ID C3W1E9_PINLA Unreviewed; 1209 AA.
AC C3W1E9;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 49.
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:ACP52126.1};
GN ORFNames=PLC-3015 {ECO:0000313|EMBL:ACP52126.1};
OS Pinus lambertiana (Sugar pine).
OG Plastid; Chloroplast {ECO:0000313|EMBL:ACP52126.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Strobus.
OX NCBI_TaxID=3343 {ECO:0000313|EMBL:ACP52126.1};
RN [1] {ECO:0000313|EMBL:ACP52126.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LAMB01 {ECO:0000313|EMBL:ACP52126.1};
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:ACP52126.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LAMB01 {ECO:0000313|EMBL:ACP52126.1};
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; FJ899577; ACP52126.1; -; 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:ACP52126.1};
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:ACP52126.1};
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..406
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT DOMAIN 1017..1104
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 1209 AA; 136789 MW; 919866F7AA079D2E 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 QLRNLRPRPI
YIRTPFTCKS ISRICQLCYG RSTTHSHLIE LGEAVGIIAG QSIGEPGTQL TLRTFHTGGV
FTGDIAEHIR APFNGKIEFN DNLVYPTRTR NGHPAYLCHN NLSITIDGQN QVQNLTIPPQ
SLLLVQNDQY VESEQIIAEV RARTSSFKEK VRKNXXXXXX XEMHWSTXXX XXXXYVHGNX
XXXXXXXYLW 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
//
