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Conserved domains on  [gi|1034555538|ref|XP_016855795|]
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von Willebrand factor A domain-containing protein 5B1 isoform X9 [Homo sapiens]

Protein Classification

vWA_interalpha_trypsin_inhibitor domain-containing protein( domain architecture ID 10106949)

vWA_interalpha_trypsin_inhibitor 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- ...
 19-187 1.53e-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: 1.53e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538  19 HGEFIFLIDRSSSMSGISMHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTYSEDSLAMACDDIQRMKADmGGT 98
Cdd:cd01461     2 PKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQAL-GGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538  99 NILSPLKWVIRQPVH-RGHPRLLFVITDGAVNNTGKVLELVRNHA-FSTRCYSFGIGPNVCHRLVKGLASVSEGSAELLM 176
Cdd:cd01461    81 NMNDALEAALELLNSsPGSVPQIILLTDGEVTNESQILKNVREALsGRIRLFTFGIGSDVNTYLLERLAREGRGIARRIY 160

                         170
                  ....*....|.
gi 1034555538 177 EGERLQPKMVK 187
Cdd:cd01461   161 ETDDIESQLLR 171
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 19-187 1.53e-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: 1.53e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538  19 HGEFIFLIDRSSSMSGISMHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTYSEDSLAMACDDIQRMKADmGGT 98
Cdd:cd01461     2 PKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQAL-GGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538  99 NILSPLKWVIRQPVH-RGHPRLLFVITDGAVNNTGKVLELVRNHA-FSTRCYSFGIGPNVCHRLVKGLASVSEGSAELLM 176
Cdd:cd01461    81 NMNDALEAALELLNSsPGSVPQIILLTDGEVTNESQILKNVREALsGRIRLFTFGIGSDVNTYLLERLAREGRGIARRIY 160

                         170
                  ....*....|.
gi 1034555538 177 EGERLQPKMVK 187
Cdd:cd01461   161 ETDDIESQLLR 171
VWA_3 pfam13768
von Willebrand factor type A domain;
20-173 2.00e-31

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 120.19  E-value: 2.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538  20 GEFIFLIDRSSSMSGiSMHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTYSEDSLAMACDDIQRMKADMGGTN 99
Cdd:pfam13768   1 GDVVIVVDVSSSMSG-EPKLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPLGGSD 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034555538 100 ILSPLKWVIRQPVHRGHPRLLFVITDGAVNN-TGKVLELVRNHAFSTRCYSFGIGPNVCHRLVKGLASVSEGSAE 173
Cdd:pfam13768  80 LLGALKEAVRAPASPGYIRHVLLLTDGSPMQgETRVSDLISRAPGKIRFFAYGLGASISAPMLQLLAEASNGTYE 154
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 21-203 1.05e-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: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538  21 EFIFLIDRSSSMSGISMHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSsqTYSEDSLAMAcDDIQRMKADmGGTNI 100
Cdd:COG2304    93 NLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPP--TPATDRAKIL-AAIDRLQAG-GGTAL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538 101 LSPLKWVIRQPV---HRGHPRLLFVITDGAVN----NTGKVLELVRNHAFS-TRCYSFGIGPNVCHRLVKGLASVSEGSA 172
Cdd:COG2304   169 GAGLELAYELARkhfIPGRVNRVILLTDGDANvgitDPEELLKLAEEAREEgITLTTLGVGSDYNEDLLERLADAGGGNY 248

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034555538 173 ELLMEGERLQPKMVKSLKKAMAPVLSDVTVE 203
Cdd:COG2304   249 YYIDDPEEAEKVFVREFSRIGYENRALATED 279
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 22-166 2.68e-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: 2.68e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538   22 FIFLIDRSSSMSGISMHRVKDAMLVALKSL---MPACLFNIIGFGSTFKSLFPSSQTYSEDSLAMACDDIQRMkaDMGGT 98
Cdd:smart00327   2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYK--LGGGT 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034555538   99 NILSPLKWVIRQPVH------RGHPRLLFVITDGAVNNTGK-VLELVRN-HAFSTRCYSFGIGPNVCHRLVKGLAS 166
Cdd:smart00327  80 NLGAALQYALENLFSksagsrRGAPKVVILITDGESNDGPKdLLKAAKElKRSGVKVFVVGVGNDVDEEELKKLAS 155
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 19-187 1.53e-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: 1.53e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538  19 HGEFIFLIDRSSSMSGISMHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTYSEDSLAMACDDIQRMKADmGGT 98
Cdd:cd01461     2 PKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQAL-GGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538  99 NILSPLKWVIRQPVH-RGHPRLLFVITDGAVNNTGKVLELVRNHA-FSTRCYSFGIGPNVCHRLVKGLASVSEGSAELLM 176
Cdd:cd01461    81 NMNDALEAALELLNSsPGSVPQIILLTDGEVTNESQILKNVREALsGRIRLFTFGIGSDVNTYLLERLAREGRGIARRIY 160

                         170
                  ....*....|.
gi 1034555538 177 EGERLQPKMVK 187
Cdd:cd01461   161 ETDDIESQLLR 171
VWA_3 pfam13768
von Willebrand factor type A domain;
20-173 2.00e-31

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 120.19  E-value: 2.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538  20 GEFIFLIDRSSSMSGiSMHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTYSEDSLAMACDDIQRMKADMGGTN 99
Cdd:pfam13768   1 GDVVIVVDVSSSMSG-EPKLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPLGGSD 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034555538 100 ILSPLKWVIRQPVHRGHPRLLFVITDGAVNN-TGKVLELVRNHAFSTRCYSFGIGPNVCHRLVKGLASVSEGSAE 173
Cdd:pfam13768  80 LLGALKEAVRAPASPGYIRHVLLLTDGSPMQgETRVSDLISRAPGKIRFFAYGLGASISAPMLQLLAEASNGTYE 154
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 21-203 1.05e-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: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538  21 EFIFLIDRSSSMSGISMHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSsqTYSEDSLAMAcDDIQRMKADmGGTNI 100
Cdd:COG2304    93 NLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPP--TPATDRAKIL-AAIDRLQAG-GGTAL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538 101 LSPLKWVIRQPV---HRGHPRLLFVITDGAVN----NTGKVLELVRNHAFS-TRCYSFGIGPNVCHRLVKGLASVSEGSA 172
Cdd:COG2304   169 GAGLELAYELARkhfIPGRVNRVILLTDGDANvgitDPEELLKLAEEAREEgITLTTLGVGSDYNEDLLERLADAGGGNY 248

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034555538 173 ELLMEGERLQPKMVKSLKKAMAPVLSDVTVE 203
Cdd:COG2304   249 YYIDDPEEAEKVFVREFSRIGYENRALATED 279
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 20-165 1.74e-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: 83.19  E-value: 1.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538  20 GEFIFLIDRSSSMSGISMHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTYSEDSLAmacDDIQRMKADmGGTN 99
Cdd:COG2425   119 GPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVEDLPLTADDGLEDAI---EFLSGLFAG-GGTD 194

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538 100 ILSPLKWV---IRQPvhRGHPRLLFVITDGAVNNT-GKVLELVRNHAFSTRCYSFGIGPNVCHRLVKGLA 165
Cdd:COG2425   195 IAPALRAAlelLEEP--DYRNADIVLITDGEAGVSpEELLREVRAKESGVRLFTVAIGDAGNPGLLEALA 262
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 23-166 1.76e-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: 1.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538  23 IFLIDRSSSMSGISMHRVKDAMLVALKSLMPACL---FNIIGFGSTFKSLFPSSQTYSEDSLAmacDDIQRMKAD-MGGT 98
Cdd:cd00198     4 VFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPgdrVGLVTFGSNARVVLPLTTDTDKADLL---EAIDALKKGlGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034555538  99 NILSPLKWVIRQ---PVHRGHPRLLFVITDGAVN-NTGKVLELVRN-HAFSTRCYSFGIGPNVCHRLVKGLAS 166
Cdd:cd00198    81 NIGAALRLALELlksAKRPNARRVIILLTDGEPNdGPELLAEAARElRKLGITVYTIGIGDDANEDELKEIAD 153
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 22-166 2.68e-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: 2.68e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538   22 FIFLIDRSSSMSGISMHRVKDAMLVALKSL---MPACLFNIIGFGSTFKSLFPSSQTYSEDSLAMACDDIQRMkaDMGGT 98
Cdd:smart00327   2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYK--LGGGT 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034555538   99 NILSPLKWVIRQPVH------RGHPRLLFVITDGAVNNTGK-VLELVRN-HAFSTRCYSFGIGPNVCHRLVKGLAS 166
Cdd:smart00327  80 NLGAALQYALENLFSksagsrRGAPKVVILITDGESNDGPKdLLKAAKElKRSGVKVFVVGVGNDVDEEELKKLAS 155
VWA pfam00092
von Willebrand factor type A domain;
23-166 3.56e-08

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 53.82  E-value: 3.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538  23 IFLIDRSSSMSGISMHRVKDAMLVALKSL---MPACLFNIIGFGSTFKSLFPSSQTYSEDSLAmacDDIQRMK-ADMGGT 98
Cdd:pfam00092   3 VFLLDGSGSIGGDNFEKVKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEFPLNDYSSKEELL---SAVDNLRyLGGGTT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034555538  99 NILSPLKWVIRQPVHR------GHPRLLFVITDGaVNNTGKVLELVRN-HAFSTRCYSFGIGPNVCHRLVKgLAS 166
Cdd:pfam00092  80 NTGKALKYALENLFSSaagarpGAPKVVVLLTDG-RSQDGDPEEVARElKSAGVTVFAVGVGNADDEELRK-IAS 152
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
21-156 9.62e-08

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: 9.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538  21 EFIFLIDRSSSMSGISMHRVKDAMLVALKSLMPA------CLFNIIGFGSTFKSLFPSSqtysedslamACDDIQ--RMK 92
Cdd:COG4245     7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDpyaletVEVSVITFDGEAKVLLPLT----------DLEDFQppDLS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034555538  93 ADmGGTNILSPLKWVIRQ----------PVHRGHPRLLFVITDGAVN--NTGKVLELVRNHAFSTRC--YSFGIGPNV 156
Cdd:COG4245    77 AS-GGTPLGAALELLLDLierrvqkytaEGKGDWRPVVFLITDGEPTdsDWEAALQRLKDGEAAKKAniFAIGVGPDA 153
VWA_2 pfam13519
von Willebrand factor type A domain;
22-123 3.50e-07

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 49.21  E-value: 3.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538  22 FIFLIDRSSSMSGIS-----MHRVKDAMLVALKSlMPACLFNIIGFGSTFKSLFPSSqtyseDSLAMACDDIQRMKADMG 96
Cdd:pfam13519   1 LVFVLDTSGSMRNGDygptrLEAAKDAVLALLKS-LPGDRVGLVTFGDGPEVLIPLT-----KDRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1034555538  97 GTNILSPLK----WVIRQPvhRGHPRLLFVI 123
Cdd:pfam13519  75 GTNLAAALQlaraALKHRR--KNQPRRIVLI 103
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 22-155 6.89e-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: 6.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538  22 FIFLIDRSSSMSGIS-MHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSsqTYSEDSLAMAcddIQRMKADmGGTNI 100
Cdd:COG1240    95 VVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRDRVGLVAFGGEAEVLLPL--TRDREALKRA---LDELPPG-GGTPL 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538 101 LSPLKWVIR--QPVHRGHPRLLFVITDGaVNNTGKV--LELVRN-HAFSTRCYSFGIGPN 155
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 ...
 23-153 9.03e-06

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: 9.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538  23 IFLIDRSSSMSGISMHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTyseDSLAMACDDIQRMKADM------G 96
Cdd:cd01463    17 VILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPCFND---TLVQATTSNKKVLKEALdmleakG 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538  97 GTNILSPLKW---VIRQPVHRGHP-------RLLFVITDGAVNNTGKVLELV---RNHAFSTRCYSFGIG 153
Cdd:cd01463    94 IANYTKALEFafsLLLKNLQSNHSgsrsqcnQAIMLITDGVPENYKEIFDKYnwdKNSEIPVRVFTYLIG 163
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 22-172 2.90e-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: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538  22 FIFLIDRSSSMSGISMHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTYSEDSLAMAcddIQRMKADmGGTNIL 101
Cdd:cd01465     3 LVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAETVLPATPVRDKAAILAA---IDRLTAG-GSTAGG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538 102 SPLKWVIRQPVH----RGHPRLLfVITDGAvNNTG-----KVLELV---RNHAFSTRCysFGIGPNVCHRLVKGLASVSE 169
Cdd:cd01465    79 AGIQLGYQEAQKhfvpGGVNRIL-LATDGD-FNVGetdpdELARLVaqkRESGITLST--LGFGDNYNEDLMEAIADAGN 154


                  ...
gi 1034555538 170 GSA 172
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 ...
 25-171 3.78e-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: 44.69  E-value: 3.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538  25 LIDRSSSMSGISMHRVKDAMLVALKSLMPACLFNIIGFGSTFKSLFPSSQTySEDSLAMACDDIQRMKADmGGTNILSPL 104
Cdd:cd01466     6 VLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLSPLRRM-TAKGKRSAKRVVDGLQAG-GGTNVVGGL 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538 105 KW---VIRQPVHRGHPRLLFVITDGAVNNTGKVlelVRNHAFSTRCYSFGIGPNVCHRLVKGLASVSEGS 171
Cdd:cd01466    84 KKalkVLGDRRQKNPVASIMLLSDGQDNHGAVV---LRADNAPIPIHTFGLGASHDPALLAFIAEITGGT 150
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 23-154 2.13e-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: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555538  23 IFLIDRSSSMSGISMHRVKDAMLVALKSlmpaclFNIIG---------FGSTFKSLFPSSQTYSEDSLAMACDDIQRMka 93
Cdd:cd01450     4 VFLLDGSESVGPENFEKVKDFIEKLVEK------LDIGPdktrvglvqYSDDVRVEFSLNDYKSKDDLLKAVKNLKYL-- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034555538  94 DMGGTNILSPLKWVIRQ-----PVHRGHPRLLFVITDGAVNNTGKVLELVRN-HAFSTRCYSFGIGP 154
Cdd:cd01450    76 GGGGTNTGKALQYALEQlfsesNARENVPKVIIVLTDGRSDDGGDPKEAAAKlKDEGIKVFVVGVGP 142
 
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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