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Conserved domains on  [gi|1831512145|ref|NP_001368221|]
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VWFA domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 113-281 5.40e-71

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: 216.50  E-value: 5.40e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 113 LDLVLVLDFSTTTDPVYNSYKDLSKRLVSQLKIGPHYTQVAAVTFATVGRTRVRFNLKKYQTQEEVLRGIDNLKSRGGTT 192
Cdd:cd01476     1 LDLLFVLDSSGSVRGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 193 AIGAGIEKALTQLDESEGARPGIaTKVMVVFTDGWSNKgpDPEKRARDAVsSGFEMYTVAYTAHTPGAVtlNNETLSAIS 272
Cdd:cd01476    81 ATGAAIEVALQQLDPSEGRREGI-PKVVVVLTDGRSHD--DPEKQARILR-AVPNIETFAVGTGDPGTV--DTEELHSIT 154


                  ....*....
gi 1831512145 273 GDVHHTFTD 281
Cdd:cd01476   155 GNEDHIFTD 163
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 2-68 1.10e-26

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


The actual alignment was detected with superfamily member cd01476:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 163  Bit Score: 102.48  E-value: 1.10e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831512145   2 AQRNVSIPTLVMVVTDGRSADDPKGPGQILQAQPNTWVFAAATGDPEKVDTRELMDITGNINHIVMH 68
Cdd:cd01476    97 EGRREGIPKVVVVLTDGRSHDDPEKQARILRAVPNIETFAVGTGDPGTVDTEELHSITGNEDHIFTD 163
 
Name Accession Description Interval E-value
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 113-281 5.40e-71

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: 216.50  E-value: 5.40e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 113 LDLVLVLDFSTTTDPVYNSYKDLSKRLVSQLKIGPHYTQVAAVTFATVGRTRVRFNLKKYQTQEEVLRGIDNLKSRGGTT 192
Cdd:cd01476     1 LDLLFVLDSSGSVRGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 193 AIGAGIEKALTQLDESEGARPGIaTKVMVVFTDGWSNKgpDPEKRARDAVsSGFEMYTVAYTAHTPGAVtlNNETLSAIS 272
Cdd:cd01476    81 ATGAAIEVALQQLDPSEGRREGI-PKVVVVLTDGRSHD--DPEKQARILR-AVPNIETFAVGTGDPGTV--DTEELHSIT 154


                  ....*....
gi 1831512145 273 GDVHHTFTD 281
Cdd:cd01476   155 GNEDHIFTD 163
VWA pfam00092
von Willebrand factor type A domain;
114-289 1.37e-32

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 118.53  E-value: 1.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 114 DLVLVLDFSTTTDPVY-NSYKDLSKRLVSQLKIGPHYTQVAAVTFAtvGRTRVRFNLKKYQTQEEVLRGIDNLKSR-GGT 191
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNfEKVKEFLKKLVESLDIGPDGTRVGLVQYS--SDVRTEFPLNDYSSKEELLSAVDNLRYLgGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 192 TAIGAGIEKALTQL-DESEGARPGiATKVMVVFTDGWSNKGpDPEKRARDAVSSGFEMYTVAYTAHTpgavtlnNETLSA 270
Cdd:pfam00092  79 TNTGKALKYALENLfSSAAGARPG-APKVVVLLTDGRSQDG-DPEEVARELKSAGVTVFAVGVGNAD-------DEELRK 149

                         170       180
                  ....*....|....*....|.
gi 1831512145 271 ISG--DVHHTFTDVTFQALID 289
Cdd:pfam00092 150 IASepGEGHVFTVSDFEALED 170
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 114-291 2.50e-31

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: 115.24  E-value: 2.50e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145  114 DLVLVLDFS-TTTDPVYNSYKDLSKRLVSQLKIGPHYTQVAAVTFATvgRTRVRFNLKKYQTQEEVLRGIDNLK-SRGGT 191
Cdd:smart00327   1 DVVFLLDGSgSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSD--DARVLFPLNDSRSKDALLEALASLSyKLGGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145  192 TAIGAGIEKALTQL-DESEGARPGiATKVMVVFTDGWSNKGP-DPEKRARDAVSSGFEMYTVAYTAHTPGAVtlnNETLS 269
Cdd:smart00327  79 TNLGAALQYALENLfSKSAGSRRG-APKVVILITDGESNDGPkDLLKAAKELKRSGVKVFVVGVGNDVDEEE---LKKLA 154

                          170       180
                   ....*....|....*....|..
gi 1831512145  270 AISGDVHHtFTDVTFQALIDKI 291
Cdd:smart00327 155 SAPGGVYV-FLPELLDLLIDLL 175
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 2-68 1.10e-26

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


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 102.48  E-value: 1.10e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831512145   2 AQRNVSIPTLVMVVTDGRSADDPKGPGQILQAQPNTWVFAAATGDPEKVDTRELMDITGNINHIVMH 68
Cdd:cd01476    97 EGRREGIPKVVVVLTDGRSHDDPEKQARILRAVPNIETFAVGTGDPGTVDTEELHSITGNEDHIFTD 163
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 113-272 2.05e-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: 68.81  E-value: 2.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 113 LDLVLVLD--FSTTTDPVYNSYKDLSKRLVSQLkigPHYTQVAAVTFATVGRTRVRFNLKKyqtqEEVLRGIDNLKSRGG 190
Cdd:COG1240    93 RDVVLVVDasGSMAAENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTRDR----EALKRALDELPPGGG 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 191 TtAIGAGIEKALTQLDESEGARPgiatKVMVVFTDGWSNKGP-DPEKRARDAVSSGFEMYTVAYtahtpGAVTLNNETLS 269
Cdd:COG1240   166 T-PLGDALALALELLKRADPARR----KVIVLLTDGRDNAGRiDPLEAAELAAAAGIRIYTIGV-----GTEAVDEGLLR 235


                  ...
gi 1831512145 270 AIS 272
Cdd:COG1240   236 EIA 238
VWA pfam00092
von Willebrand factor type A domain;
8-61 3.04e-03

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 37.64  E-value: 3.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1831512145   8 IPTLVMVVTDGRSAD-DPKGPGQILQAQpNTWVFAAATGDpekVDTRELMDITGN 61
Cdd:pfam00092 103 APKVVVLLTDGRSQDgDPEEVARELKSA-GVTVFAVGVGN---ADDEELRKIASE 153
 
Name Accession Description Interval E-value
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 113-281 5.40e-71

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: 216.50  E-value: 5.40e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 113 LDLVLVLDFSTTTDPVYNSYKDLSKRLVSQLKIGPHYTQVAAVTFATVGRTRVRFNLKKYQTQEEVLRGIDNLKSRGGTT 192
Cdd:cd01476     1 LDLLFVLDSSGSVRGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 193 AIGAGIEKALTQLDESEGARPGIaTKVMVVFTDGWSNKgpDPEKRARDAVsSGFEMYTVAYTAHTPGAVtlNNETLSAIS 272
Cdd:cd01476    81 ATGAAIEVALQQLDPSEGRREGI-PKVVVVLTDGRSHD--DPEKQARILR-AVPNIETFAVGTGDPGTV--DTEELHSIT 154


                  ....*....
gi 1831512145 273 GDVHHTFTD 281
Cdd:cd01476   155 GNEDHIFTD 163
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 113-279 3.32e-37

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: 130.10  E-value: 3.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 113 LDLVLVLDFSTTTDPV-YNSYKDLSKRLVSQLKIGPHYTQVAAVTFAtvGRTRVRFNLKKYQTQEEVLRGIDNLKSRGGT 191
Cdd:cd01450     1 LDIVFLLDGSESVGPEnFEKVKDFIEKLVEKLDIGPDKTRVGLVQYS--DDVRVEFSLNDYKSKDDLLKAVKNLKYLGGG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 192 -TAIGAGIEKALTQLDESEGARPGiATKVMVVFTDGWSNKGPDPEKRARDAVSSGFEMYTVAYTAHtpgavtlNNETLSA 270
Cdd:cd01450    79 gTNTGKALQYALEQLFSESNAREN-VPKVIIVLTDGRSDDGGDPKEAAAKLKDEGIKVFVVGVGPA-------DEEELRE 150

                         170
                  ....*....|.
gi 1831512145 271 ISGD--VHHTF 279
Cdd:cd01450   151 IASCpsERHVF 161
VWA pfam00092
von Willebrand factor type A domain;
114-289 1.37e-32

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 118.53  E-value: 1.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 114 DLVLVLDFSTTTDPVY-NSYKDLSKRLVSQLKIGPHYTQVAAVTFAtvGRTRVRFNLKKYQTQEEVLRGIDNLKSR-GGT 191
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNfEKVKEFLKKLVESLDIGPDGTRVGLVQYS--SDVRTEFPLNDYSSKEELLSAVDNLRYLgGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 192 TAIGAGIEKALTQL-DESEGARPGiATKVMVVFTDGWSNKGpDPEKRARDAVSSGFEMYTVAYTAHTpgavtlnNETLSA 270
Cdd:pfam00092  79 TNTGKALKYALENLfSSAAGARPG-APKVVVLLTDGRSQDG-DPEEVARELKSAGVTVFAVGVGNAD-------DEELRK 149

                         170       180
                  ....*....|....*....|.
gi 1831512145 271 ISG--DVHHTFTDVTFQALID 289
Cdd:pfam00092 150 IASepGEGHVFTVSDFEALED 170
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 114-291 2.50e-31

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: 115.24  E-value: 2.50e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145  114 DLVLVLDFS-TTTDPVYNSYKDLSKRLVSQLKIGPHYTQVAAVTFATvgRTRVRFNLKKYQTQEEVLRGIDNLK-SRGGT 191
Cdd:smart00327   1 DVVFLLDGSgSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSD--DARVLFPLNDSRSKDALLEALASLSyKLGGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145  192 TAIGAGIEKALTQL-DESEGARPGiATKVMVVFTDGWSNKGP-DPEKRARDAVSSGFEMYTVAYTAHTPGAVtlnNETLS 269
Cdd:smart00327  79 TNLGAALQYALENLfSKSAGSRRG-APKVVILITDGESNDGPkDLLKAAKELKRSGVKVFVVGVGNDVDEEE---LKKLA 154

                          170       180
                   ....*....|....*....|..
gi 1831512145  270 AISGDVHHtFTDVTFQALIDKI 291
Cdd:smart00327 155 SAPGGVYV-FLPELLDLLIDLL 175
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 2-68 1.10e-26

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


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 102.48  E-value: 1.10e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831512145   2 AQRNVSIPTLVMVVTDGRSADDPKGPGQILQAQPNTWVFAAATGDPEKVDTRELMDITGNINHIVMH 68
Cdd:cd01476    97 EGRREGIPKVVVVLTDGRSHDDPEKQARILRAVPNIETFAVGTGDPGTVDTEELHSITGNEDHIFTD 163
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 113-290 5.03e-26

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: 101.28  E-value: 5.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 113 LDLVLVLDFSTTTDPV-YNSYKDLSKRLVSQLKIGPHYTQVAAVTFATVGRTRvrFNLKKYQTQEEVLRGIDNLKSRGGT 191
Cdd:cd01469     1 MDIVFVLDGSGSIYPDdFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTE--FTLNEYRTKEEPLSLVKHISQLLGL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 192 TAIGAGIEKALTQL-DESEGARPGiATKVMVVFTDGWSNKGPDPEKRARDAVSSGFEMYTVAYTAHTPGAVTLnnETLSA 270
Cdd:cd01469    79 TNTATAIQYVVTELfSESNGARKD-ATKVLVVITDGESHDDPLLKDVIPQAEREGIIRYAIGVGGHFQRENSR--EELKT 155

                         170       180
                  ....*....|....*....|..
gi 1831512145 271 ISGD--VHHTFTDVTFQALIDK 290
Cdd:cd01469   156 IASKppEEHFFNVTDFAALKDI 177
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 114-284 6.56e-23

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: 92.68  E-value: 6.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 114 DLVLVLDFSTTTDPV-YNSYKDLSKRLVSQLKIGPHYTQVAAVTFAtvGRTRVRFNLKKYQTQEEVLRGIDNLKSRGGTT 192
Cdd:cd01472     2 DIVFLVDGSESIGLSnFNLVKDFVKRVVERLDIGPDGVRVGVVQYS--DDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 193 AIGAGIEKALTQL-DESEGARPGIAtKVMVVFTDGWSNkgPDPEKRARDAVSSGFEMYTVAYTAHtpgavtlNNETLSAI 271
Cdd:cd01472    80 NTGKALKYVRENLfTEASGSREGVP-KVLVVITDGKSQ--DDVEEPAVELKQAGIEVFAVGVKNA-------DEEELKQI 149

                         170
                  ....*....|....*
gi 1831512145 272 S--GDVHHTFTDVTF 284
Cdd:cd01472   150 AsdPKELYVFNVADF 164
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 113-253 9.08e-21

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: 86.85  E-value: 9.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 113 LDLVLVLDFS-TTTDPVYNSYKDLSKRLVSQLKIGPHYTQVAAVTFATvgRTRVRFNLKKYQTQEEVLRGIDNLKSR-GG 190
Cdd:cd00198     1 ADIVFLLDVSgSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGS--NARVVLPLTTDTDKADLLEAIDALKKGlGG 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831512145 191 TTAIGAGIEKALTQLDEsegARPGIATKVMVVFTDGWSNKGP-DPEKRARDAVSSGFEMYTVAY 253
Cdd:cd00198    79 GTNIGAALRLALELLKS---AKRPNARRVIILLTDGEPNDGPeLLAEAARELRKLGITVYTIGI 139
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 114-259 2.18e-20

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: 85.80  E-value: 2.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 114 DLVLVLDFS-TTTDPVYNSYKDLSKRLVSQLKIGPHYTQVAAVTFAtvGRTRVRFNLKKYQTQEEVLRGIDNLKSRGGTT 192
Cdd:cd01482     2 DIVFLVDGSwSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYS--DDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831512145 193 AIGAGIEKALTQ-LDESEGARPGIAtKVMVVFTDGWSNKgpDPEKRARDAVSSGFEMYTVAYTAHTPG 259
Cdd:cd01482    80 RTGKALTHVREKnFTPDAGARPGVP-KVVILITDGKSQD--DVELPARVLRNLGVNVFAVGVKDADES 144
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 113-251 8.23e-14

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: 69.34  E-value: 8.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 113 LDLVLVLDFSTTTDPV-YNSYKDLSKRLVSQLKIGPHYTQVAAVTFATvgRTRVRFNLKKYQTQEEVLRGIDNLK--SRG 189
Cdd:cd01475     3 TDLVFLIDSSRSVRPEnFELVKQFLNQIIDSLDVGPDATRVGLVQYSS--TVKQEFPLGRFKSKADLKRAVRRMEylETG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831512145 190 GTT--AIGAGIEKALTqldESEGARPG--IATKVMVVFTDGWSNKG-PDPEKRARDavsSGFEMYTV 251
Cdd:cd01475    81 TMTglAIQYAMNNAFS---EAEGARPGseRVPRVGIVVTDGRPQDDvSEVAAKARA---LGIEMFAV 141
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 113-272 2.05e-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: 68.81  E-value: 2.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 113 LDLVLVLD--FSTTTDPVYNSYKDLSKRLVSQLkigPHYTQVAAVTFATVGRTRVRFNLKKyqtqEEVLRGIDNLKSRGG 190
Cdd:COG1240    93 RDVVLVVDasGSMAAENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTRDR----EALKRALDELPPGGG 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 191 TtAIGAGIEKALTQLDESEGARPgiatKVMVVFTDGWSNKGP-DPEKRARDAVSSGFEMYTVAYtahtpGAVTLNNETLS 269
Cdd:COG1240   166 T-PLGDALALALELLKRADPARR----KVIVLLTDGRDNAGRiDPLEAAELAAAAGIRIYTIGV-----GTEAVDEGLLR 235


                  ...
gi 1831512145 270 AIS 272
Cdd:COG1240   236 EIA 238
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 111-289 9.33e-12

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: 62.79  E-value: 9.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 111 CELDLVLVLDFSTT-----TDPVYNSYKDLSKRLVSQ--LKIGPHYTQVAAVTFATVGRTRVRFnLKKYQTQEEVLRGID 183
Cdd:cd01480     1 GPVDITFVLDSSESvglqnFDITKNFVKRVAERFLKDyyRKDPAGSWRVGVVQYSDQQEVEAGF-LRDIRNYTSLKEAVD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 184 NLKSRGGTTAIGAGIEKALTQLDESegaRPGIATKVMVVFTDGWSNKGPD--PEKRARDAVSSGFEMYTVAYTAHtpgav 261
Cdd:cd01480    80 NLEYIGGGTFTDCALKYATEQLLEG---SHQKENKFLLVITDGHSDGSPDggIEKAVNEADHLGIKIFFVAVGSQ----- 151

                         170       180
                  ....*....|....*....|....*...
gi 1831512145 262 tlNNETLSAISGDVHHTFTDVTFQALID 289
Cdd:cd01480   152 --NEEPLSRIACDGKSALYRENFAELLW 177
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 114-287 4.48e-11

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: 60.60  E-value: 4.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 114 DLVLVLDFSTTTDP----VYNSYKDLSKRLVSqlkigPHyTQVAAVTFATvgRTRVRFNLKKYQtqEEVLRGIDNLKS-- 187
Cdd:cd01474     6 DLYFVLDKSGSVAAnwieIYDFVEQLVDRFNS-----PG-LRFSFITFST--RATKILPLTDDS--SAIIKGLEVLKKvt 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 188 RGGTTAIGAGIEKALTQL-DESEGARpgIATKVMVVFTDGWSNKGP--DPEKRARDAVSSGFEMYTVaytahtpGAVTLN 264
Cdd:cd01474    76 PSGQTYIHEGLENANEQIfNRNGGGR--ETVSVIIALTDGQLLLNGhkYPEHEAKLSRKLGAIVYCV-------GVTDFL 146

                         170       180
                  ....*....|....*....|....
gi 1831512145 265 NETLSAISGDVHHTF-TDVTFQAL 287
Cdd:cd01474   147 KSQLINIADSKEYVFpVTSGFQAL 170
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 113-239 1.80e-08

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: 53.16  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 113 LDLVLVLDFSTT--TDPVYNSYKDLSKRLVSQLKIGPHYTQVAAVTFATVGRTRVRF---NLKKYQTQEEVLRGIDNLKS 187
Cdd:cd01471     1 LDLYLLVDGSGSigYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLsspNSTNKDLALNAIRALLSLYY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1831512145 188 RGGTTAIGAGIEKALTQLDESEGARPGiATKVMVVFTDGWSNKGPDPEKRAR 239
Cdd:cd01471    81 PNGSTNTTSALLVVEKHLFDTRGNREN-APQLVIIMTDGIPDSKFRTLKEAR 131
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 113-286 2.25e-08

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: 52.66  E-value: 2.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 113 LDLVLVLDFSTT-TDPVYNSYKDLSKRLVSQLkiGPHyTQVAAVTFAtvGRTRVRFNLKKYQTQEEVLRGIDNLKSRGGT 191
Cdd:cd01465     1 LNLVFVIDRSGSmDGPKLPLVKSALKLLVDQL--RPD-DRLAIVTYD--GAAETVLPATPVRDKAAILAAIDRLTAGGST 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 192 tAIGAGIEKALTQLdeSEGARPGiATKVMVVFTDGWSNKGP-DPEKRARDAVS---SGFEMYTVAYTAHtpgavtLNNET 267
Cdd:cd01465    76 -AGGAGIQLGYQEA--QKHFVPG-GVNRILLATDGDFNVGEtDPDELARLVAQkreSGITLSTLGFGDN------YNEDL 145

                         170       180
                  ....*....|....*....|.
gi 1831512145 268 LSAI--SGDVHHTFTDVTFQA 286
Cdd:cd01465   146 MEAIadAGNGNTAYIDNLAEA 166
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 114-246 3.90e-08

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: 51.94  E-value: 3.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 114 DLVLVLDFSTTTDPV-YNSYKDLSKRLVSQLKIGPHYTQVAAVTFA-TVgrtRVRFNLKKYQTQEEVLRGIDNLKSRGG- 190
Cdd:cd01481     2 DIVFLIDGSDNVGSGnFPAIRDFIERIVQSLDVGPDKIRVAVVQFSdTP---RPEFYLNTHSTKADVLGAVRRLRLRGGs 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 191 ----------------TTAIGAGIEKALTQL------DESEGA--RPGIATKVMVVFTDGWSNKGPDPEKRARDAVSSGF 246
Cdd:cd01481    79 qlntgsaldyvvknlfTKSAGSRIEEGVPQFlvlitgGKSQDDveRPAVALKRAGIVPFAIGARNADLAELQQIAFDPSF 158
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 114-252 1.13e-07

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: 50.79  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 114 DLVLVLDFST---TTDPVYNSYKDLSKRLVSQLKIGPHYTQVAAVTFATVGRTRVRFNLKkYQTQEEVLRGIDNLKSRGG 190
Cdd:cd01467     4 DIMIALDVSGsmlAQDFVKPSRLEAAKEVLSDFIDRRENDRIGLVVFAGAAFTQAPLTLD-RESLKELLEDIKIGLAGQG 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831512145 191 TtAIGAGIEKALTQLDESEGARpgiatKVMVVFTDGWSNKGP-DPEKRARDAVSSGFEMYTVA 252
Cdd:cd01467    83 T-AIGDAIGLAIKRLKNSEAKE-----RVIVLLTDGENNAGEiDPATAAELAKNKGVRIYTIG 139
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 114-252 6.38e-06

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 46.60  E-value: 6.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 114 DLVLVLDFST--TTDPVYNSyKDLSKRLVSQLKigpHYTQVAAVTFATVGRTRVRfnLKKYQTQEEVLRGIDNLKSRGGT 191
Cdd:COG2425   120 PVVLCVDTSGsmAGSKEAAA-KAAALALLRALR---PNRRFGVILFDTEVVEDLP--LTADDGLEDAIEFLSGLFAGGGT 193

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831512145 192 tAIGAGIEKALTQLDESEGARpgiatKVMVVFTDGWSNKGPDPEKRARDAVSSGFEMYTVA 252
Cdd:COG2425   194 -DIAPALRAALELLEEPDYRN-----ADIVLITDGEAGVSPEELLREVRAKESGVRLFTVA 248
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 113-254 9.15e-05

VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. The members of this subgroup lack the MIDAS motif. This subgroup is found only in C. elegans and the members identified thus far are always found fused to a C-Lectin type domain. Biochemical function thus far has not be attributed to any of the members of this subgroup.


Pssm-ID: 238754 [Multi-domain]  Cd Length: 193  Bit Score: 42.41  E-value: 9.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 113 LDLVLVLDFS--TTTDPVYNSYKDLSKRLVSQLKIG-----PHYTQVAAVTF---ATVgrtrvRFNLKKYQTQEEV---L 179
Cdd:cd01477    20 LDIVFVVDNSkgMTQGGLWQVRATISSLFGSSSQIGtdyddPRSTRVGLVTYnsnATV-----VADLNDLQSFDDLysqI 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831512145 180 RGIDNLKSRGGTTAIGAGIEKALTQLDE-SEGARPGIaTKVMVVFTDGWSNKGP-DPEKRARDAVSSGFEMYTVAYT 254
Cdd:cd01477    95 QGSLTDVSSTNASYLDTGLQAAEQMLAAgKRTSRENY-KKVVIVFASDYNDEGSnDPRPIAARLKSTGIAIITVAFT 170
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 114-226 1.64e-03

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 38.84  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 114 DLVLVLDFSTTTDpvYNSYK----DLSKRLVSQLKIGPHYTQVAAVTFATVGRTRVRFNLKKYQTQEEVLRGIDNLKSR- 188
Cdd:cd01473     2 DLTLILDESASIG--YSNWRkdviPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERYDKNELLKKINDLKNSy 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1831512145 189 --GGTTAIGAGIEKALTQLDESEGARPGiATKVMVVFTDG 226
Cdd:cd01473    80 rsGGETYIVEALKYGLKNYTKHGNRRKD-APKVTMLFTDG 118
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 151-246 2.21e-03

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


Pssm-ID: 238728 [Multi-domain]  Cd Length: 178  Bit Score: 38.41  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831512145 151 QVAAVTFatvgrtrvrfnlkkYQTQEEVL----RGIDNLKSR------GGTTAIGAGIEKAlTQLDESEGARPGIATkVM 220
Cdd:cd01451    39 KVALIAF--------------RGTEAEVLlpptRSVELAKRRlarlptGGGTPLAAGLLAA-YELAAEQARDPGQRP-LI 102

                          90       100
                  ....*....|....*....|....*.
gi 1831512145 221 VVFTDGWSNKGPDPEKRARDAVSSGF 246
Cdd:cd01451   103 VVITDGRANVGPDPTADRALAAARKL 128
VWA pfam00092
von Willebrand factor type A domain;
8-61 3.04e-03

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 37.64  E-value: 3.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1831512145   8 IPTLVMVVTDGRSAD-DPKGPGQILQAQpNTWVFAAATGDpekVDTRELMDITGN 61
Cdd:pfam00092 103 APKVVVLLTDGRSQDgDPEEVARELKSA-GVTVFAVGVGN---ADDEELRKIASE 153
 
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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