RPO1C_HALMA
ID RPO1C_HALMA Reviewed; 395 AA.
AC Q5UZR5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
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};
GN OrderedLocusNames=rrnAC2427;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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}.
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DR EMBL; AY596297; AAV47238.1; -; Genomic_DNA.
DR RefSeq; WP_005537132.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5UZR5; -.
DR SMR; Q5UZR5; -.
DR STRING; 272569.rrnAC2427; -.
DR EnsemblBacteria; AAV47238; AAV47238; rrnAC2427.
DR GeneID; 40153326; -.
DR KEGG; hma:rrnAC2427; -.
DR PATRIC; fig|272569.17.peg.3041; -.
DR eggNOG; arCOG04256; Archaea.
DR HOGENOM; CLU_037097_1_0_2; -.
DR OMA; TPMMTVY; -.
DR Proteomes; UP000001169; Chromosome I.
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; Reference proteome; Transcription; Transferase.
FT CHAIN 1..395
FT /note="DNA-directed RNA polymerase subunit Rpo1C"
FT /id="PRO_1000080473"
SQ SEQUENCE 395 AA; 43671 MW; ECF4966E834AAD6F CRC64;
MTAHDVSADI EAVVEDTELP RRLKDEVYST IEERGVGVDD ADRIAKAVET RYLDTRVDPL
DPVGTVSAQS IGEPGTQMTM NTFHYAGVAE IDVTQGLPRL IELVDARKTP DTPMMTVHLD
EEYATDRERA HEVVWKIEAT RILALGDIST NVADMLVEID LNEDTLLERW PTVNDTDAIA
EEIAETIESN LGVSTRQAGT LIEFGPEEPS YRDLLQLVEE LREIVFKGIE EITRVVIRKE
ETDNGEEFVL YTEGSDFGEV LDIEGVDASR TTCNNIHEIY RELGVEAARE TLINETMNTL
EEQGLDDVNV RHLMLVADIM TNEGTIESIG RHGISGSKDS VLARAAFEVT VNHLLDAAIH
GEVDELDGVT ENVIVGKPIK LGTGDVNLRM GTTQD