ID   RPOC2_HELSJ             Reviewed;        1058 AA.
AC   Q2EEX0;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta'';
DE            EC=2.7.7.6;
DE   AltName: Full=PEP;
DE   AltName: Full=Plastid-encoded RNA polymerase subunit beta'';
DE            Short=RNA polymerase subunit beta'';
GN   Name=rpoC2;
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=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. RpoC2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; DQ398104; ABD33972.1; -; Genomic_DNA.
DR   RefSeq; YP_635924.1; NC_008100.1.
DR   AlphaFoldDB; Q2EEX0; -.
DR   PRIDE; Q2EEX0; -.
DR   GeneID; 4100415; -.
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; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.274.100; -; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR   InterPro; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   PANTHER; PTHR19376; PTHR19376; 2.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW   Plastid; Transcription; Transferase; Zinc.
FT   CHAIN           1..1058
FT                   /note="DNA-directed RNA polymerase subunit beta''"
FT                   /id="PRO_0000309003"
FT   BINDING         235
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   BINDING         304
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   BINDING         311
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT   BINDING         314
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A8T7"
SQ   SEQUENCE   1058 AA;  122966 MW;  07340DBFCC5AD2CB CRC64;
     MIKTSQIAKY IFLLKKAEFI KSEKKHVILN KTTLKKMVFI LQNKYDEQTV FFILEKLKEI
     GFHLATQSGL SLGIDDLKSF PDKKKLITET RTDLNNNEEH FLLQNISPLE KSKYLITKWN
     DVNNFIIQRI KKVFLKKEPL NPLALMAFSG ARGNISQVSQ LIGLRGLMTD PLGKLVEFPI
     QGNFREGMTL TEYFISCYGA RKGLVDTALR TATAGYLTRR LVYVVQHIFI SIEDCNVTNG
     ISVEINEKSS NSLIGLTLLK NFYNKNIFIA KNTIISPTLV KLLLNSYNYL SHKKSIVCRS
     ILTCQLQHTL CQFCYGWDNA RAKRVAIGEA IGIIAAQSIG EPGTQLTLRT FHTGGVGGFS
     GANWISYNSP FDGFIKFKKP VIGNILRSWI VMPHYTSLNL VYKLTPSFNE LNLTLFIFDK
     LKNELYNKTL KNEGLLFVRE GDFIKKGQLL FSEININFKN SNLLKTYIPY YSLETGLIIS
     PKLALNKYLY PLWIFLFNII KLNLDSLNSK KFTVYKNYSI LEKNDLIDLK TILFEIHFIQ
     KSKKFNLKKQ EYLLYQNLKM SLCKSHYDYS TYKKLNVAFQ QNNQKLNFFY NKKLKSSLVS
     NNINLLWTSS SYSINILTKS IFNIIVFEYL YLSLLIKNKY ILWILSKNLK KKDKFHFFKY
     TSTSSSKIEI FRLNSKKNSL NIRKNKLFFY SQNYKKNKVS NILFGNSIFL KFPLKKINTF
     FSQIKQKTIN LKEKKTSNVE GEFIGFQLKN NIKFWYSISP NSLFSFKKDN KKNRYNFNFI
     RKNSNISGFL VSNTIKTFTL QKGIPLIFPS DTIYHKMEKD FIFKNELLCS FKSLKPETQD
     IIQGIPRVEK LLEGRPLPFY KPKVELYKIW QFFLKNLGFL KIKNSLFNLK KVESKVYLNN
     FKPNLNIGDI CYLAYFHSKS NFGLDIASII SNVYLQEGVN ISFKHIELIV RELTSLVEII
     NPGDSGFIVK EKIHWLLIYN YNKRLKSLNL KEISYMPIFL GMTEITKKKN SFGVAGSFQN
     LREIIIDHTF TRKTDYLLGL HENVLFNKII PAGTGFFF