ID A0A218LNL4_PSAJU Unreviewed; 1475 AA. AC A0A218LNL4; DT 27-SEP-2017, integrated into UniProtKB/TrEMBL. DT 27-SEP-2017, sequence version 1. DT 24-JUL-2024, entry version 27. DE RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324}; DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01324}; DE AltName: Full=PEP {ECO:0000256|HAMAP-Rule:MF_01324}; DE AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324}; DE Short=RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324}; GN Name=rpoC2 {ECO:0000256|HAMAP-Rule:MF_01324, GN ECO:0000313|EMBL:ASD42860.1}; OS Psathyrostachys juncea (Russian wildrye). OG Plastid; Chloroplast {ECO:0000313|EMBL:ASD42860.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Pooideae; Triticodae; Triticeae; Hordeinae; Psathyrostachys. OX NCBI_TaxID=4586 {ECO:0000313|EMBL:ASD42860.1}; RN [1] {ECO:0000313|EMBL:ASD42860.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=28622761; DOI=10.1186/s12862-017-0989-9; RA Bernhardt N., Brassac J., Kilian B., Blattner F.R.; RT "Dated tribe-wide whole chloroplast genome phylogeny indicates recurrent RT hybridizations within Triticeae."; RL BMC Evol. Biol. 17:141-141(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|HAMAP-Rule:MF_01324}. 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|HAMAP-Rule:MF_01324}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01324}; CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01324}; 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_01324}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP- CC Rule:MF_01324}. CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2 CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01324}. 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; KY636111; ASD42860.1; -; Genomic_DNA. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW. 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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule. DR CDD; cd02655; RNAP_beta'_C; 1. DR Gene3D; 1.10.132.30; -; 1. DR Gene3D; 1.10.150.390; -; 1. DR Gene3D; 1.10.1790.20; -; 1. DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1. DR HAMAP; MF_01324; RNApol_bact_RpoC2; 1. DR InterPro; IPR012756; DNA-dir_RpoC2_beta_pp. DR InterPro; IPR050254; RNA_pol_beta'_chain. DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf. DR InterPro; IPR007083; RNA_pol_Rpb1_4. DR InterPro; IPR007081; RNA_pol_Rpb1_5. DR InterPro; IPR038120; Rpb1_funnel_sf. DR PANTHER; PTHR48355; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1. DR PANTHER; PTHR48355:SF1; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1. DR Pfam; PF05000; RNA_pol_Rpb1_4; 1. DR Pfam; PF04998; RNA_pol_Rpb1_5; 2. DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 2. PE 3: Inferred from homology; KW Chloroplast {ECO:0000313|EMBL:ASD42860.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478, KW ECO:0000256|HAMAP-Rule:MF_01324}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01324}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP- KW Rule:MF_01324}; KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:ASD42860.1}; KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP- KW Rule:MF_01324}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01324}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01324}. FT DOMAIN 93..157 FT /note="RNA polymerase Rpb1" FT /evidence="ECO:0000259|Pfam:PF05000" FT DOMAIN 207..399 FT /note="RNA polymerase Rpb1" FT /evidence="ECO:0000259|Pfam:PF04998" FT DOMAIN 1288..1375 FT /note="RNA polymerase Rpb1" FT /evidence="ECO:0000259|Pfam:PF04998" FT REGION 658..752 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 613..640 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 674..702 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 725..742 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 220 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324" FT BINDING 296 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324" FT BINDING 303 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324" FT BINDING 306 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324" SQ SEQUENCE 1475 AA; 169843 MW; 0DC5E11DED01F493 CRC64; MAERANLVFH NKEIXXTGMK RLISRLIDHF GMGYTSHILD QLKTLGFHQA TTTSISLGIE DLLTIPSKGW LVQDAEQQSF LLEKHYYYGA VHAVEKLRQS VEIWYATSEY LKQEMNSNFR ITDPSNPVYL MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII SXXXXXXXXX XXXXXXXXXX XXXXXXVEVV QHIIVRRRDC GTIRGISVSP QNGMTEKLFV QTLIGRVLAD DIYIGSRCIA ARNQDIGIGL VNRFITAFRA QPFRAQPIYI RTPFTCRSTS WICQLCYGRS PTHSDLVELG EAVGIIAGQS IGEPGTQLTL RTFHTGGVFT GGTADLVRSP SNGKIQFNEN LVHPTRTRHG QPAFLCYIDL HVTIQSQDIL YSVNIPSKSL ILVQNDQYVK SEQVIAEIRA GTSTLHFKER VQKHIYSESD GEMHWSTDVY HAPEYQYGNL RRLPKTSHLW ILSVSMCRSS IGSFSLHNDQ DQMNTYXXKD REILDYSTSD RIMSNGHWNF IYPSIFQDNS DLLAKKRRNR FLIPLQYHHE QEKELISCFG ISIEIPFMGV LRRNTIFAYF DDPRYRKDKK GSGIVKFRYR TLEEEYRTRE EDSEEEYETL EDEYRTREDE YETLSKYGIL EDEYEYETLE DEYGSPENEY GNPENEYRTL EKDSEEEYGN AESKYRTQED EYGTLEEDSE DEYGSPGESA EDKYGTLEED SEEDSEDEYE SPEEDSILKK EGLIEHRGTK EFSLKYQKEV DRFFFILQEL HILPRSSSLK ILDNSIIXXX TQLTKNTRSR LGGLVRVKRK KSHTELKIFS GDIHFPEEAD KILGGCLIPP ERQKKDSKES KKRKNWVYVQ RKKILKSKEK YFVSVRPTVA YEMDEGRNLA TLFPQDLLQE ENNLQLRLVN FISHENSKLT QRIYHTNSQF VRTCLVVNWE QEEKEKAGAS LVEVRANDLI RDFLRIELVK STISYTRKRY DRTSAGPIPH NRLDRANMNS FYSKAKIESL SQHQEAIGTL LNRNKEYHSL MILSASNCSR IGLFKNSKHP XXXXXXXXXX XXXXXXXXXX XXXASISHFY SSYYLLTHNK ILLKKYLFLD NLKQTFQVLQ GLKYSLIDEN KRISNFDSNI MLDPFLLNCH FVHHDSWEET LAIIHLGQFI CENVCLFKSH IKKSGQIFIV NMDSFVIRAA KPYLATTGAT VNGXXXXXXX XXXXLVTFIY EKSRSSDITQ GLPKVEQIFE ARSIDSLSPN LERRIEDWNE RIPRILGVPW GFLIGAELTI AQSRISLVNK IQKVYRSQGV QIHNRHIEII IRQVTSKVRV SEDGMSNVFX XXXXXXXXXX XXXXXXLDES IYYQAILLGI TRASLNTQSF ISEASFQETA RVLAKAALRG RIDWLKGLKE NVVLGGIIPV GTGFLKFVHR SPQDKNLYFE IKKKNLFASE MRDFLFLHTE LVSSDSDVTN NFYET //