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 56-209 7.04e-16

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 78.83  E-value: 7.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  56 KRADVVFIIDSSRSVNTHD-YAKVKEFIvdiLQFLDIGPDVTRVGLLQYGSTVKNEFSLkTfkrkSEVERAVKRMRHLST 134
Cdd:COG1240   91 RGRDVVLVVDASGSMAAENrLEAAKGAL---LDFLDDYRPRDRVGLVAFGGEAEVLLPL-T----RDREALKRALDELPP 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 135 GTMT--GLAIQYALNIAfseaegaRPLRENVPRVIMIVTDGRPQDSVA---EVAAKARDTGILIFAIGVG--QVDFNTLK 207
Cdd:COG1240  163 GGGTplGDALALALELL-------KRADPARRKVIVLLTDGRDNAGRIdplEAAELAAAAGIRIYTIGVGteAVDEGLLR 235


                 ..
gi 156523168 208 AI 209
Cdd:COG1240  236 EI 237
Matrilin_ccoil pfam10393
Trimeric coiled-coil oligomerization domain of matrilin; This short domain is a coiled coil ...
 913-955 7.82e-16

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


Pssm-ID: 463070  Cd Length: 43  Bit Score: 72.00  E-value: 7.82e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 156523168  913 EKQDQCKCENLIMFQNLANEEVRKLTQRLEEMTQRMEALENRL 955
Cdd:pfam10393   1 VEEDPCKCEAIVAFQTKVESEIQALTTKLEEVTKRIEALENRL 43
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 655-828 4.81e-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: 4.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 655 PVDLVFVIDGSKS-LGEDNFEIVKQFVTGIIDSLaisPKAARVGLLQYSTLVRT--EFTlrnfSSAKDMKKAVAHMKYMG 731
Cdd:COG1240   92 GRDVVLVVDASGSmAAENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVllPLT----RDREALKRALDELPPGG 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 732 KGSMtGLALKHMFERsftqvegARPLSARVPRVAIVFTDGRA---QDDVSEWASKAQASGITMYAVGVGKAI--EEELQE 806
Cdd:COG1240  165 GTPL-GDALALALEL-------LKRADPARRKVIVLLTDGRDnagRIDPLEAAELAAAAGIRIYTIGVGTEAvdEGLLRE 236

                        170       180
                 ....*....|....*....|..
gi 156523168 807 IASEpTEKHLFYAEDFSTMGEI 828
Cdd:COG1240  237 IAEA-TGGRYFRADDLSELAAI 257
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 656-803 1.56e-14

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 72.80  E-value: 1.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 656 VDLVFVIDGSKSLGEDN-FEIVKQFVTGIIDSLAISPKAARVGLLQYSTLVRTEFTLR-NFSSAKDMKKAVAH---MKYM 730
Cdd:cd01471    1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSsPNSTNKDLALNAIRallSLYY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 731 GKGSM-TGLAL----KHMFErsftqVEGARPlsaRVPRVAIVFTDG---RAQDDVSEwASKAQASGITMYAVGVGKAIEE 802
Cdd:cd01471   81 PNGSTnTTSALlvveKHLFD-----TRGNRE---NAPQLVIIMTDGipdSKFRTLKE-ARKLRERGVIIAVLGVGQGVNH 151


                 .
gi 156523168 803 E 803
Cdd:cd01471  152 E 152
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 661-830 8.36e-14

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: 71.16  E-value: 8.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 661 VIDGSKSLGEDNFEIVKQFVTGIIDSLA---ISPkaaRVGLLQYSTLVRTEFTLRNFSS--AKDMKKAVAHMKYMGKGSM 735
Cdd:cd01470    6 ALDASDSIGEEDFDEAKNAIKTLIEKISsyeVSP---RYEIISYASDPKEIVSIRDFNSndADDVIKRLEDFNYDDHGDK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 736 TG----LALKHMFERsfTQVEGARPLSA--RVPRVAIVFTDGRAQ---------DDVSEWASKAQASGIT------MYAV 794
Cdd:cd01470   83 TGtntaAALKKVYER--MALEKVRNKEAfnETRHVIILFTDGKSNmggsplptvDKIKNLVYKNNKSDNPredyldVYVF 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 156523168 795 GVGKAI-EEELQEIASE-PTEKHLFYAEDFSTMGEISD 830
Cdd:cd01470  161 GVGDDVnKEELNDLASKkDNERHFFKLKDYEDLQEVFD 198
VWA_2 pfam13519
von Willebrand factor type A domain;
60-170 9.85e-13

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 65.01  E-value: 9.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168   60 VVFIIDSSRSVNTHDYAK-----VKEFIVDILQFLDIgpdvTRVGLLQYGSTVKNEFSLKtfKRKSEVERAVKRMRHLST 134
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPtrleaAKDAVLALLKSLPG----DRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 156523168  135 GTMTGLAIQYALNIAFSEaegarplRENVPRVIMIV 170
Cdd:pfam13519  75 GTNLAAALQLARAALKHR-------RKNQPRRIVLI 103
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 54-209 6.56e-11

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 64.35  E-value: 6.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  54 ENKRADVVFIIDSSRSVNTHDYAKVKEFIVDILQFLdiGPDvTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRhLS 133
Cdd:COG2304   88 ERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQL--RPG-DRVSIVTFAGDARVLLPPTPATDRAKILAAIDRLQ-AG 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 134 TGTMTGLAIQYALNIAfseaegARPLRENVPRVIMIVTDGRP------QDSVAEVAAKARDTGILIFAIGVGQvDFN--T 205
Cdd:COG2304  164 GGTALGAGLELAYELA------RKHFIPGRVNRVILLTDGDAnvgitdPEELLKLAEEAREEGITLTTLGVGS-DYNedL 236


                 ....
gi 156523168 206 LKAI 209
Cdd:COG2304  237 LERL 240
VWA_2 pfam13519
von Willebrand factor type A domain;
658-768 3.07e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 58.07  E-value: 3.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  658 LVFVIDGSKS-----LGEDNFEIVKQFVTGIIDSLAISpkaaRVGLLQYSTLVRTEFTLRnfSSAKDMKKAVAHMKYMGK 732
Cdd:pfam13519   1 LVFVLDTSGSmrngdYGPTRLEAAKDAVLALLKSLPGD----RVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 156523168  733 GSMTGLALKHMFERSFTQvegarplSARVPRVAIVF 768
Cdd:pfam13519  75 GTNLAAALQLARAALKHR-------RKNQPRRIVLI 103
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 654-837 7.01e-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: 59.45  E-value: 7.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 654 GPVDLVFVIDGSKSLGEDNFEIVkQFVTGIIDSLaISPKAaRVGLLQYSTLVRTEFTLRNFSSA-----KDMKKAV-AHM 727
Cdd:cd01474    3 GHFDLYFVLDKSGSVAANWIEIY-DFVEQLVDRF-NSPGL-RFSFITFSTRATKILPLTDDSSAiikglEVLKKVTpSGQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 728 KYMGKGsmtglaLKHMFERSFTQVEGARplsaRVPRVAIVFTDGRAQDDV----SEWASKAQASGITMYAVGVGKAIEEE 803
Cdd:cd01474   80 TYIHEG------LENANEQIFNRNGGGR----ETVSVIIALTDGQLLLNGhkypEHEAKLSRKLGAIVYCVGVTDFLKSQ 149

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 156523168 804 LQEIASEPteKHLFYAED-FSTMGEISDKLQKGIC 837
Cdd:cd01474  150 LINIADSK--EYVFPVTSgFQALSGIIESVVKKAC 182
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
56-230 1.62e-09

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 58.40  E-value: 1.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  56 KRADVVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVT---RVGLLQYGSTVKNEFSLktfkrkSEVERAVkrMRHL 132
Cdd:COG4245    4 RRLPVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYALetvEVSVITFDGEAKVLLPL------TDLEDFQ--PPDL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 133 ST--GTMTGLAIQYALNI-----AFSEAEGARPLRenvpRVIMIVTDGRPQDSVAEVAAKA-----RDTGILIFAIGVGQ 200
Cdd:COG4245   76 SAsgGTPLGAALELLLDLierrvQKYTAEGKGDWR----PVVFLITDGEPTDSDWEAALQRlkdgeAAKKANIFAIGVGP 151

                        170       180       190
                 ....*....|....*....|....*....|.
gi 156523168 201 -VDFNTLKAIGSephEDHVFLVANFSQIETL 230
Cdd:COG4245  152 dADTEVLKQLTD---PVRALDALDGLDFREF 179
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 655-808 6.56e-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: 58.19  E-value: 6.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 655 PVDLVFVIDGSKSLGEDNFEIVKQFVTGIIDSLaisPKAARVGLLQYSTLVRTEFTLRNFSSAKDMKKAVAHMK-----Y 729
Cdd:COG2304   91 PLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQL---RPGDRVSIVTFAGDARVLLPPTPATDRAKILAAIDRLQagggtA 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 730 MGKGSMTGLALkhmFERSFTqvegarplSARVPRVaIVFTDGRA------QDDVSEWASKAQASGITMYAVGVGKAI-EE 802
Cdd:COG2304  168 LGAGLELAYEL---ARKHFI--------PGRVNRV-ILLTDGDAnvgitdPEELLKLAEEAREEGITLTTLGVGSDYnED 235


                 ....*.
gi 156523168 803 ELQEIA 808
Cdd:COG2304  236 LLERLA 241
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 408-443 2.86e-08

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


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 50.32  E-value: 2.86e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  408 CALNKPGCEHECINTEEGYYCRCRRGYTLDPNGKTC 443
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 657-837 4.08e-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: 54.25  E-value: 4.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 657 DLVFVIDGSKSLGEDNFEI-VKQFVTGIIDSLAISPKAARVGLLQYSTLVRTEFTLRNFSSAKD---MKKAVAHMKYMGK 732
Cdd:cd01473    2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERYDKnelLKKINDLKNSYRS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 733 GSMTGL--ALKHMFErSFTQVEGARplsARVPRVAIVFTDG----RAQDDVSEWASKAQASGITMYAVGVGKAIEEELQE 806
Cdd:cd01473   82 GGETYIveALKYGLK-NYTKHGNRR---KDAPKVTMLFTDGndtsASKKELQDISLLYKEENVKLLVVGVGAASENKLKL 157

                        170       180       190
                 ....*....|....*....|....*....|....
gi 156523168 807 IA--SEPTEKHLF-YAEDFSTMGEISDKLQKGIC 837
Cdd:cd01473  158 LAgcDINNDNCPNvIKTEWNNLNGISKFLTDKIC 191
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 326-361 7.19e-08

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


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 49.16  E-value: 7.19e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  326 CASENHGCEHECVNADGSYLCRCPKGFALNPDKKTC 361
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 367-402 1.12e-07

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


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 48.78  E-value: 1.12e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  367 CASPNHGCQHECVNTDDSYACRCLKGFTLNPDQKTC 402
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 563-605 3.16e-07

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 52.39  E-value: 3.16e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 156523168 563 GKTCRRKDVCQAVDHGCEHACVSTGESYVCKCMEGFRLAEDGK 605
Cdd:cd01475  181 GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 244-279 3.41e-07

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


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 47.24  E-value: 3.41e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  244 CSILEHNCAHFCINTPGSYVCRCKQGYILNSDEKTC 279
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 531-566 3.73e-07

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


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 47.24  E-value: 3.73e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  531 CALGKHGCEHLCISSGDSFVCRCFEGYILRGDGKTC 566
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 59-239 4.73e-07

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 51.16  E-value: 4.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  59 DVVFIIDSSRSVNthDYAKVKEFI---VDILQFLDIGPDVTRVGLLQYGSTVK--NEFSLKTFKRKSE-VERAVKRMRHL 132
Cdd:cd01473    2 DLTLILDESASIG--YSNWRKDVIpftEKIINNLNISKDKVHVGILLFAEKNRdvVPFSDEERYDKNElLKKINDLKNSY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 133 STGTMTGL--AIQYAL-NIAFSEAEgarplRENVPRVIMIVTDGRPQDS----VAEVAAKARDTGILIFAIGVGQVDFNT 205
Cdd:cd01473   80 RSGGETYIveALKYGLkNYTKHGNR-----RKDAPKVTMLFTDGNDTSAskkeLQDISLLYKEENVKLLVVGVGAASENK 154

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 156523168 206 LKAIG--SEPHEDHVFLV-ANFSQIETLTSVFQKKLC 239
Cdd:cd01473  155 LKLLAgcDINNDNCPNVIkTEWNNLNGISKFLTDKIC 191
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 580-646 6.09e-07

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 51.23  E-value: 6.09e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156523168 580 EHacVSTGESYvcKCMEGFRLAEDGKRCRRKDVCKSTHHGCEHICVNRGNSYICKCSKGFILAEDGR 646
Cdd:cd01475  161 DH--VFYVEDF--STIEELTKKFQGKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 522-565 1.70e-06

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 50.08  E-value: 1.70e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 156523168 522 GKTCAKLDACALGKHGCEHLCISSGDSFVCRCFEGYILRGDGKT 565
Cdd:cd01475  181 GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 656-821 1.71e-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: 49.25  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 656 VDLVFVIDGSKSLG------EDNFEIVKQFVTGIIDSLaispKAARVGLLQYS--TLVRTEFT-----LRNFssAKDMKK 722
Cdd:cd01467    3 RDIMIALDVSGSMLaqdfvkPSRLEAAKEVLSDFIDRR----ENDRIGLVVFAgaAFTQAPLTldresLKEL--LEDIKI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 723 AVAhmkymGKGSMTG----LALKHmfersFTQVEGarplsarVPRVAIVFTDG-RAQDDVSEWASK--AQASGITMYAVG 795
Cdd:cd01467   77 GLA-----GQGTAIGdaigLAIKR-----LKNSEA-------KERVIVLLTDGeNNAGEIDPATAAelAKNKGVRIYTIG 139

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 156523168 796 VGKA------------IEEELQEIASEpTEKHLFYAED 821
Cdd:cd01467  140 VGKSgsgpkpdgstilDEDSLVEIADK-TGGRIFRALD 176
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 490-525 2.86e-06

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


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 44.54  E-value: 2.86e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  490 CLLSRHGCEYSCVNTDRSFVCECPEGHVLRSDGKTC 525
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 613-648 3.92e-06

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


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 44.16  E-value: 3.92e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  613 CKSTHHGCEHICVNRGNSYICKCSKGFILAEDGRRC 648
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 572-607 4.16e-06

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


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 44.16  E-value: 4.16e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  572 CQAVDHGCEHACVSTGESYVCKCMEGFRLAEDGKRC 607
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 449-484 5.37e-06

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


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 43.77  E-value: 5.37e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  449 CAEQDHGCEQLCLNTEDSFVCQCSEGFLINDDLKTC 484
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 55-240 7.17e-06

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 49.96  E-value: 7.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  55 NKRADVVFIIDSSRSVNTHDY-AKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEvERAVKRMRHL- 132
Cdd:PTZ00441  40 NEEVDLYLLVDGSGSIGYHNWiTHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASKDK-EQALIIVKSLr 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 133 STGTMTGlaiQYALNIAFSEAE---GARPLRENVPRVIMIVTDGRP---QDSVaEVAAKARDTGILIFAIGVGQ---VDF 203
Cdd:PTZ00441 119 KTYLPYG---KTNMTDALLEVRkhlNDRVNRENAIQLVILMTDGIPnskYRAL-EESRKLKDRNVKLAVIGIGQginHQF 194

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 156523168 204 NTLKAiGSEPHED--HVFLVANFSQIETLTSVFQKKLCT 240
Cdd:PTZ00441 195 NRLLA-GCRPREGkcKFYSDADWEEAKNLIKPFIAKVCT 232
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 285-320 1.14e-05

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


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 43.00  E-value: 1.14e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 156523168  285 CAADDHGCEQLCVNLLGSFVCQCYSGYALAVDGKRC 320
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 58-240 1.42e-05

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


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 46.73  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  58 ADVVFIIDSSRSVNtHDYAKVKEFIVDIL-QFLDIGpdvTRVGLLQYGSTVKNEFSLKTFKrkSEVERAVKRMRHLSTGT 136
Cdd:cd01474    5 FDLYFVLDKSGSVA-ANWIEIYDFVEQLVdRFNSPG---LRFSFITFSTRATKILPLTDDS--SAIIKGLEVLKKVTPSG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 137 MTglAIQYALNIA----FSEAEGARplRENvpRVIMIVTDGR----PQDSVAEVAAKARDTGILIFAIGVgqVDFNTLKA 208
Cdd:cd01474   79 QT--YIHEGLENAneqiFNRNGGGR--ETV--SVIIALTDGQlllnGHKYPEHEAKLSRKLGAIVYCVGV--TDFLKSQL 150

                        170       180       190
                 ....*....|....*....|....*....|...
gi 156523168 209 IGSEPHEDHVFLV-ANFSQIETLTSVFQKKLCT 240
Cdd:cd01474  151 INIADSKEYVFPVtSGFQALSGIIESVVKKACI 183
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 58-204 1.27e-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: 43.42  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  58 ADVVFIIDSSRSVNTHDYAKVKE---FIVDILQFLDigpdvtRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRmrhLST 134
Cdd:cd01465    1 LNLVFVIDRSGSMDGPKLPLVKSalkLLVDQLRPDD------RLAIVTYDGAAETVLPATPVRDKAAILAAIDR---LTA 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156523168 135 GTMTGLA--IQYALNIAfseAEGARPLRENvpRVIMIvTDGRPQ------DSVAEVAAKARDTGILIFAIGVGQvDFN 204
Cdd:cd01465   72 GGSTAGGagIQLGYQEA---QKHFVPGGVN--RILLA-TDGDFNvgetdpDELARLVAQKRESGITLSTLGFGD-NYN 142
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 646-809 1.30e-03

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: 40.87  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 646 RRCKRCTEGP-VDLVFVIDGSKSLGEDNFEIVKQFVTGIIDSLAI------SPKAARVGLLQYSTLVRTEFTLRNFSSAK 718
Cdd:cd01477    9 RECGSDIKNLwLDIVFVVDNSKGMTQGGLWQVRATISSLFGSSSQigtdydDPRSTRVGLVTYNSNATVVADLNDLQSFD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168 719 DMKKAV---------AHMKYMGKGSmtgLALKHMFErsftqvEGARPLSARVPRVAIVFT---DGRAQDDVSEWASKAQA 786
Cdd:cd01477   89 DLYSQIqgsltdvssTNASYLDTGL---QAAEQMLA------AGKRTSRENYKKVVIVFAsdyNDEGSNDPRPIAARLKS 159

                        170       180
                 ....*....|....*....|....*..
gi 156523168 787 SGITMYAVGVGKAIEEELQ----EIAS 809
Cdd:cd01477  160 TGIAIITVAFTQDESSNLLdklgKIAS 186
EGF_CA smart00179
Calcium-binding EGF-like domain;
405-443 1.83e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.84  E-value: 1.83e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 156523168   405 INYCALNKPgCEH--ECINTEEGYYCRCRRGYTldpNGKTC 443
Cdd:smart00179   2 IDECASGNP-CQNggTCVNTVGSYRCECPPGYT---DGRNC 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
364-402 2.12e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.84  E-value: 2.12e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 156523168   364 IDYCASPnHGCQH--ECVNTDDSYACRCLKGFTlnpDQKTC 402
Cdd:smart00179   2 IDECASG-NPCQNggTCVNTVGSYRCECPPGYT---DGRNC 38
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
 244-273 2.49e-03

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 36.42  E-value: 2.49e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 156523168  244 CSILEHNCAH--FCINTPGSYVCRCKQGYILN 273
Cdd:pfam12947   1 CSDNNGGCHPnaTCTNTGGSFTCTCNDGYTGD 32
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 405-443 3.44e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 36.08  E-value: 3.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 156523168 405 INYCALNKP-GCEHECINTEEGYYCRCRRGYTldpnGKTC 443
Cdd:cd00054    2 IDECASGNPcQNGGTCVNTVGSYRCSCPPGYT----GRNC 37
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 59-212 5.03e-03

vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- two heavy chains and one light chain (bikunin). Bikunin confers the protease-inhibitor function while the heavy chains are involved in rendering stability to the extracellular matrix by binding to hyaluronic acid. The heavy chains carry the VWA domain with a conserved MIDAS motif. Although the exact role of the VWA domains remains unknown, it has been speculated to be involved in mediating protein-protein interactions with the components of the extracellular matrix.


Pssm-ID: 238738 [Multi-domain]  Cd Length: 171  Bit Score: 38.74  E-value: 5.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523168  59 DVVFIIDSSRSVNTHDYAKVKEFIVDILQflDIGPDvTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLStgTMT 138
Cdd:cd01461    4 EVVFVIDTSGSMSGTKIEQTKEALLTALK--DLPPG-DYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQ--ALG 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156523168 139 GLAIQYALNIAFSEAEGARplreNVPRVIMIVTDGRPQD--SVAEVAAKARDTGILIFAIGVGQ-VDFNTLKAIGSE 212
Cdd:cd01461   79 GTNMNDALEAALELLNSSP----GSVPQIILLTDGEVTNesQILKNVREALSGRIRLFTFGIGSdVNTYLLERLARE 151
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 364-395 6.60e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 35.31  E-value: 6.60e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 156523168 364 IDYCASPNhGCQH--ECVNTDDSYACRCLKGFTL 395
Cdd:cd00054    2 IDECASGN-PCQNggTCVNTVGSYRCSCPPGYTG 34
EGF_CA smart00179
Calcium-binding EGF-like domain;
287-321 7.18e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 35.30  E-value: 7.18e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 156523168   287 ADDHGCEQ--LCVNLLGSFVCQCYSGYalaVDGKRCE 321
Cdd:smart00179   6 ASGNPCQNggTCVNTVGSYRCECPPGY---TDGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
249-279 8.32e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 34.92  E-value: 8.32e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 156523168   249 HNCAH--FCINTPGSYVCRCKQGYilnSDEKTC 279
Cdd:smart00179   9 NPCQNggTCVNTVGSYRCECPPGY---TDGRNC 38
 
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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