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Conserved domains on  [gi|2462503607|ref|XP_054190360|]
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von Willebrand factor A domain-containing protein 5B1 isoform X2 [Homo sapiens]

Protein Classification

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- ...
 359-527 7.01e-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: 208.61  E-value: 7.01e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  359 HGEFIFLIDRSSSMSGISMHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTYSEDSLAMACDDIQRMKADmGGT 438
Cdd:cd01461      2 PKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQAL-GGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  439 NILSPLKWVIRQPVH-RGHPRLLFVITDGAVNNTGKVLELVRNHA-FSTRCYSFGIGPNVCHRLVKGLASVSEGSAELLM 516
Cdd:cd01461     81 NMNDALEAALELLNSsPGSVPQIILLTDGEVTNESQILKNVREALsGRIRLFTFGIGSDVNTYLLERLAREGRGIARRIY 160

                          170
                   ....*....|.
gi 2462503607  517 EGERLQPKMVK 527
Cdd:cd01461    161 ETDDIESQLLR 171
VIT_2 pfam13757
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 2-79 1.88e-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: 134.90  E-value: 1.88e-37
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462503607    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 1.10e-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: 1.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607   15 LTASDVTSCVSGYALGLTASLTYGNLEAQPFQGLFVYPLDECTTVIGFEAVIADRVVTVQIKDKAK--------LESGHf 86
Cdd:pfam08487    1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEakkeyeeaVARGK- 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607   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- ...
 359-527 7.01e-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: 208.61  E-value: 7.01e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  359 HGEFIFLIDRSSSMSGISMHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTYSEDSLAMACDDIQRMKADmGGT 438
Cdd:cd01461      2 PKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQAL-GGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  439 NILSPLKWVIRQPVH-RGHPRLLFVITDGAVNNTGKVLELVRNHA-FSTRCYSFGIGPNVCHRLVKGLASVSEGSAELLM 516
Cdd:cd01461     81 NMNDALEAALELLNSsPGSVPQIILLTDGEVTNESQILKNVREALsGRIRLFTFGIGSDVNTYLLERLAREGRGIARRIY 160

                          170
                   ....*....|.
gi 2462503607  517 EGERLQPKMVK 527
Cdd:cd01461    161 ETDDIESQLLR 171
VIT_2 pfam13757
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 2-79 1.88e-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: 134.90  E-value: 1.88e-37
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462503607    2 PGLLNWITGAALPLTASDVTSCVSGYALGLTASLTYGNLEAQPFQGLFVYPLDECTTVIGFEAVIADRVVTVQIKDKA 79
Cdd:pfam13757    1 PGLLNWSTRTPLPLKASRVSACVNGYSLGVTASLTYYNPQPYPVEGVFVYPLDEGTTVVGFEAEIAGRVISVQLKERE 78
VWA_3 pfam13768
von Willebrand factor type A domain;
360-513 1.73e-31

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 120.96  E-value: 1.73e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  360 GEFIFLIDRSSSMSGiSMHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTYSEDSLAMACDDIQRMKADMGGTN 439
Cdd:pfam13768    1 GDVVIVVDVSSSMSG-EPKLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPLGGSD 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462503607  440 ILSPLKWVIRQPVHRGHPRLLFVITDGAVNN-TGKVLELVRNHAFSTRCYSFGIGPNVCHRLVKGLASVSEGSAE 513
Cdd:pfam13768   80 LLGALKEAVRAPASPGYIRHVLLLTDGSPMQgETRVSDLISRAPGKIRFFAYGLGASISAPMLQLLAEASNGTYE 154
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 361-543 1.55e-17

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: 1.55e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  361 EFIFLIDRSSSMSGISMHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSsqTYSEDSLAMAcDDIQRMKADmGGTNI 440
Cdd:COG2304     93 NLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPP--TPATDRAKIL-AAIDRLQAG-GGTAL 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  441 LSPLKWVIRQPV---HRGHPRLLFVITDGAVN----NTGKVLELVRNHAFS-TRCYSFGIGPNVCHRLVKGLASVSEGSA 512
Cdd:COG2304    169 GAGLELAYELARkhfIPGRVNRVILLTDGDANvgitDPEELLKLAEEAREEgITLTTLGVGSDYNEDLLERLADAGGGNY 248

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2462503607  513 ELLMEGERLQPKMVKSLKKAMAPVLSDVTVE 543
Cdd:COG2304    249 YYIDDPEEAEKVFVREFSRIGYENRALATED 279
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 362-506 3.78e-13

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: 69.02  E-value: 3.78e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607   362 FIFLIDRSSSMSGISMHRVKDAMLVALKSL---MPACLFNIIGFGSTFKSLFPSSQTYSEDSLAMACDDIQRMkaDMGGT 438
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYK--LGGGT 79

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462503607   439 NILSPLKWVIRQPVH------RGHPRLLFVITDGAVNNTGK-VLELVRN-HAFSTRCYSFGIGPNVCHRLVKGLAS 506
Cdd:smart00327   80 NLGAALQYALENLFSksagsrRGAPKVVILITDGESNDGPKdLLKAAKElKRSGVKVFVVGVGNDVDEEELKKLAS 155
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 15-146 1.10e-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: 1.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607   15 LTASDVTSCVSGYALGLTASLTYGNLEAQPFQGLFVYPLDECTTVIGFEAVIADRVVTVQIKDKAK--------LESGHf 86
Cdd:pfam08487    1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEakkeyeeaVARGK- 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607   87 DASHVRspTVTGNIlqdgvsiaphsctpgkvtldedlerilFVANLGTIAPMENVTIFIS 146
Cdd:pfam08487   80 TAGLLE--QDTPDV---------------------------FTTSVGNIPPGEKVTVELT 110
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
18-118 3.45e-03

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 38.88  E-value: 3.45e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607    18 SDVTSCVSGYalglTASLTYGNlEAQPFQGLFVYPLDECTTVIGFEAVIADRVVTV-QIKDKAK--------LESGHfDA 88
Cdd:smart00609   24 SKVTSRFAHT----VVTSRVVN-RAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVgEIKEKEVaqkqyekaVSQGK-TA 97

                            90       100       110
                    ....*....|....*....|....*....|
gi 2462503607    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- ...
 359-527 7.01e-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: 208.61  E-value: 7.01e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  359 HGEFIFLIDRSSSMSGISMHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTYSEDSLAMACDDIQRMKADmGGT 438
Cdd:cd01461      2 PKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQAL-GGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  439 NILSPLKWVIRQPVH-RGHPRLLFVITDGAVNNTGKVLELVRNHA-FSTRCYSFGIGPNVCHRLVKGLASVSEGSAELLM 516
Cdd:cd01461     81 NMNDALEAALELLNSsPGSVPQIILLTDGEVTNESQILKNVREALsGRIRLFTFGIGSDVNTYLLERLAREGRGIARRIY 160

                          170
                   ....*....|.
gi 2462503607  517 EGERLQPKMVK 527
Cdd:cd01461    161 ETDDIESQLLR 171
VIT_2 pfam13757
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 2-79 1.88e-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: 134.90  E-value: 1.88e-37
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462503607    2 PGLLNWITGAALPLTASDVTSCVSGYALGLTASLTYGNLEAQPFQGLFVYPLDECTTVIGFEAVIADRVVTVQIKDKA 79
Cdd:pfam13757    1 PGLLNWSTRTPLPLKASRVSACVNGYSLGVTASLTYYNPQPYPVEGVFVYPLDEGTTVVGFEAEIAGRVISVQLKERE 78
VWA_3 pfam13768
von Willebrand factor type A domain;
360-513 1.73e-31

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 120.96  E-value: 1.73e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  360 GEFIFLIDRSSSMSGiSMHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTYSEDSLAMACDDIQRMKADMGGTN 439
Cdd:pfam13768    1 GDVVIVVDVSSSMSG-EPKLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPLGGSD 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462503607  440 ILSPLKWVIRQPVHRGHPRLLFVITDGAVNN-TGKVLELVRNHAFSTRCYSFGIGPNVCHRLVKGLASVSEGSAE 513
Cdd:pfam13768   80 LLGALKEAVRAPASPGYIRHVLLLTDGSPMQgETRVSDLISRAPGKIRFFAYGLGASISAPMLQLLAEASNGTYE 154
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 361-543 1.55e-17

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: 1.55e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  361 EFIFLIDRSSSMSGISMHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSsqTYSEDSLAMAcDDIQRMKADmGGTNI 440
Cdd:COG2304     93 NLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPP--TPATDRAKIL-AAIDRLQAG-GGTAL 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  441 LSPLKWVIRQPV---HRGHPRLLFVITDGAVN----NTGKVLELVRNHAFS-TRCYSFGIGPNVCHRLVKGLASVSEGSA 512
Cdd:COG2304    169 GAGLELAYELARkhfIPGRVNRVILLTDGDANvgitDPEELLKLAEEAREEgITLTTLGVGSDYNEDLLERLADAGGGNY 248

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2462503607  513 ELLMEGERLQPKMVKSLKKAMAPVLSDVTVE 543
Cdd:COG2304    249 YYIDDPEEAEKVFVREFSRIGYENRALATED 279
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 360-505 1.60e-17

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 83.96  E-value: 1.60e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  360 GEFIFLIDRSSSMSGISMHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTYSEDSLAmacDDIQRMKADmGGTN 439
Cdd:COG2425    119 GPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVEDLPLTADDGLEDAI---EFLSGLFAG-GGTD 194

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  440 ILSPLKWV---IRQPvhRGHPRLLFVITDGAVNNT-GKVLELVRNHAFSTRCYSFGIGPNVCHRLVKGLA 505
Cdd:COG2425    195 IAPALRAAlelLEEP--DYRNADIVLITDGEAGVSpEELLREVRAKESGVRLFTVAIGDAGNPGLLEALA 262
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 363-506 2.47e-14

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: 71.83  E-value: 2.47e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  363 IFLIDRSSSMSGISMHRVKDAMLVALKSLMPACL---FNIIGFGSTFKSLFPSSQTYSEDSLAmacDDIQRMKAD-MGGT 438
Cdd:cd00198      4 VFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPgdrVGLVTFGSNARVVLPLTTDTDKADLL---EAIDALKKGlGGGT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462503607  439 NILSPLKWVIRQ---PVHRGHPRLLFVITDGAVN-NTGKVLELVRN-HAFSTRCYSFGIGPNVCHRLVKGLAS 506
Cdd:cd00198     81 NIGAALRLALELlksAKRPNARRVIILLTDGEPNdGPELLAEAARElRKLGITVYTIGIGDDANEDELKEIAD 153
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 362-506 3.78e-13

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: 69.02  E-value: 3.78e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607   362 FIFLIDRSSSMSGISMHRVKDAMLVALKSL---MPACLFNIIGFGSTFKSLFPSSQTYSEDSLAMACDDIQRMkaDMGGT 438
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYK--LGGGT 79

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462503607   439 NILSPLKWVIRQPVH------RGHPRLLFVITDGAVNNTGK-VLELVRN-HAFSTRCYSFGIGPNVCHRLVKGLAS 506
Cdd:smart00327   80 NLGAALQYALENLFSksagsrRGAPKVVILITDGESNDGPKdLLKAAKElKRSGVKVFVVGVGNDVDEEELKKLAS 155
VWA pfam00092
von Willebrand factor type A domain;
363-506 5.01e-08

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 53.82  E-value: 5.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  363 IFLIDRSSSMSGISMHRVKDAMLVALKSL---MPACLFNIIGFGSTFKSLFPSSQTYSEDSLAmacDDIQRMK-ADMGGT 438
Cdd:pfam00092    3 VFLLDGSGSIGGDNFEKVKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEFPLNDYSSKEELL---SAVDNLRyLGGGTT 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462503607  439 NILSPLKWVIRQPVHR------GHPRLLFVITDGaVNNTGKVLELVRN-HAFSTRCYSFGIGPNVCHRLVKgLAS 506
Cdd:pfam00092   80 NTGKALKYALENLFSSaagarpGAPKVVVLLTDG-RSQDGDPEEVARElKSAGVTVFAVGVGNADDEELRK-IAS 152
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
361-496 1.36e-07

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 53.00  E-value: 1.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  361 EFIFLIDRSSSMSGISMHRVKDAMLVALKSLMPA------CLFNIIGFGSTFKSLFPSSqtysedslamACDDIQ--RMK 432
Cdd:COG4245      7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDpyaletVEVSVITFDGEAKVLLPLT----------DLEDFQppDLS 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462503607  433 ADmGGTNILSPLKWVIRQ----------PVHRGHPRLLFVITDGAVN--NTGKVLELVRNHAFSTRC--YSFGIGPNV 496
Cdd:COG4245     77 AS-GGTPLGAALELLLDLierrvqkytaEGKGDWRPVVFLITDGEPTdsDWEAALQRLKDGEAAKKAniFAIGVGPDA 153
VWA_2 pfam13519
von Willebrand factor type A domain;
362-463 4.84e-07

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 49.21  E-value: 4.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  362 FIFLIDRSSSMSGIS-----MHRVKDAMLVALKSlMPACLFNIIGFGSTFKSLFPSSqtyseDSLAMACDDIQRMKADMG 436
Cdd:pfam13519    1 LVFVLDTSGSMRNGDygptrLEAAKDAVLALLKS-LPGDRVGLVTFGDGPEVLIPLT-----KDRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462503607  437 GTNILSPLK----WVIRQPvhRGHPRLLFVI 463
Cdd:pfam13519   75 GTNLAAALQlaraALKHRR--KNQPRRIVLI 103
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 362-495 9.89e-07

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 51.48  E-value: 9.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  362 FIFLIDRSSSMSGIS-MHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSsqTYSEDSLAMAcddIQRMKADmGGTNI 440
Cdd:COG1240     95 VVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRDRVGLVAFGGEAEVLLPL--TRDREALKRA---LDELPPG-GGTPL 168

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  441 LSPLKWVIR--QPVHRGHPRLLFVITDGaVNNTGKV--LELVRN-HAFSTRCYSFGIGPN 495
Cdd:COG1240    169 GDALALALEllKRADPARRKVIVLLTDG-RDNAGRIdpLEAAELaAAAGIRIYTIGVGTE 227
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 363-493 1.27e-05

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: 47.39  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  363 IFLIDRSSSMSGISMHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTyseDSLAMACDDIQRMKADM------G 436
Cdd:cd01463     17 VILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPCFND---TLVQATTSNKKVLKEALdmleakG 93

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  437 GTNILSPLKW---VIRQPVHRGHP-------RLLFVITDGAVNNTGKVLELV---RNHAFSTRCYSFGIG 493
Cdd:cd01463     94 IANYTKALEFafsLLLKNLQSNHSgsrsqcnQAIMLITDGVPENYKEIFDKYnwdKNSEIPVRVFTYLIG 163
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 362-512 4.08e-05

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: 45.34  E-value: 4.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  362 FIFLIDRSSSMSGISMHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTYSEDSLAMAcddIQRMKADmGGTNIL 441
Cdd:cd01465      3 LVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAETVLPATPVRDKAAILAA---IDRLTAG-GSTAGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  442 SPLKWVIRQPVH----RGHPRLLfVITDGAvNNTG-----KVLELV---RNHAFSTRCysFGIGPNVCHRLVKGLASVSE 509
Cdd:cd01465     79 AGIQLGYQEAQKhfvpGGVNRIL-LATDGD-FNVGetdpdELARLVaqkRESGITLST--LGFGDNYNEDLMEAIADAGN 154


                   ...
gi 2462503607  510 GSA 512
Cdd:cd01465    155 GNT 157
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 365-511 4.55e-05

VWA C3HC4-type: 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. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known.


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 45.07  E-value: 4.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  365 LIDRSSSMSGISMHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTySEDSLAMACDDIQRMKADmGGTNILSPL 444
Cdd:cd01466      6 VLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLSPLRRM-TAKGKRSAKRVVDGLQAG-GGTNVVGGL 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  445 KW---VIRQPVHRGHPRLLFVITDGAVNNTGKVlelVRNHAFSTRCYSFGIGPNVCHRLVKGLASVSEGS 511
Cdd:cd01466     84 KKalkVLGDRRQKNPVASIMLLSDGQDNHGAVV---LRADNAPIPIHTFGLGASHDPALLAFIAEITGGT 150
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 15-146 1.10e-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: 1.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607   15 LTASDVTSCVSGYALGLTASLTYGNLEAQPFQGLFVYPLDECTTVIGFEAVIADRVVTVQIKDKAK--------LESGHf 86
Cdd:pfam08487    1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEakkeyeeaVARGK- 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607   87 DASHVRspTVTGNIlqdgvsiaphsctpgkvtldedlerilFVANLGTIAPMENVTIFIS 146
Cdd:pfam08487   80 TAGLLE--QDTPDV---------------------------FTTSVGNIPPGEKVTVELT 110
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 363-494 2.99e-04

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: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 42.66  E-value: 2.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607  363 IFLIDRSSSMSGISMHRVKDAMLVALKSlmpaclFNIIG---------FGSTFKSLFPSSQTYSEDSLAMACDDIQRMka 433
Cdd:cd01450      4 VFLLDGSESVGPENFEKVKDFIEKLVEK------LDIGPdktrvglvqYSDDVRVEFSLNDYKSKDDLLKAVKNLKYL-- 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462503607  434 DMGGTNILSPLKWVIRQ-----PVHRGHPRLLFVITDGAVNNTGKVLELVRN-HAFSTRCYSFGIGP 494
Cdd:cd01450     76 GGGGTNTGKALQYALEQlfsesNARENVPKVIIVLTDGRSDDGGDPKEAAAKlKDEGIKVFVVGVGP 142
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
18-118 3.45e-03

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 38.88  E-value: 3.45e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462503607    18 SDVTSCVSGYalglTASLTYGNlEAQPFQGLFVYPLDECTTVIGFEAVIADRVVTV-QIKDKAK--------LESGHfDA 88
Cdd:smart00609   24 SKVTSRFAHT----VVTSRVVN-RAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVgEIKEKEVaqkqyekaVSQGK-TA 97

                            90       100       110
                    ....*....|....*....|....*....|
gi 2462503607    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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