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Conserved domains on  [gi|38195082|ref|NP_938057|]
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von Willebrand factor A domain-containing protein 5A isoform 2 [Homo sapiens]

Protein Classification

VWA domain-containing protein( domain architecture ID 10652061)

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
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
1-131 2.48e-52

Vault protein Inter-alpha-Trypsin domain;


:

Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 171.39  E-value: 2.48e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38195082      1 MVHFCGLLTLHREPVPLKSISVSVNIYEFVAGVSATLNYENEEkVPLEAFFVFPMDEDSAVYSFEAL-VDGKKIVAELQD 79
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRA-VPAQEVTFDVELPKTAFISNFAMtIDGKTYVGEIKE 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 38195082     80 KMKARTNYEKAISQGHQAFLLEGDSSSRDVFSCNVgNLQPGSKAAVTLKYVQ 131
Cdd:smart00609  80 KEVAQKQYEKAVSQGKTAGLVRASGRSMEQFTVSV-NVAPGSKVTFELTYEE 130
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 278-408 5.28e-44

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: 150.83  E-value: 5.28e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38195082 278 TCGEFIFLMDRSGSMQSPMssqdtsqlrIQAAKETLILLLKSLPIGCYFNIYGFGSSYEACFPESVKYTQQTMEEALGRV 357
Cdd:cd01461   1 LPKEVVFVIDTSGSMSGTK---------IEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYV 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 38195082 358 KLMQADlGGTEILAPLQNIYRGPSI-PGHPLQLFVFTDGEVTDTFSVIKEVR 408
Cdd:cd01461  72 NRLQAL-GGTNMNDALEAALELLNSsPGSVPQIILLTDGEVTNESQILKNVR 122
 
Name Accession Description Interval E-value
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
1-131 2.48e-52

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 171.39  E-value: 2.48e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38195082      1 MVHFCGLLTLHREPVPLKSISVSVNIYEFVAGVSATLNYENEEkVPLEAFFVFPMDEDSAVYSFEAL-VDGKKIVAELQD 79
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRA-VPAQEVTFDVELPKTAFISNFAMtIDGKTYVGEIKE 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 38195082     80 KMKARTNYEKAISQGHQAFLLEGDSSSRDVFSCNVgNLQPGSKAAVTLKYVQ 131
Cdd:smart00609  80 KEVAQKQYEKAVSQGKTAGLVRASGRSMEQFTVSV-NVAPGSKVTFELTYEE 130
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 278-408 5.28e-44

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: 150.83  E-value: 5.28e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38195082 278 TCGEFIFLMDRSGSMQSPMssqdtsqlrIQAAKETLILLLKSLPIGCYFNIYGFGSSYEACFPESVKYTQQTMEEALGRV 357
Cdd:cd01461   1 LPKEVVFVIDTSGSMSGTK---------IEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYV 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 38195082 358 KLMQADlGGTEILAPLQNIYRGPSI-PGHPLQLFVFTDGEVTDTFSVIKEVR 408
Cdd:cd01461  72 NRLQAL-GGTNMNDALEAALELLNSsPGSVPQIILLTDGEVTNESQILKNVR 122
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 17-129 1.16e-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: 137.62  E-value: 1.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38195082    17 LKSISVSVNIYEFVAGVSATLNYENEEKVPLEAFFVFPMDEDSAVYSFEALVDGKKIVAELQDKMKARTNYEKAISQGHQ 96
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 38195082    97 AFLLEgdSSSRDVFSCNVGNLQPGSKAAVTLKY 129
Cdd:pfam08487  81 AGLLE--QDTPDVFTTSVGNIPPGEKVTVELTY 111
VWA_3 pfam13768
von Willebrand factor type A domain;
280-408 1.31e-12

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 65.11  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38195082   280 GEFIFLMDRSGSMQSPmssqdtsqlrIQAAKETLILLLKSLPIGCYFNIYGFGSSYEACFPESVKYTQQTMEEALGRVKL 359
Cdd:pfam13768   1 GDVVIVVDVSSSMSGE----------PKLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKT 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 38195082   360 MQADLGGTEILAPLQNIYRGPSIPGHPLQLFVFTDGEVTD-TFSVIKEVR 408
Cdd:pfam13768  71 LQPPLGGSDLLGALKEAVRAPASPGYIRHVLLLTDGSPMQgETRVSDLIS 120
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 280-415 3.65e-11

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 63.16  E-value: 3.65e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38195082 280 GEFIFLMDRSGSMQSPmssqdtsqlRIQAAKETLILLLKSLPIGCYFNIYGFGSSYEACFPESVKYTQQTMEEALGRVKL 359
Cdd:COG2425 119 GPVVLCVDTSGSMAGS---------KEAAAKAAALALLRALRPNRRFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLFA 189

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38195082 360 MqadlGGTEILAPL---QNIYRGPsiPGHPLQLFVFTDGEVT-DTFSVIKEVRINRQKHR 415
Cdd:COG2425 190 G----GGTDIAPALraaLELLEEP--DYRNADIVLITDGEAGvSPEELLREVRAKESGVR 243
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 282-415 2.94e-07

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: 50.15  E-value: 2.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38195082    282 FIFLMDRSGSMqspmssqdtSQLRIQAAKETLILLLKSLPIGC---YFNIYGFGSSYEACFPESVKYTQQTMEEALGRVK 358
Cdd:smart00327   2 VVFLLDGSGSM---------GGNRFELAKEFVLKLVEQLDIGPdgdRVGLVTFSDDARVLFPLNDSRSKDALLEALASLS 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38195082    359 lmQADLGGTEILAPLQNIY------RGPSIPGHPLQLFVFTDGEVTDTFSVIKEVrINRQKHR 415
Cdd:smart00327  73 --YKLGGGTNLGAALQYALenlfskSAGSRRGAPKVVILITDGESNDGPKDLLKA-AKELKRS 132
 
Name Accession Description Interval E-value
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
1-131 2.48e-52

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 171.39  E-value: 2.48e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38195082      1 MVHFCGLLTLHREPVPLKSISVSVNIYEFVAGVSATLNYENEEkVPLEAFFVFPMDEDSAVYSFEAL-VDGKKIVAELQD 79
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRA-VPAQEVTFDVELPKTAFISNFAMtIDGKTYVGEIKE 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 38195082     80 KMKARTNYEKAISQGHQAFLLEGDSSSRDVFSCNVgNLQPGSKAAVTLKYVQ 131
Cdd:smart00609  80 KEVAQKQYEKAVSQGKTAGLVRASGRSMEQFTVSV-NVAPGSKVTFELTYEE 130
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 278-408 5.28e-44

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: 150.83  E-value: 5.28e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38195082 278 TCGEFIFLMDRSGSMQSPMssqdtsqlrIQAAKETLILLLKSLPIGCYFNIYGFGSSYEACFPESVKYTQQTMEEALGRV 357
Cdd:cd01461   1 LPKEVVFVIDTSGSMSGTK---------IEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYV 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 38195082 358 KLMQADlGGTEILAPLQNIYRGPSI-PGHPLQLFVFTDGEVTDTFSVIKEVR 408
Cdd:cd01461  72 NRLQAL-GGTNMNDALEAALELLNSsPGSVPQIILLTDGEVTNESQILKNVR 122
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 17-129 1.16e-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: 137.62  E-value: 1.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38195082    17 LKSISVSVNIYEFVAGVSATLNYENEEKVPLEAFFVFPMDEDSAVYSFEALVDGKKIVAELQDKMKARTNYEKAISQGHQ 96
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 38195082    97 AFLLEgdSSSRDVFSCNVGNLQPGSKAAVTLKY 129
Cdd:pfam08487  81 AGLLE--QDTPDVFTTSVGNIPPGEKVTVELTY 111
VIT_2 pfam13757
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 6-80 3.26e-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: 3.26e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38195082     6 GLLTLH-REPVPLKSISVSVNIYEFVAGVSATLNYENEEKVPLEAFFVFPMDEDSAVYSFEALVDGKKIVAELQDK 80
Cdd:pfam13757   2 GLLNWStRTPLPLKASRVSACVNGYSLGVTASLTYYNPQPYPVEGVFVYPLDEGTTVVGFEAEIAGRVISVQLKER 77
VWA_3 pfam13768
von Willebrand factor type A domain;
280-408 1.31e-12

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 65.11  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38195082   280 GEFIFLMDRSGSMQSPmssqdtsqlrIQAAKETLILLLKSLPIGCYFNIYGFGSSYEACFPESVKYTQQTMEEALGRVKL 359
Cdd:pfam13768   1 GDVVIVVDVSSSMSGE----------PKLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKT 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 38195082   360 MQADLGGTEILAPLQNIYRGPSIPGHPLQLFVFTDGEVTD-TFSVIKEVR 408
Cdd:pfam13768  71 LQPPLGGSDLLGALKEAVRAPASPGYIRHVLLLTDGSPMQgETRVSDLIS 120
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 280-415 3.65e-11

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 63.16  E-value: 3.65e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38195082 280 GEFIFLMDRSGSMQSPmssqdtsqlRIQAAKETLILLLKSLPIGCYFNIYGFGSSYEACFPESVKYTQQTMEEALGRVKL 359
Cdd:COG2425 119 GPVVLCVDTSGSMAGS---------KEAAAKAAALALLRALRPNRRFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLFA 189

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38195082 360 MqadlGGTEILAPL---QNIYRGPsiPGHPLQLFVFTDGEVT-DTFSVIKEVRINRQKHR 415
Cdd:COG2425 190 G----GGTDIAPALraaLELLEEP--DYRNADIVLITDGEAGvSPEELLREVRAKESGVR 243
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 225-408 7.26e-11

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 62.43  E-value: 7.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38195082 225 DRDVELLIYYNEVHTPSVVLEMGMPNMKPGHLMgdpsAMVSFYPNIPEDQ---PSNtcgeFIFLMDRSGSMQSPmssqdt 301
Cdd:COG2304  42 AVRLEELVNFFPYDYPLPTGRLAQSPWNPQTRL----LLVGLQPPKAAAEerpPLN----LVFVIDVSGSMSGD------ 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38195082 302 sqlRIQAAKETLILLLKSLPIGCYFNIYGFGSSYEACFPeSVKYTQqtMEEALGRVKLMQADlGGTEILAPLQNIY---R 378
Cdd:COG2304 108 ---KLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLP-PTPATD--RAKILAAIDRLQAG-GGTALGAGLELAYelaR 180

                       170       180       190
                ....*....|....*....|....*....|
gi 38195082 379 GPSIPGHPLQLFVFTDGEVTDTFSVIKEVR 408
Cdd:COG2304 181 KHFIPGRVNRVILLTDGDANVGITDPEELL 210
VWA_2 pfam13519
von Willebrand factor type A domain;
282-374 3.01e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 54.22  E-value: 3.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38195082   282 FIFLMDRSGSMqspmSSQDTSQLRIQAAKETLILLLKSLPiGCYFNIYGFGSSYEACFPesVKYTQQTMEEALGRVklmQ 361
Cdd:pfam13519   1 LVFVLDTSGSM----RNGDYGPTRLEAAKDAVLALLKSLP-GDRVGLVTFGDGPEVLIP--LTKDRAKILRALRRL---E 70

                          90
                  ....*....|...
gi 38195082   362 ADLGGTEILAPLQ 374
Cdd:pfam13519  71 PKGGGTNLAAALQ 83
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 283-399 5.37e-09

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: 54.88  E-value: 5.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38195082 283 IFLMDRSGSMQSPmssqdtsqlRIQAAKETLILLLKSLPIGC---YFNIYGFGSSYEACFPESVKYTQQTMEEALGRVKL 359
Cdd:cd00198   4 VFLLDVSGSMGGE---------KLDKAKEALKALVSSLSASPpgdRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKK 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 38195082 360 MQAdlGGTEILAPLQ---NIYRGPSIPGHPLQLFVFTDGEVTD 399
Cdd:cd00198  75 GLG--GGTNIGAALRlalELLKSAKRPNARRVIILLTDGEPND 115
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 282-415 2.94e-07

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: 50.15  E-value: 2.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38195082    282 FIFLMDRSGSMqspmssqdtSQLRIQAAKETLILLLKSLPIGC---YFNIYGFGSSYEACFPESVKYTQQTMEEALGRVK 358
Cdd:smart00327   2 VVFLLDGSGSM---------GGNRFELAKEFVLKLVEQLDIGPdgdRVGLVTFSDDARVLFPLNDSRSKDALLEALASLS 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38195082    359 lmQADLGGTEILAPLQNIY------RGPSIPGHPLQLFVFTDGEVTDTFSVIKEVrINRQKHR 415
Cdd:smart00327  73 --YKLGGGTNLGAALQYALenlfskSAGSRRGAPKVVILITDGESNDGPKDLLKA-AKELKRS 132
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 282-399 1.15e-04

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: 43.39  E-value: 1.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38195082 282 FIFLMDRSGSMQSPMssqdtsqlRIQAAKETLILLLKSLPIGCYFNIYGFGSSYEACFPesvkYTQQTmEEALGRVKLMQ 361
Cdd:COG1240  95 VVLVVDASGSMAAEN--------RLEAAKGALLDFLDDYRPRDRVGLVAFGGEAEVLLP----LTRDR-EALKRALDELP 161

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 38195082 362 ADlGGTEILAPLQNIYR--GPSIPGHPLQLFVFTDGEVTD 399
Cdd:COG1240 162 PG-GGTPLGDALALALEllKRADPARRKVIVLLTDGRDNA 200
VWA pfam00092
von Willebrand factor type A domain;
283-400 1.40e-04

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 42.26  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38195082   283 IFLMDRSGSMqspmssqdtSQLRIQAAKETLILLLKSLPIGC---YFNIYGFGSSYEacfpESVKYTQ-QTMEEALGRVK 358
Cdd:pfam00092   3 VFLLDGSGSI---------GGDNFEKVKEFLKKLVESLDIGPdgtRVGLVQYSSDVR----TEFPLNDySSKEELLSAVD 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 38195082   359 LMQADLGGTE-----ILAPLQNIYRGP--SIPGHPLQLFVFTDGEVTDT 400
Cdd:pfam00092  70 NLRYLGGGTTntgkaLKYALENLFSSAagARPGAPKVVVLLTDGRSQDG 118
 
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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