RPOA_WHEAT
ID RPOA_WHEAT Reviewed; 339 AA.
AC P12073;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=DNA-directed RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
DE Short=PEP {ECO:0000255|HAMAP-Rule:MF_00059};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00059};
DE AltName: Full=Plastid-encoded RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
DE Short=RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
GN Name=rpoA {ECO:0000255|HAMAP-Rule:MF_00059};
OS Triticum aestivum (Wheat).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Mardler;
RX PubMed=2671938; DOI=10.1093/nar/17.15.6394;
RA Hird S.M., Dyer T.A., Gray J.C.;
RT "Nucleotide sequence of the rpoA gene in wheat chloroplast DNA.";
RL Nucleic Acids Res. 17:6394-6394(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring;
RA Ogihara Y., Isono K., Kojima T., Endo A., Hanaoka M., Shiina T.,
RA Terachi T., Utsugi S., Murata M., Mori N., Takumi S., Ikeo K., Gojobori T.,
RA Murai R., Murai K., Matsuoka Y., Ohnishi Y., Tajiri H., Tsunewaki K.;
RT "Chinese spring wheat (Triticum aestivum L.) chloroplast genome: complete
RT sequence and contig clones.";
RL Plant Mol. Biol. Rep. 18:243-253(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 322-339.
RC STRAIN=cv. Mardler;
RX PubMed=1868207; DOI=10.1007/bf00023441;
RA Hird S.M., Wilson R.J., Dyer T.A., Gray J.C.;
RT "Nucleotide sequence of the wheat chloroplast petB and petD genes encoding
RT apocytochrome b-563 and subunit IV of the cytochrome bf complex.";
RL Plant Mol. Biol. 16:745-747(1991).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_00059}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_00059};
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.
CC {ECO:0000255|HAMAP-Rule:MF_00059}.
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:0000255|HAMAP-Rule:MF_00059}.
CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00059}.
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DR EMBL; X15595; CAA33618.1; -; Genomic_DNA.
DR EMBL; AB042240; BAB47065.1; -; Genomic_DNA.
DR EMBL; X54751; CAA38553.1; -; Genomic_DNA.
DR PIR; S05314; RNWTA.
DR RefSeq; NP_114289.1; NC_002762.1.
DR AlphaFoldDB; P12073; -.
DR SMR; P12073; -.
DR STRING; 4565.EPlTAEP00000010059; -.
DR PRIDE; P12073; -.
DR GeneID; 803149; -.
DR KEGG; taes:803149; -.
DR eggNOG; ENOG502QRS7; Eukaryota.
DR HOGENOM; CLU_053084_2_0_1; -.
DR Proteomes; UP000019116; Chloroplast.
DR Genevisible; P12073; TA.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 3: Inferred from homology;
KW Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW Reference proteome; Transcription; Transferase.
FT CHAIN 1..339
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_0000175503"
FT REGION 10..233
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT REGION 264..339
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT CONFLICT 5
FT /note="E -> V (in Ref. 1; CAA33618)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="H -> L (in Ref. 1; CAA33618)"
FT /evidence="ECO:0000305"
FT CONFLICT 203..205
FT /note="IWT -> YGS (in Ref. 1; CAA33618)"
FT /evidence="ECO:0000305"
FT CONFLICT 338..339
FT /note="SF -> CI (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 38869 MW; 044063ED91F3F6D1 CRC64;
MVREEVAGST QTLQWKCVES RVDSKRLYYG RFILSPLRKG QADTVGIALR RALLGEIEGT
CITRAKFGSV PHEYSTIAGI EESVQEILLN LKEIVLRSNL YGVRDASICV KGPRYITAQD
IILPPSVEIV DTAQPIANLT EPIDFCIDLQ IKRDRGYQTE LRKNYQDGSY PIDAVSMPVR
NVNYSIFSCG NGNEKHEILF LEIWTNGSLT PKEALYEASR NLIDLFLPFL HAEEEGASFE
ENKNRFTPPL FTFQKRLTNL KKNKKGIPLN CIFIDQLELT SRTYNCLKRA NIHTLLDLLS
KTEEDLLRID SFRMEDRKHI WDTLEKHLPI DLLKNKLSF
