ID C3W0D5_PINBN Unreviewed; 1222 AA.
AC C3W0D5;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01324};
DE AltName: Full=PEP {ECO:0000256|HAMAP-Rule:MF_01324};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
DE Short=RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324};
GN Name=rpoC2 {ECO:0000256|HAMAP-Rule:MF_01324,
GN ECO:0000313|EMBL:ACP51762.1};
GN ORFNames=PLC-1215 {ECO:0000313|EMBL:ACP51762.1};
OS Pinus banksiana (Jack pine) (Pinus divaricata).
OG Plastid; Chloroplast {ECO:0000313|EMBL:ACP51762.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=3353 {ECO:0000313|EMBL:ACP51762.1};
RN [1] {ECO:0000313|EMBL:ACP51762.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BANK03 {ECO:0000313|EMBL:ACP51762.1};
RX PubMed=19954512; DOI=10.1186/1741-7007-7-84;
RA Parks M., Cronn R., Liston A.;
RT "Increasing phylogenetic resolution at low taxonomic levels using massively
RT parallel sequencing of chloroplast genomes.";
RL BMC Biol. 7:84-84(2009).
RN [2] {ECO:0000313|EMBL:ACP51762.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BANK03 {ECO:0000313|EMBL:ACP51762.1};
RA Parks M.B., Liston A., Cronn R.C.;
RL Submitted (APR-2009) 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:0000256|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:0000256|HAMAP-Rule:MF_01324};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01324};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01324}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC Rule:MF_01324}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01324}.
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DR EMBL; FJ899571; ACP51762.1; -; Genomic_DNA.
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; 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; PTHR48355; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
DR PANTHER; PTHR48355:SF2; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000313|EMBL:ACP51762.1};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_01324};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01324};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01324}; Plastid {ECO:0000313|EMBL:ACP51762.1};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_01324};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01324};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01324}.
FT DOMAIN 106..183
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF05000"
FT DOMAIN 185..410
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT DOMAIN 1027..1114
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1222 AA; 139031 MW; FCAF3EAE9495BEE9 CRC64;
MKIWRFFLMK ERTRLPFDNL PFYNKVMDKT AIKKLISRLI DHFGMTYTSH ILDQLKTSGF
QQATDTAISL GIDDLLTAPS KGWLVQDAEQ QGSVSEKQNH YGNVHAVEKL RQSIEIWYAT
SEYLRKEMNP NFSMTDPLNP VHVMSFSGAR GSTSQVHQLV GMRGLMSDPQ GQIIDLPIRR
NLREGLSLTE YIISCYGARK GVVDTAVRTA DAGYLTRRLV EVVQHIVVRR TDCGTIQGIF
VSPIRGRERD RNEIVVRTQI LIGRVLADDV YINRRCIATR NQDIGVGLAN QLINLRTQPI
YIRTPFTCKS ISRICQLCYG RSTTHSHLIE LGEAVGIIAG QSIGEPGTQL TLRTFHTGGV
FTGDIAEHIR APFNGKIEFN ENLVYPTRTR NGHPAYLCHN NLSITIDGQD QVQNLTIPSQ
SLLLVQNDQY VESEQLIAEV RARTSSFKEK VRKNIYSDXX XXMHWSTXXX XXXXYVQGNX
XXXLRTGYLW ILSGGIYGSR VVPFPFHKYQ DQVYVQPFVA KHQSFSDSYV DQVEHRSGDS
NCYEKEEQIF SYSETETDRT ISNEHRDSIY VFSPNNYNIK GKKQMNRFIV SLQCDKEWEK
RIIPCPDAIL RIPKSGILQR NSIFGYSNVE HGIPDGSNMT TPFSLDLSRE GDNLQIKISY
SISYEDGERI QVSIPLVRTC LGFDWEQIDS IESEAYVSLI SVRTNKIVNN MVQISLMKYP
PFFMGRRDNK TSSNLMFHNN LDHTNLFSSN GASQLISKHQ GTICSLSNGE EDSGSFMVLS
PSDYFRIVLF NDSKCYDTGN QSNRKDPMRK IIEFSGLLGN LHSITNRFPS SHFLTYKKVL
SKKHSIFHNS FNTFQVPKYY FMDENMIIYH FDPCRNIISN LLGPNWCSSS SESEFCEKTF
PVVSLGQLIP ESVWISEDEP LPESGQIIAV DEESLVIRSA KPYLATRKAT VHSHYGEILD
KGDTLITLIY ERFKSSDIIQ GLPKVEQLSE ARLNNSISMN LKESFENWTG DMTRFLGSLW
GLFISARITM EQSQIHLVNQ IQKVYRSQGV RIGDKHIEII VRQMTSKVLI SEDGTANVFS
PGELIGLSRA QRMDRALEEA IYYQTMLLGI TRASLNTQSF ISEASFQETA RVLAKAALQG
RIDWLKGLKE NVILGGMIPA GTGQHIHRSG KRNGIDPRIG NRNLFSNKVK DILFHHEKVD
FFSFQAKSYK YHNILKKKIK ES
//
