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Conserved domains on  [gi|1985430095|ref|XP_039355487|]
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von Willebrand factor A domain-containing protein 5A-like isoform X2 [Mauremys reevesii]

Protein Classification

VIT and VWA domain-containing protein( domain architecture ID 10553342)

VIT (vault protein inter-alpha-trypsin) and 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
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 278-414 6.92e-36

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 cd01461:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 171  Bit Score: 129.64  E-value: 6.92e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095 278 SGEFIFLLDRSGSMrcpidgrdrSPQRIDSAKETLVLLLKSLPLGCYFNIYGFGSRFESFYPQSVAYTQQTMAESLQRIQ 357
Cdd:cd01461     2 PKEVVFVIDTSGSM---------SGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVN 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1985430095 358 QLQADlGGTEILAPLRAIYRSPCRD-GHPRQLFVFTDGEVGNTKDVITEVQRH-QRSHR 414
Cdd:cd01461    73 RLQAL-GGTNMNDALEAALELLNSSpGSVPQIILLTDGEVTNESQILKNVREAlSGRIR 130
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 16-128 1.56e-33

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: 121.44  E-value: 1.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095  16 LRSGSVTVLIRGFVADVGCELLYRNDEQGPVEAVFVFPVDAEAAVYAFQARLGGACIQAQLREKKQAQEMYGDALAGGQS 95
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1985430095  96 SFLLQQEgaGGDVFSCSLGNLPPGEEAALTLRY 128
Cdd:pfam08487  81 AGLLEQD--TPDVFTTSVGNIPPGEKVTVELTY 111
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 278-414 6.92e-36

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: 129.64  E-value: 6.92e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095 278 SGEFIFLLDRSGSMrcpidgrdrSPQRIDSAKETLVLLLKSLPLGCYFNIYGFGSRFESFYPQSVAYTQQTMAESLQRIQ 357
Cdd:cd01461     2 PKEVVFVIDTSGSM---------SGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVN 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1985430095 358 QLQADlGGTEILAPLRAIYRSPCRD-GHPRQLFVFTDGEVGNTKDVITEVQRH-QRSHR 414
Cdd:cd01461    73 RLQAL-GGTNMNDALEAALELLNSSpGSVPQIILLTDGEVTNESQILKNVREAlSGRIR 130
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 16-128 1.56e-33

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: 121.44  E-value: 1.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095  16 LRSGSVTVLIRGFVADVGCELLYRNDEQGPVEAVFVFPVDAEAAVYAFQARLGGACIQAQLREKKQAQEMYGDALAGGQS 95
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1985430095  96 SFLLQQEgaGGDVFSCSLGNLPPGEEAALTLRY 128
Cdd:pfam08487  81 AGLLEQD--TPDVFTTSVGNIPPGEKVTVELTY 111
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
4-129 1.85e-18

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 80.87  E-value: 1.85e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095    4 CGLLNSSNKPVPLRSGSVTVLIRGFVADVGCELLYRNdEQGPVEAVFVFPVDAEAAVYAFQA-RLGGACIQAQLREKKQA 82
Cdd:smart00609   5 RGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVN-RAVPAQEVTFDVELPKTAFISNFAmTIDGKTYVGEIKEKEVA 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1985430095   83 QEMYGDALAGGQSSFLLQQEGAGGDVFSCSLgNLPPGEEAALTLRYV 129
Cdd:smart00609  84 QKQYEKAVSQGKTAGLVRASGRSMEQFTVSV-NVAPGSKVTFELTYE 129
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 156-414 1.76e-12

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 67.01  E-value: 1.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095 156 GWDGEDVTQGVPRVPQGELPYTLSLSATLQSPHGIDRVLSNCSLTPLSYTAGNWTSAQVSLAeapPWGRDVELLVYYAEP 235
Cdd:COG2425     1 GVPDAAAAARLAALLLAPAPATALLLAGLLRAALALGLALALRAALLALLLLLLRAALALLT---LLAGLVLLALDALLL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095 236 HKPSAVLELGLPGAEPGSLMGDPAVMVTLLPSLPEAVPGqsPSGEFIFLLDRSGSMRCPidgrdrspqRIDSAKETLVLL 315
Cdd:COG2425    78 AALLAALLDALLLAVLLLALLLLAALLLLAAPASAAVPL--LEGPVVLCVDTSGSMAGS---------KEAAAKAAALAL 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095 316 LKSLPLGCYFNIYGFGSRFESFYPQSvayTQQTMAESLQRIQQLQADlGGTEILAPLRA---IYRSPcrDGHPRQLFVFT 392
Cdd:COG2425   147 LRALRPNRRFGVILFDTEVVEDLPLT---ADDGLEDAIEFLSGLFAG-GGTDIAPALRAaleLLEEP--DYRNADIVLIT 220

                         250       260
                  ....*....|....*....|...
gi 1985430095 393 DGEVGNT-KDVITEVQRHQRSHR 414
Cdd:COG2425   221 DGEAGVSpEELLREVRAKESGVR 243
VWA_3 pfam13768
von Willebrand factor type A domain;
279-411 2.87e-11

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 61.26  E-value: 2.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095 279 GEFIFLLDRSGSMRCPIDgrdrspqridSAKETLVLLLKSLPLGCYFNIYGFGSRFESFYPQSVAYTQQTMAESLQRIQQ 358
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEPK----------LQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKT 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1985430095 359 LQADLGGTEILAPLRAIYRSPCRDGHPRQLFVFTDGEVGN-TKDVITEVQRHQR 411
Cdd:pfam13768  71 LQPPLGGSDLLGALKEAVRAPASPGYIRHVLLLTDGSPMQgETRVSDLISRAPG 124
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 281-409 2.48e-05

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: 44.37  E-value: 2.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095  281 FIFLLDRSGSMRcpidgrdrsPQRIDSAKETLVL---LLKSLPLGCYFNIYGFGSRFESFYPQSVAYTQQTMAESLQRIQ 357
Cdd:smart00327   2 VVFLLDGSGSMG---------GNRFELAKEFVLKlveQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLS 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985430095  358 qlQADLGGTEILAPLRAIY------RSPCRDGHPRQLFVFTDGEV----GNTKDVITEVQRH 409
Cdd:smart00327  73 --YKLGGGTNLGAALQYALenlfskSAGSRRGAPKVVILITDGESndgpKDLLKAAKELKRS 132
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 278-414 6.92e-36

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: 129.64  E-value: 6.92e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095 278 SGEFIFLLDRSGSMrcpidgrdrSPQRIDSAKETLVLLLKSLPLGCYFNIYGFGSRFESFYPQSVAYTQQTMAESLQRIQ 357
Cdd:cd01461     2 PKEVVFVIDTSGSM---------SGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVN 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1985430095 358 QLQADlGGTEILAPLRAIYRSPCRD-GHPRQLFVFTDGEVGNTKDVITEVQRH-QRSHR 414
Cdd:cd01461    73 RLQAL-GGTNMNDALEAALELLNSSpGSVPQIILLTDGEVTNESQILKNVREAlSGRIR 130
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 16-128 1.56e-33

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: 121.44  E-value: 1.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095  16 LRSGSVTVLIRGFVADVGCELLYRNDEQGPVEAVFVFPVDAEAAVYAFQARLGGACIQAQLREKKQAQEMYGDALAGGQS 95
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1985430095  96 SFLLQQEgaGGDVFSCSLGNLPPGEEAALTLRY 128
Cdd:pfam08487  81 AGLLEQD--TPDVFTTSVGNIPPGEKVTVELTY 111
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
4-129 1.85e-18

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 80.87  E-value: 1.85e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095    4 CGLLNSSNKPVPLRSGSVTVLIRGFVADVGCELLYRNdEQGPVEAVFVFPVDAEAAVYAFQA-RLGGACIQAQLREKKQA 82
Cdd:smart00609   5 RGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVN-RAVPAQEVTFDVELPKTAFISNFAmTIDGKTYVGEIKEKEVA 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1985430095   83 QEMYGDALAGGQSSFLLQQEGAGGDVFSCSLgNLPPGEEAALTLRYV 129
Cdd:smart00609  84 QKQYEKAVSQGKTAGLVRASGRSMEQFTVSV-NVAPGSKVTFELTYE 129
VIT_2 pfam13757
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 5-80 1.47e-12

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: 62.87  E-value: 1.47e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1985430095   5 GLLN-SSNKPVPLRSGSVTVLIRGFVADVGCELLYRNDEQGPVEAVFVFPVDAEAAVYAFQARLGGACIQAQLREKK 80
Cdd:pfam13757   2 GLLNwSTRTPLPLKASRVSACVNGYSLGVTASLTYYNPQPYPVEGVFVYPLDEGTTVVGFEAEIAGRVISVQLKERE 78
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 156-414 1.76e-12

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 67.01  E-value: 1.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095 156 GWDGEDVTQGVPRVPQGELPYTLSLSATLQSPHGIDRVLSNCSLTPLSYTAGNWTSAQVSLAeapPWGRDVELLVYYAEP 235
Cdd:COG2425     1 GVPDAAAAARLAALLLAPAPATALLLAGLLRAALALGLALALRAALLALLLLLLRAALALLT---LLAGLVLLALDALLL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095 236 HKPSAVLELGLPGAEPGSLMGDPAVMVTLLPSLPEAVPGqsPSGEFIFLLDRSGSMRCPidgrdrspqRIDSAKETLVLL 315
Cdd:COG2425    78 AALLAALLDALLLAVLLLALLLLAALLLLAAPASAAVPL--LEGPVVLCVDTSGSMAGS---------KEAAAKAAALAL 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095 316 LKSLPLGCYFNIYGFGSRFESFYPQSvayTQQTMAESLQRIQQLQADlGGTEILAPLRA---IYRSPcrDGHPRQLFVFT 392
Cdd:COG2425   147 LRALRPNRRFGVILFDTEVVEDLPLT---ADDGLEDAIEFLSGLFAG-GGTDIAPALRAaleLLEEP--DYRNADIVLIT 220

                         250       260
                  ....*....|....*....|...
gi 1985430095 393 DGEVGNT-KDVITEVQRHQRSHR 414
Cdd:COG2425   221 DGEAGVSpEELLREVRAKESGVR 243
VWA_3 pfam13768
von Willebrand factor type A domain;
279-411 2.87e-11

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 61.26  E-value: 2.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095 279 GEFIFLLDRSGSMRCPIDgrdrspqridSAKETLVLLLKSLPLGCYFNIYGFGSRFESFYPQSVAYTQQTMAESLQRIQQ 358
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEPK----------LQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKT 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1985430095 359 LQADLGGTEILAPLRAIYRSPCRDGHPRQLFVFTDGEVGN-TKDVITEVQRHQR 411
Cdd:pfam13768  71 LQPPLGGSDLLGALKEAVRAPASPGYIRHVLLLTDGSPMQgETRVSDLISRAPG 124
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 203-409 2.84e-10

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 60.89  E-value: 2.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095 203 SYTAGNWTSAQVSLAEAPPWGRDVELLVYYAEPHKPSAVLELGLPGAEPGSLMgdpaVMVTLLPslPEAVPGQSPSGEFI 282
Cdd:COG2304    22 AASSSNRRRLLVGGEPPPAAAVRLEELVNFFPYDYPLPTGRLAQSPWNPQTRL----LLVGLQP--PKAAAEERPPLNLV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095 283 FLLDRSGSMrcpidgrdrSPQRIDSAKETLVLLLKSLPLGCYFNIYGFGSRFESFYPQSVAYTQQTMaesLQRIQQLQAD 362
Cdd:COG2304    96 FVIDVSGSM---------SGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPPTPATDRAKI---LAAIDRLQAG 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1985430095 363 lGGTEILAPLRAIY---RSPCRDGHPRQLFVFTDGEVGNTKDVITEVQRH 409
Cdd:COG2304   164 -GGTALGAGLELAYelaRKHFIPGRVNRVILLTDGDANVGITDPEELLKL 212
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 282-395 1.01e-07

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: 51.41  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095 282 IFLLDRSGSMrcpidgrdrSPQRIDSAKE---TLVLLLKSLPLGCYFNIYGFGSRFESFYPQSVAYTQQTMAESLQRIQQ 358
Cdd:cd00198     4 VFLLDVSGSM---------GGEKLDKAKEalkALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKK 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1985430095 359 LQAdlGGTEILAPLRAIYR---SPCRDGHPRQLFVFTDGE 395
Cdd:cd00198    75 GLG--GGTNIGAALRLALEllkSAKRPNARRVIILLTDGE 112
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 208-395 1.87e-07

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: 51.86  E-value: 1.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095 208 NWTSAQVSLAEAPPWGRDVELLVYYAEPHKPSAVLELGLPGAEPGSLMGDPAVMVTLLPSLPEAVPGQSPSGEFIFLLDR 287
Cdd:COG1240    22 LLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095 288 SGSMrcpidgrdRSPQRIDSAKETLVLLLKSLPLGCYFNIYGFGSRfesfypqsvAYTQQTMAESLQRIQQLQADL---G 364
Cdd:COG1240   102 SGSM--------AAENRLEAAKGALLDFLDDYRPRDRVGLVAFGGE---------AEVLLPLTRDREALKRALDELppgG 164

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1985430095 365 GTEILAPLRAIYR--SPCRDGHPRQLFVFTDGE 395
Cdd:COG1240   165 GTPLGDALALALEllKRADPARRKVIVLLTDGR 197
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 281-409 2.48e-05

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: 44.37  E-value: 2.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095  281 FIFLLDRSGSMRcpidgrdrsPQRIDSAKETLVL---LLKSLPLGCYFNIYGFGSRFESFYPQSVAYTQQTMAESLQRIQ 357
Cdd:smart00327   2 VVFLLDGSGSMG---------GNRFELAKEFVLKlveQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLS 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985430095  358 qlQADLGGTEILAPLRAIY------RSPCRDGHPRQLFVFTDGEV----GNTKDVITEVQRH 409
Cdd:smart00327  73 --YKLGGGTNLGAALQYALenlfskSAGSRRGAPKVVILITDGESndgpKDLLKAAKELKRS 132
VWA_2 pfam13519
von Willebrand factor type A domain;
281-391 3.75e-05

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 42.28  E-value: 3.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985430095 281 FIFLLDRSGSMRcpidGRDRSPQRIDSAKEtLVLLLKSLPLGCYFNIYGFGSRFESFYPqsVAYTQQTMaesLQRIQQLQ 360
Cdd:pfam13519   1 LVFVLDTSGSMR----NGDYGPTRLEAAKD-AVLALLKSLPGDRVGLVTFGDGPEVLIP--LTKDRAKI---LRALRRLE 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1985430095 361 ADLGGTEILAPLR---AIYRSPCRdGHPRQLFVF 391
Cdd:pfam13519  71 PKGGGTNLAAALQlarAALKHRRK-NQPRRIVLI 103
 
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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