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Conserved domains on  [gi|446763218|ref|WP_000840474|]
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fertility inhibition protein FinO [Escherichia coli]

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;
1-185 3.93e-107

fertility inhibition protein FinO;


:

Pssm-ID: 184304 [Multi-domain]  Cd Length: 186  Bit Score: 304.48  E-value: 3.93e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446763218   1 MAEQKRPVLTLKRKTEGETPVRSRKTIINVTTPPKWKVKKQKLAEKAAREAELAAKKAQARQALSIYLTLPSLDEAVNTL 80
Cdd:PRK13754   1 MTEQKRPVLTLKRKTEGETPVRSRKTIINVTTPPKWKVKKQKLAEKAAREAELAAKKAQARQALSIYLNLPPLDEAVNTL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446763218  81 KPWWPGLFDGNTPRLLACGIREVLLDEVSQRNIPLSHKKLRRALKAITRSESYLGAMKAGACRYDTEGYVTEHITQEEEQ 160
Cdd:PRK13754  81 KPWWPGLFDGDTPRLLACGIREVLLEDVAQRNIPLSHKKLRRALKAITRSESYLCAMKAGACRYDTEGYVTEHISQEEEA 160

                        170       180
                 ....*....|....*....|....*
gi 446763218 161 YAQARLEKVRRQNRIKDELRAILAE 185
Cdd:PRK13754 161 YAAERLDKIRRQNRIKAELQAVLDE 185
 
Name Accession Description Interval E-value
PRK13754 PRK13754
fertility inhibition protein FinO;
1-185 3.93e-107

fertility inhibition protein FinO;


Pssm-ID: 184304 [Multi-domain]  Cd Length: 186  Bit Score: 304.48  E-value: 3.93e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446763218   1 MAEQKRPVLTLKRKTEGETPVRSRKTIINVTTPPKWKVKKQKLAEKAAREAELAAKKAQARQALSIYLTLPSLDEAVNTL 80
Cdd:PRK13754   1 MTEQKRPVLTLKRKTEGETPVRSRKTIINVTTPPKWKVKKQKLAEKAAREAELAAKKAQARQALSIYLNLPPLDEAVNTL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446763218  81 KPWWPGLFDGNTPRLLACGIREVLLDEVSQRNIPLSHKKLRRALKAITRSESYLGAMKAGACRYDTEGYVTEHITQEEEQ 160
Cdd:PRK13754  81 KPWWPGLFDGDTPRLLACGIREVLLEDVAQRNIPLSHKKLRRALKAITRSESYLCAMKAGACRYDTEGYVTEHISQEEEA 160

                        170       180
                 ....*....|....*....|....*
gi 446763218 161 YAQARLEKVRRQNRIKDELRAILAE 185
Cdd:PRK13754 161 YAAERLDKIRRQNRIKAELQAVLDE 185
FinO_conjug_rep cd00236
FinO bacterial conjugation repressor domain; the basic protein FinO is part of the the two ...
 38-181 3.27e-48

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: 153.90  E-value: 3.27e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446763218  38 VKKQKLAEKAAREAELAAKKAQARQALSIYLTLPSLDEAVNTLKPWWPGLFDGNTPRLLACGIREVLLDEVSQ-RNIPLS 116
Cdd:cd00236    1 VGKNKLAEKADREAELAAKKKPARQALSIYLNLPTVEYAVECLKKWFPGLFPGDTPRLLKCGIKDGILQDVAQhPNIPLT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446763218 117 HKKLRRALKAITRSESYLGAMKAGACRYDTEGYVTEHITQEEEQYAQARLEKVRRQNRIKDELRA 181
Cdd:cd00236   81 HEELRCAVKAITRRESYLQAMVAGAPRYDLEGYVAGHISQEAEVYAARLLDKIRRQQRIKKELKR 145
ProQ pfam04352
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 75-178 1.25e-28

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: 102.30  E-value: 1.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446763218   75 EAVNTLKPWWPGLFDGNT-PRLLACGIREVLLDEvsQRNIPLSHKKLRRALKAITRSESYLGAMKAGACRYDTEGYVTEH 153
Cdd:pfam04352   3 ELIARLAERFPLAFPAEGeKLPLKIGIFQDLLEL--ADDLGLSKTQLRQALRTYTRSWRYLAAMKEGAARVDLDGNPAGE 80

                          90       100
                  ....*....|....*....|....*
gi 446763218  154 ITQEEEQYAQARLEKVRRQNRIKDE 178
Cdd:pfam04352  81 VTAEHAEHARQQLARRRQKRAQRRA 105
ProQ smart00945
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 70-181 6.11e-27

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: 98.20  E-value: 6.11e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446763218    70 LPSLDEAVNTLKPWWPGLFDGN-TPRLLACGIREVLLDEVSQRNIPlSHKKLRRALKAITRSESYLGAMKAGACRYDTEG 148
Cdd:smart00945   2 LDDVKALLEKLQERFPLCFGANgAPKPLKIGIFQDLLARLEEDEKV-SKTALREALRTYTRSWRYLKAVKAGAVRVDLQG 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 446763218   149 YVTEHITQEEEQYAQARLEKVRRQNRIKDELRA 181
Cdd:smart00945  81 NPAEEVTEEHAAHALKKLKERREKRAAKAAAQR 113
ProQ COG3109
sRNA-binding protein ProQ [Signal transduction mechanisms];
84-174 7.15e-16

sRNA-binding protein ProQ [Signal transduction mechanisms];


Pssm-ID: 442343 [Multi-domain]  Cd Length: 153  Bit Score: 70.78  E-value: 7.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446763218  84 WPGLFDGNTPRLLACGIREVLLDEVSQRniPLSHKKLRRALKAITRSESYLGAMKAGACRYDTEGYVTEHITQEEEQYAQ 163
Cdd:COG3109   24 FPACFDLEEPKPLKIGIFQDLAARLPDD--ELSKTQLRRALRRYTRSWRYLKAVKEGAQRVDLDGNPAGEVTEEHAEHAR 101

                         90
                 ....*....|.
gi 446763218 164 ARLEKVRRQNR 174
Cdd:COG3109  102 EQLAERKAKVA 112
 
Name Accession Description Interval E-value
PRK13754 PRK13754
fertility inhibition protein FinO;
1-185 3.93e-107

fertility inhibition protein FinO;


Pssm-ID: 184304 [Multi-domain]  Cd Length: 186  Bit Score: 304.48  E-value: 3.93e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446763218   1 MAEQKRPVLTLKRKTEGETPVRSRKTIINVTTPPKWKVKKQKLAEKAAREAELAAKKAQARQALSIYLTLPSLDEAVNTL 80
Cdd:PRK13754   1 MTEQKRPVLTLKRKTEGETPVRSRKTIINVTTPPKWKVKKQKLAEKAAREAELAAKKAQARQALSIYLNLPPLDEAVNTL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446763218  81 KPWWPGLFDGNTPRLLACGIREVLLDEVSQRNIPLSHKKLRRALKAITRSESYLGAMKAGACRYDTEGYVTEHITQEEEQ 160
Cdd:PRK13754  81 KPWWPGLFDGDTPRLLACGIREVLLEDVAQRNIPLSHKKLRRALKAITRSESYLCAMKAGACRYDTEGYVTEHISQEEEA 160

                        170       180
                 ....*....|....*....|....*
gi 446763218 161 YAQARLEKVRRQNRIKDELRAILAE 185
Cdd:PRK13754 161 YAAERLDKIRRQNRIKAELQAVLDE 185
FinO_conjug_rep cd00236
FinO bacterial conjugation repressor domain; the basic protein FinO is part of the the two ...
 38-181 3.27e-48

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: 153.90  E-value: 3.27e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446763218  38 VKKQKLAEKAAREAELAAKKAQARQALSIYLTLPSLDEAVNTLKPWWPGLFDGNTPRLLACGIREVLLDEVSQ-RNIPLS 116
Cdd:cd00236    1 VGKNKLAEKADREAELAAKKKPARQALSIYLNLPTVEYAVECLKKWFPGLFPGDTPRLLKCGIKDGILQDVAQhPNIPLT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446763218 117 HKKLRRALKAITRSESYLGAMKAGACRYDTEGYVTEHITQEEEQYAQARLEKVRRQNRIKDELRA 181
Cdd:cd00236   81 HEELRCAVKAITRRESYLQAMVAGAPRYDLEGYVAGHISQEAEVYAARLLDKIRRQQRIKKELKR 145
ProQ pfam04352
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 75-178 1.25e-28

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: 102.30  E-value: 1.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446763218   75 EAVNTLKPWWPGLFDGNT-PRLLACGIREVLLDEvsQRNIPLSHKKLRRALKAITRSESYLGAMKAGACRYDTEGYVTEH 153
Cdd:pfam04352   3 ELIARLAERFPLAFPAEGeKLPLKIGIFQDLLEL--ADDLGLSKTQLRQALRTYTRSWRYLAAMKEGAARVDLDGNPAGE 80

                          90       100
                  ....*....|....*....|....*
gi 446763218  154 ITQEEEQYAQARLEKVRRQNRIKDE 178
Cdd:pfam04352  81 VTAEHAEHARQQLARRRQKRAQRRA 105
ProQ smart00945
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 70-181 6.11e-27

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: 98.20  E-value: 6.11e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446763218    70 LPSLDEAVNTLKPWWPGLFDGN-TPRLLACGIREVLLDEVSQRNIPlSHKKLRRALKAITRSESYLGAMKAGACRYDTEG 148
Cdd:smart00945   2 LDDVKALLEKLQERFPLCFGANgAPKPLKIGIFQDLLARLEEDEKV-SKTALREALRTYTRSWRYLKAVKAGAVRVDLQG 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 446763218   149 YVTEHITQEEEQYAQARLEKVRRQNRIKDELRA 181
Cdd:smart00945  81 NPAEEVTEEHAAHALKKLKERREKRAAKAAAQR 113
FinO_N pfam12602
Fertility inhibition protein N terminal; This domain family is found in bacteria, and is ...
 1-53 3.30e-25

Fertility inhibition protein N terminal; This domain family is found in bacteria, and is typically between 62 and 102 amino acids in length. The family is found in association with pfam04352. The FinOP (fertility inhibition) system of F-like plasmids consists of an antisense RNA (FinP) and a 22 kDa protein (FinO) which act in concert to prevent the translation of TraJ, the positive regulator of the transfer operon.


Pssm-ID: 315304  Cd Length: 62  Bit Score: 92.51  E-value: 3.30e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446763218    1 MAEQKRPVLTLKRKTEGETPVRSRKTIINVTTPPKWKVKKQKLAEKAAREAEL 53
Cdd:pfam12602   1 MTEQKRPVLTLKRKTNGTAPARSRKTIINVTTPPKWKVKKQKLAEKAKREAEL 53
ProQ COG3109
sRNA-binding protein ProQ [Signal transduction mechanisms];
84-174 7.15e-16

sRNA-binding protein ProQ [Signal transduction mechanisms];


Pssm-ID: 442343 [Multi-domain]  Cd Length: 153  Bit Score: 70.78  E-value: 7.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446763218  84 WPGLFDGNTPRLLACGIREVLLDEVSQRniPLSHKKLRRALKAITRSESYLGAMKAGACRYDTEGYVTEHITQEEEQYAQ 163
Cdd:COG3109   24 FPACFDLEEPKPLKIGIFQDLAARLPDD--ELSKTQLRRALRRYTRSWRYLKAVKEGAQRVDLDGNPAGEVTEEHAEHAR 101

                         90
                 ....*....|.
gi 446763218 164 ARLEKVRRQNR 174
Cdd:COG3109  102 EQLAERKAKVA 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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