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Conserved domains on  [gi|306518578|ref|NP_034900|]
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matrilin-3 precursor [Mus musculus]

Protein Classification

vWFA and FXa_inhibition domain-containing protein( domain architecture ID 10208632)

protein containing domains vWFA, FXa_inhibition, and Matrilin_ccoil

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 75-298 1.77e-107

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: 318.56  E-value: 1.77e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  75 RPLDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGATDTRVAVVNYASTVKIEFQLNTYSDKQALKQAVARITPLSTG 154
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 155 TMSGLAIQTAMEEAFTVEAGARGPMSNIPKVAIIVTDGRPQDQVNEVAARARASGIELYAVGVDRADMESLKMMASKPLE 234
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 306518578 235 EHVFYVETYGVIEKLSARFQETFCAL-DQCMLGTHQCQHVCVSdGDGKHHCECSQGYTLNADGKT 298
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICVVpDLCATLSHVCQQVCIS-TPGSYLCACTEGYALLEDNKT 224
Matrilin_ccoil super family cl10527
Trimeric coiled-coil oligomerization domain of matrilin; This short domain is a coiled coil ...
 438-478 1.44e-10

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.


The actual alignment was detected with superfamily member pfam10393:

Pssm-ID: 463070  Cd Length: 43  Bit Score: 56.21  E-value: 1.44e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 306518578  438 EDACGCGATLAFQEKVSSHLQKLNTKLDNILKKLKVTEYGQ 478
Cdd:pfam10393   3 EDPCKCEAIVAFQTKVESEIQALTTKLEEVTKRIEALENRL 43
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 347-383 1.07e-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: 1.07e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 306518578  347 CASGTHGCQHICVNDGaGSHHCECFEGYTLNADKKTC 383
Cdd:pfam14670   1 CSVNNGGCSHLCLNTP-GGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 305-341 6.30e-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: 6.30e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 306518578  305 CALSTHGCEQICVNdRNGSYHCECYGGYALNADRRTC 341
Cdd:pfam14670   1 CSVNNGGCSHLCLN-TPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 389-425 8.13e-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: 42.61  E-value: 8.13e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 306518578  389 CALGTHGCQHICVsDGAVAYHCDCFPGYTLNDDKKTC 425
Cdd:pfam14670   1 CSVNNGGCSHLCL-NTPGGYTCSCPEGYELQDDGRTC 36
 
Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 75-298 1.77e-107

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: 318.56  E-value: 1.77e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  75 RPLDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGATDTRVAVVNYASTVKIEFQLNTYSDKQALKQAVARITPLSTG 154
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 155 TMSGLAIQTAMEEAFTVEAGARGPMSNIPKVAIIVTDGRPQDQVNEVAARARASGIELYAVGVDRADMESLKMMASKPLE 234
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 306518578 235 EHVFYVETYGVIEKLSARFQETFCAL-DQCMLGTHQCQHVCVSdGDGKHHCECSQGYTLNADGKT 298
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICVVpDLCATLSHVCQQVCIS-TPGSYLCACTEGYALLEDNKT 224
VWA pfam00092
von Willebrand factor type A domain;
78-252 1.70e-62

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 200.96  E-value: 1.70e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578   78 DLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGATDTRVAVVNYASTVKIEFQLNTYSDKQALKQAVARITPLSTGTMS 157
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  158 -GLAIQTAMEEAFTVEAGARgpmSNIPKVAIIVTDGRPQD-QVNEVAARARASGIELYAVGVDRADMESLKMMASKPLEE 235
Cdd:pfam00092  81 tGKALKYALENLFSSAAGAR---PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                         170
                  ....*....|....*..
gi 306518578  236 HVFYVETYGVIEKLSAR 252
Cdd:pfam00092 158 HVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 78-242 9.94e-46

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: 157.23  E-value: 9.94e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578    78 DLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGATDTRVAVVNYASTVKIEFQLNTYSDKQALKQAVARITPLSTG-TM 156
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGgTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578   157 SGLAIQTAMEEAFTVEAGARgpmSNIPKVAIIVTDGRPQD---QVNEVAARARASGIELYAVGVDRA-DMESLKMMASKP 232
Cdd:smart00327  81 LGAALQYALENLFSKSAGSR---RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAP 157

                          170
                   ....*....|
gi 306518578   233 LEEHVFYVET 242
Cdd:smart00327 158 GGVYVFLPEL 167
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 75-225 9.17e-16

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 77.45  E-value: 9.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  75 RPLDLVFIIDSSRSVR--PLEftKVKTFVSRIIDTLdiGATDtRVAVVNYASTVKIEFQLNTYSDKQALKQAVARITPlS 152
Cdd:COG2304   90 PPLNLVFVIDVSGSMSgdKLE--LAKEAAKLLVDQL--RPGD-RVSIVTFAGDARVLLPPTPATDRAKILAAIDRLQA-G 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 153 TGTMSGLAIQTAMEEAftveagARGPMSNIPKVAIIVTDGRP------QDQVNEVAARARASGIELYAVGV----DRADM 222
Cdd:COG2304  164 GGTALGAGLELAYELA------RKHFIPGRVNRVILLTDGDAnvgitdPEELLKLAEEAREEGITLTTLGVgsdyNEDLL 237


                 ...
gi 306518578 223 ESL 225
Cdd:COG2304  238 ERL 240
Matrilin_ccoil pfam10393
Trimeric coiled-coil oligomerization domain of matrilin; This short domain is a coiled coil ...
 438-478 1.44e-10

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: 56.21  E-value: 1.44e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 306518578  438 EDACGCGATLAFQEKVSSHLQKLNTKLDNILKKLKVTEYGQ 478
Cdd:pfam10393   3 EDPCKCEAIVAFQTKVESEIQALTTKLEEVTKRIEALENRL 43
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 347-383 1.07e-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: 1.07e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 306518578  347 CASGTHGCQHICVNDGaGSHHCECFEGYTLNADKKTC 383
Cdd:pfam14670   1 CSVNNGGCSHLCLNTP-GGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 305-341 6.30e-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: 6.30e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 306518578  305 CALSTHGCEQICVNdRNGSYHCECYGGYALNADRRTC 341
Cdd:pfam14670   1 CSVNNGGCSHLCLN-TPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 389-425 8.13e-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: 42.61  E-value: 8.13e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 306518578  389 CALGTHGCQHICVsDGAVAYHCDCFPGYTLNDDKKTC 425
Cdd:pfam14670   1 CSVNNGGCSHLCL-NTPGGYTCSCPEGYELQDDGRTC 36
 
Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 75-298 1.77e-107

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: 318.56  E-value: 1.77e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  75 RPLDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGATDTRVAVVNYASTVKIEFQLNTYSDKQALKQAVARITPLSTG 154
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 155 TMSGLAIQTAMEEAFTVEAGARGPMSNIPKVAIIVTDGRPQDQVNEVAARARASGIELYAVGVDRADMESLKMMASKPLE 234
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 306518578 235 EHVFYVETYGVIEKLSARFQETFCAL-DQCMLGTHQCQHVCVSdGDGKHHCECSQGYTLNADGKT 298
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICVVpDLCATLSHVCQQVCIS-TPGSYLCACTEGYALLEDNKT 224
VWA pfam00092
von Willebrand factor type A domain;
78-252 1.70e-62

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 200.96  E-value: 1.70e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578   78 DLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGATDTRVAVVNYASTVKIEFQLNTYSDKQALKQAVARITPLSTGTMS 157
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  158 -GLAIQTAMEEAFTVEAGARgpmSNIPKVAIIVTDGRPQD-QVNEVAARARASGIELYAVGVDRADMESLKMMASKPLEE 235
Cdd:pfam00092  81 tGKALKYALENLFSSAAGAR---PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                         170
                  ....*....|....*..
gi 306518578  236 HVFYVETYGVIEKLSAR 252
Cdd:pfam00092 158 HVFTVSDFEALEDLQDQ 174
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 78-242 6.72e-56

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: 183.58  E-value: 6.72e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  78 DLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGATDTRVAVVNYASTVKIEFQLNTYSDKQALKQAVARITPLSTGTMS 157
Cdd:cd01472    2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 158 GLAIQTAMEEAFTVEAGARgpmSNIPKVAIIVTDGRPQDQVNEVAARARASGIELYAVGVDRADMESLKMMASKPLEEHV 237
Cdd:cd01472   82 GKALKYVRENLFTEASGSR---EGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYV 158


                 ....*
gi 306518578 238 FYVET 242
Cdd:cd01472  159 FNVAD 163
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 77-238 2.18e-52

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: 174.02  E-value: 2.18e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  77 LDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGATDTRVAVVNYASTVKIEFQLNTYSDKQALKQAVARITPL-STGT 155
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLgGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 156 MSGLAIQTAMEEAFTvEAGARgpmSNIPKVAIIVTDGRPQD--QVNEVAARARASGIELYAVGVDRADMESLKMMASKPL 233
Cdd:cd01450   81 NTGKALQYALEQLFS-ESNAR---ENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156


                 ....*
gi 306518578 234 EEHVF 238
Cdd:cd01450  157 ERHVF 161
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 78-241 2.28e-52

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: 174.40  E-value: 2.28e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  78 DLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGATDTRVAVVNYASTVKIEFQLNTYSDKQALKQAVARITPLSTGTMS 157
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 158 GLAIQTAMEEAFTVEAGARgpmSNIPKVAIIVTDGRPQDQVNEVAARARASGIELYAVGVDRADMESLKMMASKPLEEHV 237
Cdd:cd01482   82 GKALTHVREKNFTPDAGAR---PGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHV 158


                 ....
gi 306518578 238 FYVE 241
Cdd:cd01482  159 FNVA 162
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 78-242 9.94e-46

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: 157.23  E-value: 9.94e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578    78 DLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGATDTRVAVVNYASTVKIEFQLNTYSDKQALKQAVARITPLSTG-TM 156
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGgTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578   157 SGLAIQTAMEEAFTVEAGARgpmSNIPKVAIIVTDGRPQD---QVNEVAARARASGIELYAVGVDRA-DMESLKMMASKP 232
Cdd:smart00327  81 LGAALQYALENLFSKSAGSR---RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAP 157

                          170
                   ....*....|
gi 306518578   233 LEEHVFYVET 242
Cdd:smart00327 158 GGVYVFLPEL 167
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 78-243 2.34e-35

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: 129.37  E-value: 2.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  78 DLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGATDTRVAVVNYASTVKIEFQLNTYSDKQALKQAVARITPLS-TGTM 156
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGgSQLN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 157 SGLAIQTAMEEAFTVEAGARGPmSNIPKVAIIVTDGRPQDQVNEVAARARASGIELYAVGVDRADMESLKMMASKPleEH 236
Cdd:cd01481   82 TGSALDYVVKNLFTKSAGSRIE-EGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP--SF 158


                 ....*..
gi 306518578 237 VFYVETY 243
Cdd:cd01481  159 VFQVSDF 165
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 77-243 4.45e-35

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 129.01  E-value: 4.45e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  77 LDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGATDTRVAVVNYASTVKIEFQLNTYSDKQALKQAVARITPLSTGTM 156
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 157 SGLAIQTAMEEAFTVEAGARgpmSNIPKVAIIVTDGRPQD--QVNEVAARARASGIELYAVGV-----DRADMESLKMMA 229
Cdd:cd01469   81 TATAIQYVVTELFSESNGAR---KDATKVLVVITDGESHDdpLLKDVIPQAEREGIIRYAIGVgghfqRENSREELKTIA 157

                        170
                 ....*....|....
gi 306518578 230 SKPLEEHVFYVETY 243
Cdd:cd01469  158 SKPPEEHFFNVTDF 171
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 77-238 9.08e-31

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 116.51  E-value: 9.08e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  77 LDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGATDTRVAVVNYASTVKIEFQLNTYSDKQALKQAVARITP-LSTGT 155
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 156 MSGLAIQTAMEEAFtveagaRGPMSNIPKVAIIVTDGRPQDQ---VNEVAARARASGIELYAVGV-DRADMESLKMMASK 231
Cdd:cd00198   81 NIGAALRLALELLK------SAKRPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIgDDANEDELKEIADK 154


                 ....*..
gi 306518578 232 PLEEHVF 238
Cdd:cd00198  155 TTGGAVF 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 77-238 2.36e-24

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


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 99.01  E-value: 2.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  77 LDLVFIIDSSRSVRPLeFTKVKTFVSRIIDTLDIGATDTRVAVVNYAS--TVKIEFQLNTYSDKQALKQAVARITPLSTG 154
Cdd:cd01476    1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGrgRQRVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 155 TMSGLAIQTAMEEaFTVEAGARgpmSNIPKVAIIVTDGRPQDQVNEVAARARAS-GIELYAVGV-DRA--DMESLKMMAS 230
Cdd:cd01476   80 TATGAAIEVALQQ-LDPSEGRR---EGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTgDPGtvDTEELHSITG 155


                 ....*...
gi 306518578 231 KplEEHVF 238
Cdd:cd01476  156 N--EDHIF 161
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 76-237 1.52e-21

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 91.68  E-value: 1.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  76 PLDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTL------DIGATDTRVAVVNYASTVKIEFQ-LNTYSDKQALKQAVARI 148
Cdd:cd01480    2 PVDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGfLRDIRNYTSLKEAVDNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 149 TPLSTGTMSGLAIQTAMEEAFtveagaRGPMSNIPKVAIIVTDGRPQDQ----VNEVAARARASGIELYAVGVDRADMES 224
Cdd:cd01480   82 EYIGGGTFTDCALKYATEQLL------EGSHQKENKFLLVITDGHSDGSpdggIEKAVNEADHLGIKIFFVAVGSQNEEP 155

                        170
                 ....*....|...
gi 306518578 225 LKMMASKPLEEHV 237
Cdd:cd01480  156 LSRIACDGKSALY 168
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 75-225 9.17e-16

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 77.45  E-value: 9.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  75 RPLDLVFIIDSSRSVR--PLEftKVKTFVSRIIDTLdiGATDtRVAVVNYASTVKIEFQLNTYSDKQALKQAVARITPlS 152
Cdd:COG2304   90 PPLNLVFVIDVSGSMSgdKLE--LAKEAAKLLVDQL--RPGD-RVSIVTFAGDARVLLPPTPATDRAKILAAIDRLQA-G 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 153 TGTMSGLAIQTAMEEAftveagARGPMSNIPKVAIIVTDGRP------QDQVNEVAARARASGIELYAVGV----DRADM 222
Cdd:COG2304  164 GGTALGAGLELAYELA------RKHFIPGRVNRVILLTDGDAnvgitdPEELLKLAEEAREEGITLTTLGVgsdyNEDLL 237


                 ...
gi 306518578 223 ESL 225
Cdd:COG2304  238 ERL 240
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 29-229 1.62e-15

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 76.52  E-value: 1.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  29 PGRLARASVRRLGTRVPGGSPGHLSALATSTRAPYSGGRGAGVC-KSRPLDLVFIIDSSRSVRPLE-FTKVKTFVSRIID 106
Cdd:COG1240   44 LAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALArPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLD 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 107 TLDigaTDTRVAVVNYASTVKIefQLNTYSDKQALKQAVARITPlSTGTMSGLAIQTAMEEAFTVEAGARgpmsnipKVA 186
Cdd:COG1240  124 DYR---PRDRVGLVAFGGEAEV--LLPLTRDREALKRALDELPP-GGGTPLGDALALALELLKRADPARR-------KVI 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 306518578 187 IIVTDGRP---QDQVNEVAARARASGIELYAVGV--DRADMESLKMMA 229
Cdd:COG1240  191 VLLTDGRDnagRIDPLEAAELAAAAGIRIYTIGVgtEAVDEGLLREIA 238
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 77-216 2.59e-13

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 68.18  E-value: 2.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  77 LDLVFIIDSSRSVRPL-EFTKVKTFVSRIIDTLDIGATDTRVAVVNYASTVKIEFQLNTY--SDKQALKQAVA--RITPL 151
Cdd:cd01471    1 LDLYLLVDGSGSIGYSnWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPnsTNKDLALNAIRalLSLYY 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 152 STG-TMSGLAIQTAMEEAFTveagARGPMSNIPKVAIIVTDG---RPQDQVNEVAA-RARASGIELYAVG 216
Cdd:cd01471   81 PNGsTNTTSALLVVEKHLFD----TRGNRENAPQLVIIMTDGipdSKFRTLKEARKlRERGVIIAVLGVG 146
VWA_2 pfam13519
von Willebrand factor type A domain;
79-189 1.21e-11

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 61.15  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578   79 LVFIIDSSRSVR-----PLEFTKVKTFVSRIIDTLDigatDTRVAVVNYASTVKIEFQLNtySDKQALKQAVARITPLST 153
Cdd:pfam13519   1 LVFVLDTSGSMRngdygPTRLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 306518578  154 GTMSGLAIQTAMEEAFTveagargPMSNIPKVAIIV 189
Cdd:pfam13519  75 GTNLAAALQLARAALKH-------RRKNQPRRIVLI 103
Matrilin_ccoil pfam10393
Trimeric coiled-coil oligomerization domain of matrilin; This short domain is a coiled coil ...
 438-478 1.44e-10

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: 56.21  E-value: 1.44e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 306518578  438 EDACGCGATLAFQEKVSSHLQKLNTKLDNILKKLKVTEYGQ 478
Cdd:pfam10393   3 EDPCKCEAIVAFQTKVESEIQALTTKLEEVTKRIEALENRL 43
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 77-225 1.08e-09

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: 57.28  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  77 LDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIgatDTRVAVVNYASTVKIEFQLNTYSDKQALKQAVARITPlSTGTM 156
Cdd:cd01465    1 LNLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRP---DDRLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTA-GGSTA 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 306518578 157 SGLAIQTAMEEAftVEAGARGPMSNIpkvaIIVTDGRPQ------DQVNEVAARARASGIELYAVGVDRADMESL 225
Cdd:cd01465   77 GGAGIQLGYQEA--QKHFVPGGVNRI----LLATDGDFNvgetdpDELARLVAQKRESGITLSTLGFGDNYNEDL 145
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
73-226 1.84e-09

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 57.24  E-value: 1.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  73 KSRPLDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTL--DIGATDT-RVAVVNYASTVKIEFQLNTYSDKQALKQAVARIT 149
Cdd:COG4245    2 PMRRLPVYLLLDTSGSMSGEPIEALNEGLQALIDELrqDPYALETvEVSVITFDGEAKVLLPLTDLEDFQPPDLSASGGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 150 PLstgtmsGLAIQTAMEEaftVEAGARGPMSNI----PKVAIIVTDGRPQDQ-----VNEVAARARASGIELYAVGVDR- 219
Cdd:COG4245   82 PL------GAALELLLDL---IERRVQKYTAEGkgdwRPVVFLITDGEPTDSdweaaLQRLKDGEAAKKANIFAIGVGPd 152


                 ....*..
gi 306518578 220 ADMESLK 226
Cdd:COG4245  153 ADTEVLK 159
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 78-240 1.85e-07

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: 51.36  E-value: 1.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  78 DLVFIIDSSRSVRPlEFTKVKTFVSRIIDTLDigATDTRVAVVNYASTVKIEFQLNTYSDK--QALkQAVARITPlSTGT 155
Cdd:cd01474    6 DLYFVLDKSGSVAA-NWIEIYDFVEQLVDRFN--SPGLRFSFITFSTRATKILPLTDDSSAiiKGL-EVLKKVTP-SGQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 156 MSGLAIQTAMEEAFTVEAGARgpmsNIPKVAIIVTDGR-----PQDQVNEvAARARASGIELYAVGVDRADMESLKMMAS 230
Cdd:cd01474   81 YIHEGLENANEQIFNRNGGGR----ETVSVIIALTDGQlllngHKYPEHE-AKLSRKLGAIVYCVGVTDFLKSQLINIAD 155

                        170
                 ....*....|
gi 306518578 231 KPleEHVFYV 240
Cdd:cd01474  156 SK--EYVFPV 163
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 347-383 1.07e-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: 1.07e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 306518578  347 CASGTHGCQHICVNDGaGSHHCECFEGYTLNADKKTC 383
Cdd:pfam14670   1 CSVNNGGCSHLCLNTP-GGYTCSCPEGYELQDDGRTC 36
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 74-241 3.16e-06

VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The alpha 2 and delta subunits result from proteolytic processing of a single gene product and carries at its N-terminus the VWA and cache domains, The alpha 2 delta gene family has orthologues in D. melanogaster and C. elegans but none have been detected in aither A. thaliana or yeast. The exact biochemical function of the VWA domain is not known but the alpha 2 delta complex has been shown to regulate various functional properties of the channel complex.


Pssm-ID: 238740 [Multi-domain]  Cd Length: 190  Bit Score: 47.77  E-value: 3.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  74 SRPLDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLdigATDTRVAVVNYASTV-------KIEFQLNTYSDKQALKQAVA 146
Cdd:cd01463   11 TSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTL---SDNDFFNIITFSNEVnpvvpcfNDTLVQATTSNKKVLKEALD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 147 RITPLSTGTMSglaiqTAMEEAFTV-----EAGARGPMSNIPKVAIIVTDGRPQ--DQVNEVAARARASGIEL----YAV 215
Cdd:cd01463   88 MLEAKGIANYT-----KALEFAFSLllknlQSNHSGSRSQCNQAIMLITDGVPEnyKEIFDKYNWDKNSEIPVrvftYLI 162

                        170       180
                 ....*....|....*....|....*.
gi 306518578 216 GVDRADMESLKMMASkplEEHVFYVE 241
Cdd:cd01463  163 GREVTDRREIQWMAC---ENKGYYSH 185
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 305-341 6.30e-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: 6.30e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 306518578  305 CALSTHGCEQICVNdRNGSYHCECYGGYALNADRRTC 341
Cdd:pfam14670   1 CSVNNGGCSHLCLN-TPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 389-425 8.13e-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: 42.61  E-value: 8.13e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 306518578  389 CALGTHGCQHICVsDGAVAYHCDCFPGYTLNDDKKTC 425
Cdd:pfam14670   1 CSVNNGGCSHLCL-NTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 263-299 2.67e-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: 41.07  E-value: 2.67e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 306518578  263 CMLGTHQCQHVCVsDGDGKHHCECSQGYTLNADGKTC 299
Cdd:pfam14670   1 CSVNNGGCSHLCL-NTPGGYTCSCPEGYELQDDGRTC 36
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 78-229 1.95e-04

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 42.30  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  78 DLVFIIDSSRSVRPLEFTK-VKTFVSRIIDTLDIGATDTRVAVVNYA---STVKIEFQLNTYSDKQALKqavaRITPLST 153
Cdd:cd01473    2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAeknRDVVPFSDEERYDKNELLK----KINDLKN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 154 GTMSGLA--IQTAMEEAFTVEAGARGPMSNIPKVAIIVTDGRPQD----QVNEVAARARASGIELYAVGVDRADMESLKM 227
Cdd:cd01473   78 SYRSGGEtyIVEALKYGLKNYTKHGNRRKDAPKVTMLFTDGNDTSaskkELQDISLLYKEENVKLLVVGVGAASENKLKL 157


                 ..
gi 306518578 228 MA 229
Cdd:cd01473  158 LA 159
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 77-257 1.18e-03

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


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 39.96  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  77 LDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGATDTRVAVVNYASTVKIEFQLNTYSDKQA------LKQAVARITP 150
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDAddvikrLEDFNYDDHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 151 LSTGTMSGLAIQTAMEEafTVEAGARGPM--SNIPKVAIIVTDGR------PQDQV---------NEVAARARASGIELY 213
Cdd:cd01470   81 DKTGTNTAAALKKVYER--MALEKVRNKEafNETRHVIILFTDGKsnmggsPLPTVdkiknlvykNNKSDNPREDYLDVY 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 306518578 214 AVGV-DRADMESLKMMAS-KPLEEHVFYVETYgviEKLsarfQETF 257
Cdd:cd01470  159 VFGVgDDVNKEELNDLASkKDNERHFFKLKDY---EDL----QEVF 197
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 75-233 2.22e-03

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


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 38.86  E-value: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  75 RPLDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTL--DIGATDT-RVAVVNYASTVKIEFQLNTYSDKQAlkqavaRITPL 151
Cdd:cd01464    2 RRLPIYLLLDTSGSMAGEPIEALNQGLQMLQSELrqDPYALESvEISVITFDSAARVIVPLTPLESFQP------PRLTA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 152 STGTMSGLAIQTAMEEAFT-VEAGARGPMSNIPKVAIIVTDGRPQDQVNEVAARARASG-----IELYAVGVDrADMESL 225
Cdd:cd01464   76 SGGTSMGAALELALDCIDRrVQRYRADQKGDWRPWVFLLTDGEPTDDLTAAIERIKEARdskgrIVACAVGPK-ADLDTL 154


                 ....*...
gi 306518578 226 KMMASKPL 233
Cdd:cd01464  155 KQITEGVP 162
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 76-230 2.95e-03

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


Pssm-ID: 238738 [Multi-domain]  Cd Length: 171  Bit Score: 38.74  E-value: 2.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  76 PLDLVFIIDSSRSV--RPLEftKVKTFVSRIIDTLDIGAtdtRVAVVNYASTVKIEFQLNTYSDKQALKQAVARITPLSt 153
Cdd:cd01461    2 PKEVVFVIDTSGSMsgTKIE--QTKEALLTALKDLPPGD---YFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQ- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 154 gTMSGLAIQTAMEEAFTVEAGARGPMSNIpkvaIIVTDGRPQD--QVNEVAARARASGIELYAVGV-DRADMESLKMMAS 230
Cdd:cd01461   76 -ALGGTNMNDALEAALELLNSSPGSVPQI----ILLTDGEVTNesQILKNVREALSGRIRLFTFGIgSDVNTYLLERLAR 150
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
 283-303 3.49e-03

Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteriztic pattern 'ababcc'. They are found in blood coagulation proteins such as fibrillin, Clr and Cls, thrombomodulin, and the LDL receptor. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal cysteine residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In cEGFs the C-terminal thiol resides on the C-terminal beta-sheet, resulting in long loop-lengths between the cysteine residues of disulfide 'c', typically C[10+]XC. These longer loop-lengths may have arisen by selective cysteine loss from a four-disulfide EGF template such as laminin or integrin. Tandem cEGF domains have five linking residues between terminal cysteines of adjacent domains. cEGF domains may or may not bind calcium in the linker region. cEGF domains with the consensus motif CXN4X[F,Y]XCXC are hydroxylated exclusively on the asparagine residue.


Pssm-ID: 463661  Cd Length: 22  Bit Score: 34.69  E-value: 3.49e-03
                          10        20
                  ....*....|....*....|.
gi 306518578  283 HCECSQGYTLNADGKTCSAID 303
Cdd:pfam12662   1 TCSCPPGYQLDPDGRTCVDID 21
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
 409-430 3.73e-03

Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteriztic pattern 'ababcc'. They are found in blood coagulation proteins such as fibrillin, Clr and Cls, thrombomodulin, and the LDL receptor. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal cysteine residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In cEGFs the C-terminal thiol resides on the C-terminal beta-sheet, resulting in long loop-lengths between the cysteine residues of disulfide 'c', typically C[10+]XC. These longer loop-lengths may have arisen by selective cysteine loss from a four-disulfide EGF template such as laminin or integrin. Tandem cEGF domains have five linking residues between terminal cysteines of adjacent domains. cEGF domains may or may not bind calcium in the linker region. cEGF domains with the consensus motif CXN4X[F,Y]XCXC are hydroxylated exclusively on the asparagine residue.


Pssm-ID: 463661  Cd Length: 22  Bit Score: 34.69  E-value: 3.73e-03
                          10        20
                  ....*....|....*....|..
gi 306518578  409 HCDCFPGYTLNDDKKTCSDIEE 430
Cdd:pfam12662   1 TCSCPPGYQLDPDGRTCVDIDE 22
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 77-231 4.20e-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: 38.56  E-value: 4.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578  77 LDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGATD------TRVAVVNYASTVKIEFQLNTYSDKQALKQAV-ARIT 149
Cdd:cd01477   20 LDIVFVVDNSKGMTQGGLWQVRATISSLFGSSSQIGTDyddprsTRVGLVTYNSNATVVADLNDLQSFDDLYSQIqGSLT 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306518578 150 PLSTGTMSGLaiQTAMEEAFTV-EAGARGPMSNIPKVAIIVT-----DGrpQDQVNEVAARARASGIELYAVG----VDR 219
Cdd:cd01477  100 DVSSTNASYL--DTGLQAAEQMlAAGKRTSRENYKKVVIVFAsdyndEG--SNDPRPIAARLKSTGIAIITVAftqdESS 175

                        170
                 ....*....|..
gi 306518578 220 ADMESLKMMASK 231
Cdd:cd01477  176 NLLDKLGKIASP 187
 
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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