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Annotation rule MF_00863
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General rule information [?]

Accession MF_00863
Dates 18-JUN-2021 (Created)
28-JUN-2022 (Last updated, Version 5)
Name RNApol_arch_Rpo1N
Scope
Archaea
Templates B8YB53 (RPO1N_SACSH); P11512 (RPO1N_SULAC); Q980R2 (RPO1N_SACS2): [Recover all]
Triggered by

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="29105" /ligand_label="1     C   1
BINDING     61     61       /ligand="Zn(2+)" /ligand_id="29105" /ligand_label="1     C   1
BINDING     68     68       /ligand="Zn(2+)" /ligand_id="29105" /ligand_label="1     C   1
BINDING     71     71       /ligand="Zn(2+)" /ligand_id="29105" /ligand_label="1     H   1
BINDING     98     98       /ligand="Zn(2+)" /ligand_id="29105" /ligand_label="2     C   2
BINDING     101     101       /ligand="Zn(2+)" /ligand_id="29105" /ligand_label="2     C   2
BINDING     146     146       /ligand="Zn(2+)" /ligand_id="29105" /ligand_label="2     C   2
BINDING     149     149       /ligand="Zn(2+)" /ligand_id="29105" /ligand_label="2     C   2
BINDING     456     456       /ligand="Mg(2+)" /ligand_id="18420     D   3
BINDING     458     458       /ligand="Mg(2+)" /ligand_id="18420     D   3
BINDING     460     460       /ligand="Mg(2+)" /ligand_id="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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