ID A0A165ZAG2_9EURY Unreviewed; 876 AA.
AC A0A165ZAG2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=rpoC_2 {ECO:0000313|EMBL:KZX10469.1};
GN Synonyms=rpo1N {ECO:0000256|HAMAP-Rule:MF_00863}, rpoA1
GN {ECO:0000256|HAMAP-Rule:MF_00863};
GN ORFNames=MBCUR_17600 {ECO:0000313|EMBL:KZX10469.1};
OS Methanobrevibacter curvatus.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=49547 {ECO:0000313|EMBL:KZX10469.1, ECO:0000313|Proteomes:UP000077245};
RN [1] {ECO:0000313|EMBL:KZX10469.1, ECO:0000313|Proteomes:UP000077245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11111 {ECO:0000313|EMBL:KZX10469.1,
RC ECO:0000313|Proteomes:UP000077245};
RA Poehlein A., Seedorf H., Daniel R.;
RT "Genome sequence of Methanobrevibacter curvatus DSM 11111.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZX10469.1}.
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DR EMBL; LWMV01000212; KZX10469.1; -; Genomic_DNA.
DR RefSeq; WP_067092534.1; NZ_LWMV01000212.1.
DR AlphaFoldDB; A0A165ZAG2; -.
DR STRING; 49547.MBCUR_17600; -.
DR PATRIC; fig|49547.3.peg.1866; -.
DR OrthoDB; 371812at2157; -.
DR Proteomes; UP000077245; Unassembled WGS sequence.
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 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:UP000077245};
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 201..505
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
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 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 451
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00863"
SQ SEQUENCE 876 AA; 98534 MW; DBD9DD437803EC09 CRC64;
MKEIIKKIDH INFGLMSPEN IRKNSVIKIV TPDTYDEDGY PIENGLMDPH LGVIDPSLKC
KTCGSKGGEC LGHFGSIDLA RPVVHVGFAD NIYKILRSVC NECGRVLLTD TEIENFKYEI
LMAMDNEESI NEIIKRVQDA AKKDKCPHCE EKQSDIKIDK PTSINDGDYR LTASEIRDRL
ERITDEDALV LGVNPKVARP EWMVLTVLPV PPVTVRPSIT LETGERSEDD LTHKLVDILR
INQRLSENME AGAPQLIVED LWELLQYHVT TYFDNEASGV PPARHRSGRP LKTLAQRLKG
KEGRFRSNLS GKRVNFSART VISPDPNISI NEVGVPEMIA TEVTVPVHVN DWNIEELKKY
ILNGPEVHPG ANYVIRSDDR KIRVYDDTKD SIIENIEPGW VVERHLKDGD IVLFNRQPSL
HRMSMMAHEV KVLPYKTFRL NLCVCPPYNA DFDGDEMNMH VFQTDESRAE AKSLMRVQEH
ILSPRFGGPI IGAIHDHISG AYLLTRNGST FTEEQAFQII RKAKLPIPKR KNPNDNPELG
TNWTGKELFS LLLPEKLNLE YKGEICKNCQ VCKERDCEFD SYVVIEDGEL KYGALDEKAY
GSFSGKILDK IVKDYGSDTA KEFLDRSTNM AISGIMKVGI TTSTNDEEIP QEAQDRIQAH
LDDAEENVDR HVKAYEEGEL EALPGRSLEE TLEMKIMQVL GEARDKSGEI AESYFAMETN
HSVVMAKTGA RASMLNLTQI TACVGQQSVR GGRISRGYIE RTLPHFRKNE LGAKARGFVH
SSYKSGLDPV EFFFHAMGGR EGLVDTAIRT AQSGYMQRRL VNALQDLKVT ENGLVQDNKG
NVIQTMFGED GVDPAKSDHG KAADLDKIIK EMRIKK
//
