ID A0A220T5U5_PHEAM Unreviewed; 328 AA. AC A0A220T5U5; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 19-JAN-2022, entry version 18. 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:ASK51019.1}; OS Phellodendron amurense (Amur cork tree). OG Plastid; Chloroplast {ECO:0000313|EMBL:ASK51019.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Sapindales; Rutaceae; Amyridoideae; Phellodendron. OX NCBI_TaxID=68554 {ECO:0000313|EMBL:ASK51019.1}; RN [1] {ECO:0000313|EMBL:ASK51019.1} RP NUCLEOTIDE SEQUENCE. RA Chen K.-K.; RT "Characterization of the complete chloroplast genome of the Tertiary relict RT tree Phellodendron amurense (Sapindales: Rutaceae) using Illumina RT sequencing technology."; RL Conserv Genet Resour 0:0-0(2017). 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; KY707335; ASK51019.1; -; 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:ASK51019.1}; 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:ASK51019.1}; 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..233 FT /note="RPOLD" FT /evidence="ECO:0000259|SMART:SM00662" FT REGION 1..236 FT /note="Alpha N-terminal domain (alpha-NTD)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00059" FT REGION 270..328 FT /note="Alpha C-terminal domain (alpha-CTD)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00059" SQ SEQUENCE 328 AA; 37387 MW; BBCDCC357BAC07E5 CRC64; MVREKVKVST RALQWKCVES RADSKRLYYG RFILSPLMKG QADTIGIAMR RVLLGEIEGT CITRAKSEKI PHEYSTIVGI QESVHEILMN LKEIVLRSNL YGTCDALICV KGPGDVTAQD ILLPPSVEIV DKTQHIASLT EPIDLCIGLQ IERSRGYNIK TPNNFQDGNC YPIDAAFMPV RNANHSIQSY GNGNEKQEIL FLEIWTNGSL TPKEALHEAS RSLIDLFIPF LQAADENLHL ENNQYKVTLP FFTFHDRLAK LTKKKKEIAL KSIFIDQSEL SPRIYNCLKK SNIHTLFELL NKSQEDLMKI EHFRLEDVKQ IMGILENK //