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Conserved domains on  [gi|556197416|ref|WP_023280883|]
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MULTISPECIES: fertility inhibition protein FinO [Gammaproteobacteria]

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;
1-197 1.23e-74

fertility inhibition protein FinO;


:

Pssm-ID: 184304 [Multi-domain]  Cd Length: 186  Bit Score: 222.82  E-value: 1.23e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556197416   1 MSEEKRPVLSLKRKPAENSTAPAEATpapgvvrrkkVVVVSSPPAWKAKKAKLEKAKQAAEAdarnaaPAPDKAVKTPPP 80
Cdd:PRK13754   1 MTEQKRPVLTLKRKTEGETPVRSRKT----------IINVTTPPKWKVKKQKLAEKAAREAE------LAAKKAQARQAL 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556197416  81 VRYLRLLPPEQAIMTLKAFWPQLFDGNSPRLLATGMREQLFADIVNRDLPLSHKQVIKCLKSLTRSAGYLSRMKVGASRY 160
Cdd:PRK13754  65 SIYLNLPPLDEAVNTLKPWWPGLFDGDTPRLLACGIREVLLEDVAQRNIPLSHKKLRRALKAITRSESYLCAMKAGACRY 144

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 556197416 161 DLQGNAVATVTAEEAQYASERmMKELLRAERKMSQTL 197
Cdd:PRK13754 145 DTEGYVTEHISQEEEAYAAER-LDKIRRQNRIKAELQ 180
 
Name Accession Description Interval E-value
PRK13754 PRK13754
fertility inhibition protein FinO;
1-197 1.23e-74

fertility inhibition protein FinO;


Pssm-ID: 184304 [Multi-domain]  Cd Length: 186  Bit Score: 222.82  E-value: 1.23e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556197416   1 MSEEKRPVLSLKRKPAENSTAPAEATpapgvvrrkkVVVVSSPPAWKAKKAKLEKAKQAAEAdarnaaPAPDKAVKTPPP 80
Cdd:PRK13754   1 MTEQKRPVLTLKRKTEGETPVRSRKT----------IINVTTPPKWKVKKQKLAEKAAREAE------LAAKKAQARQAL 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556197416  81 VRYLRLLPPEQAIMTLKAFWPQLFDGNSPRLLATGMREQLFADIVNRDLPLSHKQVIKCLKSLTRSAGYLSRMKVGASRY 160
Cdd:PRK13754  65 SIYLNLPPLDEAVNTLKPWWPGLFDGDTPRLLACGIREVLLEDVAQRNIPLSHKKLRRALKAITRSESYLCAMKAGACRY 144

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 556197416 161 DLQGNAVATVTAEEAQYASERmMKELLRAERKMSQTL 197
Cdd:PRK13754 145 DTEGYVTEHISQEEEAYAAER-LDKIRRQNRIKAELQ 180
ProQ COG3109
sRNA-binding protein ProQ [Signal transduction mechanisms];
86-195 4.84e-28

sRNA-binding protein ProQ [Signal transduction mechanisms];


Pssm-ID: 442343 [Multi-domain]  Cd Length: 153  Bit Score: 102.75  E-value: 4.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556197416  86 LLPPEQAIMTLKAFWPQLFDGNSPRLLATGMREQLFADIvnRDLPLSHKQVIKCLKSLTRSAGYLSRMKVGASRYDLQGN 165
Cdd:COG3109   10 LESPKEVIAYLAERFPACFDLEEPKPLKIGIFQDLAARL--PDDELSKTQLRRALRRYTRSWRYLKAVKEGAQRVDLDGN 87

                         90       100       110
                 ....*....|....*....|....*....|
gi 556197416 166 AVATVTAEEAQYASERMMKELLRAERKMSQ 195
Cdd:COG3109   88 PAGEVTEEHAEHAREQLAERKAKVAARRAA 117
ProQ pfam04352
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 89-195 4.90e-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: 101.14  E-value: 4.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556197416   89 PEQAIMTLKAFWPQLFDGNS-PRLLATGMREQLFAdiVNRDLPLSHKQVIKCLKSLTRSAGYLSRMKVGASRYDLQGNAV 167
Cdd:pfam04352   1 VKELIARLAERFPLAFPAEGeKLPLKIGIFQDLLE--LADDLGLSKTQLRQALRTYTRSWRYLAAMKEGAARVDLDGNPA 78

                          90       100
                  ....*....|....*....|....*...
gi 556197416  168 ATVTAEEAQYASERMMKELLRAERKMSQ 195
Cdd:pfam04352  79 GEVTAEHAEHARQQLARRRQKRAQRRAA 106
FinO_conjug_rep cd00236
FinO bacterial conjugation repressor domain; the basic protein FinO is part of the the two ...
 82-192 7.34e-20

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: 81.48  E-value: 7.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556197416  82 RYLRLLPPEQAIMTLKAFWPQLFDGNSPRLLATGMREQLFADIV-NRDLPLSHKQVIKCLKSLTRSAGYLSRMKVGASRY 160
Cdd:cd00236   29 IYLNLPTVEYAVECLKKWFPGLFPGDTPRLLKCGIKDGILQDVAqHPNIPLTHEELRCAVKAITRRESYLQAMVAGAPRY 108

                         90       100       110
                 ....*....|....*....|....*....|..
gi 556197416 161 DLQGNAVATVTAEEAQYASERMMKELLRAERK 192
Cdd:cd00236  109 DLEGYVAGHISQEAEVYAARLLDKIRRQQRIK 140
ProQ smart00945
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 85-194 1.22e-15

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: 69.70  E-value: 1.22e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556197416    85 RLLPPEQAIMTLKAFWPQLFDGN-SPRLLATGMREQLFADIVNRDLPlSHKQVIKCLKSLTRSAGYLSRMKVGASRYDLQ 163
Cdd:smart00945   1 KLDDVKALLEKLQERFPLCFGANgAPKPLKIGIFQDLLARLEEDEKV-SKTALREALRTYTRSWRYLKAVKAGAVRVDLQ 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 556197416   164 GNAVATVTAEEAQYASERmmkeLLRAERKMS 194
Cdd:smart00945  80 GNPAEEVTEEHAAHALKK----LKERREKRA 106
 
Name Accession Description Interval E-value
PRK13754 PRK13754
fertility inhibition protein FinO;
1-197 1.23e-74

fertility inhibition protein FinO;


Pssm-ID: 184304 [Multi-domain]  Cd Length: 186  Bit Score: 222.82  E-value: 1.23e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556197416   1 MSEEKRPVLSLKRKPAENSTAPAEATpapgvvrrkkVVVVSSPPAWKAKKAKLEKAKQAAEAdarnaaPAPDKAVKTPPP 80
Cdd:PRK13754   1 MTEQKRPVLTLKRKTEGETPVRSRKT----------IINVTTPPKWKVKKQKLAEKAAREAE------LAAKKAQARQAL 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556197416  81 VRYLRLLPPEQAIMTLKAFWPQLFDGNSPRLLATGMREQLFADIVNRDLPLSHKQVIKCLKSLTRSAGYLSRMKVGASRY 160
Cdd:PRK13754  65 SIYLNLPPLDEAVNTLKPWWPGLFDGDTPRLLACGIREVLLEDVAQRNIPLSHKKLRRALKAITRSESYLCAMKAGACRY 144

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 556197416 161 DLQGNAVATVTAEEAQYASERmMKELLRAERKMSQTL 197
Cdd:PRK13754 145 DTEGYVTEHISQEEEAYAAER-LDKIRRQNRIKAELQ 180
ProQ COG3109
sRNA-binding protein ProQ [Signal transduction mechanisms];
86-195 4.84e-28

sRNA-binding protein ProQ [Signal transduction mechanisms];


Pssm-ID: 442343 [Multi-domain]  Cd Length: 153  Bit Score: 102.75  E-value: 4.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556197416  86 LLPPEQAIMTLKAFWPQLFDGNSPRLLATGMREQLFADIvnRDLPLSHKQVIKCLKSLTRSAGYLSRMKVGASRYDLQGN 165
Cdd:COG3109   10 LESPKEVIAYLAERFPACFDLEEPKPLKIGIFQDLAARL--PDDELSKTQLRRALRRYTRSWRYLKAVKEGAQRVDLDGN 87

                         90       100       110
                 ....*....|....*....|....*....|
gi 556197416 166 AVATVTAEEAQYASERMMKELLRAERKMSQ 195
Cdd:COG3109   88 PAGEVTEEHAEHAREQLAERKAKVAARRAA 117
ProQ pfam04352
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 89-195 4.90e-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: 101.14  E-value: 4.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556197416   89 PEQAIMTLKAFWPQLFDGNS-PRLLATGMREQLFAdiVNRDLPLSHKQVIKCLKSLTRSAGYLSRMKVGASRYDLQGNAV 167
Cdd:pfam04352   1 VKELIARLAERFPLAFPAEGeKLPLKIGIFQDLLE--LADDLGLSKTQLRQALRTYTRSWRYLAAMKEGAARVDLDGNPA 78

                          90       100
                  ....*....|....*....|....*...
gi 556197416  168 ATVTAEEAQYASERMMKELLRAERKMSQ 195
Cdd:pfam04352  79 GEVTAEHAEHARQQLARRRQKRAQRRAA 106
FinO_conjug_rep cd00236
FinO bacterial conjugation repressor domain; the basic protein FinO is part of the the two ...
 82-192 7.34e-20

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: 81.48  E-value: 7.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556197416  82 RYLRLLPPEQAIMTLKAFWPQLFDGNSPRLLATGMREQLFADIV-NRDLPLSHKQVIKCLKSLTRSAGYLSRMKVGASRY 160
Cdd:cd00236   29 IYLNLPTVEYAVECLKKWFPGLFPGDTPRLLKCGIKDGILQDVAqHPNIPLTHEELRCAVKAITRRESYLQAMVAGAPRY 108

                         90       100       110
                 ....*....|....*....|....*....|..
gi 556197416 161 DLQGNAVATVTAEEAQYASERMMKELLRAERK 192
Cdd:cd00236  109 DLEGYVAGHISQEAEVYAARLLDKIRRQQRIK 140
ProQ smart00945
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 85-194 1.22e-15

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: 69.70  E-value: 1.22e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556197416    85 RLLPPEQAIMTLKAFWPQLFDGN-SPRLLATGMREQLFADIVNRDLPlSHKQVIKCLKSLTRSAGYLSRMKVGASRYDLQ 163
Cdd:smart00945   1 KLDDVKALLEKLQERFPLCFGANgAPKPLKIGIFQDLLARLEEDEKV-SKTALREALRTYTRSWRYLKAVKAGAVRVDLQ 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 556197416   164 GNAVATVTAEEAQYASERmmkeLLRAERKMS 194
Cdd:smart00945  80 GNPAEEVTEEHAAHALKK----LKERREKRA 106
PRK04950 PRK04950
ProP expression regulator; Provisional
 120-178 1.98e-03

ProP expression regulator; Provisional


Pssm-ID: 235322 [Multi-domain]  Cd Length: 213  Bit Score: 37.60  E-value: 1.98e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556197416 120 LFADIVNR---DLPLSHKQVIKCLKSLTRSAGYLSRMKVGASRYDLQGNAVATVTAEEAQYA 178
Cdd:PRK04950  38 IFQDLAERladDEKVSKTQLRSALRLYTSSWRYLYGVKAGAQRVDLDGNPCGELEEEHVEHA 99
 
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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