RPOC2_CUSEX
ID RPOC2_CUSEX Reviewed; 1379 AA.
AC A8W3B4;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE Short=RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
GN Name=rpoC2 {ECO:0000255|HAMAP-Rule:MF_01324};
OS Cuscuta exaltata (Tall dodder).
OG Plastid.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Cuscuteae; Cuscuta;
OC Cuscuta subgen. Monogynella.
OX NCBI_TaxID=476139;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17956636; DOI=10.1186/1471-2229-7-57;
RA McNeal J.R., Kuehl J.V., Boore J.L., dePamphilis C.W.;
RT "Complete plastid genome sequences suggest strong selection for retention
RT of photosynthetic genes in the parasitic plant genus Cuscuta.";
RL BMC Plant Biol. 7:57-57(2007).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_01324};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01324};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01324}.
CC -!- SUBCELLULAR LOCATION: Plastid.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01324}.
CC -!- CAUTION: Young tissue from this organism is photosynthetic and contains
CC some thylakoids, although the photosynthetic activity does not exceed
CC the light compensation point. {ECO:0000305}.
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DR EMBL; EU189132; ABW83685.1; -; Genomic_DNA.
DR RefSeq; YP_001542521.1; NC_009963.1.
DR AlphaFoldDB; A8W3B4; -.
DR GeneID; 5729574; -.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 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 PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR TIGRFAMs; TIGR02388; rpoC2_cyan; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW Plastid; Transcription; Transferase; Zinc.
FT CHAIN 1..1379
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000353556"
FT REGION 503..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1379 AA; 155671 MW; CE0873ED6FD59DD2 CRC64;
MEVLMAERIN LVFHNKVLDR TAMKRLISRL IDHFGMAYTS HILDQVKTLG FQQATATSIS
LGIDDLLTIP SKGWLVQDAE QQSFIFEKYH HYGNVHAVEK LRQSIEIWYA TSEYLRQEMN
LNFRMTDPLN PVHLMYFSGA RGNASQVHQL VGMRGLMSDP QGQMIDLPIQ SNLREGLSLT
EYIISCYGAR KGVVDTAVRT SDAGYLTRRL VEVVQHIVVR RTDCGTARGI SVSPHNGMMP
ERMFIQTLIG RVLADDIYIG PRCIATRNQN IGVGLVNRFL NFRAEPILIR TPLTCRSTSW
ICRLCYGRSP THGDLVELGE AVGIIAGQSI GEPGTQLTLR TFHTGGVFTG GTAEHVRAPS
NGKIRLNEDL VHPTRTRHGY PAFFCSIYLY VTIESQDILH HVKIPPKSFI LVQNDQYVES
EQVIAESRAG TSTFNYKEKV RKHIYSDSGG EMHWSTNVYH APEFTYGNVH LLSKTSHLWI
LLGEPCHSSL VSTSIHRDQD QMSVQSLSVK RRSTSKLSET NDEANQEIAS ADFSGKKEDR
IADFSDVNRS ICTDHYNLVY PAILPILDEN SSFFSNCLSK RRRNQFIIPL QSIQEHKNEL
MPCSSISMKT PPNANGIFWA NSILAYFDDP RYRRNNSGST KYGTLEMHST VKKEDFIKYR
GVNEFRQKMK VERFFFIPEE VHILPGSSSI MVRNHSLIGV DTQITLNLRS RVGGLVRVER
KKKIIELKIF FGDIYFPGGA DNISQHSGVL IPPGTERKTN YKESKKVKSW IDVQRITPSK
KKFFVLVRPV VTYEIMDDIT SATLFPPDLL QQRDNAQLRV VNYILHGTGK PIRGNYDTSI
QLVRTCLVFK RNQDKKSYYS EAARASVVEI RTNYLIRHFL RIDFVKAPIS YIGKRNDPLG
LGLLADNGLD WTHKNPYSEA RIHQNLNQNQ GTIHTFLNRN KESQSLSILS SSNCSRMDPA
NGAKSNNVIQ ESKKEEYPIL KISNSLGPLG TYPPIANCDS LNHLLTHNQI LVTNYFKLDN
VKPPFQVFKL KYYFIAENWK VCNYNPGSNL RLNVFDFHWN FLHHNSCAET SKIMSLGQFI
CQNVCIDKTR PPRKSGQVIL VQVDSVVIRL AKPYLATPGA TVHGLYGETF FGGDTVVTFN
YEKSISGDIT QGLPKVEQVL EVRSVDSISM NLEGRVEGWS KCITGILGIP WGFFIGAELT
IVQSRISLVN KIQKVYRAQG VHIHNRHIEI IVRQITSKVL VSEDGMSNVF SPGELIGLLR
AERTGRALEE PIHYRSVFLG ITKASLNTQS FISEASFQET ARVLSKAALG GRIDWLKGLK
ENVVLGGVIP AGTGFRGLVD PSKQYKTIPL KTNLFEGGMR DLLVHHRKLF DSFLNTSPS
