ID T1QMF4_EUCDE Unreviewed; 1392 AA.
AC T1QMF4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
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:AGC58297.1};
GN ORFNames=EDEG_CP_p011 {ECO:0000313|EMBL:AGC58297.1};
OS Eucalyptus deglupta (Mindanao gum) (Rainbow eucalyptus).
OG Plastid; Chloroplast {ECO:0000313|EMBL:AGC58297.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=106642 {ECO:0000313|EMBL:AGC58297.1};
RN [1] {ECO:0000313|EMBL:AGC58297.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23876290;
RA Bayly M.J., Rigault P., Spokevicius A., Ladiges P.Y., Ades P.K.,
RA Anderson C., Bossinger G., Merchant A., Udovicic F., Woodrow I.E.,
RA Tibbits J.;
RT "Chloroplast genome analysis of Australian eucalypts--Eucalyptus, Corymbia,
RT Angophora, Allosyncarpia and Stockwellia (Myrtaceae).";
RL Mol. Phylogenet. Evol. 69:704-716(2013).
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; KC180792; AGC58297.1; -; Genomic_DNA.
DR RefSeq; YP_008576888.1; NC_022399.1.
DR GeneID; 17082389; -.
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:SF1; 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:AGC58297.1};
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:AGC58297.1};
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 97..161
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF05000"
FT DOMAIN 176..366
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT DOMAIN 1197..1282
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1392 AA; 158464 MW; 1BF0F73B2CB4EA66 CRC64;
MEVLMAERVN LVFHNKVIDG TAIKRLISRL IDHFGMAYTS HILDQVKTLG FQQATATSIS
LGIDDLLTIP SKGWLVQDAE QQSLILEKHH HYGNVHAVEK LRQSIEVWYA TSEYLRQEMN
PNFRMTDPFN PVHIMSFSGA RGNASQVHQL VGMRGLMSDP QGQMIDLPIQ SNLREGLSLT
EYIISCYGAR KGVVDTAVRT SDAGYLTRRL VEVVQHIVVR RTDCGTIRGV SVSPRNGMMP
ERIFIQTLIG RVLADDIYMG PRCIAIRNQD IGIGLVNRFI TFRTQPISIR TPFTCRSTSW
ICRLCYGRSP THGDLVELGE AVGIIAGQSI GEPGTQLTLR TFHTGGVFTG GTAEHVRAPS
NGKIKFNDDL VHPTRTRHGH PAFLCSIDLY VTIESEDILH NVTIPPKSFL LVQNNQYVES
EQVIAEIRAG TYTFNLKERV RKHIYSESEG EMHWSTDVYH APEFTYSNVH LLPKTSHLWI
LSGGSCRSSR VPFSLYKDQD QMNLRSTERE RRYISSLSVN NDQMRYELCS SDFSGKIKED
RIPDYSELNR IISIVHCNLK YPTTFHENSD LLAKRRRNRF LIPLQSIQER KKELMPHSGI
SIELPINGIL RRNSILAYFD DPRYRRKSSG IIKYGTLGVH SVVKKEDLIE YRGIKEFKQK
CQMKLDPFFF IPEEVHIFPE SSSIMVRNNS LIGVDTRIAL NTRSRVGGLV RVERKKKRIE
LKIFSGDIHF PGETDKISRH SGILIPPGTG KTNSKESKKW KNWIYVQRIT PTKKKYFVLV
RPVVTYEVLD GINLATLFPP DLLQERDNMQ LRVVNYIVYR NGKPIRGISD TSIQLVRTCL
ILNWDQDKKS SSIEEAHTSF VEVSTNGLIR DFLRIDLVKF PISYLRKRND PSGSGLISDS
DNVSDHTNSN PFYSKTKIQQ LLSQNQGTIR TLLNKNKECP SLIILSSSNC FRMGPFNAGK
YHNVIKESIK KDPIIKIRNS IGPLGTVLQF VNFYSFYYLI THNPILVTKY LQLENLKQTF
QVINYYLMDE NGRILNPDSC SNIVLNSFNL NWYFLHHNYY HNYFEERSTI ISLGQFICEN
VCISKNGPHL KSGQVLIVQV DSVVIRSAKP YLATPGATVH GHYGEILYEG DTLVTFIYEK
SRSGDITQGL PKVEQVLEVR SIDSISMNLE KRIEGWNEHI KKILGIPWGF LIGAELTIVQ
SRISLVNKIQ KVYRSQGVQI HNRHIEIIVR QITSKVLVSE DGMSNVFLPG ELIGLLRAAR
TGRALEESIC YRAILLGITR ASLNTQSFIS EASFQETARV LAKAALRGRI DWLKGLKENV
VIGGMIPVGT GFKGLVHRSR QHKNIPLKTK KKNFFEGEIG DILFHHRELF DSSISKKFHD
TSEQSFRGFN DS
//
