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Conserved domains on  [gi|2462503609|ref|XP_054190361|]
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von Willebrand factor A domain-containing protein 5B1 isoform X3 [Homo sapiens]

Protein Classification

vWA domain-containing protein; VIT and vWA domain-containing protein( domain architecture ID 10618621)

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, hemostasis, 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
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 313-468 1.98e-51

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: 178.56  E-value: 1.98e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503609  313 MKKKSRAERKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTYSEDSLAMACDDIQRMKADmGGTNILSPLKWVIRQP 392
Cdd:cd01461     15 MSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQAL-GGTNMNDALEAALELL 93

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462503609  393 VH-RGHPRLLFVITDGAVNNTGKVLELVRNHA-FSTRCYSFGIGPNVCHRLVKGLASVSEGSAELLMEGERLQPKMVK 468
Cdd:cd01461     94 NSsPGSVPQIILLTDGEVTNESQILKNVREALsGRIRLFTFGIGSDVNTYLLERLAREGRGIARRIYETDDIESQLLR 171
VIT_2 pfam13757
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 2-79 2.82e-37

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: 134.51  E-value: 2.82e-37
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462503609    2 PGLLNWITGAALPLTASDVTSCVSGYALGLTASLTYGNLEAQPFQGLFVYPLDECTTVIGFEAVIADRVVTVQIKDKA 79
Cdd:pfam13757    1 PGLLNWSTRTPLPLKASRVSACVNGYSLGVTASLTYYNPQPYPVEGVFVYPLDEGTTVVGFEAEIAGRVISVQLKERE 78
VIT super family cl48021
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 15-146 1.07e-04

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 pfam08487:

Pssm-ID: 462492 [Multi-domain]  Cd Length: 111  Bit Score: 42.86  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503609   15 LTASDVTSCVSGYALGLTASLTYGNLEAQPFQGLFVYPLDECTTVIGFEAVIADRVVTVQIKDKAK--------LESGHf 86
Cdd:pfam08487    1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEakkeyeeaVARGK- 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503609   87 DASHVRspTVTGNIlqdgvsiaphsctpgkvtldedlerilFVANLGTIAPMENVTIFIS 146
Cdd:pfam08487   80 TAGLLE--QDTPDV---------------------------FTTSVGNIPPGEKVTVELT 110
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 313-468 1.98e-51

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: 178.56  E-value: 1.98e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503609  313 MKKKSRAERKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTYSEDSLAMACDDIQRMKADmGGTNILSPLKWVIRQP 392
Cdd:cd01461     15 MSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQAL-GGTNMNDALEAALELL 93

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462503609  393 VH-RGHPRLLFVITDGAVNNTGKVLELVRNHA-FSTRCYSFGIGPNVCHRLVKGLASVSEGSAELLMEGERLQPKMVK 468
Cdd:cd01461     94 NSsPGSVPQIILLTDGEVTNESQILKNVREALsGRIRLFTFGIGSDVNTYLLERLAREGRGIARRIYETDDIESQLLR 171
VIT_2 pfam13757
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 2-79 2.82e-37

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: 134.51  E-value: 2.82e-37
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462503609    2 PGLLNWITGAALPLTASDVTSCVSGYALGLTASLTYGNLEAQPFQGLFVYPLDECTTVIGFEAVIADRVVTVQIKDKA 79
Cdd:pfam13757    1 PGLLNWSTRTPLPLKASRVSACVNGYSLGVTASLTYYNPQPYPVEGVFVYPLDEGTTVVGFEAEIAGRVISVQLKERE 78
VWA_3 pfam13768
von Willebrand factor type A domain;
322-454 4.18e-27

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 108.25  E-value: 4.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503609  322 KDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTYSEDSLAMACDDIQRMKADMGGTNILSPLKWVIRQPVHRGHPRLL 401
Cdd:pfam13768   21 KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPLGGSDLLGALKEAVRAPASPGYIRHV 100

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462503609  402 FVITDGAVNN-TGKVLELVRNHAFSTRCYSFGIGPNVCHRLVKGLASVSEGSAE 454
Cdd:pfam13768  101 LLLTDGSPMQgETRVSDLISRAPGKIRFFAYGLGASISAPMLQLLAEASNGTYE 154
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 322-446 2.31e-08

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 56.61  E-value: 2.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503609  322 KDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTYSEDSLAmacDDIQRMKADmGGTNILSPLKWV---IRQPvhRGHP 398
Cdd:COG2425    140 KAAALALLRALRPNRRFGVILFDTEVVEDLPLTADDGLEDAI---EFLSGLFAG-GGTDIAPALRAAlelLEEP--DYRN 213

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2462503609  399 RLLFVITDGAVNNT-GKVLELVRNHAFSTRCYSFGIGPNVCHRLVKGLA 446
Cdd:COG2425    214 ADIVLITDGEAGVSpEELLREVRAKESGVRLFTVAIGDAGNPGLLEALA 262
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 338-447 9.44e-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: 9.44e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503609   338 FNIIGFGSTFKSLFPSSQTYSEDSLAMACDDIQRMkaDMGGTNILSPLKWVIRQPVH------RGHPRLLFVITDGAVNN 411
Cdd:smart00327   40 VGLVTFSDDARVLFPLNDSRSKDALLEALASLSYK--LGGGTNLGAALQYALENLFSksagsrRGAPKVVILITDGESND 117

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 2462503609   412 TGK-VLELVRN-HAFSTRCYSFGIGPNVCHRLVKGLAS 447
Cdd:smart00327  118 GPKdLLKAAKElKRSGVKVFVVGVGNDVDEEELKKLAS 155
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 15-146 1.07e-04

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: 42.86  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503609   15 LTASDVTSCVSGYALGLTASLTYGNLEAQPFQGLFVYPLDECTTVIGFEAVIADRVVTVQIKDKAK--------LESGHf 86
Cdd:pfam08487    1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEakkeyeeaVARGK- 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503609   87 DASHVRspTVTGNIlqdgvsiaphsctpgkvtldedlerilFVANLGTIAPMENVTIFIS 146
Cdd:pfam08487   80 TAGLLE--QDTPDV---------------------------FTTSVGNIPPGEKVTVELT 110
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
18-118 3.34e-03

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 38.88  E-value: 3.34e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503609    18 SDVTSCVSGYalglTASLTYGNlEAQPFQGLFVYPLDECTTVIGFEAVIADRVVTV-QIKDKAK--------LESGHfDA 88
Cdd:smart00609   24 SKVTSRFAHT----VVTSRVVN-RAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVgEIKEKEVaqkqyekaVSQGK-TA 97

                            90       100       110
                    ....*....|....*....|....*....|
gi 2462503609    89 SHVRSPTVTGNILQDGVSIAPHSctpgKVT 118
Cdd:smart00609   98 GLVRASGRSMEQFTVSVNVAPGS----KVT 123
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 313-468 1.98e-51

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: 178.56  E-value: 1.98e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503609  313 MKKKSRAERKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTYSEDSLAMACDDIQRMKADmGGTNILSPLKWVIRQP 392
Cdd:cd01461     15 MSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQAL-GGTNMNDALEAALELL 93

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462503609  393 VH-RGHPRLLFVITDGAVNNTGKVLELVRNHA-FSTRCYSFGIGPNVCHRLVKGLASVSEGSAELLMEGERLQPKMVK 468
Cdd:cd01461     94 NSsPGSVPQIILLTDGEVTNESQILKNVREALsGRIRLFTFGIGSDVNTYLLERLAREGRGIARRIYETDDIESQLLR 171
VIT_2 pfam13757
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 2-79 2.82e-37

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: 134.51  E-value: 2.82e-37
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462503609    2 PGLLNWITGAALPLTASDVTSCVSGYALGLTASLTYGNLEAQPFQGLFVYPLDECTTVIGFEAVIADRVVTVQIKDKA 79
Cdd:pfam13757    1 PGLLNWSTRTPLPLKASRVSACVNGYSLGVTASLTYYNPQPYPVEGVFVYPLDEGTTVVGFEAEIAGRVISVQLKERE 78
VWA_3 pfam13768
von Willebrand factor type A domain;
322-454 4.18e-27

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 108.25  E-value: 4.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503609  322 KDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTYSEDSLAMACDDIQRMKADMGGTNILSPLKWVIRQPVHRGHPRLL 401
Cdd:pfam13768   21 KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPLGGSDLLGALKEAVRAPASPGYIRHV 100

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462503609  402 FVITDGAVNN-TGKVLELVRNHAFSTRCYSFGIGPNVCHRLVKGLASVSEGSAE 454
Cdd:pfam13768  101 LLLTDGSPMQgETRVSDLISRAPGKIRFFAYGLGASISAPMLQLLAEASNGTYE 154
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 322-446 2.31e-08

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 56.61  E-value: 2.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503609  322 KDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTYSEDSLAmacDDIQRMKADmGGTNILSPLKWV---IRQPvhRGHP 398
Cdd:COG2425    140 KAAALALLRALRPNRRFGVILFDTEVVEDLPLTADDGLEDAI---EFLSGLFAG-GGTDIAPALRAAlelLEEP--DYRN 213

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2462503609  399 RLLFVITDGAVNNT-GKVLELVRNHAFSTRCYSFGIGPNVCHRLVKGLA 446
Cdd:COG2425    214 ADIVLITDGEAGVSpEELLREVRAKESGVRLFTVAIGDAGNPGLLEALA 262
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 338-447 9.44e-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: 9.44e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503609   338 FNIIGFGSTFKSLFPSSQTYSEDSLAMACDDIQRMkaDMGGTNILSPLKWVIRQPVH------RGHPRLLFVITDGAVNN 411
Cdd:smart00327   40 VGLVTFSDDARVLFPLNDSRSKDALLEALASLSYK--LGGGTNLGAALQYALENLFSksagsrRGAPKVVILITDGESND 117

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 2462503609   412 TGK-VLELVRN-HAFSTRCYSFGIGPNVCHRLVKGLAS 447
Cdd:smart00327  118 GPKdLLKAAKElKRSGVKVFVVGVGNDVDEEELKKLAS 155
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 313-447 1.40e-06

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: 49.49  E-value: 1.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503609  313 MKKKSRAERKDAMLVALKSLMPACL---FNIIGFGSTFKSLFPSSQTYSEDSLAmacDDIQRMKAD-MGGTNILSPLKWV 388
Cdd:cd00198     13 MGGEKLDKAKEALKALVSSLSASPPgdrVGLVTFGSNARVVLPLTTDTDKADLL---EAIDALKKGlGGGTNIGAALRLA 89

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462503609  389 IRQ---PVHRGHPRLLFVITDGAVN-NTGKVLELVRN-HAFSTRCYSFGIGPNVCHRLVKGLAS 447
Cdd:cd00198     90 LELlksAKRPNARRVIILLTDGEPNdGPELLAEAARElRKLGITVYTIGIGDDANEDELKEIAD 153
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 15-146 1.07e-04

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: 42.86  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503609   15 LTASDVTSCVSGYALGLTASLTYGNLEAQPFQGLFVYPLDECTTVIGFEAVIADRVVTVQIKDKAK--------LESGHf 86
Cdd:pfam08487    1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEakkeyeeaVARGK- 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503609   87 DASHVRspTVTGNIlqdgvsiaphsctpgkvtldedlerilFVANLGTIAPMENVTIFIS 146
Cdd:pfam08487   80 TAGLLE--QDTPDV---------------------------FTTSVGNIPPGEKVTVELT 110
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
18-118 3.34e-03

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 38.88  E-value: 3.34e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503609    18 SDVTSCVSGYalglTASLTYGNlEAQPFQGLFVYPLDECTTVIGFEAVIADRVVTV-QIKDKAK--------LESGHfDA 88
Cdd:smart00609   24 SKVTSRFAHT----VVTSRVVN-RAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVgEIKEKEVaqkqyekaVSQGK-TA 97

                            90       100       110
                    ....*....|....*....|....*....|
gi 2462503609    89 SHVRSPTVTGNILQDGVSIAPHSctpgKVT 118
Cdd:smart00609   98 GLVRASGRSMEQFTVSVNVAPGS----KVT 123
 
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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