ID RPOC2_BIGNA Reviewed; 1595 AA.
AC Q06J19;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 13-SEP-2023, entry version 57.
DE RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE Short=RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
GN Name=rpoC2 {ECO:0000255|HAMAP-Rule:MF_01324};
OS Bigelowiella natans (Pedinomonas minutissima) (Chlorarachnion sp. (strain
OS CCMP621)).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Rhizaria; Cercozoa; Chlorarachniophyceae; Bigelowiella.
OX NCBI_TaxID=227086;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16990439; DOI=10.1093/molbev/msl129;
RA Rogers M.B., Gilson P.R., Su V., McFadden G.I., Keeling P.J.;
RT "The complete chloroplast genome of the chlorarachniophyte Bigelowiella
RT natans: evidence for independent origins of chlorarachniophyte and euglenid
RT secondary endosymbionts.";
RL Mol. Biol. Evol. 24:54-62(2007).
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_01324}.
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_01324};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01324};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01324};
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_01324}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_01324}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01324}.
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DR EMBL; DQ851108; ABG91440.1; -; Genomic_DNA.
DR RefSeq; YP_778608.1; NC_008408.1.
DR AlphaFoldDB; Q06J19; -.
DR SMR; Q06J19; -.
DR GeneID; 4353025; -.
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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd02655; RNAP_beta'_C; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 1.10.1790.20; -; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR HAMAP; MF_01324; RNApol_bact_RpoC2; 1.
DR InterPro; IPR012756; DNA-dir_RpoC2_beta_pp.
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 NCBIfam; TIGR02388; rpoC2_cyan; 1.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF54; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 3.
PE 3: Inferred from homology;
KW Chloroplast; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT CHAIN 1..1595
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000310398"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1595 AA; 185962 MW; D420BC00F300AABB CRC64;
MEKIFFNYPF NKGKLKTLLI WSILNTGQYN MINLVENLKK VGFQYATTAG ISLGIDDLKT
ISTKYDLIEK TNDNIKDITN HLNLAVLNEV EHSQKLINSW QKISEILKIN INKKFKTVNK
LNPIYMMAFS GARGNISQVR QLIGMRGLMA DPNGQIIHLP IKSNFREGLT VTEYLISCYG
ARKGVVDTAL RTATAGYLTR RLVDTAQHVI ISQLDCGTKQ GIFLSNLYQG TDILLALKDQ
LYGRVLGKDI KINSLMYLKN QQIDDSLSIL LANHLKRVFI RSPLTCKASN STLCQLCYGW
NLSHSKLISL GEIVGVIAAQ SIGEPGTQLT MRTFHTGGVF SGNVKSQLYS PFDGIVEYSS
SLYGDIVNLY NGNFAFLVKR KGLIIINPII KKIKPKKFEA ILYTLVFVKN NEKVKKNQLI
AQQSNKISNT QQIEGKYTVN SKLEGEILFD ENHLSTNKKK IWILHGKIYK SVFPLQLFPK
KNDFLSYKFP LAQAKLLNLS ASFLKVCVVR KKRHFIKDNI SQSNEILLFT EYPLYKFLIK
NIKNYHQFQF FYPIQNKIKE VEKSLRINNK VIKDNRIKIP FNSIAKSKLL NLLNKRLEQN
TFFSKNTFSN YYENTDERTT WFTQNSILKY NAIYFYKSSK SVEAKTSRKI PITFNSKNFL
IKEKLFFIKN NSVLLPIFSS DFFTKFTLKN EYFKPKHNIQ RKLGFLSPTS YFKYISNNYF
LKYLNFYQKH ISVEMNDIIK VKLYYKQEFE EKTNFKKQNL HKIDSKINLF MNKLILVIEH
LILTKLFSTK INNINYLLFY FNYLKYLKES NKFTIFYCNK KKETIFDLLF LLKTLNTTSN
LIILAENKIS TKLLSEFIYQ TIYLIKNNIT INSTNSVLEN FNYFQQRKED LFQHRNIFEK
VPNFSGKRFS NLSLNINNEN YSISKAENKM LIQDLLTLTI LNNNIKYFNS HKSFLDKRFF
YNESLPIPKI LKDFTSILNR INFWSFSSSQ FYKKHFLFAL KTDNLINIKN KNFIFISRIP
QIQAVNFALK KSLKSSFDLK SYEILQYNLK FPLGFYSLIK MIIEERSLFD IDYFQKFIIQ
YKNFSFHLIN KKLKNIFTNN SYGSFTDEST LLESKYFNKR RPTKTTFSKL MNQIKFKFFI
KVPLLLSTFS KKDTVLFNIF ITNKKENFRN YKIVNMLTND FYKNLNLQTH SSEKNSQLKL
SSKNLEIFNL FYTSSIINVI MKKSITNFNK NFFIDNLFQF SKTHFNWLPK WDTIVRIQFL
SPYQGEIIAQ NIVKYSGYKT LYNHLMILTK NEKLQVSIFR NKNQETIIKK DTKNYFITKP
HCCKIYPKFG SLIYSTSQVS PGKKINQSGQ IIEKSNSFLV LRKGTPLLSP ITGIFYVWNG
DFVSQGSPIM TLLYNKLKTG DIVQGIPKIE HFFEARKGNV DLIQTNLYIK LLAFFKKYNK
TLSEYRAVKR SILKIQKIII DGVCRVYCSQ GILVSRKHFE VIVKQMTSKV KIVNGGETGL
LEGEFINFQK LEKINTNLYH RRVVYEPLVL GITKVSLRTE SFISSASFQE TTKVLSQAAL
EKRIDFLNGL KENVILGKLI PGGTGLIVKI ITNKI
//
