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Conserved domains on  [gi|2017363581|ref|NP_001380877|]
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von Willebrand factor A domain-containing protein 5A [Rattus norvegicus]

Protein Classification

vWA domain-containing protein; VIT and vWA domain-containing protein( domain architecture ID 10250901)

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| 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
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 278-456 2.12e-62

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: 207.07  E-value: 2.12e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 278 VCGEFVFLMDRSGSMQTPMrteensqlrIEAAKETLLLLLKSLPMGCYFNIYGFGSSYEQFFPESVKYTQETIEEAVERV 357
Cdd:cd01461     1 LPKEVVFVIDTSGSMSGTK---------IEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 358 KRLDADlGGTEILTPLRNIYKTSSI-PGHPLQLFVFTDGEVSDTYSVIREVKLNSK-KHRCFSFGIGQGASTSLIKNIAR 435
Cdd:cd01461    72 NRLQAL-GGTNMNDALEAALELLNSsPGSVPQIILLTDGEVTNESQILKNVREALSgRIRLFTFGIGSDVNTYLLERLAR 150

                         170       180
                  ....*....|....*....|.
gi 2017363581 436 VSGGTAEFITGKDRMQAKALG 456
Cdd:cd01461   151 EGRGIARRIYETDDIESQLLR 171
VIT_2 super family cl02699
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 1-131 1.42e-46

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.


The actual alignment was detected with superfamily member smart00609:

Pssm-ID: 470654 [Multi-domain]  Cd Length: 130  Bit Score: 162.14  E-value: 1.42e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581    1 MEHHWGLITGNKEKVPLKSISVTLSINDFVAAVAATLHYENEEkVPIEAMFVFPMDEDSAVYSFEAL-VDGKKIVAELQD 79
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRA-VPAQEVTFDVELPKTAFISNFAMtIDGKTYVGEIKE 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2017363581   80 KTKAHSKYEEALSQGHQAYLLEEDDYSRDVFSCNVgNLQPGTKVAVTLRYVQ 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 2.12e-62

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: 207.07  E-value: 2.12e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 278 VCGEFVFLMDRSGSMQTPMrteensqlrIEAAKETLLLLLKSLPMGCYFNIYGFGSSYEQFFPESVKYTQETIEEAVERV 357
Cdd:cd01461     1 LPKEVVFVIDTSGSMSGTK---------IEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 358 KRLDADlGGTEILTPLRNIYKTSSI-PGHPLQLFVFTDGEVSDTYSVIREVKLNSK-KHRCFSFGIGQGASTSLIKNIAR 435
Cdd:cd01461    72 NRLQAL-GGTNMNDALEAALELLNSsPGSVPQIILLTDGEVTNESQILKNVREALSgRIRLFTFGIGSDVNTYLLERLAR 150

                         170       180
                  ....*....|....*....|.
gi 2017363581 436 VSGGTAEFITGKDRMQAKALG 456
Cdd:cd01461   151 EGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
1-131 1.42e-46

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 162.14  E-value: 1.42e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581    1 MEHHWGLITGNKEKVPLKSISVTLSINDFVAAVAATLHYENEEkVPIEAMFVFPMDEDSAVYSFEAL-VDGKKIVAELQD 79
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRA-VPAQEVTFDVELPKTAFISNFAMtIDGKTYVGEIKE 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2017363581   80 KTKAHSKYEEALSQGHQAYLLEEDDYSRDVFSCNVgNLQPGTKVAVTLRYVQ 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 8.38e-40

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: 142.24  E-value: 8.38e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581  17 LKSISVTLSINDFVAAVAATLHYENEEKVPIEAMFVFPMDEDSAVYSFEALVDGKKIVAELQDKTKAHSKYEEALSQGHQ 96
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2017363581  97 AYLLEEDDysRDVFSCNVGNLQPGTKVAVTLRY 129
Cdd:pfam08487  81 AGLLEQDT--PDVFTTSVGNIPPGEKVTVELTY 111
VWA_3 pfam13768
von Willebrand factor type A domain;
280-443 8.48e-19

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 83.98  E-value: 8.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 280 GEFVFLMDRSGSMQTPmrteensqlrIEAAKETLLLLLKSLPMGCYFNIYGFGSSYEQFFPESVKYTQETIEEAVERVKR 359
Cdd:pfam13768   1 GDVVIVVDVSSSMSGE----------PKLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKT 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 360 LDADLGGTEILTPLRNIYKTSSIPGHPLQLFVFTDGEV-SDTYSVIREVKLNSKKHRCFSFGIGQGASTSLIKNIARVSG 438
Cdd:pfam13768  71 LQPPLGGSDLLGALKEAVRAPASPGYIRHVLLLTDGSPmQGETRVSDLISRAPGKIRFFAYGLGASISAPMLQLLAEASN 150


                  ....*
gi 2017363581 439 GTAEF 443
Cdd:pfam13768 151 GTYEF 155
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 281-444 1.27e-16

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 81.30  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 281 EFVFLMDRSGSMQTPmrteensqlRIEAAKETLLLLLKSLPMGCYFNIYGFGSSYEQFFPeSVKYTQetIEEAVERVKRL 360
Cdd:COG2304    93 NLVFVIDVSGSMSGD---------KLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLP-PTPATD--RAKILAAIDRL 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 361 DADlGGTEILTPLRNIY---KTSSIPGHPLQLFVFTDGE----VSDTYSVIREVKLNSKKH-RCFSFGIGQGASTSLIKN 432
Cdd:COG2304   161 QAG-GGTALGAGLELAYelaRKHFIPGRVNRVILLTDGDanvgITDPEELLKLAEEAREEGiTLTTLGVGSDYNEDLLER 239

                         170
                  ....*....|..
gi 2017363581 433 IARVSGGTAEFI 444
Cdd:COG2304   240 LADAGGGNYYYI 251
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 282-443 1.05e-11

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: 64.01  E-value: 1.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581  282 FVFLMDRSGSMqtpmrteenSQLRIEAAKETLLLLLKSL---PMGCYFNIYGFGSSYEQFFPESVKYTQETIEEAVERVK 358
Cdd:smart00327   2 VVFLLDGSGSM---------GGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLS 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581  359 RLDAdlGGTEILTPLRNIYKTSSI------PGHPLQLFVFTDGEVSDTYSVIREV--KLNSKKHRCFSFGIGQGASTSLI 430
Cdd:smart00327  73 YKLG--GGTNLGAALQYALENLFSksagsrRGAPKVVILITDGESNDGPKDLLKAakELKRSGVKVFVVGVGNDVDEEEL 150

                          170
                   ....*....|...
gi 2017363581  431 KNIARVSGGTAEF 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 2.12e-62

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: 207.07  E-value: 2.12e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 278 VCGEFVFLMDRSGSMQTPMrteensqlrIEAAKETLLLLLKSLPMGCYFNIYGFGSSYEQFFPESVKYTQETIEEAVERV 357
Cdd:cd01461     1 LPKEVVFVIDTSGSMSGTK---------IEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 358 KRLDADlGGTEILTPLRNIYKTSSI-PGHPLQLFVFTDGEVSDTYSVIREVKLNSK-KHRCFSFGIGQGASTSLIKNIAR 435
Cdd:cd01461    72 NRLQAL-GGTNMNDALEAALELLNSsPGSVPQIILLTDGEVTNESQILKNVREALSgRIRLFTFGIGSDVNTYLLERLAR 150

                         170       180
                  ....*....|....*....|.
gi 2017363581 436 VSGGTAEFITGKDRMQAKALG 456
Cdd:cd01461   151 EGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
1-131 1.42e-46

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 162.14  E-value: 1.42e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581    1 MEHHWGLITGNKEKVPLKSISVTLSINDFVAAVAATLHYENEEkVPIEAMFVFPMDEDSAVYSFEAL-VDGKKIVAELQD 79
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRA-VPAQEVTFDVELPKTAFISNFAMtIDGKTYVGEIKE 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2017363581   80 KTKAHSKYEEALSQGHQAYLLEEDDYSRDVFSCNVgNLQPGTKVAVTLRYVQ 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 8.38e-40

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: 142.24  E-value: 8.38e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581  17 LKSISVTLSINDFVAAVAATLHYENEEKVPIEAMFVFPMDEDSAVYSFEALVDGKKIVAELQDKTKAHSKYEEALSQGHQ 96
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2017363581  97 AYLLEEDDysRDVFSCNVGNLQPGTKVAVTLRY 129
Cdd:pfam08487  81 AGLLEQDT--PDVFTTSVGNIPPGEKVTVELTY 111
VWA_3 pfam13768
von Willebrand factor type A domain;
280-443 8.48e-19

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 83.98  E-value: 8.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 280 GEFVFLMDRSGSMQTPmrteensqlrIEAAKETLLLLLKSLPMGCYFNIYGFGSSYEQFFPESVKYTQETIEEAVERVKR 359
Cdd:pfam13768   1 GDVVIVVDVSSSMSGE----------PKLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKT 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 360 LDADLGGTEILTPLRNIYKTSSIPGHPLQLFVFTDGEV-SDTYSVIREVKLNSKKHRCFSFGIGQGASTSLIKNIARVSG 438
Cdd:pfam13768  71 LQPPLGGSDLLGALKEAVRAPASPGYIRHVLLLTDGSPmQGETRVSDLISRAPGKIRFFAYGLGASISAPMLQLLAEASN 150


                  ....*
gi 2017363581 439 GTAEF 443
Cdd:pfam13768 151 GTYEF 155
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 281-444 1.27e-16

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 81.30  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 281 EFVFLMDRSGSMQTPmrteensqlRIEAAKETLLLLLKSLPMGCYFNIYGFGSSYEQFFPeSVKYTQetIEEAVERVKRL 360
Cdd:COG2304    93 NLVFVIDVSGSMSGD---------KLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLP-PTPATD--RAKILAAIDRL 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 361 DADlGGTEILTPLRNIY---KTSSIPGHPLQLFVFTDGE----VSDTYSVIREVKLNSKKH-RCFSFGIGQGASTSLIKN 432
Cdd:COG2304   161 QAG-GGTALGAGLELAYelaRKHFIPGRVNRVILLTDGDanvgITDPEELLKLAEEAREEGiTLTTLGVGSDYNEDLLER 239

                         170
                  ....*....|..
gi 2017363581 433 IARVSGGTAEFI 444
Cdd:COG2304   240 LADAGGGNYYYI 251
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 262-435 2.79e-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: 79.72  E-value: 2.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 262 AMVSFYPDIPEVNASKVCGEFVFLMDRSGSMQTPmrteensqlRIEAAKETLLLLLKSLPMGCYFNIYGFGSSYEQFFPE 341
Cdd:COG2425   101 AALLLLAAPASAAVPLLEGPVVLCVDTSGSMAGS---------KEAAAKAAALALLRALRPNRRFGVILFDTEVVEDLPL 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 342 SVKytqETIEEAVERVKRLDADlGGTEILTPLRNIYKT-SSIPGHPLQLFVFTDGEV-SDTYSVIREVKLNSKKHRCFSF 419
Cdd:COG2425   172 TAD---DGLEDAIEFLSGLFAG-GGTDIAPALRAALELlEEPDYRNADIVLITDGEAgVSPEELLREVRAKESGVRLFTV 247

                         170
                  ....*....|....*.
gi 2017363581 420 GIGQGASTSLIKNIAR 435
Cdd:COG2425   248 AIGDAGNPGLLEALAD 263
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 283-443 1.33e-13

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: 69.13  E-value: 1.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 283 VFLMDRSGSMqtpmrTEENSQLRIEAAKETLLLLLKSLPmGCYFNIYGFGSSYEQFFPESVKYTQETIEEAVERVKRLDA 362
Cdd:cd00198     4 VFLLDVSGSM-----GGEKLDKAKEALKALVSSLSASPP-GDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 363 dlGGTEILTPLR---NIYKTSSIPGHPLQLFVFTDGEVSDTYSVIREV--KLNSKKHRCFSFGIGQGASTSLIKNIARVS 437
Cdd:cd00198    78 --GGTNIGAALRlalELLKSAKRPNARRVIILLTDGEPNDGPELLAEAarELRKLGITVYTIGIGDDANEDELKEIADKT 155


                  ....*.
gi 2017363581 438 GGTAEF 443
Cdd:cd00198   156 TGGAVF 161
VIT_2 pfam13757
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 5-81 2.19e-13

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: 65.95  E-value: 2.19e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017363581   5 WGLI-TGNKEKVPLKSISVTLSINDFVAAVAATLHYENEEKVPIEAMFVFPMDEDSAVYSFEALVDGKKIVAELQDKT 81
Cdd:pfam13757   1 PGLLnWSTRTPLPLKASRVSACVNGYSLGVTASLTYYNPQPYPVEGVFVYPLDEGTTVVGFEAEIAGRVISVQLKERE 78
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 282-443 1.05e-11

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: 64.01  E-value: 1.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581  282 FVFLMDRSGSMqtpmrteenSQLRIEAAKETLLLLLKSL---PMGCYFNIYGFGSSYEQFFPESVKYTQETIEEAVERVK 358
Cdd:smart00327   2 VVFLLDGSGSM---------GGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLS 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581  359 RLDAdlGGTEILTPLRNIYKTSSI------PGHPLQLFVFTDGEVSDTYSVIREV--KLNSKKHRCFSFGIGQGASTSLI 430
Cdd:smart00327  73 YKLG--GGTNLGAALQYALENLFSksagsrRGAPKVVILITDGESNDGPKDLLKAakELKRSGVKVFVVGVGNDVDEEEL 150

                          170
                   ....*....|...
gi 2017363581  431 KNIARVSGGTAEF 443
Cdd:smart00327 151 KKLASAPGGVYVF 163
VWA_2 pfam13519
von Willebrand factor type A domain;
282-374 2.61e-07

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 49.60  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 282 FVFLMDRSGSMqtpmRTEENSQLRIEAAKETLLLLLKSLPmGCYFNIYGFGSSYEQFFPesVKYTQETIEEAVErvkRLD 361
Cdd:pfam13519   1 LVFVLDTSGSM----RNGDYGPTRLEAAKDAVLALLKSLP-GDRVGLVTFGDGPEVLIP--LTKDRAKILRALR---RLE 70

                          90
                  ....*....|...
gi 2017363581 362 ADLGGTEILTPLR 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 1.83e-06

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: 50.32  E-value: 1.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 282 FVFLMDRSGSMQtpmrtEENsqlRIEAAKETLLLLLKSLPMGCYFNIYGFGSSYEQFFPesvkYTQEtIEEAVERVKRLD 361
Cdd:COG1240    95 VVLVVDASGSMA-----AEN---RLEAAKGALLDFLDDYRPRDRVGLVAFGGEAEVLLP----LTRD-REALKRALDELP 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 362 ADlGGTEILTPLRNIYKT--SSIPGHPLQLFVFTDGEVSDTYSVIREV--KLNSKKHRCFSFGIG-QGASTSLIKNIARV 436
Cdd:COG1240   162 PG-GGTPLGDALALALELlkRADPARRKVIVLLTDGRDNAGRIDPLEAaeLAAAAGIRIYTIGVGtEAVDEGLLREIAEA 240


                  ....*....
gi 2017363581 437 SGGTAEFIT 445
Cdd:COG1240   241 TGGRYFRAD 249
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
274-434 1.59e-05

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 46.46  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 274 NASKVCgEFVFLMDRSGSMQTpmrteensqLRIEAAKETLLLLLKSL------PMGCYFNIYGFGSSYEQFFPesvkYTq 347
Cdd:COG4245     1 NPMRRL-PVYLLLDTSGSMSG---------EPIEALNEGLQALIDELrqdpyaLETVEVSVITFDGEAKVLLP----LT- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 348 eTIEEAVerVKRLDADlGGT----------EILTPLRNIYKTSSIPGHPLQLFVFTDGEVSDTY--SVIREVKLNSKKHR 415
Cdd:COG4245    66 -DLEDFQ--PPDLSAS-GGTplgaalelllDLIERRVQKYTAEGKGDWRPVVFLITDGEPTDSDweAALQRLKDGEAAKK 141

                         170       180
                  ....*....|....*....|.
gi 2017363581 416 C--FSFGIGQGASTSLIKNIA 434
Cdd:COG4245   142 AniFAIGVGPDADTEVLKQLT 162
VWA pfam00092
von Willebrand factor type A domain;
283-434 1.86e-05

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 45.73  E-value: 1.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 283 VFLMDRSGSMqtpmrTEENSQLRIEAAKETLLLLLKSlPMGCYFNIYGFGSSYEQFFPesvkYTQ-ETIEEAVERVKRLD 361
Cdd:pfam00092   3 VFLLDGSGSI-----GGDNFEKVKEFLKKLVESLDIG-PDGTRVGLVQYSSDVRTEFP----LNDySSKEELLSAVDNLR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 362 ADLGGTE-----ILTPLRNIYKTS--SIPGHPLQLFVFTDGEVSDTY--SVIREVKlnSKKHRCFSFGIGQGASTSLiKN 432
Cdd:pfam00092  73 YLGGGTTntgkaLKYALENLFSSAagARPGAPKVVVLLTDGRSQDGDpeEVARELK--SAGVTVFAVGVGNADDEEL-RK 149


                  ..
gi 2017363581 433 IA 434
Cdd:pfam00092 150 IA 151
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 282-445 3.69e-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: 41.87  E-value: 3.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 282 FVFLMDRSGSMQTPmrteensqlRIEAAKETLLLLLKSLPMGCYFNIYGFGSSYEQFFPESVKYTQETIEEAVErvkRLD 361
Cdd:cd01465     3 LVFVIDRSGSMDGP---------KLPLVKSALKLLVDQLRPDDRLAIVTYDGAAETVLPATPVRDKAAILAAID---RLT 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017363581 362 ADlGGTEILTPLRNIYKT---SSIPGHPLQLFVFTDGEVSDTYSVIREVKLNSKKHR-----CFSFGIGQGASTSLIKNI 433
Cdd:cd01465    71 AG-GSTAGGAGIQLGYQEaqkHFVPGGVNRILLATDGDFNVGETDPDELARLVAQKResgitLSTLGFGDNYNEDLMEAI 149

                         170
                  ....*....|..
gi 2017363581 434 ARVSGGTAEFIT 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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