RPOA_EUGAN
ID RPOA_EUGAN Reviewed; 207 AA.
AC Q8SL94;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=DNA-directed RNA polymerase subunit alpha;
DE Short=PEP;
DE EC=2.7.7.6;
DE AltName: Full=Plastid-encoded RNA polymerase subunit alpha;
DE Short=RNA polymerase subunit alpha;
GN Name=rpoA;
OS Euglena anabaena (Euglenaria anabaena).
OG Plastid; Chloroplast.
OC Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC Euglenales; Euglenaceae; Euglenaria.
OX NCBI_TaxID=38273;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=UTEX 373;
RX PubMed=11861918; DOI=10.1093/nar/30.5.1247;
RA Sheveleva E.V., Giordani N.V., Hallick R.B.;
RT "Identification and comparative analysis of the chloroplast alpha-subunit
RT gene of DNA-dependent RNA polymerase from seven Euglena species.";
RL Nucleic Acids Res. 30:1247-1254(2002).
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 -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC {ECO:0000305}.
CC -!- CAUTION: The C-terminal domain thought to be required for interaction
CC with some regulatory factors is missing from this protein.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY047483; AAL83360.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8SL94; -.
DR SMR; Q8SL94; -.
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: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; IPR036603; RBP11-like.
DR InterPro; IPR036643; RNApol_insert_sf.
DR SUPFAM; SSF56553; SSF56553; 1.
PE 3: Inferred from homology;
KW Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW Transcription; Transferase.
FT CHAIN 1..207
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_0000175505"
SQ SEQUENCE 207 AA; 24508 MW; E89F8AAFFCDADA22 CRC64;
MKLLKISILR QSTFKNKKYN LFKIKTNRDF NPLVIGTKIR RNLIKETKGT KITQASLFVL
NKKSKEKLYH SLNEFTNIEE ISEKTNEIIK NLERLKIKLV NKNLKKKIIC ITLTKENSFF
KEIYKTIKIS NLNQKICTIK SHNVEIKLLL KIEKEKGIKF NPIETINFII PKKNNENNSS
LFLETIRNDQ TFTELYQSLK LIYNQQI