RPOA_BIGNA
ID RPOA_BIGNA Reviewed; 358 AA.
AC Q06J39;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=DNA-directed RNA polymerase subunit alpha;
DE Short=RNAP subunit alpha;
DE EC=2.7.7.6;
DE AltName: Full=RNA polymerase subunit alpha;
DE AltName: Full=Transcriptase subunit alpha;
GN Name=rpoA;
OS Bigelowiella natans (Pedinomonas minutissima) (Chlorarachnion sp. (strain
OS CCMP621)).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Rhizaria; Cercozoa; Chlorarachniophyceae; Bigelowiella.
OX NCBI_TaxID=227086;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16990439; DOI=10.1093/molbev/msl129;
RA Rogers M.B., Gilson P.R., Su V., McFadden G.I., Keeling P.J.;
RT "The complete chloroplast genome of the chlorarachniophyte Bigelowiella
RT natans: evidence for independent origins of chlorarachniophyte and euglenid
RT secondary endosymbionts.";
RL Mol. Biol. Evol. 24:54-62(2007).
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: Homodimer. The RNAP catalytic core consists of 2 alpha, 1
CC beta, 1 beta' and 1 omega subunit. When a sigma factor is associated
CC with the core the holoenzyme is formed, which can initiate
CC transcription (By similarity). {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}.
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DR EMBL; DQ851108; ABG91420.1; -; Genomic_DNA.
DR RefSeq; YP_778588.1; NC_008408.1.
DR AlphaFoldDB; Q06J39; -.
DR SMR; Q06J39; -.
DR GeneID; 4353005; -.
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; 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.
PE 3: Inferred from homology;
KW Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW Transcription; Transferase.
FT CHAIN 1..358
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_0000296912"
FT REGION 1..244
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000250"
FT REGION 287..358
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 358 AA; 41666 MW; 78BF74ACD1F40082 CRC64;
MENKLFSCIE SRLRGKRNYY SRFYIGPFLK NQAFLYSNVL RRVLLSDSSN IVITAVNIVG
AKHEYSLLPG VRESSLDLLL NLKELVFVKD IYTKFNKSYF AYLKSNGPKI IRCSDIILPN
TIYAVDSTQY IATISNNKSL ILKMKLTANL LNNFYSNLNY ELNSLLSYYT NDILEKTNFS
LIIDPNFSCV NKVNSSLISL DNLENYNDSI SLEVWTNSSY SPRIIIQNSI KSMVNLFLSI
YDTSFIDIKL ENSDNFLENH LVSLSNRATF FKKSFFNICT EFNTVKYKTS FDKNLTLISI
DELDLSIYSK FLLKRHNILT LYDLFKIDKR VLERFYNISY KTLQSIERKM VKYGTVNK