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Conserved domains on  [gi|1005580185|ref|WP_061671620|]
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MULTISPECIES: ProQ/FINO family protein [Enterobacteriaceae]

Protein Classification

RNA chaperone ProQ( domain architecture ID 10083255)

RNA chaperone ProQ controls levels of the transporter ProP, which mediates osmolyte accumulation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FinO_conjug_rep cd00236
FinO bacterial conjugation repressor domain; the basic protein FinO is part of the the two ...
 47-200 1.48e-60

FinO bacterial conjugation repressor domain; the basic protein FinO is part of the the two component FinOP system which is responsible for repressing bacterial conjugation; the FinOP system represses the transfer (tra) operon of the F-plasmid which encodes the proteins responsible for conjugative transfer of this plasmid from host to recipient Escherichia coli cells; antisense RNA, FinP is thought to interact with traJ mRNA to occlude its ribosome binding site, blocking traJ translation and thereby inhibiting transcription of the tra operon; FinO protects FinP against degradation by binding to FinP and sterically blocking the cellular endonuclease RNase E; FinO also also binds to the complementary stem-loop structures in traJ mRNA and promotes duplex formation between FinP and traJ RNA in vitro; this domain contains two independent RNA binding regions


:

Pssm-ID: 238145  Cd Length: 146  Bit Score: 185.87  E-value: 1.48e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005580185  47 AGINSSAVETHIPEAPARKKKKKRHRFPRPSHW-TREYTHECVEKIkalFPHLRAEGGgFIPLKIGINNDISAFLAEHPE 125
Cdd:cd00236     1 VGKNKLAEKADREAELAAKKKPARQALSIYLNLpTVEYAVECLKKW---FPGLFPGDT-PRLLKCGIKDGILQDVAQHPN 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005580185 126 TELTMDEWLCAVSCITSRRVYLQRTaVAGVPRYGLDGHPKGQVSdseaQSAGRRLATLEQKWLRMQAQQENISGQ 200
Cdd:cd00236    77 IPLTHEELRCAVKAITRRESYLQAM-VAGAPRYDLEGYVAGHIS----QEAEVYAARLLDKIRRQQRIKKELKRV 146
 
Name Accession Description Interval E-value
FinO_conjug_rep cd00236
FinO bacterial conjugation repressor domain; the basic protein FinO is part of the the two ...
 47-200 1.48e-60

FinO bacterial conjugation repressor domain; the basic protein FinO is part of the the two component FinOP system which is responsible for repressing bacterial conjugation; the FinOP system represses the transfer (tra) operon of the F-plasmid which encodes the proteins responsible for conjugative transfer of this plasmid from host to recipient Escherichia coli cells; antisense RNA, FinP is thought to interact with traJ mRNA to occlude its ribosome binding site, blocking traJ translation and thereby inhibiting transcription of the tra operon; FinO protects FinP against degradation by binding to FinP and sterically blocking the cellular endonuclease RNase E; FinO also also binds to the complementary stem-loop structures in traJ mRNA and promotes duplex formation between FinP and traJ RNA in vitro; this domain contains two independent RNA binding regions


Pssm-ID: 238145  Cd Length: 146  Bit Score: 185.87  E-value: 1.48e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005580185  47 AGINSSAVETHIPEAPARKKKKKRHRFPRPSHW-TREYTHECVEKIkalFPHLRAEGGgFIPLKIGINNDISAFLAEHPE 125
Cdd:cd00236     1 VGKNKLAEKADREAELAAKKKPARQALSIYLNLpTVEYAVECLKKW---FPGLFPGDT-PRLLKCGIKDGILQDVAQHPN 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005580185 126 TELTMDEWLCAVSCITSRRVYLQRTaVAGVPRYGLDGHPKGQVSdseaQSAGRRLATLEQKWLRMQAQQENISGQ 200
Cdd:cd00236    77 IPLTHEELRCAVKAITRRESYLQAM-VAGAPRYDLEGYVAGHIS----QEAEVYAARLLDKIRRQQRIKKELKRV 146
ProQ pfam04352
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 85-181 4.89e-12

ProQ/FINO family; This family includes ProQ, which is required for full activation of the osmoprotectant transporter, ProP, in Escherichia coli. This family includes several bacterial fertility inhibition (FINO) proteins. The conjugative transfer of F-like plasmids is repressed by FinO, an RNA binding protein. FinO interacts with the F-plasmid encoded traJ mRNA and its antisense RNA, FinP, stabilising FinP against endonucleolytic degradation and facilitating sense-antisense RNA recognition. ProQ operates as an RNA-chaperone, binding RNA and bringing about both RNA strand-exchange and RNA duplexing. This suggests that in fact it does not regulate ProP transcription but rather regulates ProP translation through activity as an RNA-binding protein.


Pssm-ID: 461270  Cd Length: 106  Bit Score: 59.93  E-value: 4.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005580185  85 HECVEKIKALFPHLRAEGGGFIPLKIGINNDISAFLAEHPETELTMDEwlcAVSCITSRRVYLQRTaVAGVPRYGLDGHP 164
Cdd:pfam04352   2 KELIARLAERFPLAFPAEGEKLPLKIGIFQDLLELADDLGLSKTQLRQ---ALRTYTRSWRYLAAM-KEGAARVDLDGNP 77

                          90
                  ....*....|....*..
gi 1005580185 165 KGQVSDSEAQSAGRRLA 181
Cdd:pfam04352  78 AGEVTAEHAEHARQQLA 94
ProQ COG3109
sRNA-binding protein ProQ [Signal transduction mechanisms];
80-195 2.55e-11

sRNA-binding protein ProQ [Signal transduction mechanisms];


Pssm-ID: 442343 [Multi-domain]  Cd Length: 153  Bit Score: 59.22  E-value: 2.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005580185  80 TREYTHECVEKIKALFPHLRAeGGGFIPLKIGINNDISAFLaehPETELTMDEWLCAVSCITSRRVYLqRTAVAGVPRYG 159
Cdd:COG3109     9 KLESPKEVIAYLAERFPACFD-LEEPKPLKIGIFQDLAARL---PDDELSKTQLRRALRRYTRSWRYL-KAVKEGAQRVD 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1005580185 160 LDGHPKGQVSDSEAQSAGRRLATLEQKWLRMQAQQE 195
Cdd:COG3109    84 LDGNPAGEVTEEHAEHAREQLAERKAKVAARRAAEQ 119
ProQ smart00945
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 84-194 3.30e-10

ProQ/FINO family; This family includes ProQ, which is required for full activation of the osmoprotectant transporter, ProQ, in Escherichia coli.


Pssm-ID: 198013 [Multi-domain]  Cd Length: 113  Bit Score: 55.06  E-value: 3.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005580185   84 THECVEKIKALFPHLRAEGGGFIPLKIGINNDIsafLAEHPETELTMDEWL-CAVSCITSRRVYLQRTaVAGVPRYGLDG 162
Cdd:smart00945   5 VKALLEKLQERFPLCFGANGAPKPLKIGIFQDL---LARLEEDEKVSKTALrEALRTYTRSWRYLKAV-KAGAVRVDLQG 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1005580185  163 HPKGQVSDSEAQSAGRRLATLEQKWLRMQAQQ 194
Cdd:smart00945  81 NPAEEVTEEHAAHALKKLKERREKRAAKAAAQ 112
 
Name Accession Description Interval E-value
FinO_conjug_rep cd00236
FinO bacterial conjugation repressor domain; the basic protein FinO is part of the the two ...
 47-200 1.48e-60

FinO bacterial conjugation repressor domain; the basic protein FinO is part of the the two component FinOP system which is responsible for repressing bacterial conjugation; the FinOP system represses the transfer (tra) operon of the F-plasmid which encodes the proteins responsible for conjugative transfer of this plasmid from host to recipient Escherichia coli cells; antisense RNA, FinP is thought to interact with traJ mRNA to occlude its ribosome binding site, blocking traJ translation and thereby inhibiting transcription of the tra operon; FinO protects FinP against degradation by binding to FinP and sterically blocking the cellular endonuclease RNase E; FinO also also binds to the complementary stem-loop structures in traJ mRNA and promotes duplex formation between FinP and traJ RNA in vitro; this domain contains two independent RNA binding regions


Pssm-ID: 238145  Cd Length: 146  Bit Score: 185.87  E-value: 1.48e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005580185  47 AGINSSAVETHIPEAPARKKKKKRHRFPRPSHW-TREYTHECVEKIkalFPHLRAEGGgFIPLKIGINNDISAFLAEHPE 125
Cdd:cd00236     1 VGKNKLAEKADREAELAAKKKPARQALSIYLNLpTVEYAVECLKKW---FPGLFPGDT-PRLLKCGIKDGILQDVAQHPN 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005580185 126 TELTMDEWLCAVSCITSRRVYLQRTaVAGVPRYGLDGHPKGQVSdseaQSAGRRLATLEQKWLRMQAQQENISGQ 200
Cdd:cd00236    77 IPLTHEELRCAVKAITRRESYLQAM-VAGAPRYDLEGYVAGHIS----QEAEVYAARLLDKIRRQQRIKKELKRV 146
ProQ pfam04352
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 85-181 4.89e-12

ProQ/FINO family; This family includes ProQ, which is required for full activation of the osmoprotectant transporter, ProP, in Escherichia coli. This family includes several bacterial fertility inhibition (FINO) proteins. The conjugative transfer of F-like plasmids is repressed by FinO, an RNA binding protein. FinO interacts with the F-plasmid encoded traJ mRNA and its antisense RNA, FinP, stabilising FinP against endonucleolytic degradation and facilitating sense-antisense RNA recognition. ProQ operates as an RNA-chaperone, binding RNA and bringing about both RNA strand-exchange and RNA duplexing. This suggests that in fact it does not regulate ProP transcription but rather regulates ProP translation through activity as an RNA-binding protein.


Pssm-ID: 461270  Cd Length: 106  Bit Score: 59.93  E-value: 4.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005580185  85 HECVEKIKALFPHLRAEGGGFIPLKIGINNDISAFLAEHPETELTMDEwlcAVSCITSRRVYLQRTaVAGVPRYGLDGHP 164
Cdd:pfam04352   2 KELIARLAERFPLAFPAEGEKLPLKIGIFQDLLELADDLGLSKTQLRQ---ALRTYTRSWRYLAAM-KEGAARVDLDGNP 77

                          90
                  ....*....|....*..
gi 1005580185 165 KGQVSDSEAQSAGRRLA 181
Cdd:pfam04352  78 AGEVTAEHAEHARQQLA 94
ProQ COG3109
sRNA-binding protein ProQ [Signal transduction mechanisms];
80-195 2.55e-11

sRNA-binding protein ProQ [Signal transduction mechanisms];


Pssm-ID: 442343 [Multi-domain]  Cd Length: 153  Bit Score: 59.22  E-value: 2.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005580185  80 TREYTHECVEKIKALFPHLRAeGGGFIPLKIGINNDISAFLaehPETELTMDEWLCAVSCITSRRVYLqRTAVAGVPRYG 159
Cdd:COG3109     9 KLESPKEVIAYLAERFPACFD-LEEPKPLKIGIFQDLAARL---PDDELSKTQLRRALRRYTRSWRYL-KAVKEGAQRVD 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1005580185 160 LDGHPKGQVSDSEAQSAGRRLATLEQKWLRMQAQQE 195
Cdd:COG3109    84 LDGNPAGEVTEEHAEHAREQLAERKAKVAARRAAEQ 119
ProQ smart00945
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 84-194 3.30e-10

ProQ/FINO family; This family includes ProQ, which is required for full activation of the osmoprotectant transporter, ProQ, in Escherichia coli.


Pssm-ID: 198013 [Multi-domain]  Cd Length: 113  Bit Score: 55.06  E-value: 3.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005580185   84 THECVEKIKALFPHLRAEGGGFIPLKIGINNDIsafLAEHPETELTMDEWL-CAVSCITSRRVYLQRTaVAGVPRYGLDG 162
Cdd:smart00945   5 VKALLEKLQERFPLCFGANGAPKPLKIGIFQDL---LARLEEDEKVSKTALrEALRTYTRSWRYLKAV-KAGAVRVDLQG 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1005580185  163 HPKGQVSDSEAQSAGRRLATLEQKWLRMQAQQ 194
Cdd:smart00945  81 NPAEEVTEEHAAHALKKLKERREKRAAKAAAQ 112
 
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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