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Database: UniProt
Entry: R4L2P0_PINTA
LinkDB: R4L2P0_PINTA
Original site: R4L2P0_PINTA 
ID   R4L2P0_PINTA            Unreviewed;      1220 AA.
AC   R4L2P0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
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:AGL11172.1};
OS   Pinus taeda (Loblolly pine).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AGL11172.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=3352 {ECO:0000313|EMBL:AGL11172.1};
RN   [1] {ECO:0000313|EMBL:AGL11172.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Liu T.Y., Huang S.W., Li Q.F., Wang J.B., Liu C.X., Ning H.G., Zhou H.B.,
RA   Chen J.H.;
RL   Submitted (DEC-2012) 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|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; KC427273; AGL11172.1; -; Genomic_DNA.
DR   RefSeq; YP_008082326.1; NC_021440.1.
DR   AlphaFoldDB; R4L2P0; -.
DR   GeneID; 15824446; -.
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:AGL11172.1};
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:AGL11172.1};
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   1220 AA;  138770 MW;  2D7A9EBCDACF7017 CRC64;
     MKIWRFFLMK ERTRLLFDNL PFYNKVMDKT AIKKLISRLI DHFGMTYTSH ILDQLKTSGF
     QQATDTAISL GIDDLLTAPS KGWLVQDAEQ QGYVSEKQNH 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 QVQNLTIPPQ
     SLLLVQNDQY VESEQLIAEV RARTSSFKEK VRKNIYSDLE GEMHWSTNVC HAPEYVQGNV
     HPILRTGYLW ILSGGIYGSR VVPFPFHKYQ DQVYVQPFVA KHQSLSDSYV DQVEHRSGDS
     NCYEKEEQIF SYSETETDRT ISNEHRDSIY VFSPNNYNIK GKKQMNRFIV SLQCDKEWEK
     RIIPCPDAIL RIPKSGILQR NSIFGYSNVE HGIPDGSNMT TPFSLDLSRE GDNLQIKISY
     SISYEDGERI QVSIPLVRTC LGFDWEQIDS IESEAYVSLI SVRTNKIVNN MVQISLMKYP
     PFFMGRRDNK TSSNLMFHNN LDHTNLFSSN GASQLISKHQ GTICSLSNGK 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 DILFHHDKVD
     FFSFQGNSHK YHNILKQQLK
//
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