ID   RPO1C_METTW             Reviewed;         449 AA.
AC   P09847;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=DNA-directed RNA polymerase subunit Rpo1C {ECO:0000255|HAMAP-Rule:MF_00411};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00411};
DE   AltName: Full=DNA-directed RNA polymerase subunit A'' {ECO:0000255|HAMAP-Rule:MF_00411};
GN   Name=rpo1C {ECO:0000255|HAMAP-Rule:MF_00411};
GN   Synonyms=rpoA2 {ECO:0000255|HAMAP-Rule:MF_00411};
OS   Methanothermobacter thermautotrophicus (strain Winter) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=79930;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT.
RX   PubMed=2843811; DOI=10.1093/nar/16.16.8113;
RA   Berghoefer B., Kroeckel L., Koertner C., Truss M., Schallenberg J.,
RA   Klein A.;
RT   "Relatedness of archaebacterial RNA polymerase core subunits to their
RT   eubacterial and eukaryotic equivalents.";
RL   Nucleic Acids Res. 16:8113-8128(1988).
CC   -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC       transcription of DNA into RNA using the four ribonucleoside
CC       triphosphates as substrates. Forms part of the jaw domain.
CC       {ECO:0000255|HAMAP-Rule:MF_00411}.
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_00411};
CC   -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000255|HAMAP-
CC       Rule:MF_00411, ECO:0000269|PubMed:2843811}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00411}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00411}.
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DR   EMBL; X08038; CAA30839.1; -; Genomic_DNA.
DR   PIR; S02197; S02197.
DR   AlphaFoldDB; P09847; -.
DR   SMR; P09847; -.
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:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   CDD; cd06528; RNAP_A; 1.
DR   HAMAP; MF_00411; RNApol_arch_Rpo1C; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR012757; RPO1C.
DR   PANTHER; PTHR19376; PTHR19376; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR   TIGRFAMs; TIGR02389; RNA_pol_rpoA2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; DNA-binding; DNA-directed RNA polymerase;
KW   Nucleotidyltransferase; Transcription; Transferase.
FT   CHAIN           1..449
FT                   /note="DNA-directed RNA polymerase subunit Rpo1C"
FT                   /id="PRO_0000074018"
FT   REGION          1..68
FT                   /note="Unknown"
FT   REGION          69..449
FT                   /note="DNA-directed RNA polymerase subunit Rpo1C"
SQ   SEQUENCE   449 AA;  50796 MW;  6856FAA82E1A390C CRC64;
     MQDVIKKIED YSSRNGIMLP NPVTEYVAGI AEEEKLKDPE LHDLVRLFSR ICERNRGLEG
     EELLKAVEDE YLRILKVREL VKRKRAKFPP RLIEEIAEAI KRHGLSDDEL DELVRGVRRA
     YERAMVEAGE AVGTVAAQSV GEPGTQMTMR TFHYAGVAEL NVTLGLPRLI EIVDARKKIS
     TPTMSIYFEG DRKYDEEFVR KKANKICKST LNDVLKNFSI QYADMSVEAE LDEEKIREKH
     LEYDDIIAKV EKTFKKVEID NNILRFEPPK PTIRELRLLA DKVRKLQISG VKNIGKVVIR
     KEDDEWVIHT EGSNLGDRFK EEGVDKVRTT TNDIHEIETV LGIEAARNAI IHEAKRTMEE
     QGLTVDIRHI MLVADMMTAD GSVKSIGRHG ISGEKASVLA RASFEETGKH LLRASIRGEV
     DHLTGIIENI IIGQPIPLGT GSVSVIMKK