ID F6I8V7_OLEEU Unreviewed; 1394 AA.
AC F6I8V7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
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:CBR24610.1};
GN ORFNames=BN443_0170 {ECO:0000313|EMBL:CCQ09092.1};
OS Olea europaea subsp. europaea.
OG Plastid; Chloroplast {ECO:0000313|EMBL:CBR24610.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Oleaceae; Oleeae; Olea.
OX NCBI_TaxID=158383 {ECO:0000313|EMBL:CBR24610.1};
RN [1] {ECO:0000313|EMBL:CBR24610.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21569271; DOI=10.1186/1471-2229-11-80;
RA Besnard G., Hernandez P., Dorado G., Khadari B., Vargas P., Savolainen V.;
RT "Genomic profiling of plastid DNA variation in the Mediterranean olive
RT tree.";
RL BMC Plant Biol. 11:80-80(2011).
RN [2] {ECO:0000313|EMBL:CBR24610.1}
RP NUCLEOTIDE SEQUENCE.
RA Hernandez P., Dorado G.;
RT "Olive tree chloroplast sequencing. Grupo PAI AGR-248 (Biotecnologia
RT Agroalimentaria), Universidad de Cordoba, Junta de Andalucia (Spain).";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CCQ09092.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Stavrovouni 11 {ECO:0000313|EMBL:CCQ09092.1};
RA Besnard G.;
RT "Pleistocene genetic legacy and the domestication of the olive tree.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AUT84654.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Stavrovouni Monastery 11 {ECO:0000313|EMBL:AUT84654.1};
RA Van de Paer C., Bouchez O., Besnard G.;
RT "Evolutionary mitogenomics of the olive family (Oleaceae).";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:QOY46445.1}
RP NUCLEOTIDE SEQUENCE.
RA Haddad N.J., Migdadi H.M., Brake M.H., Ayoub S.J., Obeidat W.M.,
RA Abusini Y.A., Aburumman A.A., Al-Shagour B.E., Al-Anasweh E.N.,
RA Sadder M.T.;
RT "The complete chloroplast genome sequence of the historical olive (Olea
RT europaea subsp. europaea) cultivar Mehras, in Jordan.";
RL Submitted (SEP-2020) 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; MG255761; AUT84654.1; -; Genomic_DNA.
DR EMBL; FN996972; CBR24610.1; -; Genomic_DNA.
DR EMBL; HF558645; CCQ09092.1; -; Genomic_DNA.
DR EMBL; MW072292; QOY46445.1; -; 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: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:CBR24610.1};
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:CBR24610.1};
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..396
FT /note="RNA polymerase Rpb1"
FT /evidence="ECO:0000259|Pfam:PF04998"
FT DOMAIN 1199..1284
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 1394 AA; 158165 MW; 48F3EA95DFD56F8E CRC64;
MEVLMAERAN LVFHNKVIDG TAMKRLISRL IDHFGMAYTS HILDQVKTLG FHQATATSIS
LGIDDLLTIP SKRWLVQDAE QQSLILEKHH HYGNVHAVEK LRQSIEIWYA TSEYLRQEMN
PNFRMTDPFN PVHLMSFSGA RGNASQVHQL VGMRGLMSDP QGQMIDLPIQ SNLREGLSLT
EYIISCYGAR KGVVDTAVRT SDAGYLTRRL VEVVQHIVVR RTDCGTTRGI SVSPRNGMMP
ERIFIQTLMG RVLADDIYTG TRCIASRNQD IGIGLVNRFI TFRAQPISIR TPFTCRSASW
ICRLCYGRSP THGDLVELGE AVGIIAGQSI GEPGTQLTLR TFHTGGVFTG GTAEHVRAPS
NGKIKFNEDL VHPTRTRHGH PAFLCSIDLY VTIESEDILH NVNIPSKSFL LVQNDQYVES
EQVIAEIRAG TSTLNFKEKV RKHIYSDSDG EMHWSTDVYH PPEFTYGNVH LLPKTSHLWI
LLGGPCRSSL VSLSLHKDQD QINAHSRSVK RRYTSNLSET NDPERQKLFS SYFYGKKKKE
DRISDYSDLN RIRCNGRCNL IYPTILHQNS DLFSKRRRNR FIIPLQSIQE RENELMPRSG
ISIEIPPNGI FRRNSILAYF DDPRYRRKSS GITKYGTIEM HSIVKKEDLI EYRGVKAFRP
KYQMKVDRFF FIPEEVHILP GSSSIMVRNN SLIGVDTQIT LNIRSRVGGF VRVERKKKRI
ELKIFSGDIH FPGETDKISR HSGVLIPPGT GKLNSKESKK WKNWIYVQRI TPSKKKYFVL
VRLVVTYEIT DGINLATLFP PDLLQERDSV QLRVVNYILY GNGKPIRGIS DTDIQLVRTC
LVLNWDQDKK KSSSSEEARA SFVEIRTNGL IRHFLRIDLV KSPISYIGKR NDPSGSGLLS
DNGSDCTNIN PFSSIYSKAR IQQSLNQNQG TIHTLLNRNT GFQSLIILSS SNCFRMGPFN
DVIKYHNVIK ESIQITKDPR IPIKNSLGPF GTAFPIVNFY SFYHLITHNQ ILVNNYLQLD
NLKQTFQVIK YYLMDENEKI YNPEPGSNII LNPFNLNWYS LHHNYCQETS TIISLGQFIC
ENVCIAKNAP HLKSGQVILV QVDSVVIRSA KPYLATPGAT VHGHYGEILY EGDTLITFIY
EKSRSGDITQ GLPKVEQVLE VRSIDSISMN LEKRVEGWNE RITRILGMPW GFLIGAELTI
VQSRISLVNK IQKVYRSQGV QIHNRHIEII VRQITSKVLV SEDGMSNVFS PGELIGLLRA
ERMGRALEEA VCYRAVLLGI TRASLNTQSF ISEASFQETA RVLAKAALRG RIDWLKGLKE
NVVLGGMIPL GTGFKGLVPP SKQDNNSLLE TKKKNLFEGE MRDILFHHRK LFDSCLSKNF
HDTSEQSFIG FNDS
//
