ID A0A6H1XEV8_PRUMU Unreviewed; 683 AA. AC A0A6H1XEV8; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 29-SEP-2021, entry version 6. DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01323}; DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01323}; DE AltName: Full=PEP {ECO:0000256|HAMAP-Rule:MF_01323}; DE AltName: Full=Plastid-encoded RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01323}; DE Short=RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01323}; GN Name=rpoC1 {ECO:0000256|HAMAP-Rule:MF_01323, GN ECO:0000313|EMBL:QJA14058.1}; OS Prunus mume (Japanese apricot) (Armeniaca mume). OG Plastid; Chloroplast {ECO:0000313|EMBL:QJA14058.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus. OX NCBI_TaxID=102107 {ECO:0000313|EMBL:QJA14058.1}; RN [1] {ECO:0000313|EMBL:QJA14058.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Leaf {ECO:0000313|EMBL:QJA14058.1}; RX PubMed=31666958; RA Xue S., Shi T., Luo W., Ni X., Iqbal S., Ni Z., Huang X., Yao D., Shen Z., RA Gao Z.; RT "Comparative analysis of the complete chloroplast genome among Prunus mume, RT P. armeniaca, and P. salicina."; RL Hortic Res 6:0-89(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|HAMAP-Rule:MF_01323, ECO:0000256|RuleBase:RU004279}. 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:ARBA00000097, CC ECO:0000256|HAMAP-Rule:MF_01323, ECO:0000256|RuleBase:RU004279}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01323}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01323}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01323}; CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01323}; 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_01323}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP- CC Rule:MF_01323}. CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1 CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01323}. 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; MH700953; QJA14058.1; -; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.274.100; -; 1. DR HAMAP; MF_01323; RNApol_bact_RpoC1; 1. DR InterPro; IPR000722; RNA_pol_asu. DR InterPro; IPR006592; RNA_pol_N. DR InterPro; IPR007080; RNA_pol_Rpb1_1. DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf. DR InterPro; IPR034678; RNApol_RpoC1. DR Pfam; PF04997; RNA_pol_Rpb1_1; 1. DR Pfam; PF00623; RNA_pol_Rpb1_2; 2. DR SMART; SM00663; RPOLA_N; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000313|EMBL:QJA14058.1}; KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478, KW ECO:0000256|HAMAP-Rule:MF_01323}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01323}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01323}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP- KW Rule:MF_01323}; Plastid {ECO:0000313|EMBL:QJA14058.1}; KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP- KW Rule:MF_01323}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01323}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01323}. FT DOMAIN 263..544 FT /note="RPOLA_N" FT /evidence="ECO:0000259|SMART:SM00663" FT METAL 69 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT METAL 71 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT METAL 87 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT METAL 90 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT METAL 490 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT METAL 492 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT METAL 494 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" SQ SEQUENCE 683 AA; 78831 MW; 192CE8694D665EDB CRC64; MIDQYKHQQL RIGLVSPQQI SAWAQKILPN GEIVGEVTKP YTFHYKTNKP EKDGLFCERI FGPIKSGICA CGNYRVIGDE KKDPRFCEQC GVEFVDSRIR RYQMGYIKLA CPVTHVWYLK RLPSYIANLL DKPLKELEGL VYCDVFSFAR PIAKKPTFLR LRGSFEYEIQ SWKYSIPLFF TTQGFDTFRN REISTGAGAI REQLADLDLR IIIDYSLVEW KELGEEGPTG NEWEDRKVGR RKDFLVRRME LAKHFIRTNI EPEWMVLCLL PVLPPELRPI IQIDGGKLMS SDINELYRRV IYRNNTLIDL LTTSRSTPGE LVMCQEKLVQ EAVDTLLDNG IRGQPMRDGH NKVYKSFSDV IEGKEGRFRE TLLGKRVDYS GRSVIVVGPS LSLHRCGLPR EIAIELFQTF VIRGLIRQHF ASNIGVAKSK IREKEPVVWE ILHEVMQGHP VLLNRAPTLH RLGIQAFQPI LVEGHAICLH PLVCKGFNAD FDGDQMAVHV PLSLEAQAEA RLLMFSHMNL LSPAIGDPIS VPTQDMLIGL YVLTSGNRRG ICANRYNPCN RRNYQNKRID DNNYKYTKEK EPFFCNSYDA IGAYRQKRIN LDSPLWLRWR LDQRVITSRE TPIEVHYESL GTYHEIYGHY LIVRSIKKEI ICIYVRTTVG HISLYREIEE AIQGFCRAYS YGT //