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   16-JUN-2009, entry version 14.
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).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; 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
CC       of DNA into RNA using the four ribonucleoside triphosphates as
CC       substrates.
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1).
CC   -!- SUBUNIT: In plastids the minimal PEP RNA polymerase catalytic core
CC       is composed of four subunits: alpha, beta, beta', and beta''. When
CC       a (nuclear-encoded) sigma factor is associated with the core the
CC       holoenzyme is formed, which can initiate transcription (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- DOMAIN: The N-terminal domain is essential for RNAP assembly and
CC       basal transcription, whereas the C-terminal domain is involved in
CC       interaction with transcriptional regulators and with upstream
CC       promoter elements (By similarity).
CC   -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC   -!- CAUTION: Could be the product of a pseudogene. There are 3 rpoA-
CC       like genes in this organism (found in the inverted repeat). None
CC       of them are convincing as rpoA, and it may be that the functional
CC       gene is in the nucleus. This gene however is found in the correct
CC       operon context.
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DR   EMBL; DQ897681; ABI17299.1; -; Genomic_DNA.
DR   EMBL; DQ897681; ABI17341.1; -; Genomic_DNA.
DR   RefSeq; YP_784107.1; -.
DR   RefSeq; YP_784149.1; -.
DR   GeneID; 4362839; -.
DR   GeneID; 4362958; -.
DR   BRENDA; 2.7.7.6; 280179.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:HAMAP.
DR   GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:HAMAP.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-dependent; IEA:HAMAP.
DR   HAMAP; MF_00059; atypical; 1.
DR   InterPro; IPR011262; DNA-dir_RNA_pol_insert.
DR   Gene3D; G3DSA:2.170.120.12; RNAP_insert; 1.
PE   5: Uncertain;
KW   Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW   Plastid; Transcription; Transferase.
FT   CHAIN         1    574       Putative DNA-directed RNA polymerase
FT                                subunit alpha-like 1.
FT                                /FTId=PRO_0000296901.
FT   REGION        1    352       Alpha N-terminal domain (alpha-NTD) (By
FT                                similarity).
FT   REGION      419    574       Alpha C-terminal domain (alpha-CTD) (By
FT                                similarity).
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
//