ID   RPO1C_HALMO             Reviewed;         393 AA.
AC   P15353;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 76.
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   Halococcus morrhuae (Micrococcus morrhuae).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halococcaceae; Halococcus.
OX   NCBI_TaxID=2250;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 17082 / DSM 1307 / JCM 8876 / NBRC 14719 / NCIMB 787;
RX   PubMed=2495365; DOI=10.1016/0022-2836(89)90519-6;
RA   Leffers H., Gropp F., Lottspeich F., Zillig W., Garrett R.A.;
RT   "Sequence, organization, transcription and evolution of RNA polymerase
RT   subunit genes from the archaebacterial extreme halophiles Halobacterium
RT   halobium and Halococcus morrhuae.";
RL   J. Mol. Biol. 206:1-17(1989).
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}.
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}.
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; X57145; CAA40432.1; -; Genomic_DNA.
DR   PIR; S03576; S03576.
DR   AlphaFoldDB; P15353; -.
DR   SMR; P15353; -.
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   3: Inferred from homology;
KW   Cytoplasm; DNA-binding; DNA-directed RNA polymerase;
KW   Nucleotidyltransferase; Transcription; Transferase.
FT   CHAIN           1..393
FT                   /note="DNA-directed RNA polymerase subunit Rpo1C"
FT                   /id="PRO_0000074014"
SQ   SEQUENCE   393 AA;  42993 MW;  D0FCE267F725A10F CRC64;
     MTEITNAIER TVEGTDLPKR LKDEVYESIE GRDVTDEQAV SIAEAVESRY LDTRVEPLDP
     VGTVSAQSIG EPGTQMTMNT FHYAGVAEID VTQGLPRLIE LVDARKTPDT PMMTVYLDDQ
     HAENREKAHE VVWNIESTRI LALGDVSTNV ADMLVQVNLN EQTLDERMIS AETVAEIIED
     SLGVEVTQTG TTIEFGPAEP SYRRLLQLVE ELREIVFKGI EEVSRVVIRK EDVDDGEEFI
     LYTEGSAFGD VLDIEGVDAS RTTCNNIHEV YRNLGVEAAR ETIIDETMNT LEEQGLGDVN
     IRHLMLVADI MTAEGTIESI GRHGISGNKN SVLARAAFEV TVNHLLDAAV HGEVDDLDGV
     TENVIVGKPI KLGTGDVNLR MGGATTDGSG RAD