NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|3647275|emb|CAA12110|]
View 

matrilin-3 [Homo sapiens]

Protein Classification

matrilin; VIT and vWA domain-containing protein( domain architecture ID 10208640)

matrilin acts as the component of the extracellular matrix of cartilage| VIT (vault protein inter-alpha-trypsin) and vWA (von Willebrand factor type A) domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 80-303 1.75e-110

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: 326.26  E-value: 1.75e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275   80 RPLDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGPADTRVAVVNYASTVKIEFQLQAYTDKQSLKQAVGRITPLSTG 159
Cdd:cd01475   1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275  160 TMSGLAIQTAMDEAFTVEAGAREPSSNIPKVAIIVTDGRPQDQVNEVAARAQASGIELYAVGVDRADMASLKMMASEPLE 239
Cdd:cd01475  81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3647275  240 EHVFYVETYGVIEKLSSRFQETFCAL-DPCVLGTHQCQHVCISdGEGKHHCECSQGYTLNADKKT 303
Cdd:cd01475 161 DHVFYVEDFSTIEELTKKFQGKICVVpDLCATLSHVCQQVCIS-TPGSYLCACTEGYALLEDNKT 224
Matrilin_ccoil pfam10393
Trimeric coiled-coil oligomerization domain of matrilin; This short domain is a coiled coil ...
 441-483 3.21e-13

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: 63.91  E-value: 3.21e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 3647275    441 STEDACGCEATLAFQDKVSSYLQRLNTKLDDILEKLKINEYGQ 483
Cdd:pfam10393   1 VEEDPCKCEAIVAFQTKVESEIQALTTKLEEVTKRIEALENRL 43
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 310-346 4.94e-09

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: 4.94e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 3647275    310 CALNTHGCEHICVNdRSGSYHCECYEGYTLNEDRKTC 346
Cdd:pfam14670   1 CSVNNGGCSHLCLN-TPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 352-388 2.66e-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: 46.85  E-value: 2.66e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 3647275    352 CALGTHGCQHICVNdRTGSHHCECYEGYTLNADKKTC 388
Cdd:pfam14670   1 CSVNNGGCSHLCLN-TPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 394-430 9.78e-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: 45.31  E-value: 9.78e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 3647275    394 CALGSHGCQHICVsDGAASYHCDCYPGYTLNEDKKTC 430
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 ...
 80-303 1.75e-110

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: 326.26  E-value: 1.75e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275   80 RPLDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGPADTRVAVVNYASTVKIEFQLQAYTDKQSLKQAVGRITPLSTG 159
Cdd:cd01475   1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275  160 TMSGLAIQTAMDEAFTVEAGAREPSSNIPKVAIIVTDGRPQDQVNEVAARAQASGIELYAVGVDRADMASLKMMASEPLE 239
Cdd:cd01475  81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3647275  240 EHVFYVETYGVIEKLSSRFQETFCAL-DPCVLGTHQCQHVCISdGEGKHHCECSQGYTLNADKKT 303
Cdd:cd01475 161 DHVFYVEDFSTIEELTKKFQGKICVVpDLCATLSHVCQQVCIS-TPGSYLCACTEGYALLEDNKT 224
VWA pfam00092
von Willebrand factor type A domain;
83-257 1.46e-61

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 198.65  E-value: 1.46e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275     83 DLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGPADTRVAVVNYASTVKIEFQLQAYTDKQSLKQAVGRITPLSTGTMS 162
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275    163 -GLAIQTAMDEAFTVEAGAREpssNIPKVAIIVTDGRPQD-QVNEVAARAQASGIELYAVGVDRADMASLKMMASEPLEE 240
Cdd:pfam00092  81 tGKALKYALENLFSSAAGARP---GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                         170
                  ....*....|....*..
gi 3647275    241 HVFYVETYGVIEKLSSR 257
Cdd:pfam00092 158 HVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 83-247 3.46e-44

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: 153.38  E-value: 3.46e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275      83 DLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGPADTRVAVVNYASTVKIEFQLQAYTDKQSLKQAVGRITPLSTG-TM 161
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGgTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275     162 SGLAIQTAMDEAFTVEAGAREpssNIPKVAIIVTDGRPQD---QVNEVAARAQASGIELYAVGVDRA-DMASLKMMASEP 237
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRR---GAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAP 157

                          170
                   ....*....|
gi 3647275     238 LEEHVFYVET 247
Cdd:smart00327 158 GGVYVFLPEL 167
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 28-236 4.69e-17

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: 80.75  E-value: 4.69e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275   28 PDPVARPGFRRLETRGPGGSPGRRPSPAAPDGAPASGTSEPGRARGAGVcKSRPLDLVFIIDSSRSVRPLE-FTKVKTFV 106
Cdd:COG1240  40 LALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALAR-PQRGRDVVLVVDASGSMAAENrLEAAKGAL 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275  107 SRIIDTLdigPADTRVAVVNYASTVkieFQLQAYT-DKQSLKQAVGRITPlSTGTMSGLAIQTAMDEaftveagAREPSS 185
Cdd:COG1240 119 LDFLDDY---RPRDRVGLVAFGGEA---EVLLPLTrDREALKRALDELPP-GGGTPLGDALALALEL-------LKRADP 184

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 3647275  186 NIPKVAIIVTDGRP---QDQVNEVAARAQASGIELYAVGV--DRADMASLKMMASE 236
Cdd:COG1240 185 ARRKVIVLLTDGRDnagRIDPLEAAELAAAAGIRIYTIGVgtEAVDEGLLREIAEA 240
Matrilin_ccoil pfam10393
Trimeric coiled-coil oligomerization domain of matrilin; This short domain is a coiled coil ...
 441-483 3.21e-13

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: 63.91  E-value: 3.21e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 3647275    441 STEDACGCEATLAFQDKVSSYLQRLNTKLDDILEKLKINEYGQ 483
Cdd:pfam10393   1 VEEDPCKCEAIVAFQTKVESEIQALTTKLEEVTKRIEALENRL 43
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 310-346 4.94e-09

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: 4.94e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 3647275    310 CALNTHGCEHICVNdRSGSYHCECYEGYTLNEDRKTC 346
Cdd:pfam14670   1 CSVNNGGCSHLCLN-TPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 352-388 2.66e-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: 46.85  E-value: 2.66e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 3647275    352 CALGTHGCQHICVNdRTGSHHCECYEGYTLNADKKTC 388
Cdd:pfam14670   1 CSVNNGGCSHLCLN-TPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 394-430 9.78e-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: 45.31  E-value: 9.78e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 3647275    394 CALGSHGCQHICVsDGAASYHCDCYPGYTLNEDKKTC 430
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 ...
 80-303 1.75e-110

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: 326.26  E-value: 1.75e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275   80 RPLDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGPADTRVAVVNYASTVKIEFQLQAYTDKQSLKQAVGRITPLSTG 159
Cdd:cd01475   1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275  160 TMSGLAIQTAMDEAFTVEAGAREPSSNIPKVAIIVTDGRPQDQVNEVAARAQASGIELYAVGVDRADMASLKMMASEPLE 239
Cdd:cd01475  81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3647275  240 EHVFYVETYGVIEKLSSRFQETFCAL-DPCVLGTHQCQHVCISdGEGKHHCECSQGYTLNADKKT 303
Cdd:cd01475 161 DHVFYVEDFSTIEELTKKFQGKICVVpDLCATLSHVCQQVCIS-TPGSYLCACTEGYALLEDNKT 224
VWA pfam00092
von Willebrand factor type A domain;
83-257 1.46e-61

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 198.65  E-value: 1.46e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275     83 DLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGPADTRVAVVNYASTVKIEFQLQAYTDKQSLKQAVGRITPLSTGTMS 162
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275    163 -GLAIQTAMDEAFTVEAGAREpssNIPKVAIIVTDGRPQD-QVNEVAARAQASGIELYAVGVDRADMASLKMMASEPLEE 240
Cdd:pfam00092  81 tGKALKYALENLFSSAAGARP---GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                         170
                  ....*....|....*..
gi 3647275    241 HVFYVETYGVIEKLSSR 257
Cdd:pfam00092 158 HVFTVSDFEALEDLQDQ 174
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 83-247 1.83e-54

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


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 179.73  E-value: 1.83e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275   83 DLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGPADTRVAVVNYASTVKIEFQLQAYTDKQSLKQAVGRITPLSTGTMS 162
Cdd:cd01472   2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275  163 GLAIQTAMDEAFTVEAGAREpssNIPKVAIIVTDGRPQDQVNEVAARAQASGIELYAVGVDRADMASLKMMASEPLEEHV 242
Cdd:cd01472  82 GKALKYVRENLFTEASGSRE---GVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYV 158


                ....*
gi 3647275  243 FYVET 247
Cdd:cd01472 159 FNVAD 163
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 83-246 1.62e-51

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 172.09  E-value: 1.62e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275   83 DLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGPADTRVAVVNYASTVKIEFQLQAYTDKQSLKQAVGRITPLSTGTMS 162
Cdd:cd01482   2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275  163 GLAIQTAMDEAFTVEAGAREpssNIPKVAIIVTDGRPQDQVNEVAARAQASGIELYAVGVDRADMASLKMMASEPLEEHV 242
Cdd:cd01482  82 GKALTHVREKNFTPDAGARP---GVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHV 158


                ....
gi 3647275  243 FYVE 246
Cdd:cd01482 159 FNVA 162
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 82-243 4.79e-50

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: 168.24  E-value: 4.79e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275   82 LDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGPADTRVAVVNYASTVKIEFQLQAYTDKQSLKQAVGRITPL-STGT 160
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLgGGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275  161 MSGLAIQTAMDEAFTvEAGAREpssNIPKVAIIVTDGRPQD--QVNEVAARAQASGIELYAVGVDRADMASLKMMASEPL 238
Cdd:cd01450  81 NTGKALQYALEQLFS-ESNARE---NVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156


                ....*
gi 3647275  239 EEHVF 243
Cdd:cd01450 157 ERHVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 83-247 3.46e-44

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: 153.38  E-value: 3.46e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275      83 DLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGPADTRVAVVNYASTVKIEFQLQAYTDKQSLKQAVGRITPLSTG-TM 161
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGgTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275     162 SGLAIQTAMDEAFTVEAGAREpssNIPKVAIIVTDGRPQD---QVNEVAARAQASGIELYAVGVDRA-DMASLKMMASEP 237
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRR---GAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAP 157

                          170
                   ....*....|
gi 3647275     238 LEEHVFYVET 247
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 ...
 83-248 8.01e-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: 125.13  E-value: 8.01e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275   83 DLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGPADTRVAVVNYASTVKIEFQLQAYTDKQSLKQAVGRITPLS-TGTM 161
Cdd:cd01481   2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGgSQLN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275  162 SGLAIQTAMDEAFTVEAGARePSSNIPKVAIIVTDGRPQDQVNEVAARAQASGIELYAVGVDRADMASLKMMASEPleEH 241
Cdd:cd01481  82 TGSALDYVVKNLFTKSAGSR-IEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP--SF 158


                ....*..
gi 3647275  242 VFYVETY 248
Cdd:cd01481 159 VFQVSDF 165
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 82-248 4.17e-33

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 123.62  E-value: 4.17e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275   82 LDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGPADTRVAVVNYASTVKIEFQLQAYTDKQSLKQAVGRITPLSTGTM 161
Cdd:cd01469   1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275  162 SGLAIQTAMDEAFTVEAGAREpssNIPKVAIIVTDGRPQD--QVNEVAARAQASGIELYAVGV-----DRADMASLKMMA 234
Cdd:cd01469  81 TATAIQYVVTELFSESNGARK---DATKVLVVITDGESHDdpLLKDVIPQAEREGIIRYAIGVgghfqRENSREELKTIA 157

                       170
                ....*....|....
gi 3647275  235 SEPLEEHVFYVETY 248
Cdd:cd01469 158 SKPPEEHFFNVTDF 171
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 82-243 4.57e-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: 112.27  E-value: 4.57e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275   82 LDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGPADTRVAVVNYASTVKIEFQLQAYTDKQSLKQAVGRITP-LSTGT 160
Cdd:cd00198   1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275  161 MSGLAIQTAMDEAFtveagaREPSSNIPKVAIIVTDGRPQDQ---VNEVAARAQASGIELYAVGV-DRADMASLKMMASE 236
Cdd:cd00198  81 NIGAALRLALELLK------SAKRPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIgDDANEDELKEIADK 154


                ....*..
gi 3647275  237 PLEEHVF 243
Cdd:cd00198 155 TTGGAVF 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 82-243 4.38e-25

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


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 100.94  E-value: 4.38e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275   82 LDLVFIIDSSRSVRPLeFTKVKTFVSRIIDTLDIGPADTRVAVVNYAS--TVKIEFQLQAYTDKQSLKQAVGRITPLSTG 159
Cdd:cd01476   1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGrgRQRVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275  160 TMSGLAIQTAMDEaFTVEAGAREpssNIPKVAIIVTDGRPQDQVNEVA--ARAQAsGIELYAVGV-DRA--DMASLKMMA 234
Cdd:cd01476  80 TATGAAIEVALQQ-LDPSEGRRE---GIPKVVVVLTDGRSHDDPEKQAriLRAVP-NIETFAVGTgDPGtvDTEELHSIT 154


                ....*....
gi 3647275  235 SEplEEHVF 243
Cdd:cd01476 155 GN--EDHIF 161
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 81-224 1.25e-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: 92.06  E-value: 1.25e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275   81 PLDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTL------DIGPADTRVAVVNYASTVKIEFQ-LQAYTDKQSLKQAVGRI 153
Cdd:cd01480   2 PVDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGfLRDIRNYTSLKEAVDNL 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3647275  154 TPLSTGTMSGLAIQTAMDEAFtveagaREPSSNIPKVAIIVTDGRPQDQ----VNEVAARAQASGIELYAVGVDR 224
Cdd:cd01480  82 EYIGGGTFTDCALKYATEQLL------EGSHQKENKFLLVITDGHSDGSpdggIEKAVNEADHLGIKIFFVAVGS 150
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 28-236 4.69e-17

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: 80.75  E-value: 4.69e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275   28 PDPVARPGFRRLETRGPGGSPGRRPSPAAPDGAPASGTSEPGRARGAGVcKSRPLDLVFIIDSSRSVRPLE-FTKVKTFV 106
Cdd:COG1240  40 LALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALAR-PQRGRDVVLVVDASGSMAAENrLEAAKGAL 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275  107 SRIIDTLdigPADTRVAVVNYASTVkieFQLQAYT-DKQSLKQAVGRITPlSTGTMSGLAIQTAMDEaftveagAREPSS 185
Cdd:COG1240 119 LDFLDDY---RPRDRVGLVAFGGEA---EVLLPLTrDREALKRALDELPP-GGGTPLGDALALALEL-------LKRADP 184

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 3647275  186 NIPKVAIIVTDGRP---QDQVNEVAARAQASGIELYAVGV--DRADMASLKMMASE 236
Cdd:COG1240 185 ARRKVIVLLTDGRDnagRIDPLEAAELAAAAGIRIYTIGVgtEAVDEGLLREIAEA 240
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 80-230 1.30e-15

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 77.06  E-value: 1.30e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275   80 RPLDLVFIIDSSRSVR--PLEftKVKTFVSRIIDTLdigPADTRVAVVNYASTVKIEFQLQAYTDKQSLKQAVGRITPlS 157
Cdd:COG2304  90 PPLNLVFVIDVSGSMSgdKLE--LAKEAAKLLVDQL---RPGDRVSIVTFAGDARVLLPPTPATDRAKILAAIDRLQA-G 163

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275  158 TGTMSGLAIQTAMDEAftveagAREPSSNIPKVAIIVTDGRP------QDQVNEVAARAQASGIELYAVGV----DRADM 227
Cdd:COG2304 164 GGTALGAGLELAYELA------RKHFIPGRVNRVILLTDGDAnvgitdPEELLKLAEEAREEGITLTTLGVgsdyNEDLL 237


                ...
gi 3647275  228 ASL 230
Cdd:COG2304 238 ERL 240
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 82-215 3.42e-14

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 70.88  E-value: 3.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275   82 LDLVFIIDSSRSVRPL-EFTKVKTFVSRIIDTLDIGPADTRVAVVNYASTVKIEFQLQAY--TDKQSLKQAVG--RITPL 156
Cdd:cd01471   1 LDLYLLVDGSGSIGYSnWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPnsTNKDLALNAIRalLSLYY 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3647275  157 STG-TMSGLAIQTAMDEAFTVeAGAREpssNIPKVAIIVTDG---RPQDQVNEVAARAQASGI 215
Cdd:cd01471  81 PNGsTNTTSALLVVEKHLFDT-RGNRE---NAPQLVIIMTDGipdSKFRTLKEARKLRERGVI 139
Matrilin_ccoil pfam10393
Trimeric coiled-coil oligomerization domain of matrilin; This short domain is a coiled coil ...
 441-483 3.21e-13

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: 63.91  E-value: 3.21e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 3647275    441 STEDACGCEATLAFQDKVSSYLQRLNTKLDDILEKLKINEYGQ 483
Cdd:pfam10393   1 VEEDPCKCEAIVAFQTKVESEIQALTTKLEEVTKRIEALENRL 43
VWA_2 pfam13519
von Willebrand factor type A domain;
84-194 1.29e-11

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 61.15  E-value: 1.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275     84 LVFIIDSSRSVR-----PLEFTKVKTFVSRIIDTLdigpADTRVAVVNYASTVKIEFQLQayTDKQSLKQAVGRITPLST 158
Cdd:pfam13519   1 LVFVLDTSGSMRngdygPTRLEAAKDAVLALLKSL----PGDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 3647275    159 GTMSGLAIQTAMDEAFtveagarEPSSNIPKVAIIV 194
Cdd:pfam13519  75 GTNLAAALQLARAALK-------HRRKNQPRRIVLI 103
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
78-231 2.49e-10

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 59.94  E-value: 2.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275   78 KSRPLDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTL--DIGPADT-RVAVVNYASTVKiefQLQAYTDKQSLKqavgrIT 154
Cdd:COG4245   2 PMRRLPVYLLLDTSGSMSGEPIEALNEGLQALIDELrqDPYALETvEVSVITFDGEAK---VLLPLTDLEDFQ-----PP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275  155 PLST--GTMSGLAIQTAMDEaftVEAGAREPSSNI----PKVAIIVTDGRPQDQ-----VNEVAARAQASGIELYAVGVD 223
Cdd:COG4245  74 DLSAsgGTPLGAALELLLDL---IERRVQKYTAEGkgdwRPVVFLITDGEPTDSdweaaLQRLKDGEAAKKANIFAIGVG 150


                ....*....
gi 3647275  224 R-ADMASLK 231
Cdd:COG4245 151 PdADTEVLK 159
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 82-222 4.26e-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: 55.74  E-value: 4.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275   82 LDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLdiGPADtRVAVVNYASTVKIEFQLQAYTDKQSLKQAVGRITPlSTGTM 161
Cdd:cd01465   1 LNLVFVIDRSGSMDGPKLPLVKSALKLLVDQL--RPDD-RLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTA-GGSTA 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3647275  162 SGLAIQTAMDEAftVEAGAREPSSNIpkvaIIVTDGRP---QDQVNEVAARAQA---SGIELYAVGV 222
Cdd:cd01465  77 GGAGIQLGYQEA--QKHFVPGGVNRI----LLATDGDFnvgETDPDELARLVAQkreSGITLSTLGF 137
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 310-346 4.94e-09

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: 4.94e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 3647275    310 CALNTHGCEHICVNdRSGSYHCECYEGYTLNEDRKTC 346
Cdd:pfam14670   1 CSVNNGGCSHLCLN-TPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 352-388 2.66e-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: 46.85  E-value: 2.66e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 3647275    352 CALGTHGCQHICVNdRTGSHHCECYEGYTLNADKKTC 388
Cdd:pfam14670   1 CSVNNGGCSHLCLN-TPGGYTCSCPEGYELQDDGRTC 36
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 83-245 4.74e-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: 50.20  E-value: 4.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275   83 DLVFIIDSSRSVR---PLEFTKVKTFVSRIIDTldigpaDTRVAVVNYASTVKIEFQLQAYTDK--QSLkQAVGRITPlS 157
Cdd:cd01474   6 DLYFVLDKSGSVAanwIEIYDFVEQLVDRFNSP------GLRFSFITFSTRATKILPLTDDSSAiiKGL-EVLKKVTP-S 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275  158 TGTMSGLAIQTAMDEAFTVEAGAREPSSnipkVAIIVTDGR-----PQDQVNEvAARAQASGIELYAVGVDRADMASLKM 232
Cdd:cd01474  78 GQTYIHEGLENANEQIFNRNGGGRETVS----VIIALTDGQlllngHKYPEHE-AKLSRKLGAIVYCVGVTDFLKSQLIN 152

                       170
                ....*....|...
gi 3647275  233 MASEPleEHVFYV 245
Cdd:cd01474 153 IADSK--EYVFPV 163
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 394-430 9.78e-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: 45.31  E-value: 9.78e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 3647275    394 CALGSHGCQHICVsDGAASYHCDCYPGYTLNEDKKTC 430
Cdd:pfam14670   1 CSVNNGGCSHLCL-NTPGGYTCSCPEGYELQDDGRTC 36
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 79-246 3.98e-05

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: 44.31  E-value: 3.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275   79 SRPLDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLdiGPADTrVAVVNYASTV-------KIEFQLQAYTDKQSLKQAVG 151
Cdd:cd01463  11 TSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTL--SDNDF-FNIITFSNEVnpvvpcfNDTLVQATTSNKKVLKEALD 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275  152 RITPLSTGT-MSGL--AIQTAMDEAFTVEAGARepsSNIPKVAIIVTDGRPQ------DQVNEVAARAQASGIELYAVGV 222
Cdd:cd01463  88 MLEAKGIANyTKALefAFSLLLKNLQSNHSGSR---SQCNQAIMLITDGVPEnykeifDKYNWDKNSEIPVRVFTYLIGR 164

                       170       180
                ....*....|....*....|....
gi 3647275  223 DRADMASLKMMASeplEEHVFYVE 246
Cdd:cd01463 165 EVTDRREIQWMAC---ENKGYYSH 185
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 268-304 1.43e-04

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: 39.15  E-value: 1.43e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 3647275    268 CVLGTHQCQHVCISDGEGkHHCECSQGYTLNADKKTC 304
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGG-YTCSCPEGYELQDDGRTC 36
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 81-236 1.14e-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: 39.89  E-value: 1.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275   81 PLDLVFIIDSSRSV--RPLEftKVKTFVSRIIDtlDIGPADtRVAVVNYASTVKIEF-QLQAYTDkQSLKQAVGRITPLS 157
Cdd:cd01461   2 PKEVVFVIDTSGSMsgTKIE--QTKEALLTALK--DLPPGD-YFNIIGFSDTVEEFSpSSVSATA-ENVAAAIEYVNRLQ 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275  158 tgTMSGLAIQTAMDEAFTVeagaREPSSNIPKVAIIVTDGRPQD--QVNEVAARAQASGIELYAVGV-DRADMASLKMMA 234
Cdd:cd01461  76 --ALGGTNMNDALEAALEL----LNSSPGSVPQIILLTDGEVTNesQILKNVREALSGRIRLFTFGIgSDVNTYLLERLA 149


                ..
gi 3647275  235 SE 236
Cdd:cd01461 150 RE 151
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 83-234 4.30e-03

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: 38.45  E-value: 4.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3647275   83 DLVFIIDSSRSVRPLEFTK-VKTFVSRIIDTLDIGPADTRVAVVNYASTVK--IEFQLQAYTDKQSLKQAVGRITPlSTG 159
Cdd:cd01473   2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEKNRdvVPFSDEERYDKNELLKKINDLKN-SYR 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3647275  160 TMSGLAIQTAMDEAFTVEAGAREPSSNIPKVAIIVTDGRPQD----QVNEVAARAQASGIELYAVGVDRADMASLKMMA 234
Cdd:cd01473  81 SGGETYIVEALKYGLKNYTKHGNRRKDAPKVTMLFTDGNDTSaskkELQDISLLYKEENVKLLVVGVGAASENKLKLLA 159
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH