RPOC2_PINKO
ID RPOC2_PINKO Reviewed; 1209 AA.
AC Q85X62;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 68.
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 Pinus koraiensis (Korean pine).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Strobus.
OX NCBI_TaxID=88728;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KangWon16;
RA Noh E.W., Lee J.S., Choi Y.I., Han M.S., Yi Y.S., Han S.U.;
RT "Complete nucleotide sequence of Pinus koraiensis.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
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; AY228468; AAO74001.1; -; Genomic_DNA.
DR RefSeq; NP_817153.1; NC_004677.2.
DR AlphaFoldDB; Q85X62; -.
DR GeneID; 806978; -.
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:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 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 PANTHER; PTHR19376; PTHR19376; 2.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR TIGRFAMs; TIGR02388; rpoC2_cyan; 1.
PE 3: Inferred from homology;
KW Chloroplast; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT CHAIN 1..1209
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000067941"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1209 AA; 136747 MW; 5D4FFAC8B4AF0352 CRC64;
MKIWRFLLMK KQTRLPFDNL PFYNKVMDKT AIKKLISRLI DHFGMTYTSH ILDQLKTSGF
KQATDTAISL GIDDLLTAPS KGWLVQDAEQ QGSVSEKQNH YGNLHAVEKL RQSIEIWYAT
SEYLRKEMNT NFSMTDPLNP VHVMSFSGAR GNTSQVHQLV GMRGLMSDPQ GQIIDLPIRR
NLREGLSLTE YIISCYGARK GVVDTAVRTA DAGYLTRRLV EVVQQIVVRR TDCGTVQGIF
VSPIRGRERD INEVVVRTQI LIGRVLADDV YINRRCIATR NQDIGVGLAN QLRNIRPRPI
YIRTPFTCKS ISRICQLCYG RSTTHSHLIE LGEAVGIIAG QSIGEPGTQL TLRTFHTGGV
FTGDIAEHIR APFNGKIEFN ENLVYPTRTR NGHPAYLCHN NLSITIDGQN QVQNLTIPPQ
SLLLVQNDQY VESEQIIAEV RARTSSFKEK VRKNIYSDLE GEMHWSTNVC HAPEYVHGNV
HSILRTGYLW ILSGGIYGSG VVPFPFHKYQ DQVDVQPFVA KHTDSYVDQV EHRSGDSNCY
GKEEQIFSYS ETETDRTISN EHRDSIYVTF SPKNYNMKGK KQMNRFIVSL QCDKEWGKRI
IPCPDAILRI PKSGILQINS IFGYSNVEHG IPDGPNMTTP FSLDLSREGD NLQIQISNSI
LYEDGERIQV MSDTSIPLVR TCLGFDWEQI DSIESEAYVS LISVRTNKIV NNMVQISLMK
YPPFFMGRRD NKASSNLMFH NNLDHTNLFS SNGASQLISK HQGTICSLSN GEEDSGSFMV
LSPSDCFRIV LFNDSKCYDT GNKSNRKDPM RKIIEFSGLL GHLHSITSRF PSSQFITDKK
VLSKKHSIFH NYFMDENMRI SHFDPCRNII SNLLGPNWCS SSSEFCKKTF PVVSLGQLIP
ESVWISEDEP LPESGQIIAV DEESLVIRSA KPYLATRKAT VHGHYGEILD KGDTLITLIY
ERLKSSDIIQ GLPKVEQLSE ARLNNSISMN LKESFENWTG DMTRFLGSLW GLFISARITM
EQSQIHLVNQ IQKVYRSQGV RIGDKHIEII VRQMTSKVLI SEDGTANVFS PGELIGLSRA
QRMDRALEET IYYQTMLLGI TRASLNTQSF ISEASFQETA RVLAKAALQG RIDWLKGLKE
NVILGGMIPA GTGQHIHRSG KRNGIDPRIG NRNLFSNKVK DILFHHDKVS FFSIQENYHN
ILKQPLKES
