AC   MF_00863;
DC   Protein; auto
TR   HAMAP; MF_00863; -; 1; level=0
XX
Names: RNApol_arch_Rpo1N
XX
ID   RPO1N
DE   RecName: Full=DNA-directed RNA polymerase subunit Rpo1N;
DE            EC=2.7.7.6;
DE   AltName: Full=DNA-directed RNA polymerase subunit A';
GN   Name=rpo1N; Synonyms=rpoA1;
XX
CC   -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC       transcription of DNA into RNA using the four ribonucleoside
CC       triphosphates as substrates. Forms the clamp head domain.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.6;
case <FTGroup:3>
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
end case
case <FTGroup:1> and <FTGroup:2>
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds at least 2 Zn(2+) per subunit.
end case
CC   -!- SUBUNIT: Part of the RNA polymerase complex.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
XX
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 1-2; trigger=no
DR   Pfam; PF04983; RNA_pol_Rpb1_3; 1; trigger=no
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 1; trigger=no
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1; trigger=no
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1; trigger=no
DR   NCBIfam; TIGR02390; RNA_pol_rpoA1; 1; trigger=no
XX
KW   Cytoplasm
KW   DNA-binding
KW   DNA-directed RNA polymerase
case <FTGroup:3>
KW   Magnesium
end case
KW   Metal-binding
KW   Nucleotidyltransferase
KW   Transcription
KW   Transferase
case <FTGroup:1> and <FTGroup:2>
KW   Zinc
end case
XX
GO   GO:0005737; C:cytoplasm
GO   GO:0003677; F:DNA binding
GO   GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity
case <FTGroup:3>
GO   GO:0000287; F:magnesium ion binding
end case
GO   GO:0006351; P:DNA-templated transcription
case <FTGroup:1> and <FTGroup:2>
GO   GO:0008270; F:zinc ion binding
end case
XX
FT   From: RPO1N_SACSH (B8YB53)
FT   BINDING         58
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Group: 1; Condition: C
FT   BINDING         61
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Group: 1; Condition: C
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Group: 1; Condition: C
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   Group: 1; Condition: H
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Group: 2; Condition: C
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Group: 2; Condition: C
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Group: 2; Condition: C
FT   BINDING         149
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   Group: 2; Condition: C
FT   BINDING         456
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 3; Condition: D
FT   BINDING         458
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 3; Condition: D
FT   BINDING         460
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 3; Condition: D
XX
Size: 820-1070;
Related: None;
Template: B8YB53; P11512; Q980R2;
Scope:
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: 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.
# Revision 1.7 2023/06/01
//