RPOC1_ANEMR
ID RPOC1_ANEMR Reviewed; 699 AA.
AC B0YPL9;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 45.
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 Aneura mirabilis (Parasitic liverwort) (Cryptothallus mirabilis).
OG Plastid; Non-photosynthetic plastid.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Jungermanniopsida; Metzgeriidae; Metzgeriales; Aneuraceae; Aneura.
OX NCBI_TaxID=280810;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18056074; DOI=10.1093/molbev/msm267;
RA Wickett N.J., Zhang Y., Hansen S.K., Roper J.M., Kuehl J.V., Plock S.A.,
RA Wolf P.G., dePamphilis C.W., Boore J.L., Goffinet B.;
RT "Functional gene losses occur with minimal size reduction in the plastid
RT genome of the parasitic liverwort Aneura mirabilis.";
RL Mol. Biol. Evol. 25:393-401(2008).
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 -!- SUBCELLULAR LOCATION: Plastid.
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; EU043314; ABS54466.1; -; Genomic_DNA.
DR RefSeq; YP_001687205.1; NC_010359.1.
DR AlphaFoldDB; B0YPL9; -.
DR SMR; B0YPL9; -.
DR GeneID; 5952164; -.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; 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 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 DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT CHAIN 1..699
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353472"
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 699 AA; 81058 MW; 80D48343F03D05E8 CRC64;
MIHRIKYQRL RIELASPEQI RNWAERKLPD GEIVGRVTKP YTLHYKTHKP EKDGLFRERI
FGPVRSGVCI CGRYKGIASG KETTKFCEHC GVDLTRSRIR RYRMGYIELA CPVTHVWYLK
RLPSCIANLL DKPLKELESL VHCDLFTARP INEKPTLLKL HGLFKYEDQS WRDVFPRFFS
CGGFEIFRDR EIATGGDAIK KQLIDLDLQS VMSHAHSEWE ELTKQESTGT DWGDRKIQRN
KDLLVRRMKL SKYFVQTNIE PEWMVLSLLP VLPPELRPMI ELGEGELITS DLNELYRRVI
YRNNTLLDFL ARSDSTPRGL IICQKRLVQE AVDALIDNGI RGQPMRDNHN RPYKSFSDLL
GGKEGRFREN LLGKRVDYSG RSVIVVGPSL PLHRCGLPRE MAIELFQAFV IRGLIGRNLA
PNLRAAKTMI RGNKPMIWKI LQEVIEEHPI LLNRAPTLHR LGIQAFQPVL VHGRAIHLHP
LVCSGFNADF DGDQMAVHVP LSLEAQVEAR LLMLSRRNVL SPATGEPLCI PSQDMLLGLY
ALTMENRRGI YGNKYSLDSN KETYLKNFSF PKIPYFHGYE DVYKAHQQRE IHSHSVLWLR
WQTNFRMITS TPREEPIEIQ YETSGISYRI YNHYQLEINA QREIISIYIC TTVGRVLFNQ
RIDEAIQGTC QASSRQTMLY IGNKEDRFLS SEKLNRRYK
