ID   RPAL1_PELHO             Reviewed;         574 AA.
AC   Q06FN2;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Putative DNA-directed RNA polymerase subunit alpha-like 1;
DE            Short=Putative PEP 1;
DE            EC=2.7.7.6;
DE   AltName: Full=Putative plastid-encoded RNA polymerase subunit alpha 1;
DE            Short=Putative RNA polymerase subunit alpha 1;
GN   Name=rpoAL1-A; Synonyms=ORF574;
GN   and
GN   Name=rpoAL1-B; Synonyms=ORF574;
OS   Pelargonium hortorum (Common geranium) (Pelargonium inquinans x Pelargonium
OS   zonale).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Geraniales; Geraniaceae; Pelargonium.
OX   NCBI_TaxID=4031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Ringo White;
RX   PubMed=16916942; DOI=10.1093/molbev/msl089;
RA   Chumley T.W., Palmer J.D., Mower J.P., Fourcade H.M., Calie P.J.,
RA   Boore J.L., Jansen R.K.;
RT   "The complete chloroplast genome sequence of Pelargonium x hortorum:
RT   organization and evolution of the largest and most highly rearranged
RT   chloroplast genome of land plants.";
RL   Mol. Biol. Evol. 23:2175-2190(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}.
CC   -!- CAUTION: Could be the product of a pseudogene. There are 3 rpoA-like
CC       genes in this organism (found in the inverted repeat). None of them are
CC       convincing as rpoA, and it may be that the functional gene is in the
CC       nucleus. This gene however is found in the correct operon context.
CC       {ECO:0000305}.
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DR   EMBL; DQ897681; ABI17299.1; -; Genomic_DNA.
DR   EMBL; DQ897681; ABI17341.1; -; Genomic_DNA.
DR   RefSeq; YP_784107.1; NC_008454.1.
DR   RefSeq; YP_784149.1; NC_008454.1.
DR   AlphaFoldDB; Q06FN2; -.
DR   SMR; Q06FN2; -.
DR   GeneID; 4362839; -.
DR   GeneID; 4362958; -.
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; -; 2.
DR   InterPro; IPR011773; DNA-dir_RpoA.
DR   InterPro; IPR036603; RBP11-like.
DR   InterPro; IPR036643; RNApol_insert_sf.
DR   PANTHER; PTHR32108; PTHR32108; 2.
DR   SUPFAM; SSF55257; SSF55257; 1.
DR   SUPFAM; SSF56553; SSF56553; 1.
PE   5: Uncertain;
KW   Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW   Transcription; Transferase.
FT   CHAIN           1..574
FT                   /note="Putative DNA-directed RNA polymerase subunit alpha-
FT                   like 1"
FT                   /id="PRO_0000296901"
FT   REGION          1..352
FT                   /note="Alpha N-terminal domain (alpha-NTD)"
FT                   /evidence="ECO:0000250"
FT   REGION          419..574
FT                   /note="Alpha C-terminal domain (alpha-CTD)"
FT                   /evidence="ECO:0000250"
FT   REGION          534..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   574 AA;  66533 MW;  A95901B4F66096ED CRC64;
     MTNNKNFADW DSLECKDLHN DLLYGRFALS PLTAKESRLL KKGLREALLT GILCLRFTHA
     KIQNACKNLN LMNIVGIQES LDEILKNFGK IILTGKLEEF VGKGPFVAIL DVRGPLNAMA
     VDIELPPGIK VEIETQHIAT ITEPIPFVVE LRIELVSSTS KGETGITDEE GFSIDPNPPI
     QKVNSSIQGY EYGGQTFQTL FIEILSTSPT VPNKALLLVS MKIMNLFQIV LQAKYLDYKE
     LEKGIHVGVF CVSALRAEQS KWIKTILEDA LYMVGGRKHQ GPLTDEEDDS IDSNFTPVQN
     LDCRIESYEE EGQTFQRLFL EIWTKSPTEP QEALWEASAK ILELFSLFLQ TSKENEKDLK
     QIIKDWTENK RKHQEVLRLL DSEESGSIGW ITKMKLAYMH MTLLSMNAMY ILLVHRLKPD
     YDRYNSITDQ IVQELRASLN KLREIQKGEY SEQRILVHSI AQEIEAALQK YETTYKLDDF
     VIKAKKDMIT MIWDKERADL ESSLIRWESD EDYLNLKKMN PVEMDRSFAE LQYQETLRKE
     QDEQSSQQQK DQMEKRRWER QNRERERKRG NREF