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Conserved domains on  [gi|567353299|gb|AHC85496|]
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von Willebrand factor A [Pseudomonas monteilii SB3078]

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 ...
 198-392 1.72e-16

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 cd01456:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 206  Bit Score: 77.47  E-value: 1.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567353299 198 QPPEFSVVLDTSGSMllnvAATPEDEKwffqhinddpnidqqrvaqltqapIRMDVAKSSLTHLINDLHPAVDMRVVTFD 277
Cdd:cd01456   19 LPPNVAIVLDNSGSM----REVDGGGE------------------------TRLDNAKAALDETANALPDGTRLGLWTFS 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567353299 278 G------------CRAPLDHGV--FKLAQRPALIEGIQAL-VPNDGTALAASLDMTArTMNGRDRDGMILMFIDGADGCE 342
Cdd:cd01456   71 GdgdnpldvrvlvPKGCLTAPVngFPSAQRSALDAALNSLqTPTGWTPLAAALAEAA-AYVDPGRVNVVVLITDGEDTCG 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 567353299 343 QDVCAVAQRIAREQ---PRLRVNLINI---SNSNLASCVAENTGGR-IYSANDAEQI 392
Cdd:cd01456  150 PDPCEVARELAKRRtpaPPIKVNVIDFggdADRAELEAIAEATGGTyAYNQSDLASL 206
 
Name Accession Description Interval E-value
vWA_ywmD_type cd01456
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 198-392 1.72e-16

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: 77.47  E-value: 1.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567353299 198 QPPEFSVVLDTSGSMllnvAATPEDEKwffqhinddpnidqqrvaqltqapIRMDVAKSSLTHLINDLHPAVDMRVVTFD 277
Cdd:cd01456   19 LPPNVAIVLDNSGSM----REVDGGGE------------------------TRLDNAKAALDETANALPDGTRLGLWTFS 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567353299 278 G------------CRAPLDHGV--FKLAQRPALIEGIQAL-VPNDGTALAASLDMTArTMNGRDRDGMILMFIDGADGCE 342
Cdd:cd01456   71 GdgdnpldvrvlvPKGCLTAPVngFPSAQRSALDAALNSLqTPTGWTPLAAALAEAA-AYVDPGRVNVVVLITDGEDTCG 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 567353299 343 QDVCAVAQRIAREQ---PRLRVNLINI---SNSNLASCVAENTGGR-IYSANDAEQI 392
Cdd:cd01456  150 PDPCEVARELAKRRtpaPPIKVNVIDFggdADRAELEAIAEATGGTyAYNQSDLASL 206
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 204-399 3.91e-14

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: 71.89  E-value: 3.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567353299 204 VVLDTSGSMllnvaatpedekwffqhinddpnidqqrvaqltQAPIRMDVAKSSLTHLINDLHPAVDMRVVTFDGcRA-- 281
Cdd:COG1240   97 LVVDASGSM---------------------------------AAENRLEAAKGALLDFLDDYRPRDRVGLVAFGG-EAev 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567353299 282 --PLDHgvfklaQRPALIEGIQALVPNDGTALAASLDMTARTMNGRDRDGMILMFI--DGADGC-EQDVCAVAQRIAREq 356
Cdd:COG1240  143 llPLTR------DREALKRALDELPPGGGTPLGDALALALELLKRADPARRKVIVLltDGRDNAgRIDPLEAAELAAAA- 215

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 567353299 357 pRLRVNLINIS----NSNLASCVAENTGGRIYSANDAEQIAAALKDA 399
Cdd:COG1240  216 -GIRIYTIGVGteavDEGLLREIAEATGGRYFRADDLSELAAIYREI 261
 
Name Accession Description Interval E-value
vWA_ywmD_type cd01456
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 198-392 1.72e-16

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: 77.47  E-value: 1.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567353299 198 QPPEFSVVLDTSGSMllnvAATPEDEKwffqhinddpnidqqrvaqltqapIRMDVAKSSLTHLINDLHPAVDMRVVTFD 277
Cdd:cd01456   19 LPPNVAIVLDNSGSM----REVDGGGE------------------------TRLDNAKAALDETANALPDGTRLGLWTFS 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567353299 278 G------------CRAPLDHGV--FKLAQRPALIEGIQAL-VPNDGTALAASLDMTArTMNGRDRDGMILMFIDGADGCE 342
Cdd:cd01456   71 GdgdnpldvrvlvPKGCLTAPVngFPSAQRSALDAALNSLqTPTGWTPLAAALAEAA-AYVDPGRVNVVVLITDGEDTCG 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 567353299 343 QDVCAVAQRIAREQ---PRLRVNLINI---SNSNLASCVAENTGGR-IYSANDAEQI 392
Cdd:cd01456  150 PDPCEVARELAKRRtpaPPIKVNVIDFggdADRAELEAIAEATGGTyAYNQSDLASL 206
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 204-399 3.91e-14

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: 71.89  E-value: 3.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567353299 204 VVLDTSGSMllnvaatpedekwffqhinddpnidqqrvaqltQAPIRMDVAKSSLTHLINDLHPAVDMRVVTFDGcRA-- 281
Cdd:COG1240   97 LVVDASGSM---------------------------------AAENRLEAAKGALLDFLDDYRPRDRVGLVAFGG-EAev 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567353299 282 --PLDHgvfklaQRPALIEGIQALVPNDGTALAASLDMTARTMNGRDRDGMILMFI--DGADGC-EQDVCAVAQRIAREq 356
Cdd:COG1240  143 llPLTR------DREALKRALDELPPGGGTPLGDALALALELLKRADPARRKVIVLltDGRDNAgRIDPLEAAELAAAA- 215

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 567353299 357 pRLRVNLINIS----NSNLASCVAENTGGRIYSANDAEQIAAALKDA 399
Cdd:COG1240  216 -GIRIYTIGVGteavDEGLLREIAEATGGRYFRADDLSELAAIYREI 261
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 202-355 8.65e-06

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


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 45.73  E-value: 8.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567353299 202 FSVVLDTSGSMllnvaatpedekwffqhinDDPNIDQqrvaqltqapirmdvAKSSLTHLINDLHPAVDMRVVTFDGcRA 281
Cdd:cd01465    3 LVFVIDRSGSM-------------------DGPKLPL---------------VKSALKLLVDQLRPDDRLAIVTYDG-AA 47

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567353299 282 PLDHGVFKLAQRPALIEGIQALVPNDGTALAASLDM---TARTMNGRDRDGMILMFIDG-ADGCEQDVCAVAQRIARE 355
Cdd:cd01465   48 ETVLPATPVRDKAAILAAIDRLTAGGSTAGGAGIQLgyqEAQKHFVPGGVNRILLATDGdFNVGETDPDELARLVAQK 125
 
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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