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Conserved domains on  [gi|194306644|ref|NP_001123614|]
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von Willebrand factor A domain-containing protein 5A isoform 1 [Homo sapiens]

Protein Classification

VWA domain-containing protein( domain architecture ID 10652053)

VWA (von Willebrand factor type A) domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 278-456 5.72e-61

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: 203.22  E-value: 5.72e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644 278 TCGEFIFLMDRSGSMQSPMssqdtsqlrIQAAKETLILLLKSLPIGCYFNIYGFGSSYEACFPESVKYTQQTMEEALGRV 357
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTK---------IEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644 358 KLMQADlGGTEILAPLQNIYRGPSI-PGHPLQLFVFTDGEVTDTFSVIKEVRIN-RQKHRCFSFGIGEGTSTSLIKGIAR 435
Cdd:cd01461   72 NRLQAL-GGTNMNDALEAALELLNSsPGSVPQIILLTDGEVTNESQILKNVREAlSGRIRLFTFGIGSDVNTYLLERLAR 150

                        170       180
                 ....*....|....*....|.
gi 194306644 436 ASGGTSEFITGKDRMQSKALR 456
Cdd:cd01461  151 EGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
1-131 7.70e-51

Vault protein Inter-alpha-Trypsin domain;


:

Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 173.70  E-value: 7.70e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644     1 MVHFCGLLTLHREPVPLKSISVSVNIYEFVAGVSATLNYENEEkVPLEAFFVFPMDEDSAVYSFEAL-VDGKKIVAELQD 79
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRA-VPAQEVTFDVELPKTAFISNFAMtIDGKTYVGEIKE 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 194306644    80 KMKARTNYEKAISQGHQAFLLEGDSSSRDVFSCNVgNLQPGSKAAVTLKYVQ 131
Cdd:smart00609  80 KEVAQKQYEKAVSQGKTAGLVRASGRSMEQFTVSV-NVAPGSKVTFELTYEE 130
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 278-456 5.72e-61

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: 203.22  E-value: 5.72e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644 278 TCGEFIFLMDRSGSMQSPMssqdtsqlrIQAAKETLILLLKSLPIGCYFNIYGFGSSYEACFPESVKYTQQTMEEALGRV 357
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTK---------IEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644 358 KLMQADlGGTEILAPLQNIYRGPSI-PGHPLQLFVFTDGEVTDTFSVIKEVRIN-RQKHRCFSFGIGEGTSTSLIKGIAR 435
Cdd:cd01461   72 NRLQAL-GGTNMNDALEAALELLNSsPGSVPQIILLTDGEVTNESQILKNVREAlSGRIRLFTFGIGSDVNTYLLERLAR 150

                        170       180
                 ....*....|....*....|.
gi 194306644 436 ASGGTSEFITGKDRMQSKALR 456
Cdd:cd01461  151 EGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
1-131 7.70e-51

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 173.70  E-value: 7.70e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644     1 MVHFCGLLTLHREPVPLKSISVSVNIYEFVAGVSATLNYENEEkVPLEAFFVFPMDEDSAVYSFEAL-VDGKKIVAELQD 79
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRA-VPAQEVTFDVELPKTAFISNFAMtIDGKTYVGEIKE 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 194306644    80 KMKARTNYEKAISQGHQAFLLEGDSSSRDVFSCNVgNLQPGSKAAVTLKYVQ 131
Cdd:smart00609  80 KEVAQKQYEKAVSQGKTAGLVRASGRSMEQFTVSV-NVAPGSKVTFELTYEE 130
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 17-129 6.64e-39

Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilization and tumour metastasis as well as in plasma protease inhibition. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (pfam00092) in ITI heavy chains (ITIHs) and their precursors.


Pssm-ID: 462492 [Multi-domain]  Cd Length: 111  Bit Score: 139.54  E-value: 6.64e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644   17 LKSISVSVNIYEFVAGVSATLNYENEEKVPLEAFFVFPMDEDSAVYSFEALVDGKKIVAELQDKMKARTNYEKAISQGHQ 96
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 194306644   97 AFLLEgdSSSRDVFSCNVGNLQPGSKAAVTLKY 129
Cdd:pfam08487  81 AGLLE--QDTPDVFTTSVGNIPPGEKVTVELTY 111
VWA_3 pfam13768
von Willebrand factor type A domain;
280-443 4.67e-23

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 96.31  E-value: 4.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644  280 GEFIFLMDRSGSMQSPmssqdtsqlrIQAAKETLILLLKSLPIGCYFNIYGFGSSYEACFPESVKYTQQTMEEALGRVKL 359
Cdd:pfam13768   1 GDVVIVVDVSSSMSGE----------PKLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKT 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644  360 MQADLGGTEILAPLQNIYRGPSIPGHPLQLFVFTDGEVTD-TFSVIKEVRINRQKHRCFSFGIGEGTSTSLIKGIARASG 438
Cdd:pfam13768  71 LQPPLGGSDLLGALKEAVRAPASPGYIRHVLLLTDGSPMQgETRVSDLISRAPGKIRFFAYGLGASISAPMLQLLAEASN 150


                  ....*
gi 194306644  439 GTSEF 443
Cdd:pfam13768 151 GTYEF 155
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 225-473 7.24e-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: 84.77  E-value: 7.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644 225 DRDVELLIYYNEVHTPSVVLEMGMPNMKPGHLMgdpsAMVSFYPNIPEDQ---PSNtcgeFIFLMDRSGSMQSPmssqdt 301
Cdd:COG2304   42 AVRLEELVNFFPYDYPLPTGRLAQSPWNPQTRL----LLVGLQPPKAAAEerpPLN----LVFVIDVSGSMSGD------ 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644 302 sqlRIQAAKETLILLLKSLPIGCYFNIYGFGSSYEACFPeSVKYTQqtMEEALGRVKLMQADlGGTEILAPLQNIY---R 378
Cdd:COG2304  108 ---KLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLP-PTPATD--RAKILAAIDRLQAG-GGTALGAGLELAYelaR 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644 379 GPSIPGHPLQLFVFTDGE----VTDTFSVIKEVRINRQKH-RCFSFGIGEGTSTSLIKGIARASGGTSEFITGKDRMQSK 453
Cdd:COG2304  181 KHFIPGRVNRVILLTDGDanvgITDPEELLKLAEEAREEGiTLTTLGVGSDYNEDLLERLADAGGGNYYYIDDPEEAEKV 260

                        250       260
                 ....*....|....*....|....
gi 194306644 454 ALRTLKR----SLQPVVEDVSLSW 473
Cdd:COG2304  261 FVREFSRigyeNRALATEDFPLPY 284
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 282-443 6.42e-13

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: 67.48  E-value: 6.42e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644   282 FIFLMDRSGSMqspmssqdtSQLRIQAAKETLILLLKSLPIGC---YFNIYGFGSSYEACFPESVKYTQQTMEEALGRVK 358
Cdd:smart00327   2 VVFLLDGSGSM---------GGNRFELAKEFVLKLVEQLDIGPdgdRVGLVTFSDDARVLFPLNDSRSKDALLEALASLS 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644   359 lmQADLGGTEILAPLQNIY------RGPSIPGHPLQLFVFTDGEVTDTFSVIKEV--RINRQKHRCFSFGIGEGTSTSLI 430
Cdd:smart00327  73 --YKLGGGTNLGAALQYALenlfskSAGSRRGAPKVVILITDGESNDGPKDLLKAakELKRSGVKVFVVGVGNDVDEEEL 150

                          170
                   ....*....|...
gi 194306644   431 KGIARASGGTSEF 443
Cdd:smart00327 151 KKLASAPGGVYVF 163
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 278-456 5.72e-61

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: 203.22  E-value: 5.72e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644 278 TCGEFIFLMDRSGSMQSPMssqdtsqlrIQAAKETLILLLKSLPIGCYFNIYGFGSSYEACFPESVKYTQQTMEEALGRV 357
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTK---------IEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644 358 KLMQADlGGTEILAPLQNIYRGPSI-PGHPLQLFVFTDGEVTDTFSVIKEVRIN-RQKHRCFSFGIGEGTSTSLIKGIAR 435
Cdd:cd01461   72 NRLQAL-GGTNMNDALEAALELLNSsPGSVPQIILLTDGEVTNESQILKNVREAlSGRIRLFTFGIGSDVNTYLLERLAR 150

                        170       180
                 ....*....|....*....|.
gi 194306644 436 ASGGTSEFITGKDRMQSKALR 456
Cdd:cd01461  151 EGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
1-131 7.70e-51

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 173.70  E-value: 7.70e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644     1 MVHFCGLLTLHREPVPLKSISVSVNIYEFVAGVSATLNYENEEkVPLEAFFVFPMDEDSAVYSFEAL-VDGKKIVAELQD 79
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRA-VPAQEVTFDVELPKTAFISNFAMtIDGKTYVGEIKE 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 194306644    80 KMKARTNYEKAISQGHQAFLLEGDSSSRDVFSCNVgNLQPGSKAAVTLKYVQ 131
Cdd:smart00609  80 KEVAQKQYEKAVSQGKTAGLVRASGRSMEQFTVSV-NVAPGSKVTFELTYEE 130
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 17-129 6.64e-39

Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilization and tumour metastasis as well as in plasma protease inhibition. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (pfam00092) in ITI heavy chains (ITIHs) and their precursors.


Pssm-ID: 462492 [Multi-domain]  Cd Length: 111  Bit Score: 139.54  E-value: 6.64e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644   17 LKSISVSVNIYEFVAGVSATLNYENEEKVPLEAFFVFPMDEDSAVYSFEALVDGKKIVAELQDKMKARTNYEKAISQGHQ 96
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 194306644   97 AFLLEgdSSSRDVFSCNVGNLQPGSKAAVTLKY 129
Cdd:pfam08487  81 AGLLE--QDTPDVFTTSVGNIPPGEKVTVELTY 111
VWA_3 pfam13768
von Willebrand factor type A domain;
280-443 4.67e-23

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 96.31  E-value: 4.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644  280 GEFIFLMDRSGSMQSPmssqdtsqlrIQAAKETLILLLKSLPIGCYFNIYGFGSSYEACFPESVKYTQQTMEEALGRVKL 359
Cdd:pfam13768   1 GDVVIVVDVSSSMSGE----------PKLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKT 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644  360 MQADLGGTEILAPLQNIYRGPSIPGHPLQLFVFTDGEVTD-TFSVIKEVRINRQKHRCFSFGIGEGTSTSLIKGIARASG 438
Cdd:pfam13768  71 LQPPLGGSDLLGALKEAVRAPASPGYIRHVLLLTDGSPMQgETRVSDLISRAPGKIRFFAYGLGASISAPMLQLLAEASN 150


                  ....*
gi 194306644  439 GTSEF 443
Cdd:pfam13768 151 GTYEF 155
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 225-473 7.24e-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: 84.77  E-value: 7.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644 225 DRDVELLIYYNEVHTPSVVLEMGMPNMKPGHLMgdpsAMVSFYPNIPEDQ---PSNtcgeFIFLMDRSGSMQSPmssqdt 301
Cdd:COG2304   42 AVRLEELVNFFPYDYPLPTGRLAQSPWNPQTRL----LLVGLQPPKAAAEerpPLN----LVFVIDVSGSMSGD------ 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644 302 sqlRIQAAKETLILLLKSLPIGCYFNIYGFGSSYEACFPeSVKYTQqtMEEALGRVKLMQADlGGTEILAPLQNIY---R 378
Cdd:COG2304  108 ---KLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLP-PTPATD--RAKILAAIDRLQAG-GGTALGAGLELAYelaR 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644 379 GPSIPGHPLQLFVFTDGE----VTDTFSVIKEVRINRQKH-RCFSFGIGEGTSTSLIKGIARASGGTSEFITGKDRMQSK 453
Cdd:COG2304  181 KHFIPGRVNRVILLTDGDanvgITDPEELLKLAEEAREEGiTLTTLGVGSDYNEDLLERLADAGGGNYYYIDDPEEAEKV 260

                        250       260
                 ....*....|....*....|....
gi 194306644 454 ALRTLKR----SLQPVVEDVSLSW 473
Cdd:COG2304  261 FVREFSRigyeNRALATEDFPLPY 284
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 280-435 4.61e-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: 78.95  E-value: 4.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644 280 GEFIFLMDRSGSMQSPmssqdtsqlRIQAAKETLILLLKSLPIGCYFNIYGFGSSYEACFPESVKYTQQTMEEALGRVKL 359
Cdd:COG2425  119 GPVVLCVDTSGSMAGS---------KEAAAKAAALALLRALRPNRRFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLFA 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644 360 MqadlGGTEILAPL---QNIYRGPsiPGHPLQLFVFTDGEVT-DTFSVIKEVRINRQKHRCFSFGIGEGTSTSLIKGIAR 435
Cdd:COG2425  190 G----GGTDIAPALraaLELLEEP--DYRNADIVLITDGEAGvSPEELLREVRAKESGVRLFTVAIGDAGNPGLLEALAD 263
VIT_2 pfam13757
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 6-80 6.14e-14

Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilization and tumour metastasis as well as in plasma protease inhibition. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (pfam00092) in ITI heavy chains (ITIHs) and their precursors.


Pssm-ID: 404621  Cd Length: 78  Bit Score: 67.49  E-value: 6.14e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194306644    6 GLLTLH-REPVPLKSISVSVNIYEFVAGVSATLNYENEEKVPLEAFFVFPMDEDSAVYSFEALVDGKKIVAELQDK 80
Cdd:pfam13757   2 GLLNWStRTPLPLKASRVSACVNGYSLGVTASLTYYNPQPYPVEGVFVYPLDEGTTVVGFEAEIAGRVISVQLKER 77
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 282-443 6.42e-13

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: 67.48  E-value: 6.42e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644   282 FIFLMDRSGSMqspmssqdtSQLRIQAAKETLILLLKSLPIGC---YFNIYGFGSSYEACFPESVKYTQQTMEEALGRVK 358
Cdd:smart00327   2 VVFLLDGSGSM---------GGNRFELAKEFVLKLVEQLDIGPdgdRVGLVTFSDDARVLFPLNDSRSKDALLEALASLS 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644   359 lmQADLGGTEILAPLQNIY------RGPSIPGHPLQLFVFTDGEVTDTFSVIKEV--RINRQKHRCFSFGIGEGTSTSLI 430
Cdd:smart00327  73 --YKLGGGTNLGAALQYALenlfskSAGSRRGAPKVVILITDGESNDGPKDLLKAakELKRSGVKVFVVGVGNDVDEEEL 150

                          170
                   ....*....|...
gi 194306644   431 KGIARASGGTSEF 443
Cdd:smart00327 151 KKLASAPGGVYVF 163
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 283-443 1.28e-12

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: 66.44  E-value: 1.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644 283 IFLMDRSGSMQSPmssqdtsqlRIQAAKETLILLLKSLPIGC---YFNIYGFGSSYEACFPESVKYTQQTMEEALGRVKL 359
Cdd:cd00198    4 VFLLDVSGSMGGE---------KLDKAKEALKALVSSLSASPpgdRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644 360 MQAdlGGTEILAPLQ---NIYRGPSIPGHPLQLFVFTDGEVTDTFSVIKEV--RINRQKHRCFSFGIGEGTSTSLIKGIA 434
Cdd:cd00198   75 GLG--GGTNIGAALRlalELLKSAKRPNARRVIILLTDGEPNDGPELLAEAarELRKLGITVYTIGIGDDANEDELKEIA 152


                 ....*....
gi 194306644 435 RASGGTSEF 443
Cdd:cd00198  153 DKTTGGAVF 161
VWA_2 pfam13519
von Willebrand factor type A domain;
282-374 6.94e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 53.84  E-value: 6.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644  282 FIFLMDRSGSMqspmSSQDTSQLRIQAAKETLILLLKSLPiGCYFNIYGFGSSYEACFPesVKYTQQTMEEALGRVklmQ 361
Cdd:pfam13519   1 LVFVLDTSGSM----RNGDYGPTRLEAAKDAVLALLKSLP-GDRVGLVTFGDGPEVLIP--LTKDRAKILRALRRL---E 70

                          90
                  ....*....|...
gi 194306644  362 ADLGGTEILAPLQ 374
Cdd:pfam13519  71 PKGGGTNLAAALQ 83
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 282-445 5.35e-08

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: 54.94  E-value: 5.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644 282 FIFLMDRSGSMQSPMssqdtsqlRIQAAKETLILLLKSLPIGCYFNIYGFGSSYEACFPesvkYTQQTmEEALGRVKLMQ 361
Cdd:COG1240   95 VVLVVDASGSMAAEN--------RLEAAKGALLDFLDDYRPRDRVGLVAFGGEAEVLLP----LTRDR-EALKRALDELP 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644 362 ADlGGTEILAPLQNIYR--GPSIPGHPLQLFVFTDGEVTDTFSVIKEV--RINRQKHRCFSFGIG-EGTSTSLIKGIARA 436
Cdd:COG1240  162 PG-GGTPLGDALALALEllKRADPARRKVIVLLTDGRDNAGRIDPLEAaeLAAAAGIRIYTIGVGtEAVDEGLLREIAEA 240


                 ....*....
gi 194306644 437 SGGTSEFIT 445
Cdd:COG1240  241 TGGRYFRAD 249
VWA pfam00092
von Willebrand factor type A domain;
283-434 4.75e-06

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 47.65  E-value: 4.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644  283 IFLMDRSGSMqspmssqdtSQLRIQAAKETLILLLKSLPIGC---YFNIYGFGSSYEacfpESVKYTQ-QTMEEALGRVK 358
Cdd:pfam00092   3 VFLLDGSGSI---------GGDNFEKVKEFLKKLVESLDIGPdgtRVGLVQYSSDVR----TEFPLNDySSKEELLSAVD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644  359 LMQADLGGTE-----ILAPLQNIYRGP--SIPGHPLQLFVFTDGEVTDT--FSVIKEVRinRQKHRCFSFGIGEGTSTSL 429
Cdd:pfam00092  70 NLRYLGGGTTntgkaLKYALENLFSSAagARPGAPKVVVLLTDGRSQDGdpEEVARELK--SAGVTVFAVGVGNADDEEL 147


                  ....*
gi 194306644  430 IKgIA 434
Cdd:pfam00092 148 RK-IA 151
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 282-445 1.54e-04

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: 43.03  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644 282 FIFLMDRSGSMQSPmssqdtsqlRIQAAKETLILLLKSLPIGCYFNIYGFGSSYEACFPESVKYTQQTMEEALGRVKLMq 361
Cdd:cd01465    3 LVFVIDRSGSMDGP---------KLPLVKSALKLLVDQLRPDDRLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTAG- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194306644 362 adlGGTEILAPLQNIYRGPS---IPGHPLQLFVFTDGEVTDTFSVIKEVRINRQKHR-----CFSFGIGEGTSTSLIKGI 433
Cdd:cd01465   73 ---GSTAGGAGIQLGYQEAQkhfVPGGVNRILLATDGDFNVGETDPDELARLVAQKResgitLSTLGFGDNYNEDLMEAI 149

                        170
                 ....*....|..
gi 194306644 434 ARASGGTSEFIT 445
Cdd:cd01465  150 ADAGNGNTAYID 161
 
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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