RPOC1_ANTAG
ID RPOC1_ANTAG Reviewed; 681 AA.
AC Q85CL6;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 75.
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 Anthoceros angustus (Hornwort) (Anthoceros formosae).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Anthocerotophyta;
OC Anthocerotopsida; Anthocerotidae; Anthocerotales; Anthocerotaceae;
OC Anthoceros.
OX NCBI_TaxID=48387;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX PubMed=12527781; DOI=10.1093/nar/gkg155;
RA Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.;
RT "The complete nucleotide sequence of the hornwort (Anthoceros formosae)
RT chloroplast genome: insight into the earliest land plants.";
RL Nucleic Acids Res. 31:716-721(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RC TISSUE=Thallus;
RX PubMed=12711687; DOI=10.1093/nar/gkg327;
RA Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.;
RT "RNA editing in hornwort chloroplasts makes more than half the genes
RT functional.";
RL Nucleic Acids Res. 31:2417-2423(2003).
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 -!- RNA EDITING: Modified_positions=43 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 56 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 87 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 123 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 238 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 240 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 270 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 273 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 290 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 296 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 335 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 341 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 344 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 355 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 368 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 375 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 384 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 390 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 398 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 406 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 435 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 457 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 466 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 477 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 481 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 486 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 494 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 512 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 523 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 548 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 653 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 654 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}; Note=The nonsense codons at positions
CC 240, 344, 375, 494 and 548 are modified to sense codons.;
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01323, ECO:0000305}.
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DR EMBL; AB086179; BAC55327.1; -; Genomic_DNA.
DR EMBL; AB087419; BAC55418.1; -; mRNA.
DR RefSeq; NP_777391.1; NC_004543.1.
DR AlphaFoldDB; Q85CL6; -.
DR SMR; Q85CL6; -.
DR GeneID; 2553424; -.
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; 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 SMART; SM00663; RPOLA_N; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Plastid; RNA editing; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..681
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067860"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 491
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
SQ SEQUENCE 681 AA; 78871 MW; 164735C163338CDB CRC64;
MIYQEENQHL RIGLASPEEI RGWAERTLPN GEVVGRITEP YTLHYKTHKP EKDGLFCERI
FGPIKSGICA CGKYRSIENQ REYSKICEQC GVEFTESRVR RYRMGYIELA CPVTHVWYLK
RLPSYIANLL AKPLKELESL VYCDLFLARP IAKKPTLLKL RGLFKYEDQS WKEIFPRFFS
PRGFEAFQDR EVATGGNAIE KGLASLNLQI VMDRAYMEWR NLTEQKSTGN EWEDRKIQRR
KDLLVRRMEL AKNFLQTNMK PEWMVLSLLP VLPPELRPMI ELGEGELITS DLNELYRRVI
YRNNTLLDFL ARGRSTPGGL VVCQKRLVQE AVDALIDNGI RGQPMRDSHN RAYKSFSDLI
EGKEGRFREN LLGKRVDYSG RSVIVAGPYL PLHECGLPKE MAVELFQAFV IRGLIGRYLA
PNLRAAKSMI QDKEPIIWKI LKEVIQGHPV LLNRAPTLHR LGIQAFEPIL VEGRAIRLHP
LVCAGFNADF DGDQMAVHIP LSLEAQVEAR LLMFSHTNLL SPVTGNPVSV PSQDMLLGIY
VSTIRSNRGI YQNQYHPYDY RNKNFSYKMF YFHSYDDILK AEKQKQINLH SPLWLRWQVD
LHIVTSIDRE VPIEIQYESL GTSSQIYENY QFRKNRKEKI LSMYICTTAG RILFNQQIEE
AIQGFFEVSQ HRSRPLPAII A
