ID   RPOA_MARPO              Reviewed;         340 AA.
AC   P06270;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 132.
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   Marchantia polymorpha (Liverwort) (Marchantia aquatica).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=3197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3199436; DOI=10.1016/0022-2836(88)90003-4;
RA   Fukuzawa H., Kohchi T., Sano T., Shirai H., Umesono K., Inokuchi H.,
RA   Ozeki H., Ohyama K.;
RT   "Structure and organization of Marchantia polymorpha chloroplast genome.
RT   III. Gene organization of the large single copy region from rbcL to
RT   trnI(CAU).";
RL   J. Mol. Biol. 203:333-351(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   DOI=10.1038/322572a0;
RA   Ohyama K., Fukuzawa H., Kohchi T., Shirai H., Sano T., Sano S., Umesono K.,
RA   Shiki Y., Takeuchi M., Chang Z., Aota S., Inokuchi H., Ozeki H.;
RT   "Chloroplast gene organization deduced from complete sequence of liverwort
RT   Marchantia polymorpha chloroplast DNA.";
RL   Nature 322:572-574(1986).
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; X04465; CAA28117.1; -; Genomic_DNA.
DR   PIR; A00687; RNLVA.
DR   RefSeq; NP_039331.1; NC_001319.1.
DR   AlphaFoldDB; P06270; -.
DR   SMR; P06270; -.
DR   GeneID; 2702564; -.
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.
DR   TIGRFAMs; TIGR02027; rpoA; 1.
PE   3: Inferred from homology;
KW   Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW   Transcription; Transferase.
FT   CHAIN           1..340
FT                   /note="DNA-directed RNA polymerase subunit alpha"
FT                   /id="PRO_0000175469"
FT   REGION          1..233
FT                   /note="Alpha N-terminal domain (alpha-NTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT   REGION          265..340
FT                   /note="Alpha C-terminal domain (alpha-CTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
SQ   SEQUENCE   340 AA;  39241 MW;  D81D1F85C774B52A CRC64;
     MIQDEIKVST QTLQWKCIES KIESKRLLYS RFAISPFRKG QANTVGIAMR RALLNEIEGA
     SITYAKIKKV KHEYSTIIGL QESIHDILIN LKEIVLKSES FEPQKAYISV LGPKKITAQD
     IKGPSCIKIM IIAQYIATLN KDILLEIELN IEKDRGYRIE NLQKYQEGLF PVDAVFMPIR
     NANYSVHSFE SEKKIKEILF LEIWTDGSLT PKEALYEASR NLIDLFIPLI NSEKKEKNFG
     IEKTNESNMS YFPFQSVSLD IEKMTKDVAF KHIFIDQLEL PARAYNCLKK VNVHTIADLL
     HYSEDDLIKI KNFGKKSVEQ VLEALKKRFS IQLPKNKNYL