HAMAP rule MF_00863

General rule information [?]

Accession	MF_00863
Dates	18-JUN-2021 (Created) 19-NOV-2022 (Last updated, Version 6)

Name	RNApol_arch_Rpo1N

Scope

Archaea

Templates

B8YB53 (RPO1N_SACSH); P11512 (RPO1N_SULAC); Q980R2 (RPO1N_SACS2): [Recover all]

Triggered by

HAMAP; MF_00863 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier

RPO1N

Protein name

RecName:		Full=DNA-directed RNA polymerase subunit Rpo1N;
		EC 2.7.7.6;
AltName:		Full=DNA-directed RNA polymerase subunit A';

Gene name

rpo1N, rpoA1

Comments [?]

Function	DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms the clamp head domain.
Catalytic activity	RHEA:21248: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1) EC 2.7.7.6

case <FTGroup:3>

Cofactor

Mg(2+)

end case

case <FTGroup:1> and <FTGroup:2>

Cofactor

Zn(2+)
Note: Binds at least 2 Zn(2+) per subunit

end case

Subunit	Part of the RNA polymerase complex.
Subcellular location	Cytoplasm.
Similarity	Belongs to the RNA polymerase beta' chain family.

Cross-references [?]

Pfam	PF00623; RNA_pol_Rpb1_2; 1-2;
	PF04983; RNA_pol_Rpb1_3; 1;
	PF04997; RNA_pol_Rpb1_1; 1;
	PF04998; RNA_pol_Rpb1_5; 1;
	PF05000; RNA_pol_Rpb1_4; 1;
TIGRFAMs	TIGR02390; RNA_pol_rpoA1; 1;

Keywords [?]

Cytoplasm
DNA-binding
DNA-directed RNA polymerase

case <FTGroup:3>

Magnesium

end case

Metal-binding
Nucleotidyltransferase
Transcription
Transferase

case <FTGroup:1> and <FTGroup:2>

Zinc

end case

Gene Ontology [?]

GO:0005737; Cellular component: cytoplasm.
GO:0003677; Molecular function: DNA binding.
GO:0003899; Molecular function: DNA-directed 5'-3' RNA polymerase activity.

case <FTGroup:3>

GO:0000287; Molecular function: magnesium ion binding.

end case

GO:0006351; Biological process: DNA-templated transcription.

case <FTGroup:1> and <FTGroup:2>

GO:0008270; Molecular function: zinc ion binding.

end case

Features [?]

From: RPO1N_SACSH (B8YB53)

Key From To Description Tag Condition FTGroup

BINDING 58 58 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1 C 1

BINDING 61 61 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1 C 1

BINDING 68 68 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1 C 1

BINDING 71 71 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1 H 1

BINDING 98 98 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2 C 2

BINDING 101 101 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2 C 2

BINDING 146 146 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2 C 2

BINDING 149 149 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2 C 2

BINDING 456 456 /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420 D 3

BINDING 458 458 /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420 D 3

BINDING 460 460 /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420 D 3

Additional information [?]

Size range	820-1070 amino acids
Related rules	None
Fusion	None
Comments	Intein deleted in METJA. In some archaea (including Thaumarchaeota and Korarchaeum cryptofilum) Rpo1N and Rpo1C are fused. A third Zn(2+) is present in S.acidocaldarius; the residues which bind this Zn are conserved in other known Sulfolobales and a few other archaea.

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