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RPO1N_METTH
ID   RPO1N_METTH             Reviewed;         870 AA.
AC   O27125;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 123.
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};
GN   OrderedLocusNames=MTH_1051;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
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; AE000666; AAB85542.1; -; Genomic_DNA.
DR   PIR; G69006; G69006.
DR   RefSeq; WP_010876677.1; NC_000916.1.
DR   AlphaFoldDB; O27125; -.
DR   SMR; O27125; -.
DR   STRING; 187420.MTH_1051; -.
DR   EnsemblBacteria; AAB85542; AAB85542; MTH_1051.
DR   GeneID; 1471459; -.
DR   KEGG; mth:MTH_1051; -.
DR   PATRIC; fig|187420.15.peg.1030; -.
DR   HOGENOM; CLU_000487_3_1_2; -.
DR   OMA; AVCPPYN; -.
DR   Proteomes; UP000005223; 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; 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; Reference proteome; Transcription;
KW   Transferase; Zinc.
FT   CHAIN           1..870
FT                   /note="DNA-directed RNA polymerase subunit Rpo1N"
FT                   /id="PRO_0000074004"
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   870 AA;  98078 MW;  05BB2C2C80CFD211 CRC64;
     MRGILKKISQ INFGLMSPED IRKMSVTQIV TPDTYDEDGY PIENGLMDPR LGVIDPSLRC
     RTCGAKGGEC PGHFGSINLA RPVIHVGFAD TIHKILRSTC RKCGRVLLTE TEIEEYRQRI
     LDAMEKEESL TPIIKEIYAE ARRDKCPHCE EEQEEIKLDK PVSIVEGDYK LTPSEVRERL
     ERISDDDALI LGVNPEVARP EWMVLTVLPV PPVTVRPSIT LETGERSEDD LTHKLVDILR
     INQRLKENME AGAPQLIVED LWELLQYHVT TYFDNEASGV PPARHRSGRP LKTLAQRLKG
     KEGRFRSNLS GKRVNFSART VISPDPNISI NEVGVPEIIA REVTVPVYVT EWNIDRMREY
     IENGPDVHPG ANYVIRPDGR KIRIYNETKE VVLENLKPGY IVERHLKDGD IVLFNRQPSL
     HRMSMMAHQV RVLPYKTFRL NLCVCPPYNA DFDGDEMNMH VFQTEESRAE AKTLMRVQEH
     ILSPRFGGPI IGGIHDHISG AYLLTRKSAV FSEEKVFQIL KKAGLPLPDS RGRDWTGKEI
     FSMVLPDDLN MVYRAEVCRK CEECLEMECE NDAYVVIENG QLISGVIDEK AYGAFAGKIL
     DHIVKEYGTD AAREFLDSAT KLAIAGIMHA GFTTSTNDEE IPEEARERIE AHLRNAEARV
     DQLIEAYENG ELEPLPGRSL EETLEMKIMQ VLGEARDKSG EIAESYFDMD ENHAVIMALT
     GARGSMLNLT QITACVGQQS VRGGRISRGY DNRTLPHFKK GELGAKSRGF VHSSYKEGLD
     PIEFFFHAMG GREGLVDTAI RTAQSGYMQR RLVNALQDLT VDENGRVVDN RGVIIQNRFG
     EDGVDPAKSD YGKIVDLDKL VEEIRLKSKG
 
 
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