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Conserved domains on  [gi|171846231|ref|NP_034899|]
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cartilage matrix protein precursor [Mus musculus]

Protein Classification

cartilage matrix protein( domain architecture ID 10107140)

cartilage matrix protein is a major component of the extracellular matrix of non-articular cartilage

CATH:  3.40.50.410
Gene Ontology:  GO:0030198|GO:0002062|GO:0005509
PubMed:  10830113|12388743|12579041
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 42-265 9.50e-136

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: 390.98  E-value: 9.50e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  42 RPTDLVFVVDSSRSVRPVEFEKVKVFLSQVIESLDVGPNATRVGLVNYASTVKPEFPLRAHGSKASLLQAVRRIQPLSTG 121
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 122 TMTGLALQFAITKALSDAEGGRARSPDISKVVIVVTDGRPQDSVRDVSERARASGIELFAIGVGRVDKATLRQIASEPQD 201
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 171846231 202 EHVDYVESYNVIEKLAKKFQEAFCVVSDLCATGDHDCEQLCVSSPGSYTCACHEGFTLNSDGKT 265
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 276-499 6.56e-122

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: 355.92  E-value: 6.56e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 276 SATDLVFLIDGSKSVRPENFELVKKFINQIVDTLDVSDRLAQVGLVQYSSSIRQEFPLGRFHTKKDIKAAVRNMSYMEKG 355
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 356 TMTGAALKYLIDNSFTVSSGARPGAQ---KVGIVFTDGRSQDYINDAARKAKDLGFKMFAVGVGNAVEEELREIASEPVA 432
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGSErvpRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171846231 433 DHYFYTADFKTINQIGKKLQKQICVEEDPCACESILKFEAKVEGLLQAltrkLEAVSGRLAVLENRI 499
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICVVPDLCATLSHVCQQVCISTPGSY----LCACTEGYALLEDNK 223
 
Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 42-265 9.50e-136

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: 390.98  E-value: 9.50e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  42 RPTDLVFVVDSSRSVRPVEFEKVKVFLSQVIESLDVGPNATRVGLVNYASTVKPEFPLRAHGSKASLLQAVRRIQPLSTG 121
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 122 TMTGLALQFAITKALSDAEGGRARSPDISKVVIVVTDGRPQDSVRDVSERARASGIELFAIGVGRVDKATLRQIASEPQD 201
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 171846231 202 EHVDYVESYNVIEKLAKKFQEAFCVVSDLCATGDHDCEQLCVSSPGSYTCACHEGFTLNSDGKT 265
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 276-499 6.56e-122

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: 355.92  E-value: 6.56e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 276 SATDLVFLIDGSKSVRPENFELVKKFINQIVDTLDVSDRLAQVGLVQYSSSIRQEFPLGRFHTKKDIKAAVRNMSYMEKG 355
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 356 TMTGAALKYLIDNSFTVSSGARPGAQ---KVGIVFTDGRSQDYINDAARKAKDLGFKMFAVGVGNAVEEELREIASEPVA 432
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGSErvpRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171846231 433 DHYFYTADFKTINQIGKKLQKQICVEEDPCACESILKFEAKVEGLLQAltrkLEAVSGRLAVLENRI 499
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICVVPDLCATLSHVCQQVCISTPGSY----LCACTEGYALLEDNK 223
VWA pfam00092
von Willebrand factor type A domain;
279-447 1.14e-67

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 214.83  E-value: 1.14e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  279 DLVFLIDGSKSVRPENFELVKKFINQIVDTLDVSDRLAQVGLVQYSSSIRQEFPLGRFHTKKDIKAAVRNMSYMEKGTM- 357
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  358 TGAALKYLIDNSFTVSSGARPGAQKVGIVFTDGRSQDY-INDAARKAKDLGFKMFAVGVGNAVEEELREIASEPVADHYF 436
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                         170
                  ....*....|.
gi 171846231  437 YTADFKTINQI 447
Cdd:pfam00092 161 TVSDFEALEDL 171
VWA pfam00092
von Willebrand factor type A domain;
45-219 6.90e-63

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 202.51  E-value: 6.90e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231   45 DLVFVVDSSRSVRPVEFEKVKVFLSQVIESLDVGPNATRVGLVNYASTVKPEFPLRAHGSKASLLQAVRRIQPLSTGTM- 123
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  124 TGLALQFAITKALSDAEGGRarsPDISKVVIVVTDGRPQD-SVRDVSERARASGIELFAIGVGRVDKATLRQIASEPQDE 202
Cdd:pfam00092  81 TGKALKYALENLFSSAAGAR---PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                         170
                  ....*....|....*..
gi 171846231  203 HVDYVESYNVIEKLAKK 219
Cdd:pfam00092 158 HVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 279-447 1.72e-52

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: 175.34  E-value: 1.72e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231   279 DLVFLIDGSKSVRPENFELVKKFINQIVDTLDVSDRLAQVGLVQYSSSIRQEFPLGRFHTKKDIKAAVRNMSY-MEKGTM 357
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231   358 TGAALKYLIDNSFTVSSGARPGAQKVGIVFTDGRSQDYIND---AARKAKDLGFKMFAVGVGNAV-EEELREIASEPVAD 433
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDllkAAKELKRSGVKVFVVGVGNDVdEEELKKLASAPGGV 160

                          170
                   ....*....|....
gi 171846231   434 HYFYTADFKTINQI 447
Cdd:smart00327 161 YVFLPELLDLLIDL 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 45-208 4.68e-46

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 158.39  E-value: 4.68e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231    45 DLVFVVDSSRSVRPVEFEKVKVFLSQVIESLDVGPNATRVGLVNYASTVKPEFPLRAHGSKASLLQAVRRIQPLSTG-TM 123
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGgTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231   124 TGLALQFAITKALSDAEGGRarsPDISKVVIVVTDGRPQDS---VRDVSERARASGIELFAIGVGR-VDKATLRQIASEP 199
Cdd:smart00327  81 LGAALQYALENLFSKSAGSR---RGAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNdVDEEELKKLASAP 157


                   ....*....
gi 171846231   200 QDEHVDYVE 208
Cdd:smart00327 158 GGVYVFLPE 166
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 40-198 4.14e-20

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: 90.00  E-value: 4.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  40 RTRPTDLVFVVDSSRSVRPVE-FEKVKVFLSQVIESLDVGpnaTRVGLVNYASTVKPEFPLRAhgSKASLLQAVRRIQPl 118
Cdd:COG1240   89 PQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPR---DRVGLVAFGGEAEVLLPLTR--DREALKRALDELPP- 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 119 STGTMTGLALQFAITKAlsdaeggRARSPDISKVVIVVTDGRPQDSVRD---VSERARASGIELFAIGVG--RVDKATLR 193
Cdd:COG1240  163 GGGTPLGDALALALELL-------KRADPARRKVIVLLTDGRDNAGRIDpleAAELAAAAGIRIYTIGVGteAVDEGLLR 235


                 ....*
gi 171846231 194 QIASE 198
Cdd:COG1240  236 EIAEA 240
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 270-451 7.56e-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: 77.29  E-value: 7.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 270 RGGGSGSATDLVFLIDGSKSVRPEN-FELVKKFINQIVDTLDVSDRlaqVGLVQYSSSIRQEFPLGRfhTKKDIKAAVRN 348
Cdd:COG1240   85 ALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRDR---VGLVAFGGEAEVLLPLTR--DREALKRALDE 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 349 MSyMEKGTMTGAALKYLIDnsftVSSGARPGAQKVGIVFTDGR---SQDYINDAARKAKDLGFKMFAVGVGNAV--EEEL 423
Cdd:COG1240  160 LP-PGGGTPLGDALALALE----LLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTEAvdEGLL 234

                        170       180
                 ....*....|....*....|....*...
gi 171846231 424 REIASEPVAdHYFYTADFKTINQIGKKL 451
Cdd:COG1240  235 REIAEATGG-RYFRADDLSELAAIYREI 261
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 43-196 8.29e-08

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 53.85  E-value: 8.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231   43 PTDLVFVVDSSRSVRPV---EFEKVKVFLSQVIesldvGPNaTRVGLVNYASTVKPEFPLraHGSKASLLQAVRRIQPLS 119
Cdd:TIGR03436  53 PLTVGLVIDTSGSMRNDldrARAAAIRFLKTVL-----RPN-DRVFVVTFNTRLRLLQDF--TSDPRLLEAALNRLKPPL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  120 TGTM----------TGLALQFAIT-KALSDAEGGRARSPDiSKVVIVVTDG---RPQDSVRDVSERARASGIELFAIGVG 185
Cdd:TIGR03436 125 RTDYnssgafvrdgGGTALYDAITlAALEQLANALAGIPG-RKALIVISDGgdnRSRDTLERAIDAAQRADVAIYSIDAR 203

                         170
                  ....*....|.
gi 171846231  186 RVDKATLRQIA 196
Cdd:TIGR03436 204 GLRAPDLGAGA 214
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 279-458 4.34e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 46.11  E-value: 4.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 279 DLVFLIDGSKSVRPENF-ELVKKFINQIVDTLDVSDRLAQVGLVQYSSSIRQEFPLGRFHTKKDIKA--AVRNM--SYME 353
Cdd:PTZ00441  44 DLYLLVDGSGSIGYHNWiTHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASKDKEQAliIVKSLrkTYLP 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 354 KGT--MTGAAL---KYLIDNSftvssgARPGAQKVGIVFTDGrSQDYINDA---ARKAKDLGFKMFAVGVGNAVEEEL-R 424
Cdd:PTZ00441 124 YGKtnMTDALLevrKHLNDRV------NRENAIQLVILMTDG-IPNSKYRAleeSRKLKDRNVKLAVIGIGQGINHQFnR 196

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 171846231 425 EIA----SEPVADHYFYTADFKTINQIgKKLQKQICVE 458
Cdd:PTZ00441 197 LLAgcrpREGKCKFYSDADWEEAKNLI-KPFIAKVCTE 233
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 45-251 1.50e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 44.18  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  45 DLVFVVDSSRSV-RPVEFEKVKVFLSQVIESLDVGPNATRVGLVNYASTVKPEFPLRAHGS--KASLLQAVRRIQ----P 117
Cdd:PTZ00441  44 DLYLLVDGSGSIgYHNWITHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASkdKEQALIIVKSLRktylP 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 118 LSTGTMTGLALQfaITKALSDaeggRARSPDISKVVIVVTDGRPqDSVRDVSERARA---SGIELFAIGVGR-VDKATLR 193
Cdd:PTZ00441 124 YGKTNMTDALLE--VRKHLND----RVNRENAIQLVILMTDGIP-NSKYRALEESRKlkdRNVKLAVIGIGQgINHQFNR 196

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 171846231 194 QIAS-EPQDEHVDYVES--YNVIEKLAKKFQEAFCVVSDLCATgdhdCEQLCVSSPGSYTC 251
Cdd:PTZ00441 197 LLAGcRPREGKCKFYSDadWEEAKNLIKPFIAKVCTEVERTAS----CGPWDEWTPCSVTC 253
 
Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 42-265 9.50e-136

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: 390.98  E-value: 9.50e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  42 RPTDLVFVVDSSRSVRPVEFEKVKVFLSQVIESLDVGPNATRVGLVNYASTVKPEFPLRAHGSKASLLQAVRRIQPLSTG 121
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 122 TMTGLALQFAITKALSDAEGGRARSPDISKVVIVVTDGRPQDSVRDVSERARASGIELFAIGVGRVDKATLRQIASEPQD 201
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 171846231 202 EHVDYVESYNVIEKLAKKFQEAFCVVSDLCATGDHDCEQLCVSSPGSYTCACHEGFTLNSDGKT 265
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 276-499 6.56e-122

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: 355.92  E-value: 6.56e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 276 SATDLVFLIDGSKSVRPENFELVKKFINQIVDTLDVSDRLAQVGLVQYSSSIRQEFPLGRFHTKKDIKAAVRNMSYMEKG 355
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 356 TMTGAALKYLIDNSFTVSSGARPGAQ---KVGIVFTDGRSQDYINDAARKAKDLGFKMFAVGVGNAVEEELREIASEPVA 432
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGSErvpRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171846231 433 DHYFYTADFKTINQIGKKLQKQICVEEDPCACESILKFEAKVEGLLQAltrkLEAVSGRLAVLENRI 499
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICVVPDLCATLSHVCQQVCISTPGSY----LCACTEGYALLEDNK 223
VWA pfam00092
von Willebrand factor type A domain;
279-447 1.14e-67

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 214.83  E-value: 1.14e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  279 DLVFLIDGSKSVRPENFELVKKFINQIVDTLDVSDRLAQVGLVQYSSSIRQEFPLGRFHTKKDIKAAVRNMSYMEKGTM- 357
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  358 TGAALKYLIDNSFTVSSGARPGAQKVGIVFTDGRSQDY-INDAARKAKDLGFKMFAVGVGNAVEEELREIASEPVADHYF 436
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                         170
                  ....*....|.
gi 171846231  437 YTADFKTINQI 447
Cdd:pfam00092 161 TVSDFEALEDL 171
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 278-441 2.57e-64

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: 205.98  E-value: 2.57e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 278 TDLVFLIDGSKSVRPENFELVKKFINQIVDTLDVSDRLAQVGLVQYSSSIRQEFPLGRFHTKKDIKAAVRNMSYMEKGTM 357
Cdd:cd01482    1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 358 TGAALKYLIDNSFTVSSGARPGAQKVGIVFTDGRSQDYINDAARKAKDLGFKMFAVGVGNAVEEELREIASEPVADHYFY 437
Cdd:cd01482   81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                 ....
gi 171846231 438 TADF 441
Cdd:cd01482  161 VADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 278-441 4.19e-64

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: 205.15  E-value: 4.19e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 278 TDLVFLIDGSKSVRPENFELVKKFINQIVDTLDVSDRLAQVGLVQYSSSIRQEFPLGRFHTKKDIKAAVRNMSYMEKGTM 357
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 358 TGAALKYLIDNSFTVSSGARPGAQKVGIVFTDGRSQDYINDAARKAKDLGFKMFAVGVGNAVEEELREIASEPVADHYFY 437
Cdd:cd01472   81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                 ....
gi 171846231 438 TADF 441
Cdd:cd01472  161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
45-219 6.90e-63

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 202.51  E-value: 6.90e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231   45 DLVFVVDSSRSVRPVEFEKVKVFLSQVIESLDVGPNATRVGLVNYASTVKPEFPLRAHGSKASLLQAVRRIQPLSTGTM- 123
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  124 TGLALQFAITKALSDAEGGRarsPDISKVVIVVTDGRPQD-SVRDVSERARASGIELFAIGVGRVDKATLRQIASEPQDE 202
Cdd:pfam00092  81 TGKALKYALENLFSSAAGAR---PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                         170
                  ....*....|....*..
gi 171846231  203 HVDYVESYNVIEKLAKK 219
Cdd:pfam00092 158 HVFTVSDFEALEDLQDQ 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 278-436 2.15e-58

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: 190.20  E-value: 2.15e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 278 TDLVFLIDGSKSVRPENFELVKKFINQIVDTLDVSDRLAQVGLVQYSSSIRQEFPLGRFHTKKDIKAAVRNMSYMEK-GT 356
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 357 MTGAALKYLIDNSFTvSSGARPGAQKVGIVFTDGRSQD--YINDAARKAKDLGFKMFAVGVGNAVEEELREIASEPVADH 434
Cdd:cd01450   81 NTGKALQYALEQLFS-ESNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSERH 159


                 ..
gi 171846231 435 YF 436
Cdd:cd01450  160 VF 161
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 44-204 2.58e-53

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: 177.10  E-value: 2.58e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  44 TDLVFVVDSSRSVRPVEFEKVKVFLSQVIESLDVGPNATRVGLVNYASTVKPEFPLRAHGSKASLLQAVRRIQPL-STGT 122
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLgGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 123 MTGLALQFAITKALSdaegGRARSPDISKVVIVVTDGRPQD--SVRDVSERARASGIELFAIGVGRVDKATLRQIASEPQ 200
Cdd:cd01450   81 NTGKALQYALEQLFS----ESNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156


                 ....
gi 171846231 201 DEHV 204
Cdd:cd01450  157 ERHV 160
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 279-447 1.72e-52

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: 175.34  E-value: 1.72e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231   279 DLVFLIDGSKSVRPENFELVKKFINQIVDTLDVSDRLAQVGLVQYSSSIRQEFPLGRFHTKKDIKAAVRNMSY-MEKGTM 357
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231   358 TGAALKYLIDNSFTVSSGARPGAQKVGIVFTDGRSQDYIND---AARKAKDLGFKMFAVGVGNAV-EEELREIASEPVAD 433
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDllkAAKELKRSGVKVFVVGVGNDVdEEELKKLASAPGGV 160

                          170
                   ....*....|....
gi 171846231   434 HYFYTADFKTINQI 447
Cdd:smart00327 161 YVFLPELLDLLIDL 174
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 44-208 5.77e-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: 170.87  E-value: 5.77e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  44 TDLVFVVDSSRSVRPVEFEKVKVFLSQVIESLDVGPNATRVGLVNYASTVKPEFPLRAHGSKASLLQAVRRIQPLSTGTM 123
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 124 TGLALQFAITKALSDAEGgraRSPDISKVVIVVTDGRPQDSVRDVSERARASGIELFAIGVGRVDKATLRQIASEPQDEH 203
Cdd:cd01472   81 TGKALKYVRENLFTEASG---SREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELY 157


                 ....*
gi 171846231 204 VDYVE 208
Cdd:cd01472  158 VFNVA 162
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 44-208 1.41e-48

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: 164.77  E-value: 1.41e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  44 TDLVFVVDSSRSVRPVEFEKVKVFLSQVIESLDVGPNATRVGLVNYASTVKPEFPLRAHGSKASLLQAVRRIQPLSTGTM 123
Cdd:cd01482    1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 124 TGLALQFAITKALSDAEGGRarsPDISKVVIVVTDGRPQDSVRDVSERARASGIELFAIGVGRVDKATLRQIASEPQDEH 203
Cdd:cd01482   81 TGKALTHVREKNFTPDAGAR---PGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETH 157


                 ....*
gi 171846231 204 VDYVE 208
Cdd:cd01482  158 VFNVA 162
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 45-208 4.68e-46

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 158.39  E-value: 4.68e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231    45 DLVFVVDSSRSVRPVEFEKVKVFLSQVIESLDVGPNATRVGLVNYASTVKPEFPLRAHGSKASLLQAVRRIQPLSTG-TM 123
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGgTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231   124 TGLALQFAITKALSDAEGGRarsPDISKVVIVVTDGRPQDS---VRDVSERARASGIELFAIGVGR-VDKATLRQIASEP 199
Cdd:smart00327  81 LGAALQYALENLFSKSAGSR---RGAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNdVDEEELKKLASAP 157


                   ....*....
gi 171846231   200 QDEHVDYVE 208
Cdd:smart00327 158 GGVYVFLPE 166
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 278-441 4.81e-38

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 137.10  E-value: 4.81e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 278 TDLVFLIDGSKSVRPENFELVKKFINQIVDTLDVSDRLAQVGLVQYSSSIRQEFPLGRFHTKKDIKAAVRNMSYMEKGTM 357
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 358 TGAALKYLIDNSFTVSSGARPGAQKVGIVFTDGRSQD--YINDAARKAKDLGFKMFAVGVGNAVE-----EELREIASEP 430
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDdpLLKDVIPQAEREGIIRYAIGVGGHFQrensrEELKTIASKP 160

                        170
                 ....*....|.
gi 171846231 431 VADHYFYTADF 441
Cdd:cd01469  161 PEEHFFNVTDF 171
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 45-200 3.62e-36

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: 131.68  E-value: 3.62e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  45 DLVFVVDSSRSVRPVEFEKVKVFLSQVIESLDVGPNATRVGLVNYASTVKPEFPLRAHGSKASLLQAVRRIQPLS-TGTM 123
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGgSQLN 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171846231 124 TGLALQFAITKALSDAEGGRARSpDISKVVIVVTDGRPQDSVRDVSERARASGIELFAIGVGRVDKATLRQIASEPQ 200
Cdd:cd01481   82 TGSALDYVVKNLFTKSAGSRIEE-GVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPS 157
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 279-441 1.29e-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: 130.14  E-value: 1.29e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 279 DLVFLIDGSKSVRPENFELVKKFINQIVDTLDVSDRLAQVGLVQYSSSIRQEFPLGRFHTKKDIKAAVRNMSYME-KGTM 357
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGgSQLN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 358 TGAALKYLIDNSFTVSSGAR--PGAQKVGIVFTDGRSQDYINDAARKAKDLGFKMFAVGVGNAVEEELREIASEPvaDHY 435
Cdd:cd01481   82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP--SFV 159


                 ....*.
gi 171846231 436 FYTADF 441
Cdd:cd01481  160 FQVSDF 165
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 279-436 7.74e-33

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: 122.67  E-value: 7.74e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 279 DLVFLIDGSKSVRPENFELVKKFINQIVDTLDVSDRLAQVGLVQYSSSIRQEFPLGRFHTKKDIKAAVRNMSY-MEKGTM 357
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGGTN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 358 TGAALKYLIDNsftVSSGARPGAQKVGIVFTDGRSQDYIND---AARKAKDLGFKMFAVGVGN-AVEEELREIASEPVAD 433
Cdd:cd00198   82 IGAALRLALEL---LKSAKRPNARRVIILLTDGEPNDGPELlaeAARELRKLGITVYTIGIGDdANEDELKEIADKTTGG 158


                 ...
gi 171846231 434 HYF 436
Cdd:cd00198  159 AVF 161
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 44-210 1.97e-31

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: 119.38  E-value: 1.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  44 TDLVFVVDSSRSVRPVEFEKVKVFLSQVIESLDVGPNATRVGLVNYASTVKPEFPLRAHGSKASLLQAVRRIQPLSTGTM 123
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 124 TGLALQFAITKALSDAEGGRarsPDISKVVIVVTDGRPQDS--VRDVSERARASGIELFAIGVG-----RVDKATLRQIA 196
Cdd:cd01469   81 TATAIQYVVTELFSESNGAR---KDATKVLVVITDGESHDDplLKDVIPQAEREGIIRYAIGVGghfqrENSREELKTIA 157

                        170
                 ....*....|....
gi 171846231 197 SEPQDEHVDYVESY 210
Cdd:cd01469  158 SKPPEEHFFNVTDF 171
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 45-204 1.13e-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: 116.51  E-value: 1.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  45 DLVFVVDSSRSVRPVEFEKVKVFLSQVIESLDVGPNATRVGLVNYASTVKPEFPLRAHGSKASLLQAVRRIQP-LSTGTM 123
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGGTN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 124 TGLALQFAITKALsdaeggRARSPDISKVVIVVTDGRPQDS---VRDVSERARASGIELFAIGVG-RVDKATLRQIASEP 199
Cdd:cd00198   82 IGAALRLALELLK------SAKRPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIGdDANEDELKEIADKT 155


                 ....*
gi 171846231 200 QDEHV 204
Cdd:cd00198  156 TGGAV 160
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 45-200 5.96e-30

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: 114.80  E-value: 5.96e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  45 DLVFVVDSSRSVRPVeFEKVKVFLSQVIESLDVGPNATRVGLVNYAS--TVKPEFPLRAHGSKASLLQAVRRIQPLSTGT 122
Cdd:cd01476    2 DLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGrgRQRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 123 MTGLALQFAiTKALSDAEGGRarsPDISKVVIVVTDGRPQDSVRDVSERARAS-GIELFAIGVG---RVDKATLRQIASE 198
Cdd:cd01476   81 ATGAAIEVA-LQQLDPSEGRR---EGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGdpgTVDTEELHSITGN 156


                 ..
gi 171846231 199 PQ 200
Cdd:cd01476  157 ED 158
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 279-435 1.24e-29

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: 114.79  E-value: 1.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 279 DLVFLIDGSKSVRPENFELVKKFINQIVDTL-------DVSDRlAQVGLVQYSSSIRQEFPLGRFHT-KKDIKAAVRNMS 350
Cdd:cd01480    4 DITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrkDPAGS-WRVGVVQYSDQQEVEAGFLRDIRnYTSLKEAVDNLE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 351 YMEKGTMTGAALKYLIDNSFTVSSGarpGAQKVGIVFTDGRSQ----DYINDAARKAKDLGFKMFAVGVGNAVEEELREI 426
Cdd:cd01480   83 YIGGGTFTDCALKYATEQLLEGSHQ---KENKFLLVITDGHSDgspdGGIEKAVNEADHLGIKIFFVAVGSQNEEPLSRI 159


                 ....*....
gi 171846231 427 ASEPVADHY 435
Cdd:cd01480  160 ACDGKSALY 168
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 279-436 8.74e-27

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: 105.94  E-value: 8.74e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 279 DLVFLIDGSKSVRPEnFELVKKFINQIVDTLDVSDRLAQVGLVQYSSSIRQ--EFPLGRFHTKKDIKAAVRNMSYMEKGT 356
Cdd:cd01476    2 DLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 357 MTGAALKYLIdNSFTVSSGARPGAQKVGIVFTDGRSQDYINDAARKAKDL-GFKMFAVGVGN---AVEEELREIASEPva 432
Cdd:cd01476   81 ATGAAIEVAL-QQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGDpgtVDTEELHSITGNE-- 157


                 ....
gi 171846231 433 DHYF 436
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 ...
 43-205 5.43e-23

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: 95.92  E-value: 5.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  43 PTDLVFVVDSSRSVRPVEFEKVKVFLSQVIESL------DVGPNATRVGLVNYASTVKPEFP-LRAHGSKASLLQAVRRI 115
Cdd:cd01480    2 PVDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGfLRDIRNYTSLKEAVDNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 116 QPLSTGTMTGLALQFAITKALsdaeggRARSPDISKVVIVVTDGRPQ----DSVRDVSERARASGIELFAIGVGRVDKAT 191
Cdd:cd01480   82 EYIGGGTFTDCALKYATEQLL------EGSHQKENKFLLVITDGHSDgspdGGIEKAVNEADHLGIKIFFVAVGSQNEEP 155

                        170
                 ....*....|....
gi 171846231 192 LRQIASEPQDEHVD 205
Cdd:cd01480  156 LSRIACDGKSALYR 169
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 40-198 4.14e-20

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: 90.00  E-value: 4.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  40 RTRPTDLVFVVDSSRSVRPVE-FEKVKVFLSQVIESLDVGpnaTRVGLVNYASTVKPEFPLRAhgSKASLLQAVRRIQPl 118
Cdd:COG1240   89 PQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPR---DRVGLVAFGGEAEVLLPLTR--DREALKRALDELPP- 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 119 STGTMTGLALQFAITKAlsdaeggRARSPDISKVVIVVTDGRPQDSVRD---VSERARASGIELFAIGVG--RVDKATLR 193
Cdd:COG1240  163 GGGTPLGDALALALELL-------KRADPARRKVIVLLTDGRDNAGRIDpleAAELAAAAGIRIYTIGVGteAVDEGLLR 235


                 ....*
gi 171846231 194 QIASE 198
Cdd:COG1240  236 EIAEA 240
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 40-224 6.76e-19

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 87.08  E-value: 6.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  40 RTRPTDLVFVVDSSRSVRPVEFEKVKVFLSQVIESLDVGpnaTRVGLVNYASTVKPEFPLRAHGSKASLLQAVRRIQPlS 119
Cdd:COG2304   88 ERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPG---DRVSIVTFAGDARVLLPPTPATDRAKILAAIDRLQA-G 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 120 TGTmtglALQFAITKALSDAEggRARSPDISKVVIVVTDGRP------QDSVRDVSERARASGIELFAIGVGR-VDKATL 192
Cdd:COG2304  164 GGT----ALGAGLELAYELAR--KHFIPGRVNRVILLTDGDAnvgitdPEELLKLAEEAREEGITLTTLGVGSdYNEDLL 237

                        170       180       190
                 ....*....|....*....|....*....|..
gi 171846231 193 RQIASEPQDEHvDYVESynvIEKLAKKFQEAF 224
Cdd:COG2304  238 ERLADAGGGNY-YYIDD---PEEAEKVFVREF 265
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 45-202 4.48e-18

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 82.05  E-value: 4.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  45 DLVFVVDSSRSVRPV-EFEKVKVFLSQVIESLDVGPNATRVGLVNYASTVKPEFPLRAHGS--KASLLQAVRRIQ--PLS 119
Cdd:cd01471    2 DLYLLVDGSGSIGYSnWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNStnKDLALNAIRALLslYYP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 120 TG-TMTGLALQfAITKALSDAEGGRarsPDISKVVIVVTDGRPQDSVRDVSE----RARASGIELFAIGVGrVDKATLRQ 194
Cdd:cd01471   82 NGsTNTTSALL-VVEKHLFDTRGNR---ENAPQLVIIMTDGIPDSKFRTLKEarklRERGVIIAVLGVGQG-VNHEENRS 156


                 ....*...
gi 171846231 195 IASEPQDE 202
Cdd:cd01471  157 LVGCDPDD 164
Matrilin_ccoil pfam10393
Trimeric coiled-coil oligomerization domain of matrilin; This short domain is a coiled coil ...
 457-499 1.69e-16

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


Pssm-ID: 463070  Cd Length: 43  Bit Score: 73.16  E-value: 1.69e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 171846231  457 VEEDPCACESILKFEAKVEGLLQALTRKLEAVSGRLAVLENRI 499
Cdd:pfam10393   1 VEEDPCKCEAIVAFQTKVESEIQALTTKLEEVTKRIEALENRL 43
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 270-451 7.56e-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: 77.29  E-value: 7.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 270 RGGGSGSATDLVFLIDGSKSVRPEN-FELVKKFINQIVDTLDVSDRlaqVGLVQYSSSIRQEFPLGRfhTKKDIKAAVRN 348
Cdd:COG1240   85 ALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRDR---VGLVAFGGEAEVLLPLTR--DREALKRALDE 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 349 MSyMEKGTMTGAALKYLIDnsftVSSGARPGAQKVGIVFTDGR---SQDYINDAARKAKDLGFKMFAVGVGNAV--EEEL 423
Cdd:COG1240  160 LP-PGGGTPLGDALALALE----LLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTEAvdEGLL 234

                        170       180
                 ....*....|....*....|....*...
gi 171846231 424 REIASEPVAdHYFYTADFKTINQIGKKL 451
Cdd:COG1240  235 REIAEATGG-RYFRADDLSELAAIYREI 261
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 279-427 8.37e-16

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 75.50  E-value: 8.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 279 DLVFLIDGSKSVRPEN-FELVKKFINQIVDTLDVSDRLAQVGLVQYSSSIRQEFPLGR-FHTKKD----IKAAVRNMSYM 352
Cdd:cd01471    2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpNSTNKDlalnAIRALLSLYYP 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 171846231 353 EKGTMTGAALKYLIDNSFTvSSGARPGAQKVGIVFTDGRSQDYIN--DAARKAKDLGFKMFAVGVGNAVE-EELREIA 427
Cdd:cd01471   82 NGSTNTTSALLVVEKHLFD-TRGNRENAPQLVIIMTDGIPDSKFRtlKEARKLRERGVIIAVLGVGQGVNhEENRSLV 158
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 279-458 1.58e-14

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 73.98  E-value: 1.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 279 DLVFLIDGSKSVRPENFELVKKFINQIVDTLDVSDRlaqVGLVQYSSSIRQEFPLGRFHTKKDIKAAVRNMSyMEKGTMT 358
Cdd:COG2304   93 NLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDR---VSIVTFAGDARVLLPPTPATDRAKILAAIDRLQ-AGGGTAL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 359 GAALKYLIDnsfTVSSGARPGAQKVGIVFTDGR------SQDYINDAARKAKDLGFKMFAVGVGNAV-EEELREIasepv 431
Cdd:COG2304  169 GAGLELAYE---LARKHFIPGRVNRVILLTDGDanvgitDPEELLKLAEEAREEGITLTTLGVGSDYnEDLLERL----- 240

                        170       180       190
                 ....*....|....*....|....*....|.
gi 171846231 432 ADH----YFYTADFKTINQIGKKLQKQICVE 458
Cdd:COG2304  241 ADAgggnYYYIDDPEEAEKVFVREFSRIGYE 271
VWA_2 pfam13519
von Willebrand factor type A domain;
46-156 2.32e-14

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 68.86  E-value: 2.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231   46 LVFVVDSSRSVR-----PVEFEKVKVFLSQVIESLdvgpNATRVGLVNYASTVKPEFPLRahGSKASLLQAVRRIQPLST 120
Cdd:pfam13519   1 LVFVLDTSGSMRngdygPTRLEAAKDAVLALLKSL----PGDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 171846231  121 GTMTGLALQFAiTKALSDaeggraRSPDISKVVIVV 156
Cdd:pfam13519  75 GTNLAAALQLA-RAALKH------RRKNQPRRIVLI 103
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 231-266 4.41e-14

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: 66.11  E-value: 4.41e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 171846231  231 CATGDHDCEQLCVSSPGSYTCACHEGFTLNSDGKTC 266
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
40-198 8.17e-14

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 69.95  E-value: 8.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  40 RTRPTDLVFVVDSSRSVRPVEFEKVKVFLSQVIESLDVGPNAT---RVGLVNYASTVKPEFPLrahgskasllQAVRRIQ 116
Cdd:COG4245    2 PMRRLPVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYALetvEVSVITFDGEAKVLLPL----------TDLEDFQ 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 117 P--LST--GTMTGLALQFAIT-----KALSDAEGGRARSPdiskVVIVVTDGRPQDS-----VRDVSERARASGIELFAI 182
Cdd:COG4245   72 PpdLSAsgGTPLGAALELLLDlierrVQKYTAEGKGDWRP----VVFLITDGEPTDSdweaaLQRLKDGEAAKKANIFAI 147

                        170
                 ....*....|....*..
gi 171846231 183 GVGR-VDKATLRQIASE 198
Cdd:COG4245  148 GVGPdADTEVLKQLTDP 164
VWA_2 pfam13519
von Willebrand factor type A domain;
280-387 1.02e-12

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 64.24  E-value: 1.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  280 LVFLIDGSKSVR-----PENFELVKKFINQIVDTLDVSdrlaQVGLVQYSSSIRQEFPLGRfhTKKDIKAAVRNMSYMEK 354
Cdd:pfam13519   1 LVFVLDTSGSMRngdygPTRLEAAKDAVLALLKSLPGD----RVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 171846231  355 GTMTGAALKYLIDnsftVSSGARPGAQKVGIVF 387
Cdd:pfam13519  75 GTNLAAALQLARA----ALKHRRKNQPRRIVLI 103
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 279-456 3.42e-10

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: 59.25  E-value: 3.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 279 DLVFLIDGSKSVRPENFEL-VKKFINQIVDTLDVSDRLAQVGLVQYSSSIRQEFPLG---RFHTKKDIKAA--VRNMSYM 352
Cdd:cd01473    2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSdeeRYDKNELLKKIndLKNSYRS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 353 EKGTMTGAALKYLIDNsFTVSSGARPGAQKVGIVFTDGRSQDY----INDAARKAKDLGFKMFAVGVGNAVEEELREIAS 428
Cdd:cd01473   82 GGETYIVEALKYGLKN-YTKHGNRRKDAPKVTMLFTDGNDTSAskkeLQDISLLYKEENVKLLVVGVGAASENKLKLLAG 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 171846231 429 EPVADH---YFYTADFKTINQIGKKLQKQIC 456
Cdd:cd01473  161 CDINNDncpNVIKTEWNNLNGISKFLTDKIC 191
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 46-216 6.66e-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: 58.05  E-value: 6.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  46 LVFVVDSSRSVRPVEFEKVKVFLSQVIESLDvgpNATRVGLVNYASTVKPEFPLRAHGSKASLLQAVRRIQPlSTGTMTG 125
Cdd:cd01465    3 LVFVIDRSGSMDGPKLPLVKSALKLLVDQLR---PDDRLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTA-GGSTAGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 126 LALQFAITKAlsdaegGRARSPDISKVVIVVTDGRPQ------DSVRDVSERARASGIELFAIGVGRVDKATLRQIASEP 199
Cdd:cd01465   79 AGIQLGYQEA------QKHFVPGGVNRILLATDGDFNvgetdpDELARLVAQKRESGITLSTLGFGDNYNEDLMEAIADA 152

                        170
                 ....*....|....*..
gi 171846231 200 QDEHVDYVESYNVIEKL 216
Cdd:cd01465  153 GNGNTAYIDNLAEARKV 169
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 280-451 9.93e-09

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


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 54.59  E-value: 9.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 280 LVFLIDGSKSVRPENFELVKKFINQIVDTLDVSDRLAqvgLVQYSSSIRQEFPLGRFHTKKDIKAAVRNMSyMEKGTMTG 359
Cdd:cd01465    3 LVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLA---IVTYDGAAETVLPATPVRDKAAILAAIDRLT-AGGSTAGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 360 AALKYLIDnsfTVSSGARPGAQKVGIVFTDG------RSQDYINDAARKAKDLGFKMFAVGVGNAVEEELREIASEPVAD 433
Cdd:cd01465   79 AGIQLGYQ---EAQKHFVPGGVNRILLATDGdfnvgeTDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAIADAGNG 155

                        170
                 ....*....|....*...
gi 171846231 434 HYFYTAdfkTINQIGKKL 451
Cdd:cd01465  156 NTAYID---NLAEARKVF 170
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 43-196 8.29e-08

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 53.85  E-value: 8.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231   43 PTDLVFVVDSSRSVRPV---EFEKVKVFLSQVIesldvGPNaTRVGLVNYASTVKPEFPLraHGSKASLLQAVRRIQPLS 119
Cdd:TIGR03436  53 PLTVGLVIDTSGSMRNDldrARAAAIRFLKTVL-----RPN-DRVFVVTFNTRLRLLQDF--TSDPRLLEAALNRLKPPL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  120 TGTM----------TGLALQFAIT-KALSDAEGGRARSPDiSKVVIVVTDG---RPQDSVRDVSERARASGIELFAIGVG 185
Cdd:TIGR03436 125 RTDYnssgafvrdgGGTALYDAITlAALEQLANALAGIPG-RKALIVISDGgdnRSRDTLERAIDAAQRADVAIYSIDAR 203

                         170
                  ....*....|.
gi 171846231  186 RVDKATLRQIA 196
Cdd:TIGR03436 204 GLRAPDLGAGA 214
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 45-208 1.07e-07

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: 51.24  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  45 DLVFVVDSSRSVRPVEFEKVKVFLSQVIESLDvgpNATRVGLVNYASTVKPEFPLR---AHGsKASLLQAVRRIQPLSTG 121
Cdd:cd01466    2 DLVAVLDVSGSMAGDKLQLVKHALRFVISSLG---DADRLSIVTFSTSAKRLSPLRrmtAKG-KRSAKRVVDGLQAGGGT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 122 TMTGlalqfAITKALSDAEGGRARSPDISkvVIVVTDGRPQDSVRDVseRARASGIELFAIGVGRVDKATLRQIASEPQD 201
Cdd:cd01466   78 NVVG-----GLKKALKVLGDRRQKNPVAS--IMLLSDGQDNHGAVVL--RADNAPIPIHTFGLGASHDPALLAFIAEITG 148


                 ....*..
gi 171846231 202 EHVDYVE 208
Cdd:cd01466  149 GTFSYVK 155
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 47-199 4.00e-07

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: 50.03  E-value: 4.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  47 VFVVDSSRSVRPVEFEKVKVFLSQVIESLDVGPNATR---VGLVNYASTVKPEFPLrahgskASLLQAVRRIQPLSTGTM 123
Cdd:cd01464    7 YLLLDTSGSMAGEPIEALNQGLQMLQSELRQDPYALEsveISVITFDSAARVIVPL------TPLESFQPPRLTASGGTS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 124 TGLALQFAI-----TKALSDAEGgrarSPDISKVVIVVTDGRPQDSVRDVSER---ARASGIELFAIGVG-RVDKATLRQ 194
Cdd:cd01464   81 MGAALELALdcidrRVQRYRADQ----KGDWRPWVFLLTDGEPTDDLTAAIERikeARDSKGRIVACAVGpKADLDTLKQ 156


                 ....*
gi 171846231 195 IASEP 199
Cdd:cd01464  157 ITEGV 161
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 278-446 5.48e-07

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: 49.98  E-value: 5.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 278 TDLVFLIDGSKSVRPENFELVKKFINQIVDTLDVSDRLAQVGLVQYSS------SIRQEFPlgrfHTKKDIKAAVRNMSY 351
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASdpkeivSIRDFNS----NDADDVIKRLEDFNY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 352 MEKGTMTG----AALKYLID----------NSFTVSsgarpgaQKVGIVFTDGRS----------QD-----YINDAARK 402
Cdd:cd01470   77 DDHGDKTGtntaAALKKVYErmalekvrnkEAFNET-------RHVIILFTDGKSnmggsplptvDKiknlvYKNNKSDN 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 171846231 403 AKDLGFKMFAVGVG-NAVEEELREIASE-PVADHYFYTADFKTINQ 446
Cdd:cd01470  150 PREDYLDVYVFGVGdDVNKEELNDLASKkDNERHFFKLKDYEDLQE 195
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
278-451 1.11e-06

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 49.15  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 278 TDLVFLIDGSKSVRPENFELVKKFINQIVDTLDvSDRLAQ----VGLVQYSSSIRQEFPL---GRFHTKkDIKAAVrnms 350
Cdd:COG4245    6 LPVYLLLDTSGSMSGEPIEALNEGLQALIDELR-QDPYALetveVSVITFDGEAKVLLPLtdlEDFQPP-DLSASG---- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 351 ymekGTMTGAALKYL---IDNSFTVSSGARPGAQKVGIVF-TDGRSQDY-INDAARKAKDLGFK----MFAVGVG-NAVE 420
Cdd:COG4245   80 ----GTPLGAALELLldlIERRVQKYTAEGKGDWRPVVFLiTDGEPTDSdWEAALQRLKDGEAAkkanIFAIGVGpDADT 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 171846231 421 EELREIASEPVAdhyFYTADFKTINQIGKKL 451
Cdd:COG4245  156 EVLKQLTDPVRA---LDALDGLDFREFFKWL 183
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 45-216 2.16e-06

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


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 48.28  E-value: 2.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  45 DLVFVVDSSRSVRPvEFEKVKVFLSQVIESLdVGPNaTRVGLVNYASTVKPEFPLRAHGSKASL-LQAVRRIQPlSTGTM 123
Cdd:cd01474    6 DLYFVLDKSGSVAA-NWIEIYDFVEQLVDRF-NSPG-LRFSFITFSTRATKILPLTDDSSAIIKgLEVLKKVTP-SGQTY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 124 TGLALQFAITKALSDAEGGRarspDISKVVIVVTDGR-----PQDSVRDvSERARASGIELFAIGVGRVDKATLRQIASE 198
Cdd:cd01474   82 IHEGLENANEQIFNRNGGGR----ETVSVIIALTDGQlllngHKYPEHE-AKLSRKLGAIVYCVGVTDFLKSQLINIADS 156

                        170
                 ....*....|....*....
gi 171846231 199 PqdEHVDYV-ESYNVIEKL 216
Cdd:cd01474  157 K--EYVFPVtSGFQALSGI 173
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 269-458 1.05e-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: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 269 CRGGgsgsaTDLVFLIDGSKSVR---PENF----ELVKKFIN---QIVDTLDVSDRLAQVGLVQYSSSIRQEFplgrfht 338
Cdd:cd01474    1 CAGH-----FDLYFVLDKSGSVAanwIEIYdfveQLVDRFNSpglRFSFITFSTRATKILPLTDDSSAIIKGL------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 339 kKDIKAAV-RNMSYMEKGtmtgaaLKYLIDNSFTVSSGARPGAqKVGIVFTDGRSQD----YINDAARKAKDLGFKMFAV 413
Cdd:cd01474   69 -EVLKKVTpSGQTYIHEG------LENANEQIFNRNGGGRETV-SVIIALTDGQLLLnghkYPEHEAKLSRKLGAIVYCV 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 171846231 414 GVGNAVEEELREIASEPvaDHYFYTAD-FKTINQIGKKLQKQICVE 458
Cdd:cd01474  141 GVTDFLKSQLINIADSK--EYVFPVTSgFQALSGIIESVVKKACIE 184
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 44-203 1.42e-05

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: 45.74  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  44 TDLVFVVDSSRSVRPVEFEKVKVFLSQVIE---SLDVGPNatrVGLVNYASTVKPEFPLR------AHGSKASLLQAVRR 114
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEkisSYEVSPR---YEIISYASDPKEIVSIRdfnsndADDVIKRLEDFNYD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 115 IQPLSTGTMTGLALQ-----FAITKalsdaEGGRARSPDISKVVIVVTDGR------PQDSVRDV---------SERARA 174
Cdd:cd01470   78 DHGDKTGTNTAAALKkvyerMALEK-----VRNKEAFNETRHVIILFTDGKsnmggsPLPTVDKIknlvyknnkSDNPRE 152

                        170       180       190
                 ....*....|....*....|....*....|
gi 171846231 175 SGIELFAIGVGR-VDKATLRQIASEPQDEH 203
Cdd:cd01470  153 DYLDVYVFGVGDdVNKEELNDLASKKDNER 182
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 279-406 2.48e-05

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: 45.11  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 279 DLVFLIDGSKSVRPENFELVKKFINQIVDT-----LDVSD-RLAQVGLVQYSSSIRQEFPLGRFHTKKDI---------K 343
Cdd:cd01477   21 DIVFVVDNSKGMTQGGLWQVRATISSLFGSssqigTDYDDpRSTRVGLVTYNSNATVVADLNDLQSFDDLysqiqgsltD 100

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 171846231 344 AAVRNMSYMEKGtmTGAALKyLIDNSFtvsSGARPGAQKVGIVFTDGRSQDYINDAARKAKDL 406
Cdd:cd01477  101 VSSTNASYLDTG--LQAAEQ-MLAAGK---RTSRENYKKVVIVFASDYNDEGSNDPRPIAARL 157
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 279-458 4.34e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 46.11  E-value: 4.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 279 DLVFLIDGSKSVRPENF-ELVKKFINQIVDTLDVSDRLAQVGLVQYSSSIRQEFPLGRFHTKKDIKA--AVRNM--SYME 353
Cdd:PTZ00441  44 DLYLLVDGSGSIGYHNWiTHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASKDKEQAliIVKSLrkTYLP 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 354 KGT--MTGAAL---KYLIDNSftvssgARPGAQKVGIVFTDGrSQDYINDA---ARKAKDLGFKMFAVGVGNAVEEEL-R 424
Cdd:PTZ00441 124 YGKtnMTDALLevrKHLNDRV------NRENAIQLVILMTDG-IPNSKYRAleeSRKLKDRNVKLAVIGIGQGINHQFnR 196

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 171846231 425 EIA----SEPVADHYFYTADFKTINQIgKKLQKQICVE 458
Cdd:PTZ00441 197 LLAgcrpREGKCKFYSDADWEEAKNLI-KPFIAKVCTE 233
EGF_CA smart00179
Calcium-binding EGF-like domain;
225-266 4.52e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.69  E-value: 4.52e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 171846231   225 CVVSDLCATGDHdceqlCVSSPGSYTCACHEGFTlnsDGKTC 266
Cdd:smart00179   5 CASGNPCQNGGT-----CVNTVGSYRCECPPGYT---DGRNC 38
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 45-185 4.82e-05

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: 44.24  E-value: 4.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  45 DLVFVVDSSRS------VRPVEFEKVKVFLSQVIEsldvGPNATRVGLVNYASTVKPEFPLRAhgSKASLLQAVRRIQPL 118
Cdd:cd01467    4 DIMIALDVSGSmlaqdfVKPSRLEAAKEVLSDFID----RRENDRIGLVVFAGAAFTQAPLTL--DRESLKELLEDIKIG 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 171846231 119 ST--GTMTGLALQFAItKALSDAEGGrarspdiSKVVIVVTDGRPQDSVRD---VSERARASGIELFAIGVG 185
Cdd:cd01467   78 LAgqGTAIGDAIGLAI-KRLKNSEAK-------ERVIVLLTDGENNAGEIDpatAAELAKNKGVRIYTIGVG 141
EGF smart00181
Epidermal growth factor-like domain;
231-266 6.88e-05

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 39.81  E-value: 6.88e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 171846231   231 CATGdHDCEQ-LCVSSPGSYTCACHEGFTLNsdgKTC 266
Cdd:smart00181   2 CASG-GPCSNgTCINTPGSYTCSCPPGYTGD---KRC 34
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 46-177 1.10e-04

Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). In chlorophyll biosynthesis, insertion of Mg2+ into protoporphyrin IX is catalysed by magnesium chelatase in an ATP-dependent reaction. Magnesium chelatase is a three sub-unit (BchI, BchD and BchH) enzyme with a novel arrangement of domains: the C-terminal helical domain is located behind the nucleotide binding site. The BchD domain contains a AAA domain at its N-terminus and a VWA domain at its C-terminus. The VWA domain has been speculated to be involved in mediating protein-protein interactions.


Pssm-ID: 238728 [Multi-domain]  Cd Length: 178  Bit Score: 43.03  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  46 LVFVVDSSRSV---RPVEFEK--VKVFLSQVIESLDvgpnatRVGLV----NYASTVKPefPLRahgskaSLLQAVRRIQ 116
Cdd:cd01451    3 VIFVVDASGSMaarHRMAAAKgaVLSLLRDAYQRRD------KVALIafrgTEAEVLLP--PTR------SVELAKRRLA 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 117 PLSTGTMTGLA--LQFAITKALSdaeggRARSPDISKVVIVVTDGR-------PQDSVRDVSERARASGI 177
Cdd:cd01451   69 RLPTGGGTPLAagLLAAYELAAE-----QARDPGQRPLIVVITDGRanvgpdpTADRALAAARKLRARGI 133
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 229-266 1.22e-04

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: 39.16  E-value: 1.22e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 171846231 229 DLCATGdHDCE--QLCVSSPGSYTCACHEGFTlnsdGKTC 266
Cdd:cd00054    3 DECASG-NPCQngGTCVNTVGSYRCSCPPGYT----GRNC 37
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 225-266 1.26e-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: 39.38  E-value: 1.26e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 171846231 225 CVVSDLCATGdhdceQLCVSSPGSYTCACHEGFTLNsdgKTC 266
Cdd:cd00053    2 CAASNPCSNG-----GTCVNTPGSYRCVCPPGYTGD---RSC 35
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 45-251 1.50e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 44.18  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  45 DLVFVVDSSRSV-RPVEFEKVKVFLSQVIESLDVGPNATRVGLVNYASTVKPEFPLRAHGS--KASLLQAVRRIQ----P 117
Cdd:PTZ00441  44 DLYLLVDGSGSIgYHNWITHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASkdKEQALIIVKSLRktylP 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 118 LSTGTMTGLALQfaITKALSDaeggRARSPDISKVVIVVTDGRPqDSVRDVSERARA---SGIELFAIGVGR-VDKATLR 193
Cdd:PTZ00441 124 YGKTNMTDALLE--VRKHLND----RVNRENAIQLVILMTDGIP-NSKYRALEESRKlkdRNVKLAVIGIGQgINHQFNR 196

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 171846231 194 QIAS-EPQDEHVDYVES--YNVIEKLAKKFQEAFCVVSDLCATgdhdCEQLCVSSPGSYTC 251
Cdd:PTZ00441 197 LLAGcRPREGKCKFYSDadWEEAKNLIKPFIAKVCTEVERTAS----CGPWDEWTPCSVTC 253
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
 250-266 3.15e-04

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: 37.77  E-value: 3.15e-04
                          10
                  ....*....|....*..
gi 171846231  250 TCACHEGFTLNSDGKTC 266
Cdd:pfam12662   1 TCSCPPGYQLDPDGRTC 17
VWA_3 pfam13768
von Willebrand factor type A domain;
45-196 3.23e-04

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 41.23  E-value: 3.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231   45 DLVFVVDSSRSVRpVEFEKVKVFLSQVIESLdvgPNATRVGLVNYASTVKPEFPLRA---HGSKASLLQAVRRIQPLSTG 121
Cdd:pfam13768   2 DVVIVVDVSSSMS-GEPKLQKDALSVALRQL---PTGDKFAVLGFGTLPRPLFPGWRvvsPRSLQEAFQFIKTLQPPLGG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 171846231  122 TMTGLALQFAITKalsdaeggrARSPDISKVVIVVTDGRPQDSVRDVSE--RARASGIELFAIGVG-RVDKATLRQIA 196
Cdd:pfam13768  78 SDLLGALKEAVRA---------PASPGYIRHVLLLTDGSPMQGETRVSDliSRAPGKIRFFAYGLGaSISAPMLQLLA 146
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 43-198 5.30e-04

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


Pssm-ID: 238738 [Multi-domain]  Cd Length: 171  Bit Score: 40.66  E-value: 5.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  43 PTDLVFVVDSSRSVRPVEFEKVKVFLSQVIESLDVGpnaTRVGLVNYASTVKPEFPLRAHGSKASLLQAVRRIQPLST-- 120
Cdd:cd01461    2 PKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPG---DYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQAlg 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 121 GTMTGLALQFAITKalsdaeggRARSPDISKVVIVVTDGrpqdSVRDVSE------RARASGIELFAIGVGR-VDKATLR 193
Cdd:cd01461   79 GTNMNDALEAALEL--------LNSSPGSVPQIILLTDG----EVTNESQilknvrEALSGRIRLFTFGIGSdVNTYLLE 146


                 ....*
gi 171846231 194 QIASE 198
Cdd:cd01461  147 RLARE 151
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 276-395 2.38e-03

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


Pssm-ID: 238740 [Multi-domain]  Cd Length: 190  Bit Score: 39.30  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 276 SATDLVFLIDGSKSVRPENFELVKKFINQIVDTLDVSDRlaqVGLVQYSSSIrqEFPLGRFHT---------KKDIKAAV 346
Cdd:cd01463   12 SPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDF---FNIITFSNEV--NPVVPCFNDtlvqattsnKKVLKEAL 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 171846231 347 RNMSymEKGT-MTGAALKY----LIDNSFTVSSGARPGAQKVGIVFTDGRSQDY 395
Cdd:cd01463   87 DMLE--AKGIaNYTKALEFafslLLKNLQSNHSGSRSQCNQAIMLITDGVPENY 138
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 45-196 2.40e-03

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 39.22  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231  45 DLVFVVDSSRSVRPVEFEK-VKVFLSQVIESLDVGPNATRVGLVNYASTVKPEFP----LRAHgsKASLLqavRRIQPLS 119
Cdd:cd01473    2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPfsdeERYD--KNELL---KKINDLK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 120 TGTMTGL------ALQFAITKALsdaeGGRARSPDISKVVIVVTDGRPQDS----VRDVSERARASGIELFAIGVGRVDK 189
Cdd:cd01473   77 NSYRSGGetyiveALKYGLKNYT----KHGNRRKDAPKVTMLFTDGNDTSAskkeLQDISLLYKEENVKLLVVGVGAASE 152


                 ....*..
gi 171846231 190 ATLRQIA 196
Cdd:cd01473  153 NKLKLLA 159
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 279-427 2.95e-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: 38.52  E-value: 2.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 279 DLVFLIDGSKSVRPENFELVKKFINQIVDTLDVSDRLaqvGLVQYSSSIRQEFPLgRFHTKKDIKAAVRNMSYMEK--GT 356
Cdd:cd01466    2 DLVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRL---SIVTFSTSAKRLSPL-RRMTAKGKRSAKRVVDGLQAggGT 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 171846231 357 MTGAALKYLIDnsftVSSGARPGAQKVGI-VFTDGrsQDYINDAARKAKDLGFKMFAVGVGN----AVEEELREIA 427
Cdd:cd01466   78 NVVGGLKKALK----VLGDRRQKNPVASImLLSDG--QDNHGAVVLRADNAPIPIHTFGLGAshdpALLAFIAEIT 147
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 279-429 5.01e-03

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: 38.08  E-value: 5.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 279 DLVFLIDGSKS------VRPENFELVKKFINQIVDTLDvSDRlaqVGLVQYS--SSIRQEFPLGRFHTKKDIKAAVRNMS 350
Cdd:cd01467    4 DIMIALDVSGSmlaqdfVKPSRLEAAKEVLSDFIDRRE-NDR---IGLVVFAgaAFTQAPLTLDRESLKELLEDIKIGLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 351 ymEKGTMTGAALKYLIdNSFTVSSGArpgaQKVGIVFTDGRS-QDYIN--DAARKAKDLGFKMFAVGVGNA--------- 418
Cdd:cd01467   80 --GQGTAIGDAIGLAI-KRLKNSEAK----ERVIVLLTDGENnAGEIDpaTAAELAKNKGVRIYTIGVGKSgsgpkpdgs 152

                        170
                 ....*....|....
gi 171846231 419 ---VEEELREIASE 429
Cdd:cd01467  153 tilDEDSLVEIADK 166
NorD COG4548
Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];
151-195 5.17e-03

Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];


Pssm-ID: 443612 [Multi-domain]  Cd Length: 439  Bit Score: 39.32  E-value: 5.17e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 171846231 151 KVVIVVTDGRPQDS-----------VRDVSERARASGIELFAIGVGRVDKATLRQI 195
Cdd:COG4548  356 RLLLVLTDGKPNDIdvyegrygiedTRQAVREARRAGIHPFCITIDPEADDYLPRI 411
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 279-429 6.29e-03

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


Pssm-ID: 238738 [Multi-domain]  Cd Length: 171  Bit Score: 37.58  E-value: 6.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171846231 279 DLVFLIDGSKSVRPENFELVKKFINQIVDTLDVSDRLaqvGLVQYSSSIRQEFPLGRFHTKKDIKAAVRNMSYMEK--GT 356
Cdd:cd01461    4 EVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYF---NIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQAlgGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171846231 357 MTGAALKylidNSFTVSSGARPGAQKVgIVFTDG----RSQdyINDAARKAKDLGFKMFAVGVGNAVEEELREIASE 429
Cdd:cd01461   81 NMNDALE----AALELLNSSPGSVPQI-ILLTDGevtnESQ--ILKNVREALSGRIRLFTFGIGSDVNTYLLERLAR 150
 
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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