ID A0A4P8JBL5_9LILI Unreviewed; 342 AA. AC A0A4P8JBL5; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 16-OCT-2019, entry version 3. 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:QCP68187.1}; OS Lanxangia paratsaoko. OG Plastid; Chloroplast {ECO:0000313|EMBL:QCP68187.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Zingiberaceae; OC Lanxangia. OX NCBI_TaxID=252857 {ECO:0000313|EMBL:QCP68187.1}; RN [1] {ECO:0000313|EMBL:QCP68187.1} RP NUCLEOTIDE SEQUENCE. RA Gao Y., Li G., Zhang Y., Qian Z.; RT "Characterization of the complete chloroplast genome of Amomum para- RT tsaoko S. Q. Tong et Y. M. Xia(Zingiberaceae)."; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. {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, CC ChEBI:CHEBI:83400; EC=2.7.7.6; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00059}; CC -!- SUBUNIT: In plastids the minimal PEP RNA polymerase catalytic core CC is composed of four subunits: alpha, beta, beta', and beta''. When CC a (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 CC basal transcription, whereas the C-terminal domain is involved in CC interaction with transcriptional regulators and with upstream CC promoter elements. {ECO:0000256|HAMAP-Rule:MF_00059}. CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family. CC {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; MH423780; QCP68187.1; -; 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: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:QCP68187.1}; KW DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00059}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00059}; KW Plastid {ECO:0000313|EMBL:QCP68187.1}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_00059}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00059}. FT DOMAIN 29 232 RPOLD. {ECO:0000259|SMART:SM00662}. FT REGION 1 240 Alpha N-terminal domain (alpha-NTD). FT {ECO:0000256|HAMAP-Rule:MF_00059}. FT REGION 269 342 Alpha C-terminal domain (alpha-CTD). FT {ECO:0000256|HAMAP-Rule:MF_00059}. SQ SEQUENCE 342 AA; 39540 MW; B795936F13D1FF51 CRC64; MVREEVVGST RTLQWRCVES RIDSNRLYYG RFILCPLMKG QADTIGIAMR RALLGEIEGT CITCAKSEKV PHEYSTIVGI EESVHEILLN LKEIVLRSNI HGVRDASICV KGPKYVTAQD IISPPFVEIV DTTQHIANLT EPIDLCIGLQ IRRDRGYRTK LTINSQDGSY PIDAVSMPVR NANHSIHSFG NGKEKEEILF LEIWTNGSLT PKEALYEASR NLIDLFIPFL HGEEEDINFK LKENKNRFTL PIFTFQDRLT NLKKNKKEIP LKCIFIDQSE LPYRTYNCLK RSNIHTLLEL LSKSQEDLMR IEYFRIEDVK EISDTLRKHF EIDLPKNKFS FF //