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Conserved domains on  [gi|973201404|ref|XP_015220717|]
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PREDICTED: matrilin-4 isoform X2 [Lepisosteus oculatus]

Protein Classification

matrilin( domain architecture ID 10208606)

matrilin acts as the component of the extracellular matrix of cartilage

CATH:  3.40.50.410
Gene Ontology:  GO:0030198|GO:0005509|GO:0120216
PubMed:  12579041|10830113|12388743|10830110|10367731
SCOP:  3000832

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 ...
 28-247 1.99e-118

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


The actual alignment was detected with superfamily member cd01475:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 224  Bit Score: 349.76  E-value: 1.99e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  28 GPIDLVFIIDSSRSVRPFEFETMRKFMIDIIHTLDVGANATRVGVVQYSSQVQNVFSLKSFTRKADMVKAINEIIPLAQG 107
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 108 TMTGLAIQYAMSVAFSPEEGARRG---VPSVAVIVTDGRPQDRVAEVAAQARDRKIEIYAVGVARADMTSLRAMASPPLK 184
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGserVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 973201404 185 DHVFLVESFDLIHQFGLQFQDKLC-GVDLCTEMDHGCQHICVSSPGSYHCECRAGYTLNTDSKT 247
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICvVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 338-571 1.74e-113

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: 337.05  E-value: 1.74e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 338 IDLVMVIDGSKSVRPQNFELVKQFVNQVVDSLDVSAHGTRVGLVQYSSRVRTEFPLSQYKSAEDIKNAVLKVEYMEKGTM 417
Cdd:cd01475    3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 418 TGLALKHLVENSFSEAEGARPPSKGIPRVGLVFTDGRSQDDITEWAKKAKDAGITMYAVGVGKALEEELREIASEPVDKH 497
Cdd:cd01475   83 TGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLADH 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973201404 498 FFYTTDFTAINQIAENLKLNICaeesqgeiEVKDPCACESLVEFQ---QSTLSTLEQLTQklagmtaRLEDLENQLL 571
Cdd:cd01475  163 VFYVEDFSTIEELTKKFQGKIC--------VVPDLCATLSHVCQQvciSTPGSYLCACTE-------GYALLEDNKT 224
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 295-330 2.38e-10

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: 55.71  E-value: 2.38e-10
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 973201404  295 CNTVEHGCEHRCVSAPGSYHCVCPEGQLLQEDGKSC 330
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 254-289 1.03e-08

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


:

Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 51.09  E-value: 1.03e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 973201404  254 CAGGKHSCEQICVSSPGSYTCRCRAGFYLNQDKMTC 289
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
 
Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 28-247 1.99e-118

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 349.76  E-value: 1.99e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  28 GPIDLVFIIDSSRSVRPFEFETMRKFMIDIIHTLDVGANATRVGVVQYSSQVQNVFSLKSFTRKADMVKAINEIIPLAQG 107
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 108 TMTGLAIQYAMSVAFSPEEGARRG---VPSVAVIVTDGRPQDRVAEVAAQARDRKIEIYAVGVARADMTSLRAMASPPLK 184
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGserVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 973201404 185 DHVFLVESFDLIHQFGLQFQDKLC-GVDLCTEMDHGCQHICVSSPGSYHCECRAGYTLNTDSKT 247
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICvVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 338-571 1.74e-113

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: 337.05  E-value: 1.74e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 338 IDLVMVIDGSKSVRPQNFELVKQFVNQVVDSLDVSAHGTRVGLVQYSSRVRTEFPLSQYKSAEDIKNAVLKVEYMEKGTM 417
Cdd:cd01475    3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 418 TGLALKHLVENSFSEAEGARPPSKGIPRVGLVFTDGRSQDDITEWAKKAKDAGITMYAVGVGKALEEELREIASEPVDKH 497
Cdd:cd01475   83 TGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLADH 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973201404 498 FFYTTDFTAINQIAENLKLNICaeesqgeiEVKDPCACESLVEFQ---QSTLSTLEQLTQklagmtaRLEDLENQLL 571
Cdd:cd01475  163 VFYVEDFSTIEELTKKFQGKIC--------VVPDLCATLSHVCQQvciSTPGSYLCACTE-------GYALLEDNKT 224
VWA pfam00092
von Willebrand factor type A domain;
339-513 3.09e-67

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 215.60  E-value: 3.09e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  339 DLVMVIDGSKSVRPQNFELVKQFVNQVVDSLDVSAHGTRVGLVQYSSRVRTEFPLSQYKSAEDIKNAVLKVEYMEKGTM- 417
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  418 TGLALKHLVENSFSEAEGARPpskGIPRVGLVFTDGRSQD-DITEWAKKAKDAGITMYAVGVGKALEEELREIASEPVDK 496
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARP---GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                         170
                  ....*....|....*..
gi 973201404  497 HFFYTTDFTAINQIAEN 513
Cdd:pfam00092 158 HVFTVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
31-199 5.24e-58

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 191.72  E-value: 5.24e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404   31 DLVFIIDSSRSVRPFEFETMRKFMIDIIHTLDVGANATRVGVVQYSSQVQNVFSLKSFTRKADMVKAINEIIPLAQGTM- 109
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  110 TGLAIQYAMSVAFSPEEGARRGVPSVAVIVTDGRPQD-RVAEVAAQARDRKIEIYAVGVARADMTSLRAMASPPLKDHVF 188
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                         170
                  ....*....|.
gi 973201404  189 LVESFDLIHQF 199
Cdd:pfam00092 161 TVSDFEALEDL 171
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 339-510 1.76e-50

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: 171.87  E-value: 1.76e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404   339 DLVMVIDGSKSVRPQNFELVKQFVNQVVDSLDVSAHGTRVGLVQYSSRVRTEFPLSQYKSAEDIKNAVLKVEY-MEKGTM 417
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404   418 TGLALKHLVENSFSEAEGARPpskGIPRVGLVFTDGRSQD---DITEWAKKAKDAGITMYAVGVGKA-LEEELREIASEP 493
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRR---GAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAP 157

                          170
                   ....*....|....*..
gi 973201404   494 VDKHFFYTTDFTAINQI 510
Cdd:smart00327 158 GGVYVFLPELLDLLIDL 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 31-199 6.98e-49

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: 167.25  E-value: 6.98e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404    31 DLVFIIDSSRSVRPFEFETMRKFMIDIIHTLDVGANATRVGVVQYSSQVQNVFSLKSFTRKADMVKAINEIIPLAQG-TM 109
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGgTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404   110 TGLAIQYAMSVAFSPEEGARRGVPSVAVIVTDGRPQD---RVAEVAAQARDRKIEIYAVGVARA-DMTSLRAMASPPLKD 185
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160

                          170
                   ....*....|....
gi 973201404   186 HVFLVESFDLIHQF 199
Cdd:smart00327 161 YVFLPELLDLLIDL 174
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 338-514 1.59e-16

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 79.60  E-value: 1.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 338 IDLVMVIDGSKSVRPQN-FELVKQFVNQVVDSLDvsaHGTRVGLVQYSSRVRTEFPLSQykSAEDIKNAVLKVEyMEKGT 416
Cdd:COG1240   93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEVLLPLTR--DREALKRALDELP-PGGGT 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 417 MTGLALKHLVEnsfsEAEGARPPSKgipRVGLVFTDGR---SQDDITEWAKKAKDAGITMYAVGVGKAL--EEELREIAS 491
Cdd:COG1240  167 PLGDALALALE----LLKRADPARR---KVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTEAvdEGLLREIAE 239

                        170       180
                 ....*....|....*....|...
gi 973201404 492 EpVDKHFFYTTDFTAINQIAENL 514
Cdd:COG1240  240 A-TGGRYFRADDLSELAAIYREI 261
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 18-167 1.30e-13

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 71.67  E-value: 1.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  18 QRPADSKCKTGPIDLVFIIDSSRSVRPFEFETMRKFMIDIIHTLDVGanaTRVGVVQYSSQVQNVFSLKSFTRKADMVKA 97
Cdd:COG2304   80 QPPKAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPG---DRVSIVTFAGDARVLLPPTPATDRAKILAA 156

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973201404  98 INEIIPlAQGTMTGLAIQYAMSVAfspEEGARRGVPSVAVIVTDGRP------QDRVAEVAAQARDRKIEIYAVGV 167
Cdd:COG2304  157 IDRLQA-GGGTALGAGLELAYELA---RKHFIPGRVNRVILLTDGDAnvgitdPEELLKLAEEAREEGITLTTLGV 228
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 295-330 2.38e-10

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: 55.71  E-value: 2.38e-10
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 973201404  295 CNTVEHGCEHRCVSAPGSYHCVCPEGQLLQEDGKSC 330
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 254-289 1.03e-08

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


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 51.09  E-value: 1.03e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 973201404  254 CAGGKHSCEQICVSSPGSYTCRCRAGFYLNQDKMTC 289
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
248-290 1.81e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.07  E-value: 1.81e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 973201404   248 CSAIDLCAGGkhsceQICVSSPGSYTCRCRAGFylnQDKMTCT 290
Cdd:smart00179   5 CASGNPCQNG-----GTCVNTVGSYRCECPPGY---TDGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 251-282 2.89e-03

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


Pssm-ID: 238011  Cd Length: 38  Bit Score: 35.69  E-value: 2.89e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 973201404 251 IDLCAGGkHSCE--QICVSSPGSYTCRCRAGFYL 282
Cdd:cd00054    2 IDECASG-NPCQngGTCVNTVGSYRCSCPPGYTG 34
EGF_CA smart00179
Calcium-binding EGF-like domain;
289-330 3.33e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 35.30  E-value: 3.33e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 973201404   289 CTMEDLCntvehGCEHRCVSAPGSYHCVCPEGqllQEDGKSC 330
Cdd:smart00179   5 CASGNPC-----QNGGTCVNTVGSYRCECPPG---YTDGRNC 38
 
Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 28-247 1.99e-118

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 349.76  E-value: 1.99e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  28 GPIDLVFIIDSSRSVRPFEFETMRKFMIDIIHTLDVGANATRVGVVQYSSQVQNVFSLKSFTRKADMVKAINEIIPLAQG 107
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 108 TMTGLAIQYAMSVAFSPEEGARRG---VPSVAVIVTDGRPQDRVAEVAAQARDRKIEIYAVGVARADMTSLRAMASPPLK 184
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGserVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 973201404 185 DHVFLVESFDLIHQFGLQFQDKLC-GVDLCTEMDHGCQHICVSSPGSYHCECRAGYTLNTDSKT 247
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICvVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 338-571 1.74e-113

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: 337.05  E-value: 1.74e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 338 IDLVMVIDGSKSVRPQNFELVKQFVNQVVDSLDVSAHGTRVGLVQYSSRVRTEFPLSQYKSAEDIKNAVLKVEYMEKGTM 417
Cdd:cd01475    3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 418 TGLALKHLVENSFSEAEGARPPSKGIPRVGLVFTDGRSQDDITEWAKKAKDAGITMYAVGVGKALEEELREIASEPVDKH 497
Cdd:cd01475   83 TGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLADH 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973201404 498 FFYTTDFTAINQIAENLKLNICaeesqgeiEVKDPCACESLVEFQ---QSTLSTLEQLTQklagmtaRLEDLENQLL 571
Cdd:cd01475  163 VFYVEDFSTIEELTKKFQGKIC--------VVPDLCATLSHVCQQvciSTPGSYLCACTE-------GYALLEDNKT 224
VWA pfam00092
von Willebrand factor type A domain;
339-513 3.09e-67

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 215.60  E-value: 3.09e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  339 DLVMVIDGSKSVRPQNFELVKQFVNQVVDSLDVSAHGTRVGLVQYSSRVRTEFPLSQYKSAEDIKNAVLKVEYMEKGTM- 417
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  418 TGLALKHLVENSFSEAEGARPpskGIPRVGLVFTDGRSQD-DITEWAKKAKDAGITMYAVGVGKALEEELREIASEPVDK 496
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARP---GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                         170
                  ....*....|....*..
gi 973201404  497 HFFYTTDFTAINQIAEN 513
Cdd:pfam00092 158 HVFTVSDFEALEDLQDQ 174
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 338-504 1.27e-63

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: 205.92  E-value: 1.27e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 338 IDLVMVIDGSKSVRPQNFELVKQFVNQVVDSLDVSAHGTRVGLVQYSSRVRTEFPLSQYKSAEDIKNAVLKVEYMEKGTM 417
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 418 TGLALKHLVENSFSEAEGARppsKGIPRVGLVFTDGRSQDDITEWAKKAKDAGITMYAVGVGKALEEELREIASEPVDKH 497
Cdd:cd01472   81 TGKALKYVRENLFTEASGSR---EGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELY 157


                 ....*..
gi 973201404 498 FFYTTDF 504
Cdd:cd01472  158 VFNVADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 339-504 3.28e-60

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: 197.12  E-value: 3.28e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 339 DLVMVIDGSKSVRPQNFELVKQFVNQVVDSLDVSAHGTRVGLVQYSSRVRTEFPLSQYKSAEDIKNAVLKVEYMEKGTMT 418
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 419 GLALKHLVENSFSEAEGARPpskGIPRVGLVFTDGRSQDDITEWAKKAKDAGITMYAVGVGKALEEELREIASEPVDKHF 498
Cdd:cd01482   82 GKALTHVREKNFTPDAGARP---GVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHV 158


                 ....*.
gi 973201404 499 FYTTDF 504
Cdd:cd01482  159 FNVADF 164
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 338-499 4.46e-59

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: 194.05  E-value: 4.46e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 338 IDLVMVIDGSKSVRPQNFELVKQFVNQVVDSLDVSAHGTRVGLVQYSSRVRTEFPLSQYKSAEDIKNAVLKVEYMEK-GT 416
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 417 MTGLALKHLVENSFSEaegaRPPSKGIPRVGLVFTDGRSQD--DITEWAKKAKDAGITMYAVGVGKALEEELREIASEPV 494
Cdd:cd01450   81 NTGKALQYALEQLFSE----SNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156


                 ....*
gi 973201404 495 DKHFF 499
Cdd:cd01450  157 ERHVF 161
VWA pfam00092
von Willebrand factor type A domain;
31-199 5.24e-58

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 191.72  E-value: 5.24e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404   31 DLVFIIDSSRSVRPFEFETMRKFMIDIIHTLDVGANATRVGVVQYSSQVQNVFSLKSFTRKADMVKAINEIIPLAQGTM- 109
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  110 TGLAIQYAMSVAFSPEEGARRGVPSVAVIVTDGRPQD-RVAEVAAQARDRKIEIYAVGVARADMTSLRAMASPPLKDHVF 188
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                         170
                  ....*....|.
gi 973201404  189 LVESFDLIHQF 199
Cdd:pfam00092 161 TVSDFEALEDL 171
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 30-193 4.30e-51

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: 172.80  E-value: 4.30e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  30 IDLVFIIDSSRSVRPFEFETMRKFMIDIIHTLDVGANATRVGVVQYSSQVQNVFSLKSFTRKADMVKAINEIIPLAQGTM 109
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 110 TGLAIQYAMSVAFSPEEGARRGVPSVAVIVTDGRPQDRVAEVAAQARDRKIEIYAVGVARADMTSLRAMASPPLKDHVFL 189
Cdd:cd01472   81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                 ....
gi 973201404 190 VESF 193
Cdd:cd01472  161 VADF 164
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 30-188 1.05e-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: 171.71  E-value: 1.05e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  30 IDLVFIIDSSRSVRPFEFETMRKFMIDIIHTLDVGANATRVGVVQYSSQVQNVFSLKSFTRKADMVKAINEIIPLA-QGT 108
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGgGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 109 MTGLAIQYAMSVAFSPeEGARRGVPSVAVIVTDGRPQDR--VAEVAAQARDRKIEIYAVGVARADMTSLRAMASPPLKDH 186
Cdd:cd01450   81 NTGKALQYALEQLFSE-SNARENVPKVIIVLTDGRSDDGgdPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSERH 159


                 ..
gi 973201404 187 VF 188
Cdd:cd01450  160 VF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 339-510 1.76e-50

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: 171.87  E-value: 1.76e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404   339 DLVMVIDGSKSVRPQNFELVKQFVNQVVDSLDVSAHGTRVGLVQYSSRVRTEFPLSQYKSAEDIKNAVLKVEY-MEKGTM 417
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404   418 TGLALKHLVENSFSEAEGARPpskGIPRVGLVFTDGRSQD---DITEWAKKAKDAGITMYAVGVGKA-LEEELREIASEP 493
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRR---GAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAP 157

                          170
                   ....*....|....*..
gi 973201404   494 VDKHFFYTTDFTAINQI 510
Cdd:smart00327 158 GGVYVFLPELLDLLIDL 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 31-199 6.98e-49

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: 167.25  E-value: 6.98e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404    31 DLVFIIDSSRSVRPFEFETMRKFMIDIIHTLDVGANATRVGVVQYSSQVQNVFSLKSFTRKADMVKAINEIIPLAQG-TM 109
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGgTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404   110 TGLAIQYAMSVAFSPEEGARRGVPSVAVIVTDGRPQD---RVAEVAAQARDRKIEIYAVGVARA-DMTSLRAMASPPLKD 185
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160

                          170
                   ....*....|....
gi 973201404   186 HVFLVESFDLIHQF 199
Cdd:smart00327 161 YVFLPELLDLLIDL 174
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 31-193 2.72e-47

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 162.84  E-value: 2.72e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  31 DLVFIIDSSRSVRPFEFETMRKFMIDIIHTLDVGANATRVGVVQYSSQVQNVFSLKSFTRKADMVKAINEIIPLAQGTMT 110
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 111 GLAIQYAMSVAFSPEEGARRGVPSVAVIVTDGRPQDRVAEVAAQARDRKIEIYAVGVARADMTSLRAMASPPLKDHVFLV 190
Cdd:cd01482   82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFNV 161


                 ...
gi 973201404 191 ESF 193
Cdd:cd01482  162 ADF 164
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 338-510 1.03e-41

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: 148.27  E-value: 1.03e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 338 IDLVMVIDGSKSVRPQNFELVKQFVNQVVDSLDVSAHGTRVGLVQYSSRVRTEFPLSQYKSAEDIKNAVLKVEYMEKGTM 417
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 418 TGLALKHLVENSFSEAEGARPPSKgipRVGLVFTDGRSQDDITEWA--KKAKDAGITMYAVGVGKALE-----EELREIA 490
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDAT---KVLVVITDGESHDDPLLKDviPQAEREGIIRYAIGVGGHFQrensrEELKTIA 157

                        170       180
                 ....*....|....*....|
gi 973201404 491 SEPVDKHFFYTTDFTAINQI 510
Cdd:cd01469  158 SKPPEEHFFNVTDFAALKDI 177
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 339-493 4.60e-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: 129.75  E-value: 4.60e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 339 DLVMVIDGSKSVRPQNFELVKQFVNQVVDSLDVSAHGTRVGLVQYSSRVRTEFPLSQYKSAEDIKNAVLKVEYME-KGTM 417
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGgSQLN 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973201404 418 TGLALKHLVENSFSEAEGARpPSKGIPRVGLVFTDGRSQDDITEWAKKAKDAGITMYAVGVGKALEEELREIASEP 493
Cdd:cd01481   82 TGSALDYVVKNLFTKSAGSR-IEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP 156
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 30-194 2.90e-34

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 127.86  E-value: 2.90e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  30 IDLVFIIDSSRSVRPFEFETMRKFMIDIIHTLDVGANATRVGVVQYSSQVQNVFSLKSFTRKADMVKAINEIIPLAQGTM 109
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 110 TGLAIQYAMSVAFSPEEGARRGVPSVAVIVTDGRPQD--RVAEVAAQARDRKIEIYAVGVARADMTS-----LRAMASPP 182
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDdpLLKDVIPQAEREGIIRYAIGVGGHFQREnsreeLKTIASKP 160

                        170
                 ....*....|..
gi 973201404 183 LKDHVFLVESFD 194
Cdd:cd01469  161 PEEHFFNVTDFA 172
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 338-499 6.00e-34

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: 126.53  E-value: 6.00e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 338 IDLVMVIDGSKSVRPQNFELVKQFVNQVVDSLDVSAHGTRVGLVQYSSRVRTEFPLSQYKSAEDIKNAVLKVEY-MEKGT 416
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 417 MTGLALKHLVENSFSEAegarppSKGIPRVGLVFTDGRSQDDIT---EWAKKAKDAGITMYAVGVG-KALEEELREIASE 492
Cdd:cd00198   81 NIGAALRLALELLKSAK------RPNARRVIILLTDGEPNDGPEllaEAARELRKLGITVYTIGIGdDANEDELKEIADK 154


                 ....*..
gi 973201404 493 PVDKHFF 499
Cdd:cd00198  155 TTGGAVF 161
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 31-193 2.08e-31

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


Pssm-ID: 238758  Cd Length: 165  Bit Score: 119.35  E-value: 2.08e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  31 DLVFIIDSSRSVRPFEFETMRKFMIDIIHTLDVGANATRVGVVQYSSQVQNVFSLKSFTRKADMVKAINEIIPL-AQGTM 109
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRgGSQLN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 110 TGLAIQYAMSVAFSPEEGAR--RGVPSVAVIVTDGRPQDRVAEVAAQARDRKIEIYAVGVARADMTSLRAMASPPlkDHV 187
Cdd:cd01481   82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP--SFV 159


                 ....*.
gi 973201404 188 FLVESF 193
Cdd:cd01481  160 FQVSDF 165
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 30-188 2.89e-30

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 116.13  E-value: 2.89e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  30 IDLVFIIDSSRSVRPFEFETMRKFMIDIIHTLDVGANATRVGVVQYSSQVQNVFSLKSFTRKADMVKAINEIIPLA-QGT 108
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLgGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 109 MTGLAIQYAMSVAFSPeegARRGVPSVAVIVTDGRPQD---RVAEVAAQARDRKIEIYAVGV-ARADMTSLRAMASPPLK 184
Cdd:cd00198   81 NIGAALRLALELLKSA---KRPNARRVIILLTDGEPNDgpeLLAEAARELRKLGITVYTIGIgDDANEDELKEIADKTTG 157


                 ....
gi 973201404 185 DHVF 188
Cdd:cd00198  158 GAVF 161
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 338-506 8.63e-28

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 110.17  E-value: 8.63e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 338 IDLVMVIDGSKSVRPQNFELVKQFVNQVVDSL------DVSAHGTRVGLVQYSSRVRTEFPLSQ-YKSAEDIKNAVLKVE 410
Cdd:cd01480    3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRdIRNYTSLKEAVDNLE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 411 YMEKGTMTGLALKHLVENSFseaegaRPPSKGIPRVGLVFTDGRSQ----DDITEWAKKAKDAGITMYAVGVGKALEEEL 486
Cdd:cd01480   83 YIGGGTFTDCALKYATEQLL------EGSHQKENKFLLVITDGHSDgspdGGIEKAVNEADHLGIKIFFVAVGSQNEEPL 156

                        170       180
                 ....*....|....*....|
gi 973201404 487 REIASEPVDKHffYTTDFTA 506
Cdd:cd01480  157 SRIACDGKSAL--YRENFAE 174
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 339-499 2.39e-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: 102.48  E-value: 2.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 339 DLVMVIDGSKSVRPQnFELVKQFVNQVVDSLDVSAHGTRVGLVQYSSRVRT--EFPLSQYKSAEDIKNAVLKVEYMEKGT 416
Cdd:cd01476    2 DLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 417 MTGLALKHLVeNSFSEAEGARPpskGIPRVGLVFTDGRSQDDITEWAKKAK-DAGITMYAVGVG---KALEEELREIASE 492
Cdd:cd01476   81 ATGAAIEVAL-QQLDPSEGRRE---GIPKVVVVLTDGRSHDDPEKQARILRaVPNIETFAVGTGdpgTVDTEELHSITGN 156


                 ....*..
gi 973201404 493 PvdKHFF 499
Cdd:cd01476  157 E--DHIF 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 31-188 1.64e-24

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


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 100.17  E-value: 1.64e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  31 DLVFIIDSSRSVRPfEFETMRKFMIDIIHTLDVGANATRVGVVQYSSQVQN--VFSLKSFTRKADMVKAINEIIPLAQGT 108
Cdd:cd01476    2 DLLFVLDSSGSVRG-KFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 109 MTGLAIQYAMSVaFSPEEGARRGVPSVAVIVTDGRPQDRVAEVAAQARDRK-IEIYAVGV---ARADMTSLRAMASPPlk 184
Cdd:cd01476   81 ATGAAIEVALQQ-LDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVPnIETFAVGTgdpGTVDTEELHSITGNE-- 157


                 ....
gi 973201404 185 DHVF 188
Cdd:cd01476  158 DHIF 161
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 28-169 3.56e-18

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 82.43  E-value: 3.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  28 GPIDLVFIIDSSRSVRPFEFETMRKFMIDIIHTL------DVGANATRVGVVQYSSQV-------QNVFSLKSFTRKADM 94
Cdd:cd01480    1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQeveagflRDIRNYTSLKEAVDN 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 973201404  95 VKAINEiiplaqGTMTGLAIQYAMSVAFspeEGARRGVPSVAVIVTDGRPQ---DRVAEVAAQARDRK-IEIYAVGVAR 169
Cdd:cd01480   81 LEYIGG------GTFTDCALKYATEQLL---EGSHQKENKFLLVITDGHSDgspDGGIEKAVNEADHLgIKIFFVAVGS 150
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 338-514 1.59e-16

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 79.60  E-value: 1.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 338 IDLVMVIDGSKSVRPQN-FELVKQFVNQVVDSLDvsaHGTRVGLVQYSSRVRTEFPLSQykSAEDIKNAVLKVEyMEKGT 416
Cdd:COG1240   93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEVLLPLTR--DREALKRALDELP-PGGGT 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 417 MTGLALKHLVEnsfsEAEGARPPSKgipRVGLVFTDGR---SQDDITEWAKKAKDAGITMYAVGVGKAL--EEELREIAS 491
Cdd:COG1240  167 PLGDALALALE----LLKRADPARR---KVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTEAvdEGLLREIAE 239

                        170       180
                 ....*....|....*....|...
gi 973201404 492 EpVDKHFFYTTDFTAINQIAENL 514
Cdd:COG1240  240 A-TGGRYFRADDLSELAAIYREI 261
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 338-479 1.26e-15

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 75.11  E-value: 1.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 338 IDLVMVIDGSKSVRPQN-FELVKQFVNQVVDSLDVSAHGTRVGLVQYSSRVRTEFPLSQYKS-----AEDIKNAVLKVEY 411
Cdd:cd01471    1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNStnkdlALNAIRALLSLYY 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 412 MEKGTMTGLALKHLVENSFSEAeGARPpskGIPRVGLVFTDGRSQDD--ITEWAKKAKDAGITMYAVGVG 479
Cdd:cd01471   81 PNGSTNTTSALLVVEKHLFDTR-GNRE---NAPQLVIIMTDGIPDSKfrTLKEARKLRERGVIIAVLGVG 146
VWA_2 pfam13519
von Willebrand factor type A domain;
32-139 2.68e-14

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 68.86  E-value: 2.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404   32 LVFIIDSSRSVR-----PFEFETMRKFMIDIIHTLdvgaNATRVGVVQYSSQVQNVFSLKSftRKADMVKAINEIIPLAQ 106
Cdd:pfam13519   1 LVFVLDTSGSMRngdygPTRLEAAKDAVLALLKSL----PGDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 973201404  107 GTMTGLAIQYAMSVAFspeeGARRGVPSVAVIV 139
Cdd:pfam13519  75 GTNLAAALQLARAALK----HRRKNQPRRIVLI 103
VWA_2 pfam13519
von Willebrand factor type A domain;
340-438 3.88e-14

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 68.47  E-value: 3.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  340 LVMVIDGSKSVR-----PQNFELVKQFVNQVVDSLDvsahGTRVGLVQYSSRVRTEFPLSqyKSAEDIKNAVLKVEYMEK 414
Cdd:pfam13519   1 LVFVLDTSGSMRngdygPTRLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                          90       100
                  ....*....|....*....|....
gi 973201404  415 GTMTGLALKHLVENSFSEAEGARP 438
Cdd:pfam13519  75 GTNLAAALQLARAALKHRRKNQPR 98
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 18-167 1.30e-13

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 71.67  E-value: 1.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  18 QRPADSKCKTGPIDLVFIIDSSRSVRPFEFETMRKFMIDIIHTLDVGanaTRVGVVQYSSQVQNVFSLKSFTRKADMVKA 97
Cdd:COG2304   80 QPPKAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPG---DRVSIVTFAGDARVLLPPTPATDRAKILAA 156

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973201404  98 INEIIPlAQGTMTGLAIQYAMSVAfspEEGARRGVPSVAVIVTDGRP------QDRVAEVAAQARDRKIEIYAVGV 167
Cdd:COG2304  157 IDRLQA-GGGTALGAGLELAYELA---RKHFIPGRVNRVILLTDGDAnvgitdPEELLKLAEEAREEGITLTTLGV 228
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 338-490 1.46e-13

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 71.29  E-value: 1.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 338 IDLVMVIDGSKSVRPQNFELVKQFVNQVVDSLDvsaHGTRVGLVQYSSRVRTEFPLSQYKSAEDIKNAVLKVEyMEKGT- 416
Cdd:COG2304   92 LNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLR---PGDRVSIVTFAGDARVLLPPTPATDRAKILAAIDRLQ-AGGGTa 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 417 -MTGL--ALKHLVENsfseaegarPPSKGIPRVgLVFTDGR------SQDDITEWAKKAKDAGITMYAVGVGKAL-EEEL 486
Cdd:COG2304  168 lGAGLelAYELARKH---------FIPGRVNRV-ILLTDGDanvgitDPEELLKLAEEAREEGITLTTLGVGSDYnEDLL 237


                 ....
gi 973201404 487 REIA 490
Cdd:COG2304  238 ERLA 241
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 333-521 1.93e-13

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: 69.08  E-value: 1.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 333 CRSAnIDLVMVIDGSKSVR---PQNFELVKQFVNQVVDSldvsahGTRVGLVQYSSRVRTEFPLSQY-----KSAEDIKN 404
Cdd:cd01474    1 CAGH-FDLYFVLDKSGSVAanwIEIYDFVEQLVDRFNSP------GLRFSFITFSTRATKILPLTDDssaiiKGLEVLKK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 405 AVLKVE-YMEKGtmtglaLKHLVENSFSEAEGARPPSKGIprvgLVFTDGRSQDDI----TEWAKKAKDAGITMYAVGVG 479
Cdd:cd01474   74 VTPSGQtYIHEG------LENANEQIFNRNGGGRETVSVI----IALTDGQLLLNGhkypEHEAKLSRKLGAIVYCVGVT 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 973201404 480 KALEEELREIASEPvdKHFFYTTD-FTAINQIAENLKLNICAE 521
Cdd:cd01474  144 DFLKSQLINIADSK--EYVFPVTSgFQALSGIIESVVKKACIE 184
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 26-179 3.11e-13

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: 69.97  E-value: 3.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  26 KTGPIDLVFIIDSSRSVRPFE-FETMRKFMIDIIHTLDVGanaTRVGVVQYSSQvqnVFSLKSFTRKADMVK-AINEiIP 103
Cdd:COG1240   89 PQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPR---DRVGLVAFGGE---AEVLLPLTRDREALKrALDE-LP 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 104 LAQGTMTGLAIQYAMSVAFSPEEGARRgvpsVAVIVTDGRP---QDRVAEVAAQARDRKIEIYAVGV--ARADMTSLRAM 178
Cdd:COG1240  162 PGGGTPLGDALALALELLKRADPARRK----VIVLLTDGRDnagRIDPLEAAELAAAAGIRIYTIGVgtEAVDEGLLREI 237


                 .
gi 973201404 179 A 179
Cdd:COG1240  238 A 238
Matrilin_ccoil pfam10393
Trimeric coiled-coil oligomerization domain of matrilin; This short domain is a coiled coil ...
 528-570 2.48e-11

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: 58.52  E-value: 2.48e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 973201404  528 EVKDPCACESLVEFQQSTLSTLEQLTQKLAGMTARLEDLENQL 570
Cdd:pfam10393   1 VEEDPCKCEAIVAFQTKVESEIQALTTKLEEVTKRIEALENRL 43
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 213-248 1.31e-10

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: 56.48  E-value: 1.31e-10
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 973201404  213 CTEMDHGCQHICVSSPGSYHCECRAGYTLNTDSKTC 248
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 338-502 1.41e-10

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: 60.36  E-value: 1.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 338 IDLVMVIDGSKSVRPQNFELVKQFVNQVVDSLDVSahgTRVGLVQYSSRVRTEFPLSQYKSAEDIKNAVlkvEYMEKGTM 417
Cdd:cd01465    1 LNLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPD---DRLAIVTYDGAAETVLPATPVRDKAAILAAI---DRLTAGGS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 418 TGLALKhlVENSFSEAEGARPPsKGIPRVgLVFTDGRSQDDITEW------AKKAKDAGITMYAVGVGKALEEELREIAS 491
Cdd:cd01465   75 TAGGAG--IQLGYQEAQKHFVP-GGVNRI-LLATDGDFNVGETDPdelarlVAQKRESGITLSTLGFGDNYNEDLMEAIA 150

                        170
                 ....*....|.
gi 973201404 492 EPVDKHFFYTT 502
Cdd:cd01465  151 DAGNGNTAYID 161
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 295-330 2.38e-10

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: 55.71  E-value: 2.38e-10
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 973201404  295 CNTVEHGCEHRCVSAPGSYHCVCPEGQLLQEDGKSC 330
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
29-181 1.34e-09

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 58.01  E-value: 1.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  29 PIDLVFIIDSSRSVRPFEFETMRKFMIDIIHTL--DVGANAT-RVGVVQYSSQVQNVF---SLKSFTrkadmvkaINEII 102
Cdd:COG4245    5 RLPVYLLLDTSGSMSGEPIEALNEGLQALIDELrqDPYALETvEVSVITFDGEAKVLLpltDLEDFQ--------PPDLS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 103 plAQG-TMTGLAIQYAM-----SVAFSPEEGARRGVPSVaVIVTDGRPQDRVAEVAAQA-----RDRKIEIYAVGV-ARA 170
Cdd:COG4245   77 --ASGgTPLGAALELLLdlierRVQKYTAEGKGDWRPVV-FLITDGEPTDSDWEAALQRlkdgeAAKKANIFAIGVgPDA 153

                        170
                 ....*....|.
gi 973201404 171 DMTSLRAMASP 181
Cdd:COG4245  154 DTEVLKQLTDP 164
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 30-167 6.85e-09

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 55.85  E-value: 6.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  30 IDLVFIIDSSRSVRPF-EFETMRKFMIDIIHTLDVGANATRVGVVQYSSQVQNVFSLKSF--TRKADMVKAINEI--IPL 104
Cdd:cd01471    1 LDLYLLVDGSGSIGYSnWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPnsTNKDLALNAIRALlsLYY 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 973201404 105 AQG-TMTGLAIQYAMSVAFSPeEGARRGVPSVAVIVTDGRPQD--RVAEVAAQARDRKIEIYAVGV 167
Cdd:cd01471   81 PNGsTNTTSALLVVEKHLFDT-RGNRENAPQLVIIMTDGIPDSkfRTLKEARKLRERGVIIAVLGV 145
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 337-509 9.96e-09

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: 55.37  E-value: 9.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 337 NIDLVMviDGSKSVRPQNFELVKQFVNQVVD---SLDVSAhgtRVGLVQYSSRVRTEFPLSQYKSAEdiKNAVLK----V 409
Cdd:cd01470    2 NIYIAL--DASDSIGEEDFDEAKNAIKTLIEkisSYEVSP---RYEIISYASDPKEIVSIRDFNSND--ADDVIKrledF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 410 EYMEKGTMTG----LALKHLVENSFSEAEGARPPSKGIPRVGLVFTDGRSQ---------DDITEWAKKAKDAGIT---- 472
Cdd:cd01470   75 NYDDHGDKTGtntaAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNmggsplptvDKIKNLVYKNNKSDNPredy 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 973201404 473 --MYAVGVGKAL-EEELREIASE-PVDKHFFYTTDFTAINQ 509
Cdd:cd01470  155 ldVYVFGVGDDVnKEELNDLASKkDNERHFFKLKDYEDLQE 195
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 254-289 1.03e-08

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


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 51.09  E-value: 1.03e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 973201404  254 CAGGKHSCEQICVSSPGSYTCRCRAGFYLNQDKMTC 289
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 339-519 2.84e-08

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 53.86  E-value: 2.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 339 DLVMVIDGSKSVRPQNFEL-VKQFVNQVVDSLDVSAHGTRVGLVQYSSRVRTEFPLSQyKSAEDIKNAVLKVEYMEKGTM 417
Cdd:cd01473    2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSD-EERYDKNELLKKINDLKNSYR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 418 TGL------ALKHLVENSFSEaEGARppsKGIPRVGLVFTDG----RSQDDITEWAKKAKDAGITMYAVGVGKALEEELR 487
Cdd:cd01473   81 SGGetyiveALKYGLKNYTKH-GNRR---KDAPKVTMLFTDGndtsASKKELQDISLLYKEENVKLLVVGVGAASENKLK 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 973201404 488 EIA---SEPVDKHFFYTTDFTAINQIAENLKLNIC 519
Cdd:cd01473  157 LLAgcdINNDNCPNVIKTEWNNLNGISKFLTDKIC 191
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 338-503 3.32e-08

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 53.49  E-value: 3.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 338 IDLVMVIDGSKS------VRPQNFELVKQFVNQVVDSLDvsahGTRVGLVQYSSRVRTEFPLSQ-YKSA----EDIKNAV 406
Cdd:cd01467    3 RDIMIALDVSGSmlaqdfVKPSRLEAAKEVLSDFIDRRE----NDRIGLVVFAGAAFTQAPLTLdRESLkellEDIKIGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 407 LkveymEKGTMTG----LALKHLvensfseaegarPPSKGIPRVGLVFTDGRS-QDDITE--WAKKAKDAGITMYAVGVG 479
Cdd:cd01467   79 A-----GQGTAIGdaigLAIKRL------------KNSEAKERVIVLLTDGENnAGEIDPatAAELAKNKGVRIYTIGVG 141

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 973201404 480 KAL------------EEELREIASEpVDKHFFYTTD 503
Cdd:cd01467  142 KSGsgpkpdgstildEDSLVEIADK-TGGRIFRALD 176
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 30-168 1.06e-06

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: 48.81  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  30 IDLVFIIDSSRSVRPFEFETMRKFMIDIIHTLDvgaNATRVGVVQYSSQVQNVFSLKSFTRKADMVKAINEIIPlAQGTM 109
Cdd:cd01465    1 LNLVFVIDRSGSMDGPKLPLVKSALKLLVDQLR---PDDRLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTA-GGSTA 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973201404 110 TGLAIQYAMSVAfspEEGARRGVPSVAVIVTDGRPQ------DRVAEVAAQARDRKIEIYAVGVA 168
Cdd:cd01465   77 GGAGIQLGYQEA---QKHFVPGGVNRILLATDGDFNvgetdpDELARLVAQKRESGITLSTLGFG 138
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 338-491 5.59e-06

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: 47.42  E-value: 5.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 338 IDLVMVIDGSKSVRPQNFELVKQFVNQVVDSLDVSAHG------TRVGLVQYSSRVRTEFPLSQYKSAEDIKN----AVL 407
Cdd:cd01477   20 LDIVFVVDNSKGMTQGGLWQVRATISSLFGSSSQIGTDyddprsTRVGLVTYNSNATVVADLNDLQSFDDLYSqiqgSLT 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 408 KVE-----YMEKGTmtgLALKHLVENSFseaEGARppsKGIPRVGLVFT---DGRSQDDITEWAKKAKDAGITMYAVGVG 479
Cdd:cd01477  100 DVSstnasYLDTGL---QAAEQMLAAGK---RTSR---ENYKKVVIVFAsdyNDEGSNDPRPIAARLKSTGIAIITVAFT 170

                        170
                 ....*....|....*.
gi 973201404 480 K----ALEEELREIAS 491
Cdd:cd01477  171 QdessNLLDKLGKIAS 186
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 28-192 1.35e-05

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


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 45.96  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  28 GPIDLVFIIDSSRSVRPFEFEtMRKFMIDIIHTLDvgANATRVGVVQYSSQVQNVFSLKSFTRKADM-VKAINEIIPLAQ 106
Cdd:cd01474    3 GHFDLYFVLDKSGSVAANWIE-IYDFVEQLVDRFN--SPGLRFSFITFSTRATKILPLTDDSSAIIKgLEVLKKVTPSGQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 107 gTMTGLAIQYAMSVAFSPEEGARRgVPSVAVIVTDGRPQDRV----AEVAAQARDRKIEIYAVGVARADMTSLRAMASPP 182
Cdd:cd01474   80 -TYIHEGLENANEQIFNRNGGGRE-TVSVIIALTDGQLLLNGhkypEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSK 157

                        170
                 ....*....|
gi 973201404 183 lkDHVFLVES 192
Cdd:cd01474  158 --EYVFPVTS 165
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 31-179 2.28e-05

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 45.39  E-value: 2.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  31 DLVFIIDSSRSVR--PFEFETMRkFMIDIIHTLDVGANATRVGVVQYSSQVQNV--FSLKSFTRKADMVKAINEiipLAQ 106
Cdd:cd01473    2 DLTLILDESASIGysNWRKDVIP-FTEKIINNLNISKDKVHVGILLFAEKNRDVvpFSDEERYDKNELLKKIND---LKN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 107 GTMTGL------AIQYAMSvAFSPEEGARRGVPSVAVIVTDGR---PQDR-VAEVAAQARDRKIEIYAVGVARADMTSLR 176
Cdd:cd01473   78 SYRSGGetyiveALKYGLK-NYTKHGNRRKDAPKVTMLFTDGNdtsASKKeLQDISLLYKEENVKLLVVGVGAASENKLK 156


                 ...
gi 973201404 177 AMA 179
Cdd:cd01473  157 LLA 159
EGF_CA smart00179
Calcium-binding EGF-like domain;
210-248 2.32e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 41.46  E-value: 2.32e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 973201404   210 VDLCtEMDHGCQH--ICVSSPGSYHCECRAGYtlnTDSKTC 248
Cdd:smart00179   2 IDEC-ASGNPCQNggTCVNTVGSYRCECPPGY---TDGRNC 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 210-243 3.89e-05

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


Pssm-ID: 238011  Cd Length: 38  Bit Score: 41.08  E-value: 3.89e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 973201404 210 VDLCtEMDHGCQH--ICVSSPGSYHCECRAGYTLNT 243
Cdd:cd00054    2 IDEC-ASGNPCQNggTCVNTVGSYRCSCPPGYTGRN 36
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 341-494 7.75e-05

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: 43.48  E-value: 7.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 341 VMVIDGSKSVRPQNFELVKQFVNQVVDSLDVSAHGTR---VGLVQYSSRVRTEFPLSqyksaeDIKNAVLKVEYMEKGTM 417
Cdd:cd01464    7 YLLLDTSGSMAGEPIEALNQGLQMLQSELRQDPYALEsveISVITFDSAARVIVPLT------PLESFQPPRLTASGGTS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404 418 TGLALK---HLVENSFSEAEGARppsKGIPRvGLVF--TDGRSQDDITEWAKK---AKDAGITMYAVGVG-KALEEELRE 488
Cdd:cd01464   81 MGAALElalDCIDRRVQRYRADQ---KGDWR-PWVFllTDGEPTDDLTAAIERikeARDSKGRIVACAVGpKADLDTLKQ 156


                 ....*.
gi 973201404 489 IASEPV 494
Cdd:cd01464  157 ITEGVP 162
EGF_CA pfam07645
Calcium-binding EGF domain;
251-279 1.19e-04

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 39.53  E-value: 1.19e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 973201404  251 IDLCAGGKHSCEQ--ICVSSPGSYTCRCRAG 279
Cdd:pfam07645   2 VDECATGTHNCPAntVCVNTIGSFECRCPDG 32
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 215-243 9.02e-04

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 37.07  E-value: 9.02e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 973201404 215 EMDHGCQH--ICVSSPGSYHCECRAGYTLNT 243
Cdd:cd00053    3 AASNPCSNggTCVNTPGSYRCVCPPGYTGDR 33
EGF smart00181
Epidermal growth factor-like domain;
218-249 1.24e-03

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 36.73  E-value: 1.24e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 973201404   218 HGCQH-ICVSSPGSYHCECRAGYTLNtdsKTCS 249
Cdd:smart00181   6 GPCSNgTCINTPGSYTCSCPPGYTGD---KRCE 35
EGF_CA smart00179
Calcium-binding EGF-like domain;
248-290 1.81e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.07  E-value: 1.81e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 973201404   248 CSAIDLCAGGkhsceQICVSSPGSYTCRCRAGFylnQDKMTCT 290
Cdd:smart00179   5 CASGNPCQNG-----GTCVNTVGSYRCECPPGY---TDGRNCE 39
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
 232-252 2.30e-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: 35.46  E-value: 2.30e-03
                          10        20
                  ....*....|....*....|.
gi 973201404  232 HCECRAGYTLNTDSKTCSAID 252
Cdd:pfam12662   1 TCSCPPGYQLDPDGRTCVDID 21
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 30-168 2.47e-03

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


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 38.91  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  30 IDLVFIIDSSRSVRPFEFETMRKFMIDIIHTLdvgANATRVGVVQYSSQVQNVFSLKSFTRKAD-MVKAINEIIPLAQGT 108
Cdd:cd01466    1 VDLVAVLDVSGSMAGDKLQLVKHALRFVISSL---GDADRLSIVTFSTSAKRLSPLRRMTAKGKrSAKRVVDGLQAGGGT 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 973201404 109 MTGLAIQYAMSVAfspeEGARRGVPSVAVIV-TDGRPQDrvAEVAAQARDRKIEIYAVGVA 168
Cdd:cd01466   78 NVVGGLKKALKVL----GDRRQKNPVASIMLlSDGQDNH--GAVVLRADNAPIPIHTFGLG 132
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 251-282 2.89e-03

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


Pssm-ID: 238011  Cd Length: 38  Bit Score: 35.69  E-value: 2.89e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 973201404 251 IDLCAGGkHSCE--QICVSSPGSYTCRCRAGFYL 282
Cdd:cd00054    2 IDECASG-NPCQngGTCVNTVGSYRCSCPPGYTG 34
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 70-195 3.22e-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: 3.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973201404  70 VGVVQYSSQVQNVfslksftrkADMVKAINEIIPL--AQG-TMTGLAIQYAMsvafspEEGARRGVPSVA---------- 136
Cdd:cd01464   47 ISVITFDSAARVI---------VPLTPLESFQPPRltASGgTSMGAALELAL------DCIDRRVQRYRAdqkgdwrpwv 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973201404 137 VIVTDGRPQDRV---AEVAAQARDRKIEIYAVGV-ARADMTSLRAMAS--PPLKDHVFLVESFDL 195
Cdd:cd01464  112 FLLTDGEPTDDLtaaIERIKEARDSKGRIVACAVgPKADLDTLKQITEgvPLLDDALSGLNFFKW 176
EGF_CA smart00179
Calcium-binding EGF-like domain;
289-330 3.33e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 35.30  E-value: 3.33e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 973201404   289 CTMEDLCntvehGCEHRCVSAPGSYHCVCPEGqllQEDGKSC 330
Cdd:smart00179   5 CASGNPC-----QNGGTCVNTVGSYRCECPPG---YTDGRNC 38
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
 213-242 3.36e-03

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


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 35.27  E-value: 3.36e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 973201404  213 CTEMDHGC-QH-ICVSSPGSYHCECRAGYTLN 242
Cdd:pfam12947   1 CSDNNGGChPNaTCTNTGGSFTCTCNDGYTGD 32
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 248-283 6.66e-03

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 34.76  E-value: 6.66e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 973201404 248 CSAIDLCAGGkhsceQICVSSPGSYTCRCRAGFYLN 283
Cdd:cd00053    2 CAASNPCSNG-----GTCVNTPGSYRCVCPPGYTGD 32
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 217-243 7.93e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 34.28  E-value: 7.93e-03
                          10        20
                  ....*....|....*....|....*....
gi 973201404  217 DHGCQH--ICVSSPGSYHCECRAGYTLNT 243
Cdd:pfam00008   3 PNPCSNggTCVDTPGGYTCICPEGYTGKR 31
 
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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