ID   RPOC1_EUGLO             Reviewed;         575 AA.
AC   P58131;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000305};
DE            EC=2.7.7.6 {ECO:0000250|UniProtKB:P0A8T7};
DE   AltName: Full=PEP;
DE   AltName: Full=Plastid-encoded RNA polymerase subunit beta' {ECO:0000305};
DE            Short=RNA polymerase subunit beta';
GN   Name=rpoC1 {ECO:0000305};
OS   Euglena longa (Euglenophycean alga) (Astasia longa).
OG   Plastid; Non-photosynthetic plastid.
OC   Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC   Euglenales; Euglenaceae; Euglena.
OX   NCBI_TaxID=3037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCAP 1204-17a;
RX   PubMed=11212895; DOI=10.1078/s1434-4610(04)70033-4;
RA   Gockel G., Hachtel W.;
RT   "Complete gene map of the plastid genome of the nonphotosynthetic euglenoid
RT   flagellate Astasia longa.";
RL   Protist 151:347-351(2000).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000305}.
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. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Plastid.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AJ294725; CAC24618.1; -; Genomic_DNA.
DR   RefSeq; NP_075007.1; NC_002652.1.
DR   AlphaFoldDB; P58131; -.
DR   SMR; P58131; -.
DR   GeneID; 802517; -.
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   Gene3D; 4.10.860.120; -; 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   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   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT   CHAIN           1..575
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000067862"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   BINDING         85
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   BINDING         440
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   BINDING         442
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   BINDING         444
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
SQ   SEQUENCE   575 AA;  67075 MW;  C83269D0B54F8DAF CRC64;
     MRDYVKINIA SPKQILKWTE RLTPKGKYIG KLKNSKKTLD KKGKCIRGGL FCEQIFGPTK
     KNTCRCGYYK NYKKSKKEKK HIKLCRICNV EITDPIIRNY RMGYIELNIP IINILYLNIN
     PCYLAIITNL KINYLKQLHS GKAYITIKDK NQKEKKLTGG EAINDILSKI DLEKTLIKLT
     NNIHQYKEKN ITIKNFKNIL NKIKLYNYLL QTKIKFSWLL FKYLPVLPPN VRPIINMKNN
     QQISNDLNTL YASIINVNNK IIKLKESLIP DNYFINEKIL LQKKVDQLIN NEKYKENKLG
     KIINNKKLKS ITENIKGKEG IIRENMLGKT VNFSGRSVIV VEPTLNLNEC GLPKEMAINL
     FYPFIIKELI KLKLIKRLYK IKKITKILDI ILENIIKNHY ILLNRAPTLH RLNIQAFQPK
     LTIGKSIKLH PLVCSAFNAD FDGDQMGVHI PLSLKAQAEA RNILISINNC NSLKNGDPNI
     LPSQDIILGC YFSNIENCNL LYILNKIQIY TNMEKIKMEY KKENLSIHNF IWLNFKNKQQ
     IDKLKIKRKN LIKKIIFLRT TVGRILFNDI IKNFL