RPOA_SOLTU
ID RPOA_SOLTU Reviewed; 337 AA.
AC Q2VEE8; Q27S17;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 Solanum tuberosum (Potato).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Desiree;
RX PubMed=16835751; DOI=10.1007/s00299-006-0196-4;
RA Chung H.-J., Jung J.D., Park H.-W., Kim J.-H., Cha H.W., Min S.R.,
RA Jeong W.-J., Liu J.R.;
RT "The complete chloroplast genome sequences of Solanum tuberosum and
RT comparative analysis with Solanaceae species identified the presence of a
RT 241-bp deletion in cultivated potato chloroplast DNA sequence.";
RL Plant Cell Rep. 25:1369-1379(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Desiree;
RA Gargano D., Scotti N., Vezzi A., Bilardi A., Valle G., Grillo S., Cardi T.;
RT "Complete chloroplast genome sequences of Solanum tuberosum cultivar
RT Desiree and comparative analyses with other Solanaceae genomes.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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; DQ231562; ABB90071.1; -; Genomic_DNA.
DR EMBL; DQ386163; ABD47088.1; -; Genomic_DNA.
DR RefSeq; YP_635671.1; NC_008096.2.
DR AlphaFoldDB; Q2VEE8; -.
DR SMR; Q2VEE8; -.
DR STRING; 4113.PGSC0003DMT400036532; -.
DR EnsemblPlants; PGSC0003DMT400036532; PGSC0003DMT400036532; PGSC0003DMG400014075.
DR GeneID; 4099876; -.
DR Gramene; PGSC0003DMT400036532; PGSC0003DMT400036532; PGSC0003DMG400014075.
DR KEGG; sot:4099876; -.
DR eggNOG; ENOG502QRS7; Eukaryota.
DR HOGENOM; CLU_053084_2_0_1; -.
DR InParanoid; Q2VEE8; -.
DR OMA; LMKFRNF; -.
DR OrthoDB; 990306at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
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..337
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_0000225926"
FT REGION 1..233
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT REGION 265..337
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
SQ SEQUENCE 337 AA; 38637 MW; B0FE44DD90D13DF3 CRC64;
MVREKVTVST RTLQWKCVES RTDSKRLYYG RFILSPLMKG QADTIGIAMR RALLGEIEGT
CITRVKSEKV PHEYSTITGI QESVHEILMN LKEIVLRSNL YGTSDASICV KGPGYVTAQD
IILPPYVEIV DNTQHIASLT EPIDFCIGLQ IERNRGYLIK TPHNFQDGSY PIDAVFMPVR
NANHSIHSYG NGNEKQEILF IEIWTNGSLT PKEALHDASR NLIDLFIPFL HMEEDNLYLQ
DNQHTVPLSP FTFHDKLAKL IKNKKKIALK SIFIDQSELS SRIYNCLKMS NIYTLLDLLN
NSQEDLMKIE HFRSEDIKQI LGILEKYFVI DLAKNKF