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Conserved domains on  [gi|153792263|ref|NP_001093210|]
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cartilage matrix protein precursor [Danio rerio]

Protein Classification

cartilage matrix protein( domain architecture ID 10107127)

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 ...
 35-258 2.74e-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: 392.13  E-value: 2.74e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  35 KPTDVVFIVDSSRSVRPSEFEQVKVFLAKVIDGLSVGPDATRVGVVNYASRVKNEVSLKSHKTKAALVKAVSKIEPLSTG 114
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 115 TMTGLAIQFAMNVAFSEAEGGRK-SPDISKVAIIVTDGRPQDNIRDIAARAREAGIEIFAIGVGRVDMTTLRQMASEPLE 193
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPgSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792263 194 DHVDYVESYSLIEKLTKKFQEAFCaVVSDLCATGDHDCEHICISTPGSFKCACREGFTLMNDSRS 258
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKIC-VVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 265-489 3.83e-128

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: 371.33  E-value: 3.83e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 265 AATDVVFLIDGSKSVRPENFELVKKWINLIIDKLDVSETNTHVGLVQYSSTVKQEFPLGRHNSKRSLKEAVKRMDYMERG 344
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 345 TMTGHALSFLVDNSFGPNQGARPG---VPKVGIVFTDGRSQDYIGDAAKKAKALGFKMYAVGVGNAVEDELREIASEPIA 421
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGserVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153792263 422 DHYFYTADFKTMNQIAKKLQINVCQEEDPCECNSITKFQKKVEEALQAltkkLEAVTKRIAALENKIV 489
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICVVPDLCATLSHVCQQVCISTPGSY----LCACTEGYALLEDNKT 224
 
Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 35-258 2.74e-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: 392.13  E-value: 2.74e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  35 KPTDVVFIVDSSRSVRPSEFEQVKVFLAKVIDGLSVGPDATRVGVVNYASRVKNEVSLKSHKTKAALVKAVSKIEPLSTG 114
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 115 TMTGLAIQFAMNVAFSEAEGGRK-SPDISKVAIIVTDGRPQDNIRDIAARAREAGIEIFAIGVGRVDMTTLRQMASEPLE 193
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPgSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792263 194 DHVDYVESYSLIEKLTKKFQEAFCaVVSDLCATGDHDCEHICISTPGSFKCACREGFTLMNDSRS 258
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKIC-VVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 265-489 3.83e-128

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: 371.33  E-value: 3.83e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 265 AATDVVFLIDGSKSVRPENFELVKKWINLIIDKLDVSETNTHVGLVQYSSTVKQEFPLGRHNSKRSLKEAVKRMDYMERG 344
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 345 TMTGHALSFLVDNSFGPNQGARPG---VPKVGIVFTDGRSQDYIGDAAKKAKALGFKMYAVGVGNAVEDELREIASEPIA 421
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGserVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153792263 422 DHYFYTADFKTMNQIAKKLQINVCQEEDPCECNSITKFQKKVEEALQAltkkLEAVTKRIAALENKIV 489
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICVVPDLCATLSHVCQQVCISTPGSY----LCACTEGYALLEDNKT 224
VWA pfam00092
von Willebrand factor type A domain;
268-439 1.27e-63

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 204.05  E-value: 1.27e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  268 DVVFLIDGSKSVRPENFELVKKWINLIIDKLDVSETNTHVGLVQYSSTVKQEFPLGRHNSKRSLKEAVKRMDYMERGTM- 346
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  347 TGHALSFLVDNSFGPNQGARPGVPKVGIVFTDGRSQDY-IGDAAKKAKALGFKMYAVGVGNAVEDELREIASEPIADHYF 425
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                         170
                  ....*....|....
gi 153792263  426 YTADFKTMNQIAKK 439
Cdd:pfam00092 161 TVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
38-211 6.69e-60

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 194.42  E-value: 6.69e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263   38 DVVFIVDSSRSVRPSEFEQVKVFLAKVIDGLSVGPDATRVGVVNYASRVKNEVSLKSHKTKAALVKAVSKIEPLSTGTM- 116
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  117 TGLAIQFAMNVAFSEAEGGRksPDISKVAIIVTDGRPQD-NIRDIAARAREAGIEIFAIGVGRVDMTTLRQMASEPLEDH 195
Cdd:pfam00092  81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGH 158

                         170
                  ....*....|....*.
gi 153792263  196 VDYVESYSLIEKLTKK 211
Cdd:pfam00092 159 VFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 268-436 4.33e-50

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 168.79  E-value: 4.33e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263   268 DVVFLIDGSKSVRPENFELVKKWINLIIDKLDVSETNTHVGLVQYSSTVKQEFPLGRHNSKRSLKEAVKRMDY-MERGTM 346
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263   347 TGHALSFLVDNSFGPNQGARPGVPKVGIVFTDGRSQDYIGD---AAKKAKALGFKMYAVGVGNAV-EDELREIASEPIAD 422
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDllkAAKELKRSGVKVFVVGVGNDVdEEELKKLASAPGGV 160

                          170
                   ....*....|....
gi 153792263   423 HYFYTADFKTMNQI 436
Cdd:smart00327 161 YVFLPELLDLLIDL 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 38-208 3.18e-47

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 161.47  E-value: 3.18e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263    38 DVVFIVDSSRSVRPSEFEQVKVFLAKVIDGLSVGPDATRVGVVNYASRVKNEVSLKSHKTKAALVKAVSKIEPLSTG-TM 116
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGgTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263   117 TGLAIQFAMNVAFSEAEGGRksPDISKVAIIVTDGRPQD---NIRDIAARAREAGIEIFAIGVGR-VDMTTLRQMASEPL 192
Cdd:smart00327  81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNdVDEEELKKLASAPG 158

                          170
                   ....*....|....*.
gi 153792263   193 EDHVDYVESYSLIEKL 208
Cdd:smart00327 159 GVYVFLPELLDLLIDL 174
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 13-190 1.12e-18

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: 85.76  E-value: 1.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  13 LGAQATVDLRQAAAMAAGLCNTKPTDVVFIVDSSRSVR-PSEFEQVKVFLAKVIDGLsvgPDATRVGVVNYASRVKNEVS 91
Cdd:COG1240   69 LLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAaENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  92 LKSHKtkAALVKAVSKIEPlSTGTMTGLAIQFAMNVAfseaegGRKSPDISKVAIIVTDGRP---QDNIRDIAARAREAG 168
Cdd:COG1240  146 LTRDR--EALKRALDELPP-GGGTPLGDALALALELL------KRADPARRKVIVLLTDGRDnagRIDPLEAAELAAAAG 216

                        170       180
                 ....*....|....*....|....
gi 153792263 169 IEIFAIGVG--RVDMTTLRQMASE 190
Cdd:COG1240  217 IRIYTIGVGteAVDEGLLREIAEA 240
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 266-440 1.15e-13

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 71.12  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 266 ATDVVFLIDGSKSVRPEN-FELVKKWINLIIDKLDvseTNTHVGLVQYSSTVKQEFPLGRhnSKRSLKEAVKRMDyMERG 344
Cdd:COG1240   92 GRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEVLLPLTR--DREALKRALDELP-PGGG 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 345 TMTGHALsFLVDNSFgpnQGARPGVPKVGIVFTDGR---SQDYIGDAAKKAKALGFKMYAVGVGNAVEDE--LREIASEp 419
Cdd:COG1240  166 TPLGDAL-ALALELL---KRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTEAVDEglLREIAEA- 240

                        170       180
                 ....*....|....*....|.
gi 153792263 420 IADHYFYTADFKTMNQIAKKL 440
Cdd:COG1240  241 TGGRYFRADDLSELAAIYREI 261
racA PRK13182
chromosome-anchoring protein RacA;
423-488 1.37e-03

chromosome-anchoring protein RacA;


Pssm-ID: 237292 [Multi-domain]  Cd Length: 175  Bit Score: 39.65  E-value: 1.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792263 423 HYFYTADFKTM-----NQI--AKKLQ-INVCQEEDPCECNSITKFQKKVEEALQALTKKLEAVTKRIAALENKI 488
Cdd:PRK13182  35 HYIFTEEDLQLleyvkSQIeeGQNMQdTQKPSSNDVEETQVNTIVQNISSVDFEQLEAQLNTITRRLDELERQL 108
 
Name Accession Description Interval E-value
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 35-258 2.74e-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: 392.13  E-value: 2.74e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  35 KPTDVVFIVDSSRSVRPSEFEQVKVFLAKVIDGLSVGPDATRVGVVNYASRVKNEVSLKSHKTKAALVKAVSKIEPLSTG 114
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 115 TMTGLAIQFAMNVAFSEAEGGRK-SPDISKVAIIVTDGRPQDNIRDIAARAREAGIEIFAIGVGRVDMTTLRQMASEPLE 193
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPgSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792263 194 DHVDYVESYSLIEKLTKKFQEAFCaVVSDLCATGDHDCEHICISTPGSFKCACREGFTLMNDSRS 258
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKIC-VVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 265-489 3.83e-128

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: 371.33  E-value: 3.83e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 265 AATDVVFLIDGSKSVRPENFELVKKWINLIIDKLDVSETNTHVGLVQYSSTVKQEFPLGRHNSKRSLKEAVKRMDYMERG 344
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 345 TMTGHALSFLVDNSFGPNQGARPG---VPKVGIVFTDGRSQDYIGDAAKKAKALGFKMYAVGVGNAVEDELREIASEPIA 421
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGserVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153792263 422 DHYFYTADFKTMNQIAKKLQINVCQEEDPCECNSITKFQKKVEEALQAltkkLEAVTKRIAALENKIV 489
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKFQGKICVVPDLCATLSHVCQQVCISTPGSY----LCACTEGYALLEDNKT 224
VWA pfam00092
von Willebrand factor type A domain;
268-439 1.27e-63

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 204.05  E-value: 1.27e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  268 DVVFLIDGSKSVRPENFELVKKWINLIIDKLDVSETNTHVGLVQYSSTVKQEFPLGRHNSKRSLKEAVKRMDYMERGTM- 346
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  347 TGHALSFLVDNSFGPNQGARPGVPKVGIVFTDGRSQDY-IGDAAKKAKALGFKMYAVGVGNAVEDELREIASEPIADHYF 425
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                         170
                  ....*....|....
gi 153792263  426 YTADFKTMNQIAKK 439
Cdd:pfam00092 161 TVSDFEALEDLQDQ 174
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 267-430 2.66e-61

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: 197.84  E-value: 2.66e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 267 TDVVFLIDGSKSVRPENFELVKKWINLIIDKLDVSETNTHVGLVQYSSTVKQEFPLGRHNSKRSLKEAVKRMDYMERGTM 346
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 347 TGHALSFLVDNSFGPNQGARPGVPKVGIVFTDGRSQDYIGDAAKKAKALGFKMYAVGVGNAVEDELREIASEPIADHYFY 426
Cdd:cd01472   81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                 ....
gi 153792263 427 TADF 430
Cdd:cd01472  161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
38-211 6.69e-60

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 194.42  E-value: 6.69e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263   38 DVVFIVDSSRSVRPSEFEQVKVFLAKVIDGLSVGPDATRVGVVNYASRVKNEVSLKSHKTKAALVKAVSKIEPLSTGTM- 116
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  117 TGLAIQFAMNVAFSEAEGGRksPDISKVAIIVTDGRPQD-NIRDIAARAREAGIEIFAIGVGRVDMTTLRQMASEPLEDH 195
Cdd:pfam00092  81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGH 158

                         170
                  ....*....|....*.
gi 153792263  196 VDYVESYSLIEKLTKK 211
Cdd:pfam00092 159 VFTVSDFEALEDLQDQ 174
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 267-430 3.14e-57

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 187.11  E-value: 3.14e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 267 TDVVFLIDGSKSVRPENFELVKKWINLIIDKLDVSETNTHVGLVQYSSTVKQEFPLGRHNSKRSLKEAVKRMDYMERGTM 346
Cdd:cd01482    1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 347 TGHALSFLVDNSFGPNQGARPGVPKVGIVFTDGRSQDYIGDAAKKAKALGFKMYAVGVGNAVEDELREIASEPIADHYFY 426
Cdd:cd01482   81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                 ....
gi 153792263 427 TADF 430
Cdd:cd01482  161 VADF 164
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 267-425 4.35e-57

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 186.73  E-value: 4.35e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 267 TDVVFLIDGSKSVRPENFELVKKWINLIIDKLDVSETNTHVGLVQYSSTVKQEFPLGRHNSKRSLKEAVKRMDYMER-GT 345
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 346 MTGHALSFLVDNSFGPNQgARPGVPKVGIVFTDGRSQDYIG--DAAKKAKALGFKMYAVGVGNAVEDELREIASEPIADH 423
Cdd:cd01450   81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTDGRSDDGGDpkEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSERH 159


                 ..
gi 153792263 424 YF 425
Cdd:cd01450  160 VF 161
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 37-196 5.24e-52

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 173.25  E-value: 5.24e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  37 TDVVFIVDSSRSVRPSEFEQVKVFLAKVIDGLSVGPDATRVGVVNYASRVKNEVSLKSHKTKAALVKAVSKIEPL-STGT 115
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLgGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 116 MTGLAIQFAMNVAFSEAEGGRKSPdisKVAIIVTDGRPQD--NIRDIAARAREAGIEIFAIGVGRVDMTTLRQMASEPLE 193
Cdd:cd01450   81 NTGKALQYALEQLFSESNARENVP---KVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSE 157


                 ...
gi 153792263 194 DHV 196
Cdd:cd01450  158 RHV 160
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 268-436 4.33e-50

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 168.79  E-value: 4.33e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263   268 DVVFLIDGSKSVRPENFELVKKWINLIIDKLDVSETNTHVGLVQYSSTVKQEFPLGRHNSKRSLKEAVKRMDY-MERGTM 346
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYkLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263   347 TGHALSFLVDNSFGPNQGARPGVPKVGIVFTDGRSQDYIGD---AAKKAKALGFKMYAVGVGNAV-EDELREIASEPIAD 422
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDllkAAKELKRSGVKVFVVGVGNDVdEEELKKLASAPGGV 160

                          170
                   ....*....|....
gi 153792263   423 HYFYTADFKTMNQI 436
Cdd:smart00327 161 YVFLPELLDLLIDL 174
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 37-200 4.19e-49

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: 165.86  E-value: 4.19e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  37 TDVVFIVDSSRSVRPSEFEQVKVFLAKVIDGLSVGPDATRVGVVNYASRVKNEVSLKSHKTKAALVKAVSKIEPLSTGTM 116
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 117 TGLAIQFAMNVAFSEAEGGRKspDISKVAIIVTDGRPQDNIRDIAARAREAGIEIFAIGVGRVDMTTLRQMASEPLEDHV 196
Cdd:cd01472   81 TGKALKYVRENLFTEASGSRE--GVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYV 158


                 ....
gi 153792263 197 DYVE 200
Cdd:cd01472  159 FNVA 162
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 38-208 3.18e-47

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 161.47  E-value: 3.18e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263    38 DVVFIVDSSRSVRPSEFEQVKVFLAKVIDGLSVGPDATRVGVVNYASRVKNEVSLKSHKTKAALVKAVSKIEPLSTG-TM 116
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGgTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263   117 TGLAIQFAMNVAFSEAEGGRksPDISKVAIIVTDGRPQD---NIRDIAARAREAGIEIFAIGVGR-VDMTTLRQMASEPL 192
Cdd:smart00327  81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNdVDEEELKKLASAPG 158

                          170
                   ....*....|....*.
gi 153792263   193 EDHVDYVESYSLIEKL 208
Cdd:smart00327 159 GVYVFLPELLDLLIDL 174
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 37-200 1.66e-44

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: 153.60  E-value: 1.66e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  37 TDVVFIVDSSRSVRPSEFEQVKVFLAKVIDGLSVGPDATRVGVVNYASRVKNEVSLKSHKTKAALVKAVSKIEPLSTGTM 116
Cdd:cd01482    1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 117 TGLAIQFAMNVAFSEAEGGRksPDISKVAIIVTDGRPQDNIRDIAARAREAGIEIFAIGVGRVDMTTLRQMASEPLEDHV 196
Cdd:cd01482   81 TGKALTHVREKNFTPDAGAR--PGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHV 158


                 ....
gi 153792263 197 DYVE 200
Cdd:cd01482  159 FNVA 162
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 268-430 1.63e-33

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: 124.36  E-value: 1.63e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 268 DVVFLIDGSKSVRPENFELVKKWINLIIDKLDVSETNTHVGLVQYSSTVKQEFPLGRHNSKRSLKEAVKRMDYME-RGTM 346
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGgSQLN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 347 TGHALSFLVDNSFGPNQGAR--PGVPKVGIVFTDGRSQDYIGDAAKKAKALGFKMYAVGVGNAVEDELREIASEPiaDHY 424
Cdd:cd01481   82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP--SFV 159


                 ....*.
gi 153792263 425 FYTADF 430
Cdd:cd01481  160 FQVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 38-191 2.04e-33

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: 123.97  E-value: 2.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  38 DVVFIVDSSRSVRPSEFEQVKVFLAKVIDGLSVGPDATRVGVVNYASRVKNEVSLKSHKTKAALVKAVSKIEPLS-TGTM 116
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGgSQLN 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792263 117 TGLAIQFAMNVAFSEAEGGRKSPDISKVAIIVTDGRPQDNIRDIAARAREAGIEIFAIGVGRVDMTTLRQMASEP 191
Cdd:cd01481   82 TGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP 156
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 267-430 1.10e-32

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: 122.46  E-value: 1.10e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 267 TDVVFLIDGSKSVRPENFELVKKWINLIIDKLDVSETNTHVGLVQYSSTVKQEFPLGRHNSKRSLKEAVKRMDYMERGTM 346
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 347 TGHALSFLVDNSFGPNQGARPGVPKVGIVFTDGRSQD--YIGDAAKKAKALGFKMYAVGVGNAVE-----DELREIASEP 419
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDdpLLKDVIPQAEREGIIRYAIGVGGHFQrensrEELKTIASKP 160

                        170
                 ....*....|.
gi 153792263 420 IADHYFYTADF 430
Cdd:cd01469  161 PEEHFFNVTDF 171
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 37-203 8.98e-32

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: 120.15  E-value: 8.98e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  37 TDVVFIVDSSRSVRPSEFEQVKVFLAKVIDGLSVGPDATRVGVVNYASRVKNEVSLKSHKTKAALVKAVSKIEPLSTGTM 116
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 117 TGLAIQFAMNVAFSEAEGGRKspDISKVAIIVTDGRPQDNIRDIAA--RAREAGIEIFAIGVG-----RVDMTTLRQMAS 189
Cdd:cd01469   81 TATAIQYVVTELFSESNGARK--DATKVLVVITDGESHDDPLLKDVipQAEREGIIRYAIGVGghfqrENSREELKTIAS 158

                        170
                 ....*....|....
gi 153792263 190 EPLEDHVDYVESYS 203
Cdd:cd01469  159 KPPEEHFFNVTDFA 172
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 268-424 1.59e-31

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: 119.80  E-value: 1.59e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 268 DVVFLIDGSKSVRPENFELVKKWINLIIDKL------DVSETNTHVGLVQYSSTVKQEFPLGRHNSKR-SLKEAVKRMDY 340
Cdd:cd01480    4 DITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYtSLKEAVDNLEY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 341 MERGTMTGHALSFLVDNSFgpnQGARPGVPKVGIVFTDGRSQ----DYIGDAAKKAKALGFKMYAVGVGNAVEDELREIA 416
Cdd:cd01480   84 IGGGTFTDCALKYATEQLL---EGSHQKENKFLLVITDGHSDgspdGGIEKAVNEADHLGIKIFFVAVGSQNEEPLSRIA 160


                 ....*...
gi 153792263 417 SEPIADHY 424
Cdd:cd01480  161 CDGKSALY 168
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 268-425 3.20e-31

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 118.05  E-value: 3.20e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 268 DVVFLIDGSKSVRPENFELVKKWINLIIDKLDVSETNTHVGLVQYSSTVKQEFPLGRHNSKRSLKEAVKRMDY-MERGTM 346
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGGTN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 347 TGHALSFLVDNSfgpNQGARPGVPKVGIVFTDGRSQDY---IGDAAKKAKALGFKMYAVGVGN-AVEDELREIASEPIAD 422
Cdd:cd00198   82 IGAALRLALELL---KSAKRPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIGDdANEDELKEIADKTTGG 158


                 ...
gi 153792263 423 HYF 425
Cdd:cd00198  159 AVF 161
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 38-196 2.54e-29

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 112.66  E-value: 2.54e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  38 DVVFIVDSSRSVRPSEFEQVKVFLAKVIDGLSVGPDATRVGVVNYASRVKNEVSLKSHKTKAALVKAVSKIEP-LSTGTM 116
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKgLGGGTN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 117 TGLAIQFAMNVAFSEAEGGRKspdisKVAIIVTDGRPQD---NIRDIAARAREAGIEIFAIGVG-RVDMTTLRQMASEPL 192
Cdd:cd00198   82 IGAALRLALELLKSAKRPNAR-----RVIILLTDGEPNDgpeLLAEAARELRKLGITVYTIGIGdDANEDELKEIADKTT 156


                 ....
gi 153792263 193 EDHV 196
Cdd:cd00198  157 GGAV 160
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 38-196 4.99e-29

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: 112.11  E-value: 4.99e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  38 DVVFIVDSSRSVRPsEFEQVKVFLAKVIDGLSVGPDATRVGVVNYAS--RVKNEVSLKSHKTKAALVKAVSKIEPLSTGT 115
Cdd:cd01476    2 DLLFVLDSSGSVRG-KFEKYKKYIERIVEGLEIGPTATRVALITYSGrgRQRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 116 MTGLAIQFAMNVaFSEAEGGRKSpdISKVAIIVTDGRPQDNIRDIAARARE-AGIEIFAIGVG---RVDMTTLRQMASEp 191
Cdd:cd01476   81 ATGAAIEVALQQ-LDPSEGRREG--IPKVVVVLTDGRSHDDPEKQARILRAvPNIETFAVGTGdpgTVDTEELHSITGN- 156


                 ....*
gi 153792263 192 lEDHV 196
Cdd:cd01476  157 -EDHI 160
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 268-425 2.02e-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: 107.48  E-value: 2.02e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 268 DVVFLIDGSKSVRPEnFELVKKWINLIIDKLDVSETNTHVGLVQYSSTVKQ--EFPLGRHNSKRSLKEAVKRMDYMERGT 345
Cdd:cd01476    2 DLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 346 MTGHALSFLVdNSFGPNQGARPGVPKVGIVFTDGRSQDYIGDAAKKAKAL-GFKMYAVGVGN---AVEDELREIASEPia 421
Cdd:cd01476   81 ATGAAIEVAL-QQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGDpgtVDTEELHSITGNE-- 157


                 ....
gi 153792263 422 DHYF 425
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 ...
 36-203 2.04e-22

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: 94.37  E-value: 2.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  36 PTDVVFIVDSSRSVRPSEFEQVKVFLAKVIDGLSVG------PDATRVGVVNYASRVKNE-VSLKSHKTKAALVKAVSKI 108
Cdd:cd01480    2 PVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDyyrkdpAGSWRVGVVQYSDQQEVEaGFLRDIRNYTSLKEAVDNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 109 EPLSTGTMTGLAIQFAMNVAFSEAEGGRKspdisKVAIIVTDGRPQ----DNIRDIAARAREAGIEIFAIGVGRVDMTTL 184
Cdd:cd01480   82 EYIGGGTFTDCALKYATEQLLEGSHQKEN-----KFLLVITDGHSDgspdGGIEKAVNEADHLGIKIFFVAVGSQNEEPL 156

                        170
                 ....*....|....*....
gi 153792263 185 RQMASEPLEDHVDyvESYS 203
Cdd:cd01480  157 SRIACDGKSALYR--ENFA 173
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 13-190 1.12e-18

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: 85.76  E-value: 1.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  13 LGAQATVDLRQAAAMAAGLCNTKPTDVVFIVDSSRSVR-PSEFEQVKVFLAKVIDGLsvgPDATRVGVVNYASRVKNEVS 91
Cdd:COG1240   69 LLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAaENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  92 LKSHKtkAALVKAVSKIEPlSTGTMTGLAIQFAMNVAfseaegGRKSPDISKVAIIVTDGRP---QDNIRDIAARAREAG 168
Cdd:COG1240  146 LTRDR--EALKRALDELPP-GGGTPLGDALALALELL------KRADPARRKVIVLLTDGRDnagRIDPLEAAELAAAAG 216

                        170       180
                 ....*....|....*....|....
gi 153792263 169 IEIFAIGVG--RVDMTTLRQMASE 190
Cdd:COG1240  217 IRIYTIGVGteAVDEGLLREIAEA 240
Matrilin_ccoil pfam10393
Trimeric coiled-coil oligomerization domain of matrilin; This short domain is a coiled coil ...
 446-488 2.02e-18

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: 78.55  E-value: 2.02e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 153792263  446 QEEDPCECNSITKFQKKVEEALQALTKKLEAVTKRIAALENKI 488
Cdd:pfam10393   1 VEEDPCKCEAIVAFQTKVESEIQALTTKLEEVTKRIEALENRL 43
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 268-408 3.26e-14

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 70.88  E-value: 3.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 268 DVVFLIDGSKSVRPEN-FELVKKWINLIIDKLDVSETNTHVGLVQYSSTVKQEFPLGRHNSK-----RSLKEAVKRMDYM 341
Cdd:cd01471    2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTnkdlaLNAIRALLSLYYP 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 342 ERGTMTGHALSfLVDNSFGPNQGARPGVPKVGIVFTDGRSqDYIGDAAKKAKAL---GFKMYAVGVGNAV 408
Cdd:cd01471   82 NGSTNTTSALL-VVEKHLFDTRGNRENAPQLVIIMTDGIP-DSKFRTLKEARKLrerGVIIAVLGVGQGV 149
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 38-177 5.11e-14

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 70.49  E-value: 5.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  38 DVVFIVDSSRSVRPS-EFEQVKVFLAKVIDGLSVGPDATRVGVVNYASRVKNEVSLKS----HKTKAALVKAVSKIEPLS 112
Cdd:cd01471    2 DLYLLVDGSGSIGYSnWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpnstNKDLALNAIRALLSLYYP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153792263 113 TG-TMTGLAIQFAMNVAFSEAeGGRksPDISKVAIIVTDGRPQDNIRDI-AARA-REAGIEIFAIGVG 177
Cdd:cd01471   82 NGsTNTTSALLVVEKHLFDTR-GNR--ENAPQLVIIMTDGIPDSKFRTLkEARKlRERGVIIAVLGVG 146
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 266-440 1.15e-13

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 71.12  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 266 ATDVVFLIDGSKSVRPEN-FELVKKWINLIIDKLDvseTNTHVGLVQYSSTVKQEFPLGRhnSKRSLKEAVKRMDyMERG 344
Cdd:COG1240   92 GRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEVLLPLTR--DREALKRALDELP-PGGG 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 345 TMTGHALsFLVDNSFgpnQGARPGVPKVGIVFTDGR---SQDYIGDAAKKAKALGFKMYAVGVGNAVEDE--LREIASEp 419
Cdd:COG1240  166 TPLGDAL-ALALELL---KRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTEAVDEglLREIAEA- 240

                        170       180
                 ....*....|....*....|.
gi 153792263 420 IADHYFYTADFKTMNQIAKKL 440
Cdd:COG1240  241 TGGRYFRADDLSELAAIYREI 261
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 224-259 3.41e-13

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: 63.42  E-value: 3.41e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 153792263  224 CATGDHDCEHICISTPGSFKCACREGFTLMNDSRSC 259
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
34-190 1.09e-12

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 66.87  E-value: 1.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  34 TKPTDVVFIVDSSRSVRPSEFEQVKVFLAKVIDGLSVGPDAT---RVGVVNYASRVKNEVSLKShktkaalvkaVSKIEP 110
Cdd:COG4245    3 MRRLPVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYALetvEVSVITFDGEAKVLLPLTD----------LEDFQP 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 111 --LST--GTMTGLAIQFAMN-----VAFSEAEGgrkSPDISKVAIIVTDGRPQD-NIRDIAARAREA----GIEIFAIGV 176
Cdd:COG4245   73 pdLSAsgGTPLGAALELLLDlierrVQKYTAEG---KGDWRPVVFLITDGEPTDsDWEAALQRLKDGeaakKANIFAIGV 149

                        170
                 ....*....|....*
gi 153792263 177 GR-VDMTTLRQMASE 190
Cdd:COG4245  150 GPdADTEVLKQLTDP 164
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 268-416 2.81e-12

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 67.05  E-value: 2.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 268 DVVFLIDGSKSVRPENFELVKKWINLIIDKLDVSETnthVGLVQYSSTVKQEFPLGRHNSKRSLKEAVKRMD-----YME 342
Cdd:COG2304   93 NLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDR---VSIVTFAGDARVLLPPTPATDRAKILAAIDRLQagggtALG 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 343 RGTMTGHALsflvdnsfgPNQGARPGVPKVGIVFTDGR------SQDYIGDAAKKAKALGFKMYAVGVGNAV-EDELREI 415
Cdd:COG2304  170 AGLELAYEL---------ARKHFIPGRVNRVILLTDGDanvgitDPEELLKLAEEAREEGITLTTLGVGSDYnEDLLERL 240


                 .
gi 153792263 416 A 416
Cdd:COG2304  241 A 241
VWA_2 pfam13519
von Willebrand factor type A domain;
39-137 3.57e-12

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 62.69  E-value: 3.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263   39 VVFIVDSSRSVR-----PSEFEQVKVFLAKVIDGLsvgpDATRVGVVNYASRVKNEVSLKshKTKAALVKAVSKIEPLST 113
Cdd:pfam13519   1 LVFVLDTSGSMRngdygPTRLEAAKDAVLALLKSL----PGDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                          90       100
                  ....*....|....*....|....
gi 153792263  114 GTMTGLAIQFAMNVAFSEAEGGRK 137
Cdd:pfam13519  75 GTNLAAALQLARAALKHRRKNQPR 98
VWA_2 pfam13519
von Willebrand factor type A domain;
269-376 2.00e-11

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 60.38  E-value: 2.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  269 VVFLIDGSKSVR-----PENFELVKKWINLIIDKLDvsetNTHVGLVQYSSTVKQEFPLGRHNSKrsLKEAVKRMDYMER 343
Cdd:pfam13519   1 LVFVLDTSGSMRngdygPTRLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLTKDRAK--ILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 153792263  344 GTMTGHALSFLVDNSfgpnQGARPGVPKVGIVF 376
Cdd:pfam13519  75 GTNLAAALQLARAAL----KHRRKNQPRRIVLI 103
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 39-192 5.87e-10

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: 58.51  E-value: 5.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  39 VVFIVDSSRSVRPSEFEQVKVFLAKVIDGLSVGPDATR---VGVVNYASRVKNEVSLkshktkAALVKAVSKIEPLSTGT 115
Cdd:cd01464    6 IYLLLDTSGSMAGEPIEALNQGLQMLQSELRQDPYALEsveISVITFDSAARVIVPL------TPLESFQPPRLTASGGT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 116 MTGLAIQFAM---NVAFSEAEGGRKSpDISKVAIIVTDGRPQDNIRDIAARAREAGIE---IFAIGVG-RVDMTTLRQMA 188
Cdd:cd01464   80 SMGAALELALdciDRRVQRYRADQKG-DWRPWVFLLTDGEPTDDLTAAIERIKEARDSkgrIVACAVGpKADLDTLKQIT 158


                 ....
gi 153792263 189 SEPL 192
Cdd:cd01464  159 EGVP 162
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 40-208 3.86e-09

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


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 55.74  E-value: 3.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  40 VFIVDSSRSVRPSEFEQVKVFLAKVIDGLSvgpDATRVGVVNYASRVKNEVSLKSHKTKAALVKAVSKIEPlstGTMTgl 119
Cdd:cd01465    4 VFVIDRSGSMDGPKLPLVKSALKLLVDQLR---PDDRLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTA---GGST-- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 120 AIQFAMNVAFSEAEGGRKSPDISKVaIIVTDGRPQDNIRDI------AARAREAGIEIFAIGVGRVDMTTLRQMASEPLE 193
Cdd:cd01465   76 AGGAGIQLGYQEAQKHFVPGGVNRI-LLATDGDFNVGETDPdelarlVAQKRESGITLSTLGFGDNYNEDLMEAIADAGN 154

                        170
                 ....*....|....*
gi 153792263 194 DHVDYVESYSLIEKL 208
Cdd:cd01465  155 GNTAYIDNLAEARKV 169
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 294-445 5.29e-09

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: 55.79  E-value: 5.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 294 IIDKLDVSETNTHVGLVQYSSTVKQEFPLG---RHNSKRSLKEAVKRMDYMERGTMTG--HALSFLVDNSFGpNQGARPG 368
Cdd:cd01473   29 IINNLNISKDKVHVGILLFAEKNRDVVPFSdeeRYDKNELLKKINDLKNSYRSGGETYivEALKYGLKNYTK-HGNRRKD 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 369 VPKVGIVFTDGRSQDY----IGDAAKKAKALGFKMYAVGVGNAVEDELREIASEPIADH---YFYTADFKTMNQIAKKLQ 441
Cdd:cd01473  108 APKVTMLFTDGNDTSAskkeLQDISLLYKEENVKLLVVGVGAASENKLKLLAGCDINNDncpNVIKTEWNNLNGISKFLT 187


                 ....
gi 153792263 442 INVC 445
Cdd:cd01473  188 DKIC 191
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 267-435 7.00e-08

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: 52.68  E-value: 7.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 267 TDVVFLIDGSKSVRPENFELVKKWINLIIDKLDVSETNTHVGLVQYSSTVKQ-----EFplgRHNSKRSLKEAVKRMDYM 341
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEivsirDF---NSNDADDVIKRLEDFNYD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 342 E----RGTMTGHALSFLVDNSFGPNQGARPGVPK---VGIVFTDGRS----------QD-----YIGDAAKKAKALGFKM 399
Cdd:cd01470   78 DhgdkTGTNTAAALKKVYERMALEKVRNKEAFNEtrhVIILFTDGKSnmggsplptvDKiknlvYKNNKSDNPREDYLDV 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 153792263 400 YAVGVG-NAVEDELREIASE-PIADHYFYTADFKTMNQ 435
Cdd:cd01470  158 YVFGVGdDVNKEELNDLASKkDNERHFFKLKDYEDLQE 195
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 40-196 4.76e-06

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: 47.28  E-value: 4.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  40 VFIV-DSSRSVRPSEFEQVKVFLAKVIDGLS---VGPdatRVGVVNYASRVKNEVSL------KSHKTKAALVKAVSKIE 109
Cdd:cd01470    3 IYIAlDASDSIGEEDFDEAKNAIKTLIEKISsyeVSP---RYEIISYASDPKEIVSIrdfnsnDADDVIKRLEDFNYDDH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 110 PLSTGTMTGLAIQ-FAMNVAFSEAEGGRKSPDISKVAIIVTDGR------PQ---DNIRDI------AARAREAGIEIFA 173
Cdd:cd01470   80 GDKTGTNTAAALKkVYERMALEKVRNKEAFNETRHVIILFTDGKsnmggsPLptvDKIKNLvyknnkSDNPREDYLDVYV 159

                        170       180
                 ....*....|....*....|....*
gi 153792263 174 IGVGR-VDMTTLRQMASE-PLEDHV 196
Cdd:cd01470  160 FGVGDdVNKEELNDLASKkDNERHF 184
EGF_CA smart00179
Calcium-binding EGF-like domain;
222-259 8.09e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.62  E-value: 8.09e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 153792263   222 DLCATGdHDCEH--ICISTPGSFKCACREGFTlmnDSRSC 259
Cdd:smart00179   3 DECASG-NPCQNggTCVNTVGSYRCECPPGYT---DGRNC 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 222-254 1.06e-05

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


Pssm-ID: 238011  Cd Length: 38  Bit Score: 42.24  E-value: 1.06e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 153792263 222 DLCATGdHDCEH--ICISTPGSFKCACREGFTLMN 254
Cdd:cd00054    3 DECASG-NPCQNggTCVNTVGSYRCSCPPGYTGRN 36
EGF smart00181
Epidermal growth factor-like domain;
224-260 1.21e-05

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 42.12  E-value: 1.21e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 153792263   224 CATGdHDCEH-ICISTPGSFKCACREGFTLmndSRSCS 260
Cdd:smart00181   2 CASG-GPCSNgTCINTPGSYTCSCPPGYTG---DKRCE 35
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 224-259 2.19e-05

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: 41.31  E-value: 2.19e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 153792263 224 CATgDHDCEH--ICISTPGSFKCACREGFTLmndSRSC 259
Cdd:cd00053    2 CAA-SNPCSNggTCVNTPGSYRCVCPPGYTG---DRSC 35
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 264-384 2.51e-05

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


Pssm-ID: 238740 [Multi-domain]  Cd Length: 190  Bit Score: 45.08  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 264 NAAT---DVVFLIDGSKSVRPENFELVKKWINLIIDKLDvseTNTHVGLVQYSSTVKQEFPLGRHN-------SKRSLKE 333
Cdd:cd01463    8 QAATspkDIVILLDVSGSMTGQRLHLAKQTVSSILDTLS---DNDFFNIITFSNEVNPVVPCFNDTlvqattsNKKVLKE 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 153792263 334 AVKRM---DYMERGTMTGHALSFLVDNSFGPNQGARPGVPKVGIVFTDGRSQDY 384
Cdd:cd01463   85 ALDMLeakGIANYTKALEFAFSLLLKNLQSNHSGSRSQCNQAIMLITDGVPENY 138
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 38-188 3.43e-05

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 44.62  E-value: 3.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  38 DVVFIVDSSRSVRPSEFE-QVKVFLAKVIDGLSVGPDATRVGVVNYASRVKNEV--SLKSHKTKAALVKavsKIEPLSTG 114
Cdd:cd01473    2 DLTLILDESASIGYSNWRkDVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVpfSDEERYDKNELLK---KINDLKNS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 115 TMTGL------AIQFAM-NVAFSeaeGGRKSpDISKVAIIVTDGR---PQDN-IRDIAARAREAGIEIFAIGVGRVDMTT 183
Cdd:cd01473   79 YRSGGetyiveALKYGLkNYTKH---GNRRK-DAPKVTMLFTDGNdtsASKKeLQDISLLYKEENVKLLVVGVGAASENK 154


                 ....*
gi 153792263 184 LRQMA 188
Cdd:cd01473  155 LKLLA 159
EGF_CA pfam07645
Calcium-binding EGF domain;
222-249 1.71e-04

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 38.76  E-value: 1.71e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 153792263  222 DLCATGDHDCEH--ICISTPGSFKCACREG 249
Cdd:pfam07645   3 DECATGTHNCPAntVCVNTIGSFECRCPDG 32
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 262-447 3.16e-04

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: 41.73  E-value: 3.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 262 CSNAAtDVVFLIDGSKSVR---PENFELVKKwinlIIDKLdvSETNTHVGLVQYSSTVKQEFPLgRHNSKRSLKEAVKRM 338
Cdd:cd01474    1 CAGHF-DLYFVLDKSGSVAanwIEIYDFVEQ----LVDRF--NSPGLRFSFITFSTRATKILPL-TDDSSAIIKGLEVLK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 339 DYMERG-TMTGHALSFLVDNSFGPNQGARPgVPKVGIVFTDGRSQD----YIGDAAKKAKALGFKMYAVGVGNAVEDELR 413
Cdd:cd01474   73 KVTPSGqTYIHEGLENANEQIFNRNGGGRE-TVSVIIALTDGQLLLnghkYPEHEAKLSRKLGAIVYCVGVTDFLKSQLI 151

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 153792263 414 EIASEPiaDHYFYTAD-FKTMNQIAKKLQINVCQE 447
Cdd:cd01474  152 NIADSK--EYVFPVTSgFQALSGIIESVVKKACIE 184
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 268-418 8.38e-04

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: 40.39  E-value: 8.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 268 DVVFLIDGSKS------VRPENFELVKKWINLIIDKldvsETNTHVGLVQYSSTVKQEFPL-GRHNSKRSLKEAVKRMDy 340
Cdd:cd01467    4 DIMIALDVSGSmlaqdfVKPSRLEAAKEVLSDFIDR----RENDRIGLVVFAGAAFTQAPLtLDRESLKELLEDIKIGL- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 341 MERGTMTGHALSFLVdNSFGPNQGarpgVPKVGIVFTDGrsQDYIGD-----AAKKAKALGFKMYAVGVGNA-------- 407
Cdd:cd01467   79 AGQGTAIGDAIGLAI-KRLKNSEA----KERVIVLLTDG--ENNAGEidpatAAELAKNKGVRIYTIGVGKSgsgpkpdg 151

                        170
                 ....*....|....*
gi 153792263 408 ----VEDELREIASE 418
Cdd:cd01467  152 stilDEDSLVEIADK 166
racA PRK13182
chromosome-anchoring protein RacA;
423-488 1.37e-03

chromosome-anchoring protein RacA;


Pssm-ID: 237292 [Multi-domain]  Cd Length: 175  Bit Score: 39.65  E-value: 1.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792263 423 HYFYTADFKTM-----NQI--AKKLQ-INVCQEEDPCECNSITKFQKKVEEALQALTKKLEAVTKRIAALENKI 488
Cdd:PRK13182  35 HYIFTEEDLQLleyvkSQIeeGQNMQdTQKPSSNDVEETQVNTIVQNISSVDFEQLEAQLNTITRRLDELERQL 108
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 38-200 1.60e-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: 39.30  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  38 DVVFIVDSSRSVRPSEFEQVKVFLAKVIDGLSvgpDATRVGVVNYASRVKNEVSLK--SHKTKAALVKAVSKIEPlSTGT 115
Cdd:cd01466    2 DLVAVLDVSGSMAGDKLQLVKHALRFVISSLG---DADRLSIVTFSTSAKRLSPLRrmTAKGKRSAKRVVDGLQA-GGGT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 116 MTGLAIQFAMNVAfseaeGGRKSPDISKVAIIVTDGrpQDNIRDIAARAREAGIEIFAIGVGRVDMTTLRQMASEPLEDH 195
Cdd:cd01466   78 NVVGGLKKALKVL-----GDRRQKNPVASIMLLSDG--QDNHGAVVLRADNAPIPIHTFGLGASHDPALLAFIAEITGGT 150


                 ....*
gi 153792263 196 VDYVE 200
Cdd:cd01466  151 FSYVK 155
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 38-211 2.07e-03

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: 39.42  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263  38 DVVFIVDSSRSVRPSEFEqVKVFLAKVIDGLsVGPDaTRVGVVNYASRVKNEVSLKSHKTKaaLVKAVSKIEPLSTGTMT 117
Cdd:cd01474    6 DLYFVLDKSGSVAANWIE-IYDFVEQLVDRF-NSPG-LRFSFITFSTRATKILPLTDDSSA--IIKGLEVLKKVTPSGQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 118 --GLAIQFAMNVAFSEAEGGRKSpdiSKVAIIVTDGR-----PQDNIRDiAARAREAGIEIFAIGVGRVDMTTLRQMASE 190
Cdd:cd01474   81 yiHEGLENANEQIFNRNGGGRET---VSVIIALTDGQlllngHKYPEHE-AKLSRKLGAIVYCVGVTDFLKSQLINIADS 156

                        170       180
                 ....*....|....*....|....*.
gi 153792263 191 PleDHVDYV-ESYS----LIEKLTKK 211
Cdd:cd01474  157 K--EYVFPVtSGFQalsgIIESVVKK 180
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 270-440 2.91e-03

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: 38.41  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 270 VFLIDGSKSVRPENFELVKKWINLIIDKLDVSETnthVGLVQYSSTVKQEFPLGRHNSKRSLKEAVKRMDyMERGTMTGH 349
Cdd:cd01465    4 VFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDR---LAIVTYDGAAETVLPATPVRDKAAILAAIDRLT-AGGSTAGGA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 350 ALSFLVDNSfgpNQGARPGVPKVGIVFTDGRSQDYIGD-------AAKKAKAlGFKMYAVGVGNAVEDELREIASEPIAD 422
Cdd:cd01465   80 GIQLGYQEA---QKHFVPGGVNRILLATDGDFNVGETDpdelarlVAQKRES-GITLSTLGFGDNYNEDLMEAIADAGNG 155

                        170
                 ....*....|....*...
gi 153792263 423 HYFYTAdfkTMNQIAKKL 440
Cdd:cd01465  156 NTAYID---NLAEARKVF 170
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 268-408 5.47e-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: 37.96  E-value: 5.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792263 268 DVVFLIDGSKSVRPENFELVKKWINLIIDKLDVSET-NthvgLVQYSSTVKQEFPLGRHNSKRSLKEAVKRMDYMER--G 344
Cdd:cd01461    4 EVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYfN----IIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQAlgG 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153792263 345 TMTGHALSFLVDNSFGPnqgarPGVPKVGIVFTDG----RSQdyIGDAAKKAKALGFKMYAVGVGNAV 408
Cdd:cd01461   80 TNMNDALEAALELLNSS-----PGSVPQIILLTDGevtnESQ--ILKNVREALSGRIRLFTFGIGSDV 140
 
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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