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Conserved domains on  [gi|431482972|gb|ELH62673|]
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fertility inhibition protein [Escherichia coli KTE202]

Protein Classification

fertility inhibition protein FinO( domain architecture ID 11486840)

fertility inhibition protein FinO is one of the components on the FinOP fertility inhibition complex, which inhibits the expression of traJ gene, which in turn regulates the expression of some 20 transfer genes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13754 PRK13754
fertility inhibition protein FinO;
1-109 1.49e-67

fertility inhibition protein FinO;


:

Pssm-ID: 184304 [Multi-domain]  Cd Length: 186  Bit Score: 200.87  E-value: 1.49e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431482972   1 MNTLKPWWPGLFDGDTPRLLACGIRDVLLEDVAQRNIPLSHKKLRRALKAITRSESYLCAMKAGACRYDTEGYVTEHISQ 80
Cdd:PRK13754  77 VNTLKPWWPGLFDGDTPRLLACGIREVLLEDVAQRNIPLSHKKLRRALKAITRSESYLCAMKAGACRYDTEGYVTEHISQ 156

                         90       100
                 ....*....|....*....|....*....
gi 431482972  81 EEEAYAAARLDKIRRQNRIKAELQAVLDE 109
Cdd:PRK13754 157 EEEAYAAERLDKIRRQNRIKAELQAVLDE 185
 
Name Accession Description Interval E-value
PRK13754 PRK13754
fertility inhibition protein FinO;
1-109 1.49e-67

fertility inhibition protein FinO;


Pssm-ID: 184304 [Multi-domain]  Cd Length: 186  Bit Score: 200.87  E-value: 1.49e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431482972   1 MNTLKPWWPGLFDGDTPRLLACGIRDVLLEDVAQRNIPLSHKKLRRALKAITRSESYLCAMKAGACRYDTEGYVTEHISQ 80
Cdd:PRK13754  77 VNTLKPWWPGLFDGDTPRLLACGIREVLLEDVAQRNIPLSHKKLRRALKAITRSESYLCAMKAGACRYDTEGYVTEHISQ 156

                         90       100
                 ....*....|....*....|....*....
gi 431482972  81 EEEAYAAARLDKIRRQNRIKAELQAVLDE 109
Cdd:PRK13754 157 EEEAYAAERLDKIRRQNRIKAELQAVLDE 185
FinO_conjug_rep cd00236
FinO bacterial conjugation repressor domain; the basic protein FinO is part of the the two ...
 2-106 1.33e-47

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: 149.28  E-value: 1.33e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431482972   2 NTLKPWWPGLFDGDTPRLLACGIRDVLLEDVAQ-RNIPLSHKKLRRALKAITRSESYLCAMKAGACRYDTEGYVTEHISQ 80
Cdd:cd00236   41 ECLKKWFPGLFPGDTPRLLKCGIKDGILQDVAQhPNIPLTHEELRCAVKAITRRESYLQAMVAGAPRYDLEGYVAGHISQ 120

                         90       100
                 ....*....|....*....|....*.
gi 431482972  81 EEEAYAAARLDKIRRQNRIKAELQAV 106
Cdd:cd00236  121 EAEVYAARLLDKIRRQQRIKKELKRV 146
ProQ smart00945
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 2-105 2.65e-29

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: 101.67  E-value: 2.65e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431482972     2 NTLKPWWPGLFDGD-TPRLLACGIRDVLLEDVAQRNIPlSHKKLRRALKAITRSESYLCAMKAGACRYDTEGYVTEHISQ 80
Cdd:smart00945  10 EKLQERFPLCFGANgAPKPLKIGIFQDLLARLEEDEKV-SKTALREALRTYTRSWRYLKAVKAGAVRVDLQGNPAEEVTE 88

                           90       100
                   ....*....|....*....|....*
gi 431482972    81 EEEAYAAARLDKIRRQNRIKAELQA 105
Cdd:smart00945  89 EHAAHALKKLKERREKRAAKAAAQR 113
ProQ pfam04352
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 2-102 9.46e-29

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: 99.99  E-value: 9.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431482972    2 NTLKPWWPGLFDGDT-PRLLACGIRDVLLEdvAQRNIPLSHKKLRRALKAITRSESYLCAMKAGACRYDTEGYVTEHISQ 80
Cdd:pfam04352   6 ARLAERFPLAFPAEGeKLPLKIGIFQDLLE--LADDLGLSKTQLRQALRTYTRSWRYLAAMKEGAARVDLDGNPAGEVTA 83

                          90       100
                  ....*....|....*....|..
gi 431482972   81 EEEAYAAARLDKIRRQNRIKAE 102
Cdd:pfam04352  84 EHAEHARQQLARRRQKRAQRRA 105
ProQ COG3109
sRNA-binding protein ProQ [Signal transduction mechanisms];
8-105 1.17e-17

sRNA-binding protein ProQ [Signal transduction mechanisms];


Pssm-ID: 442343 [Multi-domain]  Cd Length: 153  Bit Score: 73.09  E-value: 1.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431482972   8 WPGLFDGDTPRLLACGIRDVLLEDVAQRniPLSHKKLRRALKAITRSESYLCAMKAGACRYDTEGYVTEHISQEEEAYAA 87
Cdd:COG3109   24 FPACFDLEEPKPLKIGIFQDLAARLPDD--ELSKTQLRRALRRYTRSWRYLKAVKEGAQRVDLDGNPAGEVTEEHAEHAR 101

                         90       100
                 ....*....|....*....|
gi 431482972  88 ARLDKI--RRQNRIKAELQA 105
Cdd:COG3109  102 EQLAERkaKVAARRAAEQAA 121
 
Name Accession Description Interval E-value
PRK13754 PRK13754
fertility inhibition protein FinO;
1-109 1.49e-67

fertility inhibition protein FinO;


Pssm-ID: 184304 [Multi-domain]  Cd Length: 186  Bit Score: 200.87  E-value: 1.49e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431482972   1 MNTLKPWWPGLFDGDTPRLLACGIRDVLLEDVAQRNIPLSHKKLRRALKAITRSESYLCAMKAGACRYDTEGYVTEHISQ 80
Cdd:PRK13754  77 VNTLKPWWPGLFDGDTPRLLACGIREVLLEDVAQRNIPLSHKKLRRALKAITRSESYLCAMKAGACRYDTEGYVTEHISQ 156

                         90       100
                 ....*....|....*....|....*....
gi 431482972  81 EEEAYAAARLDKIRRQNRIKAELQAVLDE 109
Cdd:PRK13754 157 EEEAYAAERLDKIRRQNRIKAELQAVLDE 185
FinO_conjug_rep cd00236
FinO bacterial conjugation repressor domain; the basic protein FinO is part of the the two ...
 2-106 1.33e-47

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: 149.28  E-value: 1.33e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431482972   2 NTLKPWWPGLFDGDTPRLLACGIRDVLLEDVAQ-RNIPLSHKKLRRALKAITRSESYLCAMKAGACRYDTEGYVTEHISQ 80
Cdd:cd00236   41 ECLKKWFPGLFPGDTPRLLKCGIKDGILQDVAQhPNIPLTHEELRCAVKAITRRESYLQAMVAGAPRYDLEGYVAGHISQ 120

                         90       100
                 ....*....|....*....|....*.
gi 431482972  81 EEEAYAAARLDKIRRQNRIKAELQAV 106
Cdd:cd00236  121 EAEVYAARLLDKIRRQQRIKKELKRV 146
ProQ smart00945
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 2-105 2.65e-29

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: 101.67  E-value: 2.65e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431482972     2 NTLKPWWPGLFDGD-TPRLLACGIRDVLLEDVAQRNIPlSHKKLRRALKAITRSESYLCAMKAGACRYDTEGYVTEHISQ 80
Cdd:smart00945  10 EKLQERFPLCFGANgAPKPLKIGIFQDLLARLEEDEKV-SKTALREALRTYTRSWRYLKAVKAGAVRVDLQGNPAEEVTE 88

                           90       100
                   ....*....|....*....|....*
gi 431482972    81 EEEAYAAARLDKIRRQNRIKAELQA 105
Cdd:smart00945  89 EHAAHALKKLKERREKRAAKAAAQR 113
ProQ pfam04352
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 2-102 9.46e-29

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: 99.99  E-value: 9.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431482972    2 NTLKPWWPGLFDGDT-PRLLACGIRDVLLEdvAQRNIPLSHKKLRRALKAITRSESYLCAMKAGACRYDTEGYVTEHISQ 80
Cdd:pfam04352   6 ARLAERFPLAFPAEGeKLPLKIGIFQDLLE--LADDLGLSKTQLRQALRTYTRSWRYLAAMKEGAARVDLDGNPAGEVTA 83

                          90       100
                  ....*....|....*....|..
gi 431482972   81 EEEAYAAARLDKIRRQNRIKAE 102
Cdd:pfam04352  84 EHAEHARQQLARRRQKRAQRRA 105
ProQ COG3109
sRNA-binding protein ProQ [Signal transduction mechanisms];
8-105 1.17e-17

sRNA-binding protein ProQ [Signal transduction mechanisms];


Pssm-ID: 442343 [Multi-domain]  Cd Length: 153  Bit Score: 73.09  E-value: 1.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431482972   8 WPGLFDGDTPRLLACGIRDVLLEDVAQRniPLSHKKLRRALKAITRSESYLCAMKAGACRYDTEGYVTEHISQEEEAYAA 87
Cdd:COG3109   24 FPACFDLEEPKPLKIGIFQDLAARLPDD--ELSKTQLRRALRRYTRSWRYLKAVKEGAQRVDLDGNPAGEVTEEHAEHAR 101

                         90       100
                 ....*....|....*....|
gi 431482972  88 ARLDKI--RRQNRIKAELQA 105
Cdd:COG3109  102 EQLAERkaKVAARRAAEQAA 121
 
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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