ID A0A6B9QFT1_PEGHA Unreviewed; 324 AA. AC A0A6B9QFT1; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 19-JAN-2022, entry version 8. DE RecName: Full=DNA-directed RNA polymerase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059}; DE Short=PEP {ECO:0000256|HAMAP-Rule:MF_00059}; DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_00059}; DE AltName: Full=Plastid-encoded RNA polymerase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059}; DE Short=RNA polymerase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059}; GN Name=rpoA {ECO:0000256|HAMAP-Rule:MF_00059, GN ECO:0000313|EMBL:QHE65527.1}; OS Peganum harmala (Syrian rue) (Harmal peganum). OG Plastid; Chloroplast {ECO:0000313|EMBL:QHE65527.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Sapindales; Nitrariaceae; Peganum. OX NCBI_TaxID=43879 {ECO:0000313|EMBL:QHE65527.1}; RN [1] {ECO:0000313|EMBL:QHE65527.1} RP NUCLEOTIDE SEQUENCE. RA Zhang G., Chi X.; RT "The complete chloroplast genome of Peganum harmala."; RL Mitochondrial DNA Part B Resour 4:1784-1785(2019). RN [2] {ECO:0000313|EMBL:QSX42973.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=33366688; RA Zha X., Zhao P., Gao F., Zhou Y.; RT "Complete chloroplast genome sequence of Peganum harmala, an important RT medicinal plant."; RL Mitochondrial DNA B Resour 5:652-653(2020). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of CC DNA into RNA using the four ribonucleoside triphosphates as substrates. CC {ECO:0000256|ARBA:ARBA00004026, ECO:0000256|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:0000256|ARBA:ARBA00024550, CC ECO:0000256|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:0000256|HAMAP-Rule:MF_00059}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP- CC Rule:MF_00059}. 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:0000256|HAMAP-Rule:MF_00059}. CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family. CC {ECO:0000256|ARBA:ARBA00007123, ECO:0000256|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; MK347420; QHE65527.1; -; Genomic_DNA. DR EMBL; MK341054; QSX42973.1; -; Genomic_DNA. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. 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 {ECO:0000313|EMBL:QHE65527.1}; KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478, KW ECO:0000256|HAMAP-Rule:MF_00059}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP- KW Rule:MF_00059}; Plastid {ECO:0000313|EMBL:QHE65527.1}; KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP- KW Rule:MF_00059}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00059}. FT DOMAIN 29..232 FT /note="RPOLD" FT /evidence="ECO:0000259|SMART:SM00662" FT REGION 1..237 FT /note="Alpha N-terminal domain (alpha-NTD)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00059" FT REGION 266..324 FT /note="Alpha C-terminal domain (alpha-CTD)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00059" SQ SEQUENCE 324 AA; 37080 MW; 6AF74919E219B977 CRC64; MVREKVKVST RTPQWKCVES RTDSKRLFYG RFILSPLMKG QADTIGIAMR RALLGEIEGT CITRAKSEKI PHEYSTIVGI QESVHEILMN LKEIVLRSNL YGTCDALICV KGPGYVTAQD ILLPPSVEIV DNTQHIASLT EPIDLCIGLQ IERNRGYNIK TPNHFQDGSY PIDAVFMPVR NANHSIHSYG NGNDKQEILF LEIWTNGSLT PKEALHEASR NLIDLFIPFL QATDEIENNQ YKVTLPFFTF HDRLAKLKKK KKEIALKSIF IDQSELSPRI YNCLRKSNIH TLFDLLNNSQ EDLMKIEHFR IEDVKQILGI LEKK //