HAMAP rule MF_01323

General rule information [?]

Accession	MF_01323
Dates	6-JAN-2004 (Created) 2-SEP-2024 (Last updated, Version 37)
Name	RNApol_bact_RpoC1
Scope(s)	Bacteria Cyanobacteriota Plastid
Template(s)	P22704 (RPOC1_NOSS1); P11705 (RPOC1_SPIOL); [ Recover all ]
Triggered by	HAMAP; MF_01323 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier	RPOC1
case not <OG:Chloroplast>
Protein name	RecName: Full=DNA-directed RNA polymerase subunit gamma; Short=RNAP subunit gamma; EC=2.7.7.6; AltName: Full=RNA polymerase subunit gamma; AltName: Full=Transcriptase subunit gamma;
else case <OG:Chloroplast>
Protein name	RecName: Full=DNA-directed RNA polymerase subunit beta'; EC=2.7.7.6; AltName: Full=PEP; AltName: Full=Plastid-encoded RNA polymerase subunit beta'; Short=RNA polymerase subunit beta';
end case
Gene name	Name=rpoC1;

Comments [?]

FUNCTION	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
CATALYTIC ACTIVITY	Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate; Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA- COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6;
case <FTGroup:2>
COFACTOR	Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.;
end case
case <FTGroup:1>
COFACTOR	Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 Zn(2+) ion per subunit.;
end case
case <OC:Cyanobacteriota>
SUBUNIT	In cyanobacteria the RNAP catalytic core is composed of 2 alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.
else case <OG:Chloroplast>
SUBUNIT	In plastids the minimal PEP RNA polymerase catalytic core is composed of four subunits: alpha, beta, beta', and beta''. When a (nuclear-encoded) sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.
SUBCELLULAR LOCATION	Plastid, chloroplast.
end case
SIMILARITY	Belongs to the RNA polymerase beta' chain family. RpoC1 subfamily.

Keywords [?]

case <FTGroup:1> or <FTGroup:2>
Metal-binding
end case
case <FTGroup:2>
Magnesium
end case
Transcription
Transferase
Nucleotidyltransferase
DNA-directed RNA polymerase
case <FTGroup:1>
Zinc
end case

Gene Ontology [?]

GO:0003677; Molecular function:DNA binding
GO:0003899; Molecular function:DNA-directed 5'-3' RNA polymerase activity
GO:0006351; Biological process:DNA-templated transcription
case <FTGroup:2>
GO:0000287; Molecular function:magnesium ion binding
end case
case <FTGroup:1>
GO:0008270; Molecular function:zinc ion binding
end case
case <OG:Chloroplast>
GO:0009507; Cellular component:chloroplast
end case

Cross-references [?]

Pfam	PF04997; RNA_pol_Rpb1_1; 1;
Pfam	PF00623; RNA_pol_Rpb1_2; 1-2;
Pfam	PF04983; RNA_pol_Rpb1_3; 0-1;
NCBIfam	TIGR02387; rpoC1_cyan; 1;

Features [?]

From: RPOC1_NOSS1 (P22704)
Key	From	To	Description	Tag	Condition	FTGroup
BINDING	71	71	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105"		C	1
BINDING	73	73	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105"		C	1
BINDING	86	86	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105"		C	1
BINDING	89	89	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105"		C	1
BINDING	467	467	/ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420"		D	2
BINDING	469	469	/ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420"		D	2
BINDING	471	471	/ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420"		D	2

Additional information [?]

Size range	575-760 amino acids
Related rules	MF_01322
Fusion	Nter: None Cter: MF_01324 (rpoC2)
Comments	In cyanobacteria and plastids, there are two ORFs (this one, rpoC1, MF_01323 and rpoC2, MF_01324) that together are equivalent to the beta' subunit found in all other bacteria (rpoC, MF_01322). However,in the red algae CYAM1 the rpoC1 and rpoC2 genes are fused into one ORF. This seems to be the result of evolution acting to reduce protein size rather than horizontal transfer from a bacteria. Some algal proteins with inserts and C.reinhardtii (where this protein is split in 2) are considered to be atypical.

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