RPOC2_OEDCA
ID RPOC2_OEDCA Reviewed; 2617 AA.
AC B2X1Z4;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 40.
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 Oedogonium cardiacum (Filamentous green alga).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC OCC clade; Oedogoniales; Oedogoniaceae; Oedogonium.
OX NCBI_TaxID=55995;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SAG 575-1b / CCAP 575/1B / UTEX LB 40;
RX AGRICOLA=IND44059346; DOI=10.1111/j.1529-8817.2008.00510.x;
RA Turmel M., Brouard J.-S., Gagnon C., Otis C., Lemieux C.;
RT "Deep division in the Chlorophyceae (Chlorophyta) revealed by chloroplast
RT phylogenomic analyseS.";
RL J. Phycol. 44:739-750(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 575-1b / CCAP 575/1B / UTEX LB 40;
RX PubMed=18558012; DOI=10.1186/1471-2164-9-290;
RA Brouard J.-S., Otis C., Lemieux C., Turmel M.;
RT "Chloroplast DNA sequence of the green alga Oedogonium cardiacum
RT (Chlorophyceae): unique genome architecture, derived characters shared with
RT the Chaetophorales and novel genes acquired through horizontal transfer.";
RL BMC Genomics 9:290-290(2008).
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, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_01324}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01324}.
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DR EMBL; EF587367; ABU88207.1; -; Genomic_DNA.
DR EMBL; EU677193; ACC97250.1; -; Genomic_DNA.
DR RefSeq; YP_002000445.1; NC_011031.1.
DR AlphaFoldDB; B2X1Z4; -.
DR PRIDE; B2X1Z4; -.
DR GeneID; 6440045; -.
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:transcription, DNA-templated; IEA:UniProtKB-UniRule.
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; 4.
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 Chloroplast; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT CHAIN 1..2617
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000353573"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 2617 AA; 311891 MW; DBF1F1747CEDC01B CRC64;
MKILFFMIQI KNRNKLNNKN DFIINQIEKK NTQIIITKTL KKNFKNVKLN YYWNQTFDKN
RLKNFIFWCL KNYGQNKTIK VLEILKYLGF KYATKAGLSL SIDDLIIPPT KSKLLIEAEL
TTRTAMLQYK NAQITNLERF QQIIETWHIT SEKMKDDMIY HFKTTNIFNP LYMMAFSGAR
GNVSQVRQLV GMRGLMANPQ GQILDFPIQS NFREGLTLTE YVISCYGARK GVVDTALRTA
NAGYLTRRLV DVAQHVIISN FDCGTHRGII ISEMKQGNKL LFSLRQRLLG RVLAKDVKSG
DLLIAKKNQE ISDHLSEIIA SIVKTVIIRS PLTCKTTQFI CQLCYGWSLA EGRLVGVGET
VGIIAAQSIG EPGTQLTMRT FHTGGVFAGE LLDQLIAPFD GIIKYNIYIP GNMIRTPQGK
IAFLTRIDSQ LIIQSCSNLN NQKYYTIPPY TILFIRNMET VSKNQLIAQL CSFSPSLKNS
SDLIEYKIYS DLEGEIKSTN FKILKKVTEM RDIMYQSLEW GYIWILSGKI YQLPFHSIDN
LKLQYTFQQK NNFFPIKGDF LTNSSILSQI LWINNLENVR LNFKQKHIFY QKFIKNSYNY
TCINNSNQIQ MKWLKKWQKL SEISTFLNLN KSIKTFKSNF NMDLSKENRL INIYSQNLLL
FLTIDKIRYK KFGYFIFFQN NLKNRSLRNI KNSIKQNKEI VVNFNYLKKN SLKHFIFDHK
FFIPISLEST DFVNKENSLI TSPRFFYQKL SNRFFEWFFN QENQIGSGLI QLSEIFVFKK
NLQKEISKKN QIRKKQEKNV KLKYHSLTLK KKKGLSNQFY TYNCMNSYSS ETRYFPHTSC
FLNHFNNEKI NKYLNTNYSL IFFYFRPFIQ CEKQQLSQFH YINNKKYFDN LSLLLKPTII
ASKKKQIRVN MKNTYEYLNQ KIYDLKKQLI KNKLFQKIGK YESNKFFRLI SNHIKKYQII
KKTNTHTIER VNVTKFKLVY NSGIDNFNKR NYFINHKKKR YLKTYISFHP LNFFNKIFNH
GNFLLKKKFY YKLQLIMLCK NNNDKFNSMC QVRCNSFFTT LSTNFLTKKI FFDFNFDKTH
KKDFFLKKND FISFSFFNKF SNIFISFSKS PTNYIDDTHN FMNSYKYISN EFFYLNWSNI
VNKHKIFKEY VFKNNFNKSK EMQNIKNLKK LHSSFTYYII KNQFRFAPSF QKQSINELEN
IYKKEINQVS DTYNCIIKHR LLCINQLNNN FLSYLTYVKL YEFNIYKKSP INTLIKLNLD
TYNCMNDKFN IQKFINQIEN KKNGLDNQKK CNKNMKKIFY LQILLNQLRK FYNYLFNKKT
QKLLFKNNNY KQKNIEKDIL NNNTILNSIY YKKCVPILLI KYKKIQITMN TRSLHTIYIF
NNFLIRKPSR KKNSIFVNKK ISLINNQKTH SLLKMYLIKM HSLNNLVINA YFQSVSFKWL
KKQTDRSLRK KRIFNQIFLK RLEFAKFINK NLIISHEKMQ PTVLDFSDKL NSSQQTENKK
IKTLNKKRLY KNNISKIANE ILFLYSRFLL IPKEYSTISK KQLSFLFFHP QQHLHCINPF
YKILETRTLY ELWNSNNLSF FHKSVFFTKK KFISNRKLKL KRTLKLLTLK NYLNFKKIDS
YNCMCIVSTN NYLQKINTFI FNLFHNLFHT YFQLFKNNRQ GNYIPLKYNN YYGIFQLNKK
NPKRDFSKFK YIQQKYYPDK NLFYLSEKSS IFLNKNWQLY KNKKEFLLTS QPGWICKPIK
KTHTINVDSD FLSNYSLHSI TQLLKKNLKL YNQNYINYFK SIPVSYRFCE RNLIWFNFTF
LKMIELVKKF FKDTYNCMNP LLFLPFFHSF SNFIRYNENF KNIKTSNSKK IKKNGWLINK
KSRFLKMKKS NMFFCLKKTT NKIDNIFLFV EGQEFIINNY QNLSYISDTN LLCLSKKKLF
KMSEKQYKSK SLRNNNGLIW KSQYNSIFLN KQKISQKLIF KFPNLETTFE QYLGIPFNKI
SKTFNKENNI KISYDINRKM RTYTYNYINY RNFPSNHIQQ YSEINQILTK SNSFNLINKN
YKIFKSQKSL NTFRHFLGFS IPITFDFSFQ SSHIFWNYYP NYNLSNLKLD KRKKSMEFFN
YLILKNKLLN LNIIKVKKSR HVLLYEDSIN FINIFNSIEM LLRQPCINWS TTKKINLGYQ
KNIFLAPTKT FLLLSLENSS VTNNPIALTE IFSNMEGEIL YSLKNKKNHP PFHYPLKSGD
KNKFEFNEFL QKYDRSIFLT KSDQICLKFK NEIYLNNELA FLKKFNVFKN QKHIRGLKTF
QIKSSKQIFL IFKILQKIHN NCQFSNQSIK IKLGLFLFQG DLLNTFFRNS NINNNTFNCV
SIIKNKKTTK IQKNYKRSIV CVVNHSGQII HLNQHKLTLR KGQPIFFSPH CIFHSYNSDF
IEQNKPVLSL PYQQLKTGDI VQGIPKIEQL FEARLTFAGK LEYDNLTNIL EIIFQTYKNK
LTLKLAVRRS IELVQMIIVN SIQRIYRSQG VNISDKHLEV IVKQMTKKVE IIDSGQSGFL
IGEHFDLDVV ELWNSKLSKI KHVKYKPLIL GISKASLQTD SFLSAASFQY TTRILSQSAF
FKKRDFLKGL KENIIVGNII PAGTGYLGHI EDLFETS
