ID I0A0T4_FERFK Unreviewed; 882 AA.
AC I0A0T4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo1N {ECO:0000256|HAMAP-Rule:MF_00863};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_00863};
DE AltName: Full=DNA-directed RNA polymerase subunit A' {ECO:0000256|HAMAP-Rule:MF_00863};
GN Name=rpo1N {ECO:0000256|HAMAP-Rule:MF_00863};
GN Synonyms=rpoA1 {ECO:0000256|HAMAP-Rule:MF_00863};
GN OrderedLocusNames=FFONT_0601 {ECO:0000313|EMBL:AFH42591.1};
OS Fervidicoccus fontis (strain DSM 19380 / JCM 18336 / VKM B-2539 / Kam940).
OC Archaea; Thermoproteota; Thermoprotei; Fervidicoccales; Fervidicoccaceae;
OC Fervidicoccus.
OX NCBI_TaxID=1163730 {ECO:0000313|EMBL:AFH42591.1, ECO:0000313|Proteomes:UP000007391};
RN [1] {ECO:0000313|Proteomes:UP000007391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19380 / VKM B-2539 / Kam940
RC {ECO:0000313|Proteomes:UP000007391};
RA Lebedinsky A.V., Mardanov A.V., Gumerov V.M., Beletsky A.V., Kublanov I.V.,
RA Perevalova A.A., Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Fervidicoccus fontis complete genome analysis confirms its distinct
RT phylogenetic position and predicts its environmental function.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFH42591.1, ECO:0000313|Proteomes:UP000007391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19380 / VKM B-2539 / Kam940
RC {ECO:0000313|Proteomes:UP000007391};
RX PubMed=24366681; DOI=10.1007/s00792-013-0616-7;
RA Lebedinsky A.V., Mardanov A.V., Kublanov I.V., Gumerov V.M., Beletsky A.V.,
RA Perevalova A.A., Bidzhieva S.Kh., Bonch-Osmolovskaya E.A., Skryabin K.G.,
RA Ravin N.V.;
RT "Analysis of the complete genome of Fervidococcus fontis confirms the
RT distinct phylogenetic position of the order Fervidicoccales and suggests
RT its environmental function.";
RL Extremophiles 18:295-309(2014).
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:0000256|HAMAP-Rule:MF_00863}.
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000256|RuleBase:RU004279}.
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:0000256|ARBA:ARBA00024550,
CC ECO:0000256|HAMAP-Rule:MF_00863, ECO:0000256|RuleBase:RU004279};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00863};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00863};
CC Note=Binds at least 2 Zn(2+) per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00863};
CC -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000256|HAMAP-
CC Rule:MF_00863}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00863}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|HAMAP-Rule:MF_00863, ECO:0000256|RuleBase:RU004279}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003423; AFH42591.1; -; Genomic_DNA.
DR AlphaFoldDB; I0A0T4; -.
DR STRING; 1163730.FFONT_0601; -.
DR KEGG; ffo:FFONT_0601; -.
DR eggNOG; arCOG04257; Archaea.
DR HOGENOM; CLU_000487_3_1_2; -.
DR InParanoid; I0A0T4; -.
DR OrthoDB; 371812at2157; -.
DR Proteomes; UP000007391; 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-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd02582; RNAP_archeal_A; 1.
DR Gene3D; 1.10.10.1950; -; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 2.60.40.2940; -; 1.
DR Gene3D; 4.10.320.40; -; 1.
DR Gene3D; 6.10.250.2940; -; 1.
DR Gene3D; 6.20.50.80; -; 1.
DR Gene3D; 3.30.1490.180; RNA polymerase ii; 1.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 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 NCBIfam; TIGR02390; RNA_pol_rpoA1; 1.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF37; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1; 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 SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00863};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00863};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_00863};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00863};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00863};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00863}; Reference proteome {ECO:0000313|Proteomes:UP000007391};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00863};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00863}; Zinc {ECO:0000256|HAMAP-Rule:MF_00863}.
FT DOMAIN 207..512
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT COILED 653..687
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 458
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
SQ SEQUENCE 882 AA; 100227 MW; 2F7CD5B29216F59D CRC64;
MPGVQKKIKG IKLSVLSPDE IRRMSKVQII TAETYDDDGL PIQGGVMDPR LGVIEPGQKC
PVCGNTMQSC PGHFGHIELA KPVIHIGYVK EIYDLLRGTC WKCGRILLPE EEIKQYLDLM
RRVEKYMPFL LPRLYEHIKQ KASKTTVCPH CGAAQRKIKL ERPTTFLEEE KGSSRKLAPD
EIRNRLSNTP DDDVRLFGIN PEDSRPEWFI LTVLPVPPVQ VRPSIMLETG IRAEDDLTHK
LVDIVRTNQR LKESMEAAAP PIVIDDIWEL LQYHVTTYFD NEVPGIPPAK HRTGRALKTL
AQRLKGKEGR FRGYLSGKRV DFSSRTVISP DPNIGINEVG VPEDAAKILT VPVKVTQWNL
EEMRSYVLNG PYKWPGANYI IRPDGKRVDL RYFKDRKALA SSLTPGYIIE RHLIDGDIVL
FNRQPSLHRM SIMAHQVKVL PGRTFRLNLL VCPPYNADFD GDEMNLHVPQ TEEARAEAKE
LMLVQRHILS PRYGGPIIGG LQDYISGGYL LTSKATLLEK EDVIEVLSVT GYKEELPEPA
IYSPKEFWTG KQLVSLFLPK DFTLKTKASI NAGKLKCEDE DCLNDSYIVI KKGKMHTGVI
DKKSIGAQQP ESFYHWITKE YGSDYARYIS DVMFKMFIRY IEKHGFTMSL DDVEISEEAR
EEIRKILKKA EDDVNELIRM MEEGRLEPLP GRTIEETLET KIMERLSKAR DDAGEYAANN
LDIFNNAFIM ARTGARGNIL NLTQMSATLG QQSIRGERIN RGYRNRPLPH FKENDKSPAS
RGFVYNSFRT GLNPVELFYH AAGGREGLVD TAVRTSQSGY MQRRLINALL DVRIEYDGSA
RLPDGTVVQF KYGYDQVDPA KSDHGKAVNV DRIIERVVGW RE
//
