| Accession | TIGR02383 |
| Name | Hfq |
| Function | RNA chaperone Hfq |
| Gene Symbol | hfq |
| Trusted Cutoff | 61.70 |
| Domain Trusted Cutoff | 61.70 |
| Noise Cutoff | 31.15 |
| Domain Noise Cutoff | 31.15 |
| Isology Type | equivalog |
| HMM Length | 61 |
| Mainrole Category | Regulatory functions |
| Subrole Category | Other |
| Gene Ontology Term | GO:0003723: RNA binding molecular_function |
| | GO:0006378: mRNA polyadenylation biological_process |
| | GO:0016070: RNA metabolic process biological_process |
| Author | Haft DH |
| Entry Date | Nov 29 2004 1:11PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | 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 PMID:8197116). The name hfq reflects phenomenology as a host factor for phage Q-beta RNA replication. |
| References | DR PFAM; PF01423; LSM domain
RN [1]
RM 15531892
RT Escherichia coli Hfq has distinct interaction surfaces for DsrA, rpoS and poly(A) RNAs.
RA Mikulecky PJ, Kaw MK, Brescia CC, Takach JC, Sledjeski DD, Feig AL.
RL Nat Struct Mol Biol. 2004 in press
RN [2]
RM 14561880
RT Coincident Hfq binding and RNase E cleavage sites on mRNA and small regulatory RNAs.
RA Moll I, Afonyushkin T, Vytvytska O, Kaberdin VR, Blasi U.
RL RNA. 2003 Nov;9(11):1308-14.
DR HAMAP; MF_00436; 258 of 263 |
