ID   RPOA_TUPAK              Reviewed;         577 AA.
AC   Q3ZJ77;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=DNA-directed RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
DE            Short=PEP {ECO:0000255|HAMAP-Rule:MF_00059};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00059};
DE   AltName: Full=Plastid-encoded RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
DE            Short=RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
GN   Name=rpoA {ECO:0000255|HAMAP-Rule:MF_00059};
OS   Tupiella akineta (Green alga) (Pseudendoclonium akinetum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; OUU clade;
OC   Ulotrichales; Tupiellaceae; Tupiella.
OX   NCBI_TaxID=160070;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX 1912;
RX   PubMed=15930151; DOI=10.1093/molbev/msi182;
RA   Pombert J.-F., Otis C., Lemieux C., Turmel M.;
RT   "The chloroplast genome sequence of the green alga Pseudendoclonium
RT   akinetum (Ulvophyceae) reveals unusual structural features and new insights
RT   into the branching order of chlorophyte lineages.";
RL   Mol. Biol. Evol. 22:1903-1918(2005).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000255|HAMAP-Rule:MF_00059}.
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_00059};
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.
CC       {ECO:0000255|HAMAP-Rule:MF_00059}.
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:0000255|HAMAP-Rule:MF_00059}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00059}.
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DR   EMBL; AY835431; AAV80614.1; -; Genomic_DNA.
DR   RefSeq; YP_636190.1; NC_008114.1.
DR   AlphaFoldDB; Q3ZJ77; -.
DR   SMR; Q3ZJ77; -.
DR   PRIDE; Q3ZJ77; -.
DR   GeneID; 4108814; -.
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:UniProtKB-UniRule.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.170.120.12; -; 1.
DR   Gene3D; 3.30.1360.10; -; 1.
DR   HAMAP; MF_00059; RNApol_bact_RpoA; 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..577
FT                   /note="DNA-directed RNA polymerase subunit alpha"
FT                   /id="PRO_0000296907"
FT   REGION          1..461
FT                   /note="Alpha N-terminal domain (alpha-NTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT   REGION          510..577
FT                   /note="Alpha C-terminal domain (alpha-CTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
SQ   SEQUENCE   577 AA;  66582 MW;  8DFC3118D5B52972 CRC64;
     MIKIIIKETF SFKSVLMHFL KEKVSNNKIS KKNKIMPSYT LLSCIDSRVE NLTKFYGRFE
     LGPFAPGQAL TVANALRRSL LSQLPGTSIT LVEVRGASNE YEIITGVRES ILDILLNLKQ
     IVLTSDFEIF SPQIGFLSVE GPGVIRANDL KLPSFIYAVD PNQYIATLSN SGRLNMKFLI
     CCGKNYITYN PNDSQYFEWL SLLKKSKPLI KSNSPKLNKG NINSEIDSDI SIDKKNDEVI
     FFQNANTRVV DSQTALKKGL VLKNTLRINK SSFLINSNYQ SFFPKTQQKA FSIFRKNSKT
     FLSTMGFYKE WKKEREFLKK DLYKNQEDFN KSYDFQETKK KLQTKLIKNF ETPKKKLFKV
     QNSANPFNKA FIPLTEEKVD YDSDFNLDHK STKIGYFPID AIFMPINRVN YLIESTEDIK
     LKIKDRVILE VWTNGSIHPR HAIHKAAKAL IQLFLPLQQI RTNLFLISDN SHFEEGQDKI
     KKRIDNFKKE ALLKANPQIQ ANPQLKKRNF DHRLLELDIA NLELTARPYS CLKLANINTI
     EDLISYSQED LLSIKNFGRR SLIEVQKALQ LMKLTLK