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Conserved domains on  [gi|1718691803|ref|WP_145084897|]
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von Willebrand factor type A domain-containing protein [Aureliella helgolandensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 427-741 4.58e-86

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


:

Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 276.98  E-value: 4.58e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 427 ENAFQRVDDAPLSTLSIDVDTASFVKARqLLLEAGRLPPPDAVRIEEFINYFEYEYAGPHGDdpfgadlaVANCPWAPEH 506
Cdd:COG2304     2 EAGFAAADTVPLSTSSADVDAASSSNRR-RLLVGGEPPPAAAVRLEELVNFFPYDYPLPTGR--------LAQSPWNPQT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 507 KLVRIALQATKVDLAERPKANIVFLLDVSGSMDEpNKLPLVKESIRMLVEQLGENDRVAMVVYAGAAGCVLESTRGDQQE 586
Cdd:COG2304    73 RLLLVGLQPPKAAAEERPPLNLVFVIDVSGSMSG-DKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPPTPATDRA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 587 EILGALQKLSAGGSTNGGQGIELAYNLARDHFIPGGINRVVLCTDGDFNVGVTSTNSLVELVEENAKGNTFLTVLGFGMg 666
Cdd:COG2304   152 KILAAIDRLQAGGGTALGAGLELAYELARKHFIPGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGS- 230

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1718691803 667 NTNDAMMEQISNRGNGVYGFVDSRREAHRQMVRqlagnlmtvakdvkiqvefnptkvqEYRLLGYENRIMAAADF 741
Cdd:COG2304   231 DYNEDLLERLADAGGGNYYYIDDPEEAEKVFVR-------------------------EFSRIGYENRALATEDF 280
DUF3520 pfam12034
Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. ...
 703-896 4.44e-82

Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 180 amino acids in length. This domain is found associated with pfam00092.


:

Pssm-ID: 432277  Cd Length: 182  Bit Score: 262.09  E-value: 4.44e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 703 GNLMTVAKDVKIQVEFNPTKVQEYRLLGYENRIMAAADFNNDKKDAGEIGAGHRVTALYEIVPIGdatgrQGRGDVDELR 782
Cdd:pfam12034   1 STLFTIAKDVKIQVEFNPAQVKEYRLIGYENRLLAREDFNNDKVDAGEIGAGHTVTALYEIVPVG-----SKSDLVDPLK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 783 YQPKSAGAtvvaestEEASSELLAVKLRYKQPEGNTSKLLMFPLEDQATDWSEVDRDFQWAAAMAEFGMLLRNSPHRGKA 862
Cdd:pfam12034  76 YQDAEAAA-------AANSDELATVKLRYKLPDGDKSRLIEYPVADAATAFAQASDDFRFAAAVAGFGMLLRGSEYKGDA 148

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1718691803 863 TWSSLSELSDAAAGVNPDGSRQECLQMIRRASQL 896
Cdd:pfam12034 149 SYDDVIELARGAKGEDPDGYRAEFIRLVEKAKSL 182
RskA super family cl44220
Anti-sigma-K factor RskA [Signal transduction mechanisms];
23-149 2.48e-05

Anti-sigma-K factor RskA [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG5343:

Pssm-ID: 444127 [Multi-domain]  Cd Length: 239  Bit Score: 46.55  E-value: 2.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803  23 AYALGELDGEAVSQIVAAAQREPKLAAEIAAIRATSDHISQVYQTETPagmgPERLstifsQAATSNAVPAEAAATPLPR 102
Cdd:COG5343    14 EYVLGTLSGEERREFERRLASDPELAAEVAEWEERLAPLADAVEPVAP----PPSL-----WARIEARLDAARAAAAAPA 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1718691803 103 KDASRktaaiRRGVWFGVlgTAASLATALFFSLPQMFSPLALQETAP 149
Cdd:COG5343    85 ARLWR-----RLRFWRGL--AAAAAAAALLLAVVLVWLLQPQLNPAP 124
 
Name Accession Description Interval E-value
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 427-741 4.58e-86

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 276.98  E-value: 4.58e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 427 ENAFQRVDDAPLSTLSIDVDTASFVKARqLLLEAGRLPPPDAVRIEEFINYFEYEYAGPHGDdpfgadlaVANCPWAPEH 506
Cdd:COG2304     2 EAGFAAADTVPLSTSSADVDAASSSNRR-RLLVGGEPPPAAAVRLEELVNFFPYDYPLPTGR--------LAQSPWNPQT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 507 KLVRIALQATKVDLAERPKANIVFLLDVSGSMDEpNKLPLVKESIRMLVEQLGENDRVAMVVYAGAAGCVLESTRGDQQE 586
Cdd:COG2304    73 RLLLVGLQPPKAAAEERPPLNLVFVIDVSGSMSG-DKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPPTPATDRA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 587 EILGALQKLSAGGSTNGGQGIELAYNLARDHFIPGGINRVVLCTDGDFNVGVTSTNSLVELVEENAKGNTFLTVLGFGMg 666
Cdd:COG2304   152 KILAAIDRLQAGGGTALGAGLELAYELARKHFIPGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGS- 230

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1718691803 667 NTNDAMMEQISNRGNGVYGFVDSRREAHRQMVRqlagnlmtvakdvkiqvefnptkvqEYRLLGYENRIMAAADF 741
Cdd:COG2304   231 DYNEDLLERLADAGGGNYYYIDDPEEAEKVFVR-------------------------EFSRIGYENRALATEDF 280
DUF3520 pfam12034
Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. ...
 703-896 4.44e-82

Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 180 amino acids in length. This domain is found associated with pfam00092.


Pssm-ID: 432277  Cd Length: 182  Bit Score: 262.09  E-value: 4.44e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 703 GNLMTVAKDVKIQVEFNPTKVQEYRLLGYENRIMAAADFNNDKKDAGEIGAGHRVTALYEIVPIGdatgrQGRGDVDELR 782
Cdd:pfam12034   1 STLFTIAKDVKIQVEFNPAQVKEYRLIGYENRLLAREDFNNDKVDAGEIGAGHTVTALYEIVPVG-----SKSDLVDPLK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 783 YQPKSAGAtvvaestEEASSELLAVKLRYKQPEGNTSKLLMFPLEDQATDWSEVDRDFQWAAAMAEFGMLLRNSPHRGKA 862
Cdd:pfam12034  76 YQDAEAAA-------AANSDELATVKLRYKLPDGDKSRLIEYPVADAATAFAQASDDFRFAAAVAGFGMLLRGSEYKGDA 148

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1718691803 863 TWSSLSELSDAAAGVNPDGSRQECLQMIRRASQL 896
Cdd:pfam12034 149 SYDDVIELARGAKGEDPDGYRAEFIRLVEKAKSL 182
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 526-693 4.11e-60

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: 202.12  E-value: 4.11e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 526 ANIVFLLDVSGSMDEPnKLPLVKESIRMLVEQLGENDRVAMVVYAGAAGCVLESTRGDQQEEILGALQKLSAGGSTNGGQ 605
Cdd:cd01465     1 LNLVFVIDRSGSMDGP-KLPLVKSALKLLVDQLRPDDRLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTAGGSTAGGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 606 GIELAYNLARDHFIPGGINRVVLCTDGDFNVGVTSTNSLVELVEENAKGNTFLTVLGFGmGNTNDAMMEQISNRGNGVYG 685
Cdd:cd01465    80 GIQLGYQEAQKHFVPGGVNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFG-DNYNEDLMEAIADAGNGNTA 158


                  ....*...
gi 1718691803 686 FVDSRREA 693
Cdd:cd01465   159 YIDNLAEA 166
vWF_A pfam12450
von Willebrand factor; This domain family is found in bacteria, and is approximately 100 amino ...
 418-510 9.86e-42

von Willebrand factor; This domain family is found in bacteria, and is approximately 100 amino acids in length. The family is found in association with pfam00092. There are two conserved sequence motifs: STF and DVD. There are two completely conserved residues (E and N) that may be functionally important. In hemostasis, platelet adhesion to the damaged vessel wall is mediated by several proteins, including von Willebrand factor. In solution vWF becomes immobilized via its A3 domain on the fibrillar collagen of the vessel wall and acts as an intermediary between collagen and the platelet receptor glycoprotein Ibalpha (GPIbalpha), which is the only platelet receptor that does not require prior activation for bond formation.


Pssm-ID: 432562 [Multi-domain]  Cd Length: 94  Bit Score: 147.30  E-value: 9.86e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 418 NTDRYQSLTENAFQRVDDAPLSTLSIDVDTASFVKARQLLlEAGRLPPPDAVRIEEFINYFEYEYAGPHGDDPFGADLAV 497
Cdd:pfam12450   3 NTEEYKKIEENPFISVAENPLSTFSIDVDTASYSNVRRFI-NQGQLPPADAVRIEEMINYFDYDYPQPTGDDPFSVTTEV 81

                          90
                  ....*....|...
gi 1718691803 498 ANCPWAPEHKLVR 510
Cdd:pfam12450  82 APCPWNPDHKLLR 94
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 527-693 1.08e-19

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: 87.51  E-value: 1.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803  527 NIVFLLDVSGSMdEPNKLPLVKESIRMLVEQL---GENDRVAMVVYAGAAGCVLESTRGDQQEEILGALQKLS--AGGST 601
Cdd:smart00327   1 DVVFLLDGSGSM-GGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSykLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803  602 NGGQGIELAYNL---ARDHFIPGGINRVVLCTDGDFNVGVTSTNSLV-ELVEENakgntfLTVLGFGMGNTND-AMMEQI 676
Cdd:smart00327  80 NLGAALQYALENlfsKSAGSRRGAPKVVILITDGESNDGPKDLLKAAkELKRSG------VKVFVVGVGNDVDeEELKKL 153

                          170
                   ....*....|....*..
gi 1718691803  677 SNRGNGVYGFVDSRREA 693
Cdd:smart00327 154 ASAPGGVYVFLPELLDL 170
RskA COG5343
Anti-sigma-K factor RskA [Signal transduction mechanisms];
23-149 2.48e-05

Anti-sigma-K factor RskA [Signal transduction mechanisms];


Pssm-ID: 444127 [Multi-domain]  Cd Length: 239  Bit Score: 46.55  E-value: 2.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803  23 AYALGELDGEAVSQIVAAAQREPKLAAEIAAIRATSDHISQVYQTETPagmgPERLstifsQAATSNAVPAEAAATPLPR 102
Cdd:COG5343    14 EYVLGTLSGEERREFERRLASDPELAAEVAEWEERLAPLADAVEPVAP----PPSL-----WARIEARLDAARAAAAAPA 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1718691803 103 KDASRktaaiRRGVWFGVlgTAASLATALFFSLPQMFSPLALQETAP 149
Cdd:COG5343    85 ARLWR-----RLRFWRGL--AAAAAAAALLLAVVLVWLLQPQLNPAP 124
PRK13920 PRK13920
putative anti-sigmaE protein; Provisional
 21-136 9.42e-04

putative anti-sigmaE protein; Provisional


Pssm-ID: 237558 [Multi-domain]  Cd Length: 206  Bit Score: 41.34  E-value: 9.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803  21 LTAYALGELDGEAVSQIVAAAQREPKLAAEIAAIRATSDHISQ-VYQTETPAGmgperlstifsqaatsnaVPAEAAATP 99
Cdd:PRK13920    1 LPLYALGALSPEERARVEAALEAYPELWAELRALQEALAALAEgLPPVPVPPG------------------LEERVLARL 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1718691803 100 LPRKDASRKTAAIRRGVWFGVL---GTAASLATALFFSLP 136
Cdd:PRK13920   63 RPRRLPLLPLLARAAAALALLLagyGLAAGLSWTLSLREP 102
 
Name Accession Description Interval E-value
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 427-741 4.58e-86

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 276.98  E-value: 4.58e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 427 ENAFQRVDDAPLSTLSIDVDTASFVKARqLLLEAGRLPPPDAVRIEEFINYFEYEYAGPHGDdpfgadlaVANCPWAPEH 506
Cdd:COG2304     2 EAGFAAADTVPLSTSSADVDAASSSNRR-RLLVGGEPPPAAAVRLEELVNFFPYDYPLPTGR--------LAQSPWNPQT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 507 KLVRIALQATKVDLAERPKANIVFLLDVSGSMDEpNKLPLVKESIRMLVEQLGENDRVAMVVYAGAAGCVLESTRGDQQE 586
Cdd:COG2304    73 RLLLVGLQPPKAAAEERPPLNLVFVIDVSGSMSG-DKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPPTPATDRA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 587 EILGALQKLSAGGSTNGGQGIELAYNLARDHFIPGGINRVVLCTDGDFNVGVTSTNSLVELVEENAKGNTFLTVLGFGMg 666
Cdd:COG2304   152 KILAAIDRLQAGGGTALGAGLELAYELARKHFIPGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGS- 230

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1718691803 667 NTNDAMMEQISNRGNGVYGFVDSRREAHRQMVRqlagnlmtvakdvkiqvefnptkvqEYRLLGYENRIMAAADF 741
Cdd:COG2304   231 DYNEDLLERLADAGGGNYYYIDDPEEAEKVFVR-------------------------EFSRIGYENRALATEDF 280
DUF3520 pfam12034
Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. ...
 703-896 4.44e-82

Domain of unknown function (DUF3520); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 180 amino acids in length. This domain is found associated with pfam00092.


Pssm-ID: 432277  Cd Length: 182  Bit Score: 262.09  E-value: 4.44e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 703 GNLMTVAKDVKIQVEFNPTKVQEYRLLGYENRIMAAADFNNDKKDAGEIGAGHRVTALYEIVPIGdatgrQGRGDVDELR 782
Cdd:pfam12034   1 STLFTIAKDVKIQVEFNPAQVKEYRLIGYENRLLAREDFNNDKVDAGEIGAGHTVTALYEIVPVG-----SKSDLVDPLK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 783 YQPKSAGAtvvaestEEASSELLAVKLRYKQPEGNTSKLLMFPLEDQATDWSEVDRDFQWAAAMAEFGMLLRNSPHRGKA 862
Cdd:pfam12034  76 YQDAEAAA-------AANSDELATVKLRYKLPDGDKSRLIEYPVADAATAFAQASDDFRFAAAVAGFGMLLRGSEYKGDA 148

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1718691803 863 TWSSLSELSDAAAGVNPDGSRQECLQMIRRASQL 896
Cdd:pfam12034 149 SYDDVIELARGAKGEDPDGYRAEFIRLVEKAKSL 182
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 526-693 4.11e-60

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: 202.12  E-value: 4.11e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 526 ANIVFLLDVSGSMDEPnKLPLVKESIRMLVEQLGENDRVAMVVYAGAAGCVLESTRGDQQEEILGALQKLSAGGSTNGGQ 605
Cdd:cd01465     1 LNLVFVIDRSGSMDGP-KLPLVKSALKLLVDQLRPDDRLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTAGGSTAGGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 606 GIELAYNLARDHFIPGGINRVVLCTDGDFNVGVTSTNSLVELVEENAKGNTFLTVLGFGmGNTNDAMMEQISNRGNGVYG 685
Cdd:cd01465    80 GIQLGYQEAQKHFVPGGVNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFG-DNYNEDLMEAIADAGNGNTA 158


                  ....*...
gi 1718691803 686 FVDSRREA 693
Cdd:cd01465   159 YIDNLAEA 166
vWF_A pfam12450
von Willebrand factor; This domain family is found in bacteria, and is approximately 100 amino ...
 418-510 9.86e-42

von Willebrand factor; This domain family is found in bacteria, and is approximately 100 amino acids in length. The family is found in association with pfam00092. There are two conserved sequence motifs: STF and DVD. There are two completely conserved residues (E and N) that may be functionally important. In hemostasis, platelet adhesion to the damaged vessel wall is mediated by several proteins, including von Willebrand factor. In solution vWF becomes immobilized via its A3 domain on the fibrillar collagen of the vessel wall and acts as an intermediary between collagen and the platelet receptor glycoprotein Ibalpha (GPIbalpha), which is the only platelet receptor that does not require prior activation for bond formation.


Pssm-ID: 432562 [Multi-domain]  Cd Length: 94  Bit Score: 147.30  E-value: 9.86e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 418 NTDRYQSLTENAFQRVDDAPLSTLSIDVDTASFVKARQLLlEAGRLPPPDAVRIEEFINYFEYEYAGPHGDDPFGADLAV 497
Cdd:pfam12450   3 NTEEYKKIEENPFISVAENPLSTFSIDVDTASYSNVRRFI-NQGQLPPADAVRIEEMINYFDYDYPQPTGDDPFSVTTEV 81

                          90
                  ....*....|...
gi 1718691803 498 ANCPWAPEHKLVR 510
Cdd:pfam12450  82 APCPWNPDHKLLR 94
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 434-692 4.01e-29

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: 117.35  E-value: 4.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 434 DDAPLSTLSIDVDTASFVKARQLLLEAGRLPPPDAVRIEEFINYFEYEYAGPHGDDPFGADLAVANCPWAPEHKLVRIAL 513
Cdd:COG1240     2 LALALLALLLLLALALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 514 QATKVDLAERPkANIVFLLDVSGSMDEPNKLPLVKESIRMLVEQLGENDRVAMVVYAGAAGCVLESTRgdQQEEILGALQ 593
Cdd:COG1240    82 APLALARPQRG-RDVVLVVDASGSMAAENRLEAAKGALLDFLDDYRPRDRVGLVAFGGEAEVLLPLTR--DREALKRALD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 594 KLSAGGSTNGGQGIELAYNLARDHFiPGGINRVVLCTDGDFNVGvtsTNSLVELVEENAKGNTFLTVLGFGMGNTNDAMM 673
Cdd:COG1240   159 ELPPGGGTPLGDALALALELLKRAD-PARRKVIVLLTDGRDNAG---RIDPLEAAELAAAAGIRIYTIGVGTEAVDEGLL 234

                         250
                  ....*....|....*....
gi 1718691803 674 EQISNRGNGVYGFVDSRRE 692
Cdd:COG1240   235 REIAEATGGRYFRADDLSE 253
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 526-686 1.36e-24

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: 101.10  E-value: 1.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 526 ANIVFLLDVSGSMdEPNKLPLVKESIRMLVEQL---GENDRVAMVVYAGAAGCVLESTRGDQQEEILGALQKL--SAGGS 600
Cdd:cd00198     1 ADIVFLLDVSGSM-GGEKLDKAKEALKALVSSLsasPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALkkGLGGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 601 TNGGQGIELAYNLARDHFIPGGINRVVLCTDGDFNVGVTSTNSLVELVEENakgNTFLTVLGFGMGNTNDAmMEQISNRG 680
Cdd:cd00198    80 TNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELRKL---GITVYTIGIGDDANEDE-LKEIADKT 155


                  ....*.
gi 1718691803 681 NGVYGF 686
Cdd:cd00198   156 TGGAVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 527-693 1.08e-19

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: 87.51  E-value: 1.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803  527 NIVFLLDVSGSMdEPNKLPLVKESIRMLVEQL---GENDRVAMVVYAGAAGCVLESTRGDQQEEILGALQKLS--AGGST 601
Cdd:smart00327   1 DVVFLLDGSGSM-GGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSykLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803  602 NGGQGIELAYNL---ARDHFIPGGINRVVLCTDGDFNVGVTSTNSLV-ELVEENakgntfLTVLGFGMGNTND-AMMEQI 676
Cdd:smart00327  80 NLGAALQYALENlfsKSAGSRRGAPKVVILITDGESNDGPKDLLKAAkELKRSG------VKVFVVGVGNDVDeEELKKL 153

                          170
                   ....*....|....*..
gi 1718691803  677 SNRGNGVYGFVDSRREA 693
Cdd:smart00327 154 ASAPGGVYVFLPELLDL 170
VWA pfam00092
von Willebrand factor type A domain;
527-700 6.19e-18

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 82.32  E-value: 6.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 527 NIVFLLDVSGSMDEPNkLPLVKESIRMLVEQLG---ENDRVAMVVYAGAAGCVLESTRGDQQEEILGALQKL--SAGGST 601
Cdd:pfam00092   1 DIVFLLDGSGSIGGDN-FEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLryLGGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 602 NGGQGIELAYNLARDH---FIPGGINRVVLCTDGDfnvgvtSTNSLVELVEENAKGNTFlTVLGFGMGNTNDAMMEQISN 678
Cdd:pfam00092  80 NTGKALKYALENLFSSaagARPGAPKVVVLLTDGR------SQDGDPEEVARELKSAGV-TVFAVGVGNADDEELRKIAS 152

                         170       180
                  ....*....|....*....|..
gi 1718691803 679 RGNGVYGFVDSRREAHRQMVRQ 700
Cdd:pfam00092 153 EPGEGHVFTVSDFEALEDLQDQ 174
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 427-677 9.73e-17

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 81.26  E-value: 9.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 427 ENAFQRVDDAPLSTLSIDVDTASFVKARQLLLEAGRLPPPDAVRIEEFINyFEYEYAGPHGDDPFGADLAVANCPWAPEH 506
Cdd:COG2425    21 ATALLLAGLLRAALALGLALALRAALLALLLLLLRAALALLTLLAGLVLL-ALDALLLAALLAALLDALLLAVLLLALLL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 507 KLVRIALQATKVDLAERPKANIVFLLDVSGSMDEpNKLPLVKESIRMLVEQLGENDRVAMVVYAGAAGCVLESTRGDQQE 586
Cdd:COG2425   100 LAALLLLAAPASAAVPLLEGPVVLCVDTSGSMAG-SKEAAAKAAALALLRALRPNRRFGVILFDTEVVEDLPLTADDGLE 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 587 EILGALQKLSAGGSTNGGQGIELAYNLARDhfiPGGINR-VVLCTDGDFNVgvtSTNSLVELVEENAKGNTFLTVlgfGM 665
Cdd:COG2425   179 DAIEFLSGLFAGGGTDIAPALRAALELLEE---PDYRNAdIVLITDGEAGV---SPEELLREVRAKESGVRLFTV---AI 249

                         250
                  ....*....|...
gi 1718691803 666 GNTND-AMMEQIS 677
Cdd:COG2425   250 GDAGNpGLLEALA 262
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 528-687 8.63e-13

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: 67.03  E-value: 8.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 528 IVFLLDVSGSMDEpNKLPLVKESIRMLVEQLGENDRVAMVVYAGAAG--CVLESTRGDQQEEILGALQKLSAGGSTNGGQ 605
Cdd:cd01466     3 LVAVLDVSGSMAG-DKLQLVKHALRFVISSLGDADRLSIVTFSTSAKrlSPLRRMTAKGKRSAKRVVDGLQAGGGTNVVG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 606 GIELAYNLARDHFIPGGINRVVLCTDGDFNVGVTSTNSlvelveenakGNTFLTVLGFGMGNTND-AMMEQISNRGNGVY 684
Cdd:cd01466    82 GLKKALKVLGDRRQKNPVASIMLLSDGQDNHGAVVLRA----------DNAPIPIHTFGLGASHDpALLAFIAEITGGTF 151


                  ...
gi 1718691803 685 GFV 687
Cdd:cd01466   152 SYV 154
VWA_2 pfam13519
von Willebrand factor type A domain;
528-628 2.23e-12

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 64.24  E-value: 2.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 528 IVFLLDVSGSM----DEPNKLPLVKESIRMLVEQLGeNDRVAMVVYAGaaGCVLESTRGDQQEEILGALQKLSA-GGSTN 602
Cdd:pfam13519   1 LVFVLDTSGSMrngdYGPTRLEAAKDAVLALLKSLP-GDRVGLVTFGD--GPEVLIPLTKDRAKILRALRRLEPkGGGTN 77

                          90       100
                  ....*....|....*....|....*.
gi 1718691803 603 GGQGIELAYNLARDhfIPGGINRVVL 628
Cdd:pfam13519  78 LAAALQLARAALKH--RRKNQPRRIV 101
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 527-699 5.47e-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: 64.93  E-value: 5.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 527 NIVFLLDVSGSMDEPnKLPLVKESIRMLVEQLGENDRVAMVVYAGAA---GCVLESTRGDQQEEILGALQKLSAGGSTNG 603
Cdd:cd01461     4 EVVFVIDTSGSMSGT-KIEQTKEALLTALKDLPPGDYFNIIGFSDTVeefSPSSVSATAENVAAAIEYVNRLQALGGTNM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 604 GQGIELAYN-LARDhfiPGGINRVVLCTDGDfnvgVTSTNSLVELVEENAKGNTFLTVLGFGMGnTNDAMMEQISNRGNG 682
Cdd:cd01461    83 NDALEAALElLNSS---PGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSD-VNTYLLERLAREGRG 154

                         170
                  ....*....|....*..
gi 1718691803 683 VYGFVDSRREAHRQMVR 699
Cdd:cd01461   155 IARRIYETDDIESQLLR 171
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 526-686 1.11e-09

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: 58.07  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 526 ANIVFLLDVSGSMDEPNkLPLVKESIRMLVEQL---GENDRVAMVVYAGAAGCVLESTRGDQQEEILGALQKLS--AGGS 600
Cdd:cd01450     1 LDIVFLLDGSESVGPEN-FEKVKDFIEKLVEKLdigPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKylGGGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 601 TNGGQGIELAY-NLARDHFIPGGINRV-VLCTDGDFNVGVTSTNSLVELVEENAKgntfltVLGFGMGNTNDAMMEQISN 678
Cdd:cd01450    80 TNTGKALQYALeQLFSESNARENVPKViIVLTDGRSDDGGDPKEAAAKLKDEGIK------VFVVGVGPADEEELREIAS 153


                  ....*...
gi 1718691803 679 RGNGVYGF 686
Cdd:cd01450   154 CPSERHVF 161
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
527-714 2.66e-09

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 57.63  E-value: 2.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 527 NIVFLLDVSGSMDEpNKLPLVKESIRMLVEQL------GENDRVAMVVYAGAAGCVLESTRGDQQEeilgaLQKLSAGGS 600
Cdd:COG4245     7 PVYLLLDTSGSMSG-EPIEALNEGLQALIDELrqdpyaLETVEVSVITFDGEAKVLLPLTDLEDFQ-----PPDLSASGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 601 TNGGQGIELAYNLARDHFIPGGINR-------VVLCTDG---DfnvgvTSTNSLVELVEENAKGNtFLTVLGFGMG-NTN 669
Cdd:COG4245    81 TPLGAALELLLDLIERRVQKYTAEGkgdwrpvVFLITDGeptD-----SDWEAALQRLKDGEAAK-KANIFAIGVGpDAD 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1718691803 670 DAMMEQISnrgNGVYGFVDSRREAHRQMVRQLAGNLMTVAKDVKI 714
Cdd:COG4245   155 TEVLKQLT---DPVRALDALDGLDFREFFKWLSASVSSVSRSVGP 196
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 526-638 1.36e-08

VWA BatA 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. Members of this subgroup are bacterial in origin. They are typified by the presence of a MIDAS motif.


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 55.41  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 526 ANIVFLLDVSGSMDE-----PNKLPLVKESIRMLVEQLgENDRVAMVVYAGAAGCVLESTrGDQqeEILGALQKLSAGGS 600
Cdd:cd01467     3 RDIMIALDVSGSMLAqdfvkPSRLEAAKEVLSDFIDRR-ENDRIGLVVFAGAAFTQAPLT-LDR--ESLKELLEDIKIGL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1718691803 601 TNGGQGIELAYNLARDHFIPG-GINRV-VLCTDGDFNVGV 638
Cdd:cd01467    79 AGQGTAIGDAIGLAIKRLKNSeAKERViVLLTDGENNAGE 118
VWA_3 pfam13768
von Willebrand factor type A domain;
526-686 2.88e-07

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 50.86  E-value: 2.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 526 ANIVFLLDVSGSMDEPNklPLVKESIRMLVEQLGENDRVAMVVYAGAAGCVLESTRGDQQEEILGALQKLSAGGSTNGGQ 605
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEP--KLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPLGGS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 606 GIELAYNLARDHFIPGGINR-VVLCTDGDFNVGVTSTNSLVelveENAKGNTFLTVLGFGmGNTNDAMMEQISNRGNGVY 684
Cdd:pfam13768  79 DLLGALKEAVRAPASPGYIRhVLLLTDGSPMQGETRVSDLI----SRAPGKIRFFAYGLG-ASISAPMLQLLAEASNGTY 153


                  ..
gi 1718691803 685 GF 686
Cdd:pfam13768 154 EF 155
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 518-666 1.22e-06

VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The alpha 2 and delta subunits result from proteolytic processing of a single gene product and carries at its N-terminus the VWA and cache domains, The alpha 2 delta gene family has orthologues in D. melanogaster and C. elegans but none have been detected in aither A. thaliana or yeast. The exact biochemical function of the VWA domain is not known but the alpha 2 delta complex has been shown to regulate various functional properties of the channel complex.


Pssm-ID: 238740 [Multi-domain]  Cd Length: 190  Bit Score: 49.70  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 518 VDLAERPKaNIVFLLDVSGSMDEPnKLPLVKESIRMLVEQLGENDRVAMVVYAGAA----GC----VLESTRGDQQeEIL 589
Cdd:cd01463     7 IQAATSPK-DIVILLDVSGSMTGQ-RLHLAKQTVSSILDTLSDNDFFNIITFSNEVnpvvPCfndtLVQATTSNKK-VLK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 590 GALQKLSAGGSTNGGQGIELAYNLARDHFIPGGINRVVLC-------TDgdfnvGVTSTNSLVeLVEENAKGNTFLTVLG 662
Cdd:cd01463    84 EALDMLEAKGIANYTKALEFAFSLLLKNLQSNHSGSRSQCnqaimliTD-----GVPENYKEI-FDKYNWDKNSEIPVRV 157


                  ....
gi 1718691803 663 FGMG 666
Cdd:cd01463   158 FTYL 161
vWA_ywmD_type cd01456
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 523-684 3.22e-06

VWA ywmD 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. Not much is known about the function of the members of this subgroup. All members of this subgroup however have a conserved MIDAS motif.


Pssm-ID: 238733 [Multi-domain]  Cd Length: 206  Bit Score: 48.96  E-value: 3.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 523 RPKANIVFLLDVSGSMDEP-----NKLPLVKESIRMLVEQLGENDRVAMVVYAGAA------------GCVLESTRGDQQ 585
Cdd:cd01456    18 QLPPNVAIVLDNSGSMREVdgggeTRLDNAKAALDETANALPDGTRLGLWTFSGDGdnpldvrvlvpkGCLTAPVNGFPS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 586 EEILGALQKLSAGGSTNGGQGIELAYNLARDHFIPGGINRVVLCTDGDFNVGVTSTNSLVELVEENAKGNTF-LTVLGFG 664
Cdd:cd01456    98 AQRSALDAALNSLQTPTGWTPLAAALAEAAAYVDPGRVNVVVLITDGEDTCGPDPCEVARELAKRRTPAPPIkVNVIDFG 177

                         170       180
                  ....*....|....*....|
gi 1718691803 665 mGNTNDAMMEQISNRGNGVY 684
Cdd:cd01456   178 -GDADRAELEAIAEATGGTY 196
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 526-632 4.63e-06

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 47.78  E-value: 4.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 526 ANIVFLLDVSGSMDEpnKLPLVKESIRMLVEQL---GENDRVAMVVYAGAAGCVLESTRGD--QQEEILGALQKL-SAGG 599
Cdd:cd01476     1 LDLLFVLDSSGSVRG--KFEKYKKYIERIVEGLeigPTATRVALITYSGRGRQRVRFNLPKhnDGEELLEKVDNLrFIGG 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1718691803 600 STNGGQGIELAYNlardHFIPGGINR------VVLCTDG 632
Cdd:cd01476    79 TTATGAAIEVALQ----QLDPSEGRRegipkvVVVLTDG 113
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 527-666 7.71e-06

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 47.38  E-value: 7.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 527 NIVFLLDVSGSMDEPNKLPLVKESIRMLVEQLGEND---RVAMVVYAGAAGCVLE-----STRGDQQEEILGALQKL-SA 597
Cdd:cd01471     2 DLYLLVDGSGSIGYSNWVTHVVPFLHTFVQNLNISPdeiNLYLVTFSTNAKELIRlsspnSTNKDLALNAIRALLSLyYP 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1718691803 598 GGSTNggqgIELAYNLARDHFIPGGINR------VVLCTDGDFNVGVTSTNSLVELVEENAKgntfLTVLGFGMG 666
Cdd:cd01471    82 NGSTN----TTSALLVVEKHLFDTRGNRenapqlVIIMTDGIPDSKFRTLKEARKLRERGVI----IAVLGVGQG 148
RskA COG5343
Anti-sigma-K factor RskA [Signal transduction mechanisms];
23-149 2.48e-05

Anti-sigma-K factor RskA [Signal transduction mechanisms];


Pssm-ID: 444127 [Multi-domain]  Cd Length: 239  Bit Score: 46.55  E-value: 2.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803  23 AYALGELDGEAVSQIVAAAQREPKLAAEIAAIRATSDHISQVYQTETPagmgPERLstifsQAATSNAVPAEAAATPLPR 102
Cdd:COG5343    14 EYVLGTLSGEERREFERRLASDPELAAEVAEWEERLAPLADAVEPVAP----PPSL-----WARIEARLDAARAAAAAPA 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1718691803 103 KDASRktaaiRRGVWFGVlgTAASLATALFFSLPQMFSPLALQETAP 149
Cdd:COG5343    85 ARLWR-----RLRFWRGL--AAAAAAAALLLAVVLVWLLQPQLNPAP 124
YeaD2 COG1721
Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];
526-631 4.13e-05

Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];


Pssm-ID: 441327 [Multi-domain]  Cd Length: 287  Bit Score: 46.35  E-value: 4.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 526 ANIVFLLDVSGSMD----EPNKLPLVKESIRMLVEQ-LGENDRVAMVVYAGAAGCVLESTRGDQQ-EEILGALQKLSAGG 599
Cdd:COG1721   148 LTVVLLLDTSASMRfgsgGPSKLDLAVEAAASLAYLaLRQGDRVGLLTFGDRVRRYLPPRRGRRHlLRLLEALARLEPAG 227

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1718691803 600 STNggqgIELAYNLARDHFIPGGInrVVLCTD 631
Cdd:COG1721   228 ETD----LAAALRRLARRLPRRSL--VVLISD 253
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 526-632 5.56e-05

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 44.53  E-value: 5.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 526 ANIVFLLDVSGSMDEPNkLPLVKESIRMLVEQL--GEND-RVAMVVYAGAAgcVLESTRGDQQ--EEILGALQKLS-AGG 599
Cdd:cd01472     1 ADIVFLVDGSESIGLSN-FNLVKDFVKRVVERLdiGPDGvRVGVVQYSDDP--RTEFYLNTYRskDDVLEAVKNLRyIGG 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1718691803 600 STNGGQGIELAYN--LARDHFIPGGINRV-VLCTDG 632
Cdd:cd01472    78 GTNTGKALKYVREnlFTEASGSREGVPKVlVVITDG 113
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 526-632 3.25e-04

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 42.27  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 526 ANIVFLLDVSGSMDEPNKlPLVKESIRMLVEQL--GEND-RVAMVVYAGAAGCVLESTRGDQQEEILGALQKLS-AGGST 601
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNF-NLVRSFLSSVVEAFeiGPDGvQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPyKGGNT 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1718691803 602 NGGQGIElayNLARDHFIPG-----GINRV-VLCTDG 632
Cdd:cd01482    80 RTGKALT---HVREKNFTPDagarpGVPKVvILITDG 113
PRK13920 PRK13920
putative anti-sigmaE protein; Provisional
 21-136 9.42e-04

putative anti-sigmaE protein; Provisional


Pssm-ID: 237558 [Multi-domain]  Cd Length: 206  Bit Score: 41.34  E-value: 9.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803  21 LTAYALGELDGEAVSQIVAAAQREPKLAAEIAAIRATSDHISQ-VYQTETPAGmgperlstifsqaatsnaVPAEAAATP 99
Cdd:PRK13920    1 LPLYALGALSPEERARVEAALEAYPELWAELRALQEALAALAEgLPPVPVPPG------------------LEERVLARL 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1718691803 100 LPRKDASRKTAAIRRGVWFGVL---GTAASLATALFFSLP 136
Cdd:PRK13920   63 RPRRLPLLPLLARAAAALALLLagyGLAAGLSWTLSLREP 102
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 528-637 1.51e-03

Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). In chlorophyll biosynthesis, insertion of Mg2+ into protoporphyrin IX is catalysed by magnesium chelatase in an ATP-dependent reaction. Magnesium chelatase is a three sub-unit (BchI, BchD and BchH) enzyme with a novel arrangement of domains: the C-terminal helical domain is located behind the nucleotide binding site. The BchD domain contains a AAA domain at its N-terminus and a VWA domain at its C-terminus. The VWA domain has been speculated to be involved in mediating protein-protein interactions.


Pssm-ID: 238728 [Multi-domain]  Cd Length: 178  Bit Score: 40.34  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718691803 528 IVFLLDVSGSMDEPNKLPLVKESIR-MLVEQLGENDRVAMVVYAG-AAGCVLESTRgdQQEEILGALQKLSAGGST--NG 603
Cdd:cd01451     3 VIFVVDASGSMAARHRMAAAKGAVLsLLRDAYQRRDKVALIAFRGtEAEVLLPPTR--SVELAKRRLARLPTGGGTplAA 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1718691803 604 G--QGIELAYNLARDhfiPGGINRVVLCTDGDFNVG 637
Cdd:cd01451    81 GllAAYELAAEQARD---PGQRPLIVVITDGRANVG 113
 
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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