ID   RPOA_EUGGA              Reviewed;         216 AA.
AC   Q8SL92;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 79.
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   Euglena granulata.
OG   Plastid; Chloroplast.
OC   Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC   Euglenales; Euglenaceae; Euglena.
OX   NCBI_TaxID=69255;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=UTEX 453;
RX   PubMed=11861918; DOI=10.1093/nar/30.5.1247;
RA   Sheveleva E.V., Giordani N.V., Hallick R.B.;
RT   "Identification and comparative analysis of the chloroplast alpha-subunit
RT   gene of DNA-dependent RNA polymerase from seven Euglena species.";
RL   Nucleic Acids Res. 30:1247-1254(2002).
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   -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC       {ECO:0000305}.
CC   -!- CAUTION: The C-terminal domain thought to be required for interaction
CC       with some regulatory factors is missing from this protein.
CC       {ECO:0000305}.
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DR   EMBL; AY047484; AAL83362.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8SL92; -.
DR   SMR; Q8SL92; -.
DR   PRIDE; Q8SL92; -.
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: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   InterPro; IPR036603; RBP11-like.
DR   InterPro; IPR036643; RNApol_insert_sf.
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..216
FT                   /note="DNA-directed RNA polymerase subunit alpha"
FT                   /id="PRO_0000175506"
SQ   SEQUENCE   216 AA;  25232 MW;  2F192DEA88722A64 CRC64;
     MKLVHILFVK KKSNLNSFTT VFEISLNTKY KNLFLLGNIF RQFLLGSFEG LVINEKRFYV
     SHTNSLYKDF YLVNEFSLLE EVLEPFYDVW TVFDNLRFKE KFSLSKRYYA RLLTYGSGEI
     NSKDIIVPSN LSLLENKSLF TLITDSLCID VILQILSKNG SPFNGVERVN YILENSNSGN
     INYNKLYLDI STRYFLSPME ALFECFRKTN LALSKM