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Conserved domains on  [gi|578803901|ref|XP_006712422|]
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von Willebrand factor A domain-containing protein 3B isoform X9 [Homo sapiens]

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 ...
 556-682 1.23e-43

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: 153.62  E-value: 1.23e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901  556 GQKVIARCDENGFYFPGVVKKCVSRTQALVGFSYGDTKVVSTSFITPVGGAMpCPLLQVGDYVFAKiVIPKGFDfYVPAI 635
Cdd:pfam15057   1 GQRVLARWDEDGFYYRGTVKKYLNGGQYLVEFDAGDRQVVLTRDIIALEDAM-EHPLRVGDKVLAL-HDPYSQS-YAPGI 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 578803901  636 VIALPNKHVATEKFYTVLKCNNRREFCPRSALIKISQNKYALSCSHI 682
Cdd:pfam15057  78 VLAGPERRVDADEELTVRFYDGKTATVPREEVYKLSQAYYEKAVAYI 124
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 28-177 9.28e-20

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: 90.00  E-value: 9.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901  28 IYILIDTSHSM--KSKLDLVKDKIIQFIQEQLKyKSKFNFVKFDGQAvawrEQLAEVNEDnLEQAQSWIRDIKIGSSTNT 105
Cdd:COG1240   95 VVLVVDASGSMaaENRLEAAKGALLDFLDDYRP-RDRVGLVAFGGEA----EVLLPLTRD-REALKRALDELPPGGGTPL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901 106 LSALKTA------FADKETQAIYLLTDGRPDQPPETVIDQVKRFQE--IPIYTISFNyNDEIANRFLKEVAALTGGEFHF 177
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 ...
 556-682 1.23e-43

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: 153.62  E-value: 1.23e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901  556 GQKVIARCDENGFYFPGVVKKCVSRTQALVGFSYGDTKVVSTSFITPVGGAMpCPLLQVGDYVFAKiVIPKGFDfYVPAI 635
Cdd:pfam15057   1 GQRVLARWDEDGFYYRGTVKKYLNGGQYLVEFDAGDRQVVLTRDIIALEDAM-EHPLRVGDKVLAL-HDPYSQS-YAPGI 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 578803901  636 VIALPNKHVATEKFYTVLKCNNRREFCPRSALIKISQNKYALSCSHI 682
Cdd:pfam15057  78 VLAGPERRVDADEELTVRFYDGKTATVPREEVYKLSQAYYEKAVAYI 124
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 28-177 9.28e-20

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: 90.00  E-value: 9.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901  28 IYILIDTSHSM--KSKLDLVKDKIIQFIQEQLKyKSKFNFVKFDGQAvawrEQLAEVNEDnLEQAQSWIRDIKIGSSTNT 105
Cdd:COG1240   95 VVLVVDASGSMaaENRLEAAKGALLDFLDDYRP-RDRVGLVAFGGEA----EVLLPLTRD-REALKRALDELPPGGGTPL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901 106 LSALKTA------FADKETQAIYLLTDGRPDQPPETVIDQVKRFQE--IPIYTISFNyNDEIANRFLKEVAALTGGEFHF 177
Cdd:COG1240  169 GDALALAlellkrADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAagIRIYTIGVG-TEAVDEGLLREIAEATGGRYFR 247
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 27-178 2.51e-19

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: 85.70  E-value: 2.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901  27 CIYILIDTSHSM-KSKLDLVKDKIIQFIQ--EQLKYKSKFNFVKFDGQAVAWREQLAEVNEDNLEQAQSWIRDiKIGSST 103
Cdd:cd00198    2 DIVFLLDVSGSMgGEKLDKAKEALKALVSslSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKK-GLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901 104 NTLSALKTAFA-------DKETQAIYLLTDGRPDQPPETVIDQVKRFQEIPIYTISFNYNDEIANRFLKEVAALTGGeFH 176
Cdd:cd00198   81 NIGAALRLALEllksakrPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIADKTTG-GA 159


                 ..
gi 578803901 177 FY 178
Cdd:cd00198  160 VF 161
VWA_3 pfam13768
von Willebrand factor type A domain;
28-177 1.73e-14

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 71.66  E-value: 1.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901   28 IYILIDTSHSMKSKLDLVKDKIIQFIQeQLKYKSKFNFVKFDGQAVAWREQLAEVNEDNLEQAQSWIRDIKIGSS-TNTL 106
Cdd:pfam13768   3 VVIVVDVSSSMSGEPKLQKDALSVALR-QLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPLGgSDLL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803901  107 SALKTAFADKETQA----IYLLTDGRPDQPPETVIDQVKRFQE-IPIYTISFnyNDEIANRFLKEVAALTGGEFHF 177
Cdd:pfam13768  82 GALKEAVRAPASPGyirhVLLLTDGSPMQGETRVSDLISRAPGkIRFFAYGL--GASISAPMLQLLAEASNGTYEF 155
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 28-180 4.23e-11

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: 62.47  E-value: 4.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901    28 IYILIDTSHSM-KSKLDLVKDKIIQFIQ--EQLKYKSKFNFVKFDGQAvawREQLAEVNEDNLEQAQSWIRDIKI--GSS 102
Cdd:smart00327   2 VVFLLDGSGSMgGNRFELAKEFVLKLVEqlDIGPDGDRVGLVTFSDDA---RVLFPLNDSRSKDALLEALASLSYklGGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901   103 TNTLSALKTAFA----------DKETQAIYLLTDGRPDQPPETVIDQVKRFQEIPIYTISFNYNDEIANRFLKEVAALTG 172
Cdd:smart00327  79 TNLGAALQYALEnlfsksagsrRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPG 158


                   ....*...
gi 578803901   173 GEFHFYNF 180
Cdd:smart00327 159 GVYVFLPE 166
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 30-179 5.59e-05

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: 45.76  E-value: 5.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901   30 ILIDTSHSMKSKLDLVKDKIIQFIQEQLKYKSKFNFVKFDGQAV------AWREQLaevnEDNLEQAQSWIRDIKIGSST 103
Cdd:TIGR03436  58 LVIDTSGSMRNDLDRARAAAIRFLKTVLRPNDRVFVVTFNTRLRllqdftSDPRLL----EAALNRLKPPLRTDYNSSGA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901  104 NTLSALKTAFADketqAIYL---------------------LTDG---RPDQPPETVIDQVKRfQEIPIYTISF---NYN 156
Cdd:TIGR03436 134 FVRDGGGTALYD----AITLaaleqlanalagipgrkalivISDGgdnRSRDTLERAIDAAQR-ADVAIYSIDArglRAP 208

                         170       180       190
                  ....*....|....*....|....*....|.
gi 578803901  157 DEIANR--------FLKEVAALTGGEFHFYN 179
Cdd:TIGR03436 209 DLGAGAkaglggpeALERLAEETGGRAFYVN 239
Tudor_53BP1 cd20383
Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; ...
 556-596 2.20e-03

Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; 53BP1, also called p53-binding protein 1 (p53BP1), is a double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics, and class-switch recombination (CSR) during antibody genesis. It plays a key role in the repair of DSBs in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1. It is recruited to DSB sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSB sites. 53BP1 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410454  Cd Length: 52  Bit Score: 36.86  E-value: 2.20e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 578803901 556 GQKVIARCDENGFYFPGVVKKCVSRTQALVGFSYGDTKVVS 596
Cdd:cd20383    2 GTRVFAKWSSDGYYYPGIITRVLGDGKYKVLFDDGYERDVK 42
 
Name Accession Description Interval E-value
DUF4537 pfam15057
Domain of unknown function (DUF4537); The function of this domain family is unknown. It is ...
 556-682 1.23e-43

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: 153.62  E-value: 1.23e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901  556 GQKVIARCDENGFYFPGVVKKCVSRTQALVGFSYGDTKVVSTSFITPVGGAMpCPLLQVGDYVFAKiVIPKGFDfYVPAI 635
Cdd:pfam15057   1 GQRVLARWDEDGFYYRGTVKKYLNGGQYLVEFDAGDRQVVLTRDIIALEDAM-EHPLRVGDKVLAL-HDPYSQS-YAPGI 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 578803901  636 VIALPNKHVATEKFYTVLKCNNRREFCPRSALIKISQNKYALSCSHI 682
Cdd:pfam15057  78 VLAGPERRVDADEELTVRFYDGKTATVPREEVYKLSQAYYEKAVAYI 124
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 28-177 9.28e-20

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: 90.00  E-value: 9.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901  28 IYILIDTSHSM--KSKLDLVKDKIIQFIQEQLKyKSKFNFVKFDGQAvawrEQLAEVNEDnLEQAQSWIRDIKIGSSTNT 105
Cdd:COG1240   95 VVLVVDASGSMaaENRLEAAKGALLDFLDDYRP-RDRVGLVAFGGEA----EVLLPLTRD-REALKRALDELPPGGGTPL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901 106 LSALKTA------FADKETQAIYLLTDGRPDQPPETVIDQVKRFQE--IPIYTISFNyNDEIANRFLKEVAALTGGEFHF 177
Cdd:COG1240  169 GDALALAlellkrADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAagIRIYTIGVG-TEAVDEGLLREIAEATGGRYFR 247
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 27-178 2.51e-19

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: 85.70  E-value: 2.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901  27 CIYILIDTSHSM-KSKLDLVKDKIIQFIQ--EQLKYKSKFNFVKFDGQAVAWREQLAEVNEDNLEQAQSWIRDiKIGSST 103
Cdd:cd00198    2 DIVFLLDVSGSMgGEKLDKAKEALKALVSslSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKK-GLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901 104 NTLSALKTAFA-------DKETQAIYLLTDGRPDQPPETVIDQVKRFQEIPIYTISFNYNDEIANRFLKEVAALTGGeFH 176
Cdd:cd00198   81 NIGAALRLALEllksakrPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANEDELKEIADKTTG-GA 159


                 ..
gi 578803901 177 FY 178
Cdd:cd00198  160 VF 161
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 30-177 5.82e-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: 82.07  E-value: 5.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901  30 ILIDTSHSMK-SKLDLVKDKIIQFIqEQLKYKSKFNFVKFDGQAvawREQLAEVNEDNLEQAQSWIRDIKIGSSTNTLSA 108
Cdd:COG2304   96 FVIDVSGSMSgDKLELAKEAAKLLV-DQLRPGDRVSIVTFAGDA---RVLLPPTPATDRAKILAAIDRLQAGGGTALGAG 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901 109 LKTA-------FADKETQAIYLLTDGRPD---QPPETVIDQVKRFQE--IPIYTISF--NYNDEianrFLKEVAALTGGE 174
Cdd:COG2304  172 LELAyelarkhFIPGRVNRVILLTDGDANvgiTDPEELLKLAEEAREegITLTTLGVgsDYNED----LLERLADAGGGN 247


                 ...
gi 578803901 175 FHF 177
Cdd:COG2304  248 YYY 250
VWA_3 pfam13768
von Willebrand factor type A domain;
28-177 1.73e-14

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 71.66  E-value: 1.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901   28 IYILIDTSHSMKSKLDLVKDKIIQFIQeQLKYKSKFNFVKFDGQAVAWREQLAEVNEDNLEQAQSWIRDIKIGSS-TNTL 106
Cdd:pfam13768   3 VVIVVDVSSSMSGEPKLQKDALSVALR-QLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPLGgSDLL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803901  107 SALKTAFADKETQA----IYLLTDGRPDQPPETVIDQVKRFQE-IPIYTISFnyNDEIANRFLKEVAALTGGEFHF 177
Cdd:pfam13768  82 GALKEAVRAPASPGyirhVLLLTDGSPMQGETRVSDLISRAPGkIRFFAYGL--GASISAPMLQLLAEASNGTYEF 155
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 31-176 3.78e-12

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: 65.31  E-value: 3.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901  31 LIDTSHSMKS-KLDLVKDKIIQFIQEqLKYKSKFNFVKFDGQAVAWREQLAEVNEDNLEQAQSWIRDIKIGSSTNTLSAL 109
Cdd:cd01461    8 VIDTSGSMSGtKIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGTNMNDAL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803901 110 KTAFADKET-----QAIYLLTDGRPDQpPETVIDQVKRF--QEIPIYTISFNyNDeiANRFLKEVAALTGGEFH 176
Cdd:cd01461   87 EAALELLNSspgsvPQIILLTDGEVTN-ESQILKNVREAlsGRIRLFTFGIG-SD--VNTYLLERLAREGRGIA 156
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 28-168 5.42e-12

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 67.01  E-value: 5.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901  28 IYILIDTSHSMK-SKLDLVKDKIIQFIQEQLKyKSKFNFVKFDGQAVawrEQLAEVNEDNLEQAQSWIRDIKIGSSTNTL 106
Cdd:COG2425  121 VVLCVDTSGSMAgSKEAAAKAAALALLRALRP-NRRFGVILFDTEVV---EDLPLTADDGLEDAIEFLSGLFAGGGTDIA 196

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803901 107 SALKTAFADKETQA-----IYLLTDGRPDQPPETVIDQVK-RFQEIPIYTISFnyNDEIANRFLKEVA 168
Cdd:COG2425  197 PALRAALELLEEPDyrnadIVLITDGEAGVSPEELLREVRaKESGVRLFTVAI--GDAGNPGLLEALA 262
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 28-180 4.23e-11

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: 62.47  E-value: 4.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901    28 IYILIDTSHSM-KSKLDLVKDKIIQFIQ--EQLKYKSKFNFVKFDGQAvawREQLAEVNEDNLEQAQSWIRDIKI--GSS 102
Cdd:smart00327   2 VVFLLDGSGSMgGNRFELAKEFVLKLVEqlDIGPDGDRVGLVTFSDDA---RVLFPLNDSRSKDALLEALASLSYklGGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901   103 TNTLSALKTAFA----------DKETQAIYLLTDGRPDQPPETVIDQVKRFQEIPIYTISFNYNDEIANRFLKEVAALTG 172
Cdd:smart00327  79 TNLGAALQYALEnlfsksagsrRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPG 158


                   ....*...
gi 578803901   173 GEFHFYNF 180
Cdd:smart00327 159 GVYVFLPE 166
VWA pfam00092
von Willebrand factor type A domain;
28-180 1.57e-10

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 60.75  E-value: 1.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901   28 IYILIDTSHSM-KSKLDLVKDKIIQFIQ--EQLKYKSKFNFVKFDGQAvawrEQLAEVNED-NLEQAQSWIRDIKI--GS 101
Cdd:pfam00092   2 IVFLLDGSGSIgGDNFEKVKEFLKKLVEslDIGPDGTRVGLVQYSSDV----RTEFPLNDYsSKEELLSAVDNLRYlgGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901  102 STNTLSALKTA----FADKE------TQAIYLLTDGRP-DQPPETVIDQVKRFQeIPIYTISFNYNDeiaNRFLKEVaAL 170
Cdd:pfam00092  78 TTNTGKALKYAlenlFSSAAgarpgaPKVVVLLTDGRSqDGDPEEVARELKSAG-VTVFAVGVGNAD---DEELRKI-AS 152

                         170
                  ....*....|
gi 578803901  171 TGGEFHFYNF 180
Cdd:pfam00092 153 EPGEGHVFTV 162
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
22-151 2.05e-06

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 49.15  E-value: 2.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901  22 RLHndcIYILIDTSHSMK-SKLDLVKDKIIQFIQEQLKYKS-----KFNFVKFDGQAvawrEQLAEVNEdnLEQAQswIR 95
Cdd:COG4245    5 RLP---VYLLLDTSGSMSgEPIEALNEGLQALIDELRQDPYaletvEVSVITFDGEA----KVLLPLTD--LEDFQ--PP 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803901  96 DIKIGSSTNTLSALKTAFA--DKETQA------------IYLLTDGRP-DQPPETVIDQVKRFQEIPIYTI 151
Cdd:COG4245   74 DLSASGGTPLGAALELLLDliERRVQKytaegkgdwrpvVFLITDGEPtDSDWEAALQRLKDGEAAKKANI 144
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 31-178 2.15e-06

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: 48.42  E-value: 2.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901  31 LIDTSHSMKS-KLDLVKDKIIQFIqEQLKYKSKFNFVKFDG--------QAVAWREQLAEVnednleqaqswIRDIKIGS 101
Cdd:cd01465    6 VIDRSGSMDGpKLPLVKSALKLLV-DQLRPDDRLAIVTYDGaaetvlpaTPVRDKAAILAA-----------IDRLTAGG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901 102 STNTLSALKTA-------FADKETQAIYLLTDGRP---DQPPETVIDQV--KRFQEIPIYTISF--NYNDEianrfLKEV 167
Cdd:cd01465   74 STAGGAGIQLGyqeaqkhFVPGGVNRILLATDGDFnvgETDPDELARLVaqKRESGITLSTLGFgdNYNED-----LMEA 148

                        170
                 ....*....|.
gi 578803901 168 AALTGGEFHFY 178
Cdd:cd01465  149 IADAGNGNTAY 159
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 28-178 2.42e-05

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: 46.13  E-value: 2.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901  28 IYILIDTSHSM-KSKLDLVKDKIIQFIQEQLKYKSKFNF--VKFDGQAV-------AWREQLAEVNEdNLEQAQSWIRDI 97
Cdd:cd01470    3 IYIALDASDSIgEEDFDEAKNAIKTLIEKISSYEVSPRYeiISYASDPKeivsirdFNSNDADDVIK-RLEDFNYDDHGD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901  98 KIGssTNTLSALKTAF------------ADKETQ-AIYLLTDGRPDQ--PPETVIDQVKRFqeIPIYTIS---------- 152
Cdd:cd01470   82 KTG--TNTAAALKKVYermalekvrnkeAFNETRhVIILFTDGKSNMggSPLPTVDKIKNL--VYKNNKSdnpredyldv 157

                        170       180
                 ....*....|....*....|....*...
gi 578803901 153 --FNYNDEIANRFLKEVAALTGGEFHFY 178
Cdd:cd01470  158 yvFGVGDDVNKEELNDLASKKDNERHFF 185
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 31-177 3.22e-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: 3.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901  31 LIDTSHSMKS-KLDLVKDKIiQFIQEQLKYKSKFNFVKFDGQAvAWREQLAEVNEDNLEQAQSWIRDIKIGSSTNTLSAL 109
Cdd:cd01466    6 VLDVSGSMAGdKLQLVKHAL-RFVISSLGDADRLSIVTFSTSA-KRLSPLRRMTAKGKRSAKRVVDGLQAGGGTNVVGGL 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578803901 110 KTAFA---DKETQ----AIYLLTDGRPDQppetvIDQVKRFQEIPIYTISFNYNDEIANRFLKEVAALTGGEFHF 177
Cdd:cd01466   84 KKALKvlgDRRQKnpvaSIMLLSDGQDNH-----GAVVLRADNAPIPIHTFGLGASHDPALLAFIAEITGGTFSY 153
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 30-179 5.59e-05

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: 45.76  E-value: 5.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901   30 ILIDTSHSMKSKLDLVKDKIIQFIQEQLKYKSKFNFVKFDGQAV------AWREQLaevnEDNLEQAQSWIRDIKIGSST 103
Cdd:TIGR03436  58 LVIDTSGSMRNDLDRARAAAIRFLKTVLRPNDRVFVVTFNTRLRllqdftSDPRLL----EAALNRLKPPLRTDYNSSGA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901  104 NTLSALKTAFADketqAIYL---------------------LTDG---RPDQPPETVIDQVKRfQEIPIYTISF---NYN 156
Cdd:TIGR03436 134 FVRDGGGTALYD----AITLaaleqlanalagipgrkalivISDGgdnRSRDTLERAIDAAQR-ADVAIYSIDArglRAP 208

                         170       180       190
                  ....*....|....*....|....*....|.
gi 578803901  157 DEIANR--------FLKEVAALTGGEFHFYN 179
Cdd:TIGR03436 209 DLGAGAkaglggpeALERLAEETGGRAFYVN 239
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 28-178 3.06e-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: 42.28  E-value: 3.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901  28 IYILIDTSHSM-KSKLDLVKDKIIQFIQ--EQLKYKSKFNFVKFDGQAVAWREQLAEVNEDNLEQAqswIRDIKI--GSS 102
Cdd:cd01450    3 IVFLLDGSESVgPENFEKVKDFIEKLVEklDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKA---VKNLKYlgGGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901 103 TNTLSALKTAFA---------DKETQAIYLLTDGRP--DQPPETVIDQVKRFQeIPIYTISFNYNDEianRFLKEVAAlT 171
Cdd:cd01450   80 TNTGKALQYALEqlfsesnarENVPKVIIVLTDGRSddGGDPKEAAAKLKDEG-IKVFVVGVGPADE---EELREIAS-C 154


                 ....*..
gi 578803901 172 GGEFHFY 178
Cdd:cd01450  155 PSERHVF 161
Tudor_53BP1 cd20383
Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; ...
 556-596 2.20e-03

Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; 53BP1, also called p53-binding protein 1 (p53BP1), is a double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics, and class-switch recombination (CSR) during antibody genesis. It plays a key role in the repair of DSBs in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1. It is recruited to DSB sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSB sites. 53BP1 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410454  Cd Length: 52  Bit Score: 36.86  E-value: 2.20e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 578803901 556 GQKVIARCDENGFYFPGVVKKCVSRTQALVGFSYGDTKVVS 596
Cdd:cd20383    2 GTRVFAKWSSDGYYYPGIITRVLGDGKYKVLFDDGYERDVK 42
VWA_2 pfam13519
von Willebrand factor type A domain;
28-114 7.46e-03

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 36.89  E-value: 7.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803901   28 IYILIDTSHSM------KSKLDLVKDKIIQFIQeQLKyKSKFNFVKFDGQAvawrEQLAEVNEDNlEQAQSWIRDIKIGS 101
Cdd:pfam13519   1 LVFVLDTSGSMrngdygPTRLEAAKDAVLALLK-SLP-GDRVGLVTFGDGP----EVLIPLTKDR-AKILRALRRLEPKG 73

                          90
                  ....*....|....
gi 578803901  102 -STNTLSALKTAFA 114
Cdd:pfam13519  74 gGTNLAAALQLARA 87
 
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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