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Conserved domains on  [gi|1039822623|ref|WP_064981703|]
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MULTISPECIES: DUF1194 domain-containing protein [Mesorhizobium]

Protein Classification

DUF1194 domain-containing protein( domain architecture ID 10535474)

DUF1194 domain-containing protein belongs to the vWA (von Willebrand factor type A) domain superfamily

CATH:  3.40.50.410
PubMed:  10830113|12388743|12579041
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF1194 pfam06707
Protein of unknown function (DUF1194); This family consists of several hypothetical ...
 27-230 7.87e-105

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: 302.61  E-value: 7.87e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039822623  27 AVDVELVLAVDISLSMDEKEFALQRAGYVEALRHPDFIQAVRSGNTGRIAIAYFEWAGTVRDDAVIDWQIIDGAQSANSF 106
Cdd:pfam06707   1 ACDLELVLAVDVSGSVDEEEYRLQRDGYAAALRDPEVLDALLAGPHGRIAVTYFEWSGPDDQRVVVDWTVIDSAEDAEAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039822623 107 ADKVAARPFRSFRGTSISTAIAFGTELFGRTNFAGERSVIDMSGDGPNNIG-PPVTATRDAATAKGIVINGLPILINPSP 185
Cdd:pfam06707  81 AARLAAAPRRAARRTAIGGALGFAAALLAQNPYECLRRVIDVSGDGPNNQGfPPVTAARDAAVAAGITINGLAIMGAEAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1039822623 186 TFKHLDQYYAQCVTGGPGSFVLPIYSAAEFSTAIRRKLILEVSGI 230
Cdd:pfam06707 161 ASADLDAYYRDCVIGGPGAFVEPANGFEDFAEAIRRKLVREIAGL 205
 
Name Accession Description Interval E-value
DUF1194 pfam06707
Protein of unknown function (DUF1194); This family consists of several hypothetical ...
 27-230 7.87e-105

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: 302.61  E-value: 7.87e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039822623  27 AVDVELVLAVDISLSMDEKEFALQRAGYVEALRHPDFIQAVRSGNTGRIAIAYFEWAGTVRDDAVIDWQIIDGAQSANSF 106
Cdd:pfam06707   1 ACDLELVLAVDVSGSVDEEEYRLQRDGYAAALRDPEVLDALLAGPHGRIAVTYFEWSGPDDQRVVVDWTVIDSAEDAEAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039822623 107 ADKVAARPFRSFRGTSISTAIAFGTELFGRTNFAGERSVIDMSGDGPNNIG-PPVTATRDAATAKGIVINGLPILINPSP 185
Cdd:pfam06707  81 AARLAAAPRRAARRTAIGGALGFAAALLAQNPYECLRRVIDVSGDGPNNQGfPPVTAARDAAVAAGITINGLAIMGAEAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1039822623 186 TFKHLDQYYAQCVTGGPGSFVLPIYSAAEFSTAIRRKLILEVSGI 230
Cdd:pfam06707 161 ASADLDAYYRDCVIGGPGAFVEPANGFEDFAEAIRRKLVREIAGL 205
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 30-175 3.90e-06

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: 46.17  E-value: 3.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039822623  30 VELVLAVDISLSMDEKEFALQ-RagyVEALRH--PDFIQAvRSGNtgRIAIAYFEwagtvrDDAVIDWQIIDGAQSANSF 106
Cdd:cd01467     3 RDIMIALDVSGSMLAQDFVKPsR---LEAAKEvlSDFIDR-REND--RIGLVVFA------GAAFTQAPLTLDRESLKEL 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039822623 107 ADKVAarPFRSFRGTSISTAIAFGTELFgRTNFAGERSVIDMSgDGPNNIG--PPVTATrDAATAKGIVIN 175
Cdd:cd01467    71 LEDIK--IGLAGQGTAIGDAIGLAIKRL-KNSEAKERVIVLLT-DGENNAGeiDPATAA-ELAKNKGVRIY 136
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 32-134 8.84e-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: 38.97  E-value: 8.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039822623   32 LVLAVDISLSMDEKEFALQRAgYVEalrhpDFIQAVRSGNTG-RIAIAYFewagtvrDDAVIDWQIIDGAQSANSFADKV 110
Cdd:smart00327   2 VVFLLDGSGSMGGNRFELAKE-FVL-----KLVEQLDIGPDGdRVGLVTF-------SDDARVLFPLNDSRSKDALLEAL 68

                           90       100
                   ....*....|....*....|....
gi 1039822623  111 AARPFRSFRGTSISTAIAFGTELF 134
Cdd:smart00327  69 ASLSYKLGGGTNLGAALQYALENL 92
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 2-175 1.76e-03

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: 38.77  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039822623   2 LDALRLLACLACVQPTPVASPSGALAVDVelVLAVDISLSMDEKEfALQRAgyVEALRhpDFIQAVRSGNtgRIAIAYFe 81
Cdd:COG1240    67 LLLLAVLLLLLALALAPLALARPQRGRDV--VLVVDASGSMAAEN-RLEAA--KGALL--DFLDDYRPRD--RVGLVAF- 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039822623  82 wagtvRDDAVIDWQIIDGAQSANSFADKVAARPfrsfrGTSISTAIAFGTELFGRTNFAGERSVIDMSgDGPNNIGP--P 159
Cdd:COG1240   137 -----GGEAEVLLPLTRDREALKRALDELPPGG-----GTPLGDALALALELLKRADPARRKVIVLLT-DGRDNAGRidP 205

                         170
                  ....*....|....*.
gi 1039822623 160 VTATRDAAtAKGIVIN 175
Cdd:COG1240   206 LEAAELAA-AAGIRIY 220
 
Name Accession Description Interval E-value
DUF1194 pfam06707
Protein of unknown function (DUF1194); This family consists of several hypothetical ...
 27-230 7.87e-105

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: 302.61  E-value: 7.87e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039822623  27 AVDVELVLAVDISLSMDEKEFALQRAGYVEALRHPDFIQAVRSGNTGRIAIAYFEWAGTVRDDAVIDWQIIDGAQSANSF 106
Cdd:pfam06707   1 ACDLELVLAVDVSGSVDEEEYRLQRDGYAAALRDPEVLDALLAGPHGRIAVTYFEWSGPDDQRVVVDWTVIDSAEDAEAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039822623 107 ADKVAARPFRSFRGTSISTAIAFGTELFGRTNFAGERSVIDMSGDGPNNIG-PPVTATRDAATAKGIVINGLPILINPSP 185
Cdd:pfam06707  81 AARLAAAPRRAARRTAIGGALGFAAALLAQNPYECLRRVIDVSGDGPNNQGfPPVTAARDAAVAAGITINGLAIMGAEAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1039822623 186 TFKHLDQYYAQCVTGGPGSFVLPIYSAAEFSTAIRRKLILEVSGI 230
Cdd:pfam06707 161 ASADLDAYYRDCVIGGPGAFVEPANGFEDFAEAIRRKLVREIAGL 205
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 30-175 3.90e-06

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: 46.17  E-value: 3.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039822623  30 VELVLAVDISLSMDEKEFALQ-RagyVEALRH--PDFIQAvRSGNtgRIAIAYFEwagtvrDDAVIDWQIIDGAQSANSF 106
Cdd:cd01467     3 RDIMIALDVSGSMLAQDFVKPsR---LEAAKEvlSDFIDR-REND--RIGLVVFA------GAAFTQAPLTLDRESLKEL 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039822623 107 ADKVAarPFRSFRGTSISTAIAFGTELFgRTNFAGERSVIDMSgDGPNNIG--PPVTATrDAATAKGIVIN 175
Cdd:cd01467    71 LEDIK--IGLAGQGTAIGDAIGLAIKRL-KNSEAKERVIVLLT-DGENNAGeiDPATAA-ELAKNKGVRIY 136
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 30-192 3.34e-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: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 43.32  E-value: 3.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039822623  30 VELVLAVDISLSMDEKEFALQRagyvEALRHpdFIQAVRSGNTG-RIAIAYFewagtvrDDAVIDWQIIDGAQSANSFAD 108
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAK----EALKA--LVSSLSASPPGdRVGLVTF-------GSNARVVLPLTTDTDKADLLE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039822623 109 KVAARPFRSFRGTSISTAIAFGTELFGRTNFAGERSVIDMSGDGPNNIGPPvTATRDAATAKGIVINGLPILINPSPTFK 188
Cdd:cd00198    68 AIDALKKGLGGGTNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPE-LLAEAARELRKLGITVYTIGIGDDANED 146


                  ....
gi 1039822623 189 HLDQ 192
Cdd:cd00198   147 ELKE 150
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 32-134 8.84e-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: 38.97  E-value: 8.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039822623   32 LVLAVDISLSMDEKEFALQRAgYVEalrhpDFIQAVRSGNTG-RIAIAYFewagtvrDDAVIDWQIIDGAQSANSFADKV 110
Cdd:smart00327   2 VVFLLDGSGSMGGNRFELAKE-FVL-----KLVEQLDIGPDGdRVGLVTF-------SDDARVLFPLNDSRSKDALLEAL 68

                           90       100
                   ....*....|....*....|....
gi 1039822623  111 AARPFRSFRGTSISTAIAFGTELF 134
Cdd:smart00327  69 ASLSYKLGGGTNLGAALQYALENL 92
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 2-175 1.76e-03

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: 38.77  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039822623   2 LDALRLLACLACVQPTPVASPSGALAVDVelVLAVDISLSMDEKEfALQRAgyVEALRhpDFIQAVRSGNtgRIAIAYFe 81
Cdd:COG1240    67 LLLLAVLLLLLALALAPLALARPQRGRDV--VLVVDASGSMAAEN-RLEAA--KGALL--DFLDDYRPRD--RVGLVAF- 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039822623  82 wagtvRDDAVIDWQIIDGAQSANSFADKVAARPfrsfrGTSISTAIAFGTELFGRTNFAGERSVIDMSgDGPNNIGP--P 159
Cdd:COG1240   137 -----GGEAEVLLPLTRDREALKRALDELPPGG-----GTPLGDALALALELLKRADPARRKVIVLLT-DGRDNAGRidP 205

                         170
                  ....*....|....*.
gi 1039822623 160 VTATRDAAtAKGIVIN 175
Cdd:COG1240   206 LEAAELAA-AAGIRIY 220
 
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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