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Conserved domains on  [gi|30520173|ref|NP_848852|]
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BCSC-1 [Mus musculus]

Protein Classification

VWA domain-containing protein( domain architecture ID 10250901)

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- ...
 279-456 6.76e-68

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: 222.09  E-value: 6.76e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173 279 CGEFVFLMDRSRSMNSPMsskdksqlrIDAAKETLILLLKSLPMGCYFNIYGFGATHEEFFPDSVMYNQETMQIAVKKVK 358
Cdd:cd01461   2 PKEVVFVIDTSGSMSGTK---------IEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVN 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173 359 RLLADlGGTELLTPLRKIFRKPPI-PGHPLQVFVFTDGEVVETFSVIREVMFQSK-KHRCFSFGIGEGASTSLIKNLARV 436
Cdd:cd01461  73 RLQAL-GGTNMNDALEAALELLNSsPGSVPQIILLTDGEVTNESQILKNVREALSgRIRLFTFGIGSDVNTYLLERLARE 151

                       170       180
                ....*....|....*....|
gi 30520173 437 SGGTAEFITGNDRMQSKALR 456
Cdd:cd01461 152 GRGIARRIYETDDIESQLLR 171
VIT_2 super family cl02699
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 6-131 6.76e-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.


The actual alignment was detected with superfamily member smart00609:

Pssm-ID: 470654 [Multi-domain]  Cd Length: 130  Bit Score: 143.27  E-value: 6.76e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173      6 GLLTSIRDPVALKSIAVTLSINDFVAGVSATLNYENEEkSPLEAFFVFPMDEDSAVYSFEAF-VDGKKIVAELQDKYQAH 84
Cdd:smart00609   6 GLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRA-VPAQEVTFDVELPKTAFISNFAMtIDGKTYVGEIKEKEVAQ 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 30520173     85 KRYEEALSGGYQAYLLEEDKCSRDVFCCNVgNLQPGSKVSLTLRYVQ 131
Cdd:smart00609  85 KQYEKAVSQGKTAGLVRASGRSMEQFTVSV-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- ...
 279-456 6.76e-68

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: 222.09  E-value: 6.76e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173 279 CGEFVFLMDRSRSMNSPMsskdksqlrIDAAKETLILLLKSLPMGCYFNIYGFGATHEEFFPDSVMYNQETMQIAVKKVK 358
Cdd:cd01461   2 PKEVVFVIDTSGSMSGTK---------IEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVN 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173 359 RLLADlGGTELLTPLRKIFRKPPI-PGHPLQVFVFTDGEVVETFSVIREVMFQSK-KHRCFSFGIGEGASTSLIKNLARV 436
Cdd:cd01461  73 RLQAL-GGTNMNDALEAALELLNSsPGSVPQIILLTDGEVTNESQILKNVREALSgRIRLFTFGIGSDVNTYLLERLARE 151

                       170       180
                ....*....|....*....|
gi 30520173 437 SGGTAEFITGNDRMQSKALR 456
Cdd:cd01461 152 GRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
6-131 6.76e-40

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 143.27  E-value: 6.76e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173      6 GLLTSIRDPVALKSIAVTLSINDFVAGVSATLNYENEEkSPLEAFFVFPMDEDSAVYSFEAF-VDGKKIVAELQDKYQAH 84
Cdd:smart00609   6 GLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRA-VPAQEVTFDVELPKTAFISNFAMtIDGKTYVGEIKEKEVAQ 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 30520173     85 KRYEEALSGGYQAYLLEEDKCSRDVFCCNVgNLQPGSKVSLTLRYVQ 131
Cdd:smart00609  85 KQYEKAVSQGKTAGLVRASGRSMEQFTVSV-NVAPGSKVTFELTYEE 130
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 17-129 1.20e-36

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: 133.38  E-value: 1.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173    17 LKSIAVTLSINDFVAGVSATLNYENEEKSPLEAFFVFPMDEDSAVYSFEAFVDGKKIVAELQDKYQAHKRYEEALSGGYQ 96
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 30520173    97 AYLLEEDkcSRDVFCCNVGNLQPGSKVSLTLRY 129
Cdd:pfam08487  81 AGLLEQD--TPDVFTTSVGNIPPGEKVTVELTY 111
VWA_3 pfam13768
von Willebrand factor type A domain;
280-443 7.14e-27

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 107.10  E-value: 7.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173   280 GEFVFLMDRSRSMNSPmsskdksqlrIDAAKETLILLLKSLPMGCYFNIYGFGATHEEFFPDSVMYNQETMQIAVKKVKR 359
Cdd:pfam13768   1 GDVVIVVDVSSSMSGE----------PKLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKT 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173   360 LLADLGGTELLTPLRKIFRKPPIPGHPLQVFVFTDGEVVETFSVIREVMFQSKKH-RCFSFGIGEGASTSLIKNLARVSG 438
Cdd:pfam13768  71 LQPPLGGSDLLGALKEAVRAPASPGYIRHVLLLTDGSPMQGETRVSDLISRAPGKiRFFAYGLGASISAPMLQLLAEASN 150


                  ....*
gi 30520173   439 GTAEF 443
Cdd:pfam13768 151 GTYEF 155
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 281-444 9.60e-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: 84.38  E-value: 9.60e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173 281 EFVFLMDRSRSMNSPmsskdksqlRIDAAKETLILLLKSLPMGCYFNIYGFGATHEEFFPDSVMYNQETMQiavKKVKRL 360
Cdd:COG2304  93 NLVFVIDVSGSMSGD---------KLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPPTPATDRAKIL---AAIDRL 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173 361 LADlGGTELLTPLR---KIFRKPPIPGHPLQVFVFTDGEV---VETFSVIREvMFQSKKH---RCFSFGIGEGASTSLIK 431
Cdd:COG2304 161 QAG-GGTALGAGLElayELARKHFIPGRVNRVILLTDGDAnvgITDPEELLK-LAEEAREegiTLTTLGVGSDYNEDLLE 238

                       170
                ....*....|...
gi 30520173 432 NLARVSGGTAEFI 444
Cdd:COG2304 239 RLADAGGGNYYYI 251
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 282-443 1.79e-10

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: 60.55  E-value: 1.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173    282 FVFLMDRSRSMnspmsskdkSQLRIDAAKETLILLLKSL---PMGCYFNIYGFGATHEEFFPDSVMYNQETMQIAVKKVK 358
Cdd:smart00327   2 VVFLLDGSGSM---------GGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLS 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173    359 RLLAdlGGTELLTPLRKIF------RKPPIPGHPLQVFVFTDGEV----VETFSVIREVmfQSKKHRCFSFGIGEGASTS 428
Cdd:smart00327  73 YKLG--GGTNLGAALQYALenlfskSAGSRRGAPKVVILITDGESndgpKDLLKAAKEL--KRSGVKVFVVGVGNDVDEE 148

                          170
                   ....*....|....*
gi 30520173    429 LIKNLARVSGGTAEF 443
Cdd:smart00327 149 ELKKLASAPGGVYVF 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- ...
 279-456 6.76e-68

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: 222.09  E-value: 6.76e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173 279 CGEFVFLMDRSRSMNSPMsskdksqlrIDAAKETLILLLKSLPMGCYFNIYGFGATHEEFFPDSVMYNQETMQIAVKKVK 358
Cdd:cd01461   2 PKEVVFVIDTSGSMSGTK---------IEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVN 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173 359 RLLADlGGTELLTPLRKIFRKPPI-PGHPLQVFVFTDGEVVETFSVIREVMFQSK-KHRCFSFGIGEGASTSLIKNLARV 436
Cdd:cd01461  73 RLQAL-GGTNMNDALEAALELLNSsPGSVPQIILLTDGEVTNESQILKNVREALSgRIRLFTFGIGSDVNTYLLERLARE 151

                       170       180
                ....*....|....*....|
gi 30520173 437 SGGTAEFITGNDRMQSKALR 456
Cdd:cd01461 152 GRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
6-131 6.76e-40

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 143.27  E-value: 6.76e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173      6 GLLTSIRDPVALKSIAVTLSINDFVAGVSATLNYENEEkSPLEAFFVFPMDEDSAVYSFEAF-VDGKKIVAELQDKYQAH 84
Cdd:smart00609   6 GLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRA-VPAQEVTFDVELPKTAFISNFAMtIDGKTYVGEIKEKEVAQ 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 30520173     85 KRYEEALSGGYQAYLLEEDKCSRDVFCCNVgNLQPGSKVSLTLRYVQ 131
Cdd:smart00609  85 KQYEKAVSQGKTAGLVRASGRSMEQFTVSV-NVAPGSKVTFELTYEE 130
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 17-129 1.20e-36

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: 133.38  E-value: 1.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173    17 LKSIAVTLSINDFVAGVSATLNYENEEKSPLEAFFVFPMDEDSAVYSFEAFVDGKKIVAELQDKYQAHKRYEEALSGGYQ 96
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 30520173    97 AYLLEEDkcSRDVFCCNVGNLQPGSKVSLTLRY 129
Cdd:pfam08487  81 AGLLEQD--TPDVFTTSVGNIPPGEKVTVELTY 111
VWA_3 pfam13768
von Willebrand factor type A domain;
280-443 7.14e-27

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 107.10  E-value: 7.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173   280 GEFVFLMDRSRSMNSPmsskdksqlrIDAAKETLILLLKSLPMGCYFNIYGFGATHEEFFPDSVMYNQETMQIAVKKVKR 359
Cdd:pfam13768   1 GDVVIVVDVSSSMSGE----------PKLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKT 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173   360 LLADLGGTELLTPLRKIFRKPPIPGHPLQVFVFTDGEVVETFSVIREVMFQSKKH-RCFSFGIGEGASTSLIKNLARVSG 438
Cdd:pfam13768  71 LQPPLGGSDLLGALKEAVRAPASPGYIRHVLLLTDGSPMQGETRVSDLISRAPGKiRFFAYGLGASISAPMLQLLAEASN 150


                  ....*
gi 30520173   439 GTAEF 443
Cdd:pfam13768 151 GTYEF 155
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 281-444 9.60e-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: 84.38  E-value: 9.60e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173 281 EFVFLMDRSRSMNSPmsskdksqlRIDAAKETLILLLKSLPMGCYFNIYGFGATHEEFFPDSVMYNQETMQiavKKVKRL 360
Cdd:COG2304  93 NLVFVIDVSGSMSGD---------KLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPPTPATDRAKIL---AAIDRL 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173 361 LADlGGTELLTPLR---KIFRKPPIPGHPLQVFVFTDGEV---VETFSVIREvMFQSKKH---RCFSFGIGEGASTSLIK 431
Cdd:COG2304 161 QAG-GGTALGAGLElayELARKHFIPGRVNRVILLTDGDAnvgITDPEELLK-LAEEAREegiTLTTLGVGSDYNEDLLE 238

                       170
                ....*....|...
gi 30520173 432 NLARVSGGTAEFI 444
Cdd:COG2304 239 RLADAGGGNYYYI 251
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 280-435 2.74e-15

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 76.64  E-value: 2.74e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173 280 GEFVFLMDRSRSMNSPmsskdksqlRIDAAKETLILLLKSLPMGCYFNIYGFGATHEEFFPdsvMYNQETMQIAVKKVKR 359
Cdd:COG2425 119 GPVVLCVDTSGSMAGS---------KEAAAKAAALALLRALRPNRRFGVILFDTEVVEDLP---LTADDGLEDAIEFLSG 186

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173 360 LLADlGGTELLTPLR---KIFRKPpiPGHPLQVFVFTDGEV-VETFSVIREVMFQSKKHRCFSFGIGEGASTSLIKNLAR 435
Cdd:COG2425 187 LFAG-GGTDIAPALRaalELLEEP--DYRNADIVLITDGEAgVSPEELLREVRAKESGVRLFTVAIGDAGNPGLLEALAD 263
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 283-443 3.94e-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: 67.98  E-value: 3.94e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173 283 VFLMDRSRSMNSPmsskdksqlRIDAAKETLILLLKSLPMGC---YFNIYGFGATHEEFFPDSVMYNQETMQIAVKKVKR 359
Cdd:cd00198   4 VFLLDVSGSMGGE---------KLDKAKEALKALVSSLSASPpgdRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173 360 LLAdlGGTELLTPLR---KIFRKPPIPGHPLQVFVFTDGEV-VETFSVIREV-MFQSKKHRCFSFGIGEGASTSLIKNLA 434
Cdd:cd00198  75 GLG--GGTNIGAALRlalELLKSAKRPNARRVIILLTDGEPnDGPELLAEAArELRKLGITVYTIGIGDDANEDELKEIA 152


                ....*....
gi 30520173 435 RVSGGTAEF 443
Cdd:cd00198 153 DKTTGGAVF 161
VIT_2 pfam13757
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 6-80 2.54e-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: 2.54e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30520173     6 GLL-TSIRDPVALKSIAVTLSINDFVAGVSATLNYENEEKSPLEAFFVFPMDEDSAVYSFEAFVDGKKIVAELQDK 80
Cdd:pfam13757   2 GLLnWSTRTPLPLKASRVSACVNGYSLGVTASLTYYNPQPYPVEGVFVYPLDEGTTVVGFEAEIAGRVISVQLKER 77
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 282-443 1.79e-10

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: 60.55  E-value: 1.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173    282 FVFLMDRSRSMnspmsskdkSQLRIDAAKETLILLLKSL---PMGCYFNIYGFGATHEEFFPDSVMYNQETMQIAVKKVK 358
Cdd:smart00327   2 VVFLLDGSGSM---------GGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLS 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173    359 RLLAdlGGTELLTPLRKIF------RKPPIPGHPLQVFVFTDGEV----VETFSVIREVmfQSKKHRCFSFGIGEGASTS 428
Cdd:smart00327  73 YKLG--GGTNLGAALQYALenlfskSAGSRRGAPKVVILITDGESndgpKDLLKAAKEL--KRSGVKVFVVGVGNDVDEE 148

                          170
                   ....*....|....*
gi 30520173    429 LIKNLARVSGGTAEF 443
Cdd:smart00327 149 ELKKLASAPGGVYVF 163
VWA_2 pfam13519
von Willebrand factor type A domain;
282-392 2.39e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 55.38  E-value: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173   282 FVFLMDRSRSMnspmSSKDKSQLRIDAAKETLILLLKSLPmGCYFNIYGFGATHEEFFPDSVMYNQetmqiAVKKVKRLL 361
Cdd:pfam13519   1 LVFVLDTSGSM----RNGDYGPTRLEAAKDAVLALLKSLP-GDRVGLVTFGDGPEVLIPLTKDRAK-----ILRALRRLE 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 30520173   362 ADLGGTELLTPLR---KIFRKPPiPGHPLQVFVF 392
Cdd:pfam13519  71 PKGGGTNLAAALQlarAALKHRR-KNQPRRIVLI 103
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 282-452 2.18e-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: 49.94  E-value: 2.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173 282 FVFLMDRSRSMNSPMsskdksqlRIDAAKETLILLLKSLPMGCYFNIYGFGATHEEFFPdsvmynqetMQIAVKKVKRLL 361
Cdd:COG1240  95 VVLVVDASGSMAAEN--------RLEAAKGALLDFLDDYRPRDRVGLVAFGGEAEVLLP---------LTRDREALKRAL 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173 362 ADL---GGTELLTPLR---KIFRKPPIPGHPLqVFVFTDGE----VVETFSVIREvmFQSKKHRCFSFGIG-EGASTSLI 430
Cdd:COG1240 158 DELppgGGTPLGDALAlalELLKRADPARRKV-IVLLTDGRdnagRIDPLEAAEL--AAAAGIRIYTIGVGtEAVDEGLL 234

                       170       180
                ....*....|....*....|..
gi 30520173 431 KNLARVSGGTAEFITGNDRMQS 452
Cdd:COG1240 235 REIAEATGGRYFRADDLSELAA 256
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 273-434 5.93e-04

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


Pssm-ID: 238740 [Multi-domain]  Cd Length: 190  Bit Score: 41.61  E-value: 5.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173 273 VETTTKCGEFVFLMDRSRSMnspmsskdkSQLRIDAAKETLILLLKSLPMGCYFNIYGFgatHEEFFPdSVMYNQETMQI 352
Cdd:cd01463   7 IQAATSPKDIVILLDVSGSM---------TGQRLHLAKQTVSSILDTLSDNDFFNIITF---SNEVNP-VVPCFNDTLVQ 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173 353 AVKKVKRLLAD-------LGGTELLTPLRKIF---RKPPIPGHPLQ-------VFVFTDGeVVETFSVIREVMFQSKKH- 414
Cdd:cd01463  74 ATTSNKKVLKEaldmleaKGIANYTKALEFAFsllLKNLQSNHSGSrsqcnqaIMLITDG-VPENYKEIFDKYNWDKNSe 152

                       170       180
                ....*....|....*....|....
gi 30520173 415 ---RCFSFGIG-EGASTSLIKNLA 434
Cdd:cd01463 153 ipvRVFTYLIGrEVTDRREIQWMA 176
VWA pfam00092
von Willebrand factor type A domain;
283-431 4.87e-03

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 38.80  E-value: 4.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173   283 VFLMDRSRSMnspmsskdkSQLRIDAAKETLILLLKSL---PMGCYFNIYGFGATHEEFFPDSVMYNQETMQiavKKVKR 359
Cdd:pfam00092   3 VFLLDGSGSI---------GGDNFEKVKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEFPLNDYSSKEELL---SAVDN 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173   360 LLADLGGTE-----LLTPLRKIFRKP--PIPGHPLQVFVFTDGEVVET--FSVIREVmfQSKKHRCFSFGIGEGASTSLI 430
Cdd:pfam00092  71 LRYLGGGTTntgkaLKYALENLFSSAagARPGAPKVVVLLTDGRSQDGdpEEVAREL--KSAGVTVFAVGVGNADDEELR 148


                  .
gi 30520173   431 K 431
Cdd:pfam00092 149 K 149
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
281-434 6.65e-03

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 38.75  E-value: 6.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173 281 EFVFLMDRSRSMNSpmsskdksqLRIDAAKETLILLLKSL------PMGCYFNIYGFGA---TH------EEFFPDSVMY 345
Cdd:COG4245   7 PVYLLLDTSGSMSG---------EPIEALNEGLQALIDELrqdpyaLETVEVSVITFDGeakVLlpltdlEDFQPPDLSA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520173 346 NQET-MQIAVKKVKRLLADLggTELLTPLRKIFRKPpipghplQVFVFTDGEV--VETFSVIREV--MFQSKKHRCFSFG 420
Cdd:COG4245  78 SGGTpLGAALELLLDLIERR--VQKYTAEGKGDWRP-------VVFLITDGEPtdSDWEAALQRLkdGEAAKKANIFAIG 148

                       170
                ....*....|....
gi 30520173 421 IGEGASTSLIKNLA 434
Cdd:COG4245 149 VGPDADTEVLKQLT 162
 
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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