RPOA_ANTAG
ID RPOA_ANTAG Reviewed; 340 AA.
AC Q85A01;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 Anthoceros angustus (Hornwort) (Anthoceros formosae).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Anthocerotophyta;
OC Anthocerotopsida; Anthocerotidae; Anthocerotales; Anthocerotaceae;
OC Anthoceros.
OX NCBI_TaxID=48387;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX PubMed=12527781; DOI=10.1093/nar/gkg155;
RA Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.;
RT "The complete nucleotide sequence of the hornwort (Anthoceros formosae)
RT chloroplast genome: insight into the earliest land plants.";
RL Nucleic Acids Res. 31:716-721(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RC TISSUE=Thallus;
RX PubMed=12711687; DOI=10.1093/nar/gkg327;
RA Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.;
RT "RNA editing in hornwort chloroplasts makes more than half the genes
RT functional.";
RL Nucleic Acids Res. 31:2417-2423(2003).
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 -!- RNA EDITING: Modified_positions=31 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 35 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 51 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 53 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 88 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 96 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 104 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 170 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 176 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 196 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 209 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 211 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 225 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 226 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 297 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 298 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}; Note=The nonsense codons at positions 51,
CC 104 and 196, are modified to sense codons.;
CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
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; AB086179; BAC55381.1; -; Genomic_DNA.
DR EMBL; AB087466; BAC55478.1; -; mRNA.
DR RefSeq; NP_777445.1; NC_004543.1.
DR AlphaFoldDB; Q85A01; -.
DR SMR; Q85A01; -.
DR GeneID; 2553422; -.
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:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 2.170.120.12; -; 1.
DR Gene3D; 3.30.1360.10; -; 1.
DR HAMAP; MF_00059; RNApol_bact_RpoA; 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.
DR TIGRFAMs; TIGR02027; rpoA; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW RNA editing; Transcription; Transferase.
FT CHAIN 1..340
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_0000175439"
FT REGION 1..233
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000250"
FT REGION 263..340
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 340 AA; 38894 MW; EDE2B1DF048EF4A9 CRC64;
MIQNEIPIPA EALQWKCIES KIDSERLHYG RFAISPLRPG QANTVGIAIR RALLGEIEGT
CITYVKFEKV THEYSTIMGI QESVHDILIN LKEIVLKSNS YKTQEASISI LGPKRVTAED
IVLPSSVEVI DATQHIATIT KAVYFNIKLG IRKDRGYRIE NPVKYEDGNF AVNAAFTPIR
NANYSVHSFE NEKEKQEILF IEVWTNGSLT PKEALREASQ SLINLFIPLL HEKKERENRK
LENKDEYNVL RSCFSLTNIG EVRKEISFKH IFIDQLELPA RAYNGLKKVD VHTISDLLNY
SQEDLMKIKN FGKKSIQQVV EALQKHFAIH LPKNKFSIND
