ID   RPOA_OLTVI              Reviewed;         508 AA.
AC   Q20F02;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=DNA-directed RNA polymerase subunit alpha;
DE            Short=PEP;
DE            EC=2.7.7.6;
DE   AltName: Full=Plastid-encoded RNA polymerase subunit alpha;
DE            Short=RNA polymerase subunit alpha;
GN   Name=rpoA;
OS   Oltmannsiellopsis viridis (Marine flagellate) (Oltmannsiella viridis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; Oltmannsiellopsidales;
OC   Oltmannsiellopsidaceae; Oltmannsiellopsis.
OX   NCBI_TaxID=51324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16472375; DOI=10.1186/1741-7007-4-3;
RA   Pombert J.-F., Lemieux C., Turmel M.;
RT   "The complete chloroplast DNA sequence of the green alga Oltmannsiellopsis
RT   viridis reveals a distinctive quadripartite architecture in the chloroplast
RT   genome of early diverging ulvophytes.";
RL   BMC Biol. 4:3-3(2006).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000250}.
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;
CC   -!- SUBUNIT: In plastids the minimal PEP RNA polymerase catalytic core is
CC       composed of four subunits: alpha, beta, beta', and beta''. When a
CC       (nuclear-encoded) sigma factor is associated with the core the
CC       holoenzyme is formed, which can initiate transcription (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- DOMAIN: The N-terminal domain is essential for RNAP assembly and basal
CC       transcription, whereas the C-terminal domain is involved in interaction
CC       with transcriptional regulators and with upstream promoter elements.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC       {ECO:0000305}.
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DR   EMBL; DQ291132; ABB82004.1; -; Genomic_DNA.
DR   RefSeq; YP_635843.1; NC_008099.1.
DR   AlphaFoldDB; Q20F02; -.
DR   SMR; Q20F02; -.
DR   GeneID; 4100180; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 2.170.120.12; -; 1.
DR   Gene3D; 3.30.1360.10; -; 1.
DR   InterPro; IPR011262; DNA-dir_RNA_pol_insert.
DR   InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
DR   InterPro; IPR011773; DNA-dir_RpoA.
DR   InterPro; IPR036603; RBP11-like.
DR   InterPro; IPR011260; RNAP_asu_C.
DR   InterPro; IPR036643; RNApol_insert_sf.
DR   PANTHER; PTHR32108; PTHR32108; 1.
DR   Pfam; PF01000; RNA_pol_A_bac; 1.
DR   Pfam; PF03118; RNA_pol_A_CTD; 1.
DR   Pfam; PF01193; RNA_pol_L; 1.
DR   SMART; SM00662; RPOLD; 1.
DR   SUPFAM; SSF55257; SSF55257; 1.
DR   SUPFAM; SSF56553; SSF56553; 1.
PE   3: Inferred from homology;
KW   Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW   Transcription; Transferase.
FT   CHAIN           1..508
FT                   /note="DNA-directed RNA polymerase subunit alpha"
FT                   /id="PRO_0000296900"
FT   REGION          1..380
FT                   /note="Alpha N-terminal domain (alpha-NTD)"
FT                   /evidence="ECO:0000250"
FT   REGION          434..508
FT                   /note="Alpha C-terminal domain (alpha-CTD)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   508 AA;  56731 MW;  88C077690B79E188 CRC64;
     MKHILLSCVE SRIEHNRSFY SRFQLGPFDL GQGLTVGNAF RRTLLSELSG VGITLIEIDG
     VCHEYSTLPG VRESVLDILL NLKQLVLTSD TTFTVPQVGY LNFTGPGVVT AKDLKLPVSV
     YCVDPDQPIA TLSADATLNF KFLVCQGKNY IIQTPVDKFH EYQKKILNSK LNLPLSSRTT
     LNSTFERPNQ DSLVGTPLQE GVGKTKQNKR LNAHFQRQLK QLNRLKETSF KAYKTKVGEK
     TISDEFQTNS VNHQNLTTFD LREKKLTDVT TSLQHGEEAT LLKEEGLNKL DNSSPQLENK
     LKGGRDFSGG SQLASQALPV DTLFMPIKKV NYMIDIDPAE PDRESVVLEI WTNGSIHPRQ
     AVHEAAKQLI HLFSPFLQTH LVPTTLQSTP YSKAASKTQE FSLNETSTEK VKDELGKVAF
     GSENNTAALN QQKNLVTAIQ TLDIANLNFS LRTFTFLKKE NINTVSELVE FWTRQKTEAK
     DSIQSNVQSS VLLEISNNLK NFGVLPTS