ID   RPOA_CHLRE              Reviewed;         550 AA.
AC   Q8HUH2; B7U1H5;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
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   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION, AND COMPLETE
RP   PLASTID GENOME.
RX   PubMed=12417694; DOI=10.1105/tpc.006155;
RA   Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H.,
RA   Stern D.B.;
RT   "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a
RT   sea of repeats.";
RL   Plant Cell 14:2659-2679(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-503;
RX   PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA   Smith D.R., Lee R.W.;
RT   "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT   addressing the mutational-hazard hypothesis.";
RL   BMC Evol. Biol. 9:120-120(2009).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
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; AF541867; AAN17816.1; -; Genomic_DNA.
DR   EMBL; FJ423446; ACJ50122.1; -; Genomic_DNA.
DR   EMBL; BK000554; DAA00934.1; -; Genomic_DNA.
DR   RefSeq; NP_958389.1; NC_005353.1.
DR   AlphaFoldDB; Q8HUH2; -.
DR   STRING; 3055.DAA00934; -.
DR   PaxDb; Q8HUH2; -.
DR   PRIDE; Q8HUH2; -.
DR   GeneID; 2717004; -.
DR   KEGG; cre:ChreCp033; -.
DR   eggNOG; ENOG502QRS7; Eukaryota.
DR   HOGENOM; CLU_495556_0_0_1; -.
DR   OrthoDB; 990306at2759; -.
DR   Proteomes; UP000006906; Chloroplast.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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   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; IPR036643; RNApol_insert_sf.
DR   PANTHER; PTHR32108; PTHR32108; 1.
DR   Pfam; PF01000; RNA_pol_A_bac; 1.
DR   Pfam; PF01193; RNA_pol_L; 1.
DR   SMART; SM00662; RPOLD; 1.
DR   SUPFAM; SSF55257; SSF55257; 1.
DR   SUPFAM; SSF56553; SSF56553; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW   Reference proteome; Transcription; Transferase.
FT   CHAIN           1..550
FT                   /note="DNA-directed RNA polymerase subunit alpha"
FT                   /id="PRO_0000175446"
FT   REGION          1..333
FT                   /note="Alpha N-terminal domain (alpha-NTD)"
FT                   /evidence="ECO:0000250"
FT   REGION          185..258
FT                   /note="Insert"
FT   REGION          378..550
FT                   /note="Alpha C-terminal domain (alpha-CTD)"
FT                   /evidence="ECO:0000250"
FT   VARIANT         449
FT                   /note="S -> T (in strain: CC-503)"
FT   VARIANT         548..549
FT                   /note="RK -> KN (in strain: CC-503)"
SQ   SEQUENCE   550 AA;  62290 MW;  931F910FF6359948 CRC64;
     MTIYPNLKKI MTKTQSTDFF IACKESRIEN NTNFYGCFYL GPFDESLSQT LANDLRRTLL
     SELTGLAITS IEIEGVLHKF STLTGMKEPV LDLICNLQNI VLRKETISST NMNYRATKKT
     YIGFLSVNGP RVIKAADLKL PAGLQCVDPN QYIATLAEDG FLNMKFNINE GKNYIKQKPY
     NLDVTTLKKR NILLQNFKNK IGLTALKNKQ LMSTTMEGKP LLSNSDNLRF KKSFKRMLTS
     PNQSLKNKTS LGHDTVSNPI PLDAVFMPVT KINCIIEENN VYSDFSTDPS LEFSTHLVPS
     LTTQTNLRQE STHKFVNKAN SLLQENNLFR SEKVYLPNIY IPEGEGDALS LKGVSPYSDF
     KTFLSTLNYN SLYQTSLFLN QSLGQNKLLP WQANTLFFDV TNFADSQSND VNMNMDLAGD
     KTSVQKIHST GISNTDAQLN KLSLTKIKSF LGSSDKLQNK TYQSFLQPKY ASSNLRTLLT
     QRSLQKNQSV FMHSFLDDQA KHKELTSNTL RANKFQVMKT VVSIPPKTFK TNPINTFHNQ
     SLTFEYARKF