RPOC1_OLTVI
ID RPOC1_OLTVI Reviewed; 1021 AA.
AC Q20EX2;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01323};
DE AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01323};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
DE Short=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
GN Name=rpoC1 {ECO:0000255|HAMAP-Rule:MF_01323};
OS Oltmannsiellopsis viridis (Marine flagellate) (Oltmannsiella viridis).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; Oltmannsiellopsidales;
OC Oltmannsiellopsidaceae; Oltmannsiellopsis.
OX NCBI_TaxID=51324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16472375; DOI=10.1186/1741-7007-4-3;
RA Pombert J.-F., Lemieux C., Turmel M.;
RT "The complete chloroplast DNA sequence of the green alga Oltmannsiellopsis
RT viridis reveals a distinctive quadripartite architecture in the chloroplast
RT genome of early diverging ulvophytes.";
RL BMC Biol. 4:3-3(2006).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_01323}.
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:0000255|HAMAP-Rule:MF_01323};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01323}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_01323}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01323}.
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DR EMBL; DQ291132; ABB81941.1; -; Genomic_DNA.
DR RefSeq; YP_635873.1; NC_008099.1.
DR AlphaFoldDB; Q20EX2; -.
DR SMR; Q20EX2; -.
DR PRIDE; Q20EX2; -.
DR GeneID; 4100133; -.
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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01323; RNApol_bact_RpoC1; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR034678; RNApol_RpoC1.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 2.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR SMART; SM00663; RPOLA_N; 1.
PE 3: Inferred from homology;
KW Chloroplast; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Plastid; Transcription; Transferase.
FT CHAIN 1..1021
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353509"
FT REGION 161..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 804
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 806
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 808
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
SQ SEQUENCE 1021 AA; 115139 MW; 3F48C5D66F058DB8 CRC64;
MPTGSPVDAT EGSNHSTRRG VLKKRVASFS NGIHIKSIRI GLASPERIRQ WAERVLPDGT
VVGQVTNPQT VNYKTLKPEK GGLFCEQIFG SIQDTDLTTT RDRRSRLGYI QLVSPVTHVW
YLKALPSYIA ILLDLPKKHV ESISYCTETL SVPVAVHQTT GTLAPNTSTG RATTETNGDR
GHASPISVEL NPSTNQNSME LFDAPRLTKS SSNLKLTSDL GKAKQPLLLW ESSSRSKWLR
GNHGDFQANS NLIFQLNEKC LWFNTFYNSL KLEKSWNLEF PESARNSFVK KKPSKSPTGP
SNTSSGDSLG KDGTMDHVSP HKANLWGSSP LKREGWVKSA QQTLTQGSQS YPYANGLSFN
EGKSKEMGVG ALRPQGSENS LFGTHDPFDH LSTHQVKSEQ NLFKTPTFDN SKQSNTAENR
DSFSRTSARS WIINNYYSVL QTCRWKSPSD WDLFLFYMTS SVNSLDKPIP CYQNRIYDSS
GLPFDFPISG GAAIRNLLLN FDPVREDLSL IARQIENQSA KYNQEIRVLE QLYVNGLFMT
RTQRKVLFAL WRQRTKVLRR LKLVRYFRQT NMRPQWMVLS VLPVLPPDLR PIIQMNGNQV
AVSDLNKLYQ KVIFRNQRML RFARGQYTIN NSPEMRYAGR LLQEAVDALI ANGKGGGATI
SDANNRPLKS LSDMLKGKKG RFRQNLLGKR VDYSGRSVIV VGPKLKLHEC GLPKEMAIEL
FQPFLIRQLR TNKIAATIVG AKKLIRSGDQ IIWEVLKQVL QNHPILLNRA PTLHRLGIQA
FQPKLVDGRA ILLHPLVCPA FNADFDGDQM AVHVPLSYEA RSEAWKLIWA RNNILSPATG
EPILTPSQDM ILGCYYLTTT DRIRFKSTWL ASKSQQTGDS EASFAMLRPK HGPSGRKPTQ
DLCTKGSAFF APDNTAKQSE ASFALSFFSS QEEVLLAYHH HKLSLHSLIW LKWEQDFEAN
TTFESPLEIR VDKNGNSTHL YRNNLYRFNS KGEKLQQFIR TTPGRILLNQ TISQTLFTKQ
V
