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Conserved domains on  [gi|1952959430|ref|XP_038407008|]
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von Willebrand factor A domain-containing protein 3B isoform X1 [Canis lupus familiaris]

Protein Classification

VWA domain-containing protein; VWA domain-containing protein; vWA domain-containing protein( domain architecture ID 10077493)

VWA (von Willebrand factor type A) domain-containing protein similar to mammalian von Willebrand factor that plays an essential role in the formation of a platelet plug, to stop bleeding, by anchoring blood platelets to the damaged vessel wall under conditions of high shear stress; VWA (von Willebrand factor type A) domain-containing protein; VWA (von Willebrand factor type A) domain-containing protein similar to mammalian von Willebrand factor that plays an essential role in the formation of a platelet plug, to stop bleeding, by anchoring blood platelets to the damaged vessel wall under conditions of high shear stress; VWA (von Willebrand factor type A) domain-containing protein similar to mammalian von Willebrand factor that plays an essential role in the formation of a platelet plug, to stop bleeding, by anchoring blood platelets to the damaged vessel wall under conditions of high shear stress; VWA (von Willebrand factor type A) domain-containing protein, similar to Dictyostelium discoideum integrin beta-like protein A and mammalian calcium-activated chloride channel regulator; VWA (von Willebrand factor type A) domain-containing protein with an extracellular solute-binding protein (SBP) domain; VWA (von Willebrand factor type A) domain-containing protein, similar to Dictyostelium discoideum integrin beta-like protein A and mammalian calcium-activated chloride channel regulator; VWA (von Willebrand factor type A) domain-containing protein; VWA (von Willebrand factor type A) domain-containing protein similar to Bos taurus von Willebrand factor A domain-containing protein 7; VWA (von Willebrand factor type A) domain-containing protein similar to mammalian von Willebrand factor that plays an essential role in the formation of a platelet plug, to stop bleeding, by anchoring blood platelets to the damaged vessel wall under conditions of high shear stress; VWA (von Willebrand factor type A) domain-containing protein with C-terminal prealbumin-like fold domain that is similar to Corynebacterium diphtheriae domain 1 and domain 3 of surface-anchored protein fimbrial subunit SpaA; VWA (von Willebrand factor type A) domain-containing protein; VWA (von Willebrand factor type A) domain-containing protein similar to Bos taurus von Willebrand factor A domain-containing protein 7; VWA (von Willebrand factor type A) domain-containing protein; VWA (von Willebrand factor type A) domain-containing protein similar to Bos taurus von Willebrand factor A domain-containing protein 7; VWA (von Willebrand factor type A) domain-containing protein, similar to Dictyostelium discoideum integrin beta-like protein A and mammalian calcium-activated chloride channel regulator; VWA (von Willebrand factor type A) domain-containing protein; VWA (von Willebrand factor type A) domain-containing protein similar to mammalian von Willebrand factor that plays an essential role in the formation of a platelet plug, to stop bleeding, by anchoring blood platelets to the damaged vessel wall under conditions of high shear stress; VWA (von Willebrand factor type A) domain-containing protein; VWA (von Willebrand factor type A) domain-containing protein with C-terminal prealbumin-like fold domain that is similar to bacterial pilin adhesin subunit SpaC; von Willebrand factor type A (vWA) domain containing protein, often found at C-terminus of CalY family proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF4537 pfam15057
Domain of unknown function (DUF4537); The function of this domain family is unknown. It is ...
 1034-1160 1.05e-44

Domain of unknown function (DUF4537); The function of this domain family is unknown. It is found in eukaryotes, and is typically between 119 and 141 amino acids in length. In humans, it is found in the chromosomal position C11orf16.


:

Pssm-ID: 464475 [Multi-domain]  Cd Length: 124  Bit Score: 157.47  E-value: 1.05e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430 1034 GQKVIARCDENGFYFPGVVKKCVSPTHALVGFRYGDTKVVPTSFITPVGGAMpCPLLQVGDYVFAKiVIPNGFDfYVPAI 1113
Cdd:pfam15057    1 GQRVLARWDEDGFYYRGTVKKYLNGGQYLVEFDAGDRQVVLTRDIIALEDAM-EHPLRVGDKVLAL-HDPYSQS-YAPGI 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1952959430 1114 VIALPNQDMAEDKFYTVLKCNNRREFCPRSALIKISQNKYALSCSHI 1160
Cdd:pfam15057   78 VLAGPERRVDADEELTVRFYDGKTATVPREEVYKLSQAYYEKAVAYI 124
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 509-658 7.17e-18

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: 84.99  E-value: 7.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  509 IYILIDTSHSM--KSKLDLVKDKIIQFIQEQLKyKRKFNFVQFDAQAvawqEKLVEINEDnLRGAQSWIRDIQIGSSTNT 586
Cdd:COG1240     95 VVLVVDASGSMaaENRLEAAKGALLDFLDDYRP-RDRVGLVAFGGEA----EVLLPLTRD-REALKRALDELPPGGGTPL 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  587 LHALQIA------FADKETQVIYLLTDGRPDQPPEMVIEQVKVFQK--IPIYTISFNyNDEIANGFLKELASLTGGEFHF 658
Cdd:COG1240    169 GDALALAlellkrADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAagIRIYTIGVG-TEAVDEGLLREIAEATGGRYFR 247
 
Name Accession Description Interval E-value
DUF4537 pfam15057
Domain of unknown function (DUF4537); The function of this domain family is unknown. It is ...
 1034-1160 1.05e-44

Domain of unknown function (DUF4537); The function of this domain family is unknown. It is found in eukaryotes, and is typically between 119 and 141 amino acids in length. In humans, it is found in the chromosomal position C11orf16.


Pssm-ID: 464475 [Multi-domain]  Cd Length: 124  Bit Score: 157.47  E-value: 1.05e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430 1034 GQKVIARCDENGFYFPGVVKKCVSPTHALVGFRYGDTKVVPTSFITPVGGAMpCPLLQVGDYVFAKiVIPNGFDfYVPAI 1113
Cdd:pfam15057    1 GQRVLARWDEDGFYYRGTVKKYLNGGQYLVEFDAGDRQVVLTRDIIALEDAM-EHPLRVGDKVLAL-HDPYSQS-YAPGI 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1952959430 1114 VIALPNQDMAEDKFYTVLKCNNRREFCPRSALIKISQNKYALSCSHI 1160
Cdd:pfam15057   78 VLAGPERRVDADEELTVRFYDGKTATVPREEVYKLSQAYYEKAVAYI 124
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 509-658 7.17e-18

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: 84.99  E-value: 7.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  509 IYILIDTSHSM--KSKLDLVKDKIIQFIQEQLKyKRKFNFVQFDAQAvawqEKLVEINEDnLRGAQSWIRDIQIGSSTNT 586
Cdd:COG1240     95 VVLVVDASGSMaaENRLEAAKGALLDFLDDYRP-RDRVGLVAFGGEA----EVLLPLTRD-REALKRALDELPPGGGTPL 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  587 LHALQIA------FADKETQVIYLLTDGRPDQPPEMVIEQVKVFQK--IPIYTISFNyNDEIANGFLKELASLTGGEFHF 658
Cdd:COG1240    169 GDALALAlellkrADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAagIRIYTIGVG-TEAVDEGLLREIAEATGGRYFR 247
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 508-659 1.17e-17

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: 81.46  E-value: 1.17e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  508 CIYILIDTSHSM-KSKLDLVKDKIIQFIQEQLKYKRK--FNFVQFDAQAVAWQEKLVEINEDNLRGAQSWIRDiQIGSST 584
Cdd:cd00198      2 DIVFLLDVSGSMgGEKLDKAKEALKALVSSLSASPPGdrVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKK-GLGGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  585 NTLHALQIAFA-------DKETQVIYLLTDGRPDQPPEMVIEQVKVFQKIPIYTISFNYNDEIANGFLKELASLTGGeFH 657
Cdd:cd00198     81 NIGAALRLALEllksakrPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIADKTTG-GA 159


                   ..
gi 1952959430  658 FY 659
Cdd:cd00198    160 VF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 509-661 4.37e-14

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: 71.72  E-value: 4.37e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430   509 IYILIDTSHSM-KSKLDLVKDKIIQFIQEQLKYKRK--FNFVQFDAQAVAWQEKLVEINEDNLRGAqswIRDIQI--GSS 583
Cdd:smart00327    2 VVFLLDGSGSMgGNRFELAKEFVLKLVEQLDIGPDGdrVGLVTFSDDARVLFPLNDSRSKDALLEA---LASLSYklGGG 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430   584 TNTLHALQIAFA----------DKETQVIYLLTDGRPDQPPEMVIEQVKVFQKIPIYTISFNYNDEIANGFLKELASLTG 653
Cdd:smart00327   79 TNLGAALQYALEnlfsksagsrRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPG 158


                    ....*...
gi 1952959430   654 GEFHFYNF 661
Cdd:smart00327  159 GVYVFLPE 166
VWA_3 pfam13768
von Willebrand factor type A domain;
509-658 1.53e-12

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 66.65  E-value: 1.53e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  509 IYILIDTSHSMKSKLDLVKDKIIQFIQeQLKYKRKFNFVQFDAQAVAWQEKLVEINEDNLRGAQSWIRDIQIGSS-TNTL 587
Cdd:pfam13768    3 VVIVVDVSSSMSGEPKLQKDALSVALR-QLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPLGgSDLL 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952959430  588 HALQIAFA--DKETQV--IYLLTDGRPDQPPEMVIEQV-KVFQKIPIYTISFnyNDEIANGFLKELASLTGGEFHF 658
Cdd:pfam13768   82 GALKEAVRapASPGYIrhVLLLTDGSPMQGETRVSDLIsRAPGKIRFFAYGL--GASISAPMLQLLAEASNGTYEF 155
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 511-660 2.82e-04

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 44.61  E-value: 2.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  511 ILIDTSHSMKSKLDLVKDKIIQFIQEQLKYKRKFNFVQFDAQAVAWQE---------------KLVEINEDNLRGAQSWI 575
Cdd:TIGR03436   58 LVIDTSGSMRNDLDRARAAAIRFLKTVLRPNDRVFVVTFNTRLRLLQDftsdprlleaalnrlKPPLRTDYNSSGAFVRD 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  576 RDIQIGSSTNTLHALQIAFADKETQ----VIYLLTDG---RPDQPPEMVIEQVkvfQK--IPIYTISF---------NYN 637
Cdd:TIGR03436  138 GGGTALYDAITLAALEQLANALAGIpgrkALIVISDGgdnRSRDTLERAIDAA---QRadVAIYSIDArglrapdlgAGA 214

                          170       180
                   ....*....|....*....|....*
gi 1952959430  638 DEIANG--FLKELASLTGGEFHFYN 660
Cdd:TIGR03436  215 KAGLGGpeALERLAEETGGRAFYVN 239
 
Name Accession Description Interval E-value
DUF4537 pfam15057
Domain of unknown function (DUF4537); The function of this domain family is unknown. It is ...
 1034-1160 1.05e-44

Domain of unknown function (DUF4537); The function of this domain family is unknown. It is found in eukaryotes, and is typically between 119 and 141 amino acids in length. In humans, it is found in the chromosomal position C11orf16.


Pssm-ID: 464475 [Multi-domain]  Cd Length: 124  Bit Score: 157.47  E-value: 1.05e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430 1034 GQKVIARCDENGFYFPGVVKKCVSPTHALVGFRYGDTKVVPTSFITPVGGAMpCPLLQVGDYVFAKiVIPNGFDfYVPAI 1113
Cdd:pfam15057    1 GQRVLARWDEDGFYYRGTVKKYLNGGQYLVEFDAGDRQVVLTRDIIALEDAM-EHPLRVGDKVLAL-HDPYSQS-YAPGI 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1952959430 1114 VIALPNQDMAEDKFYTVLKCNNRREFCPRSALIKISQNKYALSCSHI 1160
Cdd:pfam15057   78 VLAGPERRVDADEELTVRFYDGKTATVPREEVYKLSQAYYEKAVAYI 124
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 509-658 7.17e-18

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: 84.99  E-value: 7.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  509 IYILIDTSHSM--KSKLDLVKDKIIQFIQEQLKyKRKFNFVQFDAQAvawqEKLVEINEDnLRGAQSWIRDIQIGSSTNT 586
Cdd:COG1240     95 VVLVVDASGSMaaENRLEAAKGALLDFLDDYRP-RDRVGLVAFGGEA----EVLLPLTRD-REALKRALDELPPGGGTPL 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  587 LHALQIA------FADKETQVIYLLTDGRPDQPPEMVIEQVKVFQK--IPIYTISFNyNDEIANGFLKELASLTGGEFHF 658
Cdd:COG1240    169 GDALALAlellkrADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAagIRIYTIGVG-TEAVDEGLLREIAEATGGRYFR 247
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 508-659 1.17e-17

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: 81.46  E-value: 1.17e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  508 CIYILIDTSHSM-KSKLDLVKDKIIQFIQEQLKYKRK--FNFVQFDAQAVAWQEKLVEINEDNLRGAQSWIRDiQIGSST 584
Cdd:cd00198      2 DIVFLLDVSGSMgGEKLDKAKEALKALVSSLSASPPGdrVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKK-GLGGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  585 NTLHALQIAFA-------DKETQVIYLLTDGRPDQPPEMVIEQVKVFQKIPIYTISFNYNDEIANGFLKELASLTGGeFH 657
Cdd:cd00198     81 NIGAALRLALEllksakrPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIADKTTG-GA 159


                   ..
gi 1952959430  658 FY 659
Cdd:cd00198    160 VF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 509-661 4.37e-14

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: 71.72  E-value: 4.37e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430   509 IYILIDTSHSM-KSKLDLVKDKIIQFIQEQLKYKRK--FNFVQFDAQAVAWQEKLVEINEDNLRGAqswIRDIQI--GSS 583
Cdd:smart00327    2 VVFLLDGSGSMgGNRFELAKEFVLKLVEQLDIGPDGdrVGLVTFSDDARVLFPLNDSRSKDALLEA---LASLSYklGGG 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430   584 TNTLHALQIAFA----------DKETQVIYLLTDGRPDQPPEMVIEQVKVFQKIPIYTISFNYNDEIANGFLKELASLTG 653
Cdd:smart00327   79 TNLGAALQYALEnlfsksagsrRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPG 158


                    ....*...
gi 1952959430   654 GEFHFYNF 661
Cdd:smart00327  159 GVYVFLPE 166
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 511-658 6.12e-13

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 70.90  E-value: 6.12e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  511 ILIDTSHSMK-SKLDLVKDKIIQFIqEQLKYKRKFNFVQFDAQAvawqEKLVE-INEDNLRGAQSWIRDIQIGSSTNTLH 588
Cdd:COG2304     96 FVIDVSGSMSgDKLELAKEAAKLLV-DQLRPGDRVSIVTFAGDA----RVLLPpTPATDRAKILAAIDRLQAGGGTALGA 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  589 ALQIAFA--------DKETQVIyLLTDGRPD---QPPEMVIEQVKVFQK--IPIYTISF--NYNDEiangFLKELASLTG 653
Cdd:COG2304    171 GLELAYElarkhfipGRVNRVI-LLTDGDANvgiTDPEELLKLAEEAREegITLTTLGVgsDYNED----LLERLADAGG 245


                   ....*
gi 1952959430  654 GEFHF 658
Cdd:COG2304    246 GNYYY 250
VWA_3 pfam13768
von Willebrand factor type A domain;
509-658 1.53e-12

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 66.65  E-value: 1.53e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  509 IYILIDTSHSMKSKLDLVKDKIIQFIQeQLKYKRKFNFVQFDAQAVAWQEKLVEINEDNLRGAQSWIRDIQIGSS-TNTL 587
Cdd:pfam13768    3 VVIVVDVSSSMSGEPKLQKDALSVALR-QLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPLGgSDLL 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952959430  588 HALQIAFA--DKETQV--IYLLTDGRPDQPPEMVIEQV-KVFQKIPIYTISFnyNDEIANGFLKELASLTGGEFHF 658
Cdd:pfam13768   82 GALKEAVRapASPGYIrhVLLLTDGSPMQGETRVSDLIsRAPGKIRFFAYGL--GASISAPMLQLLAEASNGTYEF 155
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 509-649 1.91e-11

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 65.86  E-value: 1.91e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  509 IYILIDTSHSMK-SKLDLVKDKIIQFIQEQLKyKRKFNFVQFDAQAVawqEKLVEINEDNLRGAQSWIRDIQIGSSTNTL 587
Cdd:COG2425    121 VVLCVDTSGSMAgSKEAAAKAAALALLRALRP-NRRFGVILFDTEVV---EDLPLTADDGLEDAIEFLSGLFAGGGTDIA 196

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952959430  588 HALQIAFADKETQ-----VIYLLTDGRPDQPPEMVIEQVK-VFQKIPIYTISFnyNDEIANGFLKELA 649
Cdd:COG2425    197 PALRAALELLEEPdyrnaDIVLITDGEAGVSPEELLREVRaKESGVRLFTVAI--GDAGNPGLLEALA 262
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 512-658 3.52e-11

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: 63.00  E-value: 3.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  512 LIDTSHSMKS-KLDLVKDKIIQFIQEqLKYKRKFNFVQFDAQAVAWQEKLVEINEDNLRGAQSWIRDIQIGSSTNTLHAL 590
Cdd:cd01461      8 VIDTSGSMSGtKIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGTNMNDAL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  591 QIAFADKET-----QVIYLLTDG---RPDQPPEMVIEQVKvfQKIPIYTISF----NYNdeiangFLKELASLTGGEFHF 658
Cdd:cd01461     87 EAALELLNSspgsvPQIILLTDGevtNESQILKNVREALS--GRIRLFTFGIgsdvNTY------LLERLAREGRGIARR 158
VWA pfam00092
von Willebrand factor type A domain;
509-661 2.32e-10

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 60.75  E-value: 2.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  509 IYILIDTSHSM-KSKLDLVKDKIIQFIQEQLKYKRKFNF--VQFDAQAVawqeklVEI--NEDNLRGA-QSWIRDIQI-- 580
Cdd:pfam00092    2 IVFLLDGSGSIgGDNFEKVKEFLKKLVESLDIGPDGTRVglVQYSSDVR------TEFplNDYSSKEElLSAVDNLRYlg 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  581 GSSTNT----LHALQIAFADKE------TQVIYLLTDGRP-DQPPEMVIEQVKVfQKIPIYTISFNyNDEIANgfLKELA 649
Cdd:pfam00092   76 GGTTNTgkalKYALENLFSSAAgarpgaPKVVVLLTDGRSqDGDPEEVARELKS-AGVTVFAVGVG-NADDEE--LRKIA 151

                          170
                   ....*....|..
gi 1952959430  650 SlTGGEFHFYNF 661
Cdd:pfam00092  152 S-EPGEGHVFTV 162
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 509-659 3.58e-05

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: 45.36  E-value: 3.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  509 IYILIDTSHSM-KSKLDLVKDKIIQFIQEQLKYKRK--FNFVQFDAQAVAWqeklVEINEDNLRGA-QSWIRDIQI--GS 582
Cdd:cd01450      3 IVFLLDGSESVgPENFEKVKDFIEKLVEKLDIGPDKtrVGLVQYSDDVRVE----FSLNDYKSKDDlLKAVKNLKYlgGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  583 STNTLHALQIAFA---------DKETQVIYLLTDGRPD---QPPEMVIEQVKvfQKIPIYTISFNYNDEianGFLKELAS 650
Cdd:cd01450     79 GTNTGKALQYALEqlfsesnarENVPKVIIVLTDGRSDdggDPKEAAAKLKD--EGIKVFVVGVGPADE---EELREIAS 153


                   ....*....
gi 1952959430  651 lTGGEFHFY 659
Cdd:cd01450    154 -CPSERHVF 161
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 512-658 1.98e-04

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: 43.15  E-value: 1.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  512 LIDTSHSMKS-KLDLVKDKIiQFIQEQLKYKRKFNFVQFDAQAVAWQeKLVEINEDNLRGAQSWIRDIQIGSSTNTLHAL 590
Cdd:cd01466      6 VLDVSGSMAGdKLQLVKHAL-RFVISSLGDADRLSIVTFSTSAKRLS-PLRRMTAKGKRSAKRVVDGLQAGGGTNVVGGL 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952959430  591 QIAFA---DKETQ----VIYLLTDGRpDQPPEMVIEQvkvfQKIPIYTISFNYNDEIANGFLKELASLTGGEFHF 658
Cdd:cd01466     84 KKALKvlgDRRQKnpvaSIMLLSDGQ-DNHGAVVLRA----DNAPIPIHTFGLGASHDPALLAFIAEITGGTFSY 153
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 511-660 2.82e-04

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 44.61  E-value: 2.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  511 ILIDTSHSMKSKLDLVKDKIIQFIQEQLKYKRKFNFVQFDAQAVAWQE---------------KLVEINEDNLRGAQSWI 575
Cdd:TIGR03436   58 LVIDTSGSMRNDLDRARAAAIRFLKTVLRPNDRVFVVTFNTRLRLLQDftsdprlleaalnrlKPPLRTDYNSSGAFVRD 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  576 RDIQIGSSTNTLHALQIAFADKETQ----VIYLLTDG---RPDQPPEMVIEQVkvfQK--IPIYTISF---------NYN 637
Cdd:TIGR03436  138 GGGTALYDAITLAALEQLANALAGIpgrkALIVISDGgdnRSRDTLERAIDAA---QRadVAIYSIDArglrapdlgAGA 214

                          170       180
                   ....*....|....*....|....*
gi 1952959430  638 DEIANG--FLKELASLTGGEFHFYN 660
Cdd:TIGR03436  215 KAGLGGpeALERLAEETGGRAFYVN 239
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
509-622 3.80e-04

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 42.99  E-value: 3.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  509 IYILIDTSHSMK-SKLDLVKDKIIQFIQEQLKYKR-----KFNFVQFDAQAvAWQEKLVEIneDNLRgaqswIRDIQIGS 582
Cdd:COG4245      8 VYLLLDTSGSMSgEPIEALNEGLQALIDELRQDPYaletvEVSVITFDGEA-KVLLPLTDL--EDFQ-----PPDLSASG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1952959430  583 STNTLHALQ--IAFADKETQ------------VIYLLTDGRP-DQPPEMVIEQVK 622
Cdd:COG4245     80 GTPLGAALEllLDLIERRVQkytaegkgdwrpVVFLITDGEPtDSDWEAALQRLK 134
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 509-659 7.98e-04

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 42.27  E-value: 7.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  509 IYILIDTSHSM-KSKLDLVKDKIIQFIQEQLKYKRKFNF--VQFDAQAVAWQeKLVEINEDNLRGAQSWIRDIQI----- 580
Cdd:cd01470      3 IYIALDASDSIgEEDFDEAKNAIKTLIEKISSYEVSPRYeiISYASDPKEIV-SIRDFNSNDADDVIKRLEDFNYddhgd 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  581 GSSTNTLHALQIAF------------ADKETQ-VIYLLTDGRPDQ--PPEMVIEQVKVFQKIPIYTIS----------FN 635
Cdd:cd01470     82 KTGTNTAAALKKVYermalekvrnkeAFNETRhVIILFTDGKSNMggSPLPTVDKIKNLVYKNNKSDNpredyldvyvFG 161

                          170       180
                   ....*....|....*....|....
gi 1952959430  636 YNDEIANGFLKELASLTGGEFHFY 659
Cdd:cd01470    162 VGDDVNKEELNDLASKKDNERHFF 185
VWA_2 pfam13519
von Willebrand factor type A domain;
509-618 3.43e-03

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 38.43  E-value: 3.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  509 IYILIDTSHSM------KSKLDLVKDKIIQFIQeQLKyKRKFNFVQFDAQAvawqEKLVEINEDNlRGAQSWIRDIQIGS 582
Cdd:pfam13519    1 LVFVLDTSGSMrngdygPTRLEAAKDAVLALLK-SLP-GDRVGLVTFGDGP----EVLIPLTKDR-AKILRALRRLEPKG 73

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1952959430  583 -STNTLHALQIAFAdketqviyLLTDGRPDQPPEMVI 618
Cdd:pfam13519   74 gGTNLAAALQLARA--------ALKHRRKNQPRRIVL 102
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 512-659 5.16e-03

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: 39.18  E-value: 5.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  512 LIDTSHSMKS-KLDLVKDKIIQFIqEQLKYKRKFNFVQFD--------AQAVAWQEKLVEInednlrgaqswIRDIQIGS 582
Cdd:cd01465      6 VIDRSGSMDGpKLPLVKSALKLLV-DQLRPDDRLAIVTYDgaaetvlpATPVRDKAAILAA-----------IDRLTAGG 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952959430  583 STNTLHALQIA-------FADKETQVIYLLTDGRP---DQPPEMVIEQV--KVFQKIPIYTISF--NYNDEiangfLKEL 648
Cdd:cd01465     74 STAGGAGIQLGyqeaqkhFVPGGVNRILLATDGDFnvgETDPDELARLVaqKRESGITLSTLGFgdNYNED-----LMEA 148

                          170
                   ....*....|.
gi 1952959430  649 ASLTGGEFHFY 659
Cdd:cd01465    149 IADAGNGNTAY 159
 
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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