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Conserved domains on  [gi|338817988|sp|O00339|]
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RecName: Full=Matrilin-2; Flags: Precursor

Protein Classification

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 ...
 54-276 1.15e-133

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: 400.22  E-value: 1.15e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  54 KRADLVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTG 133
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 134 TMTGLAIQYALNIAFSEAEGARPLRENVPRVIMIVTDGRPQDSVAEVAAKARDTGILIFAIGVGQVDFNTLKSIGSEPHE 213
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817988 214 DHVFLVANFSQIETLTSVFQKKLC-TAHMCSTLEHNCAHFCINIPGSYVCRCKQGYILNSDQTT 276
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICvVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 652-892 5.46e-125

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: 377.88  E-value: 5.46e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 652 GPIDLVFVIDGSKSLGEENFEVVKQFVTGIIDSLTISPKAARVGLLQYSTQVHTEFTLRNFNSAKDMKKAVAHMKYMGKG 731
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 732 SMTGLALKHMFERSFTQGEGARPLSTRVPRAAIVFTDGRAQDDVSEWASKAKANGITMYAVGVGKAIEEELQEIASEPTN 811
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 812 KHLFYAEDFSTMDEISEKLKKGICEaledsdgrQDSPAGELPKTVQQPTESEPVTIniqdllscsNFAVQHRYLFEEDNL 891
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICV--------VPDLCATLSHVCQQVCISTPGSY---------LCACTEGYALLEDNK 223


                 .
gi 338817988 892 L 892
Cdd:cd01475  224 T 224
Matrilin_ccoil pfam10393
Trimeric coiled-coil oligomerization domain of matrilin; This short domain is a coiled coil ...
 911-953 6.55e-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: 72.38  E-value: 6.55e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 338817988  911 EKHDQCKCENLIMFQNLANEEVRKLTQRLEEMTQRMEALENRL 953
Cdd:pfam10393   1 VEEDPCKCEAIVAFQTKVESEIQALTTKLEEVTKRIEALENRL 43
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 365-400 1.21e-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: 51.47  E-value: 1.21e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  365 CASSNHGCQHECVNTDDSYSCHCLKGFTLNPDKKTC 400
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 438-481 5.76e-08

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: 54.31  E-value: 5.76e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 338817988 438 GKTCSRVDHCAQQDHGCEQLCLNTEDSFVCQCSEGFLINEDLKT 481
Cdd:cd01475  181 GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 520-563 9.51e-08

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: 53.93  E-value: 9.51e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 338817988 520 GKTCAKLDSCALGDHGCEHSCVSSEDSFVCQCFEGYILREDGKT 563
Cdd:cd01475  181 GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 324-359 1.19e-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: 48.39  E-value: 1.19e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  324 CASENHGCEHECVNADGSYLCQCHEGFALNPDKKTC 359
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 561-603 2.25e-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: 52.77  E-value: 2.25e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 338817988 561 GKTCRRKDVCQAIDHGCEHICVNSDDSYTCECLEGFRLAEDGK 603
Cdd:cd01475  181 GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 602-644 3.72e-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: 52.00  E-value: 3.72e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 338817988 602 GKRCRRKDVCKSTHHGCEHICVNNGNSYICKCSEGFVLAEDGR 644
Cdd:cd01475  181 GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 406-441 7.68e-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: 46.47  E-value: 7.68e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  406 CALNKPGCEHECVNMEESYYCRCHRGYTLDPNGKTC 441
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 283-318 2.19e-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: 44.93  E-value: 2.19e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  283 CAMEDHNCEQLCVNVPGSFVCQCYSGYALAEDGKRC 318
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 488-523 8.20e-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: 40.69  E-value: 8.20e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  488 CLLSDHGCEYSCVNMDRSFACQCPEGHVLRSDGKTC 523
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 ...
 54-276 1.15e-133

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: 400.22  E-value: 1.15e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  54 KRADLVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTG 133
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 134 TMTGLAIQYALNIAFSEAEGARPLRENVPRVIMIVTDGRPQDSVAEVAAKARDTGILIFAIGVGQVDFNTLKSIGSEPHE 213
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817988 214 DHVFLVANFSQIETLTSVFQKKLC-TAHMCSTLEHNCAHFCINIPGSYVCRCKQGYILNSDQTT 276
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICvVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 652-892 5.46e-125

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: 377.88  E-value: 5.46e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 652 GPIDLVFVIDGSKSLGEENFEVVKQFVTGIIDSLTISPKAARVGLLQYSTQVHTEFTLRNFNSAKDMKKAVAHMKYMGKG 731
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 732 SMTGLALKHMFERSFTQGEGARPLSTRVPRAAIVFTDGRAQDDVSEWASKAKANGITMYAVGVGKAIEEELQEIASEPTN 811
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 812 KHLFYAEDFSTMDEISEKLKKGICEaledsdgrQDSPAGELPKTVQQPTESEPVTIniqdllscsNFAVQHRYLFEEDNL 891
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICV--------VPDLCATLSHVCQQVCISTPGSY---------LCACTEGYALLEDNK 223


                 .
gi 338817988 892 L 892
Cdd:cd01475  224 T 224
VWA pfam00092
von Willebrand factor type A domain;
57-230 1.35e-60

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 204.05  E-value: 1.35e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988   57 DLVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTGTM- 135
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  136 TGLAIQYALNIAFSEAEGARPlreNVPRVIMIVTDGRPQD-SVAEVAAKARDTGILIFAIGVGQVDFNTLKSIGSEPHED 214
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARP---GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                         170
                  ....*....|....*.
gi 338817988  215 HVFLVANFSQIETLTS 230
Cdd:pfam00092 158 HVFTVSDFEALEDLQD 173
VWA pfam00092
von Willebrand factor type A domain;
655-829 5.28e-60

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 202.12  E-value: 5.28e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  655 DLVFVIDGSKSLGEENFEVVKQFVTGIIDSLTISPKAARVGLLQYSTQVHTEFTLRNFNSAKDMKKAVAHMKYMGKGSM- 733
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  734 TGLALKHMFERSFTQGEGARPlstRVPRAAIVFTDGRAQD-DVSEWASKAKANGITMYAVGVGKAIEEELQEIASEPTNK 812
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARP---GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                         170
                  ....*....|....*..
gi 338817988  813 HLFYAEDFSTMDEISEK 829
Cdd:pfam00092 158 HVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 655-827 1.12e-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: 1.12e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988   655 DLVFVIDGSKSLGEENFEVVKQFVTGIIDSLTISPKAARVGLLQYSTQVHTEFTLRNFNSAKDMKKAVAHMKY-MGKGSM 733
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988   734 TGLALKHMFERSFTQGEGARPlstRVPRAAIVFTDGRAQD---DVSEWASKAKANGITMYAVGVGKAI-EEELQEIASEP 809
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRR---GAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVdEEELKKLASAP 157

                          170
                   ....*....|....*...
gi 338817988   810 TNKHLFYAEDFSTMDEIS 827
Cdd:smart00327 158 GGVYVFLPELLDLLIDLL 175
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 57-228 2.71e-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: 2.71e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988    57 DLVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMR-HLSTGTM 135
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988   136 TGLAIQYALNIAFSEAEGARPlreNVPRVIMIVTDGRPQDS---VAEVAAKARDTGILIFAIGVGQ-VDFNTLKSIGSEP 211
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRR---GAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNdVDEEELKKLASAP 157

                          170
                   ....*....|....*..
gi 338817988   212 HEDHVFLVANFSQIETL 228
Cdd:smart00327 158 GGVYVFLPELLDLLIDL 174
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 653-826 1.73e-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: 80.37  E-value: 1.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 653 PIDLVFVIDGSKSLGEEN-FEVVKQFVTGIIDSLtisPKAARVGLLQYSTQVHT--EFTlrnfNSAKDMKKAVAHMKYMG 729
Cdd:COG1240   92 GRDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVllPLT----RDREALKRALDELPPGG 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 730 KGSMtGLALKHMFERsftqgegARPLSTRVPRAAIVFTDGRA---QDDVSEWASKAKANGITMYAVGVGKAI--EEELQE 804
Cdd:COG1240  165 GTPL-GDALALALEL-------LKRADPARRKVIVLLTDGRDnagRIDPLEAAELAAAAGIRIYTIGVGTEAvdEGLLRE 236

                        170       180
                 ....*....|....*....|..
gi 338817988 805 IASEpTNKHLFYAEDFSTMDEI 826
Cdd:COG1240  237 IAEA-TGGRYFRADDLSELAAI 257
Matrilin_ccoil pfam10393
Trimeric coiled-coil oligomerization domain of matrilin; This short domain is a coiled coil ...
 911-953 6.55e-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: 72.38  E-value: 6.55e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 338817988  911 EKHDQCKCENLIMFQNLANEEVRKLTQRLEEMTQRMEALENRL 953
Cdd:pfam10393   1 VEEDPCKCEAIVAFQTKVESEIQALTTKLEEVTKRIEALENRL 43
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 54-207 2.05e-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: 77.29  E-value: 2.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  54 KRADLVFIIDSSRSVNTHD-YAKVKEFIvdiLQFLDIGPDVTRVGLLQYGSTVKNEFSLkTfkrkSEVERAVKRMRHLST 132
Cdd:COG1240   91 RGRDVVLVVDASGSMAAENrLEAAKGAL---LDFLDDYRPRDRVGLVAFGGEAEVLLPL-T----RDREALKRALDELPP 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 133 GTMT--GLAIQYALNIAfseaegaRPLRENVPRVIMIVTDGRPQDSVA---EVAAKARDTGILIFAIGVG--QVDFNTLK 205
Cdd:COG1240  163 GGGTplGDALALALELL-------KRADPARRKVIVLLTDGRDNAGRIdplEAAELAAAAGIRIYTIGVGteAVDEGLLR 235


                 ..
gi 338817988 206 SI 207
Cdd:COG1240  236 EI 237
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 365-400 1.21e-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: 51.47  E-value: 1.21e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  365 CASSNHGCQHECVNTDDSYSCHCLKGFTLNPDKKTC 400
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 438-481 5.76e-08

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: 54.31  E-value: 5.76e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 338817988 438 GKTCSRVDHCAQQDHGCEQLCLNTEDSFVCQCSEGFLINEDLKT 481
Cdd:cd01475  181 GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 520-563 9.51e-08

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: 53.93  E-value: 9.51e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 338817988 520 GKTCAKLDSCALGDHGCEHSCVSSEDSFVCQCFEGYILREDGKT 563
Cdd:cd01475  181 GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 324-359 1.19e-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: 48.39  E-value: 1.19e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  324 CASENHGCEHECVNADGSYLCQCHEGFALNPDKKTC 359
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 561-603 2.25e-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: 52.77  E-value: 2.25e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 338817988 561 GKTCRRKDVCQAIDHGCEHICVNSDDSYTCECLEGFRLAEDGK 603
Cdd:cd01475  181 GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 602-644 3.72e-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: 52.00  E-value: 3.72e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 338817988 602 GKRCRRKDVCKSTHHGCEHICVNNGNSYICKCSEGFVLAEDGR 644
Cdd:cd01475  181 GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 570-605 3.79e-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: 3.79e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  570 CQAIDHGCEHICVNSDDSYTCECLEGFRLAEDGKRC 605
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 406-441 7.68e-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: 46.47  E-value: 7.68e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  406 CALNKPGCEHECVNMEESYYCRCHRGYTLDPNGKTC 441
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 611-646 7.99e-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: 46.08  E-value: 7.99e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  611 CKSTHHGCEHICVNNGNSYICKCSEGFVLAEDGRRC 646
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 283-318 2.19e-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: 44.93  E-value: 2.19e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  283 CAMEDHNCEQLCVNVPGSFVCQCYSGYALAEDGKRC 318
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 48-238 3.42e-06

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 50.73  E-value: 3.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  48 ESSCeNKRADLVFIIDSSRSVNTHDY-AKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEvERAVKR 126
Cdd:PTZ00441  36 EEVC-NEEVDLYLLVDGSGSIGYHNWiTHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASKDK-EQALII 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 127 MRHL-STGTMTGlaiQYALNIAFSEAE---GARPLRENVPRVIMIVTDGRP---QDSVaEVAAKARDTGILIFAIGVGQ- 198
Cdd:PTZ00441 114 VKSLrKTYLPYG---KTNMTDALLEVRkhlNDRVNRENAIQLVILMTDGIPnskYRAL-EESRKLKDRNVKLAVIGIGQg 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 338817988 199 --VDFNTLkSIGSEPHED--HVFLVANFSQIETLTSVFQKKLCT 238
Cdd:PTZ00441 190 inHQFNRL-LAGCRPREGkcKFYSDADWEEAKNLIKPFIAKVCT 232
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 529-564 4.67e-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: 4.67e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  529 CALGDHGCEHSCVSSEDSFVCQCFEGYILREDGKTC 564
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 447-482 9.65e-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: 43.00  E-value: 9.65e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  447 CAQQDHGCEQLCLNTEDSFVCQCSEGFLINEDLKTC 482
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 488-523 8.20e-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: 40.69  E-value: 8.20e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  488 CLLSDHGCEYSCVNMDRSFACQCPEGHVLRSDGKTC 523
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
362-400 4.08e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.77  E-value: 4.08e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 338817988   362 IDYCASsNHGCQH--ECVNTDDSYSCHCLKGFTlnpDKKTC 400
Cdd:smart00179   2 IDECAS-GNPCQNggTCVNTVGSYRCECPPGYT---DGRNC 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 362-393 1.43e-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: 37.23  E-value: 1.43e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 338817988 362 IDYCASsNHGCQH--ECVNTDDSYSCHCLKGFTL 393
Cdd:cd00054    2 IDECAS-GNPCQNggTCVNTVGSYRCSCPPGYTG 34
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 480-522 6.33e-03

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: 39.29  E-value: 6.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 338817988 480 KTCSRVDYCLLSDHGCEYSCVNMDRSFACQCPEGHVLRSDGKT 522
Cdd:cd01475  182 KICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
EGF_CA smart00179
Calcium-binding EGF-like domain;
281-319 7.68e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 34.92  E-value: 7.68e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 338817988   281 DLCAmEDHNCEQ--LCVNVPGSFVCQCYSGYalaEDGKRCV 319
Cdd:smart00179   3 DECA-SGNPCQNggTCVNTVGSYRCECPPGY---TDGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
403-441 8.73e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 34.92  E-value: 8.73e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 338817988   403 INYCALNKPgCEH--ECVNMEESYYCRCHRGYTldpNGKTC 441
Cdd:smart00179   2 IDECASGNP-CQNggTCVNTVGSYRCECPPGYT---DGRNC 38
 
Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 54-276 1.15e-133

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: 400.22  E-value: 1.15e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  54 KRADLVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTG 133
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 134 TMTGLAIQYALNIAFSEAEGARPLRENVPRVIMIVTDGRPQDSVAEVAAKARDTGILIFAIGVGQVDFNTLKSIGSEPHE 213
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817988 214 DHVFLVANFSQIETLTSVFQKKLC-TAHMCSTLEHNCAHFCINIPGSYVCRCKQGYILNSDQTT 276
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICvVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 652-892 5.46e-125

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: 377.88  E-value: 5.46e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 652 GPIDLVFVIDGSKSLGEENFEVVKQFVTGIIDSLTISPKAARVGLLQYSTQVHTEFTLRNFNSAKDMKKAVAHMKYMGKG 731
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 732 SMTGLALKHMFERSFTQGEGARPLSTRVPRAAIVFTDGRAQDDVSEWASKAKANGITMYAVGVGKAIEEELQEIASEPTN 811
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 812 KHLFYAEDFSTMDEISEKLKKGICEaledsdgrQDSPAGELPKTVQQPTESEPVTIniqdllscsNFAVQHRYLFEEDNL 891
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICV--------VPDLCATLSHVCQQVCISTPGSY---------LCACTEGYALLEDNK 223


                 .
gi 338817988 892 L 892
Cdd:cd01475  224 T 224
VWA pfam00092
von Willebrand factor type A domain;
57-230 1.35e-60

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 204.05  E-value: 1.35e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988   57 DLVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTGTM- 135
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  136 TGLAIQYALNIAFSEAEGARPlreNVPRVIMIVTDGRPQD-SVAEVAAKARDTGILIFAIGVGQVDFNTLKSIGSEPHED 214
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARP---GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                         170
                  ....*....|....*.
gi 338817988  215 HVFLVANFSQIETLTS 230
Cdd:pfam00092 158 HVFTVSDFEALEDLQD 173
VWA pfam00092
von Willebrand factor type A domain;
655-829 5.28e-60

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 202.12  E-value: 5.28e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  655 DLVFVIDGSKSLGEENFEVVKQFVTGIIDSLTISPKAARVGLLQYSTQVHTEFTLRNFNSAKDMKKAVAHMKYMGKGSM- 733
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  734 TGLALKHMFERSFTQGEGARPlstRVPRAAIVFTDGRAQD-DVSEWASKAKANGITMYAVGVGKAIEEELQEIASEPTNK 812
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARP---GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                         170
                  ....*....|....*..
gi 338817988  813 HLFYAEDFSTMDEISEK 829
Cdd:pfam00092 158 HVFTVSDFEALEDLQDQ 174
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 655-820 8.63e-57

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: 192.89  E-value: 8.63e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 655 DLVFVIDGSKSLGEENFEVVKQFVTGIIDSLTISPKAARVGLLQYSTQVHTEFTLRNFNSAKDMKKAVAHMKYMGKGSMT 734
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 735 GLALKHMFERSFTQGEGARPlstRVPRAAIVFTDGRAQDDVSEWASKAKANGITMYAVGVGKAIEEELQEIASEPTNKHL 814
Cdd:cd01482   82 GKALTHVREKNFTPDAGARP---GVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHV 158


                 ....*.
gi 338817988 815 FYAEDF 820
Cdd:cd01482  159 FNVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 654-820 2.41e-55

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: 188.98  E-value: 2.41e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 654 IDLVFVIDGSKSLGEENFEVVKQFVTGIIDSLTISPKAARVGLLQYSTQVHTEFTLRNFNSAKDMKKAVAHMKYMGKGSM 733
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 734 TGLALKHMFERSFTQGEGARPlstRVPRAAIVFTDGRAQDDVSEWASKAKANGITMYAVGVGKAIEEELQEIASEPTNKH 813
Cdd:cd01472   81 TGKALKYVRENLFTEASGSRE---GVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELY 157


                 ....*..
gi 338817988 814 LFYAEDF 820
Cdd:cd01472  158 VFNVADF 164
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 56-217 7.20e-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: 187.50  E-value: 7.20e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  56 ADLVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHL-STGT 134
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLgGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 135 MTGLAIQYALNIAFSEaegaRPLRENVPRVIMIVTDGRPQD--SVAEVAAKARDTGILIFAIGVGQVDFNTLKSIGSEPH 212
Cdd:cd01450   81 NTGKALQYALEQLFSE----SNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156


                 ....*
gi 338817988 213 EDHVF 217
Cdd:cd01450  157 ERHVF 161
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 654-815 1.52e-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: 186.34  E-value: 1.52e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 654 IDLVFVIDGSKSLGEENFEVVKQFVTGIIDSLTISPKAARVGLLQYSTQVHTEFTLRNFNSAKDMKKAVAHMKYM-GKGS 732
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLgGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 733 MTGLALKHMFERSFTQGeGARPlstRVPRAAIVFTDGRAQD--DVSEWASKAKANGITMYAVGVGKAIEEELQEIASEPT 810
Cdd:cd01450   81 NTGKALQYALEQLFSES-NARE---NVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156


                 ....*
gi 338817988 811 NKHLF 815
Cdd:cd01450  157 ERHVF 161
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 56-222 2.54e-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: 180.50  E-value: 2.54e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  56 ADLVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTGTM 135
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 136 TGLAIQYALNIAFSEAEGArplRENVPRVIMIVTDGRPQDSVAEVAAKARDTGILIFAIGVGQVDFNTLKSIGSEPHEDH 215
Cdd:cd01472   81 TGKALKYVRENLFTEASGS---REGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELY 157


                 ....*..
gi 338817988 216 VFLVANF 222
Cdd:cd01472  158 VFNVADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 56-222 6.43e-50

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: 173.63  E-value: 6.43e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  56 ADLVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTGTM 135
Cdd:cd01482    1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 136 TGLAIQYALNIAFSEAEGARPlreNVPRVIMIVTDGRPQDSVAEVAAKARDTGILIFAIGVGQVDFNTLKSIGSEPHEDH 215
Cdd:cd01482   81 TGKALTHVREKNFTPDAGARP---GVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH 157


                 ....*..
gi 338817988 216 VFLVANF 222
Cdd:cd01482  158 VFNVADF 164
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 655-827 1.12e-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: 1.12e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988   655 DLVFVIDGSKSLGEENFEVVKQFVTGIIDSLTISPKAARVGLLQYSTQVHTEFTLRNFNSAKDMKKAVAHMKY-MGKGSM 733
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988   734 TGLALKHMFERSFTQGEGARPlstRVPRAAIVFTDGRAQD---DVSEWASKAKANGITMYAVGVGKAI-EEELQEIASEP 809
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRR---GAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVdEEELKKLASAP 157

                          170
                   ....*....|....*...
gi 338817988   810 TNKHLFYAEDFSTMDEIS 827
Cdd:smart00327 158 GGVYVFLPELLDLLIDLL 175
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 57-228 2.71e-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: 2.71e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988    57 DLVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMR-HLSTGTM 135
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988   136 TGLAIQYALNIAFSEAEGARPlreNVPRVIMIVTDGRPQDS---VAEVAAKARDTGILIFAIGVGQ-VDFNTLKSIGSEP 211
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRR---GAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNdVDEEELKKLASAP 157

                          170
                   ....*....|....*..
gi 338817988   212 HEDHVFLVANFSQIETL 228
Cdd:smart00327 158 GGVYVFLPELLDLLIDL 174
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 57-228 6.12e-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: 145.58  E-value: 6.12e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  57 DLVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTGTMT 136
Cdd:cd01469    2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 137 GLAIQYALNIAFSEAEGARPlreNVPRVIMIVTDGRPQDS--VAEVAAKARDTGILIFAIGVGQVdFNT------LKSIG 208
Cdd:cd01469   82 ATAIQYVVTELFSESNGARK---DATKVLVVITDGESHDDplLKDVIPQAEREGIIRYAIGVGGH-FQRensreeLKTIA 157

                        170       180
                 ....*....|....*....|
gi 338817988 209 SEPHEDHVFLVANFSQIETL 228
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 ...
 56-222 5.19e-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: 139.77  E-value: 5.19e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  56 ADLVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRhLSTGTM 135
Cdd:cd01481    1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLR-LRGGSQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 136 --TGLAIQYALNIAFSEAEGARpLRENVPRVIMIVTDGRPQDSVAEVAAKARDTGILIFAIGVGQVDFNTLKSIGSEPhe 213
Cdd:cd01481   80 lnTGSALDYVVKNLFTKSAGSR-IEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP-- 156


                 ....*....
gi 338817988 214 DHVFLVANF 222
Cdd:cd01481  157 SFVFQVSDF 165
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 654-826 1.41e-36

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: 135.95  E-value: 1.41e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 654 IDLVFVIDGSKSLGEENFEVVKQFVTGIIDSLTISPKAARVGLLQYSTQVHTEFTLRNFNSAKDMKKAVAHMKYMGKGSM 733
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 734 TGLALKHMFERSFTQGEGARPLSTRVpraAIVFTDGRAQDDVSEWA--SKAKANGITMYAVGVGKAIE-----EELQEIA 806
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKV---LVVITDGESHDDPLLKDviPQAEREGIIRYAIGVGGHFQrensrEELKTIA 157

                        170       180
                 ....*....|....*....|
gi 338817988 807 SEPTNKHLFYAEDFSTMDEI 826
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 ...
 655-820 8.44e-34

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: 127.44  E-value: 8.44e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 655 DLVFVIDGSKSLGEENFEVVKQFVTGIIDSLTISPKAARVGLLQYSTQVHTEFTLRNFNSAKDMKKAVAHMKYM-GKGSM 733
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRgGSQLN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 734 TGLALKHMFERSFTQGEGARpLSTRVPRAAIVFTDGRAQDDVSEWASKAKANGITMYAVGVGKAIEEELQEIASEPtnKH 813
Cdd:cd01481   82 TGSALDYVVKNLFTKSAGSR-IEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP--SF 158


                 ....*..
gi 338817988 814 LFYAEDF 820
Cdd:cd01481  159 VFQVSDF 165
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 56-217 1.29e-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: 121.35  E-value: 1.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  56 ADLVFIIDSSRSVNtHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKN--EFSLKTFKRKSEVERAVKRMRHLSTG 133
Cdd:cd01476    1 LDLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 134 TMTGLAIQYALNIaFSEAEGARplrENVPRVIMIVTDGRPQDSVAEVAAKARDT-GILIFAIGVG---QVDFNTLKSIGS 209
Cdd:cd01476   80 TATGAAIEVALQQ-LDPSEGRR---EGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGdpgTVDTEELHSITG 155


                 ....*...
gi 338817988 210 EphEDHVF 217
Cdd:cd01476  156 N--EDHIF 161
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 56-217 7.70e-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: 116.13  E-value: 7.70e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  56 ADLVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRH-LSTGT 134
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 135 MTGLAIQYALNIAFSEAegarplRENVPRVIMIVTDGRPQDS---VAEVAAKARDTGILIFAIGVG-QVDFNTLKSIGSE 210
Cdd:cd00198   81 NIGAALRLALELLKSAK------RPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIGdDANEDELKEIADK 154


                 ....*..
gi 338817988 211 PHEDHVF 217
Cdd:cd00198  155 TTGGAVF 161
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 654-815 1.74e-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: 114.97  E-value: 1.74e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 654 IDLVFVIDGSKSLGEENFEVVKQFVTGIIDSLTISPKAARVGLLQYSTQVHTEFTLRNFNSAKDMKKAVAHMKY-MGKGS 732
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 733 MTGLALKHMFERSFTQGEGARplstrvPRAAIVFTDGRAQDD---VSEWASKAKANGITMYAVGVG-KAIEEELQEIASE 808
Cdd:cd00198   81 NIGAALRLALELLKSAKRPNA------RRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIGdDANEDELKEIADK 154


                 ....*..
gi 338817988 809 PTNKHLF 815
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 ...
 652-825 2.01e-26

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: 107.09  E-value: 2.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 652 GPIDLVFVIDGSKSLGEENFEVVKQFVTGIIDSL------TISPKAARVGLLQYSTQVHTEFT-LRNFNSAKDMKKAVAH 724
Cdd:cd01480    1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGfLRDIRNYTSLKEAVDN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 725 MKYMGKGSMTGLALKhmfersFTQGEGARPLSTRVPRAAIVFTDGRAQ----DDVSEWASKAKANGITMYAVGVGKAIEE 800
Cdd:cd01480   81 LEYIGGGTFTDCALK------YATEQLLEGSHQKENKFLLVITDGHSDgspdGGIEKAVNEADHLGIKIFFVAVGSQNEE 154

                        170       180
                 ....*....|....*....|....*
gi 338817988 801 ELQEIASEPTNKHlfYAEDFSTMDE 825
Cdd:cd01480  155 PLSRIACDGKSAL--YRENFAELLW 177
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 655-815 1.39e-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: 98.24  E-value: 1.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 655 DLVFVIDGSKSLGEEnFEVVKQFVTGIIDSLTISPKAARVGLLQYS--TQVHTEFTLRNFNSAKDMKKAVAHMKYMGKGS 732
Cdd:cd01476    2 DLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 733 MTGLALKHMFERsFTQGEGARPlstRVPRAAIVFTDGRAQDDVSEWASKAKAN-GITMYAVGVG---KAIEEELQEIASE 808
Cdd:cd01476   81 ATGAAIEVALQQ-LDPSEGRRE---GIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGdpgTVDTEELHSITGN 156


                 ....*..
gi 338817988 809 PtnKHLF 815
Cdd:cd01476  157 E--DHIF 161
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 57-198 4.36e-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: 4.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  57 DLVFIIDSSRSVNTHD-YAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEvERAVKRMRHLSTG-- 133
Cdd:cd01471    2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNK-DLALNAIRALLSLyy 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817988 134 ----TMTGLAIQYALNIAFSeaegARPLRENVPRVIMIVTDG---RPQDSVAEvAAKARDTGILIFAIGVGQ 198
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 ...
 56-216 9.58e-18

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: 82.05  E-value: 9.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  56 ADLVFIIDSSRSVNTHDYAKVKEFIVDILQFL------DIGPDVTRVGLLQYGSTVKNEFSLKTFKR-KSEVERAVKRMR 128
Cdd:cd01480    3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDIRnYTSLKEAVDNLE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 129 HLSTGTMTGLAIQYALNIAFSeaegARPLRENvpRVIMIVTDGRPQDSVA----EVAAKARDTGILIFAIGVGQVDFNTL 204
Cdd:cd01480   83 YIGGGTFTDCALKYATEQLLE----GSHQKEN--KFLLVITDGHSDGSPDggieKAVNEADHLGIKIFFVAVGSQNEEPL 156

                        170
                 ....*....|..
gi 338817988 205 KSIGSEPHEDHV 216
Cdd:cd01480  157 SRIACDGKSALY 168
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 653-826 1.73e-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: 80.37  E-value: 1.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 653 PIDLVFVIDGSKSLGEEN-FEVVKQFVTGIIDSLtisPKAARVGLLQYSTQVHT--EFTlrnfNSAKDMKKAVAHMKYMG 729
Cdd:COG1240   92 GRDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVllPLT----RDREALKRALDELPPGG 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 730 KGSMtGLALKHMFERsftqgegARPLSTRVPRAAIVFTDGRA---QDDVSEWASKAKANGITMYAVGVGKAI--EEELQE 804
Cdd:COG1240  165 GTPL-GDALALALEL-------LKRADPARRKVIVLLTDGRDnagRIDPLEAAELAAAAGIRIYTIGVGTEAvdEGLLRE 236

                        170       180
                 ....*....|....*....|..
gi 338817988 805 IASEpTNKHLFYAEDFSTMDEI 826
Cdd:COG1240  237 IAEA-TGGRYFRADDLSELAAI 257
Matrilin_ccoil pfam10393
Trimeric coiled-coil oligomerization domain of matrilin; This short domain is a coiled coil ...
 911-953 6.55e-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: 72.38  E-value: 6.55e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 338817988  911 EKHDQCKCENLIMFQNLANEEVRKLTQRLEEMTQRMEALENRL 953
Cdd:pfam10393   1 VEEDPCKCEAIVAFQTKVESEIQALTTKLEEVTKRIEALENRL 43
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 54-207 2.05e-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: 77.29  E-value: 2.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  54 KRADLVFIIDSSRSVNTHD-YAKVKEFIvdiLQFLDIGPDVTRVGLLQYGSTVKNEFSLkTfkrkSEVERAVKRMRHLST 132
Cdd:COG1240   91 RGRDVVLVVDASGSMAAENrLEAAKGAL---LDFLDDYRPRDRVGLVAFGGEAEVLLPL-T----RDREALKRALDELPP 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 133 GTMT--GLAIQYALNIAfseaegaRPLRENVPRVIMIVTDGRPQDSVA---EVAAKARDTGILIFAIGVG--QVDFNTLK 205
Cdd:COG1240  163 GGGTplGDALALALELL-------KRADPARRKVIVLLTDGRDNAGRIdplEAAELAAAAGIRIYTIGVGteAVDEGLLR 235


                 ..
gi 338817988 206 SI 207
Cdd:COG1240  236 EI 237
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 654-801 2.23e-15

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: 75.50  E-value: 2.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 654 IDLVFVIDGSKSLGEEN-FEVVKQFVTGIIDSLTISPKAARVGLLQYSTQVHTEFTLRNFNSA-KDMKKAVAH---MKYM 728
Cdd:cd01471    1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTnKDLALNAIRallSLYY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 729 GKGSM-TGLAL----KHMFErsftqGEGARPlstRVPRAAIVFTDG---RAQDDVSEwASKAKANGITMYAVGVGKAIEE 800
Cdd:cd01471   81 PNGSTnTTSALlvveKHLFD-----TRGNRE---NAPQLVIIMTDGipdSKFRTLKE-ARKLRERGVIIAVLGVGQGVNH 151


                 .
gi 338817988 801 E 801
Cdd:cd01471  152 E 152
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 659-825 1.99e-13

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: 70.01  E-value: 1.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 659 VIDGSKSLGEENFEVVKQFVTGIID---SLTISPkaaRVGLLQYSTQVHTEFTLRNFNS--AKDMKKAVAHMKYMGKGSM 733
Cdd:cd01470    6 ALDASDSIGEEDFDEAKNAIKTLIEkisSYEVSP---RYEIISYASDPKEIVSIRDFNSndADDVIKRLEDFNYDDHGDK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 734 TG----LALKHMFERSFTQGEGARPLSTRVPRAAIVFTDGRAQ---------DDVSEWASKAKANGIT------MYAVGV 794
Cdd:cd01470   83 TGtntaAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNmggsplptvDKIKNLVYKNNKSDNPredyldVYVFGV 162

                        170       180       190
                 ....*....|....*....|....*....|...
gi 338817988 795 GKAI-EEELQEIASEPTN-KHLFYAEDFSTMDE 825
Cdd:cd01470  163 GDDVnKEELNDLASKKDNeRHFFKLKDYEDLQE 195
VWA_2 pfam13519
von Willebrand factor type A domain;
58-168 1.30e-12

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 64.62  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988   58 LVFIIDSSRSVNTHDYAK-----VKEFIVDILQFLDIgpdvTRVGLLQYGSTVKNEFSLKtfKRKSEVERAVKRMRHLST 132
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPtrleaAKDAVLALLKSLPG----DRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 338817988  133 GTMTGLAIQYALNIAFSEaegarplRENVPRVIMIV 168
Cdd:pfam13519  75 GTNLAAALQLARAALKHR-------RKNQPRRIVLI 103
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 52-202 7.04e-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: 7.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  52 ENKRADLVFIIDSSRSVNTHDYAKVKEFIVDILQFLdiGPDvTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRhLS 131
Cdd:COG2304   88 ERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQL--RPG-DRVSIVTFAGDARVLLPPTPATDRAKILAAIDRLQ-AG 163

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817988 132 TGTMTGLAIQYALNIAfseaegARPLRENVPRVIMIVTDGRP------QDSVAEVAAKARDTGILIFAIGVGQvDFN 202
Cdd:COG2304  164 GGTALGAGLELAYELA------RKHFIPGRVNRVILLTDGDAnvgitdPEELLKLAEEAREEGITLTTLGVGS-DYN 233
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 653-852 1.06e-10

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 63.58  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 653 PIDLVFVIDGSKSLGEENFEVVKQFVTGIIDSLTisPKAaRVGLLQYSTQVHTEFTLRNFNSAKDMKKAVAHMK-----Y 727
Cdd:COG2304   91 PLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLR--PGD-RVSIVTFAGDARVLLPPTPATDRAKILAAIDRLQagggtA 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 728 MGKGSMTGLALkhmFERSFTQGegarplstrVPRAAIVFTDGRA------QDDVSEWASKAKANGITMYAVGVGKAIEEE 801
Cdd:COG2304  168 LGAGLELAYEL---ARKHFIPG---------RVNRVILLTDGDAnvgitdPEELLKLAEEAREEGITLTTLGVGSDYNED 235

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 338817988 802 LQEIASEPTNKHLFYAEDFSTMDEISEKLKKGIC-EALEDSDGRQDSPAGEL 852
Cdd:COG2304  236 LLERLADAGGGNYYYIDDPEEAEKVFVREFSRIGyENRALATEDFPLPYGTL 287
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 652-835 5.29e-09

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: 56.75  E-value: 5.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 652 GPIDLVFVIDGSKSLGEENFEVVkQFVTGIIDSLTiSPKAaRVGLLQYSTQVHTEFTLRNFNSA-----KDMKKAV-AHM 725
Cdd:cd01474    3 GHFDLYFVLDKSGSVAANWIEIY-DFVEQLVDRFN-SPGL-RFSFITFSTRATKILPLTDDSSAiikglEVLKKVTpSGQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 726 KYMGKGsmtglaLKHMFERSFTQGEGARplstRVPRAAIVFTDGRAQDDV----SEWASKAKANGITMYAVGVGKAIEEE 801
Cdd:cd01474   80 TYIHEG------LENANEQIFNRNGGGR----ETVSVIIALTDGQLLLNGhkypEHEAKLSRKLGAIVYCVGVTDFLKSQ 149

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 338817988 802 LQEIASEPtnKHLFYAED-FSTMDEISEKLKKGIC 835
Cdd:cd01474  150 LINIADSK--EYVFPVTSgFQALSGIIESVVKKAC 182
VWA_2 pfam13519
von Willebrand factor type A domain;
656-754 6.90e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 54.22  E-value: 6.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  656 LVFVIDGSKS-----LGEENFEVVKQFVTGIIDSLTISpkaaRVGLLQYSTQVHTEFTLRnfNSAKDMKKAVAHMKYMGK 730
Cdd:pfam13519   1 LVFVLDTSGSmrngdYGPTRLEAAKDAVLALLKSLPGD----RVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                          90       100
                  ....*....|....*....|....
gi 338817988  731 GSMTGLALKHMFERSFTQGEGARP 754
Cdd:pfam13519  75 GTNLAAALQLARAALKHRRKNQPR 98
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
54-228 8.28e-09

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 56.47  E-value: 8.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  54 KRADLVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVT---RVGLLQYGSTVKNEFSLktfkrkSEVERAVkrMRHL 130
Cdd:COG4245    4 RRLPVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYALetvEVSVITFDGEAKVLLPL------TDLEDFQ--PPDL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 131 ST--GTMTGLAIQYALNI-----AFSEAEGARPLRenvpRVIMIVTDGRPQDSVAEVAAKA-----RDTGILIFAIGVGQ 198
Cdd:COG4245   76 SAsgGTPLGAALELLLDLierrvQKYTAEGKGDWR----PVVFLITDGEPTDSDWEAALQRlkdgeAAKKANIFAIGVGP 151

                        170       180       190
                 ....*....|....*....|....*....|.
gi 338817988 199 -VDFNTLKSIGSephEDHVFLVANFSQIETL 228
Cdd:COG4245  152 dADTEVLKQLTD---PVRALDALDGLDFREF 179
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 365-400 1.21e-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: 51.47  E-value: 1.21e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  365 CASSNHGCQHECVNTDDSYSCHCLKGFTLNPDKKTC 400
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 438-481 5.76e-08

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: 54.31  E-value: 5.76e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 338817988 438 GKTCSRVDHCAQQDHGCEQLCLNTEDSFVCQCSEGFLINEDLKT 481
Cdd:cd01475  181 GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 520-563 9.51e-08

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: 53.93  E-value: 9.51e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 338817988 520 GKTCAKLDSCALGDHGCEHSCVSSEDSFVCQCFEGYILREDGKT 563
Cdd:cd01475  181 GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 655-835 1.04e-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: 53.09  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 655 DLVFVIDGSKSLGEENFEV-VKQFVTGIIDSLTISPKAARVGLLQYSTQVHTEFTLRNFNSAKD---MKKAVAHMKYMGK 730
Cdd:cd01473    2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERYDKnelLKKINDLKNSYRS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 731 GSMTGL--ALKHMFErSFTQGEGARplsTRVPRAAIVFTDG----RAQDDVSEWASKAKANGITMYAVGVGKAIEEELQE 804
Cdd:cd01473   82 GGETYIveALKYGLK-NYTKHGNRR---KDAPKVTMLFTDGndtsASKKELQDISLLYKEENVKLLVVGVGAASENKLKL 157

                        170       180       190
                 ....*....|....*....|....*....|....
gi 338817988 805 IA---SEPTNKHLFYAEDFSTMDEISEKLKKGIC 835
Cdd:cd01473  158 LAgcdINNDNCPNVIKTEWNNLNGISKFLTDKIC 191
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 324-359 1.19e-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: 48.39  E-value: 1.19e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  324 CASENHGCEHECVNADGSYLCQCHEGFALNPDKKTC 359
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 561-603 2.25e-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: 52.77  E-value: 2.25e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 338817988 561 GKTCRRKDVCQAIDHGCEHICVNSDDSYTCECLEGFRLAEDGK 603
Cdd:cd01475  181 GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 57-237 3.27e-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: 51.55  E-value: 3.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  57 DLVFIIDSSRSVNthDYAKVKEFI---VDILQFLDIGPDVTRVGLLQYGSTVK--NEFSLKTFKRKSE-VERAVKRMRHL 130
Cdd:cd01473    2 DLTLILDESASIG--YSNWRKDVIpftEKIINNLNISKDKVHVGILLFAEKNRdvVPFSDEERYDKNElLKKINDLKNSY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 131 STGTMTGL--AIQYAL-NIAFSEAEgarplRENVPRVIMIVTDGRPQDS----VAEVAAKARDTGILIFAIGVGQVDFNT 203
Cdd:cd01473   80 RSGGETYIveALKYGLkNYTKHGNR-----RKDAPKVTMLFTDGNDTSAskkeLQDISLLYKEENVKLLVVGVGAASENK 154

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 338817988 204 LKSIG--SEPHEDHVFLV-ANFSQIETLTSVFQKKLC 237
Cdd:cd01473  155 LKLLAgcDINNDNCPNVIkTEWNNLNGISKFLTDKIC 191
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 602-644 3.72e-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: 52.00  E-value: 3.72e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 338817988 602 GKRCRRKDVCKSTHHGCEHICVNNGNSYICKCSEGFVLAEDGR 644
Cdd:cd01475  181 GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 570-605 3.79e-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: 3.79e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  570 CQAIDHGCEHICVNSDDSYTCECLEGFRLAEDGKRC 605
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 406-441 7.68e-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: 46.47  E-value: 7.68e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  406 CALNKPGCEHECVNMEESYYCRCHRGYTLDPNGKTC 441
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 611-646 7.99e-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: 46.08  E-value: 7.99e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  611 CKSTHHGCEHICVNNGNSYICKCSEGFVLAEDGRRC 646
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 242-277 8.64e-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: 46.08  E-value: 8.64e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  242 CSTLEHNCAHFCINIPGSYVCRCKQGYILNSDQTTC 277
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 654-819 9.86e-07

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 50.02  E-value: 9.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 654 IDLVFVIDGSKSLGEENF------EVVKQFVTGIIDSLtispKAARVGLLQYS--TQVHTEFT-----LRNFnsAKDMKK 720
Cdd:cd01467    3 RDIMIALDVSGSMLAQDFvkpsrlEAAKEVLSDFIDRR----ENDRIGLVVFAgaAFTQAPLTldresLKEL--LEDIKI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 721 AVAhmkymGKGSMTG----LALKHmfersFTQGEGarplstrVPRAAIVFTDG-RAQDDVSEWASK--AKANGITMYAVG 793
Cdd:cd01467   77 GLA-----GQGTAIGdaigLAIKR-----LKNSEA-------KERVIVLLTDGeNNAGEIDPATAAelAKNKGVRIYTIG 139

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 338817988 794 VGKA------------IEEELQEIASEpTNKHLFYAED 819
Cdd:cd01467  140 VGKSgsgpkpdgstilDEDSLVEIADK-TGGRIFRALD 176
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 283-318 2.19e-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: 44.93  E-value: 2.19e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  283 CAMEDHNCEQLCVNVPGSFVCQCYSGYALAEDGKRC 318
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 48-238 3.42e-06

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 50.73  E-value: 3.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  48 ESSCeNKRADLVFIIDSSRSVNTHDY-AKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEvERAVKR 126
Cdd:PTZ00441  36 EEVC-NEEVDLYLLVDGSGSIGYHNWiTHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASKDK-EQALII 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 127 MRHL-STGTMTGlaiQYALNIAFSEAE---GARPLRENVPRVIMIVTDGRP---QDSVaEVAAKARDTGILIFAIGVGQ- 198
Cdd:PTZ00441 114 VKSLrKTYLPYG---KTNMTDALLEVRkhlNDRVNRENAIQLVILMTDGIPnskYRAL-EESRKLKDRNVKLAVIGIGQg 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 338817988 199 --VDFNTLkSIGSEPHED--HVFLVANFSQIETLTSVFQKKLCT 238
Cdd:PTZ00441 190 inHQFNRL-LAGCRPREGkcKFYSDADWEEAKNLIKPFIAKVCT 232
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 529-564 4.67e-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: 4.67e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  529 CALGDHGCEHSCVSSEDSFVCQCFEGYILREDGKTC 564
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 56-238 6.48e-06

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: 47.89  E-value: 6.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  56 ADLVFIIDSSRSVNtHDYAKVKEFIVDIL-QFLDIGpdvTRVGLLQYGSTVKNEFSLKTFKrkSEVERAVKRMRHLSTGT 134
Cdd:cd01474    5 FDLYFVLDKSGSVA-ANWIEIYDFVEQLVdRFNSPG---LRFSFITFSTRATKILPLTDDS--SAIIKGLEVLKKVTPSG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 135 MTglAIQYALNIA----FSEAEGARplRENvpRVIMIVTDGR----PQDSVAEVAAKARDTGILIFAIGVgqVDFNTLKS 206
Cdd:cd01474   79 QT--YIHEGLENAneqiFNRNGGGR--ETV--SVIIALTDGQlllnGHKYPEHEAKLSRKLGAIVYCVGV--TDFLKSQL 150

                        170       180       190
                 ....*....|....*....|....*....|...
gi 338817988 207 IGSEPHEDHVFLV-ANFSQIETLTSVFQKKLCT 238
Cdd:cd01474  151 INIADSKEYVFPVtSGFQALSGIIESVVKKACI 183
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 447-482 9.65e-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: 43.00  E-value: 9.65e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  447 CAQQDHGCEQLCLNTEDSFVCQCSEGFLINEDLKTC 482
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 56-202 1.53e-05

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


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 46.11  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988  56 ADLVFIIDSSRSVNTHDYAKVKE---FIVDILQFLDigpdvtRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRmrhLST 132
Cdd:cd01465    1 LNLVFVIDRSGSMDGPKLPLVKSalkLLVDQLRPDD------RLAIVTYDGAAETVLPATPVRDKAAILAAIDR---LTA 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817988 133 GTMTGLA--IQYALNIAfseAEGARPLRENvpRVIMIvTDGRPQ------DSVAEVAAKARDTGILIFAIGVGQvDFN 202
Cdd:cd01465   72 GGSTAGGagIQLGYQEA---QKHFVPGGVN--RILLA-TDGDFNvgetdpDELARLVAQKRESGITLSTLGFGD-NYN 142
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 488-523 8.20e-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: 40.69  E-value: 8.20e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 338817988  488 CLLSDHGCEYSCVNMDRSFACQCPEGHVLRSDGKTC 523
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
362-400 4.08e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.77  E-value: 4.08e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 338817988   362 IDYCASsNHGCQH--ECVNTDDSYSCHCLKGFTlnpDKKTC 400
Cdd:smart00179   2 IDECAS-GNPCQNggTCVNTVGSYRCECPPGYT---DGRNC 38
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 644-718 1.03e-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: 41.25  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817988 644 RRCKKCTEGP-IDLVFVIDGSKSLGEENFEVVKQFVTGIIDSLTI------SPKAARVGLLQYSTQVHTEFTLRNFNSAK 716
Cdd:cd01477    9 RECGSDIKNLwLDIVFVVDNSKGMTQGGLWQVRATISSLFGSSSQigtdydDPRSTRVGLVTYNSNATVVADLNDLQSFD 88


                 ..
gi 338817988 717 DM 718
Cdd:cd01477   89 DL 90
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 362-393 1.43e-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: 37.23  E-value: 1.43e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 338817988 362 IDYCASsNHGCQH--ECVNTDDSYSCHCLKGFTL 393
Cdd:cd00054    2 IDECAS-GNPCQNggTCVNTVGSYRCSCPPGYTG 34
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 480-522 6.33e-03

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: 39.29  E-value: 6.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 338817988 480 KTCSRVDYCLLSDHGCEYSCVNMDRSFACQCPEGHVLRSDGKT 522
Cdd:cd01475  182 KICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
 242-271 6.47e-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: 35.27  E-value: 6.47e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 338817988  242 CSTLEHNCAH--FCINIPGSYVCRCKQGYILN 271
Cdd:pfam12947   1 CSDNNGGCHPnaTCTNTGGSFTCTCNDGYTGD 32
EGF_CA smart00179
Calcium-binding EGF-like domain;
281-319 7.68e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 34.92  E-value: 7.68e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 338817988   281 DLCAmEDHNCEQ--LCVNVPGSFVCQCYSGYalaEDGKRCV 319
Cdd:smart00179   3 DECA-SGNPCQNggTCVNTVGSYRCECPPGY---TDGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
403-441 8.73e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 34.92  E-value: 8.73e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 338817988   403 INYCALNKPgCEH--ECVNMEESYYCRCHRGYTldpNGKTC 441
Cdd:smart00179   2 IDECASGNP-CQNggTCVNTVGSYRCECPPGYT---DGRNC 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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