RPAL2_PELHO
ID RPAL2_PELHO Reviewed; 322 AA.
AC Q06FN4;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Putative DNA-directed RNA polymerase subunit alpha-like 2;
DE Short=Putative PEP 2;
DE EC=2.7.7.6;
DE AltName: Full=Putative plastid-encoded RNA polymerase subunit alpha 2;
DE Short=Putative RNA polymerase subunit alpha 2;
GN Name=rpoAL2-A; Synonyms=ORF332;
GN and
GN Name=rpoAL2-B; Synonyms=ORF332;
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. {ECO:0000305}.
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DR EMBL; DQ897681; ABI17301.1; -; Genomic_DNA.
DR EMBL; DQ897681; ABI17339.1; -; Genomic_DNA.
DR RefSeq; YP_784109.1; NC_008454.1.
DR RefSeq; YP_784147.1; NC_008454.1.
DR AlphaFoldDB; Q06FN4; -.
DR SMR; Q06FN4; -.
DR GeneID; 4362844; -.
DR GeneID; 4362953; -.
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; -; 1.
DR InterPro; IPR011773; DNA-dir_RpoA.
DR InterPro; IPR036603; RBP11-like.
DR InterPro; IPR036643; RNApol_insert_sf.
DR PANTHER; PTHR32108; PTHR32108; 1.
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..322
FT /note="Putative DNA-directed RNA polymerase subunit alpha-
FT like 2"
FT /id="PRO_0000296902"
FT REGION 1..232
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000250"
FT REGION 280..322
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 322 AA; 36122 MW; C0DB7394BBA2A4D9 CRC64;
MSNPNNGAEW QQVEADQLDS GLYYGRFALS PLTAKQASLL KKGLPEALLT EILCLRFTHA
KIQNECVNLM NIVGIQESLD EILKNFGKII LTGKLEEFVG KGPFVAILDV RGPLNAMAVD
IELPPGIKVE IETQHIATIT EPIPFVVELK IELVSSTSKG ETGITDEEGF SIDPNPPIQK
VDTSIQCYDY QGEPFQTLFL DIWTDRTIHP HEALAQASRK IFGLLSLVFQ AEYFQYNELE
NGLRYGKFCL YPMTKEQFQW IQTALNEALA LDMSGESKHE GPVTDEEGDS IDPTFTPVQK
WDITMNSYQY SGETFQGLLS RF