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Conserved domains on  [gi|767917141|ref|XP_011509077|]
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von Willebrand factor A domain-containing protein 3B isoform X11 [Homo sapiens]

Protein Classification

vWA domain-containing protein( domain architecture ID 10076759)

vWA (von Willebrand factor type A) domain-containing protein may be involved in one of a wide variety of important cellular functions, including basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and immune defenses

CATH:  3.40.50.410
PubMed:  10830113|12388743|12579041
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 508-612 3.67e-13

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: 67.59  E-value: 3.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917141 508 CIYILIDTSHSM-KSKLDLVKDKIIQFIQ--EQLKYKSKFNFVKFDGQAVAWREQLAEVNEDNLEQAQSWIRDiKIGSST 584
Cdd:cd00198    2 DIVFLLDVSGSMgGEKLDKAKEALKALVSslSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKK-GLGGGT 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767917141 585 NTLSALKTAFA-------DKETQAIYLLTDGRPDQ 612
Cdd:cd00198   81 NIGAALRLALEllksakrPNARRVIILLTDGEPND 115
 
Name Accession Description Interval E-value
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 508-612 3.67e-13

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: 67.59  E-value: 3.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917141 508 CIYILIDTSHSM-KSKLDLVKDKIIQFIQ--EQLKYKSKFNFVKFDGQAVAWREQLAEVNEDNLEQAQSWIRDiKIGSST 584
Cdd:cd00198    2 DIVFLLDVSGSMgGEKLDKAKEALKALVSslSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKK-GLGGGT 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767917141 585 NTLSALKTAFA-------DKETQAIYLLTDGRPDQ 612
Cdd:cd00198   81 NIGAALRLALEllksakrPNARRVIILLTDGEPND 115
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 511-610 1.39e-10

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 62.81  E-value: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917141 511 ILIDTSHSMK-SKLDLVKDKIIQFIqEQLKYKSKFNFVKFDGQAvawREQLAEVNEDNLEQAQSWIRDIKIGSSTNTLSA 589
Cdd:COG2304   96 FVIDVSGSMSgDKLELAKEAAKLLV-DQLRPGDRVSIVTFAGDA---RVLLPPTPATDRAKILAAIDRLQAGGGTALGAG 171

                         90       100
                 ....*....|....*....|....*...
gi 767917141 590 LKTA-------FADKETQAIYLLTDGRP 610
Cdd:COG2304  172 LELAyelarkhFIPGRVNRVILLTDGDA 199
VWA_3 pfam13768
von Willebrand factor type A domain;
509-612 4.16e-08

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 52.78  E-value: 4.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917141  509 IYILIDTSHSMKSKLDLVKDKIIQFIQeQLKYKSKFNFVKFDGQAVAWREQLAEVNEDNLEQAQSWIRDIKIGSS-TNTL 587
Cdd:pfam13768   3 VVIVVDVSSSMSGEPKLQKDALSVALR-QLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPLGgSDLL 81

                          90       100
                  ....*....|....*....|....*....
gi 767917141  588 SALKTAFADKETQA----IYLLTDGRPDQ 612
Cdd:pfam13768  82 GALKEAVRAPASPGyirhVLLLTDGSPMQ 110
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 509-611 1.31e-05

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: 45.91  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917141   509 IYILIDTSHSM-KSKLDLVKDKIIQFIQ--EQLKYKSKFNFVKFDGQAvawREQLAEVNEDNLEQAQSWIRDIKI--GSS 583
Cdd:smart00327   2 VVFLLDGSGSMgGNRFELAKEFVLKLVEqlDIGPDGDRVGLVTFSDDA---RVLFPLNDSRSKDALLEALASLSYklGGG 78

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 767917141   584 TNTLSALKTAFA----------DKETQAIYLLTDGRPD 611
Cdd:smart00327  79 TNLGAALQYALEnlfsksagsrRGAPKVVILITDGESN 116
 
Name Accession Description Interval E-value
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 508-612 3.67e-13

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: 67.59  E-value: 3.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917141 508 CIYILIDTSHSM-KSKLDLVKDKIIQFIQ--EQLKYKSKFNFVKFDGQAVAWREQLAEVNEDNLEQAQSWIRDiKIGSST 584
Cdd:cd00198    2 DIVFLLDVSGSMgGEKLDKAKEALKALVSslSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKK-GLGGGT 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767917141 585 NTLSALKTAFA-------DKETQAIYLLTDGRPDQ 612
Cdd:cd00198   81 NIGAALRLALEllksakrPNARRVIILLTDGEPND 115
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 512-608 2.17e-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: 62.62  E-value: 2.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917141 512 LIDTSHSMKS-KLDLVKDKIIQFIQEqLKYKSKFNFVKFDGQAVAWREQLAEVNEDNLEQAQSWIRDIKIGSSTNTLSAL 590
Cdd:cd01461    8 VIDTSGSMSGtKIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGTNMNDAL 86

                         90       100
                 ....*....|....*....|...
gi 767917141 591 KTAFADKET-----QAIYLLTDG 608
Cdd:cd01461   87 EAALELLNSspgsvPQIILLTDG 109
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 511-610 1.39e-10

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 62.81  E-value: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917141 511 ILIDTSHSMK-SKLDLVKDKIIQFIqEQLKYKSKFNFVKFDGQAvawREQLAEVNEDNLEQAQSWIRDIKIGSSTNTLSA 589
Cdd:COG2304   96 FVIDVSGSMSgDKLELAKEAAKLLV-DQLRPGDRVSIVTFAGDA---RVLLPPTPATDRAKILAAIDRLQAGGGTALGAG 171

                         90       100
                 ....*....|....*....|....*...
gi 767917141 590 LKTA-------FADKETQAIYLLTDGRP 610
Cdd:COG2304  172 LELAyelarkhFIPGRVNRVILLTDGDA 199
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 509-610 3.37e-10

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: 61.11  E-value: 3.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917141 509 IYILIDTSHSM--KSKLDLVKDKIIQFIQEQLKyKSKFNFVKFDGQAvawrEQLAEVNEDnLEQAQSWIRDIKIGSSTNT 586
Cdd:COG1240   95 VVLVVDASGSMaaENRLEAAKGALLDFLDDYRP-RDRVGLVAFGGEA----EVLLPLTRD-REALKRALDELPPGGGTPL 168

                         90       100       110
                 ....*....|....*....|....*....|
gi 767917141 587 LSALKTA------FADKETQAIYLLTDGRP 610
Cdd:COG1240  169 GDALALAlellkrADPARRKVIVLLTDGRD 198
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 509-608 1.01e-08

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 56.61  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917141 509 IYILIDTSHSMK-SKLDLVKDKIIQFIQEQLKyKSKFNFVKFDGQAVawrEQLAEVNEDNLEQAQSWIRDIKIGSSTNTL 587
Cdd:COG2425  121 VVLCVDTSGSMAgSKEAAAKAAALALLRALRP-NRRFGVILFDTEVV---EDLPLTADDGLEDAIEFLSGLFAGGGTDIA 196

                         90       100
                 ....*....|....*....|....*.
gi 767917141 588 SALKTAFADKETQA-----IYLLTDG 608
Cdd:COG2425  197 PALRAALELLEEPDyrnadIVLITDG 222
VWA_3 pfam13768
von Willebrand factor type A domain;
509-612 4.16e-08

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 52.78  E-value: 4.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917141  509 IYILIDTSHSMKSKLDLVKDKIIQFIQeQLKYKSKFNFVKFDGQAVAWREQLAEVNEDNLEQAQSWIRDIKIGSS-TNTL 587
Cdd:pfam13768   3 VVIVVDVSSSMSGEPKLQKDALSVALR-QLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPLGgSDLL 81

                          90       100
                  ....*....|....*....|....*....
gi 767917141  588 SALKTAFADKETQA----IYLLTDGRPDQ 612
Cdd:pfam13768  82 GALKEAVRAPASPGyirhVLLLTDGSPMQ 110
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 509-611 1.31e-05

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: 45.91  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917141   509 IYILIDTSHSM-KSKLDLVKDKIIQFIQ--EQLKYKSKFNFVKFDGQAvawREQLAEVNEDNLEQAQSWIRDIKI--GSS 583
Cdd:smart00327   2 VVFLLDGSGSMgGNRFELAKEFVLKLVEqlDIGPDGDRVGLVTFSDDA---RVLFPLNDSRSKDALLEALASLSYklGGG 78

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 767917141   584 TNTLSALKTAFA----------DKETQAIYLLTDGRPD 611
Cdd:smart00327  79 TNLGAALQYALEnlfsksagsrRGAPKVVILITDGESN 116
VWA pfam00092
von Willebrand factor type A domain;
509-611 2.60e-05

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 45.34  E-value: 2.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917141  509 IYILIDTSHSM-KSKLDLVKDKIIQFIQ--EQLKYKSKFNFVKFDGQAvawrEQLAEVNED-NLEQAQSWIRDIKI--GS 582
Cdd:pfam00092   2 IVFLLDGSGSIgGDNFEKVKEFLKKLVEslDIGPDGTRVGLVQYSSDV----RTEFPLNDYsSKEELLSAVDNLRYlgGG 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767917141  583 STNTLSALKTA----FADKE------TQAIYLLTDGRPD 611
Cdd:pfam00092  78 TTNTGKALKYAlenlFSSAAgarpgaPKVVVLLTDGRSQ 116
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
503-610 4.90e-05

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 44.53  E-value: 4.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917141 503 RLHndcIYILIDTSHSMK-SKLDLVKDKIIQFIQEQLKYKS-----KFNFVKFDGQAvawrEQLAEVNEdnLEQAQswIR 576
Cdd:COG4245    5 RLP---VYLLLDTSGSMSgEPIEALNEGLQALIDELRQDPYaletvEVSVITFDGEA----KVLLPLTD--LEDFQ--PP 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767917141 577 DIKIGSSTNTLSALKTAFA--DKETQA------------IYLLTDGRP 610
Cdd:COG4245   74 DLSASGGTPLGAALELLLDliERRVQKytaegkgdwrpvVFLITDGEP 121
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 512-610 1.01e-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: 40.33  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917141 512 LIDTSHSMKS-KLDLVKDKIIQFIqEQLKYKSKFNFVKFDG--------QAVAWREQLAEVnednleqaqswIRDIKIGS 582
Cdd:cd01465    6 VIDRSGSMDGpKLPLVKSALKLLV-DQLRPDDRLAIVTYDGaaetvlpaTPVRDKAAILAA-----------IDRLTAGG 73

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767917141 583 STNTLSALKTA-------FADKETQAIYLLTDGRP 610
Cdd:cd01465   74 STAGGAGIQLGyqeaqkhFVPGGVNRILLATDGDF 108
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 509-641 1.35e-03

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: 40.35  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917141 509 IYILIDTSHSM-KSKLDLVKDKIIQFIQEQLKYKSKFNF--VKFDGQAV-------AWREQLAEVNEdNLEQAQSWIRDI 578
Cdd:cd01470    3 IYIALDASDSIgEEDFDEAKNAIKTLIEKISSYEVSPRYeiISYASDPKeivsirdFNSNDADDVIK-RLEDFNYDDHGD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767917141 579 KIGssTNTLSALKTAF------------ADKETQ-AIYLLTDGRPDQVPShgyPITYLAsplQIRSRIVFELSDLH 641
Cdd:cd01470   82 KTG--TNTAAALKKVYermalekvrnkeAFNETRhVIILFTDGKSNMGGS---PLPTVD---KIKNLVYKNNKSDN 149
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 509-611 2.09e-03

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: 39.20  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917141 509 IYILIDTSHSM-KSKLDLVKDKIIQFIQ--EQLKYKSKFNFVKFDGQAVAWREQLAEVNEDNLEQAqswIRDIKI--GSS 583
Cdd:cd01450    3 IVFLLDGSESVgPENFEKVKDFIEKLVEklDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKA---VKNLKYlgGGG 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767917141 584 TNTLSALKTAFA---------DKETQAIYLLTDGRPD 611
Cdd:cd01450   80 TNTGKALQYALEqlfsesnarENVPKVIIVLTDGRSD 116
VWA_2 pfam13519
von Willebrand factor type A domain;
509-595 5.79e-03

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 36.89  E-value: 5.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917141  509 IYILIDTSHSM------KSKLDLVKDKIIQFIQeQLKyKSKFNFVKFDGQAvawrEQLAEVNEDNlEQAQSWIRDIKIGS 582
Cdd:pfam13519   1 LVFVLDTSGSMrngdygPTRLEAAKDAVLALLK-SLP-GDRVGLVTFGDGP----EVLIPLTKDR-AKILRALRRLEPKG 73

                          90
                  ....*....|....
gi 767917141  583 -STNTLSALKTAFA 595
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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