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Conserved domains on  [gi|498287076|ref|WP_010601232|]
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VWA domain-containing protein [Pedobacter agri]

Protein Classification

vWA domain-containing protein( domain architecture ID 10008387)

vWA (von Willebrand factor type A) domain-containing protein may be involved in one of a wide variety of important cellular functions, including basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and immune defenses

CATH:  3.40.50.410
PubMed:  12579041|10830113|12388743
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
1-188 1.04e-83

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


:

Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 246.76  E-value: 1.04e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076   1 MRRLPVYLLLDTSGSMSGEPIEAVKNGVQVMISSLRQNPQAIETAFLSVITFDSAAQQIIPLTDLASFQMVDLRATGVTA 80
Cdd:COG4245    3 MRRLPVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYALETVEVSVITFDGEAKVLLPLTDLEDFQPPDLSASGGTP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076  81 LGEALKLVSNRIENEVAKTTTEQKGDWKPLVFIMTDGVPTD-DWLPGLAEFK----KQRVAFtVACAAGSGADTTVLKQI 155
Cdd:COG4245   83 LGAALELLLDLIERRVQKYTAEGKGDWRPVVFLITDGEPTDsDWEAALQRLKdgeaAKKANI-FAIGVGPDADTEVLKQL 161

                        170       180       190
                 ....*....|....*....|....*....|...
gi 498287076 156 TENVVSLDTADSASIGKFFQWVTASIGVTSTKV 188
Cdd:COG4245  162 TDPVRALDALDGLDFREFFKWLSASVSSVSRSV 194
 
Name Accession Description Interval E-value
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
1-188 1.04e-83

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 246.76  E-value: 1.04e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076   1 MRRLPVYLLLDTSGSMSGEPIEAVKNGVQVMISSLRQNPQAIETAFLSVITFDSAAQQIIPLTDLASFQMVDLRATGVTA 80
Cdd:COG4245    3 MRRLPVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYALETVEVSVITFDGEAKVLLPLTDLEDFQPPDLSASGGTP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076  81 LGEALKLVSNRIENEVAKTTTEQKGDWKPLVFIMTDGVPTD-DWLPGLAEFK----KQRVAFtVACAAGSGADTTVLKQI 155
Cdd:COG4245   83 LGAALELLLDLIERRVQKYTAEGKGDWRPVVFLITDGEPTDsDWEAALQRLKdgeaAKKANI-FAIGVGPDADTEVLKQL 161

                        170       180       190
                 ....*....|....*....|....*....|...
gi 498287076 156 TENVVSLDTADSASIGKFFQWVTASIGVTSTKV 188
Cdd:COG4245  162 TDPVRALDALDGLDFREFFKWLSASVSSVSRSV 194
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 1-176 1.63e-78

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: 232.62  E-value: 1.63e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076   1 MRRLPVYLLLDTSGSMSGEPIEAVKNGVQVMISSLRQNPQAIETAFLSVITFDSAAQQIIPLTDLASFQMVDLRATGVTA 80
Cdd:cd01464    1 MRRLPIYLLLDTSGSMAGEPIEALNQGLQMLQSELRQDPYALESVEISVITFDSAARVIVPLTPLESFQPPRLTASGGTS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076  81 LGEALKLVSNRIENEVAKTTTEQKGDWKPLVFIMTDGVPTDDWLPGLAEFKKQRVAFT--VACAAGSGADTTVLKQITEN 158
Cdd:cd01464   81 MGAALELALDCIDRRVQRYRADQKGDWRPWVFLLTDGEPTDDLTAAIERIKEARDSKGriVACAVGPKADLDTLKQITEG 160

                        170
                 ....*....|....*...
gi 498287076 159 VVSLDtaDSASIGKFFQW 176
Cdd:cd01464  161 VPLLD--DALSGLNFFKW 176
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 6-177 6.84e-19

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: 80.19  E-value: 6.84e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076     6 VYLLLDTSGSMSGEPIEAVKNGVQVMISSLRQNPQAIEtafLSVITFDSAAQQIIPLTDLASFQMV-------DLRATGV 78
Cdd:smart00327   2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDR---VGLVTFSDDARVLFPLNDSRSKDALlealaslSYKLGGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076    79 TALGEALKLVSNRIENEVAKttteQKGDWKPLVFIMTDGVPTDDWLPGL--AEFKKQRVAFTVACAAGSGADTTVLKQIT 156
Cdd:smart00327  79 TNLGAALQYALENLFSKSAG----SRRGAPKVVILITDGESNDGPKDLLkaAKELKRSGVKVFVVGVGNDVDEEELKKLA 154

                          170       180
                   ....*....|....*....|.
gi 498287076   157 ENVVSLDTADSASIGKFFQWV 177
Cdd:smart00327 155 SAPGGVYVFLPELLDLLIDLL 175
VWA pfam00092
von Willebrand factor type A domain;
6-156 1.58e-14

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 68.46  E-value: 1.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076    6 VYLLLDTSGSMSGEPIEAVKNGVQVMISSLRQNPQAIEtafLSVITFDSAAQQIIPLTDLASFQMV-------DLRATGV 78
Cdd:pfam00092   2 IVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTR---VGLVQYSSDVRTEFPLNDYSSKEELlsavdnlRYLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076   79 TALGEALKLVSNRIENEVAktttEQKGDWKPLVFIMTDGVPTD-DWLPGLAEFKKQRVA-FTVACaagSGADTTVLKQIT 156
Cdd:pfam00092  79 TNTGKALKYALENLFSSAA----GARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTvFAVGV---GNADDEELRKIA 151
 
Name Accession Description Interval E-value
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
1-188 1.04e-83

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 246.76  E-value: 1.04e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076   1 MRRLPVYLLLDTSGSMSGEPIEAVKNGVQVMISSLRQNPQAIETAFLSVITFDSAAQQIIPLTDLASFQMVDLRATGVTA 80
Cdd:COG4245    3 MRRLPVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYALETVEVSVITFDGEAKVLLPLTDLEDFQPPDLSASGGTP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076  81 LGEALKLVSNRIENEVAKTTTEQKGDWKPLVFIMTDGVPTD-DWLPGLAEFK----KQRVAFtVACAAGSGADTTVLKQI 155
Cdd:COG4245   83 LGAALELLLDLIERRVQKYTAEGKGDWRPVVFLITDGEPTDsDWEAALQRLKdgeaAKKANI-FAIGVGPDADTEVLKQL 161

                        170       180       190
                 ....*....|....*....|....*....|...
gi 498287076 156 TENVVSLDTADSASIGKFFQWVTASIGVTSTKV 188
Cdd:COG4245  162 TDPVRALDALDGLDFREFFKWLSASVSSVSRSV 194
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 1-176 1.63e-78

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: 232.62  E-value: 1.63e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076   1 MRRLPVYLLLDTSGSMSGEPIEAVKNGVQVMISSLRQNPQAIETAFLSVITFDSAAQQIIPLTDLASFQMVDLRATGVTA 80
Cdd:cd01464    1 MRRLPIYLLLDTSGSMAGEPIEALNQGLQMLQSELRQDPYALESVEISVITFDSAARVIVPLTPLESFQPPRLTASGGTS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076  81 LGEALKLVSNRIENEVAKTTTEQKGDWKPLVFIMTDGVPTDDWLPGLAEFKKQRVAFT--VACAAGSGADTTVLKQITEN 158
Cdd:cd01464   81 MGAALELALDCIDRRVQRYRADQKGDWRPWVFLLTDGEPTDDLTAAIERIKEARDSKGriVACAVGPKADLDTLKQITEG 160

                        170
                 ....*....|....*...
gi 498287076 159 VVSLDtaDSASIGKFFQW 176
Cdd:cd01464  161 VPLLD--DALSGLNFFKW 176
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 6-177 6.84e-19

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: 80.19  E-value: 6.84e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076     6 VYLLLDTSGSMSGEPIEAVKNGVQVMISSLRQNPQAIEtafLSVITFDSAAQQIIPLTDLASFQMV-------DLRATGV 78
Cdd:smart00327   2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDR---VGLVTFSDDARVLFPLNDSRSKDALlealaslSYKLGGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076    79 TALGEALKLVSNRIENEVAKttteQKGDWKPLVFIMTDGVPTDDWLPGL--AEFKKQRVAFTVACAAGSGADTTVLKQIT 156
Cdd:smart00327  79 TNLGAALQYALENLFSKSAG----SRRGAPKVVILITDGESNDGPKDLLkaAKELKRSGVKVFVVGVGNDVDEEELKKLA 154

                          170       180
                   ....*....|....*....|.
gi 498287076   157 ENVVSLDTADSASIGKFFQWV 177
Cdd:smart00327 155 SAPGGVYVFLPELLDLLIDLL 175
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 8-168 7.27e-18

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 79.76  E-value: 7.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076   8 LLLDTSGSMSGEPIEAVKNGVQVMISSLRqnPQAIetafLSVITFDSAAQQIIPLTDLAS----FQMVD-LRATGVTALG 82
Cdd:COG2304   96 FVIDVSGSMSGDKLELAKEAAKLLVDQLR--PGDR----VSIVTFAGDARVLLPPTPATDrakiLAAIDrLQAGGGTALG 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076  83 EALKLVSNRIEnevakttTEQKGDWKPLVFIMTDGVPT-----DDWLPGLAEFKKQRVAFTVACAAGSGADTTVLKQITE 157
Cdd:COG2304  170 AGLELAYELAR-------KHFIPGRVNRVILLTDGDANvgitdPEELLKLAEEAREEGITLTTLGVGSDYNEDLLERLAD 242

                        170
                 ....*....|....*
gi 498287076 158 ----NVVSLDTADSA 168
Cdd:COG2304  243 agggNYYYIDDPEEA 257
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 6-159 3.12e-17

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: 75.29  E-value: 3.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076   6 VYLLLDTSGSMSGEPIEAVKNGVQVMISSLRQNPQAIEtafLSVITFDSAAQQIIPLTDLAS-------FQMVDLRATGV 78
Cdd:cd00198    3 IVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDR---VGLVTFGSNARVVLPLTTDTDkadlleaIDALKKGLGGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076  79 TALGEALKLVSNRIENevaktttEQKGDWKPLVFIMTDGVPTDDWLPGLAEFK--KQRVAFTVACAAGSGADTTVLKQIT 156
Cdd:cd00198   80 TNIGAALRLALELLKS-------AKRPNARRVIILLTDGEPNDGPELLAEAARelRKLGITVYTIGIGDDANEDELKEIA 152


                 ...
gi 498287076 157 ENV 159
Cdd:cd00198  153 DKT 155
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 2-157 4.65e-16

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 74.33  E-value: 4.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076   2 RRLPVYLLLDTSGSMSGEPIEAVKNGVQVMISSLRQNPQaietafLSVITFDSAAQQIIPLTDLASF-QMVD----LRAT 76
Cdd:COG2425  117 LEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRR------FGVILFDTEVVEDLPLTADDGLeDAIEflsgLFAG 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076  77 GVTALGEALKLVSNRIENEVAKTTTeqkgdwkplVFIMTDGVPTDDWLPGLAEFKKQRVAFTVACAA-GSGADTTVLKQI 155
Cdd:COG2425  191 GGTDIAPALRAALELLEEPDYRNAD---------IVLITDGEAGVSPEELLREVRAKESGVRLFTVAiGDAGNPGLLEAL 261


                 ..
gi 498287076 156 TE 157
Cdd:COG2425  262 AD 263
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1-157 4.45e-15

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: 71.51  E-value: 4.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076   1 MRRLPVYLLLDTSGSMSGEP-IEAVKNGVQVMISSLRQNPQaietafLSVITFDSAAQQIIPLT-DLASFQMV--DLRAT 76
Cdd:COG1240   90 QRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRDR------VGLVAFGGEAEVLLPLTrDREALKRAldELPPG 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076  77 GVTALGEALKLVSNRIENEVAKTtteqkgdwKPLVFIMTDGVPTD---DWLPGLAEFKKQRV-AFTVACAAGSgADTTVL 152
Cdd:COG1240  164 GGTPLGDALALALELLKRADPAR--------RKVIVLLTDGRDNAgriDPLEAAELAAAAGIrIYTIGVGTEA-VDEGLL 234


                 ....*
gi 498287076 153 KQITE 157
Cdd:COG1240  235 REIAE 239
VWA pfam00092
von Willebrand factor type A domain;
6-156 1.58e-14

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 68.46  E-value: 1.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076    6 VYLLLDTSGSMSGEPIEAVKNGVQVMISSLRQNPQAIEtafLSVITFDSAAQQIIPLTDLASFQMV-------DLRATGV 78
Cdd:pfam00092   2 IVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTR---VGLVQYSSDVRTEFPLNDYSSKEELlsavdnlRYLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076   79 TALGEALKLVSNRIENEVAktttEQKGDWKPLVFIMTDGVPTD-DWLPGLAEFKKQRVA-FTVACaagSGADTTVLKQIT 156
Cdd:pfam00092  79 TNTGKALKYALENLFSSAA----GARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTvFAVGV---GNADDEELRKIA 151
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 8-87 7.27e-10

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


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 55.74  E-value: 7.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076   8 LLLDTSGSMSGEPIEAVKNGVQVMISSLRqnpqaiETAFLSVITFDSAAQQIIPLT---DLASF--QMVDLRATGVTALG 82
Cdd:cd01465    5 FVIDRSGSMDGPKLPLVKSALKLLVDQLR------PDDRLAIVTYDGAAETVLPATpvrDKAAIlaAIDRLTAGGSTAGG 78


                 ....*
gi 498287076  83 EALKL 87
Cdd:cd01465   79 AGIQL 83
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 4-122 2.62e-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: 51.62  E-value: 2.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076   4 LPVYLLLDTSGSMsGE--PIEAVKNGVQVMISSLRQNPQAIEtafLSVITFDSAAQQIIPLT-------DLASFQMVDLR 74
Cdd:cd01471    1 LDLYLLVDGSGSI-GYsnWVTHVVPFLHTFVQNLNISPDEIN---LYLVTFSTNAKELIRLSspnstnkDLALNAIRALL 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 498287076  75 ----ATGVTALGEALKLVsnrieNEVAKTTTEQKGDWKPLVFIMTDGVPTDD 122
Cdd:cd01471   77 slyyPNGSTNTTSALLVV-----EKHLFDTRGNRENAPQLVIIMTDGIPDSK 123
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 6-156 6.03e-08

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: 50.37  E-value: 6.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076   6 VYLLLDTSGSMSGEPIEAVKNGVQVMISSLRQNPQAIetaFLSVITFDSAAQQIIPLTDLASFQMV-------DLRATGV 78
Cdd:cd01450    3 IVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKT---RVGLVQYSDDVRVEFSLNDYKSKDDLlkavknlKYLGGGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076  79 TALGEALKLVSNRIENEVAKTTTEQKgdwkpLVFIMTDGVPTDDWLPGLA--EFKKQRVA-FTVACAAgsgADTTVLKQI 155
Cdd:cd01450   80 TNTGKALQYALEQLFSESNARENVPK-----VIIVLTDGRSDDGGDPKEAaaKLKDEGIKvFVVGVGP---ADEEELREI 151


                 .
gi 498287076 156 T 156
Cdd:cd01450  152 A 152
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 6-157 1.90e-07

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: 49.14  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076   6 VYLLLDTSGSMSGEPIEAVKNGVQVMISSLRQNPQaietafLSVITFDSAAQQIIPltdlaSFQMVD------------- 72
Cdd:cd01461    5 VVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDY------FNIIGFSDTVEEFSP-----SSVSATaenvaaaieyvnr 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076  73 LRATGVT----ALGEALKLvSNRIENEVakttteqkgdwkPLVFIMTDGVPTDdwlpglaEFK-----KQRVAFTVAC-- 141
Cdd:cd01461   74 LQALGGTnmndALEAALEL-LNSSPGSV------------PQIILLTDGEVTN-------ESQilknvREALSGRIRLft 133

                        170
                 ....*....|....*..
gi 498287076 142 -AAGSGADTTVLKQITE 157
Cdd:cd01461  134 fGIGSDVNTYLLERLAR 150
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 5-162 3.77e-07

VWA YIEM 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 have a conserved MIDAS motif, however, their biochemical function is not well characterised.


Pssm-ID: 238739 [Multi-domain]  Cd Length: 152  Bit Score: 47.73  E-value: 3.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076   5 PVYLLLDTSGSMSGEPIEAVKngvQVMISSLRQNPQAIETafLSVITFDSAAQ-QIIPLTDLASfQMVDL----RATGVT 79
Cdd:cd01462    2 PVILLVDQSGSMYGAPEEVAK---AVALALLRIALAENRD--TYLILFDSEFQtKIVDKTDDLE-EPVEFlsgvQLGGGT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076  80 ALGEALKLVSNRIENEvakttTEQKGDwkpLVFImTDGV---PTDDWLPGLAEFKKQRVAFTVACAAGSGADTTVLKQIT 156
Cdd:cd01462   76 DINKALRYALELIERR-----DPRKAD---IVLI-TDGYeggVSDELLREVELKRSRVARFVALALGDHGNPGYDRISAE 146


                 ....*.
gi 498287076 157 ENVVSL 162
Cdd:cd01462  147 DELVGR 152
VWA_2 pfam13519
von Willebrand factor type A domain;
6-95 4.34e-07

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 46.52  E-value: 4.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076    6 VYLLLDTSGSMSGE-----PIEAVKNGVQVMISSLRQNpqaietaFLSVITFDSAAQQIIPLTDLASFQMVDLRAT---- 76
Cdd:pfam13519   1 LVFVLDTSGSMRNGdygptRLEAAKDAVLALLKSLPGD-------RVGLVTFGDGPEVLIPLTKDRAKILRALRRLepkg 73

                          90
                  ....*....|....*....
gi 498287076   77 GVTALGEALKLVSNRIENE 95
Cdd:pfam13519  74 GGTNLAAALQLARAALKHR 92
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 8-121 1.18e-05

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: 43.92  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076   8 LLLDTSGSMSGEPIEAVKNGVQVMISSLRqnpqaiETAFLSVITFDSAAQQIIPL---TDLASFQ---MVD-LRATGVT- 79
Cdd:cd01466    5 AVLDVSGSMAGDKLQLVKHALRFVISSLG------DADRLSIVTFSTSAKRLSPLrrmTAKGKRSakrVVDgLQAGGGTn 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 498287076  80 ---ALGEALKLVSNRIENEVAKTtteqkgdwkplVFIMTDGVPTD 121
Cdd:cd01466   79 vvgGLKKALKVLGDRRQKNPVAS-----------IMLLSDGQDNH 112
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 6-119 3.44e-03

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


Pssm-ID: 238740 [Multi-domain]  Cd Length: 190  Bit Score: 36.99  E-value: 3.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498287076   6 VYLLLDTSGSMSGEPIEAVKNGVQVMISSLRQNPqaietaFLSVITFDSAAQQIIP----------LTDLASFQ--MVDL 73
Cdd:cd01463   16 IVILLDVSGSMTGQRLHLAKQTVSSILDTLSDND------FFNIITFSNEVNPVVPcfndtlvqatTSNKKVLKeaLDML 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 498287076  74 RATGVTALGEALKLVSNRIENEVAKTTTEQKGDWKPLVFIMTDGVP 119
Cdd:cd01463   90 EAKGIANYTKALEFAFSLLLKNLQSNHSGSRSQCNQAIMLITDGVP 135
 
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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