RPOC1_HELSJ
ID RPOC1_HELSJ Reviewed; 834 AA.
AC Q2EEW9;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000305};
DE Short=RNAP subunit gamma;
DE EC=2.7.7.6;
DE AltName: Full=RNA polymerase subunit gamma;
DE AltName: Full=Transcriptase subunit gamma;
GN Name=rpoC1;
OS Helicosporidium sp. subsp. Simulium jonesii (Green alga).
OG Plastid; Non-photosynthetic plastid.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Helicosporidium; unclassified Helicosporidium.
OX NCBI_TaxID=145475;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16630350; DOI=10.1186/1741-7007-4-12;
RA de Koning A.P., Keeling P.J.;
RT "The complete plastid genome sequence of the parasitic green alga,
RT Helicosporidium sp. is highly reduced and structured.";
RL BMC Biol. 4:12-12(2006).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000250}.
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:0000250|UniProtKB:P0A8T7};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0A8T7};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P0A8T7};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P0A8T7};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000250|UniProtKB:P0A8T7};
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC subfamily. {ECO:0000305}.
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; DQ398104; ABD33973.1; -; Genomic_DNA.
DR RefSeq; YP_635925.1; NC_008100.1.
DR AlphaFoldDB; Q2EEW9; -.
DR GeneID; 4100416; -.
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:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.274.100; -; 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 PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 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..834
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000309002"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 641
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 643
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 645
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
SQ SEQUENCE 834 AA; 98313 MW; B99E68DC7D3B5304 CRC64;
MKYFIIRSLI NKSKNFYNTI IKYNKTKLFA LELSIISPQE IQNSAEYKRE DGSIVGKVED
STFYDLEKVN NKNLFSQQIF GPLIDFTCAC GKKLNRKNKE INVCTKCGIE FLPSSIRSKR
KGYIKLNYAM LHPFYIDYCE KLLMKSKKSL HLLLNMDSFF YFPSYKNWVN FLSEKNHIYL
FLLKKILIYN RYSYIYKYST FFKNRSKFPN NKKMNKLFFY NALGFYGLNS RKTWTVLDFI
KGYNFFLGNF SKYYKKLSWY AYQQKISLNK YKSNNISINN FIDNTFNFYK NEVNSLCFKV
GGDGIEMFFL QDMAVYSIIN KFLKLRVLKL NNLINVNNKY YGKINTIIQN SKNYQYYFKH
FYLKKIAPVW MTLRRIPVLP PNLRPILDLS GKNYQKTASS GTLLFMRDIM HEGNLFISDI
NTFYREIIIH NKKAFNFFSS LPTLYYLNEL NIEYVNSKLW LLKYYLMPIQ KSITSLFDKN
PETINNFSNK KFTDLILDNV KPTSILDSLK GKYGKIRFNL LGKRVDYSGR SVIISAPHLK
IYECGIPYEM ALTLYYPFLS EYFYKKNNNI LKKNYNKSEL VLYSKSLIFT KSLQSILLSH
PIIINRAPTL HRLGIQSFLP KLTHSKAIEL HPLVCPAFNA DFDGDQMAIH VPITEIAKLE
AIQLMASSLF VYAPASGLPL LIPTQDIILG FNFYTNDLLL KTSREDKSIK QAMNQGFINE
CHIPYWIKIN TKDIFFKFLA YPLRNYIIPI ELQLNIKGFS KIIRLNTFKV TNLVFDSLDL
LIKKNYISNW LILNNTKFKY LLISFLQNKN LLTNKQVYLR TTLGNIYFNK YLNL
