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Conserved domains on  [gi|2550877039|ref|WP_302247144|]
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DUF1194 domain-containing protein [Aeromonas veronii]

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 ...
 24-228 3.43e-62

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 pfam06707:

Pssm-ID: 469594  Cd Length: 206  Bit Score: 195.14  E-value: 3.43e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550877039  24 EVDTELQLLMDVSGSVSSSEFNLQLQGYVDAFYSQDVQSAILDTSgdkLGSIAVQMVMWSGSTQQSVMTDWFHLYDMTSI 103
Cdd:pfam06707   1 ACDLELVLAVDVSGSVDEEEYRLQRDGYAAALRDPEVLDALLAGP---HGRIAVTYFEWSGPDDQRVVVDWTVIDSAEDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550877039 104 NNFAATLDALVRPYAGMTAPGSAMAFGAQQFDTNNYTAARQVMDVSGDGIQNNGLDTST-VRDQLLASGIdTINGITIGQ 182
Cdd:pfam06707  78 EAFAARLAAAPRRAARRTAIGGALGFAAALLAQNPYECLRRVIDVSGDGPNNQGFPPVTaARDAAVAAGI-TINGLAIMG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2550877039 183 DYADGV--LQEWYVENVAGGQDAFVINATTFADFGNALELKLAAEIEG 228
Cdd:pfam06707 157 AEAPASadLDAYYRDCVIGGPGAFVEPANGFEDFAEAIRRKLVREIAG 204
 
Name Accession Description Interval E-value
DUF1194 pfam06707
Protein of unknown function (DUF1194); This family consists of several hypothetical ...
 24-228 3.43e-62

Protein of unknown function (DUF1194); This family consists of several hypothetical Rhizobiales specific proteins of around 270 residues in length. The function of this family is unknown.


Pssm-ID: 369046  Cd Length: 206  Bit Score: 195.14  E-value: 3.43e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550877039  24 EVDTELQLLMDVSGSVSSSEFNLQLQGYVDAFYSQDVQSAILDTSgdkLGSIAVQMVMWSGSTQQSVMTDWFHLYDMTSI 103
Cdd:pfam06707   1 ACDLELVLAVDVSGSVDEEEYRLQRDGYAAALRDPEVLDALLAGP---HGRIAVTYFEWSGPDDQRVVVDWTVIDSAEDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550877039 104 NNFAATLDALVRPYAGMTAPGSAMAFGAQQFDTNNYTAARQVMDVSGDGIQNNGLDTST-VRDQLLASGIdTINGITIGQ 182
Cdd:pfam06707  78 EAFAARLAAAPRRAARRTAIGGALGFAAALLAQNPYECLRRVIDVSGDGPNNQGFPPVTaARDAAVAAGI-TINGLAIMG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2550877039 183 DYADGV--LQEWYVENVAGGQDAFVINATTFADFGNALELKLAAEIEG 228
Cdd:pfam06707 157 AEAPASadLDAYYRDCVIGGPGAFVEPANGFEDFAEAIRRKLVREIAG 204
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 31-191 3.42e-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: 3.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550877039  31 LLMDVSGSVSSSEFNLQLQgYVDAFysqdVQSAILDTSGDKLGsiavqMVMWSGSTqqsvmTDWFHLYDMTSINNFAATL 110
Cdd:cd00198     5 FLLDVSGSMGGEKLDKAKE-ALKAL----VSSLSASPPGDRVG-----LVTFGSNA-----RVVLPLTTDTDKADLLEAI 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550877039 111 DALVRPYAGMTAPGSAMAFGAQQFDTNNYTAARQVMDVSGDGIQNNGLDTSTVRDQLLASGIDTINGITIGQDYADGVLQ 190
Cdd:cd00198    70 DALKKGLGGGTNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANEDELK 149


                  .
gi 2550877039 191 E 191
Cdd:cd00198   150 E 150
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 31-191 8.03e-05

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 42.44  E-value: 8.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550877039   31 LLMDVSGSVSSSEFNLQLQgYVDAFysqdVQSAILDTSGDKLGsiavqMVMWSGSTqqsvmTDWFHLYDMTSINNFAATL 110
Cdd:smart00327   4 FLLDGSGSMGGNRFELAKE-FVLKL----VEQLDIGPDGDRVG-----LVTFSDDA-----RVLFPLNDSRSKDALLEAL 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550877039  111 DALVRPYAGMTAPGSAMAFGAQQFDTNNYTA---ARQVMDVSGDGIQNNG-LDTSTVRDQLLASGIdTINGITIGQDYAD 186
Cdd:smart00327  69 ASLSYKLGGGTNLGAALQYALENLFSKSAGSrrgAPKVVILITDGESNDGpKDLLKAAKELKRSGV-KVFVVGVGNDVDE 147


                   ....*
gi 2550877039  187 GVLQE 191
Cdd:smart00327 148 EELKK 152
 
Name Accession Description Interval E-value
DUF1194 pfam06707
Protein of unknown function (DUF1194); This family consists of several hypothetical ...
 24-228 3.43e-62

Protein of unknown function (DUF1194); This family consists of several hypothetical Rhizobiales specific proteins of around 270 residues in length. The function of this family is unknown.


Pssm-ID: 369046  Cd Length: 206  Bit Score: 195.14  E-value: 3.43e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550877039  24 EVDTELQLLMDVSGSVSSSEFNLQLQGYVDAFYSQDVQSAILDTSgdkLGSIAVQMVMWSGSTQQSVMTDWFHLYDMTSI 103
Cdd:pfam06707   1 ACDLELVLAVDVSGSVDEEEYRLQRDGYAAALRDPEVLDALLAGP---HGRIAVTYFEWSGPDDQRVVVDWTVIDSAEDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550877039 104 NNFAATLDALVRPYAGMTAPGSAMAFGAQQFDTNNYTAARQVMDVSGDGIQNNGLDTST-VRDQLLASGIdTINGITIGQ 182
Cdd:pfam06707  78 EAFAARLAAAPRRAARRTAIGGALGFAAALLAQNPYECLRRVIDVSGDGPNNQGFPPVTaARDAAVAAGI-TINGLAIMG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2550877039 183 DYADGV--LQEWYVENVAGGQDAFVINATTFADFGNALELKLAAEIEG 228
Cdd:pfam06707 157 AEAPASadLDAYYRDCVIGGPGAFVEPANGFEDFAEAIRRKLVREIAG 204
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 31-191 3.42e-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: 3.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550877039  31 LLMDVSGSVSSSEFNLQLQgYVDAFysqdVQSAILDTSGDKLGsiavqMVMWSGSTqqsvmTDWFHLYDMTSINNFAATL 110
Cdd:cd00198     5 FLLDVSGSMGGEKLDKAKE-ALKAL----VSSLSASPPGDRVG-----LVTFGSNA-----RVVLPLTTDTDKADLLEAI 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550877039 111 DALVRPYAGMTAPGSAMAFGAQQFDTNNYTAARQVMDVSGDGIQNNGLDTSTVRDQLLASGIDTINGITIGQDYADGVLQ 190
Cdd:cd00198    70 DALKKGLGGGTNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANEDELK 149


                  .
gi 2550877039 191 E 191
Cdd:cd00198   150 E 150
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 31-191 8.03e-05

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 42.44  E-value: 8.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550877039   31 LLMDVSGSVSSSEFNLQLQgYVDAFysqdVQSAILDTSGDKLGsiavqMVMWSGSTqqsvmTDWFHLYDMTSINNFAATL 110
Cdd:smart00327   4 FLLDGSGSMGGNRFELAKE-FVLKL----VEQLDIGPDGDRVG-----LVTFSDDA-----RVLFPLNDSRSKDALLEAL 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550877039  111 DALVRPYAGMTAPGSAMAFGAQQFDTNNYTA---ARQVMDVSGDGIQNNG-LDTSTVRDQLLASGIdTINGITIGQDYAD 186
Cdd:smart00327  69 ASLSYKLGGGTNLGAALQYALENLFSKSAGSrrgAPKVVILITDGESNDGpKDLLKAAKELKRSGV-KVFVVGVGNDVDE 147


                   ....*
gi 2550877039  187 GVLQE 191
Cdd:smart00327 148 EELKK 152
VWA pfam00092
von Willebrand factor type A domain;
31-184 1.21e-03

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 38.80  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550877039  31 LLMDVSGSVSSSEFNLQLQgyvdaFYSQDVQSAILDTSGDKLGsiavqMVMWSGSTqqsvmTDWFHLYDMTSINNFAATL 110
Cdd:pfam00092   4 FLLDGSGSIGGDNFEKVKE-----FLKKLVESLDIGPDGTRVG-----LVQYSSDV-----RTEFPLNDYSSKEELLSAV 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2550877039 111 DALVRPYAGMTAPGSAMAFGAQQFDT---NNYTAARQVMDVSGDGiQNNGLDTSTVRDQLLASGIdTINGITIGQDY 184
Cdd:pfam00092  69 DNLRYLGGGTTNTGKALKYALENLFSsaaGARPGAPKVVVLLTDG-RSQDGDPEEVARELKSAGV-TVFAVGVGNAD 143
 
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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