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Conserved domains on  [gi|489336565|ref|WP_003243782|]
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MULTISPECIES: VWA domain-containing protein [Bacillus]

Protein Classification

VWA domain-containing protein( domain architecture ID 11455327)

VWA (von Willebrand factor type A) domain-containing protein similar to Bacillus subtilis uncharacterized protein YabS

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ChlD super family cl34203
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 9-84 6.94e-10

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


The actual alignment was detected with superfamily member COG1240:

Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 57.64  E-value: 6.94e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489336565   9 ILLITDGCSNHG-EDPLAMAAFAKEQGITVNVIGIMEEnQIDPEAMKEvegIALAGGGvhQVVYASQLSQTVQMVTK 84
Cdd:COG1240  190 IVLLTDGRDNAGrIDPLEAAELAAAAGIRIYTIGVGTE-AVDEGLLRE---IAEATGG--RYFRADDLSELAAIYRE 260
ChlD super family cl34203
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 135-230 5.77e-09

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


The actual alignment was detected with superfamily member COG1240:

Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 54.94  E-value: 5.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336565 135 VLVLVDTSASMA--PKLPTVKEALIDLsvsLNSRIGNNEFAMCIFPGkkqEVELVLNWTPKLQSLSTLFAKLSTGGITPT 212
Cdd:COG1240   95 VVLVVDASGSMAaeNRLEAAKGALLDF---LDDYRPRDRVGLVAFGG---EAEVLLPLTRDREALKRALDELPPGGGTPL 168

                         90
                 ....*....|....*...
gi 489336565 213 GPAIREATLQFEKIRSRR 230
Cdd:COG1240  169 GDALALALELLKRADPAR 186
 
Name Accession Description Interval E-value
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 9-84 6.94e-10

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 57.64  E-value: 6.94e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489336565   9 ILLITDGCSNHG-EDPLAMAAFAKEQGITVNVIGIMEEnQIDPEAMKEvegIALAGGGvhQVVYASQLSQTVQMVTK 84
Cdd:COG1240  190 IVLLTDGRDNAGrIDPLEAAELAAAAGIRIYTIGVGTE-AVDEGLLRE---IAEATGG--RYFRADDLSELAAIYRE 260
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 135-230 5.77e-09

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: 54.94  E-value: 5.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336565 135 VLVLVDTSASMA--PKLPTVKEALIDLsvsLNSRIGNNEFAMCIFPGkkqEVELVLNWTPKLQSLSTLFAKLSTGGITPT 212
Cdd:COG1240   95 VVLVVDASGSMAaeNRLEAAKGALLDF---LDDYRPRDRVGLVAFGG---EAEVLLPLTRDREALKRALDELPPGGGTPL 168

                         90
                 ....*....|....*...
gi 489336565 213 GPAIREATLQFEKIRSRR 230
Cdd:COG1240  169 GDALALALELLKRADPAR 186
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 135-231 9.94e-07

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: 47.45  E-value: 9.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336565   135 VLVLVDTSASMAP-KLPTVKEALIDLSVSLNSRIGNNEFAMCIFpGKKQEVELVLNWTPKLQSLSTLFAKLS--TGGITP 211
Cdd:smart00327   2 VVFLLDGSGSMGGnRFELAKEFVLKLVEQLDIGPDGDRVGLVTF-SDDARVLFPLNDSRSKDALLEALASLSykLGGGTN 80

                           90       100
                   ....*....|....*....|..
gi 489336565   212 TGPAIREATLQF--EKIRSRRG 231
Cdd:smart00327  81 LGAALQYALENLfsKSAGSRRG 102
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 135-231 3.20e-06

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: 46.02  E-value: 3.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336565 135 VLVLVDTSASMAP-KLPTVKEALIDLSVSLNSRIGNNEFAMCIFpGKKQEVELVLNWTPKLQSLSTLFAKL--STGGITP 211
Cdd:cd00198    3 IVFLLDVSGSMGGeKLDKAKEALKALVSSLSASPPGDRVGLVTF-GSNARVVLPLTTDTDKADLLEAIDALkkGLGGGTN 81

                         90       100
                 ....*....|....*....|
gi 489336565 212 TGPAIREATLQFEKIRSRRG 231
Cdd:cd00198   82 IGAALRLALELLKSAKRPNA 101
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 9-69 1.32e-04

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: 41.29  E-value: 1.32e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489336565     9 ILLITDGCSNHGEDPLAMAA-FAKEQGITVNVIGImeENQIDPEAMKEvegIALAGGGVHQV 69
Cdd:smart00327 107 VILITDGESNDGPKDLLKAAkELKRSGVKVFVVGV--GNDVDEEELKK---LASAPGGVYVF 163
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 1-79 1.54e-04

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: 41.10  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336565   1 MNNGHLNQILLITDGCSNHGE-DP---LAMAAFAKEQGITVNVIGIMEEnqIDPEAMkevEGIALAGGGVHQVVYASQLS 76
Cdd:cd01465   92 FVPGGVNRILLATDGDFNVGEtDPdelARLVAQKRESGITLSTLGFGDN--YNEDLM---EAIADAGNGNTAYIDNLAEA 166


                 ...
gi 489336565  77 QTV 79
Cdd:cd01465  167 RKV 169
VWA pfam00092
von Willebrand factor type A domain;
9-67 2.02e-03

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 38.02  E-value: 2.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489336565    9 ILLITDGcSNHGEDPLAMAAFAKEQGITVNVIGImeeNQIDPEAMKEvegIALAGGGVH 67
Cdd:pfam00092 107 VVLLTDG-RSQDGDPEEVARELKSAGVTVFAVGV---GNADDEELRK---IASEPGEGH 158
VWA_2 pfam13519
von Willebrand factor type A domain;
135-232 3.10e-03

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 36.12  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336565  135 VLVLVDTSASMAPK--LPTVKEALIDLSVSLNSRIGNNEFAMCIFpgkKQEVELVLNWTpklQSLSTLFAKLS----TGG 208
Cdd:pfam13519   1 LVFVLDTSGSMRNGdyGPTRLEAAKDAVLALLKSLPGDRVGLVTF---GDGPEVLIPLT---KDRAKILRALRrlepKGG 74

                          90       100
                  ....*....|....*....|....
gi 489336565  209 ITPTGPAIREATLQFEKIRSRRGM 232
Cdd:pfam13519  75 GTNLAAALQLARAALKHRRKNQPR 98
 
Name Accession Description Interval E-value
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 9-84 6.94e-10

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 57.64  E-value: 6.94e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489336565   9 ILLITDGCSNHG-EDPLAMAAFAKEQGITVNVIGIMEEnQIDPEAMKEvegIALAGGGvhQVVYASQLSQTVQMVTK 84
Cdd:COG1240  190 IVLLTDGRDNAGrIDPLEAAELAAAAGIRIYTIGVGTE-AVDEGLLRE---IAEATGG--RYFRADDLSELAAIYRE 260
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 135-230 5.77e-09

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: 54.94  E-value: 5.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336565 135 VLVLVDTSASMA--PKLPTVKEALIDLsvsLNSRIGNNEFAMCIFPGkkqEVELVLNWTPKLQSLSTLFAKLSTGGITPT 212
Cdd:COG1240   95 VVLVVDASGSMAaeNRLEAAKGALLDF---LDDYRPRDRVGLVAFGG---EAEVLLPLTRDREALKRALDELPPGGGTPL 168

                         90
                 ....*....|....*...
gi 489336565 213 GPAIREATLQFEKIRSRR 230
Cdd:COG1240  169 GDALALALELLKRADPAR 186
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 135-231 9.94e-07

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: 47.45  E-value: 9.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336565   135 VLVLVDTSASMAP-KLPTVKEALIDLSVSLNSRIGNNEFAMCIFpGKKQEVELVLNWTPKLQSLSTLFAKLS--TGGITP 211
Cdd:smart00327   2 VVFLLDGSGSMGGnRFELAKEFVLKLVEQLDIGPDGDRVGLVTF-SDDARVLFPLNDSRSKDALLEALASLSykLGGGTN 80

                           90       100
                   ....*....|....*....|..
gi 489336565   212 TGPAIREATLQF--EKIRSRRG 231
Cdd:smart00327  81 LGAALQYALENLfsKSAGSRRG 102
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 135-231 3.20e-06

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: 46.02  E-value: 3.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336565 135 VLVLVDTSASMAP-KLPTVKEALIDLSVSLNSRIGNNEFAMCIFpGKKQEVELVLNWTPKLQSLSTLFAKL--STGGITP 211
Cdd:cd00198    3 IVFLLDVSGSMGGeKLDKAKEALKALVSSLSASPPGDRVGLVTF-GSNARVVLPLTTDTDKADLLEAIDALkkGLGGGTN 81

                         90       100
                 ....*....|....*....|
gi 489336565 212 TGPAIREATLQFEKIRSRRG 231
Cdd:cd00198   82 IGAALRLALELLKSAKRPNA 101
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 4-67 5.59e-06

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 46.25  E-value: 5.59e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489336565   4 GHLNQILLITDGCSNHG----EDPLAMAAFAKEQGITVNVIGI-MEENQidpeamKEVEGIALAGGGVH 67
Cdd:COG2304  186 GRVNRVILLTDGDANVGitdpEELLKLAEEAREEGITLTTLGVgSDYNE------DLLERLADAGGGNY 248
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 9-69 1.32e-04

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: 41.29  E-value: 1.32e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489336565     9 ILLITDGCSNHGEDPLAMAA-FAKEQGITVNVIGImeENQIDPEAMKEvegIALAGGGVHQV 69
Cdd:smart00327 107 VILITDGESNDGPKDLLKAAkELKRSGVKVFVVGV--GNDVDEEELKK---LASAPGGVYVF 163
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 1-79 1.54e-04

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: 41.10  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336565   1 MNNGHLNQILLITDGCSNHGE-DP---LAMAAFAKEQGITVNVIGIMEEnqIDPEAMkevEGIALAGGGVHQVVYASQLS 76
Cdd:cd01465   92 FVPGGVNRILLATDGDFNVGEtDPdelARLVAQKRESGITLSTLGFGDN--YNEDLM---EAIADAGNGNTAYIDNLAEA 166


                 ...
gi 489336565  77 QTV 79
Cdd:cd01465  167 RKV 169
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 9-42 4.49e-04

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: 40.01  E-value: 4.49e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 489336565   9 ILLITDGCSNHGE-DPLAMAAFAKEQGITVNVIGI 42
Cdd:cd01467  106 IVLLTDGENNAGEiDPATAAELAKNKGVRIYTIGV 140
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
135-225 5.53e-04

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 39.91  E-value: 5.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336565 135 VLVLVDTSASMA-PKLPTVKEALIDLSvslnSRIGNNEFA-----MCI--FPGkkqEVELVLNWTPkLQSLStlFAKLST 206
Cdd:COG4245    8 VYLLLDTSGSMSgEPIEALNEGLQALI----DELRQDPYAletveVSVitFDG---EAKVLLPLTD-LEDFQ--PPDLSA 77

                         90
                 ....*....|....*....
gi 489336565 207 GGITPTGPAIREATLQFEK 225
Cdd:COG4245   78 SGGTPLGAALELLLDLIER 96
NorD COG4548
Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];
133-230 1.36e-03

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


Pssm-ID: 443612 [Multi-domain]  Cd Length: 439  Bit Score: 39.32  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336565 133 LQVLVLVDTSASMAPKLP---TV----KEALIDLSVSLNSrIGNNeFAMCIFPGKK-QEVELVL------NWTPKlqsls 198
Cdd:COG4548  249 LAVLLLLDLSLSTDAWVGsgrRVldveREALLLLAEALEA-LGDP-FAIYGFSSDGrHRVRYYRikdfdePYDDA----- 321

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489336565 199 tlfAKLSTGGITP---T--GPAIREATLQFEKIRSRR 230
Cdd:COG4548  322 ---VRARIAGLEPgyyTrmGAAIRHATALLAAQPARR 355
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 129-236 1.41e-03

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 38.93  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336565 129 ETVHLQVLVLVDTSASMA-PKLPTVKEALIDLSVSLNSrigNNEFAMCIFPGkkqEVELVLNWTP---KLQSLSTLfAKL 204
Cdd:COG2304   88 ERPPLNLVFVIDVSGSMSgDKLELAKEAAKLLVDQLRP---GDRVSIVTFAG---DARVLLPPTPatdRAKILAAI-DRL 160

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489336565 205 STGGITPTGPAIREATLQFEKI----RSRRGMLADD 236
Cdd:COG2304  161 QAGGGTALGAGLELAYELARKHfipgRVNRVILLTD 196
VWA pfam00092
von Willebrand factor type A domain;
9-67 2.02e-03

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 38.02  E-value: 2.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489336565    9 ILLITDGcSNHGEDPLAMAAFAKEQGITVNVIGImeeNQIDPEAMKEvegIALAGGGVH 67
Cdd:pfam00092 107 VVLLTDG-RSQDGDPEEVARELKSAGVTVFAVGV---GNADDEELRK---IASEPGEGH 158
vWA_ywmD_type cd01456
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 3-65 2.42e-03

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: 37.79  E-value: 2.42e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489336565   3 NGHLNQILLITDGCSNHGEDPLAMAA-FAKEQ----GITVNVIGimeenqIDPEAMKEV-EGIALAGGG 65
Cdd:cd01456  132 PGRVNVVVLITDGEDTCGPDPCEVAReLAKRRtpapPIKVNVID------FGGDADRAElEAIAEATGG 194
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 135-235 2.73e-03

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 38.12  E-value: 2.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336565 135 VLVLVDTSASMA-PKLPTVKEALIDLsvsLNSRIGNNEFAMCIFpGKKQEVELVLNWTPKLQSLSTLFAKLSTGGITPTG 213
Cdd:COG2425  121 VVLCVDTSGSMAgSKEAAAKAAALAL---LRALRPNRRFGVILF-DTEVVEDLPLTADDGLEDAIEFLSGLFAGGGTDIA 196

                         90       100
                 ....*....|....*....|..
gi 489336565 214 PAIREAtlqFEKIRSRRGMLAD 235
Cdd:COG2425  197 PALRAA---LELLEEPDYRNAD 215
VWA_2 pfam13519
von Willebrand factor type A domain;
135-232 3.10e-03

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 36.12  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336565  135 VLVLVDTSASMAPK--LPTVKEALIDLSVSLNSRIGNNEFAMCIFpgkKQEVELVLNWTpklQSLSTLFAKLS----TGG 208
Cdd:pfam13519   1 LVFVLDTSGSMRNGdyGPTRLEAAKDAVLALLKSLPGDRVGLVTF---GDGPEVLIPLT---KDRAKILRALRrlepKGG 74

                          90       100
                  ....*....|....*....|....
gi 489336565  209 ITPTGPAIREATLQFEKIRSRRGM 232
Cdd:pfam13519  75 GTNLAAALQLARAALKHRRKNQPR 98
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 136-236 3.66e-03

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


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 37.25  E-value: 3.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336565 136 LVLV-DTSASMA-PKLPTVKEALIDLSVSLNSrigNNEFAMCIFPGkkqEVELVLNWTPK--LQSLSTLFAKLSTGGITP 211
Cdd:cd01465    3 LVFViDRSGSMDgPKLPLVKSALKLLVDQLRP---DDRLAIVTYDG---AAETVLPATPVrdKAAILAAIDRLTAGGSTA 76

                         90       100
                 ....*....|....*....|....*....
gi 489336565 212 TGP----AIREATLQFEKIRSRRGMLADD 236
Cdd:cd01465   77 GGAgiqlGYQEAQKHFVPGGVNRILLATD 105
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 9-69 4.88e-03

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 36.78  E-value: 4.88e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489336565   9 ILLITDGCSNHG-EDPLAMAAFAKEQGITVNVIGImeenqIDPEAMKEVEGIALAGGGVHQV 69
Cdd:cd00198  105 IILLTDGEPNDGpELLAEAARELRKLGITVYTIGI-----GDDANEDELKEIADKTTGGAVF 161
 
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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