ID A0A5Q2MTN0_9MAGN Unreviewed; 339 AA. AC A0A5Q2MTN0; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 12-AUG-2020, entry version 4. 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:QGG45043.1}; GN ORFNames=LiruCp053 {ECO:0000313|EMBL:QGG45043.1}; OS Lindera rubronervia. OG Plastid; Chloroplast {ECO:0000313|EMBL:QGG45043.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Lindera. OX NCBI_TaxID=2654226 {ECO:0000313|EMBL:QGG45043.1}; RN [1] {ECO:0000313|EMBL:QGG45043.1} RP NUCLEOTIDE SEQUENCE. RA Jo S., Kim Y.-K., Cheon S.-H., Fan Q., Kim K.-J.; RT "Characterization of 20 complete plastomes from the tribe Laureae RT (Lauraceae) and distribution of small inversions."; RL PLoS ONE 14:0-e0224622(2019). 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:11128, Rhea:RHEA- CC COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400; CC EC=2.7.7.6; Evidence={ECO:0000256|ARBA:ARBA00000097, 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; MG581452; QGG45043.1; -; 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 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:QGG45043.1}; 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}; KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:QGG45043.1}; 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..232 FT /note="Alpha N-terminal domain (alpha-NTD)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00059" FT REGION 262..339 FT /note="Alpha C-terminal domain (alpha-CTD)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00059" SQ SEQUENCE 339 AA; 39155 MW; 824BDBDF79EB0E1B CRC64; MVREEVAVST RTLQWKCVES RTDSKRLYYG RFVLSPLMKG QADTIGIAMR KALLGEIEGT CITRAKSEKV SHEYSTIVGI EESVHEILMN LKEIVLRSNL YGTRDASICV RGPKYVTAQD IISPPSVELV DTTQHIANLT EPIHLCIELK IERDRGYRMK SPNNYQDGSY PIDAVSMPVR NANHSIHSYG SENEKQEILF LEIWTNGSLT PKEALREASR TLIDLFIPFL HAEEEDIHFY LEDNQNRFTV SFFTFHDRLA NIRKNKKGIA LKCIFIDQSE LPSRTYNCLK RSNIHTLLDL LNNSQEDLMR IEHLRIEDVK QILDILQKHF AIYLPKNKF //