ID B7ZIN6_KETDA Unreviewed; 1222 AA.
AC B7ZIN6;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 56.
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:BAH11403.1};
OS Keteleeria davidiana (David's keteleeria) (Pseudotsuga davidiana).
OG Plastid; Chloroplast {ECO:0000313|EMBL:BAH11403.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae;
OC Keteleeria.
OX NCBI_TaxID=3324 {ECO:0000313|EMBL:BAH11403.1};
RN [1] {ECO:0000313|EMBL:BAH11403.1}
RP NUCLEOTIDE SEQUENCE.
RA Wu C., Chaw S.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAH11403.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19166950; DOI=10.1016/j.ympev.2008.12.026;
RA Wu C.-S., Lai Y.-T., Lin C.-P., Wang Y.-N., Chaw S.-M.;
RT "Evolution of reduced and compact chloroplast genomes (cpDNAs) in
RT gnetophytes: Selection toward a lower-cost strategy.";
RL Mol. Phylogenet. Evol. 52:115-124(2009).
RN [3] {ECO:0000313|EMBL:BCK60587.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Chaw 1470 {ECO:0000313|EMBL:BCK60587.1};
RA Wu C.S., Sudianto E., Chaw S.M.;
RT "Tight association of genome rearrangements with gene expression in conifer
RT plastomes.";
RL BMC Plant 21:33-33(2021).
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|ARBA:ARBA00024550,
CC 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; AP010820; BAH11403.1; -; Genomic_DNA.
DR EMBL; LC571883; BCK60587.1; -; Genomic_DNA.
DR RefSeq; YP_002519538.1; NC_011930.1.
DR AlphaFoldDB; B7ZIN6; -.
DR GeneID; 7367941; -.
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; 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:BAH11403.1};
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:BAH11403.1};
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 1032..1119
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; 138475 MW; FE988172A6E524CF CRC64;
MKIWRFFLMK ERTRLPFDNL PFYNKVMDKT AIKKLISRLI DHFGMTYTSH ILDQLKTSGF
QQATDTAISL GIDDLLTAPS KGWLVQDAEQ QGSISEKHNH YGNVHAVEKL RQSIEIWYAT
SEYLRKEMNP NFSMTDPLNP VHVMSFSGAR GNTSQVHQLV GMRGLMSDPQ GQIIDLPIRR
NLREGLSLTE YIISCYGARK GVVDTAVRTA DAGYLTRRLV EVVQHIVVRI KDCGTIKGIF
VSPIRGRERD RNEIVVRTQI LIGRVLADDV YINRRCIATR NQDIGVGLAN QLINLRTQSI
YIRTPFTCKS ISRICQLCYG RSTTHNHLIE LGEAVGIIAG QSIGEPGTQL TLRTFHTGGV
FTGDIAEHVR APFNGKIEFN ENLVYPTRTC NGHPAYLCHN NLSITIDGKD QVQNLTIPPQ
SLLLVQNDQY VESEQIIAEV RARTSSFKEK VRKNIYSDLE GEMHWSTNVC HAPEYVHGNV
HSILRTGYLW ILSGGIYGSG VVPFPFNKHQ DQVDVQLFVA KHQSLSDSYV DQMEHRSGDS
NCYGKEEKIF SYSETDRTIS NEHQDSIYVT FSPKNYNIKG KKQMNRFIVP LQFDKEWGKR
RIPCPDAILR IPKSGILQRN SIFGYSNVEY GIPDGPDMTT PFSLSLDLSR EGDNLQIQVS
NSISYEEDGE RIQVMSDTSI PLVQTCLGFD WEQIDSIESG AYASLTSVKT NKIVSNMIQI
SLMKYPLFFM GRRDNQASSN LMFHNKLYHT NLFSSNGESQ LISKHQGTIC SLSNGGEDSG
SFMVLSPSDC FRIVLFNDFK CYDTVNKSNR EDPMRKKIIE FSGLLGHLHS ITNRFPSSHF
LTYKKVLSKK HSIFHNSLNT FQVPKYYFMD ENTRISHFDP CRNIISNLLG PNWCYSPSEF
CERTFPVVSP GQFMPESVCI SEHEPLPESG QIIAVDEESL VIRSAKPYLA TRKATVHGHY
GEILDKGDTL ITLIYERFKS SDIIQGLPKV EQLSEARLNN SISMNLKESF ENWTGDMTRF
LGSLWGLFIS ARITMEQSQT HLVNQIQKVY RSQGVRICDK HIEIIVRQMT SKVLISEDGT
ANVFSPGELI GLSRAQRMNR ALEEAIYYQT MLLGITRASL NTQSFISEAS FQETARVLAK
AALQGRIDWL KGLKENVILG GIIPAGTGQH IRRSGKRNGM DPRMGNRNLF SNKVKDILFH
HDKVSFFSIQ ENSHNILKQP LK
//