HAMAP logo

HAMAP rule MF_01884

Send feedback

General rule information [?]

PURL https://purl.expasy.org/hamap/rule/MF_01884
Accession MF_01884
Dates 04-AUG-2010 (Created)
12-MAY-2026 (Last updated, Version )
Name Rho
Scope(s) Bacteria
Template(s) P0AG30 (RHO_ECOLI); P9WHF3 (RHO_MYCTU); Q5SJE9 (RHO_THET8); P52154 (RHO_MICLU); Q03222 (RHO_BACSU); Q5LAX6 (RHO_BACFN); [ Recover all ]
Triggered by HAMAP; MF_01884 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier RHO
Protein name RecName: Full=Transcription termination factor Rho;
                 EC=3.6.4.-;
AltName: Full=ATP-dependent helicase Rho;
Gene name Name=rho;

Comments [?]

FUNCTIONFacilitates transcription termination from RNA polymerase (RNAP) by binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, translocation in a 5'-3' direction on the RNA (toward RNAP), and release of the RNA from the DNA template.
FUNCTIONPlays a major role in reduction of R-loop formation across the genome; R-loops can be generated by annealing of untranslated, (often antisense) RNA to upstream DNA.
CATALYTIC ACTIVITY Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
SUBUNITHomohexamer. The homohexamer assembles into a catalytically inactive open ring structure; the active homohexamer is a closed ring which encircles RNA. Contacts RNA polymerase (RNAP) via its C-terminal domains, allowing RNA to pass through the central channel.
SUBCELLULAR LOCATIONCytoplasm.
DOMAINThe N-terminus consists of a helical bundle and an OB-fold which form the primary RNA-binding site (PBS, part of Rho RNA-BD) on the surface of the hexameric ring. The N-terminus is joined by a linker to the C-terminal domain, which has a RecA-type fold. Six C-terminal domains form a central channel through which single-stranded (ss)RNA passes; ATP binds between the protomers. The secondary RNA-binding site (SBS) is formed by Q- and R-loops in the center of the ring which recognize pyrimidine-rich RNA.
SIMILARITYBelongs to the Rho family.

Keywords [?]

ATP-binding
Cytoplasm
Hydrolase
Magnesium
Metal-binding
Nucleotide-binding
RNA-binding
Transcription
Transcription regulation
Transcription termination

Gene Ontology [?]

GO:0005524; Molecular function:ATP binding
GO:0003723; Molecular function:RNA binding
GO:0006353; Biological process:DNA-templated transcription termination
GO:0039630; Molecular function:RNA translocase activity
GO:0062176; Biological process:R-loop processing
GO:0005737; Cellular component:cytoplasm

Cross-references [?]

Pfam PF00006; ATP-synt_ab; 1;
Pfam PF07498; Rho_N; 1;
Pfam PF07497; Rho_RNA_bind; 1;
NCBIfam TIGR00767; Rho; 1;
PROSITE PS51856; RHO_RNA_BD; 1;

Features [?]

From: RHO_ECOLI (P0AG30)
Key From To Description Tag Condition FTGroup
BINDING 169 174 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 G-x-G-x-x-[GAS]
BINDING 185 185 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"		 T
BINDING 181 186 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 [KR]-x-G-K-[TS]-x
MOTIF 279 290 /note=Q-loop [PDTRSQ]-[AGSTHPG]-[STG]-G-[KR]-[ITVL]-[LM]-[STA]-G-G-[VLI]-[DEG]
MOTIF 322 326 /note=R-loop [ED]-T-[GE]-S-[RKT]
BINDING 212 212 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 R
BINDING 366 366 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 [RK]
BINDING 367 367 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 [RK]

Additional information [?]

Size range 341-849 amino acids
Related rules None
Fusion Nter: None Cter: None
Comments Rho in E.coli, B.fragilis, B.subtilis and M.tuberculosis have an in vitro 5'-3' RNA:DNA helicase activity. The relevance of this RNA:DNA helicase activity to its in vivo function(s) or mechanism of action remains uncertain.



View rule in raw text format (no links)