RPO1N_THEAC
ID RPO1N_THEAC Reviewed; 885 AA.
AC Q03585;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 115.
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}; OrderedLocusNames=Ta0391;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=1408839; DOI=10.1093/nar/20.19.5226;
RA Klenk H.-P., Renner O., Schwass V., Zillig W.;
RT "Nucleotide sequence of the genes encoding the subunits H, B, A' and A'' of
RT the DNA-dependent RNA polymerase and the initiator tRNA from Thermoplasma
RT acidophilum.";
RL Nucleic Acids Res. 20:5226-5226(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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; X68198; CAA48281.1; -; Genomic_DNA.
DR EMBL; AL445064; CAC11535.1; -; Genomic_DNA.
DR PIR; S26723; S26723.
DR RefSeq; WP_010900820.1; NC_002578.1.
DR AlphaFoldDB; Q03585; -.
DR SMR; Q03585; -.
DR STRING; 273075.Ta0391; -.
DR EnsemblBacteria; CAC11535; CAC11535; CAC11535.
DR GeneID; 1456007; -.
DR KEGG; tac:Ta0391; -.
DR eggNOG; arCOG04257; Archaea.
DR HOGENOM; CLU_000487_3_1_2; -.
DR OMA; AVCPPYN; -.
DR OrthoDB; 3905at2157; -.
DR Proteomes; UP000001024; Chromosome.
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; 1.10.274.100; -; 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; IPR042102; RNA_pol_Rpb1_3_sf.
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; Reference proteome; Transcription;
KW Transferase; Zinc.
FT CHAIN 1..885
FT /note="DNA-directed RNA polymerase subunit Rpo1N"
FT /id="PRO_0000074009"
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 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
FT BINDING 468
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863"
SQ SEQUENCE 885 AA; 100075 MW; 390C4554F02947D7 CRC64;
MMGISKRISS IKFALLSPDE IRKLSQVKVI TADTYDDDGY PIEHGLMDLH MGVIEPGLRC
ATCGGKVDEC PGHFGHIELA MPVVHVGFVK EIKMFLDATC RSCGRIKLTD DEIRTYLPEI
QKMDFETGDP EDIEILTKKY VDLASQRMVC PHCGAQQSKI ILDKPTTFRE EGTNVKITPK
EIRERLERIP DDDLIFFGFN PKTARPEWMV LTVLPVPPIN VRPSITLETG ERSEDDLTHK
LVDIIRISQR LRESRDNGSP QLIIEDLWDL LQFHVTTYFD NQTPGIPPAR HRSGRALKTL
VQRLKGKEGR FRSNLSGKRV SFSSRTVISP EPYLSVNEVG VPERAARELT VPVIVNQFNI
DEMRELIKRG RNPRDQFGRY VTGVNYVIRP DGRRIKITDQ NAAENADRID IGWTVERQLM
EGDIVLFNRQ PSLHRMSMMG HTVRILPGQT FRFNLAVCTP YNADFDGDEM NLHVIQKEEA
RAEARIIMKV QEQIMSPRFG GPIIGGIHDH VTALFLLTHN NPRYTHEEMV HIMAYLEPDL
LPEARIENGE KYYYGRDIFS TILPKGLNVR FRSKLCSGSS ERCEFEDDPS DTYVEIVDGK
MIHGTIDEAA VSPFSGAIID KIFRKFGSQE AARFIDRMTR LAVGFITYRG FSTGISDYDI
PESAVARIEE LVAQAEDRIN KLIETFRRGE LQPAPGRSVE DTLEMEILSE AGVVRDESGK
IASSYLGLKV PSVIMARSGA RATMLNISEV AGIVGQQSVR GGRLNRGYYN RTLPHFKRGD
IGADARGFVR SSYMTGLSPT EYFFHSIGGR EGLVDTAVRT SRSGYMQRRL INAFEDLKVD
DSREVKDTVG SLIQIRYGED GIDPTRSARG KAVDMNYILF DEERR
