ID S5ZUY1_9CREN Unreviewed; 890 AA.
AC S5ZUY1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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 ORFNames=N186_02335 {ECO:0000313|EMBL:AGT34854.1};
OS Thermofilum adornatum.
OC Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Thermofilum.
OX NCBI_TaxID=1365176 {ECO:0000313|EMBL:AGT34854.1, ECO:0000313|Proteomes:UP000015543};
RN [1] {ECO:0000313|EMBL:AGT34854.1, ECO:0000313|Proteomes:UP000015543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1910b {ECO:0000313|Proteomes:UP000015543};
RX PubMed=24029764;
RA Dominova I.N., Kublanov I.V., Podosokorskaya O.A., Derbikova K.S.,
RA Patrushev M.V., Toshchakov S.V.;
RT "Complete Genomic Sequence of 'Thermofilum adornatus' Strain 1910bT, a
RT Hyperthermophilic Anaerobic Organotrophic Crenarchaeon.";
RL Genome Announc. 1:e00726-13(2013).
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|ARBA:ARBA00006460, ECO:0000256|HAMAP-Rule:MF_00863,
CC 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; CP006646; AGT34854.1; -; Genomic_DNA.
DR AlphaFoldDB; S5ZUY1; -.
DR KEGG; thb:N186_02335; -.
DR PATRIC; fig|1365176.7.peg.465; -.
DR eggNOG; arCOG04257; Archaea.
DR HOGENOM; CLU_000487_3_1_2; -.
DR Proteomes; UP000015543; 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; 1.10.132.30; -; 1.
DR Gene3D; 2.40.40.20; -; 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 Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
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 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:UP000015543};
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 211..516
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT COILED 664..691
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
SQ SEQUENCE 890 AA; 100483 MW; 0140AD56564AADE2 CRC64;
MGMSTRESSK IIAGLKFGIL SPEMIRKLAV LRIETSELYD DEGFPIPGGL MDRRMGSIEP
GAVCQTCGNR FTNCPGHFGY IELARPVVHP EFTPYIALLL KATCSKCGRL KLDEERIEKA
RKRMEVYSRK WPSLKIKYAN TLLKEAAKAT ECPHCHAPQY KIKVDKPYTF YEEREEGLVR
LTPLEIWERL SRIPDKDLEV VGIDPKEARP EWMVLRVVPV VPPSVRPSIT LESGDRSEDD
LTHKLVDIIR VNQRLKENID SGSPSLVIED LWGLLQYHVA TYFDNELPGI PPARHRSGRA
LRTLAQRLKG KEGRFRGSLA GKRVDFSSRT VISPDPNLSI NEVGVPIDVA KVLTVPEKVT
SWNIEKMRQL VINGPDVWPG ANYIIKPDGS RIDLRFAKHR EELSQALAPG YIVERHLMDG
DIVLFNRQPS LHRISIMAHV VRVLPYKTFR LNLLVTIPYN ADFDGDEMNL HVPQSEEARA
EARELMLVER HIMTARYGAP IIGGLHDYIT GAYLLTRKDT LLDKKEALRL LYLGNNSEPL
VEPAILKPGP YWTGKQLVSM FLPKGLNYVG RASVAPSSGK CDEEYCENDG YILIKDGKLL
LGVFDKQAIG AEKHGTVLHE IVREYGVEKA RELMDGMFKV FVEYLDKYGF TMGVDSVEIP
PEAERDVQEI VREAEKRVQE LIEQYRSGEL QPMPGKTRKE TLEDLIMNVL AEARTRAGEI
VSRHLGLLNH AVIMARTGAR GSMLNLTQMA AIVGQQSVRG KRIERGYSGR TLSHFPVNDL
SPQAKGFVQS SFRRGLSPEE FFFHAISGRE GLVDTAVRTA QSGYMYRRLQ SAMQDFYVSY
DGTVRNSEGL VIQYRYGEDG VDPSRSDHGK PVDVDKLIKK VLAMRGERHE
//
