RPO1N_METTW
ID RPO1N_METTW Reviewed; 865 AA.
AC P09846;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo1N {ECO:0000255|HAMAP-Rule:MF_00863};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00863};
DE AltName: Full=DNA-directed RNA polymerase subunit A' {ECO:0000255|HAMAP-Rule:MF_00863};
GN Name=rpo1N {ECO:0000255|HAMAP-Rule:MF_00863};
GN Synonyms=rpoA1 {ECO:0000255|HAMAP-Rule:MF_00863}, rpoT;
OS Methanothermobacter thermautotrophicus (strain Winter) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79930;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2843811; DOI=10.1093/nar/16.16.8113;
RA Berghoefer B., Kroeckel L., Koertner C., Truss M., Schallenberg J.,
RA Klein A.;
RT "Relatedness of archaebacterial RNA polymerase core subunits to their
RT eubacterial and eukaryotic equivalents.";
RL Nucleic Acids Res. 16:8113-8128(1988).
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 {ECO:0000255|HAMAP-Rule:MF_00863}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_00863};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00863};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00863};
CC Note=Binds at least 2 Zn(2+) per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00863};
CC -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000255|HAMAP-
CC Rule:MF_00863}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00863}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00863}.
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DR EMBL; X08038; CAA30838.1; -; Genomic_DNA.
DR PIR; S02196; S02196.
DR AlphaFoldDB; P09846; -.
DR SMR; P09846; -.
DR PRIDE; P09846; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd02582; RNAP_archeal_A; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 4.10.860.120; -; 2.
DR HAMAP; MF_00863; RNApol_arch_Rpo1N; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR InterPro; IPR012758; RPO1N.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR TIGRFAMs; TIGR02390; RNA_pol_rpoA1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA-binding; DNA-directed RNA polymerase; Magnesium;
KW Metal-binding; Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT CHAIN 1..865
FT /note="DNA-directed RNA polymerase subunit Rpo1N"
FT /id="PRO_0000074005"
FT REGION 500..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 451
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
SQ SEQUENCE 865 AA; 97519 MW; 33C65710C6A4E7D6 CRC64;
MRGILKKISQ INFGLMSPED IRKMSVAQIV TPDTYDEDGY PIENELMDPR LGVIGSSLRC
RSCGAKGGEC PGHFGSINLA RPVIHVGFAD TIHKILSSIC RKCSRILLTE TEIQDYRQRI
LEAMEREESL TPIIKEIYAE ARRDRCPHCE EEQEEIKLDK PVSIVEGDYK LTPSEVRERL
ERITDNDSLL LGVNPEVARP EWMVLTVLPV PPVTVRPSIT LETGERSEDD LTHKLVDILR
INQRLKENME AGAPQLIVED LWELLQYHVT TYFDNEASGV PPARHRSGRP LKTLAQRLKG
KEGRFRSNLS GKRVNFSART VVSPDPNVSV NEVGVPELIA KEVTVPVYVT EWNIDRMKEH
IENGPDVHPG ANYVIRPDGR KIRAYNETKD VVLENLKPGY IVERHLKDGD IVLFNRQPSL
HRMSMMAHEV RVLPYKTFRL NLCVCPPYNA DFDGDEMNMH VFQTEESRAE AKTLMRVQDH
ILSPRFRDLS SGVYTTISQE HTSSQGKRLF SVRSRPPDPQ EGRAPPPDRE GREWTVKEIF
SMVLPDDLNM VYLAEICRKC DECLEMDWEN DAYVVIENGQ LITGVIDEKA YGAFAGKILD
QIVKEYGSDA AKEFLDSATK LAIAGIMHAG FTTSTNDEEI PEEAKERIEA HLRNAEARVD
QLIEAYENGE LEPLPGRSLE ETLEMKIMQV LGEAKDKSGE IAESYFDMDE NHAVIMALTG
ARGAMLNLTQ ITACVGQQSV HGGRITRGYD NRTLPHFKKG ELGAKSRGFV HSSYKEDSIL
LEFMGGREGL VDTAIRTAQS GYMQRRLVNA LQDLTVDENG RVVDNRGVII QTRFGEDGVD
PAKSDYGKIV DLDKLVQEIR LKSGK
