RPOC1_WELMI
ID RPOC1_WELMI Reviewed; 696 AA.
AC B2Y1V6; B7ZI52;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 46.
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 Welwitschia mirabilis (Tree tumbo) (Welwitschia bainesii).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Gnetopsida; Gnetidae; Welwitschiales; Welwitschiaceae;
OC Welwitschia.
OX NCBI_TaxID=3377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18452621; DOI=10.1186/1471-2148-8-130;
RA McCoy S.R., Kuehl J.V., Boore J.L., Raubeson L.A.;
RT "The complete plastid genome sequence of Welwitschia mirabilis: an
RT unusually compact plastome with accelerated divergence rates.";
RL BMC Evol. Biol. 8:130-130(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19166950; DOI=10.1016/j.ympev.2008.12.026;
RA Wu C.-S., Lai Y.-T., Lin C.-P., Wang Y.-N., Chaw S.-M.;
RT "Evolution of reduced and compact chloroplast genomes (cpDNAs) in
RT gnetophytes: Selection toward a lower-cost strategy.";
RL Mol. Phylogenet. Evol. 52:115-124(2009).
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC Note=Binds 1 Zn(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; EU342371; ABY26786.1; -; Genomic_DNA.
DR EMBL; AP009568; BAH11232.1; -; Genomic_DNA.
DR RefSeq; YP_001876573.1; NC_010654.1.
DR AlphaFoldDB; B2Y1V6; -.
DR SMR; B2Y1V6; -.
DR PRIDE; B2Y1V6; -.
DR GeneID; 6276249; -.
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: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 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; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 2.
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; Zinc.
FT CHAIN 1..696
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353516"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 506
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 508
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 510
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT CONFLICT 155
FT /note="L -> LNL (in Ref. 2; BAH11232)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 696 AA; 80297 MW; B2365AD5B7284E93 CRC64;
MIDSKKKHQK LKITLVSPEQ IRAWSETILP NGKRVGEVTN PDTLDPTTKK PQRDGLYCER
IFGPVKSGVC ACEKKPGQKK KGFAFVDRKK KKDSNFCKYC EVELVDSRIR RYRMGYIKLA
CPVAHIWYIK RVPSYIPTLI GKKKSEVIDL VYCNLFITRP AANRPTILRF RGLLQDENLP
SWIGILFPYI SSWNFVEFQE RELATGGNAI QKRLTGLDLR ILLTHSYMEW KKLLRNYKIQ
RTQREKNKIQ KRKNFLVRRI KFVKYLIQAK IKPEWMVLCL LPVLPPELRP IFVLGEQIIA
ESDLNKLYQK VLIRNKNLQS SFEMQGDPLY STGKRDFMTF QKRLLQEAVD ALLDNDRSGE
PGEDLFNRPY KSFSDVIAGK EGRFRANLLG KRVDYSGRSV IVVGPSLALH QCGLPREMAI
KLFQPFLIRN LIRRGVAPNI RAAKSLIQGR KPFIWKILQR VMLGHPVLLN RAPTLHKFGI
LAFQPILVKE HAIRLHPSVC TGFNADFDGD QMAVHVPLSI EAILESRLLM FSHTNLLSPS
SGSPITIPTQ DMLLGLYILT ADKNQDISEF RYHPSKSKKK ISSKKNPCFS NYDDVFIAYQ
QKRVQLNSPL WLRWRVADGG ILTSVDREVP IEIQHEPFGT SQEIYEHYAI QKNRMGKISN
IYIRTTVGRI LFNREIEKAF LSFSKLLESP QTNPVF