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Conserved domains on  [gi|446685354|ref|WP_000762700|]
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MULTISPECIES: VWA domain-containing protein [Gammaproteobacteria]

Protein Classification

vWA domain-containing protein( domain architecture ID 630)

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|12579041|12388743
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 498-651 4.11e-23

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.


The actual alignment was detected with superfamily member cd01454:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 174  Bit Score: 96.63  E-value: 4.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354 498 VGLVLVRDISASMANDERYIHAIKSDLALSMAAESLSKMHVSNiVFP---FKESEFEII--KTFDQS----VEESLSKFT 568
Cdd:cd01454    1 LAVTLLLDLSGSMRSDRRIDVAKKAAVLLAEALEACGVPHAIL-GFTtdaGGRERVRWIkiKDFDESlherARKRLAALS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354 569 lgcKGYYTPTGSALMAAVDLLLDSQFDRKIIFLITDGYPNKSEFTIVEVM--EKAKCNGIEIVGVGIKTDEIIGFETDTF 646
Cdd:cd01454   80 ---PGGNTRDGAAIRHAAERLLARPEKRKILLVISDGEPNDLDYYEGNVFatEDALRAVIEARKLGIEVFGITIDRDATT 156


                 ....*
gi 446685354 647 VTVDD 651
Cdd:cd01454  157 VDKEY 161
 
Name Accession Description Interval E-value
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 498-651 4.11e-23

norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate reductases. Denitrification plays a major role in completing the nitrogen cycle by converting nitrate or nitrite to nitrogen gas. The pathway for microbial denitrification has been established as NO3- ------> NO2- ------> NO -------> N2O ---------> N2. This reaction generally occurs under oxygen limiting conditions. Genetic and biochemical studies have shown that the first srep of the biochemical pathway is catalyzed by periplasmic nitrate reductases. This family is widely present in proteobacteria and firmicutes. This version of the domain is also present in some archaeal members. The function of the vWA domain in this sub-group is not known. Members of this subgroup have a conserved MIDAS motif.


Pssm-ID: 238731 [Multi-domain]  Cd Length: 174  Bit Score: 96.63  E-value: 4.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354 498 VGLVLVRDISASMANDERYIHAIKSDLALSMAAESLSKMHVSNiVFP---FKESEFEII--KTFDQS----VEESLSKFT 568
Cdd:cd01454    1 LAVTLLLDLSGSMRSDRRIDVAKKAAVLLAEALEACGVPHAIL-GFTtdaGGRERVRWIkiKDFDESlherARKRLAALS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354 569 lgcKGYYTPTGSALMAAVDLLLDSQFDRKIIFLITDGYPNKSEFTIVEVM--EKAKCNGIEIVGVGIKTDEIIGFETDTF 646
Cdd:cd01454   80 ---PGGNTRDGAAIRHAAERLLARPEKRKILLVISDGEPNDLDYYEGNVFatEDALRAVIEARKLGIEVFGITIDRDATT 156


                 ....*
gi 446685354 647 VTVDD 651
Cdd:cd01454  157 VDKEY 161
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 500-638 7.27e-12

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: 66.12  E-value: 7.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354 500 LVLVRDISASMANDERyIHAIKsDLALSMAAESLSKMHVSNIVF--------PFkesefeiikTFD-QSVEESLSKFTLG 570
Cdd:COG1240   95 VVLVVDASGSMAAENR-LEAAK-GALLDFLDDYRPRDRVGLVAFggeaevllPL---------TRDrEALKRALDELPPG 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446685354 571 ckGYyTPTGSALMAAVDLLLD-SQFDRKIIFLITDGYPNKSEFTIVEVMEKAKCNGIEIVGVGIKTDEI 638
Cdd:COG1240  164 --GG-TPLGDALALALELLKRaDPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTEAV 229
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 500-636 2.87e-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: 2.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354   500 LVLVRDISASMAndERYIHAIKSdlALSMAAESLS----KMHVSNIVF---PFKESEFEIIKTFDqSVEESLSKFTLGCK 572
Cdd:smart00327   2 VVFLLDGSGSMG--GNRFELAKE--FVLKLVEQLDigpdGDRVGLVTFsddARVLFPLNDSRSKD-ALLEALASLSYKLG 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446685354   573 GYyTPTGSALMAAVDLLLDSQ-----FDRKIIFLITDGYPNKSEFTIVEVMEKAKCNGIEIVGVGIKTD 636
Cdd:smart00327  77 GG-TNLGAALQYALENLFSKSagsrrGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGND 144
VWA pfam00092
von Willebrand factor type A domain;
500-655 2.99e-06

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 48.04  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354  500 LVLVRDISASMAND--ERYIHAIK---SDLALSMAAESLSKMHVSN---IVFPFkesefeiikTFDQSVEESLSK-FTLG 570
Cdd:pfam00092   2 IVFLLDGSGSIGGDnfEKVKEFLKklvESLDIGPDGTRVGLVQYSSdvrTEFPL---------NDYSSKEELLSAvDNLR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354  571 CKGY-YTPTGSALMAAVDLLLDSQF-----DRKIIFLITDGYPNKSEftIVEVMEKAKCNGIEIVGVGIKTD-----EII 639
Cdd:pfam00092  73 YLGGgTTNTGKALKYALENLFSSAAgarpgAPKVVVLLTDGRSQDGD--PEEVARELKSAGVTVFAVGVGNAddeelRKI 150

                         170
                  ....*....|....*...
gi 446685354  640 GFETD--TFVTVDDTSLL 655
Cdd:pfam00092 151 ASEPGegHVFTVSDFEAL 168
 
Name Accession Description Interval E-value
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 498-651 4.11e-23

norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate reductases. Denitrification plays a major role in completing the nitrogen cycle by converting nitrate or nitrite to nitrogen gas. The pathway for microbial denitrification has been established as NO3- ------> NO2- ------> NO -------> N2O ---------> N2. This reaction generally occurs under oxygen limiting conditions. Genetic and biochemical studies have shown that the first srep of the biochemical pathway is catalyzed by periplasmic nitrate reductases. This family is widely present in proteobacteria and firmicutes. This version of the domain is also present in some archaeal members. The function of the vWA domain in this sub-group is not known. Members of this subgroup have a conserved MIDAS motif.


Pssm-ID: 238731 [Multi-domain]  Cd Length: 174  Bit Score: 96.63  E-value: 4.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354 498 VGLVLVRDISASMANDERYIHAIKSDLALSMAAESLSKMHVSNiVFP---FKESEFEII--KTFDQS----VEESLSKFT 568
Cdd:cd01454    1 LAVTLLLDLSGSMRSDRRIDVAKKAAVLLAEALEACGVPHAIL-GFTtdaGGRERVRWIkiKDFDESlherARKRLAALS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354 569 lgcKGYYTPTGSALMAAVDLLLDSQFDRKIIFLITDGYPNKSEFTIVEVM--EKAKCNGIEIVGVGIKTDEIIGFETDTF 646
Cdd:cd01454   80 ---PGGNTRDGAAIRHAAERLLARPEKRKILLVISDGEPNDLDYYEGNVFatEDALRAVIEARKLGIEVFGITIDRDATT 156


                 ....*
gi 446685354 647 VTVDD 651
Cdd:cd01454  157 VDKEY 161
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 500-638 7.27e-12

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: 66.12  E-value: 7.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354 500 LVLVRDISASMANDERyIHAIKsDLALSMAAESLSKMHVSNIVF--------PFkesefeiikTFD-QSVEESLSKFTLG 570
Cdd:COG1240   95 VVLVVDASGSMAAENR-LEAAK-GALLDFLDDYRPRDRVGLVAFggeaevllPL---------TRDrEALKRALDELPPG 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446685354 571 ckGYyTPTGSALMAAVDLLLD-SQFDRKIIFLITDGYPNKSEFTIVEVMEKAKCNGIEIVGVGIKTDEI 638
Cdd:COG1240  164 --GG-TPLGDALALALELLKRaDPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTEAV 229
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 500-636 2.87e-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: 2.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354   500 LVLVRDISASMAndERYIHAIKSdlALSMAAESLS----KMHVSNIVF---PFKESEFEIIKTFDqSVEESLSKFTLGCK 572
Cdd:smart00327   2 VVFLLDGSGSMG--GNRFELAKE--FVLKLVEQLDigpdGDRVGLVTFsddARVLFPLNDSRSKD-ALLEALASLSYKLG 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446685354   573 GYyTPTGSALMAAVDLLLDSQ-----FDRKIIFLITDGYPNKSEFTIVEVMEKAKCNGIEIVGVGIKTD 636
Cdd:smart00327  77 GG-TNLGAALQYALENLFSKSagsrrGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGND 144
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 500-636 9.12e-10

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: 57.96  E-value: 9.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354 500 LVLVRDISASMA--NDERYIHAIKSdlALSMAAESLSKMHVSNIVF---PFKESEFEIIKTFDQsVEESLSKFTLGCKGY 574
Cdd:cd00198    3 IVFLLDVSGSMGgeKLDKAKEALKA--LVSSLSASPPGDRVGLVTFgsnARVVLPLTTDTDKAD-LLEAIDALKKGLGGG 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446685354 575 yTPTGSALMAAVDLLLDSQFD--RKIIFLITDGYPNKSEFTIVEVMEKAKCNGIEIVGVGIKTD 636
Cdd:cd00198   80 -TNIGAALRLALELLKSAKRPnaRRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDD 142
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
492-636 8.84e-07

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 49.92  E-value: 8.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354 492 SKNRGHVGLVLvrDISASMANDEryIHAIKSDLAlSMAAESLSKMHVSnivfpfKESEFEIIkTFDQSVEE-----SLSK 566
Cdd:COG4245    2 PMRRLPVYLLL--DTSGSMSGEP--IEALNEGLQ-ALIDELRQDPYAL------ETVEVSVI-TFDGEAKVllpltDLED 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354 567 FT---LGCKGYyTPTGSALMAAVDLLLDSQ---------FDRKIIFLITDGYPNKSEFT--IVEVMEKAKCNGIEIVGVG 632
Cdd:COG4245   70 FQppdLSASGG-TPLGAALELLLDLIERRVqkytaegkgDWRPVVFLITDGEPTDSDWEaaLQRLKDGEAAKKANIFAIG 148


                 ....
gi 446685354 633 IKTD 636
Cdd:COG4245  149 VGPD 152
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 426-633 1.20e-06

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 50.45  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354 426 PDLLIDLNVYNEALSLSHSIGSDLSVLQQVKMRGRNKTHERGITFDGNRLILSQMGVRDVFRAQSESKNRGHVG-LVLVR 504
Cdd:COG2425   46 LLALLLLLLRAALALLTLLAGLVLLALDALLLAALLAALLDALLLAVLLLALLLLAALLLLAAPASAAVPLLEGpVVLCV 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354 505 DISASMANDeryihaiKSDLALSMAAESLSKM--HVSNIVFPF-KESEFEIIKTFDQSVEESLSKFTLGCKGYYTPTGSA 581
Cdd:COG2425  126 DTSGSMAGS-------KEAAAKAAALALLRALrpNRRFGVILFdTEVVEDLPLTADDGLEDAIEFLSGLFAGGGTDIAPA 198

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446685354 582 LMAAVDLLLDSQFDRKIIFLITDGYPNKSEFTIVEVMEKAKcNGIEIVGVGI 633
Cdd:COG2425  199 LRAALELLEEPDYRNADIVLITDGEAGVSPEELLREVRAKE-SGVRLFTVAI 249
VWA pfam00092
von Willebrand factor type A domain;
500-655 2.99e-06

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 48.04  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354  500 LVLVRDISASMAND--ERYIHAIK---SDLALSMAAESLSKMHVSN---IVFPFkesefeiikTFDQSVEESLSK-FTLG 570
Cdd:pfam00092   2 IVFLLDGSGSIGGDnfEKVKEFLKklvESLDIGPDGTRVGLVQYSSdvrTEFPL---------NDYSSKEELLSAvDNLR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354  571 CKGY-YTPTGSALMAAVDLLLDSQF-----DRKIIFLITDGYPNKSEftIVEVMEKAKCNGIEIVGVGIKTD-----EII 639
Cdd:pfam00092  73 YLGGgTTNTGKALKYALENLFSSAAgarpgAPKVVVLLTDGRSQDGD--PEEVARELKSAGVTVFAVGVGNAddeelRKI 150

                         170
                  ....*....|....*...
gi 446685354  640 GFETD--TFVTVDDTSLL 655
Cdd:pfam00092 151 ASEPGegHVFTVSDFEAL 168
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 500-634 2.07e-05

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 45.36  E-value: 2.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354 500 LVLVRDISASMANDERYIhaIKsDLALSMAaESLS----KMHVS--------NIVFPFKESEF--EIIKTFDQSVEESls 565
Cdd:cd01450    3 IVFLLDGSESVGPENFEK--VK-DFIEKLV-EKLDigpdKTRVGlvqysddvRVEFSLNDYKSkdDLLKAVKNLKYLG-- 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446685354 566 kftlgckGYYTPTGSALMAAVDLLLDSQFDR----KIIFLITDGYPNKSEfTIVEVMEKAKCNGIEIVGVGIK 634
Cdd:cd01450   77 -------GGGTNTGKALQYALEQLFSESNARenvpKVIIVLTDGRSDDGG-DPKEAAAKLKDEGIKVFVVGVG 141
NorD COG4548
Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];
500-608 5.00e-04

Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];


Pssm-ID: 443612 [Multi-domain]  Cd Length: 439  Bit Score: 43.17  E-value: 5.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354 500 LVLVrDISASM----ANDERYIHAIKSdlALSMAAESLSKMhvsNIvfPF----------KESEFEIIKTFDQS----VE 561
Cdd:COG4548  252 LLLL-DLSLSTdawvGSGRRVLDVERE--ALLLLAEALEAL---GD--PFaiygfssdgrHRVRYYRIKDFDEPyddaVR 323

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446685354 562 ESLSkftlGCK-GYYTPTGSALMAAVDLLLDSQFDRKIIFLITDGYPN 608
Cdd:COG4548  324 ARIA----GLEpGYYTRMGAAIRHATALLAAQPARRRLLLVLTDGKPN 367
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 499-634 5.47e-04

VWA YIEM 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 have a conserved MIDAS motif, however, their biochemical function is not well characterised.


Pssm-ID: 238739 [Multi-domain]  Cd Length: 152  Bit Score: 40.79  E-value: 5.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354 499 GLVLVRDISASMAND-ERYIHAIKSDLALSMAAESLSkmhVSNIVF--PFKESEFEIIKTFDQSVEeSLSKFTLGcKGyy 575
Cdd:cd01462    2 PVILLVDQSGSMYGApEEVAKAVALALLRIALAENRD---TYLILFdsEFQTKIVDKTDDLEEPVE-FLSGVQLG-GG-- 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446685354 576 TPTGSALMAAVDLLLDSQFDRKIIFLITDGYPNKSEFTIVEVMEKAKCNGIEIVGVGIK 634
Cdd:cd01462   75 TDINKALRYALELIERRDPRKADIVLITDGYEGGVSDELLREVELKRSRVARFVALALG 133
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 500-653 2.34e-03

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: 39.62  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354 500 LVLVRDISASMaNDERYIHAIKSDLALSMAAESLSKMHVSNI---VF---PFKESEFeiikTFDQ-SVEESLSKFTLGCK 572
Cdd:cd01467    5 IMIALDVSGSM-LAQDFVKPSRLEAAKEVLSDFIDRRENDRIglvVFagaAFTQAPL----TLDReSLKELLEDIKIGLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354 573 GYYTPTGSALMAAVDLLLDSQFDRKIIFLITDGYPNKSEFTIVEVMEKAKCNGIEIVGVGIKTDEIIGFETDTFVTVDDT 652
Cdd:cd01467   80 GQGTAIGDAIGLAIKRLKNSEAKERVIVLLTDGENNAGEIDPATAAELAKNKGVRIYTIGVGKSGSGPKPDGSTILDEDS 159


                 .
gi 446685354 653 S 653
Cdd:cd01467  160 L 160
VWA_2 pfam13519
von Willebrand factor type A domain;
500-602 7.17e-03

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 36.50  E-value: 7.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685354  500 LVLVRDISASMAND---ERYIHAIKSdlALSMAAESLSKMHVSNIVFpfkESEFEIIKTFDQSVEESLSKFT-LGCKGYY 575
Cdd:pfam13519   1 LVFVLDTSGSMRNGdygPTRLEAAKD--AVLALLKSLPGDRVGLVTF---GDGPEVLIPLTKDRAKILRALRrLEPKGGG 75

                          90       100
                  ....*....|....*....|....*...
gi 446685354  576 TPTGSALMAAVDLLLDSQFD-RKIIFLI 602
Cdd:pfam13519  76 TNLAAALQLARAALKHRRKNqPRRIVLI 103
 
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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