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Conserved domains on  [gi|254800720|sp|B2V268|]
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RecName: Full=RNA-binding protein Hfq

Protein Classification

RNA chaperone Hfq( domain architecture ID 12182934)

RNA chaperone Hfq is an RNA-binding protein that functions as a regulator of small non-coding RNAs

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Hfq pfam17209
Hfq protein;
8-70 7.37e-37

Hfq protein;


:

Pssm-ID: 435788  Cd Length: 64  Bit Score: 117.53  E-value: 7.37e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254800720   8 LQDIFLNSARKNKIPVTVYLSTGFKLNGIVKGFDSFTVILDSEGKQMLIYKHAITTVTPEKPI 70
Cdd:pfam17209  1 LQDQFLNQLRKEKIPVTVFLVNGFQLKGVIKGFDNFTVLLESDGKQQLVYKHAISTIVPARPV 63
 
Name Accession Description Interval E-value
Hfq pfam17209
Hfq protein;
8-70 7.37e-37

Hfq protein;


Pssm-ID: 435788  Cd Length: 64  Bit Score: 117.53  E-value: 7.37e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254800720   8 LQDIFLNSARKNKIPVTVYLSTGFKLNGIVKGFDSFTVILDSEGKQMLIYKHAITTVTPEKPI 70
Cdd:pfam17209  1 LQDQFLNQLRKEKIPVTVFLVNGFQLKGVIKGFDNFTVLLESDGKQQLVYKHAISTIVPARPV 63
Hfq COG1923
sRNA-binding regulator protein Hfq [Signal transduction mechanisms];
1-68 7.58e-36

sRNA-binding regulator protein Hfq [Signal transduction mechanisms];


Pssm-ID: 441526  Cd Length: 67  Bit Score: 115.27  E-value: 7.58e-36
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254800720  1 MNKQQNnLQDIFLNSARKNKIPVTVYLSTGFKLNGIVKGFDSFTVILDSEGKQMLIYKHAITTVTPEK 68
Cdd:COG1923   1 MKKPIN-LQDQFLNQLRKERIPVTIFLVNGVKLQGKIKSFDNFTVLLERDGKQQLVYKHAISTIVPAR 67
hfq PRK00395
RNA-binding protein Hfq; Provisional
 1-77 1.68e-31

RNA-binding protein Hfq; Provisional


Pssm-ID: 179001  Cd Length: 79  Bit Score: 104.62  E-value: 1.68e-31
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254800720  1 MNKQQNnLQDIFLNSARKNKIPVTVYLSTGFKLNGIVKGFDSFTVILDSEGKQMLIYKHAITTVTPEKPILFVDNES 77
Cdd:PRK00395  1 MAKGQN-LQDPFLNALRKERVPVTIYLVNGIKLQGQIESFDNFVVLLRNTGKSQLVYKHAISTVVPARPVSLHEDEE 76
Hfq TIGR02383
RNA chaperone Hfq; This model represents the RNA-binding pleiotropic regulator Hfq, a small, ...
 6-66 4.86e-28

RNA chaperone Hfq; This model represents the RNA-binding pleiotropic regulator Hfq, a small, Sm-like protein of bacteria. It helps pair regulatory noncoding RNAs with complementary mRNA target regions. It enhances the elongation of poly(A) tails on mRNA. It appears also to protect RNase E recognition sites (A/U-rich sequences with adjacent stem-loop structures) from cleavage. Being pleiotropic, it differs in some of its activities in different species. Hfq binds the non-coding regulatory RNA DsrA (see Rfam RF00014) in the few species known to have it: Escherichia coli, Shigella flexneri, Salmonella spp. In Azorhizobium caulinodans, an hfq mutant is unable to express nifA, and Hfq is called NrfA, for nif regulatory factor (see . The name hfq reflects phenomenology as a host factor for phage Q-beta RNA replication. [Regulatory functions, Other]


Pssm-ID: 274101  Cd Length: 61  Bit Score: 95.48  E-value: 4.86e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254800720   6 NNLQDIFLNSARKNKIPVTVYLSTGFKLNGIVKGFDSFTVILDSEGKQMLIYKHAITTVTP 66
Cdd:TIGR02383  1 QNLQDQFLNQLRKERIPVTVFLVNGVQLKGVIESFDNFTVLLESQGKQQLIYKHAISTISP 61
Hfq cd01716
bacterial Hfq-like; Hfq, an abundant, ubiquitous RNA-binding protein, functions as a ...
 7-66 8.37e-28

bacterial Hfq-like; Hfq, an abundant, ubiquitous RNA-binding protein, functions as a pleiotropic regulator of RNA metabolism in prokaryotes, required for transcription of some transcripts and degradation of others. Hfq binds small RNA molecules called riboregulators that modulate the stability or translation efficiency of RNA transcripts. Hfq binds preferentially to unstructured A/U-rich RNA sequences and is similar to the eukaryotic Sm proteins in both sequence and structure. Hfq forms a homo-hexameric ring similar to the heptameric ring of the Sm proteins.


Pssm-ID: 212463  Cd Length: 60  Bit Score: 94.90  E-value: 8.37e-28
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254800720  7 NLQDIFLNSARKNKIPVTVYLSTGFKLNGIVKGFDSFTVILDSEGKQMLIYKHAITTVTP 66
Cdd:cd01716   1 NLQDQFLNTLRKEKKPVTIYLVNGVRLKGKIKSFDNFTVLLESDGKQQLIYKHAISTIVP 60
 
Name Accession Description Interval E-value
Hfq pfam17209
Hfq protein;
8-70 7.37e-37

Hfq protein;


Pssm-ID: 435788  Cd Length: 64  Bit Score: 117.53  E-value: 7.37e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254800720   8 LQDIFLNSARKNKIPVTVYLSTGFKLNGIVKGFDSFTVILDSEGKQMLIYKHAITTVTPEKPI 70
Cdd:pfam17209  1 LQDQFLNQLRKEKIPVTVFLVNGFQLKGVIKGFDNFTVLLESDGKQQLVYKHAISTIVPARPV 63
Hfq COG1923
sRNA-binding regulator protein Hfq [Signal transduction mechanisms];
1-68 7.58e-36

sRNA-binding regulator protein Hfq [Signal transduction mechanisms];


Pssm-ID: 441526  Cd Length: 67  Bit Score: 115.27  E-value: 7.58e-36
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254800720  1 MNKQQNnLQDIFLNSARKNKIPVTVYLSTGFKLNGIVKGFDSFTVILDSEGKQMLIYKHAITTVTPEK 68
Cdd:COG1923   1 MKKPIN-LQDQFLNQLRKERIPVTIFLVNGVKLQGKIKSFDNFTVLLERDGKQQLVYKHAISTIVPAR 67
hfq PRK00395
RNA-binding protein Hfq; Provisional
 1-77 1.68e-31

RNA-binding protein Hfq; Provisional


Pssm-ID: 179001  Cd Length: 79  Bit Score: 104.62  E-value: 1.68e-31
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254800720  1 MNKQQNnLQDIFLNSARKNKIPVTVYLSTGFKLNGIVKGFDSFTVILDSEGKQMLIYKHAITTVTPEKPILFVDNES 77
Cdd:PRK00395  1 MAKGQN-LQDPFLNALRKERVPVTIYLVNGIKLQGQIESFDNFVVLLRNTGKSQLVYKHAISTVVPARPVSLHEDEE 76
Hfq TIGR02383
RNA chaperone Hfq; This model represents the RNA-binding pleiotropic regulator Hfq, a small, ...
 6-66 4.86e-28

RNA chaperone Hfq; This model represents the RNA-binding pleiotropic regulator Hfq, a small, Sm-like protein of bacteria. It helps pair regulatory noncoding RNAs with complementary mRNA target regions. It enhances the elongation of poly(A) tails on mRNA. It appears also to protect RNase E recognition sites (A/U-rich sequences with adjacent stem-loop structures) from cleavage. Being pleiotropic, it differs in some of its activities in different species. Hfq binds the non-coding regulatory RNA DsrA (see Rfam RF00014) in the few species known to have it: Escherichia coli, Shigella flexneri, Salmonella spp. In Azorhizobium caulinodans, an hfq mutant is unable to express nifA, and Hfq is called NrfA, for nif regulatory factor (see . The name hfq reflects phenomenology as a host factor for phage Q-beta RNA replication. [Regulatory functions, Other]


Pssm-ID: 274101  Cd Length: 61  Bit Score: 95.48  E-value: 4.86e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254800720   6 NNLQDIFLNSARKNKIPVTVYLSTGFKLNGIVKGFDSFTVILDSEGKQMLIYKHAITTVTP 66
Cdd:TIGR02383  1 QNLQDQFLNQLRKERIPVTVFLVNGVQLKGVIESFDNFTVLLESQGKQQLIYKHAISTISP 61
Hfq cd01716
bacterial Hfq-like; Hfq, an abundant, ubiquitous RNA-binding protein, functions as a ...
 7-66 8.37e-28

bacterial Hfq-like; Hfq, an abundant, ubiquitous RNA-binding protein, functions as a pleiotropic regulator of RNA metabolism in prokaryotes, required for transcription of some transcripts and degradation of others. Hfq binds small RNA molecules called riboregulators that modulate the stability or translation efficiency of RNA transcripts. Hfq binds preferentially to unstructured A/U-rich RNA sequences and is similar to the eukaryotic Sm proteins in both sequence and structure. Hfq forms a homo-hexameric ring similar to the heptameric ring of the Sm proteins.


Pssm-ID: 212463  Cd Length: 60  Bit Score: 94.90  E-value: 8.37e-28
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254800720  7 NLQDIFLNSARKNKIPVTVYLSTGFKLNGIVKGFDSFTVILDSEGKQMLIYKHAITTVTP 66
Cdd:cd01716   1 NLQDQFLNTLRKEKKPVTIYLVNGVRLKGKIKSFDNFTVLLESDGKQQLIYKHAISTIVP 60
PRK14091 PRK14091
RNA chaperone Hfq;
1-70 2.16e-26

RNA chaperone Hfq;


Pssm-ID: 237607 [Multi-domain]  Cd Length: 165  Bit Score: 94.50  E-value: 2.16e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254800720   1 MNKQQNNLQDIFLNSARKNKIPVTVYLSTGFKLNGIVKGFDSFTVILDSEGKQMLIYKHAITTVTPEKPI 70
Cdd:PRK14091   5 MAEKVNNLQDIFLNSLRKTKTPVTMFLVKGVKLQGIITWFDNFSILLRRDGQSQLVYKHAISTIMPAHPL 74
PRK14091 PRK14091
RNA chaperone Hfq;
2-77 3.40e-18

RNA chaperone Hfq;


Pssm-ID: 237607 [Multi-domain]  Cd Length: 165  Bit Score: 73.31  E-value: 3.40e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254800720   2 NKQQNNLQDIFLNSARKNKIPVTVYLSTGFKLNGIVKGFDSFTVILDSEGKQMLIYKHAITTVTPEKPILFVDNES 77
Cdd:PRK14091  86 NKKSRLLQDVFLSAVRDSGEPVTMFLVNGVMLQGEIAAFDLFCMLLERDGYVQLVYKHAVSTVQPAGPVDLTDTED 161
 
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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